data_9H7A
# 
_entry.id   9H7A 
# 
_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   9H7A         pdb_00009h7a 10.2210/pdb9h7a/pdb 
WWPDB D_1292142452 ?            ?                   
# 
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                        9H7A 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.wood@ucl.ac.uk 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Wood 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4106-775X 
# 
_audit_author.name               'Chen, W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8180-366X 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Plos One' ? ? 1932-6203 ? ? 20 ? e0323816 e0323816 
'Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.' 2025 ? 
10.1371/journal.pone.0323816 40367241 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv    ? ? 2692-8205 ? ? ?  ? ?        ?        
'Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method'  2025 ? 
10.1101/2025.02.22.639275    ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, W.' 1 0000-0002-8180-366X 
1       'Chen, W.' 2 0000-0002-8180-366X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Transthyretin                     13777.360 2  ? ? ? ? 
2 non-polymer syn 3,5-dichlorobenzene-1-sulfonamide 226.080   1  ? ? ? ? 
3 water       nat water                             18.015    33 ? ? ? ? 
# 
_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-dichlorobenzene-1-sulfonamide 6OT 
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                    'Human Plasma' 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               'Human Plasma' 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
6OT non-polymer         . 3,5-dichlorobenzene-1-sulfonamide ? 'C6 H5 Cl2 N O2 S' 226.080 
ALA 'L-peptide linking' y ALANINE                           ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                          ? 'C3 H7 N O2 S'     121.158 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                         ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                     ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 ?   ?   ?   A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  CYS 10  10  ?   ?   ?   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  ?   ?   ?   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 ALA B . n 
B 1 100 SER 100 100 ?   ?   ?   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        6OT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   6OT 
_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 6OT 1  201 1  6OT DSF B . 
D 3 HOH 1  201 34 HOH HOH A . 
D 3 HOH 2  202 33 HOH HOH A . 
D 3 HOH 3  203 8  HOH HOH A . 
D 3 HOH 4  204 3  HOH HOH A . 
D 3 HOH 5  205 16 HOH HOH A . 
D 3 HOH 6  206 32 HOH HOH A . 
D 3 HOH 7  207 6  HOH HOH A . 
D 3 HOH 8  208 9  HOH HOH A . 
D 3 HOH 9  209 20 HOH HOH A . 
D 3 HOH 10 210 2  HOH HOH A . 
D 3 HOH 11 211 31 HOH HOH A . 
D 3 HOH 12 212 10 HOH HOH A . 
D 3 HOH 13 213 11 HOH HOH A . 
D 3 HOH 14 214 15 HOH HOH A . 
D 3 HOH 15 215 27 HOH HOH A . 
D 3 HOH 16 216 19 HOH HOH A . 
D 3 HOH 17 217 24 HOH HOH A . 
D 3 HOH 18 218 1  HOH HOH A . 
D 3 HOH 19 219 23 HOH HOH A . 
D 3 HOH 20 220 25 HOH HOH A . 
E 3 HOH 1  301 26 HOH HOH B . 
E 3 HOH 2  302 7  HOH HOH B . 
E 3 HOH 3  303 30 HOH HOH B . 
E 3 HOH 4  304 12 HOH HOH B . 
E 3 HOH 5  305 21 HOH HOH B . 
E 3 HOH 6  306 4  HOH HOH B . 
E 3 HOH 7  307 13 HOH HOH B . 
E 3 HOH 8  308 5  HOH HOH B . 
E 3 HOH 9  309 17 HOH HOH B . 
E 3 HOH 10 310 22 HOH HOH B . 
E 3 HOH 11 311 28 HOH HOH B . 
E 3 HOH 12 312 18 HOH HOH B . 
E 3 HOH 13 313 14 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A CYS 10  ? N   ? A CYS 10  N   
2  1 Y 1 A CYS 10  ? CB  ? A CYS 10  CB  
3  1 Y 1 A CYS 10  ? SG  ? A CYS 10  SG  
4  1 Y 1 A LYS 15  ? NZ  ? A LYS 15  NZ  
5  1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
6  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
7  1 Y 1 A ASP 38  ? CG  ? A ASP 38  CG  
8  1 Y 1 A ASP 38  ? OD1 ? A ASP 38  OD1 
9  1 Y 1 A ASP 38  ? OD2 ? A ASP 38  OD2 
10 1 Y 1 A ASP 39  ? CG  ? A ASP 39  CG  
11 1 Y 1 A ASP 39  ? OD1 ? A ASP 39  OD1 
12 1 Y 1 A ASP 39  ? OD2 ? A ASP 39  OD2 
13 1 Y 1 A THR 40  ? OG1 ? A THR 40  OG1 
14 1 Y 1 A THR 40  ? CG2 ? A THR 40  CG2 
15 1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
16 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
17 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
18 1 Y 1 A LYS 48  ? CD  ? A LYS 48  CD  
19 1 Y 1 A LYS 48  ? CE  ? A LYS 48  CE  
20 1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
21 1 Y 1 A GLU 51  ? CG  ? A GLU 51  CG  
22 1 Y 1 A GLU 51  ? CD  ? A GLU 51  CD  
23 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
24 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
25 1 Y 1 A GLU 61  ? CG  ? A GLU 61  CG  
26 1 Y 1 A GLU 61  ? CD  ? A GLU 61  CD  
27 1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
28 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
29 1 Y 1 A GLU 72  ? CD  ? A GLU 72  CD  
30 1 Y 1 A GLU 72  ? OE1 ? A GLU 72  OE1 
31 1 Y 1 A GLU 72  ? OE2 ? A GLU 72  OE2 
32 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
33 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
34 1 Y 1 A GLU 92  ? CD  ? A GLU 92  CD  
35 1 Y 1 A GLU 92  ? OE1 ? A GLU 92  OE1 
36 1 Y 1 A GLU 92  ? OE2 ? A GLU 92  OE2 
37 1 Y 1 A ASP 99  ? CG  ? A ASP 99  CG  
38 1 Y 1 A ASP 99  ? OD1 ? A ASP 99  OD1 
39 1 Y 1 A ASP 99  ? OD2 ? A ASP 99  OD2 
40 1 Y 1 A SER 100 ? OG  ? A SER 100 OG  
41 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
42 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
43 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
44 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
45 1 Y 1 B LYS 15  ? CD  ? B LYS 15  CD  
46 1 Y 1 B LYS 15  ? CE  ? B LYS 15  CE  
47 1 Y 1 B LYS 15  ? NZ  ? B LYS 15  NZ  
48 1 Y 1 B ARG 21  ? CZ  ? B ARG 21  CZ  
49 1 Y 1 B ARG 21  ? NH1 ? B ARG 21  NH1 
50 1 Y 1 B ARG 21  ? NH2 ? B ARG 21  NH2 
51 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
52 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
53 1 Y 1 B ASP 38  ? OD1 ? B ASP 38  OD1 
54 1 Y 1 B ASP 38  ? OD2 ? B ASP 38  OD2 
55 1 Y 1 B THR 40  ? OG1 ? B THR 40  OG1 
56 1 Y 1 B THR 40  ? CG2 ? B THR 40  CG2 
57 1 Y 1 B GLU 42  ? CG  ? B GLU 42  CG  
58 1 Y 1 B GLU 42  ? CD  ? B GLU 42  CD  
59 1 Y 1 B GLU 42  ? OE1 ? B GLU 42  OE1 
60 1 Y 1 B GLU 42  ? OE2 ? B GLU 42  OE2 
61 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
62 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
63 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
64 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
65 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
66 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
67 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
68 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
69 1 Y 1 B GLU 63  ? CG  ? B GLU 63  CG  
70 1 Y 1 B GLU 63  ? CD  ? B GLU 63  CD  
71 1 Y 1 B GLU 63  ? OE1 ? B GLU 63  OE1 
72 1 Y 1 B GLU 63  ? OE2 ? B GLU 63  OE2 
73 1 Y 1 B LYS 76  ? NZ  ? B LYS 76  NZ  
74 1 Y 1 B GLU 92  ? CG  ? B GLU 92  CG  
75 1 Y 1 B GLU 92  ? CD  ? B GLU 92  CD  
76 1 Y 1 B GLU 92  ? OE1 ? B GLU 92  OE1 
77 1 Y 1 B GLU 92  ? OE2 ? B GLU 92  OE2 
78 1 Y 1 B ASP 99  ? CG  ? B ASP 99  CG  
79 1 Y 1 B ASP 99  ? OD1 ? B ASP 99  OD1 
80 1 Y 1 B ASP 99  ? OD2 ? B ASP 99  OD2 
81 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
82 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
83 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
84 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
85 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
86 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                     9H7A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.540 
_cell.length_a_esd                 ? 
_cell.length_b                     43.450 
_cell.length_b_esd                 ? 
_cell.length_c                     64.630 
_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                         9H7A 
_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                   9H7A 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.56 
_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 
# 
_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   0.9778 
_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        0.9778 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.76 
_reflns.d_resolution_low                               64.63 
_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                                     24574 
_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                           99.99 
_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                          18.9 
_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                                0.047 
_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                              0.113 
_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                                    1.76 
_reflns_shell.d_res_low                                     1.807 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1551 
_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                               0.554 
_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                                  1.339 
_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]                            -0.01 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.03 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.329 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_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                                 9H7A 
_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                            1.76 
_refine.ls_d_res_low                             51.57 
_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                     23284 
_refine.ls_number_reflns_R_free                  1255 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19622 
_refine.ls_R_factor_R_free                       0.22649 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19456 
_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                       0.115 
_refine.pdbx_overall_ESU_R_Free                  0.112 
_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                             5.284 
_refine.overall_SU_ML                            0.081 
_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                       1.76 
_refine_hist.d_res_low                        51.57 
_refine_hist.number_atoms_solvent             33 
_refine_hist.number_atoms_total               1709 
_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        1664 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.019  0.020  1776 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  1132 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.806  1.941  2439 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.932  3.000  2774 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.530  5.000  238  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.332 22.542 59   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.173 15.000 252  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.366 15.000 6    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.115  0.200  286  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.021  1996 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  378  ? 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' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.761 
_refine_ls_shell.d_res_low                        1.807 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             98 
_refine_ls_shell.number_reflns_R_work             1551 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.223 
_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                  0.309 
# 
_struct.entry_id                     9H7A 
_struct.title                        'Human Transthyretin in Complex with 3,5-Dichlorobenzenesulfonamide' 
_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        9H7A 
_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 9H7A A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7A 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)' 6250  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  18070 ? 
# 
_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_565 -x,-y+1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 43.4500000000 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 ? GLY B 83 ? ASP B 74 GLY B 83 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA1 6 ARG B 104 ? 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  
AA3 5 HIS B 88  ? ALA B 97  ? HIS B 88  ALA B 97  
AA3 6 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA3 7 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA3 8 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA1 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA1 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA1 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA1 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA2 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA2 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA2 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA2 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N GLY A 67  ? N GLY A 67  O ALA A 97  ? O ALA A 97  
AA3 4 5 N VAL A 94  ? N VAL A 94  O GLU B 89  ? O GLU B 89  
AA3 5 6 O ALA B 91  ? O ALA B 91  N ILE B 73  ? N ILE B 73  
AA3 6 7 O GLU B 72  ? O GLU B 72  N HIS B 31  ? N HIS B 31  
AA3 7 8 N VAL B 32  ? N VAL B 32  O ALA B 45  ? O ALA B 45  
# 
_pdbx_entry_details.entry_id                   9H7A 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE B 44  ? ? -130.57 -45.95 
2 1 PRO B 102 ? ? -37.66  129.52 
# 
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 6OT 201 ? C 6OT . 
2 1 B 6OT 201 ? C 6OT . 
3 1 B 6OT 201 ? C 6OT . 
4 1 B HOH 311 ? E HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.091 22.508 -6.556  0.0395 0.0156 0.0378 -0.0082 0.0204  -0.0124 1.3244 0.8438 0.9544 0.2904  
-0.1397 -0.2465 -0.0241 -0.0328 0.0569 -0.0758 0.0152  0.1224 0.0418  -0.0441 -0.0334 
'X-RAY DIFFRACTION' 2 ? refined -12.846 19.220 -25.551 0.0739 0.0743 0.0705 -0.0211 -0.0359 -0.0215 1.5227 1.3013 1.1577 -0.0558 
0.3078  -0.6716 -0.0849 0.0516  0.0334 0.2113  -0.0595 0.2191 -0.1210 -0.0283 -0.1101 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 10 A 124 ? ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 11 B 123 ? ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A GLY 4   ? A GLY 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A LYS 9   ? A LYS 9   
10 1 Y 1 A PRO 125 ? A PRO 125 
11 1 Y 1 A LYS 126 ? A LYS 126 
12 1 Y 1 A GLU 127 ? A GLU 127 
13 1 Y 1 B GLY 1   ? B GLY 1   
14 1 Y 1 B PRO 2   ? B PRO 2   
15 1 Y 1 B THR 3   ? B THR 3   
16 1 Y 1 B GLY 4   ? B GLY 4   
17 1 Y 1 B THR 5   ? B THR 5   
18 1 Y 1 B GLY 6   ? B GLY 6   
19 1 Y 1 B GLU 7   ? B GLU 7   
20 1 Y 1 B SER 8   ? B SER 8   
21 1 Y 1 B LYS 9   ? B LYS 9   
22 1 Y 1 B CYS 10  ? B CYS 10  
23 1 Y 1 B ASP 39  ? B ASP 39  
24 1 Y 1 B SER 100 ? B SER 100 
25 1 Y 1 B ASN 124 ? B ASN 124 
26 1 Y 1 B PRO 125 ? B PRO 125 
27 1 Y 1 B LYS 126 ? B LYS 126 
28 1 Y 1 B GLU 127 ? B GLU 127 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
6OT N12  N  N N 1   
6OT C01  C  Y N 2   
6OT C02  C  Y N 3   
6OT C03  C  Y N 4   
6OT C04  C  Y N 5   
6OT C05  C  Y N 6   
6OT C06  C  Y N 7   
6OT CL7  CL N N 8   
6OT CL8  CL N N 9   
6OT S09  S  N N 10  
6OT O10  O  N N 11  
6OT O11  O  N N 12  
6OT H121 H  N N 13  
6OT H122 H  N N 14  
6OT H021 H  N N 15  
6OT H041 H  N N 16  
6OT H061 H  N N 17  
ALA N    N  N N 18  
ALA CA   C  N S 19  
ALA C    C  N N 20  
ALA O    O  N N 21  
ALA CB   C  N N 22  
ALA OXT  O  N N 23  
ALA H    H  N N 24  
ALA H2   H  N N 25  
ALA HA   H  N N 26  
ALA HB1  H  N N 27  
ALA HB2  H  N N 28  
ALA HB3  H  N N 29  
ALA HXT  H  N N 30  
ARG N    N  N N 31  
ARG CA   C  N S 32  
ARG C    C  N N 33  
ARG O    O  N N 34  
ARG CB   C  N N 35  
ARG CG   C  N N 36  
ARG CD   C  N N 37  
ARG NE   N  N N 38  
ARG CZ   C  N N 39  
ARG NH1  N  N N 40  
ARG NH2  N  N N 41  
ARG OXT  O  N N 42  
ARG H    H  N N 43  
ARG H2   H  N N 44  
ARG HA   H  N N 45  
ARG HB2  H  N N 46  
ARG HB3  H  N N 47  
ARG HG2  H  N N 48  
ARG HG3  H  N N 49  
ARG HD2  H  N N 50  
ARG HD3  H  N N 51  
ARG HE   H  N N 52  
ARG HH11 H  N N 53  
ARG HH12 H  N N 54  
ARG HH21 H  N N 55  
ARG HH22 H  N N 56  
ARG HXT  H  N N 57  
ASN N    N  N N 58  
ASN CA   C  N S 59  
ASN C    C  N N 60  
ASN O    O  N N 61  
ASN CB   C  N N 62  
ASN CG   C  N N 63  
ASN OD1  O  N N 64  
ASN ND2  N  N N 65  
ASN OXT  O  N N 66  
ASN H    H  N N 67  
ASN H2   H  N N 68  
ASN HA   H  N N 69  
ASN HB2  H  N N 70  
ASN HB3  H  N N 71  
ASN HD21 H  N N 72  
ASN HD22 H  N N 73  
ASN HXT  H  N N 74  
ASP N    N  N N 75  
ASP CA   C  N S 76  
ASP C    C  N N 77  
ASP O    O  N N 78  
ASP CB   C  N N 79  
ASP CG   C  N N 80  
ASP OD1  O  N N 81  
ASP OD2  O  N N 82  
ASP OXT  O  N N 83  
ASP H    H  N N 84  
ASP H2   H  N N 85  
ASP HA   H  N N 86  
ASP HB2  H  N N 87  
ASP HB3  H  N N 88  
ASP HD2  H  N N 89  
ASP HXT  H  N N 90  
CYS N    N  N N 91  
CYS CA   C  N R 92  
CYS C    C  N N 93  
CYS O    O  N N 94  
CYS CB   C  N N 95  
CYS SG   S  N N 96  
CYS OXT  O  N N 97  
CYS H    H  N N 98  
CYS H2   H  N N 99  
CYS HA   H  N N 100 
CYS HB2  H  N N 101 
CYS HB3  H  N N 102 
CYS HG   H  N N 103 
CYS HXT  H  N N 104 
GLU N    N  N N 105 
GLU CA   C  N S 106 
GLU C    C  N N 107 
GLU O    O  N N 108 
GLU CB   C  N N 109 
GLU CG   C  N N 110 
GLU CD   C  N N 111 
GLU OE1  O  N N 112 
GLU OE2  O  N N 113 
GLU OXT  O  N N 114 
GLU H    H  N N 115 
GLU H2   H  N N 116 
GLU HA   H  N N 117 
GLU HB2  H  N N 118 
GLU HB3  H  N N 119 
GLU HG2  H  N N 120 
GLU HG3  H  N N 121 
GLU HE2  H  N N 122 
GLU HXT  H  N N 123 
GLY N    N  N N 124 
GLY CA   C  N N 125 
GLY C    C  N N 126 
GLY O    O  N N 127 
GLY OXT  O  N N 128 
GLY H    H  N N 129 
GLY H2   H  N N 130 
GLY HA2  H  N N 131 
GLY HA3  H  N N 132 
GLY HXT  H  N N 133 
HIS N    N  N N 134 
HIS CA   C  N S 135 
HIS C    C  N N 136 
HIS O    O  N N 137 
HIS CB   C  N N 138 
HIS CG   C  Y N 139 
HIS ND1  N  Y N 140 
HIS CD2  C  Y N 141 
HIS CE1  C  Y N 142 
HIS NE2  N  Y N 143 
HIS OXT  O  N N 144 
HIS H    H  N N 145 
HIS H2   H  N N 146 
HIS HA   H  N N 147 
HIS HB2  H  N N 148 
HIS HB3  H  N N 149 
HIS HD1  H  N N 150 
HIS HD2  H  N N 151 
HIS HE1  H  N N 152 
HIS HE2  H  N N 153 
HIS HXT  H  N N 154 
HOH O    O  N N 155 
HOH H1   H  N N 156 
HOH H2   H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
# 
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 
6OT N12 S09  sing N N 1   
6OT O11 S09  doub N N 2   
6OT S09 C05  sing N N 3   
6OT S09 O10  doub N N 4   
6OT CL7 C01  sing N N 5   
6OT C06 C05  doub Y N 6   
6OT C06 C01  sing Y N 7   
6OT C05 C04  sing Y N 8   
6OT C01 C02  doub Y N 9   
6OT C04 C03  doub Y N 10  
6OT C02 C03  sing Y N 11  
6OT C03 CL8  sing N N 12  
6OT N12 H121 sing N N 13  
6OT N12 H122 sing N N 14  
6OT C02 H021 sing N N 15  
6OT C04 H041 sing N N 16  
6OT C06 H061 sing N N 17  
ALA N   CA   sing N N 18  
ALA N   H    sing N N 19  
ALA N   H2   sing N N 20  
ALA CA  C    sing N N 21  
ALA CA  CB   sing N N 22  
ALA CA  HA   sing N N 23  
ALA C   O    doub N N 24  
ALA C   OXT  sing N N 25  
ALA CB  HB1  sing N N 26  
ALA CB  HB2  sing N N 27  
ALA CB  HB3  sing N N 28  
ALA OXT HXT  sing N N 29  
ARG N   CA   sing N N 30  
ARG N   H    sing N N 31  
ARG N   H2   sing N N 32  
ARG CA  C    sing N N 33  
ARG CA  CB   sing N N 34  
ARG CA  HA   sing N N 35  
ARG C   O    doub N N 36  
ARG C   OXT  sing N N 37  
ARG CB  CG   sing N N 38  
ARG CB  HB2  sing N N 39  
ARG CB  HB3  sing N N 40  
ARG CG  CD   sing N N 41  
ARG CG  HG2  sing N N 42  
ARG CG  HG3  sing N N 43  
ARG CD  NE   sing N N 44  
ARG CD  HD2  sing N N 45  
ARG CD  HD3  sing N N 46  
ARG NE  CZ   sing N N 47  
ARG NE  HE   sing N N 48  
ARG CZ  NH1  sing N N 49  
ARG CZ  NH2  doub N N 50  
ARG NH1 HH11 sing N N 51  
ARG NH1 HH12 sing N N 52  
ARG NH2 HH21 sing N N 53  
ARG NH2 HH22 sing N N 54  
ARG OXT HXT  sing N N 55  
ASN N   CA   sing N N 56  
ASN N   H    sing N N 57  
ASN N   H2   sing N N 58  
ASN CA  C    sing N N 59  
ASN CA  CB   sing N N 60  
ASN CA  HA   sing N N 61  
ASN C   O    doub N N 62  
ASN C   OXT  sing N N 63  
ASN CB  CG   sing N N 64  
ASN CB  HB2  sing N N 65  
ASN CB  HB3  sing N N 66  
ASN CG  OD1  doub N N 67  
ASN CG  ND2  sing N N 68  
ASN ND2 HD21 sing N N 69  
ASN ND2 HD22 sing N N 70  
ASN OXT HXT  sing N N 71  
ASP N   CA   sing N N 72  
ASP N   H    sing N N 73  
ASP N   H2   sing N N 74  
ASP CA  C    sing N N 75  
ASP CA  CB   sing N N 76  
ASP CA  HA   sing N N 77  
ASP C   O    doub N N 78  
ASP C   OXT  sing N N 79  
ASP CB  CG   sing N N 80  
ASP CB  HB2  sing N N 81  
ASP CB  HB3  sing N N 82  
ASP CG  OD1  doub N N 83  
ASP CG  OD2  sing N N 84  
ASP OD2 HD2  sing N N 85  
ASP OXT HXT  sing N N 86  
CYS N   CA   sing N N 87  
CYS N   H    sing N N 88  
CYS N   H2   sing N N 89  
CYS CA  C    sing N N 90  
CYS CA  CB   sing N N 91  
CYS CA  HA   sing N N 92  
CYS C   O    doub N N 93  
CYS C   OXT  sing N N 94  
CYS CB  SG   sing N N 95  
CYS CB  HB2  sing N N 96  
CYS CB  HB3  sing N N 97  
CYS SG  HG   sing N N 98  
CYS OXT HXT  sing N N 99  
GLU N   CA   sing N N 100 
GLU N   H    sing N N 101 
GLU N   H2   sing N N 102 
GLU CA  C    sing N N 103 
GLU CA  CB   sing N N 104 
GLU CA  HA   sing N N 105 
GLU C   O    doub N N 106 
GLU C   OXT  sing N N 107 
GLU CB  CG   sing N N 108 
GLU CB  HB2  sing N N 109 
GLU CB  HB3  sing N N 110 
GLU CG  CD   sing N N 111 
GLU CG  HG2  sing N N 112 
GLU CG  HG3  sing N N 113 
GLU CD  OE1  doub N N 114 
GLU CD  OE2  sing N N 115 
GLU OE2 HE2  sing N N 116 
GLU OXT HXT  sing N N 117 
GLY N   CA   sing N N 118 
GLY N   H    sing N N 119 
GLY N   H2   sing N N 120 
GLY CA  C    sing N N 121 
GLY CA  HA2  sing N N 122 
GLY CA  HA3  sing N N 123 
GLY C   O    doub N N 124 
GLY C   OXT  sing N N 125 
GLY OXT HXT  sing N N 126 
HIS N   CA   sing N N 127 
HIS N   H    sing N N 128 
HIS N   H2   sing N N 129 
HIS CA  C    sing N N 130 
HIS CA  CB   sing N N 131 
HIS CA  HA   sing N N 132 
HIS C   O    doub N N 133 
HIS C   OXT  sing N N 134 
HIS CB  CG   sing N N 135 
HIS CB  HB2  sing N N 136 
HIS CB  HB3  sing N N 137 
HIS CG  ND1  sing Y N 138 
HIS CG  CD2  doub Y N 139 
HIS ND1 CE1  doub Y N 140 
HIS ND1 HD1  sing N N 141 
HIS CD2 NE2  sing Y N 142 
HIS CD2 HD2  sing N N 143 
HIS CE1 NE2  sing Y N 144 
HIS CE1 HE1  sing N N 145 
HIS NE2 HE2  sing N N 146 
HIS OXT HXT  sing N N 147 
HOH O   H1   sing N N 148 
HOH O   H2   sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
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                    9H7A 
_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]   0.011690 
_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]   0.023015 
_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]   0.015473 
_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  CA  . CYS A 1 10  ? -11.948 16.253 6.520   1.00 45.41  ? 10  CYS A CA  1 
ATOM   2    C  C   . CYS A 1 10  ? -11.662 15.428 5.246   1.00 42.51  ? 10  CYS A C   1 
ATOM   3    O  O   . CYS A 1 10  ? -10.543 15.359 4.799   1.00 41.14  ? 10  CYS A O   1 
ATOM   4    N  N   . PRO A 1 11  ? -12.685 14.774 4.679   1.00 35.69  ? 11  PRO A N   1 
ATOM   5    C  CA  . PRO A 1 11  ? -12.627 13.958 3.483   1.00 31.97  ? 11  PRO A CA  1 
ATOM   6    C  C   . PRO A 1 11  ? -12.433 14.683 2.156   1.00 26.13  ? 11  PRO A C   1 
ATOM   7    O  O   . PRO A 1 11  ? -12.025 14.061 1.176   1.00 27.20  ? 11  PRO A O   1 
ATOM   8    C  CB  . PRO A 1 11  ? -14.028 13.299 3.417   1.00 32.38  ? 11  PRO A CB  1 
ATOM   9    C  CG  . PRO A 1 11  ? -14.716 13.657 4.635   1.00 36.70  ? 11  PRO A CG  1 
ATOM   10   C  CD  . PRO A 1 11  ? -14.060 14.878 5.155   1.00 36.66  ? 11  PRO A CD  1 
ATOM   11   N  N   . LEU A 1 12  ? -12.727 15.963 2.106   1.00 26.77  ? 12  LEU A N   1 
ATOM   12   C  CA  . LEU A 1 12  ? -12.665 16.689 0.848   1.00 25.91  ? 12  LEU A CA  1 
ATOM   13   C  C   . LEU A 1 12  ? -12.117 18.067 1.080   1.00 27.82  ? 12  LEU A C   1 
ATOM   14   O  O   . LEU A 1 12  ? -12.687 18.824 1.886   1.00 32.32  ? 12  LEU A O   1 
ATOM   15   C  CB  . LEU A 1 12  ? -14.073 16.796 0.256   1.00 27.20  ? 12  LEU A CB  1 
ATOM   16   C  CG  . LEU A 1 12  ? -14.166 17.499 -1.093  1.00 30.00  ? 12  LEU A CG  1 
ATOM   17   C  CD1 . LEU A 1 12  ? -13.298 16.785 -2.120  1.00 28.10  ? 12  LEU A CD1 1 
ATOM   18   C  CD2 . LEU A 1 12  ? -15.658 17.594 -1.504  1.00 31.01  ? 12  LEU A CD2 1 
ATOM   19   N  N   . MET A 1 13  ? -10.985 18.356 0.443   1.00 25.68  ? 13  MET A N   1 
ATOM   20   C  CA  . MET A 1 13  ? -10.331 19.680 0.535   1.00 24.79  ? 13  MET A CA  1 
ATOM   21   C  C   . MET A 1 13  ? -10.041 20.189 -0.852  1.00 21.52  ? 13  MET A C   1 
ATOM   22   O  O   . MET A 1 13  ? -9.796  19.435 -1.762  1.00 22.93  ? 13  MET A O   1 
ATOM   23   C  CB  . MET A 1 13  ? -9.068  19.574 1.341   1.00 26.50  ? 13  MET A CB  1 
ATOM   24   C  CG  . MET A 1 13  ? -8.432  20.925 1.702   0.50 29.58  ? 13  MET A CG  1 
ATOM   25   S  SD  . MET A 1 13  ? -7.171  21.603 0.584   0.50 34.38  ? 13  MET A SD  1 
ATOM   26   C  CE  . MET A 1 13  ? -5.681  20.983 1.379   0.50 35.17  ? 13  MET A CE  1 
ATOM   27   N  N   . VAL A 1 14  ? -10.115 21.487 -1.038  1.00 21.28  ? 14  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 14  ? -9.890  22.134 -2.313  1.00 21.52  ? 14  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 14  ? -8.830  23.171 -2.079  1.00 23.99  ? 14  VAL A C   1 
ATOM   30   O  O   . VAL A 1 14  ? -8.942  23.981 -1.114  1.00 24.37  ? 14  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 14  ? -11.141 22.757 -2.881  1.00 20.84  ? 14  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 14  ? -10.841 23.546 -4.213  1.00 23.80  ? 14  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 14  ? -12.264 21.694 -3.080  1.00 24.51  ? 14  VAL A CG2 1 
ATOM   34   N  N   . LYS A 1 15  ? -7.855  23.182 -2.970  1.00 22.37  ? 15  LYS A N   1 
ATOM   35   C  CA  . LYS A 1 15  ? -6.743  24.107 -2.944  1.00 23.13  ? 15  LYS A CA  1 
ATOM   36   C  C   . LYS A 1 15  ? -6.576  24.799 -4.269  1.00 23.43  ? 15  LYS A C   1 
ATOM   37   O  O   . LYS A 1 15  ? -6.619  24.168 -5.305  1.00 21.55  ? 15  LYS A O   1 
ATOM   38   C  CB  . LYS A 1 15  ? -5.506  23.327 -2.646  1.00 24.05  ? 15  LYS A CB  1 
ATOM   39   C  CG  . LYS A 1 15  ? -4.173  24.039 -2.650  1.00 31.73  ? 15  LYS A CG  1 
ATOM   40   C  CD  . LYS A 1 15  ? -3.991  25.128 -1.638  1.00 36.55  ? 15  LYS A CD  1 
ATOM   41   C  CE  . LYS A 1 15  ? -2.520  25.603 -1.571  1.00 43.60  ? 15  LYS A CE  1 
ATOM   42   N  N   . VAL A 1 16  ? -6.450  26.116 -4.272  1.00 20.94  ? 16  VAL A N   1 
ATOM   43   C  CA  . VAL A 1 16  ? -6.392  26.842 -5.525  1.00 19.83  ? 16  VAL A CA  1 
ATOM   44   C  C   . VAL A 1 16  ? -5.196  27.819 -5.484  1.00 21.40  ? 16  VAL A C   1 
ATOM   45   O  O   . VAL A 1 16  ? -5.038  28.592 -4.516  1.00 22.89  ? 16  VAL A O   1 
ATOM   46   C  CB  . VAL A 1 16  ? -7.703  27.652 -5.761  1.00 21.07  ? 16  VAL A CB  1 
ATOM   47   C  CG1 . VAL A 1 16  ? -7.741  28.227 -7.191  1.00 21.96  ? 16  VAL A CG1 1 
ATOM   48   C  CG2 . VAL A 1 16  ? -8.985  26.742 -5.538  1.00 21.37  ? 16  VAL A CG2 1 
ATOM   49   N  N   . LEU A 1 17  ? -4.380  27.797 -6.544  1.00 20.71  ? 17  LEU A N   1 
ATOM   50   C  CA  . LEU A 1 17  ? -3.209  28.612 -6.675  1.00 20.68  ? 17  LEU A CA  1 
ATOM   51   C  C   . LEU A 1 17  ? -3.320  29.455 -7.935  1.00 21.89  ? 17  LEU A C   1 
ATOM   52   O  O   . LEU A 1 17  ? -3.925  29.017 -8.917  1.00 22.78  ? 17  LEU A O   1 
ATOM   53   C  CB  . LEU A 1 17  ? -1.984  27.733 -6.762  1.00 22.44  ? 17  LEU A CB  1 
ATOM   54   C  CG  . LEU A 1 17  ? -1.556  26.810 -5.555  1.00 28.38  ? 17  LEU A CG  1 
ATOM   55   C  CD1 . LEU A 1 17  ? -0.186  26.152 -5.935  1.00 31.37  ? 17  LEU A CD1 1 
ATOM   56   C  CD2 . LEU A 1 17  ? -1.391  27.718 -4.350  1.00 28.76  ? 17  LEU A CD2 1 
ATOM   57   N  N   . ASP A 1 18  ? -2.701  30.643 -7.875  1.00 20.48  ? 18  ASP A N   1 
ATOM   58   C  CA  . ASP A 1 18  ? -2.652  31.627 -8.993  1.00 21.20  ? 18  ASP A CA  1 
ATOM   59   C  C   . ASP A 1 18  ? -1.251  31.563 -9.604  1.00 23.00  ? 18  ASP A C   1 
ATOM   60   O  O   . ASP A 1 18  ? -0.263  31.860 -8.960  1.00 22.12  ? 18  ASP A O   1 
ATOM   61   C  CB  . ASP A 1 18  ? -3.015  32.952 -8.413  1.00 23.04  ? 18  ASP A CB  1 
ATOM   62   C  CG  . ASP A 1 18  ? -2.838  34.108 -9.341  1.00 26.18  ? 18  ASP A CG  1 
ATOM   63   O  OD1 . ASP A 1 18  ? -1.990  34.037 -10.272 1.00 26.33  ? 18  ASP A OD1 1 
ATOM   64   O  OD2 . ASP A 1 18  ? -3.535  35.125 -9.109  1.00 30.24  ? 18  ASP A OD2 1 
ATOM   65   N  N   . ALA A 1 19  ? -1.174  31.117 -10.856 1.00 20.84  ? 19  ALA A N   1 
ATOM   66   C  CA  . ALA A 1 19  ? 0.121   30.984 -11.567 1.00 20.92  ? 19  ALA A CA  1 
ATOM   67   C  C   . ALA A 1 19  ? 0.686   32.283 -12.152 1.00 22.47  ? 19  ALA A C   1 
ATOM   68   O  O   . ALA A 1 19  ? 1.850   32.288 -12.697 1.00 24.26  ? 19  ALA A O   1 
ATOM   69   C  CB  . ALA A 1 19  ? -0.032  29.856 -12.657 1.00 22.19  ? 19  ALA A CB  1 
ATOM   70   N  N   . VAL A 1 20  ? -0.076  33.383 -12.100 1.00 22.42  ? 20  VAL A N   1 
ATOM   71   C  CA  . VAL A 1 20  ? 0.368   34.727 -12.523 1.00 24.32  ? 20  VAL A CA  1 
ATOM   72   C  C   . VAL A 1 20  ? 1.104   35.394 -11.373 1.00 26.33  ? 20  VAL A C   1 
ATOM   73   O  O   . VAL A 1 20  ? 2.112   36.059 -11.658 1.00 31.84  ? 20  VAL A O   1 
ATOM   74   C  CB  . VAL A 1 20  ? -0.826  35.601 -13.020 1.00 26.97  ? 20  VAL A CB  1 
ATOM   75   C  CG1 . VAL A 1 20  ? -0.456  37.094 -13.279 1.00 29.84  ? 20  VAL A CG1 1 
ATOM   76   C  CG2 . VAL A 1 20  ? -1.459  34.974 -14.234 1.00 26.61  ? 20  VAL A CG2 1 
ATOM   77   N  N   . ARG A 1 21  ? 0.636   35.242 -10.133 1.00 23.50  ? 21  ARG A N   1 
ATOM   78   C  CA  . ARG A 1 21  ? 1.185   35.942 -8.981  1.00 26.61  ? 21  ARG A CA  1 
ATOM   79   C  C   . ARG A 1 21  ? 2.096   35.045 -8.153  1.00 27.45  ? 21  ARG A C   1 
ATOM   80   O  O   . ARG A 1 21  ? 2.812   35.513 -7.339  1.00 28.05  ? 21  ARG A O   1 
ATOM   81   C  CB  . ARG A 1 21  ? 0.021   36.446 -8.134  0.50 28.36  ? 21  ARG A CB  1 
ATOM   82   C  CG  . ARG A 1 21  ? -0.644  37.672 -8.753  0.50 31.44  ? 21  ARG A CG  1 
ATOM   83   C  CD  . ARG A 1 21  ? -2.163  37.581 -8.848  0.50 34.86  ? 21  ARG A CD  1 
ATOM   84   N  NE  . ARG A 1 21  ? -2.826  37.833 -7.583  0.50 35.78  ? 21  ARG A NE  1 
ATOM   85   C  CZ  . ARG A 1 21  ? -3.216  39.034 -7.186  0.50 39.32  ? 21  ARG A CZ  1 
ATOM   86   N  NH1 . ARG A 1 21  ? -3.071  40.065 -8.000  0.50 42.79  ? 21  ARG A NH1 1 
ATOM   87   N  NH2 . ARG A 1 21  ? -3.772  39.206 -6.006  0.50 41.04  ? 21  ARG A NH2 1 
ATOM   88   N  N   . GLY A 1 22  ? 2.027   33.744 -8.365  1.00 22.71  ? 22  GLY A N   1 
ATOM   89   C  CA  . GLY A 1 22  ? 2.715   32.723 -7.511  1.00 24.51  ? 22  GLY A CA  1 
ATOM   90   C  C   . GLY A 1 22  ? 2.248   32.745 -6.071  1.00 26.65  ? 22  GLY A C   1 
ATOM   91   O  O   . GLY A 1 22  ? 3.025   32.859 -5.109  1.00 25.11  ? 22  GLY A O   1 
ATOM   92   N  N   . SER A 1 23  ? 0.932   32.698 -5.899  1.00 25.08  ? 23  SER A N   1 
ATOM   93   C  CA  . SER A 1 23  ? 0.348   32.923 -4.613  1.00 26.80  ? 23  SER A CA  1 
ATOM   94   C  C   . SER A 1 23  ? -0.925  32.085 -4.542  1.00 24.84  ? 23  SER A C   1 
ATOM   95   O  O   . SER A 1 23  ? -1.476  31.689 -5.597  1.00 23.21  ? 23  SER A O   1 
ATOM   96   C  CB  . SER A 1 23  ? -0.019  34.402 -4.463  1.00 32.18  ? 23  SER A CB  1 
ATOM   97   O  OG  . SER A 1 23  ? -1.155  34.640 -5.344  1.00 37.09  ? 23  SER A OG  1 
ATOM   98   N  N   . PRO A 1 24  ? -1.369  31.755 -3.336  1.00 23.20  ? 24  PRO A N   1 
ATOM   99   C  CA  . PRO A 1 24  ? -2.721  31.149 -3.279  1.00 24.21  ? 24  PRO A CA  1 
ATOM   100  C  C   . PRO A 1 24  ? -3.775  32.090 -3.854  1.00 25.13  ? 24  PRO A C   1 
ATOM   101  O  O   . PRO A 1 24  ? -3.619  33.329 -3.889  1.00 25.15  ? 24  PRO A O   1 
ATOM   102  C  CB  . PRO A 1 24  ? -2.928  30.896 -1.797  1.00 28.34  ? 24  PRO A CB  1 
ATOM   103  C  CG  . PRO A 1 24  ? -2.069  31.885 -1.144  1.00 31.26  ? 24  PRO A CG  1 
ATOM   104  C  CD  . PRO A 1 24  ? -0.837  32.085 -2.017  1.00 28.45  ? 24  PRO A CD  1 
ATOM   105  N  N   . ALA A 1 25  ? -4.828  31.499 -4.358  1.00 22.57  ? 25  ALA A N   1 
ATOM   106  C  CA  . ALA A 1 25  ? -5.992  32.180 -4.923  1.00 22.56  ? 25  ALA A CA  1 
ATOM   107  C  C   . ALA A 1 25  ? -7.018  32.266 -3.769  1.00 22.49  ? 25  ALA A C   1 
ATOM   108  O  O   . ALA A 1 25  ? -7.581  31.258 -3.333  1.00 23.05  ? 25  ALA A O   1 
ATOM   109  C  CB  . ALA A 1 25  ? -6.537  31.390 -6.106  1.00 22.07  ? 25  ALA A CB  1 
ATOM   110  N  N   . ILE A 1 26  ? -7.101  33.471 -3.187  1.00 25.99  ? 26  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 26  ? -7.896  33.757 -2.020  1.00 27.60  ? 26  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 26  ? -9.344  34.197 -2.435  1.00 25.49  ? 26  ILE A C   1 
ATOM   113  O  O   . ILE A 1 26  ? -9.548  34.888 -3.463  1.00 24.34  ? 26  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 26  ? -7.202  34.930 -1.259  1.00 32.17  ? 26  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 26  ? -5.739  34.554 -0.919  1.00 33.30  ? 26  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 26  ? -7.954  35.350 0.011   1.00 34.32  ? 26  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 26  ? -4.949  35.787 -0.489  1.00 38.00  ? 26  ILE A CD1 1 
ATOM   118  N  N   . ASN A 1 27  ? -10.291 33.820 -1.597  1.00 26.08  ? 27  ASN A N   1 
ATOM   119  C  CA  A ASN A 1 27  ? -11.690 34.201 -1.751  0.50 28.21  ? 27  ASN A CA  1 
ATOM   120  C  CA  B ASN A 1 27  ? -11.701 34.171 -1.740  0.50 27.05  ? 27  ASN A CA  1 
ATOM   121  C  C   . ASN A 1 27  ? -12.352 33.708 -3.051  1.00 28.14  ? 27  ASN A C   1 
ATOM   122  O  O   . ASN A 1 27  ? -13.221 34.396 -3.635  1.00 27.37  ? 27  ASN A O   1 
ATOM   123  C  CB  A ASN A 1 27  ? -11.832 35.709 -1.571  0.50 33.48  ? 27  ASN A CB  1 
ATOM   124  C  CB  B ASN A 1 27  ? -11.923 35.655 -1.520  0.50 30.36  ? 27  ASN A CB  1 
ATOM   125  C  CG  A ASN A 1 27  ? -11.757 36.117 -0.117  0.50 36.01  ? 27  ASN A CG  1 
ATOM   126  C  CG  B ASN A 1 27  ? -13.352 35.956 -1.100  0.50 30.36  ? 27  ASN A CG  1 
ATOM   127  O  OD1 A ASN A 1 27  ? -11.043 37.064 0.236   0.50 44.15  ? 27  ASN A OD1 1 
ATOM   128  O  OD1 B ASN A 1 27  ? -14.015 35.130 -0.469  0.50 31.87  ? 27  ASN A OD1 1 
ATOM   129  N  ND2 A ASN A 1 27  ? -12.499 35.414 0.738   0.50 40.37  ? 27  ASN A ND2 1 
ATOM   130  N  ND2 B ASN A 1 27  ? -13.826 37.129 -1.442  0.50 32.19  ? 27  ASN A ND2 1 
ATOM   131  N  N   . VAL A 1 28  ? -11.975 32.507 -3.482  1.00 22.51  ? 28  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 28  ? -12.483 31.868 -4.666  1.00 22.85  ? 28  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 28  ? -13.658 31.059 -4.212  1.00 21.97  ? 28  VAL A C   1 
ATOM   134  O  O   . VAL A 1 28  ? -13.545 30.206 -3.309  1.00 22.89  ? 28  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 28  ? -11.475 30.952 -5.348  1.00 23.19  ? 28  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 28  ? -12.127 30.266 -6.572  1.00 22.96  ? 28  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 28  ? -10.214 31.757 -5.763  1.00 20.63  ? 28  VAL A CG2 1 
ATOM   138  N  N   . ALA A 1 29  ? -14.783 31.288 -4.860  1.00 20.60  ? 29  ALA A N   1 
ATOM   139  C  CA  . ALA A 1 29  ? -16.034 30.530 -4.525  1.00 22.50  ? 29  ALA A CA  1 
ATOM   140  C  C   . ALA A 1 29  ? -15.875 29.138 -5.115  1.00 21.45  ? 29  ALA A C   1 
ATOM   141  O  O   . ALA A 1 29  ? -15.430 28.969 -6.254  1.00 22.75  ? 29  ALA A O   1 
ATOM   142  C  CB  . ALA A 1 29  ? -17.263 31.264 -5.074  1.00 21.64  ? 29  ALA A CB  1 
ATOM   143  N  N   . VAL A 1 30  ? -16.354 28.133 -4.360  1.00 20.60  ? 30  VAL A N   1 
ATOM   144  C  CA  . VAL A 1 30  ? -16.378 26.760 -4.727  1.00 20.09  ? 30  VAL A CA  1 
ATOM   145  C  C   . VAL A 1 30  ? -17.716 26.127 -4.372  1.00 19.84  ? 30  VAL A C   1 
ATOM   146  O  O   . VAL A 1 30  ? -18.210 26.332 -3.242  1.00 22.81  ? 30  VAL A O   1 
ATOM   147  C  CB  . VAL A 1 30  ? -15.276 26.014 -3.949  1.00 23.01  ? 30  VAL A CB  1 
ATOM   148  C  CG1 . VAL A 1 30  ? -15.311 24.530 -4.267  1.00 23.65  ? 30  VAL A CG1 1 
ATOM   149  C  CG2 . VAL A 1 30  ? -13.891 26.670 -4.272  1.00 23.28  ? 30  VAL A CG2 1 
ATOM   150  N  N   . HIS A 1 31  ? -18.326 25.454 -5.364  1.00 21.40  ? 31  HIS A N   1 
ATOM   151  C  CA  . HIS A 1 31  ? -19.626 24.801 -5.198  1.00 22.51  ? 31  HIS A CA  1 
ATOM   152  C  C   . HIS A 1 31  ? -19.467 23.357 -5.557  1.00 21.48  ? 31  HIS A C   1 
ATOM   153  O  O   . HIS A 1 31  ? -18.891 23.014 -6.565  1.00 22.01  ? 31  HIS A O   1 
ATOM   154  C  CB  . HIS A 1 31  ? -20.673 25.420 -6.111  1.00 22.19  ? 31  HIS A CB  1 
ATOM   155  C  CG  . HIS A 1 31  ? -21.102 26.817 -5.698  1.00 27.13  ? 31  HIS A CG  1 
ATOM   156  N  ND1 . HIS A 1 31  ? -20.409 27.910 -6.038  1.00 32.71  ? 31  HIS A ND1 1 
ATOM   157  C  CD2 . HIS A 1 31  ? -22.196 27.247 -5.027  1.00 27.34  ? 31  HIS A CD2 1 
ATOM   158  C  CE1 . HIS A 1 31  ? -21.032 29.020 -5.566  1.00 27.45  ? 31  HIS A CE1 1 
ATOM   159  N  NE2 . HIS A 1 31  ? -22.120 28.622 -4.956  1.00 33.01  ? 31  HIS A NE2 1 
ATOM   160  N  N   . VAL A 1 32  ? -19.926 22.510 -4.647  1.00 21.06  ? 32  VAL A N   1 
ATOM   161  C  CA  . VAL A 1 32  ? -19.921 21.096 -4.805  1.00 18.90  ? 32  VAL A CA  1 
ATOM   162  C  C   . VAL A 1 32  ? -21.319 20.517 -4.958  1.00 21.89  ? 32  VAL A C   1 
ATOM   163  O  O   . VAL A 1 32  ? -22.248 20.950 -4.243  1.00 24.03  ? 32  VAL A O   1 
ATOM   164  C  CB  . VAL A 1 32  ? -19.250 20.398 -3.620  1.00 20.43  ? 32  VAL A CB  1 
ATOM   165  C  CG1 . VAL A 1 32  ? -19.136 18.891 -3.959  1.00 20.05  ? 32  VAL A CG1 1 
ATOM   166  C  CG2 . VAL A 1 32  ? -17.895 21.004 -3.367  1.00 22.73  ? 32  VAL A CG2 1 
ATOM   167  N  N   . PHE A 1 33  ? -21.460 19.601 -5.926  1.00 21.54  ? 33  PHE A N   1 
ATOM   168  C  CA  . PHE A 1 33  ? -22.740 18.994 -6.255  1.00 23.66  ? 33  PHE A CA  1 
ATOM   169  C  C   . PHE A 1 33  ? -22.539 17.492 -6.276  1.00 22.52  ? 33  PHE A C   1 
ATOM   170  O  O   . PHE A 1 33  ? -21.429 16.987 -6.430  1.00 23.13  ? 33  PHE A O   1 
ATOM   171  C  CB  . PHE A 1 33  ? -23.231 19.453 -7.639  1.00 23.52  ? 33  PHE A CB  1 
ATOM   172  C  CG  . PHE A 1 33  ? -23.337 20.933 -7.777  1.00 28.96  ? 33  PHE A CG  1 
ATOM   173  C  CD1 . PHE A 1 33  ? -22.221 21.700 -8.153  1.00 27.06  ? 33  PHE A CD1 1 
ATOM   174  C  CD2 . PHE A 1 33  ? -24.548 21.572 -7.522  1.00 28.31  ? 33  PHE A CD2 1 
ATOM   175  C  CE1 . PHE A 1 33  ? -22.319 23.101 -8.268  1.00 33.42  ? 33  PHE A CE1 1 
ATOM   176  C  CE2 . PHE A 1 33  ? -24.652 22.969 -7.627  1.00 32.30  ? 33  PHE A CE2 1 
ATOM   177  C  CZ  . PHE A 1 33  ? -23.526 23.746 -7.995  1.00 31.61  ? 33  PHE A CZ  1 
ATOM   178  N  N   . ARG A 1 34  ? -23.629 16.785 -6.082  1.00 24.56  ? 34  ARG A N   1 
ATOM   179  C  CA  . ARG A 1 34  ? -23.591 15.320 -6.125  1.00 23.26  ? 34  ARG A CA  1 
ATOM   180  C  C   . ARG A 1 34  ? -24.712 14.834 -7.008  1.00 27.15  ? 34  ARG A C   1 
ATOM   181  O  O   . ARG A 1 34  ? -25.853 15.315 -6.923  1.00 26.58  ? 34  ARG A O   1 
ATOM   182  C  CB  . ARG A 1 34  ? -23.768 14.753 -4.727  1.00 24.71  ? 34  ARG A CB  1 
ATOM   183  C  CG  . ARG A 1 34  ? -23.797 13.213 -4.695  1.00 25.83  ? 34  ARG A CG  1 
ATOM   184  C  CD  . ARG A 1 34  ? -23.963 12.614 -3.297  1.00 29.53  ? 34  ARG A CD  1 
ATOM   185  N  NE  . ARG A 1 34  ? -23.920 11.141 -3.342  1.00 29.93  ? 34  ARG A NE  1 
ATOM   186  C  CZ  . ARG A 1 34  ? -24.950 10.373 -3.657  1.00 31.30  ? 34  ARG A CZ  1 
ATOM   187  N  NH1 . ARG A 1 34  ? -26.157 10.895 -3.949  1.00 31.23  ? 34  ARG A NH1 1 
ATOM   188  N  NH2 . ARG A 1 34  ? -24.792 9.068  -3.660  1.00 31.68  ? 34  ARG A NH2 1 
ATOM   189  N  N   . LYS A 1 35  ? -24.448 13.806 -7.807  1.00 24.72  ? 35  LYS A N   1 
ATOM   190  C  CA  . LYS A 1 35  ? -25.427 13.364 -8.764  1.00 30.13  ? 35  LYS A CA  1 
ATOM   191  C  C   . LYS A 1 35  ? -26.480 12.529 -8.105  1.00 28.61  ? 35  LYS A C   1 
ATOM   192  O  O   . LYS A 1 35  ? -26.190 11.596 -7.353  1.00 29.83  ? 35  LYS A O   1 
ATOM   193  C  CB  . LYS A 1 35  ? -24.742 12.591 -9.924  1.00 31.14  ? 35  LYS A CB  1 
ATOM   194  C  CG  . LYS A 1 35  ? -25.641 12.427 -11.164 1.00 36.27  ? 35  LYS A CG  1 
ATOM   195  C  CD  . LYS A 1 35  ? -25.120 11.403 -12.197 1.00 36.91  ? 35  LYS A CD  1 
ATOM   196  N  N   . ALA A 1 36  ? -27.736 12.878 -8.349  1.00 31.29  ? 36  ALA A N   1 
ATOM   197  C  CA  . ALA A 1 36  ? -28.873 12.169 -7.739  1.00 36.06  ? 36  ALA A CA  1 
ATOM   198  C  C   . ALA A 1 36  ? -29.219 10.897 -8.501  1.00 39.34  ? 36  ALA A C   1 
ATOM   199  O  O   . ALA A 1 36  ? -28.768 10.720 -9.645  1.00 39.29  ? 36  ALA A O   1 
ATOM   200  C  CB  . ALA A 1 36  ? -30.102 13.102 -7.689  1.00 37.75  ? 36  ALA A CB  1 
ATOM   201  N  N   . ALA A 1 37  ? -30.030 10.051 -7.858  1.00 43.01  ? 37  ALA A N   1 
ATOM   202  C  CA  . ALA A 1 37  ? -30.680 8.873  -8.467  1.00 49.31  ? 37  ALA A CA  1 
ATOM   203  C  C   . ALA A 1 37  ? -31.378 9.179  -9.829  1.00 49.47  ? 37  ALA A C   1 
ATOM   204  O  O   . ALA A 1 37  ? -31.288 8.404  -10.748 1.00 48.82  ? 37  ALA A O   1 
ATOM   205  C  CB  . ALA A 1 37  ? -31.720 8.291  -7.485  1.00 52.34  ? 37  ALA A CB  1 
ATOM   206  N  N   . ASP A 1 38  ? -32.037 10.325 -9.946  1.00 52.58  ? 38  ASP A N   1 
ATOM   207  C  CA  . ASP A 1 38  ? -32.674 10.716 -11.217 1.00 56.73  ? 38  ASP A CA  1 
ATOM   208  C  C   . ASP A 1 38  ? -31.718 11.458 -12.180 1.00 56.93  ? 38  ASP A C   1 
ATOM   209  O  O   . ASP A 1 38  ? -32.172 12.172 -13.081 1.00 56.31  ? 38  ASP A O   1 
ATOM   210  C  CB  . ASP A 1 38  ? -33.933 11.549 -10.933 1.00 54.36  ? 38  ASP A CB  1 
ATOM   211  N  N   . ASP A 1 39  ? -30.399 11.302 -11.993 1.00 61.21  ? 39  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 39  ? -29.377 11.900 -12.903 1.00 54.09  ? 39  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 39  ? -29.210 13.439 -12.895 1.00 53.14  ? 39  ASP A C   1 
ATOM   214  O  O   . ASP A 1 39  ? -28.483 13.956 -13.733 1.00 54.07  ? 39  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 39  ? -29.598 11.435 -14.353 1.00 56.04  ? 39  ASP A CB  1 
ATOM   216  N  N   . THR A 1 40  ? -29.868 14.141 -11.963 1.00 46.87  ? 40  THR A N   1 
ATOM   217  C  CA  . THR A 1 40  ? -29.722 15.575 -11.722 1.00 45.21  ? 40  THR A CA  1 
ATOM   218  C  C   . THR A 1 40  ? -28.485 15.836 -10.823 1.00 40.59  ? 40  THR A C   1 
ATOM   219  O  O   . THR A 1 40  ? -28.136 14.966 -10.051 1.00 39.76  ? 40  THR A O   1 
ATOM   220  C  CB  . THR A 1 40  ? -30.992 16.114 -10.968 1.00 42.81  ? 40  THR A CB  1 
ATOM   221  N  N   . TRP A 1 41  ? -27.916 17.033 -10.883 1.00 43.03  ? 41  TRP A N   1 
ATOM   222  C  CA  . TRP A 1 41  ? -26.902 17.510 -9.896  1.00 38.46  ? 41  TRP A CA  1 
ATOM   223  C  C   . TRP A 1 41  ? -27.432 18.238 -8.688  1.00 38.38  ? 41  TRP A C   1 
ATOM   224  O  O   . TRP A 1 41  ? -27.766 19.415 -8.789  1.00 47.85  ? 41  TRP A O   1 
ATOM   225  C  CB  . TRP A 1 41  ? -25.954 18.481 -10.553 1.00 37.33  ? 41  TRP A CB  1 
ATOM   226  C  CG  . TRP A 1 41  ? -25.013 17.868 -11.516 1.00 39.87  ? 41  TRP A CG  1 
ATOM   227  C  CD1 . TRP A 1 41  ? -24.963 18.082 -12.889 1.00 42.57  ? 41  TRP A CD1 1 
ATOM   228  C  CD2 . TRP A 1 41  ? -23.927 16.935 -11.227 1.00 35.45  ? 41  TRP A CD2 1 
ATOM   229  N  NE1 . TRP A 1 41  ? -23.925 17.381 -13.446 1.00 43.26  ? 41  TRP A NE1 1 
ATOM   230  C  CE2 . TRP A 1 41  ? -23.266 16.667 -12.497 1.00 40.38  ? 41  TRP A CE2 1 
ATOM   231  C  CE3 . TRP A 1 41  ? -23.419 16.368 -10.084 1.00 34.06  ? 41  TRP A CE3 1 
ATOM   232  C  CZ2 . TRP A 1 41  ? -22.194 15.784 -12.591 1.00 37.15  ? 41  TRP A CZ2 1 
ATOM   233  C  CZ3 . TRP A 1 41  ? -22.338 15.507 -10.190 1.00 34.29  ? 41  TRP A CZ3 1 
ATOM   234  C  CH2 . TRP A 1 41  ? -21.744 15.223 -11.411 1.00 35.49  ? 41  TRP A CH2 1 
ATOM   235  N  N   . GLU A 1 42  ? -27.461 17.599 -7.526  1.00 32.51  ? 42  GLU A N   1 
ATOM   236  C  CA  . GLU A 1 42  ? -27.970 18.217 -6.268  1.00 33.78  ? 42  GLU A CA  1 
ATOM   237  C  C   . GLU A 1 42  ? -26.898 19.051 -5.508  1.00 29.74  ? 42  GLU A C   1 
ATOM   238  O  O   . GLU A 1 42  ? -25.745 18.590 -5.359  1.00 27.91  ? 42  GLU A O   1 
ATOM   239  C  CB  . GLU A 1 42  ? -28.451 17.129 -5.309  1.00 34.82  ? 42  GLU A CB  1 
ATOM   240  C  CG  . GLU A 1 42  ? -29.324 16.017 -5.921  1.00 42.52  ? 42  GLU A CG  1 
ATOM   241  N  N   . PRO A 1 43  ? -27.229 20.257 -5.018  1.00 29.89  ? 43  PRO A N   1 
ATOM   242  C  CA  . PRO A 1 43  ? -26.234 20.955 -4.209  1.00 30.01  ? 43  PRO A CA  1 
ATOM   243  C  C   . PRO A 1 43  ? -25.824 20.154 -2.982  1.00 32.27  ? 43  PRO A C   1 
ATOM   244  O  O   . PRO A 1 43  ? -26.674 19.620 -2.222  1.00 33.59  ? 43  PRO A O   1 
ATOM   245  C  CB  . PRO A 1 43  ? -26.978 22.230 -3.778  1.00 36.07  ? 43  PRO A CB  1 
ATOM   246  C  CG  . PRO A 1 43  ? -27.893 22.494 -4.961  1.00 38.43  ? 43  PRO A CG  1 
ATOM   247  C  CD  . PRO A 1 43  ? -28.425 21.097 -5.231  1.00 34.71  ? 43  PRO A CD  1 
ATOM   248  N  N   . PHE A 1 44  ? -24.525 20.052 -2.781  1.00 26.26  ? 44  PHE A N   1 
ATOM   249  C  CA  . PHE A 1 44  ? -23.915 19.225 -1.718  1.00 26.38  ? 44  PHE A CA  1 
ATOM   250  C  C   . PHE A 1 44  ? -23.207 20.124 -0.671  1.00 27.55  ? 44  PHE A C   1 
ATOM   251  O  O   . PHE A 1 44  ? -23.491 20.020 0.534   1.00 28.97  ? 44  PHE A O   1 
ATOM   252  C  CB  . PHE A 1 44  ? -22.991 18.185 -2.351  1.00 26.59  ? 44  PHE A CB  1 
ATOM   253  C  CG  . PHE A 1 44  ? -22.342 17.274 -1.366  1.00 26.16  ? 44  PHE A CG  1 
ATOM   254  C  CD1 . PHE A 1 44  ? -23.041 16.215 -0.844  1.00 30.01  ? 44  PHE A CD1 1 
ATOM   255  C  CD2 . PHE A 1 44  ? -21.042 17.475 -0.979  1.00 27.51  ? 44  PHE A CD2 1 
ATOM   256  C  CE1 . PHE A 1 44  ? -22.452 15.398 0.095   1.00 32.01  ? 44  PHE A CE1 1 
ATOM   257  C  CE2 . PHE A 1 44  ? -20.452 16.677 -0.033  1.00 31.28  ? 44  PHE A CE2 1 
ATOM   258  C  CZ  . PHE A 1 44  ? -21.157 15.617 0.468   1.00 31.91  ? 44  PHE A CZ  1 
ATOM   259  N  N   . ALA A 1 45  ? -22.392 21.096 -1.079  1.00 24.59  ? 45  ALA A N   1 
ATOM   260  C  CA  . ALA A 1 45  ? -21.673 21.975 -0.150  1.00 24.43  ? 45  ALA A CA  1 
ATOM   261  C  C   . ALA A 1 45  ? -21.051 23.112 -0.910  1.00 22.52  ? 45  ALA A C   1 
ATOM   262  O  O   . ALA A 1 45  ? -20.916 23.028 -2.128  1.00 22.36  ? 45  ALA A O   1 
ATOM   263  C  CB  . ALA A 1 45  ? -20.567 21.243 0.582   1.00 26.68  ? 45  ALA A CB  1 
ATOM   264  N  N   . SER A 1 46  ? -20.708 24.197 -0.207  1.00 23.87  ? 46  SER A N   1 
ATOM   265  C  CA  . SER A 1 46  ? -20.034 25.304 -0.892  1.00 23.84  ? 46  SER A CA  1 
ATOM   266  C  C   . SER A 1 46  ? -19.241 26.070 0.132   1.00 23.86  ? 46  SER A C   1 
ATOM   267  O  O   . SER A 1 46  ? -19.397 25.867 1.351   1.00 23.08  ? 46  SER A O   1 
ATOM   268  C  CB  . SER A 1 46  ? -21.085 26.190 -1.611  1.00 26.18  ? 46  SER A CB  1 
ATOM   269  O  OG  . SER A 1 46  ? -21.884 26.909 -0.702  1.00 24.91  ? 46  SER A OG  1 
ATOM   270  N  N   . GLY A 1 47  ? -18.343 26.916 -0.326  1.00 21.40  ? 47  GLY A N   1 
ATOM   271  C  CA  . GLY A 1 47  ? -17.430 27.621 0.529   1.00 23.65  ? 47  GLY A CA  1 
ATOM   272  C  C   . GLY A 1 47  ? -16.571 28.556 -0.285  1.00 24.02  ? 47  GLY A C   1 
ATOM   273  O  O   . GLY A 1 47  ? -16.762 28.671 -1.500  1.00 22.64  ? 47  GLY A O   1 
ATOM   274  N  N   . LYS A 1 48  ? -15.678 29.276 0.378   1.00 23.65  ? 48  LYS A N   1 
ATOM   275  C  CA  . LYS A 1 48  ? -14.693 30.034 -0.325  1.00 23.81  ? 48  LYS A CA  1 
ATOM   276  C  C   . LYS A 1 48  ? -13.271 29.769 0.236   1.00 20.74  ? 48  LYS A C   1 
ATOM   277  O  O   . LYS A 1 48  ? -13.068 29.434 1.397   1.00 24.65  ? 48  LYS A O   1 
ATOM   278  C  CB  . LYS A 1 48  ? -14.974 31.485 -0.341  1.00 27.20  ? 48  LYS A CB  1 
ATOM   279  C  CG  . LYS A 1 48  ? -14.943 32.119 0.969   1.00 31.05  ? 48  LYS A CG  1 
ATOM   280  N  N   . THR A 1 49  ? -12.321 29.873 -0.624  1.00 21.04  ? 49  THR A N   1 
ATOM   281  C  CA  . THR A 1 49  ? -10.925 29.590 -0.243  1.00 20.89  ? 49  THR A CA  1 
ATOM   282  C  C   . THR A 1 49  ? -10.438 30.666 0.749   1.00 23.16  ? 49  THR A C   1 
ATOM   283  O  O   . THR A 1 49  ? -10.780 31.910 0.664   1.00 23.18  ? 49  THR A O   1 
ATOM   284  C  CB  . THR A 1 49  ? -9.947  29.567 -1.458  1.00 20.83  ? 49  THR A CB  1 
ATOM   285  O  OG1 . THR A 1 49  ? -9.926  30.816 -2.138  1.00 21.95  ? 49  THR A OG1 1 
ATOM   286  C  CG2 . THR A 1 49  ? -10.254 28.453 -2.442  1.00 21.52  ? 49  THR A CG2 1 
ATOM   287  N  N   . SER A 1 50  ? -9.602  30.203 1.687   1.00 23.71  ? 50  SER A N   1 
ATOM   288  C  CA  . SER A 1 50  ? -9.042  31.074 2.742   1.00 26.40  ? 50  SER A CA  1 
ATOM   289  C  C   . SER A 1 50  ? -7.805  31.871 2.221   1.00 27.86  ? 50  SER A C   1 
ATOM   290  O  O   . SER A 1 50  ? -7.431  31.803 1.021   1.00 26.41  ? 50  SER A O   1 
ATOM   291  C  CB  . SER A 1 50  ? -8.587  30.173 3.899   1.00 28.22  ? 50  SER A CB  1 
ATOM   292  O  OG  . SER A 1 50  ? -7.428  29.494 3.461   1.00 29.78  ? 50  SER A OG  1 
ATOM   293  N  N   . GLU A 1 51  ? -7.190  32.635 3.144   1.00 29.94  ? 51  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 51  ? -5.942  33.337 2.853   1.00 33.13  ? 51  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 51  ? -4.823  32.387 2.396   1.00 32.62  ? 51  GLU A C   1 
ATOM   296  O  O   . GLU A 1 51  ? -3.895  32.793 1.659   1.00 33.87  ? 51  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 51  ? -5.538  34.256 4.050   1.00 33.07  ? 51  GLU A CB  1 
ATOM   298  N  N   . SER A 1 52  ? -4.948  31.095 2.677   1.00 30.16  ? 52  SER A N   1 
ATOM   299  C  CA  . SER A 1 52  ? -3.938  30.136 2.208   1.00 30.43  ? 52  SER A CA  1 
ATOM   300  C  C   . SER A 1 52  ? -4.338  29.417 0.917   1.00 27.73  ? 52  SER A C   1 
ATOM   301  O  O   . SER A 1 52  ? -3.626  28.540 0.452   1.00 26.53  ? 52  SER A O   1 
ATOM   302  C  CB  . SER A 1 52  ? -3.717  29.124 3.326   1.00 34.16  ? 52  SER A CB  1 
ATOM   303  O  OG  . SER A 1 52  ? -4.894  28.361 3.445   1.00 35.65  ? 52  SER A OG  1 
ATOM   304  N  N   . GLY A 1 53  ? -5.489  29.774 0.331   1.00 23.26  ? 53  GLY A N   1 
ATOM   305  C  CA  . GLY A 1 53  ? -6.004  29.157 -0.903  1.00 22.92  ? 53  GLY A CA  1 
ATOM   306  C  C   . GLY A 1 53  ? -6.701  27.878 -0.676  1.00 21.82  ? 53  GLY A C   1 
ATOM   307  O  O   . GLY A 1 53  ? -6.961  27.157 -1.627  1.00 24.21  ? 53  GLY A O   1 
ATOM   308  N  N   . GLU A 1 54  ? -6.941  27.561 0.575   1.00 23.28  ? 54  GLU A N   1 
ATOM   309  C  CA  . GLU A 1 54  ? -7.568  26.290 0.975   1.00 23.84  ? 54  GLU A CA  1 
ATOM   310  C  C   . GLU A 1 54  ? -9.005  26.448 1.404   1.00 24.17  ? 54  GLU A C   1 
ATOM   311  O  O   . GLU A 1 54  ? -9.434  27.508 1.954   1.00 25.30  ? 54  GLU A O   1 
ATOM   312  C  CB  . GLU A 1 54  ? -6.768  25.623 2.069   1.00 29.43  ? 54  GLU A CB  1 
ATOM   313  C  CG  . GLU A 1 54  ? -5.336  25.267 1.706   0.50 28.93  ? 54  GLU A CG  1 
ATOM   314  C  CD  . GLU A 1 54  ? -4.707  24.346 2.749   0.50 31.72  ? 54  GLU A CD  1 
ATOM   315  O  OE1 . GLU A 1 54  ? -4.959  24.526 3.933   0.50 34.81  ? 54  GLU A OE1 1 
ATOM   316  O  OE2 . GLU A 1 54  ? -3.958  23.434 2.378   0.50 40.75  ? 54  GLU A OE2 1 
ATOM   317  N  N   . LEU A 1 55  ? -9.799  25.395 1.123   1.00 23.84  ? 55  LEU A N   1 
ATOM   318  C  CA  . LEU A 1 55  ? -11.163 25.327 1.577   1.00 23.46  ? 55  LEU A CA  1 
ATOM   319  C  C   . LEU A 1 55  ? -11.327 23.983 2.245   1.00 23.39  ? 55  LEU A C   1 
ATOM   320  O  O   . LEU A 1 55  ? -11.224 22.933 1.583   1.00 24.98  ? 55  LEU A O   1 
ATOM   321  C  CB  . LEU A 1 55  ? -12.115 25.446 0.412   1.00 22.48  ? 55  LEU A CB  1 
ATOM   322  C  CG  . LEU A 1 55  ? -13.584 25.358 0.731   1.00 24.79  ? 55  LEU A CG  1 
ATOM   323  C  CD1 . LEU A 1 55  ? -14.081 26.122 1.925   1.00 25.65  ? 55  LEU A CD1 1 
ATOM   324  C  CD2 . LEU A 1 55  ? -14.276 25.747 -0.573  1.00 24.22  ? 55  LEU A CD2 1 
ATOM   325  N  N   . HIS A 1 56  ? -11.449 24.078 3.545   1.00 27.20  ? 56  HIS A N   1 
ATOM   326  C  CA  . HIS A 1 56  ? -11.628 22.912 4.439   1.00 31.16  ? 56  HIS A CA  1 
ATOM   327  C  C   . HIS A 1 56  ? -13.030 22.938 4.907   1.00 31.35  ? 56  HIS A C   1 
ATOM   328  O  O   . HIS A 1 56  ? -13.741 23.930 4.762   1.00 33.75  ? 56  HIS A O   1 
ATOM   329  C  CB  . HIS A 1 56  ? -10.742 23.079 5.671   1.00 34.28  ? 56  HIS A CB  1 
ATOM   330  C  CG  . HIS A 1 56  ? -9.285  22.938 5.374   1.00 39.69  ? 56  HIS A CG  1 
ATOM   331  N  ND1 . HIS A 1 56  ? -8.687  21.734 5.246   1.00 50.60  ? 56  HIS A ND1 1 
ATOM   332  C  CD2 . HIS A 1 56  ? -8.288  23.897 5.203   1.00 46.82  ? 56  HIS A CD2 1 
ATOM   333  C  CE1 . HIS A 1 56  ? -7.368  21.920 4.996   1.00 50.11  ? 56  HIS A CE1 1 
ATOM   334  N  NE2 . HIS A 1 56  ? -7.133  23.246 4.974   1.00 50.44  ? 56  HIS A NE2 1 
ATOM   335  N  N   . GLY A 1 57  ? -13.468 21.853 5.487   1.00 32.27  ? 57  GLY A N   1 
ATOM   336  C  CA  . GLY A 1 57  ? -14.777 21.880 6.171   1.00 31.96  ? 57  GLY A CA  1 
ATOM   337  C  C   . GLY A 1 57  ? -15.994 21.681 5.294   1.00 29.83  ? 57  GLY A C   1 
ATOM   338  O  O   . GLY A 1 57  ? -17.097 21.847 5.763   1.00 32.83  ? 57  GLY A O   1 
ATOM   339  N  N   . LEU A 1 58  ? -15.835 21.273 4.044   1.00 29.20  ? 58  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 58  ? -16.972 21.188 3.130   1.00 30.57  ? 58  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 58  ? -17.952 20.057 3.534   1.00 33.53  ? 58  LEU A C   1 
ATOM   342  O  O   . LEU A 1 58  ? -19.161 20.217 3.368   1.00 31.34  ? 58  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 58  ? -16.544 20.961 1.675   1.00 29.93  ? 58  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 58  ? -16.036 22.146 0.836   1.00 29.81  ? 58  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 58  ? -15.262 21.671 -0.387  1.00 29.88  ? 58  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 58  ? -17.207 23.077 0.486   1.00 29.62  ? 58  LEU A CD2 1 
ATOM   347  N  N   . THR A 1 59  ? -17.430 18.971 4.103   1.00 30.27  ? 59  THR A N   1 
ATOM   348  C  CA  . THR A 1 59  ? -18.230 17.777 4.387   1.00 31.15  ? 59  THR A CA  1 
ATOM   349  C  C   . THR A 1 59  ? -17.634 16.937 5.494   1.00 32.55  ? 59  THR A C   1 
ATOM   350  O  O   . THR A 1 59  ? -16.585 17.261 6.042   1.00 35.18  ? 59  THR A O   1 
ATOM   351  C  CB  . THR A 1 59  ? -18.437 16.891 3.118   1.00 30.56  ? 59  THR A CB  1 
ATOM   352  O  OG1 . THR A 1 59  ? -19.449 15.908 3.400   1.00 29.90  ? 59  THR A OG1 1 
ATOM   353  C  CG2 . THR A 1 59  ? -17.165 16.169 2.695   1.00 28.19  ? 59  THR A CG2 1 
ATOM   354  N  N   . THR A 1 60  ? -18.337 15.870 5.873   1.00 32.16  ? 60  THR A N   1 
ATOM   355  C  CA  . THR A 1 60  ? -17.891 15.015 6.956   1.00 31.24  ? 60  THR A CA  1 
ATOM   356  C  C   . THR A 1 60  ? -17.825 13.610 6.409   1.00 32.03  ? 60  THR A C   1 
ATOM   357  O  O   . THR A 1 60  ? -18.389 13.329 5.336   1.00 28.24  ? 60  THR A O   1 
ATOM   358  C  CB  . THR A 1 60  ? -18.865 15.043 8.139   1.00 34.65  ? 60  THR A CB  1 
ATOM   359  O  OG1 . THR A 1 60  ? -20.115 14.519 7.673   1.00 34.58  ? 60  THR A OG1 1 
ATOM   360  C  CG2 . THR A 1 60  ? -19.081 16.551 8.711   1.00 37.48  ? 60  THR A CG2 1 
ATOM   361  N  N   . GLU A 1 61  ? -17.172 12.699 7.133   1.00 33.52  ? 61  GLU A N   1 
ATOM   362  C  CA  . GLU A 1 61  ? -17.070 11.304 6.647   1.00 35.57  ? 61  GLU A CA  1 
ATOM   363  C  C   . GLU A 1 61  ? -18.431 10.622 6.473   1.00 37.23  ? 61  GLU A C   1 
ATOM   364  O  O   . GLU A 1 61  ? -18.596 9.846  5.532   1.00 39.81  ? 61  GLU A O   1 
ATOM   365  C  CB  . GLU A 1 61  ? -16.202 10.433 7.592   1.00 38.69  ? 61  GLU A CB  1 
ATOM   366  N  N   . GLU A 1 62  ? -19.373 10.904 7.370   1.00 35.64  ? 62  GLU A N   1 
ATOM   367  C  CA  . GLU A 1 62  ? -20.706 10.323 7.323   1.00 36.15  ? 62  GLU A CA  1 
ATOM   368  C  C   . GLU A 1 62  ? -21.492 10.823 6.085   1.00 32.47  ? 62  GLU A C   1 
ATOM   369  O  O   . GLU A 1 62  ? -22.148 10.064 5.426   1.00 31.79  ? 62  GLU A O   1 
ATOM   370  C  CB  . GLU A 1 62  ? -21.472 10.651 8.612   1.00 39.60  ? 62  GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 62  ? -22.081 12.046 8.751   0.50 40.76  ? 62  GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 62  ? -21.337 12.997 9.691   0.50 44.90  ? 62  GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 62  ? -20.220 12.653 10.188  0.50 46.68  ? 62  GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 62  ? -21.888 14.106 9.916   0.50 41.36  ? 62  GLU A OE2 1 
ATOM   375  N  N   . GLU A 1 63  ? -21.415 12.110 5.760   1.00 29.21  ? 63  GLU A N   1 
ATOM   376  C  CA  . GLU A 1 63  ? -22.261 12.656 4.658   1.00 28.97  ? 63  GLU A CA  1 
ATOM   377  C  C   . GLU A 1 63  ? -21.627 12.395 3.288   1.00 26.69  ? 63  GLU A C   1 
ATOM   378  O  O   . GLU A 1 63  ? -22.356 12.359 2.310   1.00 27.44  ? 63  GLU A O   1 
ATOM   379  C  CB  . GLU A 1 63  ? -22.481 14.145 4.943   1.00 30.00  ? 63  GLU A CB  1 
ATOM   380  C  CG  . GLU A 1 63  ? -22.605 15.045 3.736   1.00 30.00  ? 63  GLU A CG  1 
ATOM   381  C  CD  . GLU A 1 63  ? -22.497 16.512 4.118   1.00 30.00  ? 63  GLU A CD  1 
ATOM   382  O  OE1 . GLU A 1 63  ? -21.758 17.246 3.445   1.00 30.00  ? 63  GLU A OE1 1 
ATOM   383  O  OE2 . GLU A 1 63  ? -23.143 16.909 5.106   1.00 30.00  ? 63  GLU A OE2 1 
ATOM   384  N  N   . PHE A 1 64  ? -20.321 12.176 3.257   1.00 25.44  ? 64  PHE A N   1 
ATOM   385  C  CA  . PHE A 1 64  ? -19.577 12.043 2.004   1.00 26.43  ? 64  PHE A CA  1 
ATOM   386  C  C   . PHE A 1 64  ? -19.583 10.574 1.534   1.00 24.40  ? 64  PHE A C   1 
ATOM   387  O  O   . PHE A 1 64  ? -18.584 9.892  1.557   1.00 30.04  ? 64  PHE A O   1 
ATOM   388  C  CB  . PHE A 1 64  ? -18.166 12.531 2.166   1.00 26.21  ? 64  PHE A CB  1 
ATOM   389  C  CG  . PHE A 1 64  ? -17.389 12.676 0.874   1.00 26.01  ? 64  PHE A CG  1 
ATOM   390  C  CD1 . PHE A 1 64  ? -17.897 13.295 -0.234  1.00 25.75  ? 64  PHE A CD1 1 
ATOM   391  C  CD2 . PHE A 1 64  ? -16.057 12.263 0.857   1.00 29.85  ? 64  PHE A CD2 1 
ATOM   392  C  CE1 . PHE A 1 64  ? -17.126 13.455 -1.386  1.00 28.94  ? 64  PHE A CE1 1 
ATOM   393  C  CE2 . PHE A 1 64  ? -15.271 12.425 -0.289  1.00 29.91  ? 64  PHE A CE2 1 
ATOM   394  C  CZ  . PHE A 1 64  ? -15.811 13.023 -1.394  1.00 29.10  ? 64  PHE A CZ  1 
ATOM   395  N  N   . VAL A 1 65  ? -20.740 10.137 1.116   1.00 24.48  ? 65  VAL A N   1 
ATOM   396  C  CA  . VAL A 1 65  ? -20.971 8.743  0.685   1.00 23.77  ? 65  VAL A CA  1 
ATOM   397  C  C   . VAL A 1 65  ? -20.440 8.560  -0.726  1.00 24.17  ? 65  VAL A C   1 
ATOM   398  O  O   . VAL A 1 65  ? -20.129 9.544  -1.422  1.00 23.63  ? 65  VAL A O   1 
ATOM   399  C  CB  . VAL A 1 65  ? -22.505 8.425  0.809   1.00 24.72  ? 65  VAL A CB  1 
ATOM   400  C  CG1 . VAL A 1 65  ? -22.910 8.506  2.308   1.00 26.85  ? 65  VAL A CG1 1 
ATOM   401  C  CG2 . VAL A 1 65  ? -23.353 9.402  0.015   1.00 27.42  ? 65  VAL A CG2 1 
ATOM   402  N  N   . GLU A 1 66  ? -20.394 7.318  -1.178  1.00 25.29  ? 66  GLU A N   1 
ATOM   403  C  CA  . GLU A 1 66  ? -20.175 7.029  -2.580  1.00 27.98  ? 66  GLU A CA  1 
ATOM   404  C  C   . GLU A 1 66  ? -21.105 7.848  -3.457  1.00 27.81  ? 66  GLU A C   1 
ATOM   405  O  O   . GLU A 1 66  ? -22.318 8.009  -3.175  1.00 26.28  ? 66  GLU A O   1 
ATOM   406  C  CB  . GLU A 1 66  ? -20.521 5.612  -2.915  1.00 30.48  ? 66  GLU A CB  1 
ATOM   407  C  CG  . GLU A 1 66  ? -19.726 4.524  -2.265  1.00 36.33  ? 66  GLU A CG  1 
ATOM   408  C  CD  . GLU A 1 66  ? -20.034 3.156  -2.918  1.00 38.85  ? 66  GLU A CD  1 
ATOM   409  O  OE1 . GLU A 1 66  ? -20.782 2.325  -2.362  1.00 37.68  ? 66  GLU A OE1 1 
ATOM   410  O  OE2 . GLU A 1 66  ? -19.536 2.948  -4.042  1.00 40.45  ? 66  GLU A OE2 1 
ATOM   411  N  N   . GLY A 1 67  ? -20.558 8.341  -4.534  1.00 27.77  ? 67  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 67  ? -21.330 9.071  -5.514  1.00 27.00  ? 67  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 67  ? -20.462 9.693  -6.552  1.00 24.82  ? 67  GLY A C   1 
ATOM   414  O  O   . GLY A 1 67  ? -19.242 9.590  -6.490  1.00 23.18  ? 67  GLY A O   1 
ATOM   415  N  N   . ILE A 1 68  ? -21.091 10.337 -7.519  1.00 23.89  ? 68  ILE A N   1 
ATOM   416  C  CA  . ILE A 1 68  ? -20.359 11.163 -8.482  1.00 23.33  ? 68  ILE A CA  1 
ATOM   417  C  C   . ILE A 1 68  ? -20.555 12.587 -8.020  1.00 23.00  ? 68  ILE A C   1 
ATOM   418  O  O   . ILE A 1 68  ? -21.703 13.019 -7.761  1.00 22.96  ? 68  ILE A O   1 
ATOM   419  C  CB  . ILE A 1 68  ? -20.948 11.007 -9.882  1.00 26.39  ? 68  ILE A CB  1 
ATOM   420  C  CG1 . ILE A 1 68  ? -20.823 9.547  -10.273 1.00 29.41  ? 68  ILE A CG1 1 
ATOM   421  C  CG2 . ILE A 1 68  ? -20.213 11.894 -10.915 1.00 26.04  ? 68  ILE A CG2 1 
ATOM   422  C  CD1 . ILE A 1 68  ? -21.381 9.253  -11.655 1.00 33.47  ? 68  ILE A CD1 1 
ATOM   423  N  N   . TYR A 1 69  ? -19.451 13.261 -7.802  1.00 20.79  ? 69  TYR A N   1 
ATOM   424  C  CA  . TYR A 1 69  ? -19.365 14.603 -7.346  1.00 20.57  ? 69  TYR A CA  1 
ATOM   425  C  C   . TYR A 1 69  ? -18.817 15.553 -8.383  1.00 20.89  ? 69  TYR A C   1 
ATOM   426  O  O   . TYR A 1 69  ? -17.996 15.188 -9.176  1.00 22.92  ? 69  TYR A O   1 
ATOM   427  C  CB  . TYR A 1 69  ? -18.537 14.654 -6.049  1.00 18.92  ? 69  TYR A CB  1 
ATOM   428  C  CG  . TYR A 1 69  ? -19.198 13.922 -4.901  1.00 21.31  ? 69  TYR A CG  1 
ATOM   429  C  CD1 . TYR A 1 69  ? -19.077 12.590 -4.749  1.00 20.77  ? 69  TYR A CD1 1 
ATOM   430  C  CD2 . TYR A 1 69  ? -19.945 14.615 -3.976  1.00 21.78  ? 69  TYR A CD2 1 
ATOM   431  C  CE1 . TYR A 1 69  ? -19.631 11.910 -3.680  1.00 22.01  ? 69  TYR A CE1 1 
ATOM   432  C  CE2 . TYR A 1 69  ? -20.547 13.950 -2.906  1.00 23.16  ? 69  TYR A CE2 1 
ATOM   433  C  CZ  . TYR A 1 69  ? -20.375 12.590 -2.766  1.00 22.20  ? 69  TYR A CZ  1 
ATOM   434  O  OH  . TYR A 1 69  ? -21.008 11.979 -1.714  1.00 25.45  ? 69  TYR A OH  1 
ATOM   435  N  N   . LYS A 1 70  ? -19.276 16.769 -8.352  1.00 22.78  ? 70  LYS A N   1 
ATOM   436  C  CA  A LYS A 1 70  ? -18.763 17.847 -9.194  0.50 23.10  ? 70  LYS A CA  1 
ATOM   437  C  CA  B LYS A 1 70  ? -18.775 17.838 -9.185  0.50 24.09  ? 70  LYS A CA  1 
ATOM   438  C  C   . LYS A 1 70  ? -18.295 18.976 -8.301  1.00 23.00  ? 70  LYS A C   1 
ATOM   439  O  O   . LYS A 1 70  ? -19.028 19.453 -7.419  1.00 23.08  ? 70  LYS A O   1 
ATOM   440  C  CB  A LYS A 1 70  ? -19.851 18.379 -10.172 0.50 24.23  ? 70  LYS A CB  1 
ATOM   441  C  CB  B LYS A 1 70  ? -19.923 18.324 -10.081 0.50 26.71  ? 70  LYS A CB  1 
ATOM   442  C  CG  A LYS A 1 70  ? -19.468 19.735 -10.784 0.50 25.64  ? 70  LYS A CG  1 
ATOM   443  C  CG  B LYS A 1 70  ? -19.494 19.266 -11.183 0.50 30.26  ? 70  LYS A CG  1 
ATOM   444  C  CD  A LYS A 1 70  ? -20.251 20.164 -12.017 0.50 28.35  ? 70  LYS A CD  1 
ATOM   445  C  CD  B LYS A 1 70  ? -20.644 19.460 -12.163 0.50 35.08  ? 70  LYS A CD  1 
ATOM   446  C  CE  A LYS A 1 70  ? -21.722 20.435 -11.750 0.50 30.00  ? 70  LYS A CE  1 
ATOM   447  C  CE  B LYS A 1 70  ? -20.155 19.913 -13.539 0.50 37.17  ? 70  LYS A CE  1 
ATOM   448  N  NZ  A LYS A 1 70  ? -22.390 21.003 -12.980 0.50 30.74  ? 70  LYS A NZ  1 
ATOM   449  N  NZ  B LYS A 1 70  ? -21.306 19.861 -14.494 0.50 40.55  ? 70  LYS A NZ  1 
ATOM   450  N  N   . VAL A 1 71  ? -17.067 19.439 -8.479  1.00 20.75  ? 71  VAL A N   1 
ATOM   451  C  CA  . VAL A 1 71  ? -16.550 20.596 -7.794  1.00 23.29  ? 71  VAL A CA  1 
ATOM   452  C  C   . VAL A 1 71  ? -16.410 21.689 -8.843  1.00 23.07  ? 71  VAL A C   1 
ATOM   453  O  O   . VAL A 1 71  ? -15.648 21.477 -9.816  1.00 26.06  ? 71  VAL A O   1 
ATOM   454  C  CB  . VAL A 1 71  ? -15.187 20.273 -7.136  1.00 24.59  ? 71  VAL A CB  1 
ATOM   455  C  CG1 . VAL A 1 71  ? -14.569 21.540 -6.495  1.00 21.88  ? 71  VAL A CG1 1 
ATOM   456  C  CG2 . VAL A 1 71  ? -15.345 19.137 -6.146  1.00 26.67  ? 71  VAL A CG2 1 
ATOM   457  N  N   . GLU A 1 72  ? -17.095 22.819 -8.672  1.00 23.06  ? 72  GLU A N   1 
ATOM   458  C  CA  . GLU A 1 72  ? -17.056 23.934 -9.637  1.00 23.15  ? 72  GLU A CA  1 
ATOM   459  C  C   . GLU A 1 72  ? -16.383 25.103 -8.924  1.00 22.28  ? 72  GLU A C   1 
ATOM   460  O  O   . GLU A 1 72  ? -16.903 25.664 -7.932  1.00 23.24  ? 72  GLU A O   1 
ATOM   461  C  CB  . GLU A 1 72  ? -18.511 24.241 -10.012 1.00 28.16  ? 72  GLU A CB  1 
ATOM   462  C  CG  . GLU A 1 72  ? -18.837 24.947 -11.278 1.00 39.26  ? 72  GLU A CG  1 
ATOM   463  N  N   . ILE A 1 73  ? -15.249 25.514 -9.463  1.00 20.54  ? 73  ILE A N   1 
ATOM   464  C  CA  . ILE A 1 73  ? -14.441 26.602 -8.891  1.00 19.97  ? 73  ILE A CA  1 
ATOM   465  C  C   . ILE A 1 73  ? -14.720 27.811 -9.726  1.00 22.45  ? 73  ILE A C   1 
ATOM   466  O  O   . ILE A 1 73  ? -14.481 27.795 -10.936 1.00 22.63  ? 73  ILE A O   1 
ATOM   467  C  CB  . ILE A 1 73  ? -12.968 26.221 -8.993  1.00 22.44  ? 73  ILE A CB  1 
ATOM   468  C  CG1 . ILE A 1 73  ? -12.751 24.870 -8.318  1.00 25.55  ? 73  ILE A CG1 1 
ATOM   469  C  CG2 . ILE A 1 73  ? -12.071 27.242 -8.386  1.00 24.95  ? 73  ILE A CG2 1 
ATOM   470  C  CD1 . ILE A 1 73  ? -11.321 24.343 -8.298  1.00 25.04  ? 73  ILE A CD1 1 
ATOM   471  N  N   . ASP A 1 74  ? -15.131 28.904 -9.092  1.00 23.64  ? 74  ASP A N   1 
ATOM   472  C  CA  . ASP A 1 74  ? -15.550 30.132 -9.836  1.00 24.36  ? 74  ASP A CA  1 
ATOM   473  C  C   . ASP A 1 74  ? -14.296 30.988 -10.179 1.00 23.46  ? 74  ASP A C   1 
ATOM   474  O  O   . ASP A 1 74  ? -14.009 32.064 -9.628  1.00 23.96  ? 74  ASP A O   1 
ATOM   475  C  CB  . ASP A 1 74  ? -16.607 30.957 -9.104  1.00 27.10  ? 74  ASP A CB  1 
ATOM   476  C  CG  . ASP A 1 74  ? -17.013 32.212 -9.913  1.00 33.12  ? 74  ASP A CG  1 
ATOM   477  O  OD1 . ASP A 1 74  ? -16.615 32.301 -11.137 1.00 31.58  ? 74  ASP A OD1 1 
ATOM   478  O  OD2 . ASP A 1 74  ? -17.678 33.132 -9.334  1.00 39.56  ? 74  ASP A OD2 1 
ATOM   479  N  N   . THR A 1 75  ? -13.566 30.465 -11.181 1.00 23.76  ? 75  THR A N   1 
ATOM   480  C  CA  . THR A 1 75  ? -12.362 31.150 -11.612 1.00 23.21  ? 75  THR A CA  1 
ATOM   481  C  C   . THR A 1 75  ? -12.654 32.440 -12.332 1.00 22.20  ? 75  THR A C   1 
ATOM   482  O  O   . THR A 1 75  ? -11.885 33.378 -12.224 1.00 24.83  ? 75  THR A O   1 
ATOM   483  C  CB  . THR A 1 75  ? -11.592 30.246 -12.540 1.00 21.94  ? 75  THR A CB  1 
ATOM   484  O  OG1 . THR A 1 75  ? -12.371 29.880 -13.690 1.00 22.52  ? 75  THR A OG1 1 
ATOM   485  C  CG2 . THR A 1 75  ? -11.127 29.006 -11.768 1.00 24.98  ? 75  THR A CG2 1 
ATOM   486  N  N   . LYS A 1 76  ? -13.781 32.550 -13.033 1.00 22.64  ? 76  LYS A N   1 
ATOM   487  C  CA  . LYS A 1 76  ? -14.029 33.801 -13.760 1.00 25.58  ? 76  LYS A CA  1 
ATOM   488  C  C   . LYS A 1 76  ? -14.149 35.018 -12.811 1.00 27.23  ? 76  LYS A C   1 
ATOM   489  O  O   . LYS A 1 76  ? -13.515 36.031 -13.069 1.00 27.53  ? 76  LYS A O   1 
ATOM   490  C  CB  . LYS A 1 76  ? -15.235 33.679 -14.659 1.00 28.04  ? 76  LYS A CB  1 
ATOM   491  C  CG  . LYS A 1 76  ? -15.570 34.899 -15.539 1.00 32.70  ? 76  LYS A CG  1 
ATOM   492  C  CD  . LYS A 1 76  ? -17.003 34.819 -16.061 1.00 36.80  ? 76  LYS A CD  1 
ATOM   493  C  CE  . LYS A 1 76  ? -17.405 35.958 -17.006 1.00 40.59  ? 76  LYS A CE  1 
ATOM   494  N  NZ  . LYS A 1 76  ? -17.242 35.611 -18.453 1.00 45.80  ? 76  LYS A NZ  1 
ATOM   495  N  N   . SER A 1 77  ? -14.927 34.896 -11.716 1.00 26.91  ? 77  SER A N   1 
ATOM   496  C  CA  . SER A 1 77  ? -15.035 36.003 -10.764 1.00 27.34  ? 77  SER A CA  1 
ATOM   497  C  C   . SER A 1 77  ? -13.689 36.352 -10.150 1.00 27.68  ? 77  SER A C   1 
ATOM   498  O  O   . SER A 1 77  ? -13.382 37.524 -9.947  1.00 27.74  ? 77  SER A O   1 
ATOM   499  C  CB  . SER A 1 77  ? -16.106 35.750 -9.658  1.00 30.28  ? 77  SER A CB  1 
ATOM   500  O  OG  . SER A 1 77  ? -17.366 35.517 -10.261 1.00 31.15  ? 77  SER A OG  1 
ATOM   501  N  N   . TYR A 1 78  ? -12.887 35.349 -9.828  1.00 25.45  ? 78  TYR A N   1 
ATOM   502  C  CA  . TYR A 1 78  ? -11.522 35.553 -9.367  1.00 26.02  ? 78  TYR A CA  1 
ATOM   503  C  C   . TYR A 1 78  ? -10.692 36.474 -10.325 1.00 27.20  ? 78  TYR A C   1 
ATOM   504  O  O   . TYR A 1 78  ? -10.054 37.475 -9.865  1.00 25.96  ? 78  TYR A O   1 
ATOM   505  C  CB  . TYR A 1 78  ? -10.815 34.231 -9.170  1.00 25.37  ? 78  TYR A CB  1 
ATOM   506  C  CG  . TYR A 1 78  ? -9.376  34.414 -8.728  1.00 23.41  ? 78  TYR A CG  1 
ATOM   507  C  CD1 . TYR A 1 78  ? -9.105  34.814 -7.378  1.00 23.43  ? 78  TYR A CD1 1 
ATOM   508  C  CD2 . TYR A 1 78  ? -8.316  34.234 -9.599  1.00 23.43  ? 78  TYR A CD2 1 
ATOM   509  C  CE1 . TYR A 1 78  ? -7.841  34.968 -6.920  1.00 26.70  ? 78  TYR A CE1 1 
ATOM   510  C  CE2 . TYR A 1 78  ? -6.990  34.457 -9.163  1.00 23.64  ? 78  TYR A CE2 1 
ATOM   511  C  CZ  . TYR A 1 78  ? -6.774  34.794 -7.824  1.00 24.53  ? 78  TYR A CZ  1 
ATOM   512  O  OH  . TYR A 1 78  ? -5.500  35.003 -7.297  1.00 27.86  ? 78  TYR A OH  1 
ATOM   513  N  N   . TRP A 1 79  ? -10.631 36.133 -11.613 1.00 23.16  ? 79  TRP A N   1 
ATOM   514  C  CA  . TRP A 1 79  ? -9.816  36.940 -12.573 1.00 23.93  ? 79  TRP A CA  1 
ATOM   515  C  C   . TRP A 1 79  ? -10.377 38.308 -12.804 1.00 25.63  ? 79  TRP A C   1 
ATOM   516  O  O   . TRP A 1 79  ? -9.652  39.338 -12.792 1.00 26.59  ? 79  TRP A O   1 
ATOM   517  C  CB  . TRP A 1 79  ? -9.693  36.182 -13.874 1.00 22.79  ? 79  TRP A CB  1 
ATOM   518  C  CG  . TRP A 1 79  ? -8.846  34.989 -13.720 1.00 22.60  ? 79  TRP A CG  1 
ATOM   519  C  CD1 . TRP A 1 79  ? -9.191  33.669 -13.918 1.00 22.10  ? 79  TRP A CD1 1 
ATOM   520  C  CD2 . TRP A 1 79  ? -7.427  34.972 -13.340 1.00 23.93  ? 79  TRP A CD2 1 
ATOM   521  N  NE1 . TRP A 1 79  ? -8.098  32.857 -13.741 1.00 21.38  ? 79  TRP A NE1 1 
ATOM   522  C  CE2 . TRP A 1 79  ? -7.013  33.601 -13.396 1.00 22.86  ? 79  TRP A CE2 1 
ATOM   523  C  CE3 . TRP A 1 79  ? -6.452  35.966 -13.042 1.00 25.13  ? 79  TRP A CE3 1 
ATOM   524  C  CZ2 . TRP A 1 79  ? -5.741  33.230 -13.069 1.00 22.86  ? 79  TRP A CZ2 1 
ATOM   525  C  CZ3 . TRP A 1 79  ? -5.162  35.537 -12.702 1.00 22.91  ? 79  TRP A CZ3 1 
ATOM   526  C  CH2 . TRP A 1 79  ? -4.839  34.190 -12.715 1.00 25.09  ? 79  TRP A CH2 1 
ATOM   527  N  N   . LYS A 1 80  ? -11.698 38.376 -12.926 1.00 26.28  ? 80  LYS A N   1 
ATOM   528  C  CA  . LYS A 1 80  ? -12.354 39.659 -13.179 1.00 28.44  ? 80  LYS A CA  1 
ATOM   529  C  C   . LYS A 1 80  ? -12.092 40.641 -12.060 1.00 30.80  ? 80  LYS A C   1 
ATOM   530  O  O   . LYS A 1 80  ? -11.858 41.848 -12.366 1.00 31.39  ? 80  LYS A O   1 
ATOM   531  C  CB  . LYS A 1 80  ? -13.841 39.517 -13.450 1.00 28.87  ? 80  LYS A CB  1 
ATOM   532  C  CG  . LYS A 1 80  ? -14.152 38.856 -14.768 1.00 30.62  ? 80  LYS A CG  1 
ATOM   533  C  CD  . LYS A 1 80  ? -15.653 38.590 -14.884 1.00 39.37  ? 80  LYS A CD  1 
ATOM   534  N  N   . ALA A 1 81  ? -12.057 40.170 -10.809 1.00 31.71  ? 81  ALA A N   1 
ATOM   535  C  CA  . ALA A 1 81  ? -11.737 41.104 -9.653  1.00 32.86  ? 81  ALA A CA  1 
ATOM   536  C  C   . ALA A 1 81  ? -10.314 41.632 -9.676  1.00 35.43  ? 81  ALA A C   1 
ATOM   537  O  O   . ALA A 1 81  ? -10.033 42.689 -9.131  1.00 36.58  ? 81  ALA A O   1 
ATOM   538  C  CB  . ALA A 1 81  ? -12.060 40.467 -8.296  1.00 35.86  ? 81  ALA A CB  1 
ATOM   539  N  N   . LEU A 1 82  ? -9.410  40.922 -10.331 1.00 33.19  ? 82  LEU A N   1 
ATOM   540  C  CA  . LEU A 1 82  ? -8.072  41.387 -10.611 1.00 34.18  ? 82  LEU A CA  1 
ATOM   541  C  C   . LEU A 1 82  ? -7.908  42.139 -11.934 1.00 35.84  ? 82  LEU A C   1 
ATOM   542  O  O   . LEU A 1 82  ? -6.775  42.436 -12.304 1.00 37.31  ? 82  LEU A O   1 
ATOM   543  C  CB  . LEU A 1 82  ? -7.132  40.160 -10.616 1.00 34.64  ? 82  LEU A CB  1 
ATOM   544  C  CG  . LEU A 1 82  ? -7.128  39.459 -9.271  1.00 36.73  ? 82  LEU A CG  1 
ATOM   545  C  CD1 . LEU A 1 82  ? -6.342  38.149 -9.340  1.00 34.80  ? 82  LEU A CD1 1 
ATOM   546  C  CD2 . LEU A 1 82  ? -6.531  40.444 -8.251  1.00 37.08  ? 82  LEU A CD2 1 
ATOM   547  N  N   . GLY A 1 83  ? -8.996  42.441 -12.653 1.00 32.57  ? 83  GLY A N   1 
ATOM   548  C  CA  . GLY A 1 83  ? -8.949  43.205 -13.901 1.00 34.26  ? 83  GLY A CA  1 
ATOM   549  C  C   . GLY A 1 83  ? -8.712  42.386 -15.168 1.00 35.19  ? 83  GLY A C   1 
ATOM   550  O  O   . GLY A 1 83  ? -8.513  42.967 -16.268 1.00 34.90  ? 83  GLY A O   1 
ATOM   551  N  N   . ILE A 1 84  ? -8.741  41.055 -15.024 1.00 29.11  ? 84  ILE A N   1 
ATOM   552  C  CA  . ILE A 1 84  ? -8.490  40.148 -16.162 1.00 32.49  ? 84  ILE A CA  1 
ATOM   553  C  C   . ILE A 1 84  ? -9.803  39.587 -16.662 1.00 34.02  ? 84  ILE A C   1 
ATOM   554  O  O   . ILE A 1 84  ? -10.667 39.160 -15.875 1.00 31.62  ? 84  ILE A O   1 
ATOM   555  C  CB  . ILE A 1 84  ? -7.489  39.028 -15.749 1.00 29.46  ? 84  ILE A CB  1 
ATOM   556  C  CG1 . ILE A 1 84  ? -6.141  39.736 -15.445 1.00 36.86  ? 84  ILE A CG1 1 
ATOM   557  C  CG2 . ILE A 1 84  ? -7.414  37.920 -16.809 1.00 32.47  ? 84  ILE A CG2 1 
ATOM   558  C  CD1 . ILE A 1 84  ? -5.186  39.027 -14.532 1.00 36.58  ? 84  ILE A CD1 1 
ATOM   559  N  N   . SER A 1 85  ? -9.961  39.588 -17.982 1.00 33.79  ? 85  SER A N   1 
ATOM   560  C  CA  . SER A 1 85  ? -11.021 38.813 -18.650 1.00 31.53  ? 85  SER A CA  1 
ATOM   561  C  C   . SER A 1 85  ? -10.496 37.466 -19.075 1.00 31.54  ? 85  SER A C   1 
ATOM   562  O  O   . SER A 1 85  ? -9.861  37.343 -20.117 1.00 32.30  ? 85  SER A O   1 
ATOM   563  C  CB  . SER A 1 85  ? -11.519 39.579 -19.897 1.00 36.04  ? 85  SER A CB  1 
ATOM   564  O  OG  . SER A 1 85  ? -12.016 40.844 -19.501 1.00 37.06  ? 85  SER A OG  1 
ATOM   565  N  N   . PRO A 1 86  ? -10.828 36.420 -18.325 1.00 27.83  ? 86  PRO A N   1 
ATOM   566  C  CA  . PRO A 1 86  ? -10.262 35.091 -18.520 1.00 25.80  ? 86  PRO A CA  1 
ATOM   567  C  C   . PRO A 1 86  ? -11.008 34.299 -19.572 1.00 24.80  ? 86  PRO A C   1 
ATOM   568  O  O   . PRO A 1 86  ? -12.093 34.686 -20.000 1.00 27.31  ? 86  PRO A O   1 
ATOM   569  C  CB  . PRO A 1 86  ? -10.429 34.494 -17.150 1.00 26.16  ? 86  PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 86  ? -11.740 35.037 -16.718 1.00 28.98  ? 86  PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 86  ? -11.800 36.437 -17.219 1.00 30.33  ? 86  PRO A CD  1 
ATOM   572  N  N   . PHE A 1 87  ? -10.447 33.192 -20.010 1.00 24.69  ? 87  PHE A N   1 
ATOM   573  C  CA  . PHE A 1 87  ? -11.104 32.371 -21.019 1.00 25.98  ? 87  PHE A CA  1 
ATOM   574  C  C   . PHE A 1 87  ? -12.243 31.535 -20.452 1.00 25.78  ? 87  PHE A C   1 
ATOM   575  O  O   . PHE A 1 87  ? -13.347 31.499 -21.031 1.00 27.16  ? 87  PHE A O   1 
ATOM   576  C  CB  . PHE A 1 87  ? -10.110 31.479 -21.648 1.00 26.76  ? 87  PHE A CB  1 
ATOM   577  C  CG  . PHE A 1 87  ? -10.689 30.621 -22.675 1.00 29.71  ? 87  PHE A CG  1 
ATOM   578  C  CD1 . PHE A 1 87  ? -10.987 31.133 -23.907 1.00 31.97  ? 87  PHE A CD1 1 
ATOM   579  C  CD2 . PHE A 1 87  ? -10.899 29.309 -22.403 1.00 31.12  ? 87  PHE A CD2 1 
ATOM   580  C  CE1 . PHE A 1 87  ? -11.543 30.315 -24.874 1.00 33.12  ? 87  PHE A CE1 1 
ATOM   581  C  CE2 . PHE A 1 87  ? -11.431 28.493 -23.360 1.00 35.27  ? 87  PHE A CE2 1 
ATOM   582  C  CZ  . PHE A 1 87  ? -11.719 28.980 -24.581 1.00 30.92  ? 87  PHE A CZ  1 
ATOM   583  N  N   . HIS A 1 88  ? -11.980 30.848 -19.346 1.00 24.02  ? 88  HIS A N   1 
ATOM   584  C  CA  . HIS A 1 88  ? -12.956 29.871 -18.810 1.00 23.38  ? 88  HIS A CA  1 
ATOM   585  C  C   . HIS A 1 88  ? -14.029 30.471 -17.924 1.00 23.75  ? 88  HIS A C   1 
ATOM   586  O  O   . HIS A 1 88  ? -13.762 31.438 -17.219 1.00 24.01  ? 88  HIS A O   1 
ATOM   587  C  CB  . HIS A 1 88  ? -12.236 28.833 -18.026 1.00 22.82  ? 88  HIS A CB  1 
ATOM   588  C  CG  . HIS A 1 88  ? -11.210 28.111 -18.812 1.00 25.32  ? 88  HIS A CG  1 
ATOM   589  N  ND1 . HIS A 1 88  ? -9.878  28.526 -18.854 1.00 25.50  ? 88  HIS A ND1 1 
ATOM   590  C  CD2 . HIS A 1 88  ? -11.302 26.974 -19.613 1.00 29.33  ? 88  HIS A CD2 1 
ATOM   591  C  CE1 . HIS A 1 88  ? -9.194  27.713 -19.692 1.00 29.69  ? 88  HIS A CE1 1 
ATOM   592  N  NE2 . HIS A 1 88  ? -10.038 26.724 -20.118 1.00 32.61  ? 88  HIS A NE2 1 
ATOM   593  N  N   . GLU A 1 89  ? -15.226 29.937 -17.968 1.00 23.83  ? 89  GLU A N   1 
ATOM   594  C  CA  . GLU A 1 89  ? -16.294 30.367 -17.051 1.00 24.64  ? 89  GLU A CA  1 
ATOM   595  C  C   . GLU A 1 89  ? -16.016 29.890 -15.617 1.00 24.62  ? 89  GLU A C   1 
ATOM   596  O  O   . GLU A 1 89  ? -16.270 30.627 -14.618 1.00 26.93  ? 89  GLU A O   1 
ATOM   597  C  CB  . GLU A 1 89  ? -17.624 29.810 -17.517 1.00 27.63  ? 89  GLU A CB  1 
ATOM   598  C  CG  . GLU A 1 89  ? -18.110 30.480 -18.781 1.00 29.22  ? 89  GLU A CG  1 
ATOM   599  C  CD  . GLU A 1 89  ? -18.398 31.964 -18.619 0.50 27.49  ? 89  GLU A CD  1 
ATOM   600  O  OE1 . GLU A 1 89  ? -19.259 32.315 -17.817 0.50 28.60  ? 89  GLU A OE1 1 
ATOM   601  O  OE2 . GLU A 1 89  ? -17.803 32.783 -19.328 0.50 24.69  ? 89  GLU A OE2 1 
ATOM   602  N  N   . HIS A 1 90  ? -15.492 28.686 -15.512 1.00 25.87  ? 90  HIS A N   1 
ATOM   603  C  CA  . HIS A 1 90  ? -15.131 28.066 -14.239 1.00 28.98  ? 90  HIS A CA  1 
ATOM   604  C  C   . HIS A 1 90  ? -14.210 26.950 -14.497 1.00 28.65  ? 90  HIS A C   1 
ATOM   605  O  O   . HIS A 1 90  ? -13.926 26.664 -15.645 1.00 27.69  ? 90  HIS A O   1 
ATOM   606  C  CB  . HIS A 1 90  ? -16.374 27.581 -13.477 1.00 31.45  ? 90  HIS A CB  1 
ATOM   607  C  CG  . HIS A 1 90  ? -17.264 26.661 -14.251 1.00 33.80  ? 90  HIS A CG  1 
ATOM   608  N  ND1 . HIS A 1 90  ? -16.874 25.417 -14.606 1.00 41.23  ? 90  HIS A ND1 1 
ATOM   609  C  CD2 . HIS A 1 90  ? -18.547 26.823 -14.729 1.00 38.60  ? 90  HIS A CD2 1 
ATOM   610  C  CE1 . HIS A 1 90  ? -17.869 24.814 -15.307 1.00 38.80  ? 90  HIS A CE1 1 
ATOM   611  N  NE2 . HIS A 1 90  ? -18.902 25.660 -15.350 1.00 41.64  ? 90  HIS A NE2 1 
ATOM   612  N  N   . ALA A 1 91  ? -13.661 26.314 -13.457 1.00 26.50  ? 91  ALA A N   1 
ATOM   613  C  CA  . ALA A 1 91  ? -12.979 25.044 -13.613 1.00 27.65  ? 91  ALA A CA  1 
ATOM   614  C  C   . ALA A 1 91  ? -13.869 24.008 -12.913 1.00 33.90  ? 91  ALA A C   1 
ATOM   615  O  O   . ALA A 1 91  ? -14.294 24.224 -11.808 1.00 27.71  ? 91  ALA A O   1 
ATOM   616  C  CB  . ALA A 1 91  ? -11.593 25.079 -13.006 1.00 29.74  ? 91  ALA A CB  1 
ATOM   617  N  N   . GLU A 1 92  ? -14.183 22.883 -13.547 1.00 33.96  ? 92  GLU A N   1 
ATOM   618  C  CA  . GLU A 1 92  ? -15.093 21.942 -12.917 1.00 36.73  ? 92  GLU A CA  1 
ATOM   619  C  C   . GLU A 1 92  ? -14.418 20.585 -12.910 1.00 34.49  ? 92  GLU A C   1 
ATOM   620  O  O   . GLU A 1 92  ? -13.766 20.241 -13.887 1.00 39.54  ? 92  GLU A O   1 
ATOM   621  C  CB  . GLU A 1 92  ? -16.406 21.889 -13.676 1.00 40.27  ? 92  GLU A CB  1 
ATOM   622  C  CG  . GLU A 1 92  ? -17.023 20.512 -13.716 1.00 42.27  ? 92  GLU A CG  1 
ATOM   623  N  N   . VAL A 1 93  ? -14.448 19.872 -11.783 1.00 27.13  ? 93  VAL A N   1 
ATOM   624  C  CA  . VAL A 1 93  ? -13.799 18.599 -11.675 1.00 25.22  ? 93  VAL A CA  1 
ATOM   625  C  C   . VAL A 1 93  ? -14.936 17.627 -11.355 1.00 24.34  ? 93  VAL A C   1 
ATOM   626  O  O   . VAL A 1 93  ? -15.691 17.903 -10.426 1.00 24.35  ? 93  VAL A O   1 
ATOM   627  C  CB  . VAL A 1 93  ? -12.823 18.698 -10.502 1.00 34.14  ? 93  VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 93  ? -12.197 17.354 -10.198 1.00 35.92  ? 93  VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 93  ? -11.790 19.802 -10.762 1.00 38.71  ? 93  VAL A CG2 1 
ATOM   630  N  N   . VAL A 1 94  ? -15.068 16.513 -12.070 1.00 23.95  ? 94  VAL A N   1 
ATOM   631  C  CA  . VAL A 1 94  ? -16.147 15.614 -11.867 1.00 23.68  ? 94  VAL A CA  1 
ATOM   632  C  C   . VAL A 1 94  ? -15.562 14.251 -11.699 1.00 23.00  ? 94  VAL A C   1 
ATOM   633  O  O   . VAL A 1 94  ? -14.721 13.837 -12.487 1.00 22.71  ? 94  VAL A O   1 
ATOM   634  C  CB  . VAL A 1 94  ? -17.121 15.565 -13.079 1.00 25.66  ? 94  VAL A CB  1 
ATOM   635  C  CG1 . VAL A 1 94  ? -18.198 14.532 -12.786 1.00 25.73  ? 94  VAL A CG1 1 
ATOM   636  C  CG2 . VAL A 1 94  ? -17.662 16.950 -13.384 1.00 27.76  ? 94  VAL A CG2 1 
ATOM   637  N  N   . PHE A 1 95  ? -15.946 13.579 -10.638 1.00 22.76  ? 95  PHE A N   1 
ATOM   638  C  CA  . PHE A 1 95  ? -15.283 12.353 -10.210 1.00 22.49  ? 95  PHE A CA  1 
ATOM   639  C  C   . PHE A 1 95  ? -16.171 11.491 -9.363  1.00 24.04  ? 95  PHE A C   1 
ATOM   640  O  O   . PHE A 1 95  ? -17.016 11.965 -8.673  1.00 23.24  ? 95  PHE A O   1 
ATOM   641  C  CB  . PHE A 1 95  ? -13.943 12.690 -9.454  1.00 24.46  ? 95  PHE A CB  1 
ATOM   642  C  CG  . PHE A 1 95  ? -14.140 13.375 -8.057  1.00 21.38  ? 95  PHE A CG  1 
ATOM   643  C  CD1 . PHE A 1 95  ? -14.416 14.668 -7.912  1.00 26.14  ? 95  PHE A CD1 1 
ATOM   644  C  CD2 . PHE A 1 95  ? -14.054 12.581 -6.906  1.00 24.56  ? 95  PHE A CD2 1 
ATOM   645  C  CE1 . PHE A 1 95  ? -14.546 15.232 -6.627  1.00 23.28  ? 95  PHE A CE1 1 
ATOM   646  C  CE2 . PHE A 1 95  ? -14.165 13.110 -5.650  1.00 25.52  ? 95  PHE A CE2 1 
ATOM   647  C  CZ  . PHE A 1 95  ? -14.459 14.441 -5.509  1.00 24.53  ? 95  PHE A CZ  1 
ATOM   648  N  N   . THR A 1 96  ? -15.944 10.183 -9.435  1.00 22.67  ? 96  THR A N   1 
ATOM   649  C  CA  . THR A 1 96  ? -16.520 9.214  -8.561  1.00 26.97  ? 96  THR A CA  1 
ATOM   650  C  C   . THR A 1 96  ? -15.741 9.130  -7.274  1.00 28.65  ? 96  THR A C   1 
ATOM   651  O  O   . THR A 1 96  ? -14.491 8.944  -7.269  1.00 29.04  ? 96  THR A O   1 
ATOM   652  C  CB  . THR A 1 96  ? -16.620 7.840  -9.217  1.00 29.37  ? 96  THR A CB  1 
ATOM   653  O  OG1 . THR A 1 96  ? -17.466 7.910  -10.410 1.00 31.77  ? 96  THR A OG1 1 
ATOM   654  C  CG2 . THR A 1 96  ? -17.232 6.765  -8.250  1.00 32.84  ? 96  THR A CG2 1 
ATOM   655  N  N   . ALA A 1 97  ? -16.458 9.266  -6.169  1.00 25.42  ? 97  ALA A N   1 
ATOM   656  C  CA  . ALA A 1 97  ? -15.811 9.222  -4.850  1.00 23.53  ? 97  ALA A CA  1 
ATOM   657  C  C   . ALA A 1 97  ? -16.216 7.969  -4.043  1.00 25.66  ? 97  ALA A C   1 
ATOM   658  O  O   . ALA A 1 97  ? -17.386 7.445  -4.155  1.00 25.77  ? 97  ALA A O   1 
ATOM   659  C  CB  . ALA A 1 97  ? -16.102 10.513 -4.048  1.00 24.32  ? 97  ALA A CB  1 
ATOM   660  N  N   . ASN A 1 98  ? -15.245 7.466  -3.270  1.00 24.68  ? 98  ASN A N   1 
ATOM   661  C  CA  . ASN A 1 98  ? -15.437 6.379  -2.250  1.00 26.69  ? 98  ASN A CA  1 
ATOM   662  C  C   . ASN A 1 98  ? -15.914 5.044  -2.791  1.00 30.63  ? 98  ASN A C   1 
ATOM   663  O  O   . ASN A 1 98  ? -16.498 4.246  -2.067  1.00 35.74  ? 98  ASN A O   1 
ATOM   664  C  CB  . ASN A 1 98  ? -16.397 6.882  -1.152  1.00 26.45  ? 98  ASN A CB  1 
ATOM   665  C  CG  . ASN A 1 98  ? -16.037 8.263  -0.651  1.00 29.63  ? 98  ASN A CG  1 
ATOM   666  O  OD1 . ASN A 1 98  ? -16.830 9.221  -0.704  1.00 33.27  ? 98  ASN A OD1 1 
ATOM   667  N  ND2 . ASN A 1 98  ? -14.792 8.393  -0.230  1.00 24.72  ? 98  ASN A ND2 1 
ATOM   668  N  N   . ASP A 1 99  ? -15.630 4.777  -4.054  1.00 33.42  ? 99  ASP A N   1 
ATOM   669  C  CA  . ASP A 1 99  ? -16.139 3.558  -4.696  1.00 34.91  ? 99  ASP A CA  1 
ATOM   670  C  C   . ASP A 1 99  ? -15.498 2.308  -4.107  1.00 41.04  ? 99  ASP A C   1 
ATOM   671  O  O   . ASP A 1 99  ? -16.139 1.255  -4.011  1.00 42.26  ? 99  ASP A O   1 
ATOM   672  C  CB  . ASP A 1 99  ? -15.918 3.642  -6.231  1.00 37.71  ? 99  ASP A CB  1 
ATOM   673  N  N   . SER A 1 100 ? -14.243 2.408  -3.668  1.00 38.68  ? 100 SER A N   1 
ATOM   674  C  CA  . SER A 1 100 ? -13.571 1.289  -3.112  1.00 41.41  ? 100 SER A CA  1 
ATOM   675  C  C   . SER A 1 100 ? -13.447 1.456  -1.587  1.00 43.66  ? 100 SER A C   1 
ATOM   676  O  O   . SER A 1 100 ? -12.508 0.956  -1.001  1.00 51.16  ? 100 SER A O   1 
ATOM   677  C  CB  . SER A 1 100 ? -12.219 1.083  -3.836  1.00 41.56  ? 100 SER A CB  1 
ATOM   678  N  N   . GLY A 1 101 ? -14.394 2.156  -0.955  1.00 39.69  ? 101 GLY A N   1 
ATOM   679  C  CA  . GLY A 1 101 ? -14.275 2.598  0.451   1.00 34.99  ? 101 GLY A CA  1 
ATOM   680  C  C   . GLY A 1 101 ? -13.927 4.074  0.647   1.00 37.85  ? 101 GLY A C   1 
ATOM   681  O  O   . GLY A 1 101 ? -13.471 4.741  -0.292  1.00 31.53  ? 101 GLY A O   1 
ATOM   682  N  N   . PRO A 1 102 ? -14.084 4.586  1.879   1.00 34.11  ? 102 PRO A N   1 
ATOM   683  C  CA  . PRO A 1 102 ? -13.783 6.004  2.137   1.00 34.55  ? 102 PRO A CA  1 
ATOM   684  C  C   . PRO A 1 102 ? -12.318 6.350  1.822   1.00 33.04  ? 102 PRO A C   1 
ATOM   685  O  O   . PRO A 1 102 ? -11.403 5.570  2.117   1.00 32.34  ? 102 PRO A O   1 
ATOM   686  C  CB  . PRO A 1 102 ? -14.041 6.200  3.629   1.00 38.60  ? 102 PRO A CB  1 
ATOM   687  C  CG  . PRO A 1 102 ? -14.509 4.888  4.176   1.00 38.74  ? 102 PRO A CG  1 
ATOM   688  C  CD  . PRO A 1 102 ? -14.481 3.844  3.080   1.00 36.15  ? 102 PRO A CD  1 
ATOM   689  N  N   . ARG A 1 103 ? -12.156 7.494  1.190   1.00 30.40  ? 103 ARG A N   1 
ATOM   690  C  CA  . ARG A 1 103 ? -10.866 8.119  0.927   1.00 28.73  ? 103 ARG A CA  1 
ATOM   691  C  C   . ARG A 1 103 ? -10.921 9.610  1.290   1.00 29.38  ? 103 ARG A C   1 
ATOM   692  O  O   . ARG A 1 103 ? -12.001 10.215 1.498   1.00 29.13  ? 103 ARG A O   1 
ATOM   693  C  CB  . ARG A 1 103 ? -10.501 7.937  -0.586  1.00 29.45  ? 103 ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 103 ? -10.420 6.480  -1.085  1.00 31.36  ? 103 ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 103 ? -9.220  5.759  -0.482  1.00 34.84  ? 103 ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 103 ? -9.026  4.403  -1.038  1.00 37.89  ? 103 ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 103 ? -9.562  3.289  -0.551  1.00 38.72  ? 103 ARG A CZ  1 
ATOM   698  N  NH1 . ARG A 1 103 ? -10.415 3.316  0.484   1.00 42.63  ? 103 ARG A NH1 1 
ATOM   699  N  NH2 . ARG A 1 103 ? -9.321  2.126  -1.162  1.00 40.60  ? 103 ARG A NH2 1 
ATOM   700  N  N   . ARG A 1 104 ? -9.742  10.197 1.383   1.00 27.61  ? 104 ARG A N   1 
ATOM   701  C  CA  . ARG A 1 104 ? -9.590  11.594 1.576   1.00 29.62  ? 104 ARG A CA  1 
ATOM   702  C  C   . ARG A 1 104 ? -9.134  12.185 0.224   1.00 25.21  ? 104 ARG A C   1 
ATOM   703  O  O   . ARG A 1 104 ? -8.202  11.680 -0.400  1.00 27.86  ? 104 ARG A O   1 
ATOM   704  C  CB  . ARG A 1 104 ? -8.586  11.831 2.704   1.00 30.91  ? 104 ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 104 ? -9.050  11.158 4.035   1.00 35.61  ? 104 ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 104 ? -8.266  11.628 5.263   1.00 39.87  ? 104 ARG A CD  1 
ATOM   707  N  N   . TYR A 1 105 ? -9.748  13.262 -0.212  1.00 24.70  ? 105 TYR A N   1 
ATOM   708  C  CA  . TYR A 1 105 ? -9.461  13.816 -1.514  1.00 20.65  ? 105 TYR A CA  1 
ATOM   709  C  C   . TYR A 1 105 ? -9.098  15.212 -1.374  1.00 23.81  ? 105 TYR A C   1 
ATOM   710  O  O   . TYR A 1 105 ? -9.837  15.928 -0.699  1.00 24.09  ? 105 TYR A O   1 
ATOM   711  C  CB  . TYR A 1 105 ? -10.769 13.820 -2.380  1.00 24.95  ? 105 TYR A CB  1 
ATOM   712  C  CG  . TYR A 1 105 ? -11.272 12.465 -2.728  1.00 23.03  ? 105 TYR A CG  1 
ATOM   713  C  CD1 . TYR A 1 105 ? -10.864 11.801 -3.890  1.00 26.26  ? 105 TYR A CD1 1 
ATOM   714  C  CD2 . TYR A 1 105 ? -12.098 11.778 -1.830  1.00 24.85  ? 105 TYR A CD2 1 
ATOM   715  C  CE1 . TYR A 1 105 ? -11.290 10.511 -4.160  1.00 27.30  ? 105 TYR A CE1 1 
ATOM   716  C  CE2 . TYR A 1 105 ? -12.544 10.471 -2.118  1.00 25.85  ? 105 TYR A CE2 1 
ATOM   717  C  CZ  . TYR A 1 105 ? -12.159 9.855  -3.266  1.00 26.08  ? 105 TYR A CZ  1 
ATOM   718  O  OH  . TYR A 1 105 ? -12.635 8.570  -3.464  1.00 26.66  ? 105 TYR A OH  1 
ATOM   719  N  N   . THR A 1 106 ? -7.968  15.595 -2.002  1.00 21.65  ? 106 THR A N   1 
ATOM   720  C  CA  . THR A 1 106 ? -7.588  16.970 -2.192  1.00 21.76  ? 106 THR A CA  1 
ATOM   721  C  C   . THR A 1 106 ? -7.646  17.255 -3.656  1.00 20.93  ? 106 THR A C   1 
ATOM   722  O  O   . THR A 1 106 ? -7.003  16.551 -4.495  1.00 24.89  ? 106 THR A O   1 
ATOM   723  C  CB  . THR A 1 106 ? -6.162  17.254 -1.690  1.00 26.46  ? 106 THR A CB  1 
ATOM   724  O  OG1 . THR A 1 106 ? -6.102  16.888 -0.290  1.00 31.70  ? 106 THR A OG1 1 
ATOM   725  C  CG2 . THR A 1 106 ? -5.779  18.724 -1.896  1.00 28.46  ? 106 THR A CG2 1 
ATOM   726  N  N   . ILE A 1 107 ? -8.425  18.274 -4.000  1.00 21.34  ? 107 ILE A N   1 
ATOM   727  C  CA  . ILE A 1 107 ? -8.599  18.698 -5.349  1.00 22.16  ? 107 ILE A CA  1 
ATOM   728  C  C   . ILE A 1 107 ? -7.773  20.018 -5.419  1.00 23.47  ? 107 ILE A C   1 
ATOM   729  O  O   . ILE A 1 107 ? -8.118  20.997 -4.722  1.00 27.01  ? 107 ILE A O   1 
ATOM   730  C  CB  . ILE A 1 107 ? -10.051 18.970 -5.692  1.00 25.19  ? 107 ILE A CB  1 
ATOM   731  C  CG1 . ILE A 1 107 ? -10.973 17.761 -5.502  1.00 28.98  ? 107 ILE A CG1 1 
ATOM   732  C  CG2 . ILE A 1 107 ? -10.178 19.555 -7.115  1.00 26.05  ? 107 ILE A CG2 1 
ATOM   733  C  CD1 . ILE A 1 107 ? -10.447 16.512 -6.160  1.00 28.83  ? 107 ILE A CD1 1 
ATOM   734  N  N   . ALA A 1 108 ? -6.720  20.034 -6.229  1.00 21.82  ? 108 ALA A N   1 
ATOM   735  C  CA  . ALA A 1 108 ? -5.851  21.141 -6.391  1.00 23.72  ? 108 ALA A CA  1 
ATOM   736  C  C   . ALA A 1 108 ? -6.082  21.738 -7.786  1.00 22.21  ? 108 ALA A C   1 
ATOM   737  O  O   . ALA A 1 108 ? -6.130  21.035 -8.755  1.00 23.14  ? 108 ALA A O   1 
ATOM   738  C  CB  . ALA A 1 108 ? -4.403  20.684 -6.224  1.00 27.79  ? 108 ALA A CB  1 
ATOM   739  N  N   . ALA A 1 109 ? -6.209  23.041 -7.889  1.00 23.50  ? 109 ALA A N   1 
ATOM   740  C  CA  . ALA A 1 109 ? -6.295  23.669 -9.208  1.00 22.88  ? 109 ALA A CA  1 
ATOM   741  C  C   . ALA A 1 109 ? -5.287  24.801 -9.294  1.00 22.85  ? 109 ALA A C   1 
ATOM   742  O  O   . ALA A 1 109 ? -5.106  25.549 -8.352  1.00 21.93  ? 109 ALA A O   1 
ATOM   743  C  CB  . ALA A 1 109 ? -7.673  24.229 -9.399  1.00 24.15  ? 109 ALA A CB  1 
ATOM   744  N  N   . LEU A 1 110 ? -4.569  24.848 -10.400 1.00 20.33  ? 110 LEU A N   1 
ATOM   745  C  CA  . LEU A 1 110 ? -3.637  25.923 -10.712 1.00 21.17  ? 110 LEU A CA  1 
ATOM   746  C  C   . LEU A 1 110 ? -4.205  26.778 -11.848 1.00 19.80  ? 110 LEU A C   1 
ATOM   747  O  O   . LEU A 1 110 ? -4.447  26.284 -12.940 1.00 22.35  ? 110 LEU A O   1 
ATOM   748  C  CB  . LEU A 1 110 ? -2.303  25.291 -11.068 1.00 23.23  ? 110 LEU A CB  1 
ATOM   749  C  CG  . LEU A 1 110 ? -1.162  26.202 -11.484 1.00 26.93  ? 110 LEU A CG  1 
ATOM   750  C  CD1 . LEU A 1 110 ? -0.847  27.154 -10.345 1.00 26.16  ? 110 LEU A CD1 1 
ATOM   751  C  CD2 . LEU A 1 110 ? 0.025   25.354 -11.947 1.00 31.29  ? 110 LEU A CD2 1 
ATOM   752  N  N   . LEU A 1 111 ? -4.337  28.073 -11.608 1.00 19.51  ? 111 LEU A N   1 
ATOM   753  C  CA  . LEU A 1 111 ? -5.092  28.929 -12.500 1.00 21.47  ? 111 LEU A CA  1 
ATOM   754  C  C   . LEU A 1 111 ? -4.161  29.896 -13.253 1.00 20.85  ? 111 LEU A C   1 
ATOM   755  O  O   . LEU A 1 111 ? -3.315  30.558 -12.605 1.00 20.18  ? 111 LEU A O   1 
ATOM   756  C  CB  . LEU A 1 111 ? -6.074  29.785 -11.705 1.00 20.53  ? 111 LEU A CB  1 
ATOM   757  C  CG  . LEU A 1 111 ? -6.978  28.988 -10.757 1.00 23.25  ? 111 LEU A CG  1 
ATOM   758  C  CD1 . LEU A 1 111 ? -8.028  29.981 -10.167 1.00 22.13  ? 111 LEU A CD1 1 
ATOM   759  C  CD2 . LEU A 1 111 ? -7.616  27.862 -11.521 1.00 20.76  ? 111 LEU A CD2 1 
ATOM   760  N  N   . SER A 1 112 ? -4.400  30.021 -14.579 1.00 20.79  ? 112 SER A N   1 
ATOM   761  C  CA  . SER A 1 112 ? -3.956  31.178 -15.356 1.00 22.78  ? 112 SER A CA  1 
ATOM   762  C  C   . SER A 1 112 ? -5.114  31.696 -16.181 1.00 22.73  ? 112 SER A C   1 
ATOM   763  O  O   . SER A 1 112 ? -6.147  31.044 -16.298 1.00 22.02  ? 112 SER A O   1 
ATOM   764  C  CB  . SER A 1 112 ? -2.785  30.772 -16.284 1.00 26.00  ? 112 SER A CB  1 
ATOM   765  O  OG  . SER A 1 112 ? -1.727  30.116 -15.625 1.00 28.56  ? 112 SER A OG  1 
ATOM   766  N  N   . PRO A 1 113 ? -4.922  32.844 -16.803 1.00 21.60  ? 113 PRO A N   1 
ATOM   767  C  CA  . PRO A 1 113 ? -6.135  33.399 -17.459 1.00 21.64  ? 113 PRO A CA  1 
ATOM   768  C  C   . PRO A 1 113 ? -6.732  32.558 -18.604 1.00 21.83  ? 113 PRO A C   1 
ATOM   769  O  O   . PRO A 1 113 ? -7.963  32.489 -18.774 1.00 23.42  ? 113 PRO A O   1 
ATOM   770  C  CB  . PRO A 1 113 ? -5.653  34.763 -17.903 1.00 21.92  ? 113 PRO A CB  1 
ATOM   771  C  CG  . PRO A 1 113 ? -4.809  35.141 -16.693 1.00 22.69  ? 113 PRO A CG  1 
ATOM   772  C  CD  . PRO A 1 113 ? -3.979  33.913 -16.434 1.00 23.92  ? 113 PRO A CD  1 
ATOM   773  N  N   . TYR A 1 114 ? -5.880  31.884 -19.348 1.00 21.19  ? 114 TYR A N   1 
ATOM   774  C  CA  . TYR A 1 114 ? -6.304  31.007 -20.424 1.00 22.48  ? 114 TYR A CA  1 
ATOM   775  C  C   . TYR A 1 114 ? -5.969  29.583 -20.250 1.00 22.01  ? 114 TYR A C   1 
ATOM   776  O  O   . TYR A 1 114 ? -6.031  28.830 -21.225 1.00 25.30  ? 114 TYR A O   1 
ATOM   777  C  CB  . TYR A 1 114 ? -5.716  31.511 -21.713 1.00 23.68  ? 114 TYR A CB  1 
ATOM   778  C  CG  . TYR A 1 114 ? -6.426  32.691 -22.281 1.00 25.49  ? 114 TYR A CG  1 
ATOM   779  C  CD1 . TYR A 1 114 ? -6.279  33.953 -21.702 1.00 29.22  ? 114 TYR A CD1 1 
ATOM   780  C  CD2 . TYR A 1 114 ? -7.264  32.577 -23.394 1.00 29.42  ? 114 TYR A CD2 1 
ATOM   781  C  CE1 . TYR A 1 114 ? -6.900  35.071 -22.245 1.00 33.14  ? 114 TYR A CE1 1 
ATOM   782  C  CE2 . TYR A 1 114 ? -7.922  33.660 -23.899 1.00 29.95  ? 114 TYR A CE2 1 
ATOM   783  C  CZ  . TYR A 1 114 ? -7.730  34.913 -23.326 1.00 32.48  ? 114 TYR A CZ  1 
ATOM   784  O  OH  . TYR A 1 114 ? -8.353  36.021 -23.863 1.00 40.05  ? 114 TYR A OH  1 
ATOM   785  N  N   . SER A 1 115 ? -5.669  29.157 -19.027 1.00 22.70  ? 115 SER A N   1 
ATOM   786  C  CA  . SER A 1 115 ? -5.339  27.776 -18.772 1.00 22.62  ? 115 SER A CA  1 
ATOM   787  C  C   . SER A 1 115 ? -5.628  27.420 -17.366 1.00 23.37  ? 115 SER A C   1 
ATOM   788  O  O   . SER A 1 115 ? -5.521  28.290 -16.478 1.00 26.25  ? 115 SER A O   1 
ATOM   789  C  CB  . SER A 1 115 ? -3.825  27.604 -19.012 1.00 25.84  ? 115 SER A CB  1 
ATOM   790  O  OG  . SER A 1 115 ? -3.450  26.237 -19.045 1.00 32.15  ? 115 SER A OG  1 
ATOM   791  N  N   . TYR A 1 116 ? -5.981  26.182 -17.063 1.00 22.47  ? 116 TYR A N   1 
ATOM   792  C  CA  . TYR A 1 116 ? -5.911  25.729 -15.693 1.00 21.88  ? 116 TYR A CA  1 
ATOM   793  C  C   . TYR A 1 116 ? -5.552  24.260 -15.678 1.00 22.47  ? 116 TYR A C   1 
ATOM   794  O  O   . TYR A 1 116 ? -5.760  23.565 -16.637 1.00 21.88  ? 116 TYR A O   1 
ATOM   795  C  CB  . TYR A 1 116 ? -7.188  25.910 -14.929 1.00 24.43  ? 116 TYR A CB  1 
ATOM   796  C  CG  . TYR A 1 116 ? -8.351  25.140 -15.431 1.00 24.66  ? 116 TYR A CG  1 
ATOM   797  C  CD1 . TYR A 1 116 ? -8.599  23.839 -14.985 1.00 26.23  ? 116 TYR A CD1 1 
ATOM   798  C  CD2 . TYR A 1 116 ? -9.180  25.679 -16.379 1.00 28.28  ? 116 TYR A CD2 1 
ATOM   799  C  CE1 . TYR A 1 116 ? -9.690  23.126 -15.468 1.00 32.70  ? 116 TYR A CE1 1 
ATOM   800  C  CE2 . TYR A 1 116 ? -10.287 24.990 -16.817 1.00 31.81  ? 116 TYR A CE2 1 
ATOM   801  C  CZ  . TYR A 1 116 ? -10.529 23.738 -16.384 1.00 31.45  ? 116 TYR A CZ  1 
ATOM   802  O  OH  . TYR A 1 116 ? -11.624 23.073 -16.929 1.00 42.60  ? 116 TYR A OH  1 
ATOM   803  N  N   . SER A 1 117 ? -5.045  23.799 -14.549 1.00 22.72  ? 117 SER A N   1 
ATOM   804  C  CA  A SER A 1 117 ? -4.743  22.398 -14.357 0.50 23.21  ? 117 SER A CA  1 
ATOM   805  C  CA  B SER A 1 117 ? -4.741  22.398 -14.367 0.50 23.25  ? 117 SER A CA  1 
ATOM   806  C  C   . SER A 1 117 ? -5.398  22.011 -13.074 1.00 26.08  ? 117 SER A C   1 
ATOM   807  O  O   . SER A 1 117 ? -5.561  22.845 -12.172 1.00 23.14  ? 117 SER A O   1 
ATOM   808  C  CB  A SER A 1 117 ? -3.231  22.153 -14.261 0.50 25.77  ? 117 SER A CB  1 
ATOM   809  C  CB  B SER A 1 117 ? -3.218  22.131 -14.320 0.50 25.77  ? 117 SER A CB  1 
ATOM   810  O  OG  A SER A 1 117 ? -2.762  22.482 -12.957 0.50 28.71  ? 117 SER A OG  1 
ATOM   811  O  OG  B SER A 1 117 ? -2.507  22.774 -15.375 0.50 29.49  ? 117 SER A OG  1 
ATOM   812  N  N   . THR A 1 118 ? -5.854  20.769 -13.002 1.00 25.06  ? 118 THR A N   1 
ATOM   813  C  CA  . THR A 1 118 ? -6.419  20.269 -11.798 1.00 27.15  ? 118 THR A CA  1 
ATOM   814  C  C   . THR A 1 118 ? -5.880  18.867 -11.580 1.00 26.04  ? 118 THR A C   1 
ATOM   815  O  O   . THR A 1 118 ? -5.610  18.136 -12.514 1.00 24.75  ? 118 THR A O   1 
ATOM   816  C  CB  . THR A 1 118 ? -7.938  20.207 -11.819 1.00 26.66  ? 118 THR A CB  1 
ATOM   817  O  OG1 . THR A 1 118 ? -8.360  19.752 -10.542 1.00 34.08  ? 118 THR A OG1 1 
ATOM   818  C  CG2 . THR A 1 118 ? -8.521  19.210 -12.922 1.00 26.91  ? 118 THR A CG2 1 
ATOM   819  N  N   . THR A 1 119 ? -5.606  18.576 -10.321 1.00 28.45  ? 119 THR A N   1 
ATOM   820  C  CA  . THR A 1 119 ? -4.981  17.327 -9.896  1.00 25.64  ? 119 THR A CA  1 
ATOM   821  C  C   . THR A 1 119 ? -5.707  16.846 -8.669  1.00 25.48  ? 119 THR A C   1 
ATOM   822  O  O   . THR A 1 119 ? -6.296  17.636 -7.922  1.00 25.01  ? 119 THR A O   1 
ATOM   823  C  CB  . THR A 1 119 ? -3.454  17.451 -9.510  1.00 31.17  ? 119 THR A CB  1 
ATOM   824  O  OG1 . THR A 1 119 ? -2.772  18.218 -10.515 1.00 36.17  ? 119 THR A OG1 1 
ATOM   825  C  CG2 . THR A 1 119 ? -2.834  16.040 -9.452  1.00 29.94  ? 119 THR A CG2 1 
ATOM   826  N  N   . ALA A 1 120 ? -5.760  15.554 -8.525  1.00 23.15  ? 120 ALA A N   1 
ATOM   827  C  CA  . ALA A 1 120 ? -6.300  14.995 -7.304  1.00 24.93  ? 120 ALA A CA  1 
ATOM   828  C  C   . ALA A 1 120 ? -5.266  14.171 -6.581  1.00 23.34  ? 120 ALA A C   1 
ATOM   829  O  O   . ALA A 1 120 ? -4.536  13.411 -7.177  1.00 28.99  ? 120 ALA A O   1 
ATOM   830  C  CB  . ALA A 1 120 ? -7.612  14.209 -7.575  1.00 26.66  ? 120 ALA A CB  1 
ATOM   831  N  N   . VAL A 1 121 ? -5.183  14.389 -5.274  1.00 24.14  ? 121 VAL A N   1 
ATOM   832  C  CA  . VAL A 1 121 ? -4.446  13.572 -4.378  1.00 24.83  ? 121 VAL A CA  1 
ATOM   833  C  C   . VAL A 1 121 ? -5.451  12.794 -3.531  1.00 25.94  ? 121 VAL A C   1 
ATOM   834  O  O   . VAL A 1 121 ? -6.286  13.360 -2.818  1.00 25.38  ? 121 VAL A O   1 
ATOM   835  C  CB  . VAL A 1 121 ? -3.546  14.404 -3.470  1.00 27.53  ? 121 VAL A CB  1 
ATOM   836  C  CG1 . VAL A 1 121 ? -2.711  13.466 -2.601  1.00 30.27  ? 121 VAL A CG1 1 
ATOM   837  C  CG2 . VAL A 1 121 ? -2.728  15.393 -4.328  1.00 29.84  ? 121 VAL A CG2 1 
ATOM   838  N  N   . VAL A 1 122 ? -5.345  11.481 -3.635  1.00 23.82  ? 122 VAL A N   1 
ATOM   839  C  CA  . VAL A 1 122 ? -6.314  10.550 -3.034  1.00 25.82  ? 122 VAL A CA  1 
ATOM   840  C  C   . VAL A 1 122 ? -5.561  9.733  -2.027  1.00 28.60  ? 122 VAL A C   1 
ATOM   841  O  O   . VAL A 1 122 ? -4.562  9.081  -2.345  1.00 30.94  ? 122 VAL A O   1 
ATOM   842  C  CB  . VAL A 1 122 ? -7.036  9.648  -4.080  1.00 28.04  ? 122 VAL A CB  1 
ATOM   843  C  CG1 . VAL A 1 122 ? -8.112  8.794  -3.397  1.00 29.53  ? 122 VAL A CG1 1 
ATOM   844  C  CG2 . VAL A 1 122 ? -7.717  10.523 -5.106  1.00 28.02  ? 122 VAL A CG2 1 
ATOM   845  N  N   . THR A 1 123 ? -5.957  9.816  -0.773  1.00 27.70  ? 123 THR A N   1 
ATOM   846  C  CA  . THR A 1 123 ? -5.278  9.003  0.257   1.00 34.52  ? 123 THR A CA  1 
ATOM   847  C  C   . THR A 1 123 ? -6.199  8.182  1.136   1.00 37.02  ? 123 THR A C   1 
ATOM   848  O  O   . THR A 1 123 ? -7.409  8.448  1.199   1.00 30.35  ? 123 THR A O   1 
ATOM   849  C  CB  . THR A 1 123 ? -4.416  9.933  1.146   1.00 39.04  ? 123 THR A CB  1 
ATOM   850  O  OG1 . THR A 1 123 ? -5.255  10.733 1.995   1.00 38.64  ? 123 THR A OG1 1 
ATOM   851  C  CG2 . THR A 1 123 ? -3.558  10.826 0.287   1.00 36.47  ? 123 THR A CG2 1 
ATOM   852  N  N   . ASN A 1 124 ? -5.597  7.188  1.815   1.00 39.11  ? 124 ASN A N   1 
ATOM   853  C  CA  . ASN A 1 124 ? -6.282  6.406  2.871   1.00 50.34  ? 124 ASN A CA  1 
ATOM   854  C  C   . ASN A 1 124 ? -6.349  6.969  4.300   1.00 50.40  ? 124 ASN A C   1 
ATOM   855  O  O   . ASN A 1 124 ? -7.458  7.020  4.870   1.00 50.00  ? 124 ASN A O   1 
ATOM   856  C  CB  . ASN A 1 124 ? -5.719  5.011  2.953   1.00 54.21  ? 124 ASN A CB  1 
ATOM   857  C  CG  . ASN A 1 124 ? -6.701  3.998  2.426   1.00 61.01  ? 124 ASN A CG  1 
ATOM   858  O  OD1 . ASN A 1 124 ? -7.614  3.543  3.143   1.00 52.28  ? 124 ASN A OD1 1 
ATOM   859  N  ND2 . ASN A 1 124 ? -6.566  3.685  1.153   1.00 62.87  ? 124 ASN A ND2 1 
ATOM   860  N  N   . PRO B 1 11  ? -13.305 27.228 -37.065 1.00 40.73  ? 11  PRO B N   1 
ATOM   861  C  CA  . PRO B 1 11  ? -13.284 28.132 -35.905 1.00 38.13  ? 11  PRO B CA  1 
ATOM   862  C  C   . PRO B 1 11  ? -13.075 27.509 -34.514 1.00 36.10  ? 11  PRO B C   1 
ATOM   863  O  O   . PRO B 1 11  ? -12.831 28.240 -33.575 1.00 36.17  ? 11  PRO B O   1 
ATOM   864  C  CB  . PRO B 1 11  ? -14.677 28.760 -35.931 1.00 41.52  ? 11  PRO B CB  1 
ATOM   865  C  CG  . PRO B 1 11  ? -15.509 27.807 -36.674 1.00 43.52  ? 11  PRO B CG  1 
ATOM   866  C  CD  . PRO B 1 11  ? -14.619 27.178 -37.694 1.00 44.74  ? 11  PRO B CD  1 
ATOM   867  N  N   . LEU B 1 12  ? -13.245 26.202 -34.380 1.00 33.15  ? 12  LEU B N   1 
ATOM   868  C  CA  . LEU B 1 12  ? -13.065 25.507 -33.127 1.00 31.76  ? 12  LEU B CA  1 
ATOM   869  C  C   . LEU B 1 12  ? -12.341 24.223 -33.437 1.00 32.33  ? 12  LEU B C   1 
ATOM   870  O  O   . LEU B 1 12  ? -12.776 23.475 -34.338 1.00 32.73  ? 12  LEU B O   1 
ATOM   871  C  CB  . LEU B 1 12  ? -14.421 25.198 -32.503 1.00 32.85  ? 12  LEU B CB  1 
ATOM   872  C  CG  . LEU B 1 12  ? -14.423 24.421 -31.185 1.00 30.95  ? 12  LEU B CG  1 
ATOM   873  C  CD1 . LEU B 1 12  ? -13.592 25.090 -30.111 1.00 31.34  ? 12  LEU B CD1 1 
ATOM   874  C  CD2 . LEU B 1 12  ? -15.900 24.240 -30.784 1.00 35.98  ? 12  LEU B CD2 1 
ATOM   875  N  N   . MET B 1 13  ? -11.226 24.019 -32.750 1.00 30.41  ? 13  MET B N   1 
ATOM   876  C  CA  A MET B 1 13  ? -10.357 22.852 -32.870 0.50 31.64  ? 13  MET B CA  1 
ATOM   877  C  CA  B MET B 1 13  ? -10.431 22.790 -32.857 0.50 30.38  ? 13  MET B CA  1 
ATOM   878  C  C   . MET B 1 13  ? -10.125 22.300 -31.457 1.00 28.58  ? 13  MET B C   1 
ATOM   879  O  O   . MET B 1 13  ? -9.972  23.072 -30.518 1.00 27.82  ? 13  MET B O   1 
ATOM   880  C  CB  A MET B 1 13  ? -9.020  23.298 -33.469 0.50 34.96  ? 13  MET B CB  1 
ATOM   881  C  CB  B MET B 1 13  ? -9.115  22.996 -33.610 0.50 31.66  ? 13  MET B CB  1 
ATOM   882  C  CG  A MET B 1 13  ? -8.046  22.177 -33.805 0.50 40.64  ? 13  MET B CG  1 
ATOM   883  C  CG  B MET B 1 13  ? -8.403  21.695 -34.034 0.50 35.13  ? 13  MET B CG  1 
ATOM   884  S  SD  A MET B 1 13  ? -6.474  22.740 -34.516 0.50 49.59  ? 13  MET B SD  1 
ATOM   885  S  SD  B MET B 1 13  ? -7.128  21.053 -32.895 0.50 37.11  ? 13  MET B SD  1 
ATOM   886  C  CE  A MET B 1 13  ? -5.306  22.443 -33.183 0.50 44.34  ? 13  MET B CE  1 
ATOM   887  C  CE  B MET B 1 13  ? -5.628  21.860 -33.475 0.50 34.72  ? 13  MET B CE  1 
ATOM   888  N  N   . VAL B 1 14  ? -10.079 21.001 -31.302 1.00 27.18  ? 14  VAL B N   1 
ATOM   889  C  CA  . VAL B 1 14  ? -9.786  20.415 -29.971 1.00 27.16  ? 14  VAL B CA  1 
ATOM   890  C  C   . VAL B 1 14  ? -8.569  19.544 -30.216 1.00 27.79  ? 14  VAL B C   1 
ATOM   891  O  O   . VAL B 1 14  ? -8.536  18.763 -31.167 1.00 29.68  ? 14  VAL B O   1 
ATOM   892  C  CB  . VAL B 1 14  ? -10.946 19.530 -29.423 1.00 28.25  ? 14  VAL B CB  1 
ATOM   893  C  CG1 . VAL B 1 14  ? -10.569 18.847 -28.109 1.00 27.22  ? 14  VAL B CG1 1 
ATOM   894  C  CG2 . VAL B 1 14  ? -12.215 20.371 -29.214 1.00 27.92  ? 14  VAL B CG2 1 
ATOM   895  N  N   . LYS B 1 15  ? -7.590  19.653 -29.355 1.00 25.14  ? 15  LYS B N   1 
ATOM   896  C  CA  . LYS B 1 15  ? -6.413  18.790 -29.423 1.00 26.29  ? 15  LYS B CA  1 
ATOM   897  C  C   . LYS B 1 15  ? -6.184  18.124 -28.086 1.00 26.80  ? 15  LYS B C   1 
ATOM   898  O  O   . LYS B 1 15  ? -6.229  18.822 -27.080 1.00 24.08  ? 15  LYS B O   1 
ATOM   899  C  CB  . LYS B 1 15  ? -5.203  19.612 -29.835 1.00 28.62  ? 15  LYS B CB  1 
ATOM   900  C  CG  . LYS B 1 15  ? -3.877  18.861 -29.812 1.00 34.74  ? 15  LYS B CG  1 
ATOM   901  N  N   . VAL B 1 16  ? -5.948  16.814 -28.057 1.00 23.62  ? 16  VAL B N   1 
ATOM   902  C  CA  . VAL B 1 16  ? -5.760  16.089 -26.792 1.00 23.18  ? 16  VAL B CA  1 
ATOM   903  C  C   . VAL B 1 16  ? -4.440  15.256 -26.855 1.00 25.13  ? 16  VAL B C   1 
ATOM   904  O  O   . VAL B 1 16  ? -4.200  14.485 -27.844 1.00 24.39  ? 16  VAL B O   1 
ATOM   905  C  CB  . VAL B 1 16  ? -6.942  15.108 -26.523 1.00 22.94  ? 16  VAL B CB  1 
ATOM   906  C  CG1 . VAL B 1 16  ? -6.862  14.526 -25.087 1.00 21.81  ? 16  VAL B CG1 1 
ATOM   907  C  CG2 . VAL B 1 16  ? -8.276  15.779 -26.772 1.00 24.04  ? 16  VAL B CG2 1 
ATOM   908  N  N   . LEU B 1 17  ? -3.653  15.356 -25.763 1.00 24.21  ? 17  LEU B N   1 
ATOM   909  C  CA  . LEU B 1 17  ? -2.356  14.701 -25.631 1.00 24.49  ? 17  LEU B CA  1 
ATOM   910  C  C   . LEU B 1 17  ? -2.348  13.805 -24.390 1.00 25.34  ? 17  LEU B C   1 
ATOM   911  O  O   . LEU B 1 17  ? -3.038  14.073 -23.414 1.00 25.05  ? 17  LEU B O   1 
ATOM   912  C  CB  . LEU B 1 17  ? -1.246  15.715 -25.538 1.00 25.88  ? 17  LEU B CB  1 
ATOM   913  C  CG  . LEU B 1 17  ? -0.994  16.630 -26.747 1.00 29.19  ? 17  LEU B CG  1 
ATOM   914  C  CD1 . LEU B 1 17  ? 0.221   17.481 -26.481 1.00 35.26  ? 17  LEU B CD1 1 
ATOM   915  C  CD2 . LEU B 1 17  ? -0.888  15.822 -28.064 1.00 31.93  ? 17  LEU B CD2 1 
ATOM   916  N  N   . ASP B 1 18  ? -1.532  12.777 -24.430 1.00 22.80  ? 18  ASP B N   1 
ATOM   917  C  CA  . ASP B 1 18  ? -1.462  11.765 -23.368 1.00 22.51  ? 18  ASP B CA  1 
ATOM   918  C  C   . ASP B 1 18  ? -0.082  11.895 -22.709 1.00 21.03  ? 18  ASP B C   1 
ATOM   919  O  O   . ASP B 1 18  ? 0.920   11.653 -23.364 1.00 25.03  ? 18  ASP B O   1 
ATOM   920  C  CB  . ASP B 1 18  ? -1.663  10.407 -24.015 1.00 23.88  ? 18  ASP B CB  1 
ATOM   921  C  CG  . ASP B 1 18  ? -1.417  9.234  -23.101 1.00 28.06  ? 18  ASP B CG  1 
ATOM   922  O  OD1 . ASP B 1 18  ? -0.735  9.344  -22.065 1.00 28.36  ? 18  ASP B OD1 1 
ATOM   923  O  OD2 . ASP B 1 18  ? -1.878  8.117  -23.490 1.00 30.70  ? 18  ASP B OD2 1 
ATOM   924  N  N   . ALA B 1 19  ? -0.050  12.367 -21.458 1.00 21.78  ? 19  ALA B N   1 
ATOM   925  C  CA  . ALA B 1 19  ? 1.189   12.631 -20.728 1.00 21.92  ? 19  ALA B CA  1 
ATOM   926  C  C   . ALA B 1 19  ? 1.866   11.330 -20.174 1.00 24.06  ? 19  ALA B C   1 
ATOM   927  O  O   . ALA B 1 19  ? 3.006   11.365 -19.702 1.00 26.84  ? 19  ALA B O   1 
ATOM   928  C  CB  . ALA B 1 19  ? 0.884   13.595 -19.536 1.00 22.92  ? 19  ALA B CB  1 
ATOM   929  N  N   . VAL B 1 20  ? 1.185   10.200 -20.223 1.00 23.01  ? 20  VAL B N   1 
ATOM   930  C  CA  . VAL B 1 20  ? 1.716   8.924  -19.722 1.00 24.60  ? 20  VAL B CA  1 
ATOM   931  C  C   . VAL B 1 20  ? 2.561   8.290  -20.823 1.00 27.83  ? 20  VAL B C   1 
ATOM   932  O  O   . VAL B 1 20  ? 3.658   7.829  -20.556 1.00 32.48  ? 20  VAL B O   1 
ATOM   933  C  CB  . VAL B 1 20  ? 0.608   7.996  -19.241 1.00 28.03  ? 20  VAL B CB  1 
ATOM   934  C  CG1 . VAL B 1 20  ? 1.063   6.495  -19.113 1.00 29.87  ? 20  VAL B CG1 1 
ATOM   935  C  CG2 . VAL B 1 20  ? -0.006  8.578  -17.948 1.00 27.21  ? 20  VAL B CG2 1 
ATOM   936  N  N   . ARG B 1 21  ? 2.048   8.301  -22.046 1.00 27.62  ? 21  ARG B N   1 
ATOM   937  C  CA  . ARG B 1 21  ? 2.716   7.669  -23.221 1.00 29.63  ? 21  ARG B CA  1 
ATOM   938  C  C   . ARG B 1 21  ? 3.475   8.674  -24.123 1.00 29.04  ? 21  ARG B C   1 
ATOM   939  O  O   . ARG B 1 21  ? 4.220   8.258  -25.035 1.00 27.88  ? 21  ARG B O   1 
ATOM   940  C  CB  . ARG B 1 21  ? 1.654   6.984  -24.076 1.00 31.39  ? 21  ARG B CB  1 
ATOM   941  C  CG  . ARG B 1 21  ? 0.909   5.815  -23.412 0.50 34.90  ? 21  ARG B CG  1 
ATOM   942  C  CD  . ARG B 1 21  ? -0.346  5.458  -24.223 0.50 35.65  ? 21  ARG B CD  1 
ATOM   943  N  NE  . ARG B 1 21  ? -0.103  4.491  -25.282 0.50 41.02  ? 21  ARG B NE  1 
ATOM   944  N  N   . GLY B 1 22  ? 3.287   9.967  -23.910 1.00 25.29  ? 22  GLY B N   1 
ATOM   945  C  CA  . GLY B 1 22  ? 3.891   11.041 -24.752 1.00 26.36  ? 22  GLY B CA  1 
ATOM   946  C  C   . GLY B 1 22  ? 3.442   10.940 -26.212 1.00 27.88  ? 22  GLY B C   1 
ATOM   947  O  O   . GLY B 1 22  ? 4.245   10.890 -27.164 1.00 27.71  ? 22  GLY B O   1 
ATOM   948  N  N   . SER B 1 23  ? 2.128   10.925 -26.375 1.00 26.87  ? 23  SER B N   1 
ATOM   949  C  CA  . SER B 1 23  ? 1.538   10.764 -27.664 1.00 29.73  ? 23  SER B CA  1 
ATOM   950  C  C   . SER B 1 23  ? 0.242   11.538 -27.776 1.00 27.19  ? 23  SER B C   1 
ATOM   951  O  O   . SER B 1 23  ? -0.373  11.985 -26.779 1.00 26.25  ? 23  SER B O   1 
ATOM   952  C  CB  . SER B 1 23  ? 1.299   9.255  -27.916 1.00 34.54  ? 23  SER B CB  1 
ATOM   953  O  OG  . SER B 1 23  ? 0.162   8.903  -27.141 1.00 39.05  ? 23  SER B OG  1 
ATOM   954  N  N   . PRO B 1 24  ? -0.175  11.784 -29.012 1.00 28.69  ? 24  PRO B N   1 
ATOM   955  C  CA  . PRO B 1 24  ? -1.571  12.196 -29.181 1.00 28.72  ? 24  PRO B CA  1 
ATOM   956  C  C   . PRO B 1 24  ? -2.499  11.219 -28.501 1.00 28.92  ? 24  PRO B C   1 
ATOM   957  O  O   . PRO B 1 24  ? -2.195  10.044 -28.463 1.00 28.51  ? 24  PRO B O   1 
ATOM   958  C  CB  . PRO B 1 24  ? -1.765  12.132 -30.697 1.00 32.31  ? 24  PRO B CB  1 
ATOM   959  C  CG  . PRO B 1 24  ? -0.667  11.205 -31.198 1.00 35.18  ? 24  PRO B CG  1 
ATOM   960  C  CD  . PRO B 1 24  ? 0.504   11.548 -30.305 1.00 32.56  ? 24  PRO B CD  1 
ATOM   961  N  N   . ALA B 1 25  ? -3.630  11.719 -28.003 1.00 26.61  ? 25  ALA B N   1 
ATOM   962  C  CA  . ALA B 1 25  ? -4.659  10.886 -27.434 1.00 26.55  ? 25  ALA B CA  1 
ATOM   963  C  C   . ALA B 1 25  ? -5.655  10.609 -28.559 1.00 27.80  ? 25  ALA B C   1 
ATOM   964  O  O   . ALA B 1 25  ? -6.416  11.492 -28.934 1.00 26.31  ? 25  ALA B O   1 
ATOM   965  C  CB  . ALA B 1 25  ? -5.300  11.604 -26.243 1.00 25.55  ? 25  ALA B CB  1 
ATOM   966  N  N   . ILE B 1 26  ? -5.643  9.386  -29.071 1.00 27.78  ? 26  ILE B N   1 
ATOM   967  C  CA  . ILE B 1 26  ? -6.388  9.058  -30.316 1.00 30.90  ? 26  ILE B CA  1 
ATOM   968  C  C   . ILE B 1 26  ? -7.730  8.419  -29.933 1.00 32.03  ? 26  ILE B C   1 
ATOM   969  O  O   . ILE B 1 26  ? -7.836  7.730  -28.916 1.00 30.89  ? 26  ILE B O   1 
ATOM   970  C  CB  . ILE B 1 26  ? -5.590  8.139  -31.293 1.00 35.62  ? 26  ILE B CB  1 
ATOM   971  C  CG1 . ILE B 1 26  ? -5.611  6.660  -30.888 1.00 38.94  ? 26  ILE B CG1 1 
ATOM   972  C  CG2 . ILE B 1 26  ? -4.140  8.639  -31.434 1.00 34.48  ? 26  ILE B CG2 1 
ATOM   973  C  CD1 . ILE B 1 26  ? -5.111  5.725  -31.972 1.00 44.41  ? 26  ILE B CD1 1 
ATOM   974  N  N   . ASN B 1 27  ? -8.743  8.726  -30.728 1.00 32.60  ? 27  ASN B N   1 
ATOM   975  C  CA  . ASN B 1 27  ? -10.073 8.193  -30.562 1.00 34.68  ? 27  ASN B CA  1 
ATOM   976  C  C   . ASN B 1 27  ? -10.754 8.551  -29.282 1.00 32.58  ? 27  ASN B C   1 
ATOM   977  O  O   . ASN B 1 27  ? -11.516 7.753  -28.743 1.00 30.87  ? 27  ASN B O   1 
ATOM   978  C  CB  . ASN B 1 27  ? -10.025 6.705  -30.687 1.00 37.13  ? 27  ASN B CB  1 
ATOM   979  C  CG  . ASN B 1 27  ? -10.561 6.299  -31.961 1.00 45.59  ? 27  ASN B CG  1 
ATOM   980  O  OD1 . ASN B 1 27  ? -9.916  6.465  -33.001 1.00 45.59  ? 27  ASN B OD1 1 
ATOM   981  N  ND2 . ASN B 1 27  ? -11.823 5.902  -31.937 1.00 48.89  ? 27  ASN B ND2 1 
ATOM   982  N  N   . VAL B 1 28  ? -10.467 9.742  -28.813 1.00 30.88  ? 28  VAL B N   1 
ATOM   983  C  CA  . VAL B 1 28  ? -11.142 10.259 -27.627 1.00 30.91  ? 28  VAL B CA  1 
ATOM   984  C  C   . VAL B 1 28  ? -12.450 10.921 -28.086 1.00 28.82  ? 28  VAL B C   1 
ATOM   985  O  O   . VAL B 1 28  ? -12.424 11.739 -28.971 1.00 25.25  ? 28  VAL B O   1 
ATOM   986  C  CB  . VAL B 1 28  ? -10.314 11.268 -26.913 1.00 30.51  ? 28  VAL B CB  1 
ATOM   987  C  CG1 . VAL B 1 28  ? -11.093 11.774 -25.672 1.00 28.83  ? 28  VAL B CG1 1 
ATOM   988  C  CG2 . VAL B 1 28  ? -8.961  10.674 -26.517 1.00 30.46  ? 28  VAL B CG2 1 
ATOM   989  N  N   . ALA B 1 29  ? -13.576 10.554 -27.474 1.00 26.34  ? 29  ALA B N   1 
ATOM   990  C  CA  . ALA B 1 29  ? -14.841 11.181 -27.815 1.00 26.06  ? 29  ALA B CA  1 
ATOM   991  C  C   . ALA B 1 29  ? -14.929 12.560 -27.209 1.00 25.15  ? 29  ALA B C   1 
ATOM   992  O  O   . ALA B 1 29  ? -14.503 12.800 -26.090 1.00 25.66  ? 29  ALA B O   1 
ATOM   993  C  CB  . ALA B 1 29  ? -16.014 10.296 -27.384 1.00 27.94  ? 29  ALA B CB  1 
ATOM   994  N  N   . VAL B 1 30  ? -15.392 13.518 -28.005 1.00 24.17  ? 30  VAL B N   1 
ATOM   995  C  CA  . VAL B 1 30  ? -15.517 14.915 -27.629 1.00 23.56  ? 30  VAL B CA  1 
ATOM   996  C  C   . VAL B 1 30  ? -16.943 15.378 -27.977 1.00 25.39  ? 30  VAL B C   1 
ATOM   997  O  O   . VAL B 1 30  ? -17.374 15.217 -29.138 1.00 27.34  ? 30  VAL B O   1 
ATOM   998  C  CB  . VAL B 1 30  ? -14.527 15.800 -28.404 1.00 22.96  ? 30  VAL B CB  1 
ATOM   999  C  CG1 . VAL B 1 30  ? -14.712 17.246 -27.992 1.00 26.06  ? 30  VAL B CG1 1 
ATOM   1000 C  CG2 . VAL B 1 30  ? -13.075 15.406 -28.042 1.00 24.29  ? 30  VAL B CG2 1 
ATOM   1001 N  N   . HIS B 1 31  ? -17.657 15.909 -26.996 1.00 26.75  ? 31  HIS B N   1 
ATOM   1002 C  CA  . HIS B 1 31  ? -18.945 16.542 -27.197 1.00 27.34  ? 31  HIS B CA  1 
ATOM   1003 C  C   . HIS B 1 31  ? -18.969 17.987 -26.886 1.00 26.97  ? 31  HIS B C   1 
ATOM   1004 O  O   . HIS B 1 31  ? -18.385 18.469 -25.893 1.00 28.90  ? 31  HIS B O   1 
ATOM   1005 C  CB  . HIS B 1 31  ? -19.963 15.850 -26.325 1.00 30.46  ? 31  HIS B CB  1 
ATOM   1006 C  CG  . HIS B 1 31  ? -20.303 14.502 -26.801 1.00 34.54  ? 31  HIS B CG  1 
ATOM   1007 N  ND1 . HIS B 1 31  ? -19.585 13.435 -26.458 1.00 38.11  ? 31  HIS B ND1 1 
ATOM   1008 C  CD2 . HIS B 1 31  ? -21.336 14.051 -27.610 1.00 37.57  ? 31  HIS B CD2 1 
ATOM   1009 C  CE1 . HIS B 1 31  ? -20.120 12.334 -27.022 1.00 37.36  ? 31  HIS B CE1 1 
ATOM   1010 N  NE2 . HIS B 1 31  ? -21.181 12.700 -27.730 1.00 42.95  ? 31  HIS B NE2 1 
ATOM   1011 N  N   . VAL B 1 32  ? -19.624 18.752 -27.726 1.00 26.38  ? 32  VAL B N   1 
ATOM   1012 C  CA  . VAL B 1 32  ? -19.699 20.171 -27.556 1.00 25.96  ? 32  VAL B CA  1 
ATOM   1013 C  C   . VAL B 1 32  ? -21.174 20.528 -27.381 1.00 28.26  ? 32  VAL B C   1 
ATOM   1014 O  O   . VAL B 1 32  ? -22.052 19.973 -28.069 1.00 30.24  ? 32  VAL B O   1 
ATOM   1015 C  CB  . VAL B 1 32  ? -19.119 20.939 -28.769 1.00 27.00  ? 32  VAL B CB  1 
ATOM   1016 C  CG1 . VAL B 1 32  ? -19.127 22.455 -28.560 1.00 26.33  ? 32  VAL B CG1 1 
ATOM   1017 C  CG2 . VAL B 1 32  ? -17.737 20.440 -29.109 1.00 26.96  ? 32  VAL B CG2 1 
ATOM   1018 N  N   . PHE B 1 33  ? -21.416 21.486 -26.507 1.00 26.50  ? 33  PHE B N   1 
ATOM   1019 C  CA  . PHE B 1 33  ? -22.743 21.962 -26.156 1.00 29.28  ? 33  PHE B CA  1 
ATOM   1020 C  C   . PHE B 1 33  ? -22.780 23.487 -26.134 1.00 30.25  ? 33  PHE B C   1 
ATOM   1021 O  O   . PHE B 1 33  ? -21.776 24.148 -25.942 1.00 27.88  ? 33  PHE B O   1 
ATOM   1022 C  CB  . PHE B 1 33  ? -23.147 21.471 -24.780 1.00 30.50  ? 33  PHE B CB  1 
ATOM   1023 C  CG  . PHE B 1 33  ? -22.990 20.000 -24.588 1.00 32.62  ? 33  PHE B CG  1 
ATOM   1024 C  CD1 . PHE B 1 33  ? -21.750 19.472 -24.236 1.00 35.49  ? 33  PHE B CD1 1 
ATOM   1025 C  CD2 . PHE B 1 33  ? -24.071 19.128 -24.764 1.00 38.43  ? 33  PHE B CD2 1 
ATOM   1026 C  CE1 . PHE B 1 33  ? -21.589 18.118 -24.038 1.00 37.10  ? 33  PHE B CE1 1 
ATOM   1027 C  CE2 . PHE B 1 33  ? -23.907 17.758 -24.596 1.00 40.69  ? 33  PHE B CE2 1 
ATOM   1028 C  CZ  . PHE B 1 33  ? -22.663 17.261 -24.219 1.00 43.37  ? 33  PHE B CZ  1 
ATOM   1029 N  N   . ARG B 1 34  ? -23.967 24.035 -26.316 1.00 31.13  ? 34  ARG B N   1 
ATOM   1030 C  CA  A ARG B 1 34  ? -24.178 25.460 -26.193 0.50 32.21  ? 34  ARG B CA  1 
ATOM   1031 C  CA  B ARG B 1 34  ? -24.178 25.453 -26.188 0.50 33.18  ? 34  ARG B CA  1 
ATOM   1032 C  C   . ARG B 1 34  ? -25.211 25.634 -25.118 1.00 33.68  ? 34  ARG B C   1 
ATOM   1033 O  O   . ARG B 1 34  ? -26.171 24.833 -25.027 1.00 36.75  ? 34  ARG B O   1 
ATOM   1034 C  CB  A ARG B 1 34  ? -24.651 26.063 -27.530 0.50 33.26  ? 34  ARG B CB  1 
ATOM   1035 C  CB  B ARG B 1 34  ? -24.655 26.046 -27.520 0.50 35.68  ? 34  ARG B CB  1 
ATOM   1036 C  CG  A ARG B 1 34  ? -24.492 27.577 -27.641 0.50 33.63  ? 34  ARG B CG  1 
ATOM   1037 C  CG  B ARG B 1 34  ? -25.401 27.359 -27.376 0.50 38.59  ? 34  ARG B CG  1 
ATOM   1038 C  CD  A ARG B 1 34  ? -24.750 28.126 -29.062 0.50 36.06  ? 34  ARG B CD  1 
ATOM   1039 C  CD  B ARG B 1 34  ? -25.634 28.077 -28.703 0.50 41.92  ? 34  ARG B CD  1 
ATOM   1040 N  NE  A ARG B 1 34  ? -24.812 29.592 -29.051 0.50 37.68  ? 34  ARG B NE  1 
ATOM   1041 N  NE  B ARG B 1 34  ? -26.079 27.203 -29.785 0.50 43.17  ? 34  ARG B NE  1 
ATOM   1042 C  CZ  A ARG B 1 34  ? -25.749 30.283 -28.419 0.50 40.31  ? 34  ARG B CZ  1 
ATOM   1043 C  CZ  B ARG B 1 34  ? -25.606 27.297 -31.021 0.50 45.10  ? 34  ARG B CZ  1 
ATOM   1044 N  NH1 A ARG B 1 34  ? -26.711 29.634 -27.770 0.50 43.58  ? 34  ARG B NH1 1 
ATOM   1045 N  NH1 B ARG B 1 34  ? -24.648 28.196 -31.299 0.50 44.18  ? 34  ARG B NH1 1 
ATOM   1046 N  NH2 A ARG B 1 34  ? -25.744 31.608 -28.440 0.50 42.48  ? 34  ARG B NH2 1 
ATOM   1047 N  NH2 B ARG B 1 34  ? -26.057 26.485 -31.964 0.50 44.65  ? 34  ARG B NH2 1 
ATOM   1048 N  N   . LYS B 1 35  ? -25.042 26.665 -24.319 1.00 34.46  ? 35  LYS B N   1 
ATOM   1049 C  CA  . LYS B 1 35  ? -26.000 26.940 -23.249 1.00 37.55  ? 35  LYS B CA  1 
ATOM   1050 C  C   . LYS B 1 35  ? -27.218 27.524 -23.915 1.00 38.24  ? 35  LYS B C   1 
ATOM   1051 O  O   . LYS B 1 35  ? -27.087 28.486 -24.693 1.00 37.42  ? 35  LYS B O   1 
ATOM   1052 C  CB  . LYS B 1 35  ? -25.396 27.924 -22.205 1.00 37.70  ? 35  LYS B CB  1 
ATOM   1053 C  CG  . LYS B 1 35  ? -26.167 27.993 -20.858 1.00 41.76  ? 35  LYS B CG  1 
ATOM   1054 C  CD  . LYS B 1 35  ? -25.247 28.306 -19.668 1.00 43.38  ? 35  LYS B CD  1 
ATOM   1055 N  N   . ALA B 1 36  ? -28.392 26.935 -23.660 1.00 41.38  ? 36  ALA B N   1 
ATOM   1056 C  CA  . ALA B 1 36  ? -29.647 27.470 -24.167 1.00 46.04  ? 36  ALA B CA  1 
ATOM   1057 C  C   . ALA B 1 36  ? -30.220 28.515 -23.219 1.00 49.16  ? 36  ALA B C   1 
ATOM   1058 O  O   . ALA B 1 36  ? -29.782 28.657 -22.080 1.00 47.97  ? 36  ALA B O   1 
ATOM   1059 C  CB  . ALA B 1 36  ? -30.664 26.347 -24.399 1.00 45.87  ? 36  ALA B CB  1 
ATOM   1060 N  N   . ALA B 1 37  ? -31.206 29.248 -23.704 1.00 50.14  ? 37  ALA B N   1 
ATOM   1061 C  CA  . ALA B 1 37  ? -31.840 30.347 -22.938 1.00 55.51  ? 37  ALA B CA  1 
ATOM   1062 C  C   . ALA B 1 37  ? -32.385 29.873 -21.555 1.00 57.07  ? 37  ALA B C   1 
ATOM   1063 O  O   . ALA B 1 37  ? -32.332 30.623 -20.569 1.00 61.39  ? 37  ALA B O   1 
ATOM   1064 C  CB  . ALA B 1 37  ? -32.959 30.990 -23.769 1.00 54.77  ? 37  ALA B CB  1 
ATOM   1065 N  N   . ASP B 1 38  ? -32.805 28.608 -21.503 1.00 56.25  ? 38  ASP B N   1 
ATOM   1066 C  CA  . ASP B 1 38  ? -33.285 27.993 -20.240 1.00 57.11  ? 38  ASP B CA  1 
ATOM   1067 C  C   . ASP B 1 38  ? -32.093 27.621 -19.355 1.00 55.84  ? 38  ASP B C   1 
ATOM   1068 O  O   . ASP B 1 38  ? -32.316 26.859 -18.403 1.00 55.42  ? 38  ASP B O   1 
ATOM   1069 C  CB  . ASP B 1 38  ? -34.094 26.735 -20.548 1.00 57.93  ? 38  ASP B CB  1 
ATOM   1070 C  CG  . ASP B 1 38  ? -35.346 26.605 -19.700 1.00 62.22  ? 38  ASP B CG  1 
ATOM   1071 N  N   . THR B 1 40  ? -29.867 25.350 -19.642 1.00 46.18  ? 40  THR B N   1 
ATOM   1072 C  CA  . THR B 1 40  ? -29.655 23.937 -20.052 1.00 45.09  ? 40  THR B CA  1 
ATOM   1073 C  C   . THR B 1 40  ? -28.626 23.821 -21.180 1.00 43.54  ? 40  THR B C   1 
ATOM   1074 O  O   . THR B 1 40  ? -28.467 24.783 -21.930 1.00 41.53  ? 40  THR B O   1 
ATOM   1075 C  CB  . THR B 1 40  ? -30.961 23.268 -20.490 1.00 46.12  ? 40  THR B CB  1 
ATOM   1076 N  N   . TRP B 1 41  ? -28.004 22.653 -21.302 1.00 43.69  ? 41  TRP B N   1 
ATOM   1077 C  CA  . TRP B 1 41  ? -26.961 22.432 -22.312 1.00 42.67  ? 41  TRP B CA  1 
ATOM   1078 C  C   . TRP B 1 41  ? -27.529 21.696 -23.485 1.00 46.34  ? 41  TRP B C   1 
ATOM   1079 O  O   . TRP B 1 41  ? -28.085 20.605 -23.327 1.00 52.39  ? 41  TRP B O   1 
ATOM   1080 C  CB  . TRP B 1 41  ? -25.808 21.613 -21.718 1.00 42.39  ? 41  TRP B CB  1 
ATOM   1081 C  CG  . TRP B 1 41  ? -24.997 22.361 -20.715 1.00 42.41  ? 41  TRP B CG  1 
ATOM   1082 C  CD1 . TRP B 1 41  ? -24.929 22.157 -19.346 1.00 45.34  ? 41  TRP B CD1 1 
ATOM   1083 C  CD2 . TRP B 1 41  ? -24.103 23.486 -20.976 1.00 41.08  ? 41  TRP B CD2 1 
ATOM   1084 N  NE1 . TRP B 1 41  ? -24.088 23.048 -18.762 1.00 42.94  ? 41  TRP B NE1 1 
ATOM   1085 C  CE2 . TRP B 1 41  ? -23.560 23.880 -19.684 1.00 41.11  ? 41  TRP B CE2 1 
ATOM   1086 C  CE3 . TRP B 1 41  ? -23.717 24.171 -22.106 1.00 40.28  ? 41  TRP B CE3 1 
ATOM   1087 C  CZ2 . TRP B 1 41  ? -22.663 24.921 -19.550 1.00 41.51  ? 41  TRP B CZ2 1 
ATOM   1088 C  CZ3 . TRP B 1 41  ? -22.832 25.234 -21.965 1.00 38.10  ? 41  TRP B CZ3 1 
ATOM   1089 C  CH2 . TRP B 1 41  ? -22.314 25.595 -20.709 1.00 40.34  ? 41  TRP B CH2 1 
ATOM   1090 N  N   . GLU B 1 42  ? -27.435 22.289 -24.669 1.00 44.97  ? 42  GLU B N   1 
ATOM   1091 C  CA  . GLU B 1 42  ? -27.958 21.694 -25.887 1.00 45.88  ? 42  GLU B CA  1 
ATOM   1092 C  C   . GLU B 1 42  ? -26.753 21.164 -26.652 1.00 45.64  ? 42  GLU B C   1 
ATOM   1093 O  O   . GLU B 1 42  ? -25.799 21.909 -26.894 1.00 41.46  ? 42  GLU B O   1 
ATOM   1094 C  CB  . GLU B 1 42  ? -28.739 22.734 -26.738 1.00 44.91  ? 42  GLU B CB  1 
ATOM   1095 N  N   . PRO B 1 43  ? -26.775 19.876 -27.027 1.00 48.38  ? 43  PRO B N   1 
ATOM   1096 C  CA  . PRO B 1 43  ? -25.784 19.330 -27.957 1.00 44.51  ? 43  PRO B CA  1 
ATOM   1097 C  C   . PRO B 1 43  ? -25.664 20.100 -29.249 1.00 42.14  ? 43  PRO B C   1 
ATOM   1098 O  O   . PRO B 1 43  ? -26.664 20.496 -29.831 1.00 44.61  ? 43  PRO B O   1 
ATOM   1099 C  CB  . PRO B 1 43  ? -26.312 17.927 -28.248 1.00 49.61  ? 43  PRO B CB  1 
ATOM   1100 C  CG  . PRO B 1 43  ? -27.507 17.700 -27.361 1.00 47.61  ? 43  PRO B CG  1 
ATOM   1101 C  CD  . PRO B 1 43  ? -27.498 18.786 -26.341 1.00 50.38  ? 43  PRO B CD  1 
ATOM   1102 N  N   . PHE B 1 44  ? -24.430 20.261 -29.696 1.00 38.54  ? 44  PHE B N   1 
ATOM   1103 C  CA  . PHE B 1 44  ? -24.038 21.193 -30.735 1.00 42.08  ? 44  PHE B CA  1 
ATOM   1104 C  C   . PHE B 1 44  ? -23.186 20.476 -31.775 1.00 40.15  ? 44  PHE B C   1 
ATOM   1105 O  O   . PHE B 1 44  ? -23.416 20.595 -32.987 1.00 41.02  ? 44  PHE B O   1 
ATOM   1106 C  CB  . PHE B 1 44  ? -23.265 22.391 -30.108 1.00 40.17  ? 44  PHE B CB  1 
ATOM   1107 C  CG  . PHE B 1 44  ? -22.730 23.381 -31.118 1.00 43.93  ? 44  PHE B CG  1 
ATOM   1108 C  CD1 . PHE B 1 44  ? -23.577 24.257 -31.770 1.00 44.43  ? 44  PHE B CD1 1 
ATOM   1109 C  CD2 . PHE B 1 44  ? -21.372 23.459 -31.379 1.00 40.53  ? 44  PHE B CD2 1 
ATOM   1110 C  CE1 . PHE B 1 44  ? -23.060 25.187 -32.682 1.00 44.66  ? 44  PHE B CE1 1 
ATOM   1111 C  CE2 . PHE B 1 44  ? -20.862 24.345 -32.305 1.00 41.60  ? 44  PHE B CE2 1 
ATOM   1112 C  CZ  . PHE B 1 44  ? -21.716 25.218 -32.951 1.00 42.98  ? 44  PHE B CZ  1 
ATOM   1113 N  N   . ALA B 1 45  ? -22.229 19.695 -31.318 1.00 35.60  ? 45  ALA B N   1 
ATOM   1114 C  CA  . ALA B 1 45  ? -21.320 19.015 -32.213 1.00 35.79  ? 45  ALA B CA  1 
ATOM   1115 C  C   . ALA B 1 45  ? -20.644 17.901 -31.441 1.00 34.12  ? 45  ALA B C   1 
ATOM   1116 O  O   . ALA B 1 45  ? -20.637 17.902 -30.172 1.00 33.79  ? 45  ALA B O   1 
ATOM   1117 C  CB  . ALA B 1 45  ? -20.263 19.968 -32.780 1.00 32.76  ? 45  ALA B CB  1 
ATOM   1118 N  N   . SER B 1 46  ? -20.079 16.967 -32.179 1.00 31.47  ? 46  SER B N   1 
ATOM   1119 C  CA  . SER B 1 46  ? -19.238 15.953 -31.548 1.00 30.06  ? 46  SER B CA  1 
ATOM   1120 C  C   . SER B 1 46  ? -18.359 15.260 -32.549 1.00 32.10  ? 46  SER B C   1 
ATOM   1121 O  O   . SER B 1 46  ? -18.599 15.362 -33.768 1.00 31.54  ? 46  SER B O   1 
ATOM   1122 C  CB  . SER B 1 46  ? -20.119 14.947 -30.798 1.00 28.64  ? 46  SER B CB  1 
ATOM   1123 O  OG  . SER B 1 46  ? -20.954 14.206 -31.682 1.00 27.67  ? 46  SER B OG  1 
ATOM   1124 N  N   . GLY B 1 47  ? -17.401 14.510 -32.041 1.00 30.81  ? 47  GLY B N   1 
ATOM   1125 C  CA  . GLY B 1 47  ? -16.562 13.671 -32.868 1.00 31.66  ? 47  GLY B CA  1 
ATOM   1126 C  C   . GLY B 1 47  ? -15.519 12.960 -32.017 1.00 32.62  ? 47  GLY B C   1 
ATOM   1127 O  O   . GLY B 1 47  ? -15.609 12.937 -30.770 1.00 30.47  ? 47  GLY B O   1 
ATOM   1128 N  N   . LYS B 1 48  ? -14.585 12.291 -32.705 1.00 31.76  ? 48  LYS B N   1 
ATOM   1129 C  CA  . LYS B 1 48  ? -13.517 11.597 -32.032 1.00 32.24  ? 48  LYS B CA  1 
ATOM   1130 C  C   . LYS B 1 48  ? -12.175 12.168 -32.532 1.00 29.61  ? 48  LYS B C   1 
ATOM   1131 O  O   . LYS B 1 48  ? -12.009 12.426 -33.744 1.00 30.39  ? 48  LYS B O   1 
ATOM   1132 C  CB  . LYS B 1 48  ? -13.622 10.085 -32.266 1.00 35.85  ? 48  LYS B CB  1 
ATOM   1133 C  CG  . LYS B 1 48  ? -14.554 9.392  -31.273 0.50 35.75  ? 48  LYS B CG  1 
ATOM   1134 C  CD  . LYS B 1 48  ? -15.076 8.059  -31.781 0.50 39.22  ? 48  LYS B CD  1 
ATOM   1135 C  CE  . LYS B 1 48  ? -15.588 7.233  -30.612 0.50 38.31  ? 48  LYS B CE  1 
ATOM   1136 N  NZ  . LYS B 1 48  ? -14.654 7.412  -29.450 0.50 38.23  ? 48  LYS B NZ  1 
ATOM   1137 N  N   . THR B 1 49  ? -11.204 12.256 -31.646 1.00 27.47  ? 49  THR B N   1 
ATOM   1138 C  CA  . THR B 1 49  ? -9.869  12.745 -32.073 1.00 25.24  ? 49  THR B CA  1 
ATOM   1139 C  C   . THR B 1 49  ? -9.212  11.779 -33.091 1.00 28.29  ? 49  THR B C   1 
ATOM   1140 O  O   . THR B 1 49  ? -9.375  10.580 -33.003 1.00 26.59  ? 49  THR B O   1 
ATOM   1141 C  CB  . THR B 1 49  ? -8.905  12.954 -30.897 1.00 25.55  ? 49  THR B CB  1 
ATOM   1142 O  OG1 . THR B 1 49  ? -8.779  11.712 -30.180 1.00 25.04  ? 49  THR B OG1 1 
ATOM   1143 C  CG2 . THR B 1 49  ? -9.378  14.097 -29.995 1.00 24.21  ? 49  THR B CG2 1 
ATOM   1144 N  N   . SER B 1 50  ? -8.519  12.355 -34.075 1.00 29.07  ? 50  SER B N   1 
ATOM   1145 C  CA  . SER B 1 50  ? -7.748  11.646 -35.096 1.00 35.19  ? 50  SER B CA  1 
ATOM   1146 C  C   . SER B 1 50  ? -6.459  11.036 -34.557 1.00 33.99  ? 50  SER B C   1 
ATOM   1147 O  O   . SER B 1 50  ? -6.207  11.111 -33.336 1.00 28.90  ? 50  SER B O   1 
ATOM   1148 C  CB  . SER B 1 50  ? -7.361  12.613 -36.201 1.00 36.73  ? 50  SER B CB  1 
ATOM   1149 O  OG  . SER B 1 50  ? -6.326  13.438 -35.678 1.00 34.14  ? 50  SER B OG  1 
ATOM   1150 N  N   . GLU B 1 51  ? -5.720  10.350 -35.469 1.00 35.65  ? 51  GLU B N   1 
ATOM   1151 C  CA  . GLU B 1 51  ? -4.366  9.814  -35.187 1.00 37.67  ? 51  GLU B CA  1 
ATOM   1152 C  C   . GLU B 1 51  ? -3.406  10.868 -34.653 1.00 36.44  ? 51  GLU B C   1 
ATOM   1153 O  O   . GLU B 1 51  ? -2.442  10.566 -33.971 1.00 36.48  ? 51  GLU B O   1 
ATOM   1154 C  CB  . GLU B 1 51  ? -3.753  9.151  -36.464 1.00 37.72  ? 51  GLU B CB  1 
ATOM   1155 N  N   . SER B 1 52  ? -3.676  12.135 -34.945 1.00 37.93  ? 52  SER B N   1 
ATOM   1156 C  CA  . SER B 1 52  ? -2.853  13.217 -34.499 1.00 35.27  ? 52  SER B CA  1 
ATOM   1157 C  C   . SER B 1 52  ? -3.405  13.863 -33.218 1.00 32.68  ? 52  SER B C   1 
ATOM   1158 O  O   . SER B 1 52  ? -2.878  14.889 -32.786 1.00 29.26  ? 52  SER B O   1 
ATOM   1159 C  CB  . SER B 1 52  ? -2.789  14.261 -35.629 1.00 39.27  ? 52  SER B CB  1 
ATOM   1160 O  OG  . SER B 1 52  ? -4.055  14.896 -35.816 1.00 41.38  ? 52  SER B OG  1 
ATOM   1161 N  N   . GLY B 1 53  ? -4.461  13.276 -32.629 1.00 28.86  ? 53  GLY B N   1 
ATOM   1162 C  CA  . GLY B 1 53  ? -5.083  13.773 -31.412 1.00 28.87  ? 53  GLY B CA  1 
ATOM   1163 C  C   . GLY B 1 53  ? -5.905  15.037 -31.635 1.00 26.73  ? 53  GLY B C   1 
ATOM   1164 O  O   . GLY B 1 53  ? -6.171  15.740 -30.681 1.00 27.91  ? 53  GLY B O   1 
ATOM   1165 N  N   . GLU B 1 54  ? -6.309  15.310 -32.872 1.00 27.29  ? 54  GLU B N   1 
ATOM   1166 C  CA  . GLU B 1 54  ? -6.982  16.536 -33.240 1.00 27.87  ? 54  GLU B CA  1 
ATOM   1167 C  C   . GLU B 1 54  ? -8.399  16.216 -33.673 1.00 28.79  ? 54  GLU B C   1 
ATOM   1168 O  O   . GLU B 1 54  ? -8.672  15.170 -34.288 1.00 28.34  ? 54  GLU B O   1 
ATOM   1169 C  CB  . GLU B 1 54  ? -6.271  17.265 -34.381 1.00 30.96  ? 54  GLU B CB  1 
ATOM   1170 C  CG  . GLU B 1 54  ? -4.885  17.822 -34.094 0.50 31.22  ? 54  GLU B CG  1 
ATOM   1171 C  CD  . GLU B 1 54  ? -4.294  18.504 -35.331 0.50 35.74  ? 54  GLU B CD  1 
ATOM   1172 O  OE1 . GLU B 1 54  ? -4.314  17.899 -36.424 0.50 37.08  ? 54  GLU B OE1 1 
ATOM   1173 O  OE2 . GLU B 1 54  ? -3.823  19.658 -35.231 0.50 36.81  ? 54  GLU B OE2 1 
ATOM   1174 N  N   . LEU B 1 55  ? -9.290  17.137 -33.393 1.00 28.48  ? 55  LEU B N   1 
ATOM   1175 C  CA  . LEU B 1 55  ? -10.635 17.089 -33.909 1.00 31.10  ? 55  LEU B CA  1 
ATOM   1176 C  C   . LEU B 1 55  ? -10.944 18.439 -34.566 1.00 33.15  ? 55  LEU B C   1 
ATOM   1177 O  O   . LEU B 1 55  ? -10.960 19.486 -33.903 1.00 34.06  ? 55  LEU B O   1 
ATOM   1178 C  CB  . LEU B 1 55  ? -11.585 16.764 -32.791 1.00 31.16  ? 55  LEU B CB  1 
ATOM   1179 C  CG  . LEU B 1 55  ? -13.056 16.680 -33.121 1.00 30.19  ? 55  LEU B CG  1 
ATOM   1180 C  CD1 . LEU B 1 55  ? -13.390 15.624 -34.233 1.00 34.78  ? 55  LEU B CD1 1 
ATOM   1181 C  CD2 . LEU B 1 55  ? -13.737 16.331 -31.816 1.00 32.85  ? 55  LEU B CD2 1 
ATOM   1182 N  N   . HIS B 1 56  ? -11.110 18.373 -35.866 1.00 34.24  ? 56  HIS B N   1 
ATOM   1183 C  CA  . HIS B 1 56  ? -11.413 19.531 -36.731 1.00 39.98  ? 56  HIS B CA  1 
ATOM   1184 C  C   . HIS B 1 56  ? -12.839 19.424 -37.201 1.00 40.23  ? 56  HIS B C   1 
ATOM   1185 O  O   . HIS B 1 56  ? -13.499 18.383 -37.077 1.00 38.62  ? 56  HIS B O   1 
ATOM   1186 C  CB  . HIS B 1 56  ? -10.522 19.537 -37.990 1.00 41.25  ? 56  HIS B CB  1 
ATOM   1187 C  CG  . HIS B 1 56  ? -9.055  19.682 -37.709 1.00 45.76  ? 56  HIS B CG  1 
ATOM   1188 N  ND1 . HIS B 1 56  ? -8.479  20.875 -37.424 1.00 48.33  ? 56  HIS B ND1 1 
ATOM   1189 C  CD2 . HIS B 1 56  ? -8.034  18.738 -37.677 1.00 49.41  ? 56  HIS B CD2 1 
ATOM   1190 C  CE1 . HIS B 1 56  ? -7.166  20.693 -37.186 1.00 46.44  ? 56  HIS B CE1 1 
ATOM   1191 N  NE2 . HIS B 1 56  ? -6.894  19.386 -37.331 1.00 49.41  ? 56  HIS B NE2 1 
ATOM   1192 N  N   . GLY B 1 57  ? -13.342 20.492 -37.795 1.00 43.25  ? 57  GLY B N   1 
ATOM   1193 C  CA  . GLY B 1 57  ? -14.634 20.424 -38.479 1.00 42.99  ? 57  GLY B CA  1 
ATOM   1194 C  C   . GLY B 1 57  ? -15.831 20.336 -37.562 1.00 42.27  ? 57  GLY B C   1 
ATOM   1195 O  O   . GLY B 1 57  ? -16.905 20.003 -38.009 1.00 44.40  ? 57  GLY B O   1 
ATOM   1196 N  N   . LEU B 1 58  ? -15.678 20.667 -36.292 1.00 39.48  ? 58  LEU B N   1 
ATOM   1197 C  CA  . LEU B 1 58  ? -16.825 20.623 -35.399 1.00 40.23  ? 58  LEU B CA  1 
ATOM   1198 C  C   . LEU B 1 58  ? -17.951 21.580 -35.804 1.00 43.26  ? 58  LEU B C   1 
ATOM   1199 O  O   . LEU B 1 58  ? -19.138 21.202 -35.727 1.00 41.49  ? 58  LEU B O   1 
ATOM   1200 C  CB  . LEU B 1 58  ? -16.412 20.839 -33.949 1.00 37.44  ? 58  LEU B CB  1 
ATOM   1201 C  CG  . LEU B 1 58  ? -15.637 19.687 -33.327 1.00 36.33  ? 58  LEU B CG  1 
ATOM   1202 C  CD1 . LEU B 1 58  ? -14.862 20.184 -32.147 1.00 37.82  ? 58  LEU B CD1 1 
ATOM   1203 C  CD2 . LEU B 1 58  ? -16.606 18.594 -32.901 1.00 35.07  ? 58  LEU B CD2 1 
ATOM   1204 N  N   . THR B 1 59  ? -17.601 22.774 -36.296 1.00 41.07  ? 59  THR B N   1 
ATOM   1205 C  CA  . THR B 1 59  ? -18.587 23.778 -36.615 1.00 43.99  ? 59  THR B CA  1 
ATOM   1206 C  C   . THR B 1 59  ? -18.083 24.708 -37.710 1.00 44.55  ? 59  THR B C   1 
ATOM   1207 O  O   . THR B 1 59  ? -16.960 24.576 -38.171 1.00 44.71  ? 59  THR B O   1 
ATOM   1208 C  CB  . THR B 1 59  ? -18.962 24.559 -35.334 1.00 44.89  ? 59  THR B CB  1 
ATOM   1209 O  OG1 . THR B 1 59  ? -20.047 25.470 -35.585 1.00 46.94  ? 59  THR B OG1 1 
ATOM   1210 C  CG2 . THR B 1 59  ? -17.772 25.322 -34.795 1.00 43.53  ? 59  THR B CG2 1 
ATOM   1211 N  N   . THR B 1 60  ? -18.951 25.613 -38.148 1.00 48.41  ? 60  THR B N   1 
ATOM   1212 C  CA  . THR B 1 60  ? -18.625 26.561 -39.193 1.00 46.24  ? 60  THR B CA  1 
ATOM   1213 C  C   . THR B 1 60  ? -18.740 27.939 -38.604 1.00 43.62  ? 60  THR B C   1 
ATOM   1214 O  O   . THR B 1 60  ? -19.365 28.135 -37.533 1.00 38.03  ? 60  THR B O   1 
ATOM   1215 C  CB  . THR B 1 60  ? -19.629 26.501 -40.367 1.00 50.49  ? 60  THR B CB  1 
ATOM   1216 O  OG1 . THR B 1 60  ? -20.954 26.784 -39.866 1.00 47.69  ? 60  THR B OG1 1 
ATOM   1217 C  CG2 . THR B 1 60  ? -19.585 25.102 -41.090 1.00 52.71  ? 60  THR B CG2 1 
ATOM   1218 N  N   . GLU B 1 61  ? -18.145 28.878 -39.320 1.00 44.45  ? 61  GLU B N   1 
ATOM   1219 C  CA  . GLU B 1 61  ? -18.139 30.288 -38.957 1.00 48.22  ? 61  GLU B CA  1 
ATOM   1220 C  C   . GLU B 1 61  ? -19.573 30.812 -38.726 1.00 49.33  ? 61  GLU B C   1 
ATOM   1221 O  O   . GLU B 1 61  ? -19.811 31.570 -37.778 1.00 48.63  ? 61  GLU B O   1 
ATOM   1222 C  CB  . GLU B 1 61  ? -17.455 31.102 -40.079 1.00 50.38  ? 61  GLU B CB  1 
ATOM   1223 N  N   . GLU B 1 62  ? -20.506 30.394 -39.589 1.00 48.57  ? 62  GLU B N   1 
ATOM   1224 C  CA  . GLU B 1 62  ? -21.882 30.886 -39.567 1.00 51.78  ? 62  GLU B CA  1 
ATOM   1225 C  C   . GLU B 1 62  ? -22.603 30.366 -38.301 1.00 48.80  ? 62  GLU B C   1 
ATOM   1226 O  O   . GLU B 1 62  ? -23.353 31.124 -37.657 1.00 49.49  ? 62  GLU B O   1 
ATOM   1227 C  CB  . GLU B 1 62  ? -22.653 30.508 -40.867 0.50 52.75  ? 62  GLU B CB  1 
ATOM   1228 C  CG  . GLU B 1 62  ? -22.165 31.161 -42.173 0.50 55.85  ? 62  GLU B CG  1 
ATOM   1229 C  CD  . GLU B 1 62  ? -23.090 30.889 -43.371 0.50 59.85  ? 62  GLU B CD  1 
ATOM   1230 O  OE1 . GLU B 1 62  ? -23.099 31.672 -44.353 0.50 60.41  ? 62  GLU B OE1 1 
ATOM   1231 O  OE2 . GLU B 1 62  ? -23.830 29.880 -43.345 0.50 62.56  ? 62  GLU B OE2 1 
ATOM   1232 N  N   . GLU B 1 63  ? -22.320 29.120 -37.896 1.00 45.07  ? 63  GLU B N   1 
ATOM   1233 C  CA  . GLU B 1 63  ? -23.061 28.485 -36.771 1.00 44.21  ? 63  GLU B CA  1 
ATOM   1234 C  C   . GLU B 1 63  ? -22.542 28.887 -35.376 1.00 41.60  ? 63  GLU B C   1 
ATOM   1235 O  O   . GLU B 1 63  ? -23.273 28.828 -34.389 1.00 40.38  ? 63  GLU B O   1 
ATOM   1236 C  CB  . GLU B 1 63  ? -23.010 26.962 -36.913 1.00 30.00  ? 63  GLU B CB  1 
ATOM   1237 N  N   . PHE B 1 64  ? -21.268 29.262 -35.319 1.00 39.31  ? 64  PHE B N   1 
ATOM   1238 C  CA  . PHE B 1 64  ? -20.551 29.487 -34.081 1.00 36.63  ? 64  PHE B CA  1 
ATOM   1239 C  C   . PHE B 1 64  ? -20.682 30.926 -33.621 1.00 36.19  ? 64  PHE B C   1 
ATOM   1240 O  O   . PHE B 1 64  ? -19.726 31.697 -33.619 1.00 39.39  ? 64  PHE B O   1 
ATOM   1241 C  CB  . PHE B 1 64  ? -19.092 29.089 -34.276 1.00 35.17  ? 64  PHE B CB  1 
ATOM   1242 C  CG  . PHE B 1 64  ? -18.296 28.994 -33.015 1.00 35.22  ? 64  PHE B CG  1 
ATOM   1243 C  CD1 . PHE B 1 64  ? -18.753 28.260 -31.934 1.00 33.91  ? 64  PHE B CD1 1 
ATOM   1244 C  CD2 . PHE B 1 64  ? -17.021 29.561 -32.949 1.00 36.60  ? 64  PHE B CD2 1 
ATOM   1245 C  CE1 . PHE B 1 64  ? -17.977 28.168 -30.788 1.00 36.38  ? 64  PHE B CE1 1 
ATOM   1246 C  CE2 . PHE B 1 64  ? -16.249 29.460 -31.803 1.00 34.64  ? 64  PHE B CE2 1 
ATOM   1247 C  CZ  . PHE B 1 64  ? -16.737 28.761 -30.729 1.00 34.41  ? 64  PHE B CZ  1 
ATOM   1248 N  N   . VAL B 1 65  ? -21.866 31.250 -33.142 1.00 34.46  ? 65  VAL B N   1 
ATOM   1249 C  CA  . VAL B 1 65  ? -22.203 32.594 -32.731 1.00 35.76  ? 65  VAL B CA  1 
ATOM   1250 C  C   . VAL B 1 65  ? -21.770 32.776 -31.268 1.00 34.10  ? 65  VAL B C   1 
ATOM   1251 O  O   . VAL B 1 65  ? -21.502 31.808 -30.566 1.00 34.92  ? 65  VAL B O   1 
ATOM   1252 C  CB  . VAL B 1 65  ? -23.728 32.860 -32.850 1.00 35.99  ? 65  VAL B CB  1 
ATOM   1253 C  CG1 . VAL B 1 65  ? -24.244 32.690 -34.277 1.00 38.35  ? 65  VAL B CG1 1 
ATOM   1254 C  CG2 . VAL B 1 65  ? -24.512 31.937 -31.914 1.00 36.68  ? 65  VAL B CG2 1 
ATOM   1255 N  N   . GLU B 1 66  ? -21.735 34.024 -30.813 1.00 34.59  ? 66  GLU B N   1 
ATOM   1256 C  CA  . GLU B 1 66  ? -21.459 34.363 -29.384 1.00 36.13  ? 66  GLU B CA  1 
ATOM   1257 C  C   . GLU B 1 66  ? -22.362 33.532 -28.498 1.00 34.96  ? 66  GLU B C   1 
ATOM   1258 O  O   . GLU B 1 66  ? -23.536 33.391 -28.779 1.00 38.09  ? 66  GLU B O   1 
ATOM   1259 C  CB  . GLU B 1 66  ? -21.773 35.831 -29.101 1.00 40.46  ? 66  GLU B CB  1 
ATOM   1260 C  CG  . GLU B 1 66  ? -20.743 36.791 -29.679 1.00 42.39  ? 66  GLU B CG  1 
ATOM   1261 C  CD  . GLU B 1 66  ? -20.942 38.246 -29.199 1.00 47.14  ? 66  GLU B CD  1 
ATOM   1262 O  OE1 . GLU B 1 66  ? -21.813 38.959 -29.754 1.00 45.64  ? 66  GLU B OE1 1 
ATOM   1263 O  OE2 . GLU B 1 66  ? -20.194 38.663 -28.272 1.00 51.43  ? 66  GLU B OE2 1 
ATOM   1264 N  N   . GLY B 1 67  ? -21.837 33.022 -27.399 1.00 33.65  ? 67  GLY B N   1 
ATOM   1265 C  CA  . GLY B 1 67  ? -22.601 32.240 -26.484 1.00 33.45  ? 67  GLY B CA  1 
ATOM   1266 C  C   . GLY B 1 67  ? -21.674 31.556 -25.517 1.00 30.96  ? 67  GLY B C   1 
ATOM   1267 O  O   . GLY B 1 67  ? -20.473 31.737 -25.592 1.00 29.34  ? 67  GLY B O   1 
ATOM   1268 N  N   . ILE B 1 68  ? -22.231 30.736 -24.655 1.00 30.38  ? 68  ILE B N   1 
ATOM   1269 C  CA  . ILE B 1 68  ? -21.414 29.982 -23.702 1.00 29.46  ? 68  ILE B CA  1 
ATOM   1270 C  C   . ILE B 1 68  ? -21.435 28.554 -24.162 1.00 29.40  ? 68  ILE B C   1 
ATOM   1271 O  O   . ILE B 1 68  ? -22.511 28.015 -24.458 1.00 31.20  ? 68  ILE B O   1 
ATOM   1272 C  CB  . ILE B 1 68  ? -21.941 30.055 -22.244 1.00 31.39  ? 68  ILE B CB  1 
ATOM   1273 C  CG1 . ILE B 1 68  ? -21.941 31.516 -21.784 1.00 34.89  ? 68  ILE B CG1 1 
ATOM   1274 C  CG2 . ILE B 1 68  ? -21.068 29.157 -21.352 1.00 29.32  ? 68  ILE B CG2 1 
ATOM   1275 C  CD1 . ILE B 1 68  ? -22.451 31.771 -20.373 1.00 37.44  ? 68  ILE B CD1 1 
ATOM   1276 N  N   . TYR B 1 69  ? -20.236 27.998 -24.303 1.00 26.43  ? 69  TYR B N   1 
ATOM   1277 C  CA  . TYR B 1 69  ? -20.062 26.657 -24.822 1.00 25.55  ? 69  TYR B CA  1 
ATOM   1278 C  C   . TYR B 1 69  ? -19.344 25.783 -23.826 1.00 24.27  ? 69  TYR B C   1 
ATOM   1279 O  O   . TYR B 1 69  ? -18.551 26.259 -22.998 1.00 24.99  ? 69  TYR B O   1 
ATOM   1280 C  CB  . TYR B 1 69  ? -19.249 26.701 -26.128 1.00 28.12  ? 69  TYR B CB  1 
ATOM   1281 C  CG  . TYR B 1 69  ? -19.926 27.349 -27.279 1.00 26.30  ? 69  TYR B CG  1 
ATOM   1282 C  CD1 . TYR B 1 69  ? -19.927 28.732 -27.400 1.00 30.42  ? 69  TYR B CD1 1 
ATOM   1283 C  CD2 . TYR B 1 69  ? -20.656 26.588 -28.251 1.00 28.82  ? 69  TYR B CD2 1 
ATOM   1284 C  CE1 . TYR B 1 69  ? -20.576 29.350 -28.467 1.00 29.57  ? 69  TYR B CE1 1 
ATOM   1285 C  CE2 . TYR B 1 69  ? -21.283 27.221 -29.315 1.00 29.99  ? 69  TYR B CE2 1 
ATOM   1286 C  CZ  . TYR B 1 69  ? -21.245 28.610 -29.429 1.00 29.75  ? 69  TYR B CZ  1 
ATOM   1287 O  OH  . TYR B 1 69  ? -21.919 29.308 -30.506 1.00 31.75  ? 69  TYR B OH  1 
ATOM   1288 N  N   . LYS B 1 70  ? -19.622 24.497 -23.902 1.00 24.93  ? 70  LYS B N   1 
ATOM   1289 C  CA  . LYS B 1 70  ? -19.036 23.458 -23.051 1.00 25.06  ? 70  LYS B CA  1 
ATOM   1290 C  C   . LYS B 1 70  ? -18.445 22.448 -23.981 1.00 25.01  ? 70  LYS B C   1 
ATOM   1291 O  O   . LYS B 1 70  ? -19.096 22.004 -24.946 1.00 26.87  ? 70  LYS B O   1 
ATOM   1292 C  CB  . LYS B 1 70  ? -20.122 22.739 -22.183 1.00 26.70  ? 70  LYS B CB  1 
ATOM   1293 C  CG  . LYS B 1 70  ? -19.525 21.710 -21.284 1.00 31.17  ? 70  LYS B CG  1 
ATOM   1294 C  CD  . LYS B 1 70  ? -20.437 21.246 -20.157 1.00 33.27  ? 70  LYS B CD  1 
ATOM   1295 C  CE  . LYS B 1 70  ? -21.605 20.418 -20.637 1.00 38.21  ? 70  LYS B CE  1 
ATOM   1296 N  NZ  . LYS B 1 70  ? -22.437 19.906 -19.462 1.00 43.00  ? 70  LYS B NZ  1 
ATOM   1297 N  N   . VAL B 1 71  ? -17.199 22.067 -23.737 1.00 22.83  ? 71  VAL B N   1 
ATOM   1298 C  CA  . VAL B 1 71  ? -16.545 20.956 -24.447 1.00 24.62  ? 71  VAL B CA  1 
ATOM   1299 C  C   . VAL B 1 71  ? -16.259 19.865 -23.475 1.00 25.70  ? 71  VAL B C   1 
ATOM   1300 O  O   . VAL B 1 71  ? -15.505 20.077 -22.516 1.00 25.45  ? 71  VAL B O   1 
ATOM   1301 C  CB  . VAL B 1 71  ? -15.214 21.418 -25.080 1.00 26.09  ? 71  VAL B CB  1 
ATOM   1302 C  CG1 . VAL B 1 71  ? -14.512 20.218 -25.773 1.00 27.60  ? 71  VAL B CG1 1 
ATOM   1303 C  CG2 . VAL B 1 71  ? -15.459 22.595 -26.013 1.00 28.18  ? 71  VAL B CG2 1 
ATOM   1304 N  N   . GLU B 1 72  ? -16.894 18.717 -23.645 1.00 26.27  ? 72  GLU B N   1 
ATOM   1305 C  CA  . GLU B 1 72  ? -16.671 17.565 -22.753 1.00 27.71  ? 72  GLU B CA  1 
ATOM   1306 C  C   . GLU B 1 72  ? -15.851 16.522 -23.461 1.00 25.89  ? 72  GLU B C   1 
ATOM   1307 O  O   . GLU B 1 72  ? -16.229 16.039 -24.496 1.00 27.17  ? 72  GLU B O   1 
ATOM   1308 C  CB  . GLU B 1 72  ? -18.014 16.955 -22.304 1.00 29.74  ? 72  GLU B CB  1 
ATOM   1309 C  CG  . GLU B 1 72  ? -17.902 15.619 -21.585 0.50 30.84  ? 72  GLU B CG  1 
ATOM   1310 C  CD  . GLU B 1 72  ? -19.245 15.149 -21.031 0.50 34.89  ? 72  GLU B CD  1 
ATOM   1311 O  OE1 . GLU B 1 72  ? -20.183 15.972 -20.929 0.50 35.48  ? 72  GLU B OE1 1 
ATOM   1312 O  OE2 . GLU B 1 72  ? -19.358 13.958 -20.673 0.50 35.07  ? 72  GLU B OE2 1 
ATOM   1313 N  N   . ILE B 1 73  ? -14.707 16.188 -22.869 1.00 26.12  ? 73  ILE B N   1 
ATOM   1314 C  CA  . ILE B 1 73  ? -13.776 15.234 -23.417 1.00 26.51  ? 73  ILE B CA  1 
ATOM   1315 C  C   . ILE B 1 73  ? -13.830 13.961 -22.590 1.00 28.07  ? 73  ILE B C   1 
ATOM   1316 O  O   . ILE B 1 73  ? -13.719 14.015 -21.342 1.00 26.94  ? 73  ILE B O   1 
ATOM   1317 C  CB  . ILE B 1 73  ? -12.367 15.828 -23.332 1.00 25.96  ? 73  ILE B CB  1 
ATOM   1318 C  CG1 . ILE B 1 73  ? -12.293 17.139 -24.145 1.00 26.87  ? 73  ILE B CG1 1 
ATOM   1319 C  CG2 . ILE B 1 73  ? -11.367 14.763 -23.737 1.00 24.58  ? 73  ILE B CG2 1 
ATOM   1320 C  CD1 . ILE B 1 73  ? -11.023 17.930 -23.890 1.00 26.37  ? 73  ILE B CD1 1 
ATOM   1321 N  N   . ASP B 1 74  ? -14.058 12.831 -23.240 1.00 27.15  ? 74  ASP B N   1 
ATOM   1322 C  CA  . ASP B 1 74  ? -14.372 11.612 -22.493 1.00 29.76  ? 74  ASP B CA  1 
ATOM   1323 C  C   . ASP B 1 74  ? -13.098 10.923 -22.070 1.00 29.41  ? 74  ASP B C   1 
ATOM   1324 O  O   . ASP B 1 74  ? -12.713 9.950  -22.624 1.00 30.58  ? 74  ASP B O   1 
ATOM   1325 C  CB  . ASP B 1 74  ? -15.260 10.668 -23.265 1.00 34.76  ? 74  ASP B CB  1 
ATOM   1326 C  CG  . ASP B 1 74  ? -15.621 9.407  -22.474 1.00 39.62  ? 74  ASP B CG  1 
ATOM   1327 O  OD1 . ASP B 1 74  ? -15.101 9.150  -21.340 1.00 46.31  ? 74  ASP B OD1 1 
ATOM   1328 O  OD2 . ASP B 1 74  ? -16.469 8.682  -22.990 1.00 44.79  ? 74  ASP B OD2 1 
ATOM   1329 N  N   . THR B 1 75  ? -12.462 11.486 -21.045 1.00 27.92  ? 75  THR B N   1 
ATOM   1330 C  CA  . THR B 1 75  ? -11.114 11.014 -20.620 1.00 26.28  ? 75  THR B CA  1 
ATOM   1331 C  C   . THR B 1 75  ? -11.204 9.657  -19.964 1.00 24.83  ? 75  THR B C   1 
ATOM   1332 O  O   . THR B 1 75  ? -10.314 8.812  -20.094 1.00 25.89  ? 75  THR B O   1 
ATOM   1333 C  CB  . THR B 1 75  ? -10.497 12.047 -19.650 1.00 25.63  ? 75  THR B CB  1 
ATOM   1334 O  OG1 . THR B 1 75  ? -11.383 12.249 -18.536 1.00 25.11  ? 75  THR B OG1 1 
ATOM   1335 C  CG2 . THR B 1 75  ? -10.286 13.435 -20.362 1.00 26.87  ? 75  THR B CG2 1 
ATOM   1336 N  N   . LYS B 1 76  ? -12.311 9.393  -19.283 1.00 25.97  ? 76  LYS B N   1 
ATOM   1337 C  CA  . LYS B 1 76  ? -12.437 8.156  -18.542 1.00 26.11  ? 76  LYS B CA  1 
ATOM   1338 C  C   . LYS B 1 76  ? -12.407 6.885  -19.444 1.00 28.48  ? 76  LYS B C   1 
ATOM   1339 O  O   . LYS B 1 76  ? -11.734 5.926  -19.137 1.00 29.73  ? 76  LYS B O   1 
ATOM   1340 C  CB  . LYS B 1 76  ? -13.723 8.128  -17.690 1.00 29.06  ? 76  LYS B CB  1 
ATOM   1341 C  CG  . LYS B 1 76  ? -13.814 6.901  -16.792 0.50 27.63  ? 76  LYS B CG  1 
ATOM   1342 C  CD  . LYS B 1 76  ? -14.963 7.042  -15.779 0.50 30.11  ? 76  LYS B CD  1 
ATOM   1343 C  CE  . LYS B 1 76  ? -15.001 5.905  -14.751 0.50 32.12  ? 76  LYS B CE  1 
ATOM   1344 N  N   . SER B 1 77  ? -13.084 6.929  -20.594 1.00 31.49  ? 77  SER B N   1 
ATOM   1345 C  CA  . SER B 1 77  ? -13.060 5.791  -21.561 1.00 32.23  ? 77  SER B CA  1 
ATOM   1346 C  C   . SER B 1 77  ? -11.698 5.613  -22.179 1.00 29.37  ? 77  SER B C   1 
ATOM   1347 O  O   . SER B 1 77  ? -11.314 4.534  -22.494 1.00 28.96  ? 77  SER B O   1 
ATOM   1348 C  CB  . SER B 1 77  ? -14.046 6.012  -22.711 1.00 35.01  ? 77  SER B CB  1 
ATOM   1349 O  OG  . SER B 1 77  ? -15.348 6.131  -22.234 1.00 37.08  ? 77  SER B OG  1 
ATOM   1350 N  N   . TYR B 1 78  ? -10.998 6.726  -22.392 1.00 29.58  ? 78  TYR B N   1 
ATOM   1351 C  CA  . TYR B 1 78  ? -9.652  6.687  -22.973 1.00 28.92  ? 78  TYR B CA  1 
ATOM   1352 C  C   . TYR B 1 78  ? -8.745  5.866  -22.018 1.00 28.23  ? 78  TYR B C   1 
ATOM   1353 O  O   . TYR B 1 78  ? -8.145  4.942  -22.428 1.00 29.69  ? 78  TYR B O   1 
ATOM   1354 C  CB  . TYR B 1 78  ? -9.158  8.104  -23.195 1.00 28.92  ? 78  TYR B CB  1 
ATOM   1355 C  CG  . TYR B 1 78  ? -7.733  8.146  -23.694 1.00 28.17  ? 78  TYR B CG  1 
ATOM   1356 C  CD1 . TYR B 1 78  ? -7.443  7.851  -25.014 1.00 28.01  ? 78  TYR B CD1 1 
ATOM   1357 C  CD2 . TYR B 1 78  ? -6.682  8.458  -22.837 1.00 26.50  ? 78  TYR B CD2 1 
ATOM   1358 C  CE1 . TYR B 1 78  ? -6.153  7.845  -25.478 1.00 27.72  ? 78  TYR B CE1 1 
ATOM   1359 C  CE2 . TYR B 1 78  ? -5.381  8.433  -23.281 1.00 27.10  ? 78  TYR B CE2 1 
ATOM   1360 C  CZ  . TYR B 1 78  ? -5.114  8.155  -24.605 1.00 27.26  ? 78  TYR B CZ  1 
ATOM   1361 O  OH  . TYR B 1 78  ? -3.801  8.153  -25.129 1.00 28.45  ? 78  TYR B OH  1 
ATOM   1362 N  N   . TRP B 1 79  ? -8.703  6.224  -20.715 1.00 23.60  ? 79  TRP B N   1 
ATOM   1363 C  CA  . TRP B 1 79  ? -7.878  5.570  -19.763 1.00 25.00  ? 79  TRP B CA  1 
ATOM   1364 C  C   . TRP B 1 79  ? -8.303  4.111  -19.582 1.00 26.37  ? 79  TRP B C   1 
ATOM   1365 O  O   . TRP B 1 79  ? -7.478  3.245  -19.417 1.00 31.39  ? 79  TRP B O   1 
ATOM   1366 C  CB  . TRP B 1 79  ? -7.918  6.302  -18.435 1.00 23.29  ? 79  TRP B CB  1 
ATOM   1367 C  CG  . TRP B 1 79  ? -7.221  7.643  -18.507 1.00 21.58  ? 79  TRP B CG  1 
ATOM   1368 C  CD1 . TRP B 1 79  ? -7.742  8.881  -18.277 1.00 24.95  ? 79  TRP B CD1 1 
ATOM   1369 C  CD2 . TRP B 1 79  ? -5.841  7.889  -18.947 1.00 22.05  ? 79  TRP B CD2 1 
ATOM   1370 N  NE1 . TRP B 1 79  ? -6.792  9.856  -18.483 1.00 20.07  ? 79  TRP B NE1 1 
ATOM   1371 C  CE2 . TRP B 1 79  ? -5.638  9.313  -18.873 1.00 23.64  ? 79  TRP B CE2 1 
ATOM   1372 C  CE3 . TRP B 1 79  ? -4.784  7.097  -19.347 1.00 25.17  ? 79  TRP B CE3 1 
ATOM   1373 C  CZ2 . TRP B 1 79  ? -4.439  9.900  -19.216 1.00 21.95  ? 79  TRP B CZ2 1 
ATOM   1374 C  CZ3 . TRP B 1 79  ? -3.561  7.693  -19.692 1.00 24.46  ? 79  TRP B CZ3 1 
ATOM   1375 C  CH2 . TRP B 1 79  ? -3.406  9.101  -19.638 1.00 24.53  ? 79  TRP B CH2 1 
ATOM   1376 N  N   . LYS B 1 80  ? -9.610  3.874  -19.565 1.00 29.00  ? 80  LYS B N   1 
ATOM   1377 C  CA  A LYS B 1 80  ? -10.123 2.515  -19.394 0.50 32.87  ? 80  LYS B CA  1 
ATOM   1378 C  CA  B LYS B 1 80  ? -10.164 2.524  -19.414 0.50 31.99  ? 80  LYS B CA  1 
ATOM   1379 C  C   . LYS B 1 80  ? -9.649  1.594  -20.538 1.00 33.52  ? 80  LYS B C   1 
ATOM   1380 O  O   . LYS B 1 80  ? -9.282  0.398  -20.321 1.00 34.18  ? 80  LYS B O   1 
ATOM   1381 C  CB  A LYS B 1 80  ? -11.667 2.533  -19.323 0.50 35.02  ? 80  LYS B CB  1 
ATOM   1382 C  CB  B LYS B 1 80  ? -11.716 2.567  -19.478 0.50 32.68  ? 80  LYS B CB  1 
ATOM   1383 C  CG  A LYS B 1 80  ? -12.228 2.980  -17.976 0.50 37.62  ? 80  LYS B CG  1 
ATOM   1384 C  CG  B LYS B 1 80  ? -12.468 3.058  -18.236 0.50 33.76  ? 80  LYS B CG  1 
ATOM   1385 C  CD  A LYS B 1 80  ? -13.749 3.167  -17.993 0.50 37.02  ? 80  LYS B CD  1 
ATOM   1386 C  CD  B LYS B 1 80  ? -11.653 2.887  -16.962 0.50 31.76  ? 80  LYS B CD  1 
ATOM   1387 C  CE  A LYS B 1 80  ? -14.506 1.853  -17.910 0.50 40.49  ? 80  LYS B CE  1 
ATOM   1388 C  CE  B LYS B 1 80  ? -12.483 2.416  -15.754 0.50 31.94  ? 80  LYS B CE  1 
ATOM   1389 N  NZ  A LYS B 1 80  ? -15.702 2.059  -17.042 0.50 42.62  ? 80  LYS B NZ  1 
ATOM   1390 N  NZ  B LYS B 1 80  ? -11.641 2.242  -14.515 0.50 26.67  ? 80  LYS B NZ  1 
ATOM   1391 N  N   . ALA B 1 81  ? -9.631  2.142  -21.761 1.00 37.11  ? 81  ALA B N   1 
ATOM   1392 C  CA  . ALA B 1 81  ? -9.154  1.376  -22.935 1.00 41.66  ? 81  ALA B CA  1 
ATOM   1393 C  C   . ALA B 1 81  ? -7.657  1.032  -22.798 1.00 43.02  ? 81  ALA B C   1 
ATOM   1394 O  O   . ALA B 1 81  ? -7.179  0.042  -23.323 1.00 43.13  ? 81  ALA B O   1 
ATOM   1395 C  CB  . ALA B 1 81  ? -9.454  2.166  -24.218 1.00 40.79  ? 81  ALA B CB  1 
ATOM   1396 N  N   . LEU B 1 82  ? -6.893  1.844  -22.091 1.00 40.23  ? 82  LEU B N   1 
ATOM   1397 C  CA  . LEU B 1 82  ? -5.477  1.549  -21.897 1.00 41.01  ? 82  LEU B CA  1 
ATOM   1398 C  C   . LEU B 1 82  ? -5.211  0.732  -20.644 1.00 40.08  ? 82  LEU B C   1 
ATOM   1399 O  O   . LEU B 1 82  ? -4.068  0.376  -20.353 1.00 41.62  ? 82  LEU B O   1 
ATOM   1400 C  CB  . LEU B 1 82  ? -4.690  2.864  -21.802 1.00 39.56  ? 82  LEU B CB  1 
ATOM   1401 C  CG  . LEU B 1 82  ? -4.749  3.718  -23.072 1.00 41.67  ? 82  LEU B CG  1 
ATOM   1402 C  CD1 . LEU B 1 82  ? -4.140  5.069  -22.780 1.00 39.68  ? 82  LEU B CD1 1 
ATOM   1403 C  CD2 . LEU B 1 82  ? -4.038  2.994  -24.233 1.00 43.12  ? 82  LEU B CD2 1 
ATOM   1404 N  N   . GLY B 1 83  ? -6.249  0.465  -19.862 1.00 37.36  ? 83  GLY B N   1 
ATOM   1405 C  CA  . GLY B 1 83  ? -6.077  -0.331 -18.630 1.00 36.94  ? 83  GLY B CA  1 
ATOM   1406 C  C   . GLY B 1 83  ? -5.552  0.423  -17.434 1.00 36.27  ? 83  GLY B C   1 
ATOM   1407 O  O   . GLY B 1 83  ? -4.961  -0.181 -16.568 1.00 35.89  ? 83  GLY B O   1 
ATOM   1408 N  N   . ILE B 1 84  ? -5.828  1.742  -17.360 1.00 36.37  ? 84  ILE B N   1 
ATOM   1409 C  CA  . ILE B 1 84  ? -5.316  2.603  -16.325 1.00 33.62  ? 84  ILE B CA  1 
ATOM   1410 C  C   . ILE B 1 84  ? -6.509  3.253  -15.598 1.00 35.01  ? 84  ILE B C   1 
ATOM   1411 O  O   . ILE B 1 84  ? -7.494  3.655  -16.232 1.00 32.29  ? 84  ILE B O   1 
ATOM   1412 C  CB  . ILE B 1 84  ? -4.447  3.722  -16.943 1.00 39.38  ? 84  ILE B CB  1 
ATOM   1413 C  CG1 . ILE B 1 84  ? -3.274  3.137  -17.725 1.00 42.57  ? 84  ILE B CG1 1 
ATOM   1414 C  CG2 . ILE B 1 84  ? -3.916  4.615  -15.844 1.00 38.89  ? 84  ILE B CG2 1 
ATOM   1415 C  CD1 . ILE B 1 84  ? -2.377  4.137  -18.438 1.00 42.12  ? 84  ILE B CD1 1 
ATOM   1416 N  N   . SER B 1 85  ? -6.445  3.281  -14.275 1.00 32.53  ? 85  SER B N   1 
ATOM   1417 C  CA  . SER B 1 85  ? -7.527  3.685  -13.418 1.00 35.49  ? 85  SER B CA  1 
ATOM   1418 C  C   . SER B 1 85  ? -7.475  5.205  -13.324 1.00 33.23  ? 85  SER B C   1 
ATOM   1419 O  O   . SER B 1 85  ? -6.437  5.777  -12.949 1.00 31.85  ? 85  SER B O   1 
ATOM   1420 C  CB  . SER B 1 85  ? -7.343  3.053  -12.039 1.00 41.07  ? 85  SER B CB  1 
ATOM   1421 O  OG  . SER B 1 85  ? -8.591  2.883  -11.460 1.00 48.20  ? 85  SER B OG  1 
ATOM   1422 N  N   . PRO B 1 86  ? -8.515  5.858  -13.813 1.00 27.58  ? 86  PRO B N   1 
ATOM   1423 C  CA  . PRO B 1 86  ? -8.469  7.326  -13.791 1.00 27.38  ? 86  PRO B CA  1 
ATOM   1424 C  C   . PRO B 1 86  ? -9.258  7.935  -12.650 1.00 25.49  ? 86  PRO B C   1 
ATOM   1425 O  O   . PRO B 1 86  ? -10.147 7.315  -12.120 1.00 29.36  ? 86  PRO B O   1 
ATOM   1426 C  CB  . PRO B 1 86  ? -9.156  7.635  -15.119 1.00 27.86  ? 86  PRO B CB  1 
ATOM   1427 C  CG  . PRO B 1 86  ? -10.207 6.640  -15.238 1.00 30.87  ? 86  PRO B CG  1 
ATOM   1428 C  CD  . PRO B 1 86  ? -9.624  5.368  -14.650 1.00 28.80  ? 86  PRO B CD  1 
ATOM   1429 N  N   . PHE B 1 87  ? -9.029  9.196  -12.385 1.00 24.81  ? 87  PHE B N   1 
ATOM   1430 C  CA  . PHE B 1 87  ? -9.803  9.925  -11.385 1.00 24.55  ? 87  PHE B CA  1 
ATOM   1431 C  C   . PHE B 1 87  ? -11.069 10.551 -11.949 1.00 23.87  ? 87  PHE B C   1 
ATOM   1432 O  O   . PHE B 1 87  ? -12.126 10.411 -11.343 1.00 24.03  ? 87  PHE B O   1 
ATOM   1433 C  CB  . PHE B 1 87  ? -8.935  11.001 -10.778 1.00 24.19  ? 87  PHE B CB  1 
ATOM   1434 C  CG  . PHE B 1 87  ? -9.627  11.836 -9.787  1.00 24.26  ? 87  PHE B CG  1 
ATOM   1435 C  CD1 . PHE B 1 87  ? -9.927  11.311 -8.558  1.00 27.41  ? 87  PHE B CD1 1 
ATOM   1436 C  CD2 . PHE B 1 87  ? -9.986  13.135 -10.087 1.00 25.60  ? 87  PHE B CD2 1 
ATOM   1437 C  CE1 . PHE B 1 87  ? -10.486 12.064 -7.598  1.00 26.98  ? 87  PHE B CE1 1 
ATOM   1438 C  CE2 . PHE B 1 87  ? -10.658 13.902 -9.121  1.00 28.99  ? 87  PHE B CE2 1 
ATOM   1439 C  CZ  . PHE B 1 87  ? -10.899 13.341 -7.876  1.00 27.32  ? 87  PHE B CZ  1 
ATOM   1440 N  N   . HIS B 1 88  ? -10.962 11.297 -13.051 1.00 25.10  ? 88  HIS B N   1 
ATOM   1441 C  CA  . HIS B 1 88  ? -12.078 12.120 -13.497 1.00 23.54  ? 88  HIS B CA  1 
ATOM   1442 C  C   . HIS B 1 88  ? -13.039 11.327 -14.309 1.00 24.44  ? 88  HIS B C   1 
ATOM   1443 O  O   . HIS B 1 88  ? -12.667 10.459 -15.037 1.00 25.27  ? 88  HIS B O   1 
ATOM   1444 C  CB  . HIS B 1 88  ? -11.564 13.267 -14.339 1.00 24.63  ? 88  HIS B CB  1 
ATOM   1445 C  CG  . HIS B 1 88  ? -10.520 14.111 -13.651 1.00 25.62  ? 88  HIS B CG  1 
ATOM   1446 N  ND1 . HIS B 1 88  ? -9.203  13.790 -13.657 1.00 28.05  ? 88  HIS B ND1 1 
ATOM   1447 C  CD2 . HIS B 1 88  ? -10.632 15.282 -12.911 1.00 30.39  ? 88  HIS B CD2 1 
ATOM   1448 C  CE1 . HIS B 1 88  ? -8.514  14.675 -12.950 1.00 28.27  ? 88  HIS B CE1 1 
ATOM   1449 N  NE2 . HIS B 1 88  ? -9.364  15.613 -12.505 1.00 33.06  ? 88  HIS B NE2 1 
ATOM   1450 N  N   . GLU B 1 89  ? -14.284 11.685 -14.229 1.00 24.45  ? 89  GLU B N   1 
ATOM   1451 C  CA  . GLU B 1 89  ? -15.301 11.221 -15.177 1.00 27.00  ? 89  GLU B CA  1 
ATOM   1452 C  C   . GLU B 1 89  ? -15.050 11.698 -16.598 1.00 26.48  ? 89  GLU B C   1 
ATOM   1453 O  O   . GLU B 1 89  ? -15.282 10.939 -17.543 1.00 33.25  ? 89  GLU B O   1 
ATOM   1454 C  CB  . GLU B 1 89  ? -16.668 11.636 -14.679 1.00 29.27  ? 89  GLU B CB  1 
ATOM   1455 C  CG  . GLU B 1 89  ? -17.081 10.915 -13.415 1.00 32.03  ? 89  GLU B CG  1 
ATOM   1456 C  CD  . GLU B 1 89  ? -17.314 9.420  -13.654 1.00 37.05  ? 89  GLU B CD  1 
ATOM   1457 O  OE1 . GLU B 1 89  ? -18.159 9.062  -14.499 1.00 40.58  ? 89  GLU B OE1 1 
ATOM   1458 O  OE2 . GLU B 1 89  ? -16.661 8.600  -13.001 1.00 40.44  ? 89  GLU B OE2 1 
ATOM   1459 N  N   . HIS B 1 90  ? -14.605 12.935 -16.751 1.00 27.55  ? 90  HIS B N   1 
ATOM   1460 C  CA  . HIS B 1 90  ? -14.374 13.578 -18.021 1.00 28.94  ? 90  HIS B CA  1 
ATOM   1461 C  C   . HIS B 1 90  ? -13.685 14.860 -17.714 1.00 30.65  ? 90  HIS B C   1 
ATOM   1462 O  O   . HIS B 1 90  ? -13.572 15.304 -16.536 1.00 29.68  ? 90  HIS B O   1 
ATOM   1463 C  CB  . HIS B 1 90  ? -15.683 13.811 -18.850 1.00 30.97  ? 90  HIS B CB  1 
ATOM   1464 C  CG  . HIS B 1 90  ? -16.800 14.422 -18.057 1.00 36.47  ? 90  HIS B CG  1 
ATOM   1465 N  ND1 . HIS B 1 90  ? -16.761 15.700 -17.623 1.00 46.18  ? 90  HIS B ND1 1 
ATOM   1466 C  CD2 . HIS B 1 90  ? -17.986 13.878 -17.597 1.00 42.88  ? 90  HIS B CD2 1 
ATOM   1467 C  CE1 . HIS B 1 90  ? -17.889 15.981 -16.941 1.00 43.17  ? 90  HIS B CE1 1 
ATOM   1468 N  NE2 . HIS B 1 90  ? -18.641 14.859 -16.919 1.00 49.74  ? 90  HIS B NE2 1 
ATOM   1469 N  N   . ALA B 1 91  ? -13.177 15.503 -18.747 1.00 27.12  ? 91  ALA B N   1 
ATOM   1470 C  CA  . ALA B 1 91  ? -12.684 16.849 -18.630 1.00 29.37  ? 91  ALA B CA  1 
ATOM   1471 C  C   . ALA B 1 91  ? -13.683 17.754 -19.357 1.00 35.75  ? 91  ALA B C   1 
ATOM   1472 O  O   . ALA B 1 91  ? -14.036 17.443 -20.510 1.00 34.67  ? 91  ALA B O   1 
ATOM   1473 C  CB  . ALA B 1 91  ? -11.271 16.941 -19.221 1.00 30.67  ? 91  ALA B CB  1 
ATOM   1474 N  N   . GLU B 1 92  ? -14.177 18.819 -18.676 1.00 34.83  ? 92  GLU B N   1 
ATOM   1475 C  CA  . GLU B 1 92  ? -15.183 19.773 -19.181 1.00 34.26  ? 92  GLU B CA  1 
ATOM   1476 C  C   . GLU B 1 92  ? -14.513 21.122 -19.256 1.00 37.33  ? 92  GLU B C   1 
ATOM   1477 O  O   . GLU B 1 92  ? -13.891 21.534 -18.285 1.00 42.95  ? 92  GLU B O   1 
ATOM   1478 C  CB  . GLU B 1 92  ? -16.441 19.864 -18.282 1.00 39.46  ? 92  GLU B CB  1 
ATOM   1479 N  N   . VAL B 1 93  ? -14.583 21.789 -20.404 1.00 27.72  ? 93  VAL B N   1 
ATOM   1480 C  CA  . VAL B 1 93  ? -14.054 23.119 -20.561 1.00 27.22  ? 93  VAL B CA  1 
ATOM   1481 C  C   . VAL B 1 93  ? -15.250 24.025 -20.900 1.00 25.03  ? 93  VAL B C   1 
ATOM   1482 O  O   . VAL B 1 93  ? -15.954 23.789 -21.895 1.00 26.27  ? 93  VAL B O   1 
ATOM   1483 C  CB  . VAL B 1 93  ? -12.979 23.072 -21.643 1.00 33.43  ? 93  VAL B CB  1 
ATOM   1484 C  CG1 . VAL B 1 93  ? -12.385 24.438 -21.819 1.00 32.03  ? 93  VAL B CG1 1 
ATOM   1485 C  CG2 . VAL B 1 93  ? -11.894 22.051 -21.268 1.00 36.31  ? 93  VAL B CG2 1 
ATOM   1486 N  N   . VAL B 1 94  ? -15.525 25.045 -20.107 1.00 24.29  ? 94  VAL B N   1 
ATOM   1487 C  CA  . VAL B 1 94  ? -16.636 25.924 -20.353 1.00 23.93  ? 94  VAL B CA  1 
ATOM   1488 C  C   . VAL B 1 94  ? -16.147 27.359 -20.573 1.00 26.41  ? 94  VAL B C   1 
ATOM   1489 O  O   . VAL B 1 94  ? -15.380 27.904 -19.778 1.00 25.25  ? 94  VAL B O   1 
ATOM   1490 C  CB  . VAL B 1 94  ? -17.642 25.889 -19.171 1.00 25.76  ? 94  VAL B CB  1 
ATOM   1491 C  CG1 . VAL B 1 94  ? -18.856 26.753 -19.469 1.00 25.28  ? 94  VAL B CG1 1 
ATOM   1492 C  CG2 . VAL B 1 94  ? -18.103 24.489 -18.905 1.00 28.09  ? 94  VAL B CG2 1 
ATOM   1493 N  N   . PHE B 1 95  ? -16.589 27.991 -21.669 1.00 23.04  ? 95  PHE B N   1 
ATOM   1494 C  CA  . PHE B 1 95  ? -16.036 29.285 -22.056 1.00 25.77  ? 95  PHE B CA  1 
ATOM   1495 C  C   . PHE B 1 95  ? -17.061 30.070 -22.798 1.00 26.40  ? 95  PHE B C   1 
ATOM   1496 O  O   . PHE B 1 95  ? -17.942 29.514 -23.386 1.00 27.43  ? 95  PHE B O   1 
ATOM   1497 C  CB  . PHE B 1 95  ? -14.765 29.053 -22.858 1.00 25.82  ? 95  PHE B CB  1 
ATOM   1498 C  CG  . PHE B 1 95  ? -14.997 28.440 -24.206 1.00 27.02  ? 95  PHE B CG  1 
ATOM   1499 C  CD1 . PHE B 1 95  ? -15.083 27.088 -24.337 1.00 27.38  ? 95  PHE B CD1 1 
ATOM   1500 C  CD2 . PHE B 1 95  ? -15.099 29.222 -25.334 1.00 27.58  ? 95  PHE B CD2 1 
ATOM   1501 C  CE1 . PHE B 1 95  ? -15.289 26.540 -25.596 1.00 28.27  ? 95  PHE B CE1 1 
ATOM   1502 C  CE2 . PHE B 1 95  ? -15.253 28.659 -26.598 1.00 29.63  ? 95  PHE B CE2 1 
ATOM   1503 C  CZ  . PHE B 1 95  ? -15.367 27.309 -26.700 1.00 26.05  ? 95  PHE B CZ  1 
ATOM   1504 N  N   . THR B 1 96  ? -16.972 31.394 -22.735 1.00 29.39  ? 96  THR B N   1 
ATOM   1505 C  CA  . THR B 1 96  ? -17.799 32.228 -23.579 1.00 30.76  ? 96  THR B CA  1 
ATOM   1506 C  C   . THR B 1 96  ? -17.045 32.535 -24.855 1.00 34.97  ? 96  THR B C   1 
ATOM   1507 O  O   . THR B 1 96  ? -15.882 32.957 -24.797 1.00 33.47  ? 96  THR B O   1 
ATOM   1508 C  CB  . THR B 1 96  ? -18.067 33.602 -22.917 1.00 34.47  ? 96  THR B CB  1 
ATOM   1509 O  OG1 . THR B 1 96  ? -18.796 33.415 -21.683 1.00 35.69  ? 96  THR B OG1 1 
ATOM   1510 C  CG2 . THR B 1 96  ? -18.883 34.507 -23.889 1.00 35.44  ? 96  THR B CG2 1 
ATOM   1511 N  N   . ALA B 1 97  ? -17.744 32.437 -25.980 1.00 33.37  ? 97  ALA B N   1 
ATOM   1512 C  CA  . ALA B 1 97  ? -17.166 32.621 -27.301 1.00 34.92  ? 97  ALA B CA  1 
ATOM   1513 C  C   . ALA B 1 97  ? -17.500 33.961 -27.866 1.00 42.12  ? 97  ALA B C   1 
ATOM   1514 O  O   . ALA B 1 97  ? -18.598 34.528 -27.648 1.00 38.34  ? 97  ALA B O   1 
ATOM   1515 C  CB  . ALA B 1 97  ? -17.614 31.523 -28.255 1.00 39.57  ? 97  ALA B CB  1 
ATOM   1516 N  N   . ASN B 1 98  ? -16.469 34.499 -28.517 1.00 43.39  ? 98  ASN B N   1 
ATOM   1517 C  CA  . ASN B 1 98  ? -16.588 35.495 -29.595 1.00 46.74  ? 98  ASN B CA  1 
ATOM   1518 C  C   . ASN B 1 98  ? -16.930 36.836 -29.044 1.00 46.55  ? 98  ASN B C   1 
ATOM   1519 O  O   . ASN B 1 98  ? -17.300 37.772 -29.799 1.00 44.81  ? 98  ASN B O   1 
ATOM   1520 C  CB  . ASN B 1 98  ? -17.619 35.036 -30.616 1.00 46.71  ? 98  ASN B CB  1 
ATOM   1521 C  CG  . ASN B 1 98  ? -17.153 33.818 -31.374 1.00 48.52  ? 98  ASN B CG  1 
ATOM   1522 O  OD1 . ASN B 1 98  ? -15.926 33.641 -31.634 1.00 41.30  ? 98  ASN B OD1 1 
ATOM   1523 N  ND2 . ASN B 1 98  ? -18.104 32.979 -31.753 1.00 44.69  ? 98  ASN B ND2 1 
ATOM   1524 N  N   . ASP B 1 99  ? -16.865 36.912 -27.720 1.00 47.08  ? 99  ASP B N   1 
ATOM   1525 C  CA  . ASP B 1 99  ? -17.144 38.183 -27.029 1.00 51.11  ? 99  ASP B CA  1 
ATOM   1526 C  C   . ASP B 1 99  ? -16.392 39.321 -27.721 1.00 53.56  ? 99  ASP B C   1 
ATOM   1527 O  O   . ASP B 1 99  ? -16.988 40.408 -27.782 1.00 60.54  ? 99  ASP B O   1 
ATOM   1528 C  CB  . ASP B 1 99  ? -16.733 38.045 -25.591 1.00 46.69  ? 99  ASP B CB  1 
ATOM   1529 N  N   . GLY B 1 101 ? -15.669 39.568 -30.948 1.00 51.28  ? 101 GLY B N   1 
ATOM   1530 C  CA  . GLY B 1 101 ? -15.686 39.182 -32.369 1.00 53.30  ? 101 GLY B CA  1 
ATOM   1531 C  C   . GLY B 1 101 ? -15.092 37.816 -32.679 1.00 54.32  ? 101 GLY B C   1 
ATOM   1532 O  O   . GLY B 1 101 ? -14.278 37.338 -31.883 1.00 53.10  ? 101 GLY B O   1 
ATOM   1533 N  N   . PRO B 1 102 ? -15.559 37.109 -33.730 1.00 56.44  ? 102 PRO B N   1 
ATOM   1534 C  CA  . PRO B 1 102 ? -14.991 35.827 -34.174 1.00 56.65  ? 102 PRO B CA  1 
ATOM   1535 C  C   . PRO B 1 102 ? -13.470 35.586 -34.131 1.00 57.04  ? 102 PRO B C   1 
ATOM   1536 O  O   . PRO B 1 102 ? -12.664 36.379 -34.617 1.00 56.18  ? 102 PRO B O   1 
ATOM   1537 C  CB  . PRO B 1 102 ? -15.545 35.691 -35.589 1.00 60.71  ? 102 PRO B CB  1 
ATOM   1538 C  CG  . PRO B 1 102 ? -16.958 36.196 -35.410 1.00 63.18  ? 102 PRO B CG  1 
ATOM   1539 C  CD  . PRO B 1 102 ? -16.935 37.219 -34.269 1.00 63.48  ? 102 PRO B CD  1 
ATOM   1540 N  N   . ARG B 1 103 ? -13.097 34.456 -33.531 1.00 56.31  ? 103 ARG B N   1 
ATOM   1541 C  CA  . ARG B 1 103 ? -11.687 34.080 -33.405 1.00 55.44  ? 103 ARG B CA  1 
ATOM   1542 C  C   . ARG B 1 103 ? -11.569 32.586 -33.741 1.00 52.10  ? 103 ARG B C   1 
ATOM   1543 O  O   . ARG B 1 103 ? -12.591 31.864 -33.725 1.00 51.76  ? 103 ARG B O   1 
ATOM   1544 C  CB  . ARG B 1 103 ? -11.214 34.306 -31.965 1.00 57.63  ? 103 ARG B CB  1 
ATOM   1545 C  CG  . ARG B 1 103 ? -11.495 35.676 -31.376 1.00 58.21  ? 103 ARG B CG  1 
ATOM   1546 C  CD  . ARG B 1 103 ? -10.367 36.665 -31.635 1.00 58.68  ? 103 ARG B CD  1 
ATOM   1547 N  NE  . ARG B 1 103 ? -10.751 37.982 -31.125 1.00 64.06  ? 103 ARG B NE  1 
ATOM   1548 C  CZ  . ARG B 1 103 ? -11.633 38.806 -31.699 1.00 65.81  ? 103 ARG B CZ  1 
ATOM   1549 N  NH1 . ARG B 1 103 ? -12.240 38.482 -32.840 1.00 65.11  ? 103 ARG B NH1 1 
ATOM   1550 N  NH2 . ARG B 1 103 ? -11.912 39.979 -31.124 1.00 68.29  ? 103 ARG B NH2 1 
ATOM   1551 N  N   . ARG B 1 104 ? -10.353 32.116 -34.026 1.00 41.87  ? 104 ARG B N   1 
ATOM   1552 C  CA  . ARG B 1 104 ? -10.136 30.654 -34.061 1.00 37.64  ? 104 ARG B CA  1 
ATOM   1553 C  C   . ARG B 1 104 ? -9.745  30.257 -32.651 1.00 35.21  ? 104 ARG B C   1 
ATOM   1554 O  O   . ARG B 1 104 ? -8.923  30.956 -32.012 1.00 31.37  ? 104 ARG B O   1 
ATOM   1555 C  CB  . ARG B 1 104 ? -9.078  30.247 -35.069 1.00 37.79  ? 104 ARG B CB  1 
ATOM   1556 N  N   . TYR B 1 105 ? -10.404 29.211 -32.147 1.00 31.46  ? 105 TYR B N   1 
ATOM   1557 C  CA  . TYR B 1 105 ? -10.153 28.665 -30.844 1.00 31.07  ? 105 TYR B CA  1 
ATOM   1558 C  C   . TYR B 1 105 ? -9.604  27.271 -30.949 1.00 29.23  ? 105 TYR B C   1 
ATOM   1559 O  O   . TYR B 1 105 ? -10.241 26.464 -31.636 1.00 31.35  ? 105 TYR B O   1 
ATOM   1560 C  CB  . TYR B 1 105 ? -11.477 28.505 -30.102 1.00 33.46  ? 105 TYR B CB  1 
ATOM   1561 C  CG  . TYR B 1 105 ? -12.098 29.798 -29.717 1.00 33.48  ? 105 TYR B CG  1 
ATOM   1562 C  CD1 . TYR B 1 105 ? -11.801 30.389 -28.501 1.00 37.52  ? 105 TYR B CD1 1 
ATOM   1563 C  CD2 . TYR B 1 105 ? -13.004 30.423 -30.560 1.00 37.91  ? 105 TYR B CD2 1 
ATOM   1564 C  CE1 . TYR B 1 105 ? -12.388 31.611 -28.162 1.00 36.65  ? 105 TYR B CE1 1 
ATOM   1565 C  CE2 . TYR B 1 105 ? -13.594 31.629 -30.233 1.00 41.26  ? 105 TYR B CE2 1 
ATOM   1566 C  CZ  . TYR B 1 105 ? -13.296 32.201 -29.015 1.00 36.66  ? 105 TYR B CZ  1 
ATOM   1567 O  OH  . TYR B 1 105 ? -13.914 33.405 -28.753 1.00 42.15  ? 105 TYR B OH  1 
ATOM   1568 N  N   . THR B 1 106 ? -8.446  27.018 -30.322 1.00 28.77  ? 106 THR B N   1 
ATOM   1569 C  CA  . THR B 1 106 ? -7.915  25.677 -30.125 1.00 28.85  ? 106 THR B CA  1 
ATOM   1570 C  C   . THR B 1 106 ? -8.002  25.374 -28.659 1.00 27.33  ? 106 THR B C   1 
ATOM   1571 O  O   . THR B 1 106 ? -7.487  26.138 -27.812 1.00 26.78  ? 106 THR B O   1 
ATOM   1572 C  CB  . THR B 1 106 ? -6.462  25.509 -30.634 1.00 28.90  ? 106 THR B CB  1 
ATOM   1573 O  OG1 . THR B 1 106 ? -6.467  25.807 -32.031 1.00 33.80  ? 106 THR B OG1 1 
ATOM   1574 C  CG2 . THR B 1 106 ? -5.916  24.106 -30.469 1.00 36.98  ? 106 THR B CG2 1 
ATOM   1575 N  N   . ILE B 1 107 ? -8.716  24.324 -28.332 1.00 26.82  ? 107 ILE B N   1 
ATOM   1576 C  CA  . ILE B 1 107 ? -8.879  23.941 -26.918 1.00 25.84  ? 107 ILE B CA  1 
ATOM   1577 C  C   . ILE B 1 107 ? -7.957  22.774 -26.833 1.00 27.31  ? 107 ILE B C   1 
ATOM   1578 O  O   . ILE B 1 107 ? -8.173  21.735 -27.499 1.00 29.21  ? 107 ILE B O   1 
ATOM   1579 C  CB  . ILE B 1 107 ? -10.307 23.515 -26.545 1.00 28.02  ? 107 ILE B CB  1 
ATOM   1580 C  CG1 . ILE B 1 107 ? -11.328 24.682 -26.668 1.00 31.72  ? 107 ILE B CG1 1 
ATOM   1581 C  CG2 . ILE B 1 107 ? -10.322 22.828 -25.181 1.00 28.80  ? 107 ILE B CG2 1 
ATOM   1582 C  CD1 . ILE B 1 107 ? -10.896 25.930 -25.942 1.00 33.64  ? 107 ILE B CD1 1 
ATOM   1583 N  N   . ALA B 1 108 ? -6.920  22.916 -26.047 1.00 26.41  ? 108 ALA B N   1 
ATOM   1584 C  CA  . ALA B 1 108 ? -5.955  21.806 -25.905 1.00 25.60  ? 108 ALA B CA  1 
ATOM   1585 C  C   . ALA B 1 108 ? -6.038  21.200 -24.532 1.00 26.46  ? 108 ALA B C   1 
ATOM   1586 O  O   . ALA B 1 108 ? -6.166  21.924 -23.599 1.00 26.88  ? 108 ALA B O   1 
ATOM   1587 C  CB  . ALA B 1 108 ? -4.579  22.331 -26.165 1.00 28.66  ? 108 ALA B CB  1 
ATOM   1588 N  N   . ALA B 1 109 ? -5.928  19.893 -24.424 1.00 23.35  ? 109 ALA B N   1 
ATOM   1589 C  CA  . ALA B 1 109 ? -6.033  19.209 -23.127 1.00 22.97  ? 109 ALA B CA  1 
ATOM   1590 C  C   . ALA B 1 109 ? -4.863  18.225 -23.057 1.00 23.67  ? 109 ALA B C   1 
ATOM   1591 O  O   . ALA B 1 109 ? -4.639  17.432 -23.995 1.00 24.17  ? 109 ALA B O   1 
ATOM   1592 C  CB  . ALA B 1 109 ? -7.348  18.471 -22.913 1.00 25.41  ? 109 ALA B CB  1 
ATOM   1593 N  N   . LEU B 1 110 ? -4.177  18.232 -21.920 1.00 22.86  ? 110 LEU B N   1 
ATOM   1594 C  CA  . LEU B 1 110 ? -3.119  17.302 -21.628 1.00 21.66  ? 110 LEU B CA  1 
ATOM   1595 C  C   . LEU B 1 110 ? -3.582  16.416 -20.524 1.00 22.30  ? 110 LEU B C   1 
ATOM   1596 O  O   . LEU B 1 110 ? -3.866  16.924 -19.427 1.00 21.92  ? 110 LEU B O   1 
ATOM   1597 C  CB  . LEU B 1 110 ? -1.917  18.071 -21.155 1.00 22.53  ? 110 LEU B CB  1 
ATOM   1598 C  CG  . LEU B 1 110 ? -0.659  17.295 -20.772 1.00 25.24  ? 110 LEU B CG  1 
ATOM   1599 C  CD1 . LEU B 1 110 ? -0.137  16.457 -21.918 1.00 24.05  ? 110 LEU B CD1 1 
ATOM   1600 C  CD2 . LEU B 1 110 ? 0.408   18.269 -20.229 1.00 31.73  ? 110 LEU B CD2 1 
ATOM   1601 N  N   . LEU B 1 111 ? -3.571  15.127 -20.786 1.00 19.47  ? 111 LEU B N   1 
ATOM   1602 C  CA  . LEU B 1 111 ? -4.225  14.180 -19.893 1.00 20.65  ? 111 LEU B CA  1 
ATOM   1603 C  C   . LEU B 1 111 ? -3.247  13.307 -19.146 1.00 20.44  ? 111 LEU B C   1 
ATOM   1604 O  O   . LEU B 1 111 ? -2.335  12.661 -19.754 1.00 21.58  ? 111 LEU B O   1 
ATOM   1605 C  CB  . LEU B 1 111 ? -5.116  13.253 -20.688 1.00 21.56  ? 111 LEU B CB  1 
ATOM   1606 C  CG  . LEU B 1 111 ? -6.189  13.916 -21.508 1.00 24.16  ? 111 LEU B CG  1 
ATOM   1607 C  CD1 . LEU B 1 111 ? -7.043  12.811 -22.094 1.00 24.11  ? 111 LEU B CD1 1 
ATOM   1608 C  CD2 . LEU B 1 111 ? -7.014  14.962 -20.760 1.00 22.76  ? 111 LEU B CD2 1 
ATOM   1609 N  N   . SER B 1 112 ? -3.424  13.243 -17.816 1.00 21.82  ? 112 SER B N   1 
ATOM   1610 C  CA  . SER B 1 112 ? -2.857  12.154 -16.990 1.00 22.39  ? 112 SER B CA  1 
ATOM   1611 C  C   . SER B 1 112 ? -3.999  11.479 -16.195 1.00 25.48  ? 112 SER B C   1 
ATOM   1612 O  O   . SER B 1 112 ? -5.119  11.985 -16.097 1.00 23.50  ? 112 SER B O   1 
ATOM   1613 C  CB  . SER B 1 112 ? -1.730  12.641 -16.055 1.00 23.63  ? 112 SER B CB  1 
ATOM   1614 O  OG  . SER B 1 112 ? -0.719  13.458 -16.745 1.00 26.80  ? 112 SER B OG  1 
ATOM   1615 N  N   . PRO B 1 113 ? -3.732  10.313 -15.660 1.00 24.39  ? 113 PRO B N   1 
ATOM   1616 C  CA  . PRO B 1 113 ? -4.845  9.632  -14.968 1.00 24.71  ? 113 PRO B CA  1 
ATOM   1617 C  C   . PRO B 1 113 ? -5.499  10.393 -13.801 1.00 23.45  ? 113 PRO B C   1 
ATOM   1618 O  O   . PRO B 1 113 ? -6.707  10.273 -13.629 1.00 23.43  ? 113 PRO B O   1 
ATOM   1619 C  CB  . PRO B 1 113 ? -4.177  8.359  -14.467 1.00 23.91  ? 113 PRO B CB  1 
ATOM   1620 C  CG  . PRO B 1 113 ? -3.125  8.095  -15.469 1.00 25.56  ? 113 PRO B CG  1 
ATOM   1621 C  CD  . PRO B 1 113 ? -2.571  9.439  -15.792 1.00 23.78  ? 113 PRO B CD  1 
ATOM   1622 N  N   . TYR B 1 114 ? -4.699  11.116 -13.022 1.00 20.96  ? 114 TYR B N   1 
ATOM   1623 C  CA  . TYR B 1 114 ? -5.119  11.907 -11.915 1.00 21.68  ? 114 TYR B CA  1 
ATOM   1624 C  C   . TYR B 1 114 ? -5.028  13.384 -12.053 1.00 22.43  ? 114 TYR B C   1 
ATOM   1625 O  O   . TYR B 1 114 ? -5.181  14.116 -11.054 1.00 23.74  ? 114 TYR B O   1 
ATOM   1626 C  CB  . TYR B 1 114 ? -4.462  11.431 -10.646 1.00 22.97  ? 114 TYR B CB  1 
ATOM   1627 C  CG  . TYR B 1 114 ? -5.151  10.191 -10.071 1.00 24.42  ? 114 TYR B CG  1 
ATOM   1628 C  CD1 . TYR B 1 114 ? -5.010  8.987  -10.685 1.00 31.56  ? 114 TYR B CD1 1 
ATOM   1629 C  CD2 . TYR B 1 114 ? -5.875  10.248 -8.891  1.00 26.56  ? 114 TYR B CD2 1 
ATOM   1630 C  CE1 . TYR B 1 114 ? -5.599  7.861  -10.167 1.00 37.03  ? 114 TYR B CE1 1 
ATOM   1631 C  CE2 . TYR B 1 114 ? -6.515  9.115  -8.388  1.00 28.62  ? 114 TYR B CE2 1 
ATOM   1632 C  CZ  . TYR B 1 114 ? -6.346  7.960  -9.030  1.00 33.09  ? 114 TYR B CZ  1 
ATOM   1633 O  OH  . TYR B 1 114 ? -6.937  6.838  -8.525  1.00 47.07  ? 114 TYR B OH  1 
ATOM   1634 N  N   . SER B 1 115 ? -4.870  13.862 -13.285 1.00 22.82  ? 115 SER B N   1 
ATOM   1635 C  CA  . SER B 1 115 ? -4.643  15.293 -13.472 1.00 22.53  ? 115 SER B CA  1 
ATOM   1636 C  C   . SER B 1 115 ? -4.913  15.626 -14.931 1.00 23.06  ? 115 SER B C   1 
ATOM   1637 O  O   . SER B 1 115 ? -4.548  14.809 -15.834 1.00 24.02  ? 115 SER B O   1 
ATOM   1638 C  CB  . SER B 1 115 ? -3.154  15.629 -13.208 1.00 25.68  ? 115 SER B CB  1 
ATOM   1639 O  OG  . SER B 1 115 ? -3.028  17.057 -13.252 1.00 29.69  ? 115 SER B OG  1 
ATOM   1640 N  N   . TYR B 1 116 ? -5.440  16.800 -15.216 1.00 22.78  ? 116 TYR B N   1 
ATOM   1641 C  CA  . TYR B 1 116 ? -5.443  17.289 -16.612 1.00 21.93  ? 116 TYR B CA  1 
ATOM   1642 C  C   . TYR B 1 116 ? -5.207  18.762 -16.608 1.00 21.19  ? 116 TYR B C   1 
ATOM   1643 O  O   . TYR B 1 116 ? -5.513  19.503 -15.631 1.00 21.59  ? 116 TYR B O   1 
ATOM   1644 C  CB  . TYR B 1 116 ? -6.710  16.890 -17.421 1.00 24.11  ? 116 TYR B CB  1 
ATOM   1645 C  CG  . TYR B 1 116 ? -7.978  17.558 -16.996 1.00 24.51  ? 116 TYR B CG  1 
ATOM   1646 C  CD1 . TYR B 1 116 ? -8.300  18.847 -17.401 1.00 28.64  ? 116 TYR B CD1 1 
ATOM   1647 C  CD2 . TYR B 1 116 ? -8.853  16.915 -16.101 1.00 32.25  ? 116 TYR B CD2 1 
ATOM   1648 C  CE1 . TYR B 1 116 ? -9.490  19.439 -17.002 1.00 30.10  ? 116 TYR B CE1 1 
ATOM   1649 C  CE2 . TYR B 1 116 ? -10.005 17.516 -15.656 1.00 30.17  ? 116 TYR B CE2 1 
ATOM   1650 C  CZ  . TYR B 1 116 ? -10.304 18.776 -16.069 1.00 34.84  ? 116 TYR B CZ  1 
ATOM   1651 O  OH  . TYR B 1 116 ? -11.469 19.386 -15.646 0.50 37.38  ? 116 TYR B OH  1 
ATOM   1652 N  N   . SER B 1 117 ? -4.688  19.257 -17.728 1.00 22.15  ? 117 SER B N   1 
ATOM   1653 C  CA  . SER B 1 117 ? -4.530  20.669 -17.933 1.00 23.04  ? 117 SER B CA  1 
ATOM   1654 C  C   . SER B 1 117 ? -5.268  21.022 -19.247 1.00 21.76  ? 117 SER B C   1 
ATOM   1655 O  O   . SER B 1 117 ? -5.354  20.202 -20.164 1.00 22.02  ? 117 SER B O   1 
ATOM   1656 C  CB  . SER B 1 117 ? -3.063  21.118 -17.985 1.00 26.57  ? 117 SER B CB  1 
ATOM   1657 O  OG  . SER B 1 117 ? -2.422  20.648 -19.155 1.00 35.14  ? 117 SER B OG  1 
ATOM   1658 N  N   . THR B 1 118 ? -5.903  22.185 -19.279 1.00 23.41  ? 118 THR B N   1 
ATOM   1659 C  CA  . THR B 1 118 ? -6.506  22.641 -20.494 1.00 23.82  ? 118 THR B CA  1 
ATOM   1660 C  C   . THR B 1 118 ? -6.120  24.054 -20.727 1.00 26.68  ? 118 THR B C   1 
ATOM   1661 O  O   . THR B 1 118 ? -5.992  24.854 -19.765 1.00 29.07  ? 118 THR B O   1 
ATOM   1662 C  CB  . THR B 1 118 ? -8.008  22.432 -20.540 1.00 27.75  ? 118 THR B CB  1 
ATOM   1663 O  OG1 . THR B 1 118 ? -8.448  22.843 -21.839 1.00 36.70  ? 118 THR B OG1 1 
ATOM   1664 C  CG2 . THR B 1 118 ? -8.761  23.246 -19.477 1.00 26.45  ? 118 THR B CG2 1 
ATOM   1665 N  N   . THR B 1 119 ? -5.871  24.374 -21.979 1.00 23.91  ? 119 THR B N   1 
ATOM   1666 C  CA  . THR B 1 119 ? -5.484  25.705 -22.375 1.00 24.69  ? 119 THR B CA  1 
ATOM   1667 C  C   . THR B 1 119 ? -6.217  26.083 -23.637 1.00 24.45  ? 119 THR B C   1 
ATOM   1668 O  O   . THR B 1 119 ? -6.575  25.267 -24.379 1.00 26.92  ? 119 THR B O   1 
ATOM   1669 C  CB  . THR B 1 119 ? -3.952  25.842 -22.552 1.00 30.86  ? 119 THR B CB  1 
ATOM   1670 O  OG1 . THR B 1 119 ? -3.591  27.216 -22.703 1.00 37.59  ? 119 THR B OG1 1 
ATOM   1671 C  CG2 . THR B 1 119 ? -3.539  25.172 -23.728 1.00 28.95  ? 119 THR B CG2 1 
ATOM   1672 N  N   . ALA B 1 120 ? -6.449  27.346 -23.817 1.00 23.67  ? 120 ALA B N   1 
ATOM   1673 C  CA  . ALA B 1 120 ? -7.055  27.889 -25.013 1.00 24.04  ? 120 ALA B CA  1 
ATOM   1674 C  C   . ALA B 1 120 ? -6.055  28.742 -25.753 1.00 25.94  ? 120 ALA B C   1 
ATOM   1675 O  O   . ALA B 1 120 ? -5.389  29.589 -25.139 1.00 26.46  ? 120 ALA B O   1 
ATOM   1676 C  CB  . ALA B 1 120 ? -8.269  28.727 -24.652 1.00 25.63  ? 120 ALA B CB  1 
ATOM   1677 N  N   . VAL B 1 121 ? -5.931  28.479 -27.048 1.00 25.48  ? 121 VAL B N   1 
ATOM   1678 C  CA  . VAL B 1 121 ? -5.116  29.296 -27.972 1.00 27.23  ? 121 VAL B CA  1 
ATOM   1679 C  C   . VAL B 1 121 ? -6.121  29.975 -28.838 1.00 28.14  ? 121 VAL B C   1 
ATOM   1680 O  O   . VAL B 1 121 ? -6.885  29.342 -29.625 1.00 28.15  ? 121 VAL B O   1 
ATOM   1681 C  CB  . VAL B 1 121 ? -4.146  28.423 -28.769 1.00 29.71  ? 121 VAL B CB  1 
ATOM   1682 C  CG1 . VAL B 1 121 ? -3.258  29.280 -29.693 1.00 32.27  ? 121 VAL B CG1 1 
ATOM   1683 C  CG2 . VAL B 1 121 ? -3.364  27.534 -27.814 1.00 35.83  ? 121 VAL B CG2 1 
ATOM   1684 N  N   . VAL B 1 122 ? -6.229  31.277 -28.670 1.00 28.01  ? 122 VAL B N   1 
ATOM   1685 C  CA  . VAL B 1 122 ? -7.212  32.043 -29.373 1.00 31.76  ? 122 VAL B CA  1 
ATOM   1686 C  C   . VAL B 1 122 ? -6.492  32.954 -30.383 1.00 34.30  ? 122 VAL B C   1 
ATOM   1687 O  O   . VAL B 1 122 ? -5.747  33.819 -29.962 1.00 31.93  ? 122 VAL B O   1 
ATOM   1688 C  CB  . VAL B 1 122 ? -8.044  32.865 -28.370 1.00 32.73  ? 122 VAL B CB  1 
ATOM   1689 C  CG1 . VAL B 1 122 ? -9.130  33.625 -29.073 1.00 37.22  ? 122 VAL B CG1 1 
ATOM   1690 C  CG2 . VAL B 1 122 ? -8.675  31.940 -27.307 1.00 32.36  ? 122 VAL B CG2 1 
ATOM   1691 N  N   . THR B 1 123 ? -6.693  32.744 -31.689 1.00 37.03  ? 123 THR B N   1 
ATOM   1692 C  CA  . THR B 1 123 ? -5.965  33.491 -32.739 1.00 41.61  ? 123 THR B CA  1 
ATOM   1693 C  C   . THR B 1 123 ? -6.902  33.922 -33.866 1.00 48.44  ? 123 THR B C   1 
ATOM   1694 O  O   . THR B 1 123 ? -8.017  34.341 -33.607 1.00 49.02  ? 123 THR B O   1 
ATOM   1695 C  CB  . THR B 1 123 ? -4.836  32.653 -33.377 1.00 46.05  ? 123 THR B CB  1 
ATOM   1696 O  OG1 . THR B 1 123 ? -5.404  31.508 -34.021 1.00 53.25  ? 123 THR B OG1 1 
ATOM   1697 C  CG2 . THR B 1 123 ? -3.787  32.168 -32.332 1.00 47.45  ? 123 THR B CG2 1 
HETATM 1698 N  N12 . 6OT C 2 .   ? -1.147  21.020 -24.237 0.50 142.36 ? 201 6OT B N12 1 
HETATM 1699 C  C01 . 6OT C 2 .   ? 0.886   20.846 -28.562 0.50 110.60 ? 201 6OT B C01 1 
HETATM 1700 C  C02 . 6OT C 2 .   ? 0.024   21.691 -29.238 0.50 107.29 ? 201 6OT B C02 1 
HETATM 1701 C  C03 . 6OT C 2 .   ? -0.793  22.547 -28.524 0.50 110.26 ? 201 6OT B C03 1 
HETATM 1702 C  C04 . 6OT C 2 .   ? -0.752  22.563 -27.130 0.50 117.73 ? 201 6OT B C04 1 
HETATM 1703 C  C05 . 6OT C 2 .   ? 0.114   21.715 -26.440 0.50 126.47 ? 201 6OT B C05 1 
HETATM 1704 C  C06 . 6OT C 2 .   ? 0.935   20.855 -27.169 0.50 118.10 ? 201 6OT B C06 1 
HETATM 1705 CL CL7 . 6OT C 2 .   ? 1.928   19.751 -29.526 0.50 103.52 ? 201 6OT B CL7 1 
HETATM 1706 CL CL8 . 6OT C 2 .   ? -1.897  23.628 -29.433 0.50 102.16 ? 201 6OT B CL8 1 
HETATM 1707 S  S09 . 6OT C 2 .   ? 0.161   21.736 -24.833 0.50 144.60 ? 201 6OT B S09 1 
HETATM 1708 O  O10 . 6OT C 2 .   ? 0.202   23.096 -24.370 0.50 148.37 ? 201 6OT B O10 1 
HETATM 1709 O  O11 . 6OT C 2 .   ? 1.343   21.070 -24.353 0.50 146.39 ? 201 6OT B O11 1 
HETATM 1710 O  O   . HOH D 3 .   ? -8.717  17.536 -10.071 1.00 40.45  ? 201 HOH A O   1 
HETATM 1711 O  O   . HOH D 3 .   ? -13.342 21.235 2.208   1.00 37.02  ? 202 HOH A O   1 
HETATM 1712 O  O   . HOH D 3 .   ? -12.397 29.280 3.892   1.00 33.49  ? 203 HOH A O   1 
HETATM 1713 O  O   . HOH D 3 .   ? -11.609 31.696 -15.435 1.00 23.32  ? 204 HOH A O   1 
HETATM 1714 O  O   . HOH D 3 .   ? -12.482 8.724  -8.969  1.00 25.93  ? 205 HOH A O   1 
HETATM 1715 O  O   . HOH D 3 .   ? -14.390 18.251 3.893   1.00 31.14  ? 206 HOH A O   1 
HETATM 1716 O  O   . HOH D 3 .   ? -13.882 25.001 -17.764 1.00 26.25  ? 207 HOH A O   1 
HETATM 1717 O  O   . HOH D 3 .   ? -9.562  30.805 -17.381 1.00 24.70  ? 208 HOH A O   1 
HETATM 1718 O  O   . HOH D 3 .   ? -23.910 10.140 -7.105  1.00 35.31  ? 209 HOH A O   1 
HETATM 1719 O  O   . HOH D 3 .   ? -8.108  29.975 -14.568 1.00 22.50  ? 210 HOH A O   1 
HETATM 1720 O  O   . HOH D 3 .   ? -10.427 28.202 -14.884 1.00 36.10  ? 211 HOH A O   1 
HETATM 1721 O  O   . HOH D 3 .   ? -14.684 33.170 -7.109  1.00 27.40  ? 212 HOH A O   1 
HETATM 1722 O  O   . HOH D 3 .   ? -26.867 7.156  -3.300  1.00 27.34  ? 213 HOH A O   1 
HETATM 1723 O  O   . HOH D 3 .   ? -23.707 23.363 -3.637  1.00 32.04  ? 214 HOH A O   1 
HETATM 1724 O  O   . HOH D 3 .   ? -7.916  40.681 -19.720 1.00 39.16  ? 215 HOH A O   1 
HETATM 1725 O  O   . HOH D 3 .   ? -5.769  13.572 0.035   1.00 36.04  ? 216 HOH A O   1 
HETATM 1726 O  O   . HOH D 3 .   ? -24.625 27.015 -1.842  1.00 41.18  ? 217 HOH A O   1 
HETATM 1727 O  O   . HOH D 3 .   ? -11.421 26.688 5.023   1.00 32.39  ? 218 HOH A O   1 
HETATM 1728 O  O   . HOH D 3 .   ? -24.305 23.976 -1.127  1.00 41.24  ? 219 HOH A O   1 
HETATM 1729 O  O   . HOH D 3 .   ? -24.378 25.616 -4.513  1.00 32.67  ? 220 HOH A O   1 
HETATM 1730 O  O   . HOH E 3 .   ? -9.449  2.220  -16.272 1.00 44.21  ? 301 HOH B O   1 
HETATM 1731 O  O   . HOH E 3 .   ? -13.520 16.904 -14.497 1.00 25.52  ? 302 HOH B O   1 
HETATM 1732 O  O   . HOH E 3 .   ? -9.211  25.285 -22.355 1.00 34.68  ? 303 HOH B O   1 
HETATM 1733 O  O   . HOH E 3 .   ? -10.545 10.506 -16.744 1.00 27.12  ? 304 HOH B O   1 
HETATM 1734 O  O   . HOH E 3 .   ? -14.411 8.934  -11.568 1.00 28.44  ? 305 HOH B O   1 
HETATM 1735 O  O   . HOH E 3 .   ? -8.554  11.639 -15.149 1.00 26.39  ? 306 HOH B O   1 
HETATM 1736 O  O   . HOH E 3 .   ? -13.201 8.781  -25.092 1.00 34.27  ? 307 HOH B O   1 
HETATM 1737 O  O   . HOH E 3 .   ? -7.239  12.739 -17.721 1.00 22.74  ? 308 HOH B O   1 
HETATM 1738 O  O   . HOH E 3 .   ? -25.024 30.259 -25.246 1.00 36.89  ? 309 HOH B O   1 
HETATM 1739 O  O   . HOH E 3 .   ? -3.796  7.457  -27.968 1.00 37.04  ? 310 HOH B O   1 
HETATM 1740 O  O   . HOH E 3 .   ? -0.000  21.725 -21.671 0.50 46.48  ? 311 HOH B O   1 
HETATM 1741 O  O   . HOH E 3 .   ? -10.380 15.827 -37.151 1.00 39.26  ? 312 HOH B O   1 
HETATM 1742 O  O   . HOH E 3 .   ? -14.987 12.527 -35.636 1.00 34.12  ? 313 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    C CA  . CYS A 10  ? 0.5810 0.6085 0.5360 -0.0254 0.0475  0.0289  10  CYS A CA  
2    C C   . CYS A 10  ? 0.5429 0.5626 0.5097 -0.0223 0.0457  0.0319  10  CYS A C   
3    O O   . CYS A 10  ? 0.5257 0.5438 0.4934 -0.0209 0.0418  0.0346  10  CYS A O   
4    N N   . PRO A 11  ? 0.4549 0.4703 0.4308 -0.0216 0.0489  0.0311  11  PRO A N   
5    C CA  . PRO A 11  ? 0.4070 0.4144 0.3932 -0.0195 0.0482  0.0322  11  PRO A CA  
6    C C   . PRO A 11  ? 0.3338 0.3357 0.3232 -0.0173 0.0451  0.0249  11  PRO A C   
7    O O   . PRO A 11  ? 0.3474 0.3433 0.3428 -0.0156 0.0439  0.0259  11  PRO A O   
8    C CB  . PRO A 11  ? 0.4102 0.4165 0.4037 -0.0211 0.0526  0.0316  11  PRO A CB  
9    C CG  . PRO A 11  ? 0.4641 0.4787 0.4516 -0.0235 0.0562  0.0317  11  PRO A CG  
10   C CD  . PRO A 11  ? 0.4658 0.4846 0.4425 -0.0233 0.0538  0.0279  11  PRO A CD  
11   N N   . LEU A 12  ? 0.3428 0.3462 0.3280 -0.0174 0.0441  0.0178  12  LEU A N   
12   C CA  . LEU A 12  ? 0.3326 0.3310 0.3209 -0.0156 0.0411  0.0118  12  LEU A CA  
13   C C   . LEU A 12  ? 0.3588 0.3585 0.3397 -0.0157 0.0385  0.0076  12  LEU A C   
14   O O   . LEU A 12  ? 0.4163 0.4192 0.3925 -0.0167 0.0404  0.0038  12  LEU A O   
15   C CB  . LEU A 12  ? 0.3471 0.3441 0.3423 -0.0154 0.0430  0.0068  12  LEU A CB  
16   C CG  . LEU A 12  ? 0.3829 0.3755 0.3815 -0.0137 0.0397  0.0015  12  LEU A CG  
17   C CD1 . LEU A 12  ? 0.3597 0.3473 0.3605 -0.0130 0.0374  0.0038  12  LEU A CD1 
18   C CD2 . LEU A 12  ? 0.3928 0.3867 0.3990 -0.0138 0.0412  -0.0024 12  LEU A CD2 
19   N N   . MET A 13  ? 0.3329 0.3303 0.3126 -0.0150 0.0347  0.0083  13  MET A N   
20   C CA  . MET A 13  ? 0.3237 0.3213 0.2970 -0.0158 0.0316  0.0045  13  MET A CA  
21   C C   . MET A 13  ? 0.2827 0.2750 0.2599 -0.0143 0.0288  0.0018  13  MET A C   
22   O O   . MET A 13  ? 0.2996 0.2896 0.2819 -0.0129 0.0284  0.0041  13  MET A O   
23   C CB  . MET A 13  ? 0.3456 0.3485 0.3129 -0.0177 0.0295  0.0096  13  MET A CB  
24   C CG  . MET A 13  ? 0.3868 0.3906 0.3464 -0.0202 0.0265  0.0054  13  MET A CG  
25   S SD  . MET A 13  ? 0.4479 0.4490 0.4094 -0.0202 0.0216  0.0054  13  MET A SD  
26   C CE  . MET A 13  ? 0.4558 0.4663 0.4144 -0.0222 0.0189  0.0138  13  MET A CE  
27   N N   . VAL A 14  ? 0.2815 0.2712 0.2560 -0.0147 0.0270  -0.0033 14  VAL A N   
28   C CA  . VAL A 14  ? 0.2851 0.2701 0.2624 -0.0137 0.0241  -0.0054 14  VAL A CA  
29   C C   . VAL A 14  ? 0.3185 0.3032 0.2900 -0.0159 0.0211  -0.0061 14  VAL A C   
30   O O   . VAL A 14  ? 0.3250 0.3099 0.2909 -0.0178 0.0215  -0.0095 14  VAL A O   
31   C CB  . VAL A 14  ? 0.2763 0.2577 0.2580 -0.0120 0.0247  -0.0101 14  VAL A CB  
32   C CG1 . VAL A 14  ? 0.3147 0.2914 0.2982 -0.0113 0.0210  -0.0111 14  VAL A CG1 
33   C CG2 . VAL A 14  ? 0.3200 0.3030 0.3082 -0.0108 0.0275  -0.0095 14  VAL A CG2 
34   N N   . LYS A 15  ? 0.2977 0.2819 0.2705 -0.0161 0.0184  -0.0035 15  LYS A N   
35   C CA  . LYS A 15  ? 0.3084 0.2929 0.2773 -0.0188 0.0152  -0.0033 15  LYS A CA  
36   C C   . LYS A 15  ? 0.3129 0.2927 0.2845 -0.0184 0.0130  -0.0041 15  LYS A C   
37   O O   . LYS A 15  ? 0.2879 0.2674 0.2635 -0.0164 0.0134  -0.0022 15  LYS A O   
38   C CB  . LYS A 15  ? 0.3179 0.3094 0.2866 -0.0197 0.0143  0.0027  15  LYS A CB  
39   C CG  . LYS A 15  ? 0.4148 0.4095 0.3812 -0.0230 0.0107  0.0045  15  LYS A CG  
40   C CD  . LYS A 15  ? 0.4782 0.4730 0.4375 -0.0274 0.0087  0.0010  15  LYS A CD  
41   C CE  . LYS A 15  ? 0.5661 0.5665 0.5241 -0.0316 0.0047  0.0041  15  LYS A CE  
42   N N   . VAL A 16  ? 0.2837 0.2591 0.2527 -0.0205 0.0109  -0.0071 16  VAL A N   
43   C CA  . VAL A 16  ? 0.2705 0.2410 0.2419 -0.0202 0.0088  -0.0070 16  VAL A CA  
44   C C   . VAL A 16  ? 0.2916 0.2616 0.2599 -0.0245 0.0058  -0.0060 16  VAL A C   
45   O O   . VAL A 16  ? 0.3125 0.2805 0.2765 -0.0275 0.0051  -0.0092 16  VAL A O   
46   C CB  . VAL A 16  ? 0.2878 0.2512 0.2615 -0.0181 0.0092  -0.0113 16  VAL A CB  
47   C CG1 . VAL A 16  ? 0.2995 0.2589 0.2762 -0.0174 0.0067  -0.0094 16  VAL A CG1 
48   C CG2 . VAL A 16  ? 0.2897 0.2553 0.2671 -0.0147 0.0124  -0.0127 16  VAL A CG2 
49   N N   . LEU A 17  ? 0.2816 0.2534 0.2518 -0.0252 0.0043  -0.0021 17  LEU A N   
50   C CA  . LEU A 17  ? 0.2815 0.2541 0.2503 -0.0296 0.0016  0.0000  17  LEU A CA  
51   C C   . LEU A 17  ? 0.2982 0.2649 0.2687 -0.0299 0.0001  0.0010  17  LEU A C   
52   O O   . LEU A 17  ? 0.3089 0.2749 0.2816 -0.0267 0.0010  0.0020  17  LEU A O   
53   C CB  . LEU A 17  ? 0.2997 0.2825 0.2703 -0.0303 0.0018  0.0051  17  LEU A CB  
54   C CG  . LEU A 17  ? 0.3725 0.3635 0.3423 -0.0303 0.0025  0.0068  17  LEU A CG  
55   C CD1 . LEU A 17  ? 0.4056 0.4067 0.3797 -0.0305 0.0023  0.0131  17  LEU A CD1 
56   C CD2 . LEU A 17  ? 0.3794 0.3695 0.3437 -0.0351 0.0002  0.0037  17  LEU A CD2 
57   N N   . ASP A 18  ? 0.2821 0.2448 0.2511 -0.0345 -0.0024 0.0011  18  ASP A N   
58   C CA  . ASP A 18  ? 0.2928 0.2494 0.2633 -0.0359 -0.0043 0.0034  18  ASP A CA  
59   C C   . ASP A 18  ? 0.3129 0.2769 0.2839 -0.0397 -0.0053 0.0089  18  ASP A C   
60   O O   . ASP A 18  ? 0.3008 0.2687 0.2711 -0.0444 -0.0066 0.0095  18  ASP A O   
61   C CB  . ASP A 18  ? 0.3202 0.2659 0.2894 -0.0383 -0.0058 -0.0007 18  ASP A CB  
62   C CG  . ASP A 18  ? 0.3620 0.3000 0.3328 -0.0407 -0.0081 0.0024  18  ASP A CG  
63   O OD1 . ASP A 18  ? 0.3619 0.3050 0.3335 -0.0430 -0.0091 0.0081  18  ASP A OD1 
64   O OD2 . ASP A 18  ? 0.4170 0.3435 0.3887 -0.0402 -0.0087 -0.0009 18  ASP A OD2 
65   N N   . ALA A 19  ? 0.2839 0.2514 0.2564 -0.0377 -0.0043 0.0127  19  ALA A N   
66   C CA  . ALA A 19  ? 0.2818 0.2577 0.2554 -0.0407 -0.0040 0.0180  19  ALA A CA  
67   C C   . ALA A 19  ? 0.3027 0.2747 0.2764 -0.0461 -0.0065 0.0215  19  ALA A C   
68   O O   . ALA A 19  ? 0.3222 0.3023 0.2974 -0.0494 -0.0061 0.0263  19  ALA A O   
69   C CB  . ALA A 19  ? 0.2958 0.2774 0.2699 -0.0363 -0.0009 0.0197  19  ALA A CB  
70   N N   . VAL A 20  ? 0.3064 0.2663 0.2792 -0.0469 -0.0087 0.0197  20  VAL A N   
71   C CA  . VAL A 20  ? 0.3326 0.2857 0.3059 -0.0524 -0.0112 0.0230  20  VAL A CA  
72   C C   . VAL A 20  ? 0.3586 0.3098 0.3318 -0.0583 -0.0130 0.0204  20  VAL A C   
73   O O   . VAL A 20  ? 0.4275 0.3803 0.4019 -0.0647 -0.0146 0.0244  20  VAL A O   
74   C CB  . VAL A 20  ? 0.3704 0.3103 0.3441 -0.0499 -0.0127 0.0228  20  VAL A CB  
75   C CG1 . VAL A 20  ? 0.4098 0.3394 0.3847 -0.0554 -0.0154 0.0260  20  VAL A CG1 
76   C CG2 . VAL A 20  ? 0.3647 0.3085 0.3378 -0.0453 -0.0119 0.0260  20  VAL A CG2 
77   N N   . ARG A 21  ? 0.3244 0.2729 0.2958 -0.0571 -0.0129 0.0139  21  ARG A N   
78   C CA  . ARG A 21  ? 0.3654 0.3109 0.3348 -0.0633 -0.0149 0.0100  21  ARG A CA  
79   C C   . ARG A 21  ? 0.3715 0.3314 0.3402 -0.0652 -0.0149 0.0103  21  ARG A C   
80   O O   . ARG A 21  ? 0.3790 0.3405 0.3462 -0.0716 -0.0173 0.0087  21  ARG A O   
81   C CB  . ARG A 21  ? 0.3926 0.3255 0.3596 -0.0608 -0.0143 0.0023  21  ARG A CB  
82   C CG  . ARG A 21  ? 0.4361 0.3533 0.4052 -0.0604 -0.0151 0.0022  21  ARG A CG  
83   C CD  . ARG A 21  ? 0.4813 0.3912 0.4520 -0.0525 -0.0131 -0.0010 21  ARG A CD  
84   N NE  . ARG A 21  ? 0.4960 0.3993 0.4643 -0.0514 -0.0114 -0.0097 21  ARG A NE  
85   C CZ  . ARG A 21  ? 0.5456 0.4340 0.5144 -0.0526 -0.0114 -0.0146 21  ARG A CZ  
86   N NH1 . ARG A 21  ? 0.5918 0.4699 0.5643 -0.0546 -0.0134 -0.0106 21  ARG A NH1 
87   N NH2 . ARG A 21  ? 0.5701 0.4536 0.5357 -0.0518 -0.0091 -0.0234 21  ARG A NH2 
88   N N   . GLY A 22  ? 0.3076 0.2776 0.2778 -0.0598 -0.0125 0.0126  22  GLY A N   
89   C CA  . GLY A 22  ? 0.3257 0.3092 0.2962 -0.0597 -0.0123 0.0135  22  GLY A CA  
90   C C   . GLY A 22  ? 0.3554 0.3363 0.3208 -0.0606 -0.0130 0.0076  22  GLY A C   
91   O O   . GLY A 22  ? 0.3344 0.3219 0.2978 -0.0659 -0.0155 0.0071  22  GLY A O   
92   N N   . SER A 23  ? 0.3394 0.3110 0.3024 -0.0557 -0.0109 0.0027  23  SER A N   
93   C CA  . SER A 23  ? 0.3644 0.3319 0.3219 -0.0566 -0.0108 -0.0039 23  SER A CA  
94   C C   . SER A 23  ? 0.3402 0.3059 0.2978 -0.0492 -0.0071 -0.0060 23  SER A C   
95   O O   . SER A 23  ? 0.3187 0.2827 0.2805 -0.0442 -0.0055 -0.0036 23  SER A O   
96   C CB  . SER A 23  ? 0.4383 0.3911 0.3932 -0.0603 -0.0119 -0.0097 23  SER A CB  
97   O OG  . SER A 23  ? 0.5028 0.4456 0.4611 -0.0544 -0.0099 -0.0102 23  SER A OG  
98   N N   . PRO A 24  ? 0.3204 0.2878 0.2733 -0.0489 -0.0059 -0.0101 24  PRO A N   
99   C CA  . PRO A 24  ? 0.3339 0.2983 0.2876 -0.0424 -0.0021 -0.0126 24  PRO A CA  
100  C C   . PRO A 24  ? 0.3491 0.3007 0.3051 -0.0398 -0.0011 -0.0167 24  PRO A C   
101  O O   . PRO A 24  ? 0.3527 0.2951 0.3077 -0.0431 -0.0027 -0.0196 24  PRO A O   
102  C CB  . PRO A 24  ? 0.3872 0.3552 0.3343 -0.0440 -0.0010 -0.0166 24  PRO A CB  
103  C CG  . PRO A 24  ? 0.4265 0.3933 0.3681 -0.0513 -0.0042 -0.0195 24  PRO A CG  
104  C CD  . PRO A 24  ? 0.3881 0.3588 0.3341 -0.0547 -0.0077 -0.0134 24  PRO A CD  
105  N N   . ALA A 25  ? 0.3155 0.2664 0.2756 -0.0339 0.0013  -0.0164 25  ALA A N   
106  C CA  . ALA A 25  ? 0.3173 0.2586 0.2814 -0.0300 0.0023  -0.0190 25  ALA A CA  
107  C C   . ALA A 25  ? 0.3179 0.2568 0.2800 -0.0280 0.0058  -0.0258 25  ALA A C   
108  O O   . ALA A 25  ? 0.3227 0.2681 0.2849 -0.0253 0.0085  -0.0258 25  ALA A O   
109  C CB  . ALA A 25  ? 0.3082 0.2527 0.2778 -0.0255 0.0026  -0.0146 25  ALA A CB  
110  N N   . ILE A 26  ? 0.3662 0.2958 0.3257 -0.0301 0.0060  -0.0316 26  ILE A N   
111  C CA  . ILE A 26  ? 0.3886 0.3152 0.3447 -0.0291 0.0099  -0.0393 26  ILE A CA  
112  C C   . ILE A 26  ? 0.3615 0.2811 0.3257 -0.0223 0.0128  -0.0420 26  ILE A C   
113  O O   . ILE A 26  ? 0.3472 0.2595 0.3179 -0.0202 0.0107  -0.0395 26  ILE A O   
114  C CB  . ILE A 26  ? 0.4515 0.3700 0.4007 -0.0352 0.0088  -0.0453 26  ILE A CB  
115  C CG1 . ILE A 26  ? 0.4651 0.3923 0.4078 -0.0423 0.0049  -0.0418 26  ILE A CG1 
116  C CG2 . ILE A 26  ? 0.4820 0.3964 0.4258 -0.0348 0.0134  -0.0550 26  ILE A CG2 
117  C CD1 . ILE A 26  ? 0.5292 0.4480 0.4667 -0.0495 0.0025  -0.0466 26  ILE A CD1 
118  N N   . ASN A 27  ? 0.3681 0.2909 0.3319 -0.0193 0.0174  -0.0465 27  ASN A N   
119  C CA  A ASN A 27  ? 0.3937 0.3122 0.3659 -0.0129 0.0210  -0.0496 27  ASN A CA  
120  C CA  B ASN A 27  ? 0.3789 0.2977 0.3511 -0.0129 0.0210  -0.0495 27  ASN A CA  
121  C C   . ASN A 27  ? 0.3883 0.3103 0.3708 -0.0081 0.0191  -0.0429 27  ASN A C   
122  O O   . ASN A 27  ? 0.3774 0.2937 0.3688 -0.0034 0.0192  -0.0431 27  ASN A O   
123  C CB  A ASN A 27  ? 0.4648 0.3692 0.4380 -0.0125 0.0219  -0.0558 27  ASN A CB  
124  C CB  B ASN A 27  ? 0.4251 0.3300 0.3984 -0.0122 0.0223  -0.0560 27  ASN A CB  
125  C CG  A ASN A 27  ? 0.5010 0.4025 0.4648 -0.0156 0.0260  -0.0653 27  ASN A CG  
126  C CG  B ASN A 27  ? 0.4235 0.3263 0.4037 -0.0056 0.0281  -0.0616 27  ASN A CG  
127  O OD1 A ASN A 27  ? 0.6091 0.5012 0.5670 -0.0203 0.0248  -0.0699 27  ASN A OD1 
128  O OD1 B ASN A 27  ? 0.4397 0.3520 0.4195 -0.0038 0.0322  -0.0631 27  ASN A OD1 
129  N ND2 A ASN A 27  ? 0.5541 0.4640 0.5159 -0.0135 0.0311  -0.0684 27  ASN A ND2 
130  N ND2 B ASN A 27  ? 0.4483 0.3391 0.4358 -0.0020 0.0287  -0.0642 27  ASN A ND2 
131  N N   . VAL A 28  ? 0.3141 0.2455 0.2956 -0.0093 0.0173  -0.0372 28  VAL A N   
132  C CA  . VAL A 28  ? 0.3144 0.2503 0.3033 -0.0063 0.0153  -0.0316 28  VAL A CA  
133  C C   . VAL A 28  ? 0.2995 0.2424 0.2929 -0.0030 0.0193  -0.0332 28  VAL A C   
134  O O   . VAL A 28  ? 0.3107 0.2598 0.2993 -0.0047 0.0222  -0.0342 28  VAL A O   
135  C CB  . VAL A 28  ? 0.3180 0.2596 0.3035 -0.0094 0.0123  -0.0257 28  VAL A CB  
136  C CG1 . VAL A 28  ? 0.3114 0.2572 0.3035 -0.0066 0.0107  -0.0214 28  VAL A CG1 
137  C CG2 . VAL A 28  ? 0.2887 0.2249 0.2701 -0.0134 0.0086  -0.0236 28  VAL A CG2 
138  N N   . ALA A 29  ? 0.2788 0.2218 0.2821 0.0016  0.0193  -0.0325 29  ALA A N   
139  C CA  . ALA A 29  ? 0.2979 0.2490 0.3079 0.0047  0.0230  -0.0336 29  ALA A CA  
140  C C   . ALA A 29  ? 0.2821 0.2410 0.2918 0.0027  0.0213  -0.0287 29  ALA A C   
141  O O   . ALA A 29  ? 0.2988 0.2572 0.3086 0.0017  0.0169  -0.0245 29  ALA A O   
142  C CB  . ALA A 29  ? 0.2833 0.2332 0.3055 0.0102  0.0230  -0.0338 29  ALA A CB  
143  N N   . VAL A 30  ? 0.2690 0.2349 0.2788 0.0022  0.0252  -0.0296 30  VAL A N   
144  C CA  . VAL A 30  ? 0.2602 0.2324 0.2708 0.0004  0.0248  -0.0259 30  VAL A CA  
145  C C   . VAL A 30  ? 0.2518 0.2314 0.2705 0.0020  0.0284  -0.0268 30  VAL A C   
146  O O   . VAL A 30  ? 0.2888 0.2706 0.3074 0.0029  0.0334  -0.0302 30  VAL A O   
147  C CB  . VAL A 30  ? 0.3000 0.2733 0.3011 -0.0032 0.0260  -0.0247 30  VAL A CB  
148  C CG1 . VAL A 30  ? 0.3059 0.2841 0.3088 -0.0046 0.0263  -0.0209 30  VAL A CG1 
149  C CG2 . VAL A 30  ? 0.3076 0.2752 0.3017 -0.0053 0.0223  -0.0236 30  VAL A CG2 
150  N N   . HIS A 31  ? 0.2679 0.2516 0.2937 0.0020  0.0260  -0.0241 31  HIS A N   
151  C CA  . HIS A 31  ? 0.2761 0.2678 0.3113 0.0027  0.0287  -0.0242 31  HIS A CA  
152  C C   . HIS A 31  ? 0.2625 0.2570 0.2968 -0.0010 0.0281  -0.0214 31  HIS A C   
153  O O   . HIS A 31  ? 0.2708 0.2626 0.3026 -0.0026 0.0241  -0.0195 31  HIS A O   
154  C CB  . HIS A 31  ? 0.2673 0.2621 0.3138 0.0059  0.0258  -0.0238 31  HIS A CB  
155  C CG  . HIS A 31  ? 0.3292 0.3213 0.3801 0.0107  0.0275  -0.0267 31  HIS A CG  
156  N ND1 . HIS A 31  ? 0.4042 0.3875 0.4511 0.0121  0.0247  -0.0269 31  HIS A ND1 
157  C CD2 . HIS A 31  ? 0.3273 0.3241 0.3872 0.0144  0.0320  -0.0294 31  HIS A CD2 
158  C CE1 . HIS A 31  ? 0.3363 0.3173 0.3894 0.0168  0.0274  -0.0301 31  HIS A CE1 
159  N NE2 . HIS A 31  ? 0.4011 0.3908 0.4623 0.0186  0.0321  -0.0318 31  HIS A NE2 
160  N N   . VAL A 32  ? 0.2550 0.2543 0.2908 -0.0026 0.0328  -0.0212 32  VAL A N   
161  C CA  . VAL A 32  ? 0.2268 0.2279 0.2632 -0.0061 0.0333  -0.0186 32  VAL A CA  
162  C C   . VAL A 32  ? 0.2583 0.2672 0.3062 -0.0071 0.0347  -0.0186 32  VAL A C   
163  O O   . VAL A 32  ? 0.2813 0.2964 0.3353 -0.0053 0.0384  -0.0200 32  VAL A O   
164  C CB  . VAL A 32  ? 0.2489 0.2493 0.2781 -0.0081 0.0375  -0.0168 32  VAL A CB  
165  C CG1 . VAL A 32  ? 0.2439 0.2435 0.2745 -0.0114 0.0376  -0.0135 32  VAL A CG1 
166  C CG2 . VAL A 32  ? 0.2834 0.2781 0.3021 -0.0075 0.0359  -0.0168 32  VAL A CG2 
167  N N   . PHE A 33  ? 0.2529 0.2618 0.3038 -0.0102 0.0317  -0.0173 33  PHE A N   
168  C CA  . PHE A 33  ? 0.2734 0.2899 0.3355 -0.0125 0.0317  -0.0172 33  PHE A CA  
169  C C   . PHE A 33  ? 0.2603 0.2741 0.3212 -0.0174 0.0330  -0.0156 33  PHE A C   
170  O O   . PHE A 33  ? 0.2735 0.2793 0.3261 -0.0183 0.0326  -0.0147 33  PHE A O   
171  C CB  . PHE A 33  ? 0.2690 0.2881 0.3365 -0.0121 0.0253  -0.0179 33  PHE A CB  
172  C CG  . PHE A 33  ? 0.3371 0.3569 0.4063 -0.0069 0.0233  -0.0185 33  PHE A CG  
173  C CD1 . PHE A 33  ? 0.3189 0.3304 0.3787 -0.0049 0.0206  -0.0185 33  PHE A CD1 
174  C CD2 . PHE A 33  ? 0.3220 0.3506 0.4032 -0.0039 0.0245  -0.0188 33  PHE A CD2 
175  C CE1 . PHE A 33  ? 0.3991 0.4096 0.4610 -0.0003 0.0189  -0.0187 33  PHE A CE1 
176  C CE2 . PHE A 33  ? 0.3719 0.3996 0.4558 0.0017  0.0231  -0.0192 33  PHE A CE2 
177  C CZ  . PHE A 33  ? 0.3698 0.3875 0.4437 0.0033  0.0202  -0.0192 33  PHE A CZ  
178  N N   . ARG A 34  ? 0.2808 0.3013 0.3511 -0.0206 0.0351  -0.0150 34  ARG A N   
179  C CA  . ARG A 34  ? 0.2652 0.2822 0.3362 -0.0259 0.0366  -0.0135 34  ARG A CA  
180  C C   . ARG A 34  ? 0.3090 0.3321 0.3904 -0.0301 0.0335  -0.0149 34  ARG A C   
181  O O   . ARG A 34  ? 0.2948 0.3287 0.3864 -0.0297 0.0334  -0.0151 34  ARG A O   
182  C CB  . ARG A 34  ? 0.2826 0.3019 0.3544 -0.0271 0.0432  -0.0103 34  ARG A CB  
183  C CG  . ARG A 34  ? 0.2975 0.3122 0.3715 -0.0327 0.0451  -0.0078 34  ARG A CG  
184  C CD  . ARG A 34  ? 0.3435 0.3607 0.4180 -0.0343 0.0516  -0.0030 34  ARG A CD  
185  N NE  . ARG A 34  ? 0.3498 0.3604 0.4269 -0.0395 0.0532  0.0001  34  ARG A NE  
186  C CZ  . ARG A 34  ? 0.3627 0.3765 0.4501 -0.0451 0.0536  -0.0001 34  ARG A CZ  
187  N NH1 . ARG A 34  ? 0.3548 0.3802 0.4519 -0.0462 0.0523  -0.0026 34  ARG A NH1 
188  N NH2 . ARG A 34  ? 0.3697 0.3751 0.4588 -0.0497 0.0552  0.0026  34  ARG A NH2 
189  N N   . LYS A 35  ? 0.2810 0.2975 0.3606 -0.0347 0.0314  -0.0160 35  LYS A N   
190  C CA  . LYS A 35  ? 0.3450 0.3669 0.4328 -0.0398 0.0275  -0.0181 35  LYS A CA  
191  C C   . LYS A 35  ? 0.3201 0.3483 0.4187 -0.0447 0.0312  -0.0164 35  LYS A C   
192  O O   . LYS A 35  ? 0.3380 0.3602 0.4352 -0.0471 0.0361  -0.0140 35  LYS A O   
193  C CB  . LYS A 35  ? 0.3636 0.3754 0.4442 -0.0435 0.0241  -0.0213 35  LYS A CB  
194  C CG  . LYS A 35  ? 0.4248 0.4428 0.5107 -0.0487 0.0180  -0.0246 35  LYS A CG  
195  C CD  . LYS A 35  ? 0.4386 0.4463 0.5176 -0.0540 0.0161  -0.0291 35  LYS A CD  
196  N N   . ALA A 36  ? 0.3456 0.3870 0.4561 -0.0463 0.0290  -0.0166 36  ALA A N   
197  C CA  . ALA A 36  ? 0.3990 0.4493 0.5219 -0.0514 0.0326  -0.0146 36  ALA A CA  
198  C C   . ALA A 36  ? 0.4405 0.4873 0.5668 -0.0604 0.0300  -0.0165 36  ALA A C   
199  O O   . ALA A 36  ? 0.4444 0.4843 0.5643 -0.0623 0.0247  -0.0203 36  ALA A O   
200  C CB  . ALA A 36  ? 0.4101 0.4778 0.5463 -0.0490 0.0314  -0.0139 36  ALA A CB  
201  N N   . ALA A 37  ? 0.4822 0.5337 0.6184 -0.0661 0.0341  -0.0141 37  ALA A N   
202  C CA  . ALA A 37  ? 0.5598 0.6105 0.7030 -0.0760 0.0320  -0.0159 37  ALA A CA  
203  C C   . ALA A 37  ? 0.5572 0.6169 0.7054 -0.0796 0.0233  -0.0201 37  ALA A C   
204  O O   . ALA A 37  ? 0.5524 0.6051 0.6975 -0.0862 0.0195  -0.0242 37  ALA A O   
205  C CB  . ALA A 37  ? 0.5905 0.6509 0.7471 -0.0809 0.0375  -0.0115 37  ALA A CB  
206  N N   . ASP A 38  ? 0.5890 0.6641 0.7445 -0.0749 0.0203  -0.0189 38  ASP A N   
207  C CA  . ASP A 38  ? 0.6366 0.7219 0.7968 -0.0775 0.0114  -0.0213 38  ASP A CA  
208  C C   . ASP A 38  ? 0.6463 0.7240 0.7926 -0.0726 0.0059  -0.0239 38  ASP A C   
209  O O   . ASP A 38  ? 0.6340 0.7220 0.7834 -0.0719 -0.0013 -0.0241 38  ASP A O   
210  C CB  . ASP A 38  ? 0.5937 0.7005 0.7711 -0.0749 0.0105  -0.0177 38  ASP A CB  
211  N N   . ASP A 39  ? 0.7111 0.7719 0.8427 -0.0692 0.0092  -0.0252 39  ASP A N   
212  C CA  . ASP A 39  ? 0.6282 0.6810 0.7458 -0.0653 0.0049  -0.0276 39  ASP A CA  
213  C C   . ASP A 39  ? 0.6144 0.6733 0.7312 -0.0563 0.0028  -0.0248 39  ASP A C   
214  O O   . ASP A 39  ? 0.6313 0.6853 0.7378 -0.0540 -0.0014 -0.0261 39  ASP A O   
215  C CB  . ASP A 39  ? 0.6537 0.7073 0.7680 -0.0726 -0.0025 -0.0323 39  ASP A CB  
216  N N   . THR A 40  ? 0.5282 0.5970 0.6556 -0.0515 0.0060  -0.0212 40  THR A N   
217  C CA  . THR A 40  ? 0.5059 0.5782 0.6336 -0.0425 0.0058  -0.0189 40  THR A CA  
218  C C   . THR A 40  ? 0.4558 0.5149 0.5716 -0.0372 0.0118  -0.0188 40  THR A C   
219  O O   . THR A 40  ? 0.4484 0.5011 0.5611 -0.0396 0.0173  -0.0188 40  THR A O   
220  C CB  . THR A 40  ? 0.4644 0.5526 0.6096 -0.0396 0.0084  -0.0160 40  THR A CB  
221  N N   . TRP A 41  ? 0.4893 0.5458 0.5999 -0.0304 0.0105  -0.0180 41  TRP A N   
222  C CA  . TRP A 41  ? 0.4375 0.4847 0.5390 -0.0252 0.0159  -0.0178 41  TRP A CA  
223  C C   . TRP A 41  ? 0.4322 0.4854 0.5407 -0.0202 0.0215  -0.0167 41  TRP A C   
224  O O   . TRP A 41  ? 0.5490 0.6066 0.6625 -0.0148 0.0199  -0.0163 41  TRP A O   
225  C CB  . TRP A 41  ? 0.4288 0.4690 0.5206 -0.0211 0.0119  -0.0179 41  TRP A CB  
226  C CG  . TRP A 41  ? 0.4676 0.4991 0.5481 -0.0247 0.0087  -0.0193 41  TRP A CG  
227  C CD1 . TRP A 41  ? 0.5025 0.5351 0.5799 -0.0263 0.0018  -0.0197 41  TRP A CD1 
228  C CD2 . TRP A 41  ? 0.4187 0.4391 0.4892 -0.0268 0.0123  -0.0205 41  TRP A CD2 
229  N NE1 . TRP A 41  ? 0.5184 0.5413 0.5840 -0.0293 0.0017  -0.0219 41  TRP A NE1 
230  C CE2 . TRP A 41  ? 0.4856 0.5008 0.5476 -0.0293 0.0079  -0.0224 41  TRP A CE2 
231  C CE3 . TRP A 41  ? 0.4038 0.4189 0.4715 -0.0265 0.0185  -0.0197 41  TRP A CE3 
232  C CZ2 . TRP A 41  ? 0.4513 0.4561 0.5042 -0.0311 0.0104  -0.0240 41  TRP A CZ2 
233  C CZ3 . TRP A 41  ? 0.4129 0.4179 0.4719 -0.0282 0.0201  -0.0203 41  TRP A CZ3 
234  C CH2 . TRP A 41  ? 0.4321 0.4318 0.4845 -0.0301 0.0165  -0.0226 41  TRP A CH2 
235  N N   . GLU A 42  ? 0.3580 0.4109 0.4665 -0.0217 0.0283  -0.0163 42  GLU A N   
236  C CA  . GLU A 42  ? 0.3702 0.4294 0.4838 -0.0175 0.0349  -0.0160 42  GLU A CA  
237  C C   . GLU A 42  ? 0.3262 0.3763 0.4276 -0.0125 0.0379  -0.0172 42  GLU A C   
238  O O   . GLU A 42  ? 0.3105 0.3505 0.3995 -0.0141 0.0381  -0.0169 42  GLU A O   
239  C CB  . GLU A 42  ? 0.3806 0.4442 0.4981 -0.0221 0.0412  -0.0144 42  GLU A CB  
240  C CG  . GLU A 42  ? 0.4727 0.5426 0.6003 -0.0293 0.0389  -0.0133 42  GLU A CG  
241  N N   . PRO A 43  ? 0.3257 0.3792 0.4307 -0.0065 0.0403  -0.0188 43  PRO A N   
242  C CA  . PRO A 43  ? 0.3342 0.3790 0.4270 -0.0033 0.0434  -0.0207 43  PRO A CA  
243  C C   . PRO A 43  ? 0.3659 0.4095 0.4507 -0.0064 0.0496  -0.0199 43  PRO A C   
244  O O   . PRO A 43  ? 0.3776 0.4299 0.4690 -0.0082 0.0551  -0.0189 43  PRO A O   
245  C CB  . PRO A 43  ? 0.4065 0.4565 0.5074 0.0030  0.0464  -0.0233 43  PRO A CB  
246  C CG  . PRO A 43  ? 0.4294 0.4867 0.5442 0.0044  0.0407  -0.0216 43  PRO A CG  
247  C CD  . PRO A 43  ? 0.3782 0.4425 0.4981 -0.0023 0.0399  -0.0192 43  PRO A CD  
248  N N   . PHE A 44  ? 0.2977 0.3314 0.3688 -0.0072 0.0487  -0.0195 44  PHE A N   
249  C CA  . PHE A 44  ? 0.3027 0.3345 0.3649 -0.0103 0.0531  -0.0172 44  PHE A CA  
250  C C   . PHE A 44  ? 0.3223 0.3510 0.3735 -0.0077 0.0562  -0.0196 44  PHE A C   
251  O O   . PHE A 44  ? 0.3395 0.3734 0.3881 -0.0084 0.0624  -0.0196 44  PHE A O   
252  C CB  . PHE A 44  ? 0.3098 0.3339 0.3665 -0.0138 0.0494  -0.0141 44  PHE A CB  
253  C CG  . PHE A 44  ? 0.3076 0.3295 0.3568 -0.0166 0.0531  -0.0102 44  PHE A CG  
254  C CD1 . PHE A 44  ? 0.3529 0.3797 0.4076 -0.0204 0.0572  -0.0069 44  PHE A CD1 
255  C CD2 . PHE A 44  ? 0.3307 0.3464 0.3681 -0.0157 0.0522  -0.0092 44  PHE A CD2 
256  C CE1 . PHE A 44  ? 0.3811 0.4060 0.4290 -0.0227 0.0605  -0.0021 44  PHE A CE1 
257  C CE2 . PHE A 44  ? 0.3808 0.3959 0.4118 -0.0179 0.0551  -0.0046 44  PHE A CE2 
258  C CZ  . PHE A 44  ? 0.3856 0.4049 0.4219 -0.0213 0.0591  -0.0007 44  PHE A CZ  
259  N N   . ALA A 45  ? 0.2893 0.3107 0.3343 -0.0050 0.0524  -0.0220 45  ALA A N   
260  C CA  . ALA A 45  ? 0.2921 0.3098 0.3263 -0.0036 0.0546  -0.0250 45  ALA A CA  
261  C C   . ALA A 45  ? 0.2713 0.2811 0.3032 -0.0008 0.0496  -0.0275 45  ALA A C   
262  O O   . ALA A 45  ? 0.2689 0.2759 0.3048 -0.0006 0.0443  -0.0257 45  ALA A O   
263  C CB  . ALA A 45  ? 0.3254 0.3407 0.3476 -0.0071 0.0552  -0.0216 45  ALA A CB  
264  N N   . SER A 46  ? 0.2918 0.2979 0.3172 0.0010  0.0516  -0.0319 46  SER A N   
265  C CA  . SER A 46  ? 0.2952 0.2925 0.3182 0.0030  0.0469  -0.0339 46  SER A CA  
266  C C   . SER A 46  ? 0.3010 0.2935 0.3121 0.0021  0.0490  -0.0380 46  SER A C   
267  O O   . SER A 46  ? 0.2916 0.2884 0.2971 0.0007  0.0544  -0.0400 46  SER A O   
268  C CB  . SER A 46  ? 0.3204 0.3182 0.3561 0.0079  0.0462  -0.0359 46  SER A CB  
269  O OG  . SER A 46  ? 0.3024 0.3025 0.3415 0.0112  0.0523  -0.0410 46  SER A OG  
270  N N   . GLY A 47  ? 0.2742 0.2582 0.2807 0.0021  0.0447  -0.0390 47  GLY A N   
271  C CA  . GLY A 47  ? 0.3083 0.2872 0.3030 -0.0002 0.0454  -0.0428 47  GLY A CA  
272  C C   . GLY A 47  ? 0.3167 0.2861 0.3097 -0.0003 0.0399  -0.0429 47  GLY A C   
273  O O   . GLY A 47  ? 0.2974 0.2646 0.2983 0.0018  0.0360  -0.0399 47  GLY A O   
274  N N   . LYS A 48  ? 0.3172 0.2812 0.3002 -0.0031 0.0396  -0.0465 48  LYS A N   
275  C CA  . LYS A 48  ? 0.3228 0.2786 0.3034 -0.0047 0.0343  -0.0456 48  LYS A CA  
276  C C   . LYS A 48  ? 0.2874 0.2446 0.2562 -0.0106 0.0318  -0.0440 48  LYS A C   
277  O O   . LYS A 48  ? 0.3381 0.3000 0.2986 -0.0134 0.0344  -0.0458 48  LYS A O   
278  C CB  . LYS A 48  ? 0.3683 0.3141 0.3512 -0.0025 0.0350  -0.0514 48  LYS A CB  
279  C CG  . LYS A 48  ? 0.4207 0.3635 0.3953 -0.0042 0.0395  -0.0594 48  LYS A CG  
280  N N   . THR A 49  ? 0.2922 0.2465 0.2608 -0.0124 0.0267  -0.0399 49  THR A N   
281  C CA  . THR A 49  ? 0.2921 0.2494 0.2520 -0.0176 0.0237  -0.0372 49  THR A CA  
282  C C   . THR A 49  ? 0.3256 0.2779 0.2765 -0.0216 0.0240  -0.0437 49  THR A C   
283  O O   . THR A 49  ? 0.3287 0.2709 0.2810 -0.0207 0.0247  -0.0496 49  THR A O   
284  C CB  . THR A 49  ? 0.2911 0.2468 0.2535 -0.0188 0.0185  -0.0315 49  THR A CB  
285  O OG1 . THR A 49  ? 0.3076 0.2538 0.2727 -0.0184 0.0164  -0.0336 49  THR A OG1 
286  C CG2 . THR A 49  ? 0.2960 0.2564 0.2652 -0.0159 0.0181  -0.0259 49  THR A CG2 
287  N N   . SER A 50  ? 0.3334 0.2926 0.2751 -0.0263 0.0233  -0.0426 50  SER A N   
288  C CA  . SER A 50  ? 0.3719 0.3285 0.3029 -0.0317 0.0231  -0.0489 50  SER A CA  
289  C C   . SER A 50  ? 0.3925 0.3439 0.3221 -0.0363 0.0174  -0.0479 50  SER A C   
290  O O   . SER A 50  ? 0.3722 0.3220 0.3092 -0.0349 0.0143  -0.0423 50  SER A O   
291  C CB  . SER A 50  ? 0.3942 0.3624 0.3158 -0.0354 0.0235  -0.0464 50  SER A CB  
292  O OG  . SER A 50  ? 0.4113 0.3861 0.3342 -0.0376 0.0185  -0.0379 50  SER A OG  
293  N N   . GLU A 51  ? 0.4228 0.3722 0.3426 -0.0425 0.0164  -0.0536 51  GLU A N   
294  C CA  . GLU A 51  ? 0.4649 0.4113 0.3826 -0.0485 0.0109  -0.0527 51  GLU A CA  
295  C C   . GLU A 51  ? 0.4537 0.4119 0.3739 -0.0503 0.0064  -0.0424 51  GLU A C   
296  O O   . GLU A 51  ? 0.4689 0.4257 0.3925 -0.0533 0.0022  -0.0389 51  GLU A O   
297  C CB  . GLU A 51  ? 0.4693 0.4122 0.3749 -0.0558 0.0106  -0.0616 51  GLU A CB  
298  N N   . SER A 52  ? 0.4187 0.3879 0.3392 -0.0478 0.0076  -0.0368 52  SER A N   
299  C CA  . SER A 52  ? 0.4174 0.3969 0.3420 -0.0481 0.0042  -0.0271 52  SER A CA  
300  C C   . SER A 52  ? 0.3800 0.3585 0.3153 -0.0417 0.0055  -0.0217 52  SER A C   
301  O O   . SER A 52  ? 0.3607 0.3468 0.3003 -0.0408 0.0039  -0.0143 52  SER A O   
302  C CB  . SER A 52  ? 0.4624 0.4543 0.3812 -0.0495 0.0045  -0.0233 52  SER A CB  
303  O OG  . SER A 52  ? 0.4806 0.4724 0.4015 -0.0441 0.0095  -0.0233 52  SER A OG  
304  N N   . GLY A 53  ? 0.3248 0.2943 0.2645 -0.0372 0.0084  -0.0255 53  GLY A N   
305  C CA  . GLY A 53  ? 0.3179 0.2864 0.2666 -0.0318 0.0093  -0.0215 53  GLY A CA  
306  C C   . GLY A 53  ? 0.3013 0.2756 0.2523 -0.0281 0.0125  -0.0189 53  GLY A C   
307  O O   . GLY A 53  ? 0.3291 0.3040 0.2867 -0.0246 0.0129  -0.0152 53  GLY A O   
308  N N   . GLU A 54  ? 0.3202 0.2991 0.2653 -0.0294 0.0147  -0.0205 54  GLU A N   
309  C CA  . GLU A 54  ? 0.3246 0.3097 0.2714 -0.0268 0.0180  -0.0172 54  GLU A CA  
310  C C   . GLU A 54  ? 0.3295 0.3119 0.2770 -0.0243 0.0227  -0.0225 54  GLU A C   
311  O O   . GLU A 54  ? 0.3468 0.3246 0.2901 -0.0253 0.0243  -0.0297 54  GLU A O   
312  C CB  . GLU A 54  ? 0.3945 0.3890 0.3348 -0.0301 0.0171  -0.0128 54  GLU A CB  
313  C CG  . GLU A 54  ? 0.3859 0.3858 0.3278 -0.0319 0.0128  -0.0060 54  GLU A CG  
314  C CD  . GLU A 54  ? 0.4189 0.4296 0.3568 -0.0337 0.0120  0.0004  54  GLU A CD  
315  O OE1 . GLU A 54  ? 0.4597 0.4739 0.3891 -0.0367 0.0129  -0.0019 54  GLU A OE1 
316  O OE2 . GLU A 54  ? 0.5295 0.5455 0.4731 -0.0320 0.0107  0.0081  54  GLU A OE2 
317  N N   . LEU A 55  ? 0.3224 0.3075 0.2761 -0.0210 0.0254  -0.0194 55  LEU A N   
318  C CA  . LEU A 55  ? 0.3167 0.3022 0.2725 -0.0189 0.0303  -0.0231 55  LEU A CA  
319  C C   . LEU A 55  ? 0.3134 0.3066 0.2686 -0.0194 0.0329  -0.0177 55  LEU A C   
320  O O   . LEU A 55  ? 0.3312 0.3255 0.2924 -0.0180 0.0322  -0.0120 55  LEU A O   
321  C CB  . LEU A 55  ? 0.3023 0.2833 0.2684 -0.0148 0.0306  -0.0243 55  LEU A CB  
322  C CG  . LEU A 55  ? 0.3292 0.3122 0.3006 -0.0122 0.0355  -0.0275 55  LEU A CG  
323  C CD1 . LEU A 55  ? 0.3418 0.3253 0.3076 -0.0126 0.0398  -0.0339 55  LEU A CD1 
324  C CD2 . LEU A 55  ? 0.3200 0.2987 0.3015 -0.0087 0.0337  -0.0283 55  LEU A CD2 
325  N N   . HIS A 56  ? 0.3630 0.3608 0.3098 -0.0218 0.0356  -0.0194 56  HIS A N   
326  C CA  . HIS A 56  ? 0.4113 0.4171 0.3556 -0.0230 0.0385  -0.0138 56  HIS A CA  
327  C C   . HIS A 56  ? 0.4124 0.4199 0.3588 -0.0216 0.0445  -0.0178 56  HIS A C   
328  O O   . HIS A 56  ? 0.4436 0.4469 0.3919 -0.0198 0.0465  -0.0254 56  HIS A O   
329  C CB  . HIS A 56  ? 0.4530 0.4648 0.3846 -0.0276 0.0371  -0.0126 56  HIS A CB  
330  C CG  . HIS A 56  ? 0.5215 0.5348 0.4518 -0.0294 0.0312  -0.0072 56  HIS A CG  
331  N ND1 . HIS A 56  ? 0.6568 0.6746 0.5910 -0.0287 0.0296  0.0023  56  HIS A ND1 
332  C CD2 . HIS A 56  ? 0.6138 0.6249 0.5400 -0.0320 0.0266  -0.0100 56  HIS A CD2 
333  C CE1 . HIS A 56  ? 0.6503 0.6699 0.5836 -0.0302 0.0244  0.0055  56  HIS A CE1 
334  N NE2 . HIS A 56  ? 0.6574 0.6733 0.5857 -0.0327 0.0224  -0.0020 56  HIS A NE2 
335  N N   . GLY A 57  ? 0.4218 0.4356 0.3688 -0.0223 0.0478  -0.0125 57  GLY A N   
336  C CA  . GLY A 57  ? 0.4162 0.4341 0.3639 -0.0219 0.0545  -0.0161 57  GLY A CA  
337  C C   . GLY A 57  ? 0.3853 0.4015 0.3468 -0.0184 0.0568  -0.0175 57  GLY A C   
338  O O   . GLY A 57  ? 0.4210 0.4412 0.3850 -0.0175 0.0624  -0.0210 57  GLY A O   
339  N N   . LEU A 58  ? 0.3759 0.3874 0.3463 -0.0166 0.0529  -0.0147 58  LEU A N   
340  C CA  . LEU A 58  ? 0.3893 0.3998 0.3723 -0.0139 0.0540  -0.0165 58  LEU A CA  
341  C C   . LEU A 58  ? 0.4227 0.4398 0.4117 -0.0152 0.0587  -0.0125 58  LEU A C   
342  O O   . LEU A 58  ? 0.3909 0.4113 0.3887 -0.0136 0.0619  -0.0155 58  LEU A O   
343  C CB  . LEU A 58  ? 0.3811 0.3855 0.3706 -0.0126 0.0486  -0.0146 58  LEU A CB  
344  C CG  . LEU A 58  ? 0.3819 0.3798 0.3708 -0.0107 0.0441  -0.0187 58  LEU A CG  
345  C CD1 . LEU A 58  ? 0.3834 0.3771 0.3748 -0.0106 0.0392  -0.0151 58  LEU A CD1 
346  C CD2 . LEU A 58  ? 0.3772 0.3746 0.3737 -0.0075 0.0456  -0.0243 58  LEU A CD2 
347  N N   . THR A 59  ? 0.3819 0.4013 0.3667 -0.0180 0.0593  -0.0055 59  THR A N   
348  C CA  . THR A 59  ? 0.3895 0.4136 0.3806 -0.0199 0.0632  -0.0002 59  THR A CA  
349  C C   . THR A 59  ? 0.4086 0.4365 0.3915 -0.0230 0.0649  0.0074  59  THR A C   
350  O O   . THR A 59  ? 0.4455 0.4736 0.4177 -0.0237 0.0625  0.0086  59  THR A O   
351  C CB  . THR A 59  ? 0.3800 0.3990 0.3823 -0.0196 0.0605  0.0023  59  THR A CB  
352  O OG1 . THR A 59  ? 0.3675 0.3911 0.3774 -0.0221 0.0648  0.0059  59  THR A OG1 
353  C CG2 . THR A 59  ? 0.3528 0.3657 0.3525 -0.0199 0.0564  0.0076  59  THR A CG2 
354  N N   . THR A 60  ? 0.4008 0.4326 0.3886 -0.0253 0.0689  0.0130  60  THR A N   
355  C CA  . THR A 60  ? 0.3901 0.4261 0.3709 -0.0284 0.0708  0.0217  60  THR A CA  
356  C C   . THR A 60  ? 0.3987 0.4296 0.3887 -0.0293 0.0699  0.0295  60  THR A C   
357  O O   . THR A 60  ? 0.3487 0.3746 0.3497 -0.0286 0.0691  0.0268  60  THR A O   
358  C CB  . THR A 60  ? 0.4311 0.4772 0.4083 -0.0309 0.0778  0.0220  60  THR A CB  
359  O OG1 . THR A 60  ? 0.4253 0.4728 0.4159 -0.0315 0.0813  0.0217  60  THR A OG1 
360  C CG2 . THR A 60  ? 0.4685 0.5190 0.4368 -0.0296 0.0801  0.0118  60  THR A CG2 
361  N N   . GLU A 61  ? 0.4186 0.4505 0.4043 -0.0312 0.0700  0.0393  61  GLU A N   
362  C CA  . GLU A 61  ? 0.4438 0.4689 0.4389 -0.0318 0.0697  0.0470  61  GLU A CA  
363  C C   . GLU A 61  ? 0.4611 0.4866 0.4668 -0.0347 0.0743  0.0473  61  GLU A C   
364  O O   . GLU A 61  ? 0.4931 0.5104 0.5090 -0.0349 0.0733  0.0477  61  GLU A O   
365  C CB  . GLU A 61  ? 0.4845 0.5112 0.4741 -0.0330 0.0695  0.0591  61  GLU A CB  
366  N N   . GLU A 62  ? 0.4385 0.4739 0.4419 -0.0371 0.0796  0.0467  62  GLU A N   
367  C CA  . GLU A 62  ? 0.4404 0.4789 0.4543 -0.0404 0.0844  0.0474  62  GLU A CA  
368  C C   . GLU A 62  ? 0.3909 0.4271 0.4157 -0.0389 0.0827  0.0379  62  GLU A C   
369  O O   . GLU A 62  ? 0.3795 0.4126 0.4157 -0.0413 0.0830  0.0386  62  GLU A O   
370  C CB  . GLU A 62  ? 0.4816 0.5332 0.4898 -0.0430 0.0909  0.0485  62  GLU A CB  
371  C CG  . GLU A 62  ? 0.4948 0.5540 0.5000 -0.0406 0.0932  0.0378  62  GLU A CG  
372  C CD  . GLU A 62  ? 0.5513 0.6148 0.5398 -0.0394 0.0933  0.0352  62  GLU A CD  
373  O OE1 . GLU A 62  ? 0.5778 0.6395 0.5564 -0.0402 0.0902  0.0419  62  GLU A OE1 
374  O OE2 . GLU A 62  ? 0.5055 0.5745 0.4916 -0.0375 0.0963  0.0263  62  GLU A OE2 
375  N N   . GLU A 63  ? 0.3503 0.3882 0.3714 -0.0352 0.0806  0.0293  63  GLU A N   
376  C CA  . GLU A 63  ? 0.3440 0.3818 0.3750 -0.0334 0.0790  0.0213  63  GLU A CA  
377  C C   . GLU A 63  ? 0.3172 0.3441 0.3527 -0.0322 0.0727  0.0197  63  GLU A C   
378  O O   . GLU A 63  ? 0.3236 0.3499 0.3690 -0.0327 0.0710  0.0158  63  GLU A O   
384  N N   . PHE A 64  ? 0.3063 0.3258 0.3343 -0.0307 0.0694  0.0227  64  PHE A N   
385  C CA  . PHE A 64  ? 0.3216 0.3314 0.3514 -0.0288 0.0641  0.0205  64  PHE A CA  
386  C C   . PHE A 64  ? 0.2959 0.2980 0.3330 -0.0317 0.0645  0.0253  64  PHE A C   
387  O O   . PHE A 64  ? 0.3705 0.3658 0.4051 -0.0308 0.0635  0.0302  64  PHE A O   
388  C CB  . PHE A 64  ? 0.3232 0.3299 0.3429 -0.0259 0.0609  0.0215  64  PHE A CB  
389  C CG  . PHE A 64  ? 0.3230 0.3217 0.3437 -0.0234 0.0560  0.0182  64  PHE A CG  
390  C CD1 . PHE A 64  ? 0.3186 0.3160 0.3437 -0.0225 0.0534  0.0113  64  PHE A CD1 
391  C CD2 . PHE A 64  ? 0.3747 0.3684 0.3911 -0.0218 0.0540  0.0226  64  PHE A CD2 
392  C CE1 . PHE A 64  ? 0.3615 0.3524 0.3857 -0.0206 0.0491  0.0086  64  PHE A CE1 
393  C CE2 . PHE A 64  ? 0.3774 0.3649 0.3942 -0.0195 0.0502  0.0196  64  PHE A CE2 
394  C CZ  . PHE A 64  ? 0.3666 0.3527 0.3865 -0.0191 0.0480  0.0125  64  PHE A CZ  
395  N N   . VAL A 65  ? 0.2932 0.2968 0.3402 -0.0350 0.0659  0.0234  65  VAL A N   
396  C CA  . VAL A 65  ? 0.2841 0.2799 0.3390 -0.0389 0.0668  0.0268  65  VAL A CA  
397  C C   . VAL A 65  ? 0.2920 0.2778 0.3484 -0.0377 0.0623  0.0217  65  VAL A C   
398  O O   . VAL A 65  ? 0.2862 0.2729 0.3389 -0.0344 0.0585  0.0159  65  VAL A O   
399  C CB  . VAL A 65  ? 0.2903 0.2935 0.3556 -0.0440 0.0700  0.0263  65  VAL A CB  
400  C CG1 . VAL A 65  ? 0.3147 0.3281 0.3772 -0.0453 0.0757  0.0322  65  VAL A CG1 
401  C CG2 . VAL A 65  ? 0.3204 0.3307 0.3907 -0.0431 0.0674  0.0181  65  VAL A CG2 
402  N N   . GLU A 66  ? 0.3077 0.2837 0.3696 -0.0406 0.0630  0.0236  66  GLU A N   
403  C CA  . GLU A 66  ? 0.3441 0.3111 0.4081 -0.0409 0.0597  0.0174  66  GLU A CA  
404  C C   . GLU A 66  ? 0.3385 0.3125 0.4056 -0.0423 0.0563  0.0096  66  GLU A C   
405  O O   . GLU A 66  ? 0.3139 0.2971 0.3876 -0.0455 0.0574  0.0092  66  GLU A O   
406  C CB  . GLU A 66  ? 0.3765 0.3335 0.4483 -0.0459 0.0617  0.0186  66  GLU A CB  
407  C CG  . GLU A 66  ? 0.4537 0.4009 0.5257 -0.0451 0.0651  0.0267  66  GLU A CG  
408  C CD  . GLU A 66  ? 0.4874 0.4212 0.5676 -0.0500 0.0667  0.0254  66  GLU A CD  
409  O OE1 . GLU A 66  ? 0.4707 0.4031 0.5579 -0.0553 0.0700  0.0303  66  GLU A OE1 
410  O OE2 . GLU A 66  ? 0.5111 0.4356 0.5903 -0.0489 0.0647  0.0189  66  GLU A OE2 
411  N N   . GLY A 67  ? 0.3406 0.3111 0.4036 -0.0398 0.0521  0.0040  67  GLY A N   
412  C CA  . GLY A 67  ? 0.3280 0.3044 0.3936 -0.0409 0.0479  -0.0025 67  GLY A CA  
413  C C   . GLY A 67  ? 0.3040 0.2765 0.3625 -0.0375 0.0438  -0.0069 67  GLY A C   
414  O O   . GLY A 67  ? 0.2876 0.2534 0.3397 -0.0340 0.0444  -0.0052 67  GLY A O   
415  N N   . ILE A 68  ? 0.2900 0.2676 0.3501 -0.0385 0.0394  -0.0119 68  ILE A N   
416  C CA  . ILE A 68  ? 0.2858 0.2620 0.3387 -0.0352 0.0352  -0.0154 68  ILE A CA  
417  C C   . ILE A 68  ? 0.2790 0.2640 0.3309 -0.0312 0.0338  -0.0144 68  ILE A C   
418  O O   . ILE A 68  ? 0.2730 0.2671 0.3321 -0.0321 0.0335  -0.0146 68  ILE A O   
419  C CB  . ILE A 68  ? 0.3239 0.3005 0.3784 -0.0392 0.0308  -0.0209 68  ILE A CB  
420  C CG1 . ILE A 68  ? 0.3652 0.3316 0.4208 -0.0438 0.0329  -0.0230 68  ILE A CG1 
421  C CG2 . ILE A 68  ? 0.3223 0.2983 0.3686 -0.0362 0.0265  -0.0237 68  ILE A CG2 
422  C CD1 . ILE A 68  ? 0.4166 0.3829 0.4723 -0.0491 0.0286  -0.0295 68  ILE A CD1 
423  N N   . TYR A 69  ? 0.2545 0.2368 0.2986 -0.0268 0.0336  -0.0132 69  TYR A N   
424  C CA  . TYR A 69  ? 0.2509 0.2384 0.2924 -0.0230 0.0327  -0.0128 69  TYR A CA  
425  C C   . TYR A 69  ? 0.2570 0.2433 0.2935 -0.0208 0.0280  -0.0151 69  TYR A C   
426  O O   . TYR A 69  ? 0.2862 0.2668 0.3178 -0.0211 0.0267  -0.0160 69  TYR A O   
427  C CB  . TYR A 69  ? 0.2321 0.2183 0.2684 -0.0207 0.0363  -0.0089 69  TYR A CB  
428  C CG  . TYR A 69  ? 0.2598 0.2493 0.3005 -0.0229 0.0411  -0.0056 69  TYR A CG  
429  C CD1 . TYR A 69  ? 0.2539 0.2384 0.2967 -0.0256 0.0436  -0.0027 69  TYR A CD1 
430  C CD2 . TYR A 69  ? 0.2626 0.2599 0.3052 -0.0220 0.0434  -0.0055 69  TYR A CD2 
431  C CE1 . TYR A 69  ? 0.2674 0.2549 0.3140 -0.0280 0.0480  0.0015  69  TYR A CE1 
432  C CE2 . TYR A 69  ? 0.2775 0.2790 0.3235 -0.0244 0.0483  -0.0021 69  TYR A CE2 
433  C CZ  . TYR A 69  ? 0.2664 0.2630 0.3142 -0.0276 0.0503  0.0020  69  TYR A CZ  
434  O OH  . TYR A 69  ? 0.3049 0.3060 0.3561 -0.0302 0.0552  0.0062  69  TYR A OH  
435  N N   . LYS A 70  ? 0.2787 0.2702 0.3168 -0.0184 0.0260  -0.0158 70  LYS A N   
436  C CA  A LYS A 70  ? 0.2846 0.2749 0.3181 -0.0161 0.0217  -0.0168 70  LYS A CA  
437  C CA  B LYS A 70  ? 0.2972 0.2875 0.3308 -0.0161 0.0217  -0.0167 70  LYS A CA  
438  C C   . LYS A 70  ? 0.2846 0.2747 0.3146 -0.0125 0.0228  -0.0158 70  LYS A C   
439  O O   . LYS A 70  ? 0.2828 0.2772 0.3171 -0.0111 0.0252  -0.0161 70  LYS A O   
440  C CB  A LYS A 70  ? 0.2949 0.2910 0.3346 -0.0166 0.0171  -0.0182 70  LYS A CB  
441  C CB  B LYS A 70  ? 0.3260 0.3225 0.3664 -0.0167 0.0175  -0.0181 70  LYS A CB  
442  C CG  A LYS A 70  ? 0.3141 0.3097 0.3505 -0.0135 0.0130  -0.0176 70  LYS A CG  
443  C CG  B LYS A 70  ? 0.3728 0.3681 0.4088 -0.0153 0.0124  -0.0181 70  LYS A CG  
444  C CD  A LYS A 70  ? 0.3454 0.3460 0.3858 -0.0142 0.0073  -0.0176 70  LYS A CD  
445  C CD  B LYS A 70  ? 0.4292 0.4316 0.4720 -0.0167 0.0075  -0.0185 70  LYS A CD  
446  C CE  A LYS A 70  ? 0.3591 0.3688 0.4118 -0.0134 0.0068  -0.0173 70  LYS A CE  
447  C CE  B LYS A 70  ? 0.4582 0.4594 0.4946 -0.0173 0.0021  -0.0181 70  LYS A CE  
448  N NZ  A LYS A 70  ? 0.3651 0.3809 0.4220 -0.0136 0.0001  -0.0160 70  LYS A NZ  
449  N NZ  B LYS A 70  ? 0.4962 0.5058 0.5388 -0.0199 -0.0031 -0.0182 70  LYS A NZ  
450  N N   . VAL A 71  ? 0.2602 0.2456 0.2825 -0.0113 0.0216  -0.0151 71  VAL A N   
451  C CA  . VAL A 71  ? 0.2940 0.2783 0.3124 -0.0089 0.0217  -0.0149 71  VAL A CA  
452  C C   . VAL A 71  ? 0.2922 0.2748 0.3096 -0.0077 0.0171  -0.0153 71  VAL A C   
453  O O   . VAL A 71  ? 0.3323 0.3125 0.3454 -0.0088 0.0148  -0.0144 71  VAL A O   
454  C CB  . VAL A 71  ? 0.3141 0.2951 0.3250 -0.0093 0.0235  -0.0129 71  VAL A CB  
455  C CG1 . VAL A 71  ? 0.2819 0.2617 0.2878 -0.0080 0.0229  -0.0133 71  VAL A CG1 
456  C CG2 . VAL A 71  ? 0.3395 0.3222 0.3516 -0.0106 0.0277  -0.0110 71  VAL A CG2 
457  N N   . GLU A 72  ? 0.2903 0.2741 0.3117 -0.0053 0.0162  -0.0162 72  GLU A N   
458  C CA  . GLU A 72  ? 0.2920 0.2739 0.3138 -0.0038 0.0117  -0.0154 72  GLU A CA  
459  C C   . GLU A 72  ? 0.2840 0.2608 0.3018 -0.0021 0.0125  -0.0160 72  GLU A C   
460  O O   . GLU A 72  ? 0.2952 0.2720 0.3158 -0.0001 0.0154  -0.0184 72  GLU A O   
461  C CB  . GLU A 72  ? 0.3501 0.3376 0.3822 -0.0020 0.0100  -0.0156 72  GLU A CB  
462  C CG  . GLU A 72  ? 0.4894 0.4780 0.5243 -0.0011 0.0044  -0.0132 72  GLU A CG  
463  N N   . ILE A 73  ? 0.2656 0.2380 0.2769 -0.0033 0.0100  -0.0143 73  ILE A N   
464  C CA  . ILE A 73  ? 0.2618 0.2285 0.2685 -0.0031 0.0101  -0.0148 73  ILE A CA  
465  C C   . ILE A 73  ? 0.2933 0.2564 0.3032 -0.0014 0.0064  -0.0133 73  ILE A C   
466  O O   . ILE A 73  ? 0.2958 0.2594 0.3046 -0.0024 0.0027  -0.0101 73  ILE A O   
467  C CB  . ILE A 73  ? 0.2961 0.2616 0.2950 -0.0060 0.0097  -0.0129 73  ILE A CB  
468  C CG1 . ILE A 73  ? 0.3347 0.3041 0.3321 -0.0071 0.0130  -0.0129 73  ILE A CG1 
469  C CG2 . ILE A 73  ? 0.3310 0.2918 0.3252 -0.0071 0.0094  -0.0134 73  ILE A CG2 
470  C CD1 . ILE A 73  ? 0.3300 0.2997 0.3217 -0.0091 0.0132  -0.0105 73  ILE A CD1 
471  N N   . ASP A 74  ? 0.3088 0.2675 0.3218 0.0010  0.0074  -0.0155 74  ASP A N   
472  C CA  . ASP A 74  ? 0.3177 0.2719 0.3360 0.0036  0.0040  -0.0134 74  ASP A CA  
473  C C   . ASP A 74  ? 0.3110 0.2576 0.3227 0.0010  0.0016  -0.0112 74  ASP A C   
474  O O   . ASP A 74  ? 0.3203 0.2588 0.3314 0.0013  0.0022  -0.0131 74  ASP A O   
475  C CB  . ASP A 74  ? 0.3504 0.3024 0.3770 0.0081  0.0067  -0.0167 74  ASP A CB  
476  C CG  . ASP A 74  ? 0.4261 0.3726 0.4596 0.0115  0.0030  -0.0134 74  ASP A CG  
477  O OD1 . ASP A 74  ? 0.4073 0.3539 0.4389 0.0098  -0.0021 -0.0077 74  ASP A OD1 
478  O OD2 . ASP A 74  ? 0.5070 0.4487 0.5474 0.0157  0.0054  -0.0162 74  ASP A OD2 
479  N N   . THR A 75  ? 0.3154 0.2648 0.3224 -0.0019 -0.0012 -0.0072 75  THR A N   
480  C CA  . THR A 75  ? 0.3121 0.2565 0.3134 -0.0049 -0.0033 -0.0043 75  THR A CA  
481  C C   . THR A 75  ? 0.3001 0.2382 0.3053 -0.0035 -0.0068 -0.0006 75  THR A C   
482  O O   . THR A 75  ? 0.3366 0.2673 0.3395 -0.0054 -0.0076 0.0004  75  THR A O   
483  C CB  . THR A 75  ? 0.2959 0.2459 0.2917 -0.0078 -0.0045 -0.0011 75  THR A CB  
484  O OG1 . THR A 75  ? 0.3009 0.2556 0.2993 -0.0068 -0.0072 0.0014  75  THR A OG1 
485  C CG2 . THR A 75  ? 0.3339 0.2886 0.3265 -0.0090 -0.0009 -0.0040 75  THR A CG2 
486  N N   . LYS A 76  ? 0.3024 0.2433 0.3147 -0.0001 -0.0092 0.0019  76  LYS A N   
487  C CA  . LYS A 76  ? 0.3402 0.2750 0.3569 0.0016  -0.0130 0.0070  76  LYS A CA  
488  C C   . LYS A 76  ? 0.3633 0.2869 0.3846 0.0041  -0.0108 0.0039  76  LYS A C   
489  O O   . LYS A 76  ? 0.3705 0.2851 0.3905 0.0025  -0.0126 0.0068  76  LYS A O   
490  C CB  . LYS A 76  ? 0.3665 0.3080 0.3907 0.0049  -0.0165 0.0110  76  LYS A CB  
491  C CG  . LYS A 76  ? 0.4253 0.3622 0.4551 0.0072  -0.0212 0.0184  76  LYS A CG  
492  C CD  . LYS A 76  ? 0.4711 0.4159 0.5114 0.0116  -0.0243 0.0214  76  LYS A CD  
493  C CE  . LYS A 76  ? 0.5179 0.4597 0.5648 0.0144  -0.0297 0.0304  76  LYS A CE  
494  N NZ  . LYS A 76  ? 0.5832 0.5333 0.6238 0.0107  -0.0356 0.0378  76  LYS A NZ  
495  N N   . SER A 77  ? 0.3576 0.2813 0.3837 0.0075  -0.0066 -0.0024 77  SER A N   
496  C CA  . SER A 77  ? 0.3657 0.2782 0.3949 0.0097  -0.0036 -0.0071 77  SER A CA  
497  C C   . SER A 77  ? 0.3758 0.2809 0.3952 0.0041  -0.0026 -0.0101 77  SER A C   
498  O O   . SER A 77  ? 0.3802 0.2734 0.4004 0.0036  -0.0027 -0.0110 77  SER A O   
499  C CB  . SER A 77  ? 0.3999 0.3155 0.4351 0.0141  0.0017  -0.0140 77  SER A CB  
500  O OG  . SER A 77  ? 0.4047 0.3281 0.4509 0.0191  0.0003  -0.0107 77  SER A OG  
501  N N   . TYR A 78  ? 0.3480 0.2601 0.3589 -0.0002 -0.0016 -0.0114 78  TYR A N   
502  C CA  . TYR A 78  ? 0.3593 0.2677 0.3615 -0.0061 -0.0016 -0.0127 78  TYR A CA  
503  C C   . TYR A 78  ? 0.3770 0.2785 0.3782 -0.0094 -0.0057 -0.0067 78  TYR A C   
504  O O   . TYR A 78  ? 0.3653 0.2566 0.3646 -0.0126 -0.0057 -0.0087 78  TYR A O   
505  C CB  . TYR A 78  ? 0.3498 0.2688 0.3454 -0.0093 -0.0007 -0.0126 78  TYR A CB  
506  C CG  . TYR A 78  ? 0.3280 0.2456 0.3160 -0.0154 -0.0013 -0.0129 78  TYR A CG  
507  C CD1 . TYR A 78  ? 0.3309 0.2444 0.3148 -0.0176 0.0011  -0.0193 78  TYR A CD1 
508  C CD2 . TYR A 78  ? 0.3281 0.2491 0.3130 -0.0191 -0.0039 -0.0072 78  TYR A CD2 
509  C CE1 . TYR A 78  ? 0.3744 0.2882 0.3519 -0.0236 0.0000  -0.0196 78  TYR A CE1 
510  C CE2 . TYR A 78  ? 0.3324 0.2536 0.3121 -0.0248 -0.0046 -0.0071 78  TYR A CE2 
511  C CZ  . TYR A 78  ? 0.3460 0.2639 0.3222 -0.0271 -0.0030 -0.0132 78  TYR A CZ  
512  O OH  . TYR A 78  ? 0.3893 0.3088 0.3605 -0.0335 -0.0042 -0.0133 78  TYR A OH  
513  N N   . TRP A 79  ? 0.3237 0.2307 0.3254 -0.0095 -0.0090 0.0005  79  TRP A N   
514  C CA  . TRP A 79  ? 0.3357 0.2379 0.3358 -0.0132 -0.0125 0.0073  79  TRP A CA  
515  C C   . TRP A 79  ? 0.3590 0.2488 0.3661 -0.0106 -0.0142 0.0097  79  TRP A C   
516  O O   . TRP A 79  ? 0.3749 0.2544 0.3811 -0.0143 -0.0153 0.0112  79  TRP A O   
517  C CB  . TRP A 79  ? 0.3187 0.2308 0.3164 -0.0139 -0.0150 0.0138  79  TRP A CB  
518  C CG  . TRP A 79  ? 0.3153 0.2371 0.3064 -0.0170 -0.0131 0.0121  79  TRP A CG  
519  C CD1 . TRP A 79  ? 0.3061 0.2378 0.2959 -0.0154 -0.0118 0.0108  79  TRP A CD1 
520  C CD2 . TRP A 79  ? 0.3337 0.2563 0.3193 -0.0224 -0.0121 0.0119  79  TRP A CD2 
521  N NE1 . TRP A 79  ? 0.2968 0.2344 0.2810 -0.0187 -0.0099 0.0101  79  TRP A NE1 
522  C CE2 . TRP A 79  ? 0.3177 0.2512 0.2996 -0.0228 -0.0102 0.0111  79  TRP A CE2 
523  C CE3 . TRP A 79  ? 0.3516 0.2673 0.3357 -0.0272 -0.0130 0.0128  79  TRP A CE3 
524  C CZ2 . TRP A 79  ? 0.3174 0.2556 0.2955 -0.0267 -0.0089 0.0113  79  TRP A CZ2 
525  C CZ3 . TRP A 79  ? 0.3231 0.2449 0.3026 -0.0321 -0.0120 0.0127  79  TRP A CZ3 
526  C CH2 . TRP A 79  ? 0.3476 0.2810 0.3248 -0.0313 -0.0100 0.0122  79  TRP A CH2 
527  N N   . LYS A 80  ? 0.3644 0.2546 0.3797 -0.0041 -0.0142 0.0097  80  LYS A N   
528  C CA  . LYS A 80  ? 0.3926 0.2713 0.4169 -0.0001 -0.0157 0.0127  80  LYS A CA  
529  C C   . LYS A 80  ? 0.4270 0.2912 0.4521 -0.0008 -0.0125 0.0057  80  LYS A C   
530  O O   . LYS A 80  ? 0.4377 0.2886 0.4662 -0.0016 -0.0142 0.0093  80  LYS A O   
531  C CB  . LYS A 80  ? 0.3928 0.2765 0.4276 0.0074  -0.0162 0.0141  80  LYS A CB  
532  C CG  . LYS A 80  ? 0.4110 0.3068 0.4456 0.0075  -0.0209 0.0222  80  LYS A CG  
533  C CD  . LYS A 80  ? 0.5157 0.4190 0.5613 0.0144  -0.0215 0.0227  80  LYS A CD  
534  N N   . ALA A 81  ? 0.4393 0.3051 0.4604 -0.0014 -0.0080 -0.0038 81  ALA A N   
535  C CA  . ALA A 81  ? 0.4590 0.3109 0.4785 -0.0033 -0.0047 -0.0121 81  ALA A CA  
536  C C   . ALA A 81  ? 0.4963 0.3416 0.5083 -0.0118 -0.0068 -0.0109 81  ALA A C   
537  O O   . ALA A 81  ? 0.5156 0.3465 0.5277 -0.0141 -0.0057 -0.0153 81  ALA A O   
538  C CB  . ALA A 81  ? 0.4968 0.3535 0.5124 -0.0024 0.0006  -0.0223 81  ALA A CB  
539  N N   . LEU A 82  ? 0.4665 0.3221 0.4725 -0.0167 -0.0096 -0.0051 82  LEU A N   
540  C CA  . LEU A 82  ? 0.4818 0.3341 0.4827 -0.0247 -0.0121 -0.0015 82  LEU A CA  
541  C C   . LEU A 82  ? 0.5033 0.3502 0.5082 -0.0255 -0.0160 0.0090  82  LEU A C   
542  O O   . LEU A 82  ? 0.5234 0.3697 0.5245 -0.0325 -0.0180 0.0133  82  LEU A O   
543  C CB  . LEU A 82  ? 0.4850 0.3530 0.4781 -0.0291 -0.0123 -0.0004 82  LEU A CB  
544  C CG  . LEU A 82  ? 0.5114 0.3846 0.4997 -0.0294 -0.0090 -0.0093 82  LEU A CG  
545  C CD1 . LEU A 82  ? 0.4834 0.3724 0.4663 -0.0320 -0.0091 -0.0070 82  LEU A CD1 
546  C CD2 . LEU A 82  ? 0.5207 0.3826 0.5057 -0.0349 -0.0083 -0.0159 82  LEU A CD2 
547  N N   . GLY A 83  ? 0.4600 0.3044 0.4730 -0.0188 -0.0173 0.0139  83  GLY A N   
548  C CA  . GLY A 83  ? 0.4818 0.3211 0.4988 -0.0191 -0.0214 0.0249  83  GLY A CA  
549  C C   . GLY A 83  ? 0.4900 0.3442 0.5028 -0.0204 -0.0244 0.0339  83  GLY A C   
550  O O   . GLY A 83  ? 0.4868 0.3388 0.5006 -0.0221 -0.0279 0.0441  83  GLY A O   
551  N N   . ILE A 84  ? 0.4098 0.2787 0.4177 -0.0198 -0.0229 0.0302  84  ILE A N   
552  C CA  . ILE A 84  ? 0.4495 0.3326 0.4523 -0.0212 -0.0249 0.0366  84  ILE A CA  
553  C C   . ILE A 84  ? 0.4650 0.3553 0.4721 -0.0148 -0.0262 0.0379  84  ILE A C   
554  O O   . ILE A 84  ? 0.4327 0.3245 0.4441 -0.0101 -0.0239 0.0312  84  ILE A O   
555  C CB  . ILE A 84  ? 0.4103 0.3041 0.4050 -0.0255 -0.0222 0.0321  84  ILE A CB  
556  C CG1 . ILE A 84  ? 0.5070 0.3950 0.4985 -0.0328 -0.0220 0.0329  84  ILE A CG1 
557  C CG2 . ILE A 84  ? 0.4453 0.3534 0.4351 -0.0257 -0.0229 0.0361  84  ILE A CG2 
558  C CD1 . ILE A 84  ? 0.5029 0.3975 0.4896 -0.0367 -0.0194 0.0269  84  ILE A CD1 
559  N N   . SER A 85  ? 0.4606 0.3566 0.4667 -0.0150 -0.0301 0.0470  85  SER A N   
560  C CA  . SER A 85  ? 0.4277 0.3348 0.4355 -0.0109 -0.0322 0.0487  85  SER A CA  
561  C C   . SER A 85  ? 0.4266 0.3470 0.4249 -0.0143 -0.0310 0.0467  85  SER A C   
562  O O   . SER A 85  ? 0.4367 0.3625 0.4279 -0.0183 -0.0326 0.0527  85  SER A O   
563  C CB  . SER A 85  ? 0.4839 0.3905 0.4949 -0.0097 -0.0377 0.0601  85  SER A CB  
564  O OG  . SER A 85  ? 0.4980 0.3908 0.5194 -0.0058 -0.0385 0.0622  85  SER A OG  
565  N N   . PRO A 86  ? 0.3778 0.3037 0.3761 -0.0125 -0.0278 0.0386  86  PRO A N   
566  C CA  . PRO A 86  ? 0.3513 0.2875 0.3417 -0.0153 -0.0255 0.0354  86  PRO A CA  
567  C C   . PRO A 86  ? 0.3358 0.2822 0.3242 -0.0145 -0.0281 0.0375  86  PRO A C   
568  O O   . PRO A 86  ? 0.3653 0.3126 0.3596 -0.0114 -0.0319 0.0410  86  PRO A O   
569  C CB  . PRO A 86  ? 0.3552 0.2906 0.3481 -0.0133 -0.0214 0.0266  86  PRO A CB  
570  C CG  . PRO A 86  ? 0.3892 0.3203 0.3917 -0.0080 -0.0223 0.0254  86  PRO A CG  
571  C CD  . PRO A 86  ? 0.4079 0.3302 0.4143 -0.0074 -0.0257 0.0321  86  PRO A CD  
572  N N   . PHE A 87  ? 0.3343 0.2888 0.3149 -0.0174 -0.0262 0.0353  87  PHE A N   
573  C CA  . PHE A 87  ? 0.3486 0.3126 0.3258 -0.0178 -0.0284 0.0360  87  PHE A CA  
574  C C   . PHE A 87  ? 0.3431 0.3104 0.3261 -0.0146 -0.0278 0.0300  87  PHE A C   
575  O O   . PHE A 87  ? 0.3576 0.3301 0.3443 -0.0132 -0.0319 0.0321  87  PHE A O   
576  C CB  . PHE A 87  ? 0.3600 0.3299 0.3270 -0.0218 -0.0257 0.0346  87  PHE A CB  
577  C CG  . PHE A 87  ? 0.3962 0.3748 0.3579 -0.0230 -0.0275 0.0338  87  PHE A CG  
578  C CD1 . PHE A 87  ? 0.4248 0.4077 0.3821 -0.0250 -0.0324 0.0408  87  PHE A CD1 
579  C CD2 . PHE A 87  ? 0.4131 0.3953 0.3738 -0.0229 -0.0244 0.0264  87  PHE A CD2 
580  C CE1 . PHE A 87  ? 0.4385 0.4302 0.3896 -0.0270 -0.0346 0.0394  87  PHE A CE1 
581  C CE2 . PHE A 87  ? 0.4652 0.4547 0.4204 -0.0249 -0.0261 0.0246  87  PHE A CE2 
582  C CZ  . PHE A 87  ? 0.4101 0.4046 0.3600 -0.0272 -0.0311 0.0306  87  PHE A CZ  
583  N N   . HIS A 88  ? 0.3209 0.2866 0.3052 -0.0138 -0.0230 0.0232  88  HIS A N   
584  C CA  . HIS A 88  ? 0.3098 0.2795 0.2989 -0.0118 -0.0216 0.0175  88  HIS A CA  
585  C C   . HIS A 88  ? 0.3120 0.2787 0.3119 -0.0073 -0.0219 0.0165  88  HIS A C   
586  O O   . HIS A 88  ? 0.3168 0.2758 0.3198 -0.0057 -0.0209 0.0169  88  HIS A O   
587  C CB  . HIS A 88  ? 0.3039 0.2735 0.2897 -0.0128 -0.0163 0.0118  88  HIS A CB  
588  C CG  . HIS A 88  ? 0.3374 0.3104 0.3142 -0.0162 -0.0147 0.0119  88  HIS A CG  
589  N ND1 . HIS A 88  ? 0.3420 0.3129 0.3140 -0.0182 -0.0130 0.0142  88  HIS A ND1 
590  C CD2 . HIS A 88  ? 0.3880 0.3665 0.3598 -0.0182 -0.0140 0.0093  88  HIS A CD2 
591  C CE1 . HIS A 88  ? 0.3958 0.3715 0.3607 -0.0206 -0.0111 0.0136  88  HIS A CE1 
592  N NE2 . HIS A 88  ? 0.4318 0.4113 0.3960 -0.0205 -0.0114 0.0100  88  HIS A NE2 
593  N N   . GLU A 89  ? 0.3089 0.2817 0.3150 -0.0056 -0.0231 0.0148  89  GLU A N   
594  C CA  . GLU A 89  ? 0.3156 0.2873 0.3331 -0.0010 -0.0222 0.0131  89  GLU A CA  
595  C C   . GLU A 89  ? 0.3165 0.2848 0.3341 -0.0004 -0.0160 0.0066  89  GLU A C   
596  O O   . GLU A 89  ? 0.3457 0.3087 0.3688 0.0028  -0.0136 0.0046  89  GLU A O   
597  C CB  . GLU A 89  ? 0.3479 0.3293 0.3725 -0.0001 -0.0251 0.0134  89  GLU A CB  
598  C CG  . GLU A 89  ? 0.3660 0.3517 0.3924 0.0001  -0.0320 0.0208  89  GLU A CG  
599  C CD  . GLU A 89  ? 0.3434 0.3229 0.3783 0.0050  -0.0338 0.0259  89  GLU A CD  
600  O OE1 . GLU A 89  ? 0.3537 0.3327 0.4002 0.0098  -0.0320 0.0241  89  GLU A OE1 
601  O OE2 . GLU A 89  ? 0.3107 0.2858 0.3414 0.0041  -0.0369 0.0320  89  GLU A OE2 
602  N N   . HIS A 90  ? 0.3334 0.3046 0.3449 -0.0034 -0.0134 0.0033  90  HIS A N   
603  C CA  . HIS A 90  ? 0.3737 0.3432 0.3842 -0.0035 -0.0080 -0.0015 90  HIS A CA  
604  C C   . HIS A 90  ? 0.3716 0.3426 0.3743 -0.0068 -0.0062 -0.0026 90  HIS A C   
605  O O   . HIS A 90  ? 0.3602 0.3337 0.3583 -0.0090 -0.0086 -0.0007 90  HIS A O   
606  C CB  . HIS A 90  ? 0.4008 0.3746 0.4197 -0.0013 -0.0058 -0.0047 90  HIS A CB  
607  C CG  . HIS A 90  ? 0.4268 0.4085 0.4490 -0.0026 -0.0079 -0.0046 90  HIS A CG  
608  N ND1 . HIS A 90  ? 0.5220 0.5058 0.5387 -0.0062 -0.0069 -0.0063 90  HIS A ND1 
609  C CD2 . HIS A 90  ? 0.4824 0.4706 0.5136 -0.0012 -0.0112 -0.0031 90  HIS A CD2 
610  C CE1 . HIS A 90  ? 0.4876 0.4782 0.5085 -0.0077 -0.0095 -0.0066 90  HIS A CE1 
611  N NE2 . HIS A 90  ? 0.5192 0.5136 0.5493 -0.0047 -0.0124 -0.0043 90  HIS A NE2 
612  N N   . ALA A 91  ? 0.3454 0.3153 0.3462 -0.0073 -0.0019 -0.0054 91  ALA A N   
613  C CA  . ALA A 91  ? 0.3610 0.3327 0.3571 -0.0094 0.0005  -0.0066 91  ALA A CA  
614  C C   . ALA A 91  ? 0.4375 0.4120 0.4386 -0.0090 0.0033  -0.0095 91  ALA A C   
615  O O   . ALA A 91  ? 0.3580 0.3321 0.3627 -0.0074 0.0055  -0.0108 91  ALA A O   
616  C CB  . ALA A 91  ? 0.3899 0.3592 0.3811 -0.0102 0.0029  -0.0059 91  ALA A CB  
617  N N   . GLU A 92  ? 0.4375 0.4145 0.4385 -0.0107 0.0036  -0.0109 92  GLU A N   
618  C CA  . GLU A 92  ? 0.4699 0.4492 0.4765 -0.0110 0.0060  -0.0132 92  GLU A CA  
619  C C   . GLU A 92  ? 0.4433 0.4206 0.4467 -0.0128 0.0094  -0.0144 92  GLU A C   
620  O O   . GLU A 92  ? 0.5093 0.4854 0.5076 -0.0142 0.0087  -0.0148 92  GLU A O   
621  C CB  . GLU A 92  ? 0.5112 0.4955 0.5235 -0.0120 0.0027  -0.0138 92  GLU A CB  
622  C CG  . GLU A 92  ? 0.5348 0.5211 0.5500 -0.0148 0.0044  -0.0165 92  GLU A CG  
623  N N   . VAL A 93  ? 0.3495 0.3261 0.3554 -0.0125 0.0134  -0.0146 93  VAL A N   
624  C CA  . VAL A 93  ? 0.3267 0.3004 0.3310 -0.0134 0.0168  -0.0148 93  VAL A CA  
625  C C   . VAL A 93  ? 0.3131 0.2879 0.3238 -0.0152 0.0185  -0.0163 93  VAL A C   
626  O O   . VAL A 93  ? 0.3107 0.2885 0.3259 -0.0146 0.0195  -0.0156 93  VAL A O   
627  C CB  . VAL A 93  ? 0.4407 0.4134 0.4431 -0.0117 0.0195  -0.0120 93  VAL A CB  
628  C CG1 . VAL A 93  ? 0.4640 0.4340 0.4668 -0.0117 0.0232  -0.0108 93  VAL A CG1 
629  C CG2 . VAL A 93  ? 0.5004 0.4729 0.4976 -0.0108 0.0173  -0.0105 93  VAL A CG2 
630  N N   . VAL A 94  ? 0.3089 0.2811 0.3199 -0.0177 0.0193  -0.0187 94  VAL A N   
631  C CA  . VAL A 94  ? 0.3032 0.2760 0.3205 -0.0205 0.0205  -0.0202 94  VAL A CA  
632  C C   . VAL A 94  ? 0.2968 0.2630 0.3140 -0.0214 0.0247  -0.0204 94  VAL A C   
633  O O   . VAL A 94  ? 0.2963 0.2577 0.3088 -0.0212 0.0254  -0.0222 94  VAL A O   
634  C CB  . VAL A 94  ? 0.3266 0.3028 0.3456 -0.0240 0.0164  -0.0237 94  VAL A CB  
635  C CG1 . VAL A 94  ? 0.3247 0.3017 0.3512 -0.0278 0.0179  -0.0252 94  VAL A CG1 
636  C CG2 . VAL A 94  ? 0.3506 0.3334 0.3707 -0.0224 0.0117  -0.0224 94  VAL A CG2 
637  N N   . PHE A 95  ? 0.2924 0.2578 0.3146 -0.0219 0.0281  -0.0181 95  PHE A N   
638  C CA  . PHE A 95  ? 0.2909 0.2494 0.3141 -0.0217 0.0325  -0.0163 95  PHE A CA  
639  C C   . PHE A 95  ? 0.3084 0.2664 0.3385 -0.0244 0.0353  -0.0143 95  PHE A C   
640  O O   . PHE A 95  ? 0.2950 0.2595 0.3284 -0.0250 0.0351  -0.0129 95  PHE A O   
641  C CB  . PHE A 95  ? 0.3173 0.2754 0.3365 -0.0174 0.0340  -0.0115 95  PHE A CB  
642  C CG  . PHE A 95  ? 0.2762 0.2403 0.2957 -0.0162 0.0345  -0.0073 95  PHE A CG  
643  C CD1 . PHE A 95  ? 0.3354 0.3050 0.3527 -0.0153 0.0319  -0.0082 95  PHE A CD1 
644  C CD2 . PHE A 95  ? 0.3160 0.2792 0.3380 -0.0162 0.0381  -0.0024 95  PHE A CD2 
645  C CE1 . PHE A 95  ? 0.2980 0.2721 0.3145 -0.0144 0.0331  -0.0055 95  PHE A CE1 
646  C CE2 . PHE A 95  ? 0.3267 0.2956 0.3473 -0.0156 0.0389  0.0011  95  PHE A CE2 
647  C CZ  . PHE A 95  ? 0.3134 0.2877 0.3310 -0.0148 0.0366  -0.0012 95  PHE A CZ  
648  N N   . THR A 96  ? 0.2930 0.2428 0.3257 -0.0258 0.0386  -0.0143 96  THR A N   
649  C CA  . THR A 96  ? 0.3461 0.2935 0.3852 -0.0283 0.0421  -0.0108 96  THR A CA  
650  C C   . THR A 96  ? 0.3674 0.3152 0.4057 -0.0248 0.0450  -0.0033 96  THR A C   
651  O O   . THR A 96  ? 0.3748 0.3184 0.4101 -0.0210 0.0461  -0.0009 96  THR A O   
652  C CB  . THR A 96  ? 0.3789 0.3156 0.4215 -0.0317 0.0443  -0.0140 96  THR A CB  
653  O OG1 . THR A 96  ? 0.4088 0.3467 0.4516 -0.0363 0.0409  -0.0214 96  THR A OG1 
654  C CG2 . THR A 96  ? 0.4214 0.3545 0.4718 -0.0348 0.0482  -0.0092 96  THR A CG2 
655  N N   . ALA A 97  ? 0.3236 0.2775 0.3646 -0.0260 0.0464  0.0007  97  ALA A N   
656  C CA  . ALA A 97  ? 0.2997 0.2557 0.3386 -0.0236 0.0488  0.0082  97  ALA A CA  
657  C C   . ALA A 97  ? 0.3260 0.2782 0.3708 -0.0263 0.0529  0.0141  97  ALA A C   
658  O O   . ALA A 97  ? 0.3254 0.2773 0.3765 -0.0310 0.0542  0.0125  97  ALA A O   
659  C CB  . ALA A 97  ? 0.3076 0.2742 0.3422 -0.0225 0.0476  0.0087  97  ALA A CB  
660  N N   . ASN A 98  ? 0.3148 0.2644 0.3583 -0.0235 0.0549  0.0215  98  ASN A N   
661  C CA  . ASN A 98  ? 0.3397 0.2867 0.3877 -0.0254 0.0588  0.0301  98  ASN A CA  
662  C C   . ASN A 98  ? 0.3907 0.3261 0.4471 -0.0288 0.0614  0.0294  98  ASN A C   
663  O O   . ASN A 98  ? 0.4542 0.3880 0.5156 -0.0321 0.0645  0.0352  98  ASN A O   
664  C CB  . ASN A 98  ? 0.3335 0.2915 0.3801 -0.0283 0.0601  0.0328  98  ASN A CB  
665  C CG  . ASN A 98  ? 0.3732 0.3414 0.4112 -0.0255 0.0578  0.0315  98  ASN A CG  
666  O OD1 . ASN A 98  ? 0.4174 0.3928 0.4541 -0.0265 0.0569  0.0261  98  ASN A OD1 
667  N ND2 . ASN A 98  ? 0.3127 0.2813 0.3453 -0.0220 0.0566  0.0362  98  ASN A ND2 
668  N N   . ASP A 99  ? 0.4285 0.3553 0.4860 -0.0282 0.0603  0.0223  99  ASP A N   
669  C CA  . ASP A 99  ? 0.4490 0.3637 0.5138 -0.0324 0.0626  0.0194  99  ASP A CA  
670  C C   . ASP A 99  ? 0.5285 0.4323 0.5986 -0.0306 0.0668  0.0277  99  ASP A C   
671  O O   . ASP A 99  ? 0.5444 0.4396 0.6218 -0.0352 0.0696  0.0294  99  ASP A O   
672  C CB  . ASP A 99  ? 0.4873 0.3958 0.5498 -0.0323 0.0606  0.0088  99  ASP A CB  
673  N N   . SER A 100 ? 0.4992 0.4036 0.5668 -0.0242 0.0670  0.0339  100 SER A N   
674  C CA  . SER A 100 ? 0.5348 0.4299 0.6085 -0.0215 0.0704  0.0429  100 SER A CA  
675  C C   . SER A 100 ? 0.5606 0.4658 0.6325 -0.0207 0.0705  0.0553  100 SER A C   
676  O O   . SER A 100 ? 0.6555 0.5585 0.7297 -0.0163 0.0716  0.0647  100 SER A O   
677  C CB  . SER A 100 ? 0.5390 0.4271 0.6133 -0.0147 0.0710  0.0412  100 SER A CB  
678  N N   . GLY A 101 ? 0.5079 0.4247 0.5756 -0.0250 0.0695  0.0553  101 GLY A N   
679  C CA  . GLY A 101 ? 0.4460 0.3751 0.5085 -0.0246 0.0692  0.0649  101 GLY A CA  
680  C C   . GLY A 101 ? 0.4811 0.4235 0.5334 -0.0224 0.0655  0.0612  101 GLY A C   
681  O O   . GLY A 101 ? 0.4022 0.3440 0.4519 -0.0197 0.0628  0.0533  101 GLY A O   
682  N N   . PRO A 102 ? 0.4320 0.3861 0.4780 -0.0236 0.0656  0.0671  102 PRO A N   
683  C CA  . PRO A 102 ? 0.4369 0.4026 0.4731 -0.0221 0.0624  0.0629  102 PRO A CA  
684  C C   . PRO A 102 ? 0.4189 0.3843 0.4520 -0.0168 0.0590  0.0637  102 PRO A C   
685  O O   . PRO A 102 ? 0.4101 0.3723 0.4465 -0.0139 0.0592  0.0723  102 PRO A O   
686  C CB  . PRO A 102 ? 0.4867 0.4634 0.5164 -0.0244 0.0638  0.0705  102 PRO A CB  
687  C CG  . PRO A 102 ? 0.4879 0.4598 0.5243 -0.0273 0.0678  0.0799  102 PRO A CG  
688  C CD  . PRO A 102 ? 0.4566 0.4132 0.5039 -0.0266 0.0688  0.0780  102 PRO A CD  
689  N N   . ARG A 103 ? 0.3859 0.3548 0.4142 -0.0157 0.0560  0.0551  103 ARG A N   
690  C CA  . ARG A 103 ? 0.3652 0.3368 0.3896 -0.0118 0.0525  0.0548  103 ARG A CA  
691  C C   . ARG A 103 ? 0.3733 0.3547 0.3882 -0.0129 0.0496  0.0499  103 ARG A C   
692  O O   . ARG A 103 ? 0.3699 0.3547 0.3821 -0.0157 0.0506  0.0448  103 ARG A O   
693  C CB  . ARG A 103 ? 0.3757 0.3381 0.4051 -0.0092 0.0520  0.0479  103 ARG A CB  
694  C CG  . ARG A 103 ? 0.4008 0.3511 0.4397 -0.0080 0.0554  0.0506  103 ARG A CG  
695  C CD  . ARG A 103 ? 0.4437 0.3938 0.4863 -0.0037 0.0560  0.0612  103 ARG A CD  
696  N NE  . ARG A 103 ? 0.4834 0.4201 0.5360 -0.0015 0.0597  0.0631  103 ARG A NE  
697  C CZ  . ARG A 103 ? 0.4944 0.4238 0.5532 -0.0032 0.0629  0.0692  103 ARG A CZ  
698  N NH1 . ARG A 103 ? 0.5429 0.4779 0.5989 -0.0076 0.0633  0.0742  103 ARG A NH1 
699  N NH2 . ARG A 103 ? 0.5197 0.4351 0.5877 -0.0009 0.0664  0.0695  103 ARG A NH2 
700  N N   . ARG A 104 ? 0.3509 0.3368 0.3615 -0.0106 0.0464  0.0514  104 ARG A N   
701  C CA  . ARG A 104 ? 0.3768 0.3697 0.3790 -0.0116 0.0434  0.0462  104 ARG A CA  
702  C C   . ARG A 104 ? 0.3219 0.3104 0.3257 -0.0095 0.0411  0.0392  104 ARG A C   
703  O O   . ARG A 104 ? 0.3549 0.3403 0.3632 -0.0066 0.0406  0.0415  104 ARG A O   
704  C CB  . ARG A 104 ? 0.3923 0.3943 0.3880 -0.0118 0.0410  0.0535  104 ARG A CB  
705  C CG  . ARG A 104 ? 0.4510 0.4578 0.4441 -0.0142 0.0434  0.0616  104 ARG A CG  
706  C CD  . ARG A 104 ? 0.5044 0.5226 0.4878 -0.0160 0.0404  0.0673  104 ARG A CD  
707  N N   . TYR A 105 ? 0.3164 0.3052 0.3169 -0.0108 0.0399  0.0311  105 TYR A N   
708  C CA  . TYR A 105 ? 0.2660 0.2510 0.2677 -0.0094 0.0378  0.0251  105 TYR A CA  
709  C C   . TYR A 105 ? 0.3067 0.2961 0.3018 -0.0102 0.0346  0.0216  105 TYR A C   
710  O O   . TYR A 105 ? 0.3108 0.3031 0.3016 -0.0120 0.0350  0.0188  105 TYR A O   
711  C CB  . TYR A 105 ? 0.3208 0.3010 0.3263 -0.0105 0.0389  0.0184  105 TYR A CB  
712  C CG  . TYR A 105 ? 0.2962 0.2703 0.3087 -0.0109 0.0419  0.0199  105 TYR A CG  
713  C CD1 . TYR A 105 ? 0.3381 0.3052 0.3546 -0.0095 0.0422  0.0180  105 TYR A CD1 
714  C CD2 . TYR A 105 ? 0.3181 0.2932 0.3330 -0.0130 0.0449  0.0235  105 TYR A CD2 
715  C CE1 . TYR A 105 ? 0.3514 0.3113 0.3743 -0.0103 0.0452  0.0188  105 TYR A CE1 
716  C CE2 . TYR A 105 ? 0.3306 0.2989 0.3527 -0.0140 0.0478  0.0253  105 TYR A CE2 
717  C CZ  . TYR A 105 ? 0.3349 0.2951 0.3610 -0.0128 0.0478  0.0226  105 TYR A CZ  
718  O OH  . TYR A 105 ? 0.3425 0.2948 0.3755 -0.0144 0.0509  0.0237  105 TYR A OH  
719  N N   . THR A 106 ? 0.2795 0.2692 0.2740 -0.0088 0.0321  0.0218  106 THR A N   
720  C CA  . THR A 106 ? 0.2818 0.2736 0.2712 -0.0099 0.0288  0.0178  106 THR A CA  
721  C C   . THR A 106 ? 0.2721 0.2589 0.2642 -0.0089 0.0280  0.0133  106 THR A C   
722  O O   . THR A 106 ? 0.3217 0.3063 0.3176 -0.0069 0.0287  0.0148  106 THR A O   
723  C CB  . THR A 106 ? 0.3403 0.3383 0.3269 -0.0103 0.0261  0.0225  106 THR A CB  
724  O OG1 . THR A 106 ? 0.4058 0.4096 0.3890 -0.0117 0.0265  0.0277  106 THR A OG1 
725  C CG2 . THR A 106 ? 0.3670 0.3660 0.3484 -0.0124 0.0227  0.0181  106 THR A CG2 
726  N N   . ILE A 107 ? 0.2787 0.2636 0.2687 -0.0099 0.0267  0.0077  107 ILE A N   
727  C CA  . ILE A 107 ? 0.2898 0.2710 0.2812 -0.0094 0.0252  0.0039  107 ILE A CA  
728  C C   . ILE A 107 ? 0.3074 0.2900 0.2942 -0.0105 0.0219  0.0033  107 ILE A C   
729  O O   . ILE A 107 ? 0.3533 0.3363 0.3367 -0.0119 0.0209  0.0010  107 ILE A O   
730  C CB  . ILE A 107 ? 0.3282 0.3071 0.3218 -0.0097 0.0254  -0.0006 107 ILE A CB  
731  C CG1 . ILE A 107 ? 0.3749 0.3530 0.3734 -0.0099 0.0285  -0.0001 107 ILE A CG1 
732  C CG2 . ILE A 107 ? 0.3398 0.3160 0.3338 -0.0096 0.0228  -0.0036 107 ILE A CG2 
733  C CD1 . ILE A 107 ? 0.3731 0.3478 0.3745 -0.0092 0.0300  0.0018  107 ILE A CD1 
734  N N   . ALA A 108 ? 0.2862 0.2694 0.2733 -0.0101 0.0208  0.0050  108 ALA A N   
735  C CA  . ALA A 108 ? 0.3108 0.2956 0.2948 -0.0118 0.0179  0.0052  108 ALA A CA  
736  C C   . ALA A 108 ? 0.2929 0.2740 0.2770 -0.0118 0.0165  0.0027  108 ALA A C   
737  O O   . ALA A 108 ? 0.3044 0.2844 0.2904 -0.0105 0.0178  0.0024  108 ALA A O   
738  C CB  . ALA A 108 ? 0.3600 0.3505 0.3452 -0.0116 0.0179  0.0104  108 ALA A CB  
739  N N   . ALA A 109 ? 0.3109 0.2898 0.2924 -0.0135 0.0138  0.0009  109 ALA A N   
740  C CA  . ALA A 109 ? 0.3040 0.2802 0.2852 -0.0138 0.0120  0.0002  109 ALA A CA  
741  C C   . ALA A 109 ? 0.3042 0.2808 0.2830 -0.0164 0.0094  0.0020  109 ALA A C   
742  O O   . ALA A 109 ? 0.2935 0.2694 0.2704 -0.0183 0.0082  0.0012  109 ALA A O   
743  C CB  . ALA A 109 ? 0.3210 0.2930 0.3034 -0.0130 0.0109  -0.0030 109 ALA A CB  
744  N N   . LEU A 110 ? 0.2719 0.2502 0.2504 -0.0171 0.0090  0.0042  110 LEU A N   
745  C CA  . LEU A 110 ? 0.2829 0.2617 0.2597 -0.0202 0.0067  0.0066  110 LEU A CA  
746  C C   . LEU A 110 ? 0.2676 0.2416 0.2432 -0.0208 0.0046  0.0065  110 LEU A C   
747  O O   . LEU A 110 ? 0.2997 0.2748 0.2747 -0.0196 0.0053  0.0069  110 LEU A O   
748  C CB  . LEU A 110 ? 0.3061 0.2923 0.2842 -0.0205 0.0084  0.0102  110 LEU A CB  
749  C CG  . LEU A 110 ? 0.3521 0.3414 0.3297 -0.0243 0.0067  0.0136  110 LEU A CG  
750  C CD1 . LEU A 110 ? 0.3430 0.3313 0.3197 -0.0279 0.0038  0.0134  110 LEU A CD1 
751  C CD2 . LEU A 110 ? 0.4034 0.4016 0.3840 -0.0233 0.0097  0.0170  110 LEU A CD2 
752  N N   . LEU A 111 ? 0.2658 0.2346 0.2407 -0.0228 0.0019  0.0064  111 LEU A N   
753  C CA  . LEU A 111 ? 0.2925 0.2558 0.2675 -0.0226 -0.0005 0.0070  111 LEU A CA  
754  C C   . LEU A 111 ? 0.2854 0.2480 0.2587 -0.0263 -0.0025 0.0114  111 LEU A C   
755  O O   . LEU A 111 ? 0.2773 0.2390 0.2504 -0.0297 -0.0033 0.0121  111 LEU A O   
756  C CB  . LEU A 111 ? 0.2824 0.2384 0.2593 -0.0215 -0.0016 0.0038  111 LEU A CB  
757  C CG  . LEU A 111 ? 0.3159 0.2730 0.2945 -0.0185 0.0008  -0.0005 111 LEU A CG  
758  C CD1 . LEU A 111 ? 0.3032 0.2532 0.2845 -0.0168 0.0003  -0.0038 111 LEU A CD1 
759  C CD2 . LEU A 111 ? 0.2824 0.2437 0.2626 -0.0161 0.0019  -0.0003 111 LEU A CD2 
760  N N   . SER A 112 ? 0.2850 0.2480 0.2571 -0.0262 -0.0036 0.0144  112 SER A N   
761  C CA  . SER A 112 ? 0.3116 0.2716 0.2824 -0.0294 -0.0061 0.0193  112 SER A CA  
762  C C   . SER A 112 ? 0.3123 0.2678 0.2836 -0.0275 -0.0090 0.0210  112 SER A C   
763  O O   . SER A 112 ? 0.3025 0.2593 0.2750 -0.0241 -0.0088 0.0184  112 SER A O   
764  C CB  . SER A 112 ? 0.3507 0.3189 0.3185 -0.0320 -0.0044 0.0233  112 SER A CB  
765  O OG  . SER A 112 ? 0.3804 0.3552 0.3494 -0.0329 -0.0016 0.0224  112 SER A OG  
766  N N   . PRO A 113 ? 0.2996 0.2506 0.2706 -0.0299 -0.0117 0.0262  113 PRO A N   
767  C CA  . PRO A 113 ? 0.3008 0.2475 0.2740 -0.0273 -0.0150 0.0286  113 PRO A CA  
768  C C   . PRO A 113 ? 0.3018 0.2560 0.2717 -0.0259 -0.0157 0.0298  113 PRO A C   
769  O O   . PRO A 113 ? 0.3210 0.2748 0.2940 -0.0227 -0.0178 0.0291  113 PRO A O   
770  C CB  . PRO A 113 ? 0.3064 0.2465 0.2799 -0.0307 -0.0176 0.0349  113 PRO A CB  
771  C CG  . PRO A 113 ? 0.3172 0.2529 0.2921 -0.0334 -0.0159 0.0315  113 PRO A CG  
772  C CD  . PRO A 113 ? 0.3304 0.2765 0.3021 -0.0344 -0.0126 0.0287  113 PRO A CD  
773  N N   . TYR A 114 ? 0.2931 0.2548 0.2570 -0.0284 -0.0137 0.0311  114 TYR A N   
774  C CA  . TYR A 114 ? 0.3087 0.2776 0.2678 -0.0281 -0.0137 0.0309  114 TYR A CA  
775  C C   . TYR A 114 ? 0.3016 0.2762 0.2585 -0.0273 -0.0092 0.0251  114 TYR A C   
776  O O   . TYR A 114 ? 0.3433 0.3235 0.2945 -0.0280 -0.0082 0.0243  114 TYR A O   
777  C CB  . TYR A 114 ? 0.3249 0.2974 0.2775 -0.0318 -0.0149 0.0377  114 TYR A CB  
778  C CG  . TYR A 114 ? 0.3487 0.3168 0.3028 -0.0319 -0.0203 0.0445  114 TYR A CG  
779  C CD1 . TYR A 114 ? 0.3972 0.3560 0.3569 -0.0323 -0.0222 0.0481  114 TYR A CD1 
780  C CD2 . TYR A 114 ? 0.3982 0.3711 0.3484 -0.0318 -0.0239 0.0476  114 TYR A CD2 
781  C CE1 . TYR A 114 ? 0.4478 0.4014 0.4101 -0.0320 -0.0270 0.0553  114 TYR A CE1 
782  C CE2 . TYR A 114 ? 0.4053 0.3747 0.3580 -0.0314 -0.0293 0.0552  114 TYR A CE2 
783  C CZ  . TYR A 114 ? 0.4386 0.3978 0.3978 -0.0312 -0.0306 0.0593  114 TYR A CZ  
784  O OH  . TYR A 114 ? 0.5348 0.4895 0.4976 -0.0303 -0.0358 0.0678  114 TYR A OH  
785  N N   . SER A 115 ? 0.3095 0.2824 0.2705 -0.0258 -0.0064 0.0210  115 SER A N   
786  C CA  . SER A 115 ? 0.3073 0.2846 0.2677 -0.0245 -0.0020 0.0164  115 SER A CA  
787  C C   . SER A 115 ? 0.3159 0.2903 0.2817 -0.0221 -0.0008 0.0125  115 SER A C   
788  O O   . SER A 115 ? 0.3529 0.3231 0.3216 -0.0225 -0.0021 0.0134  115 SER A O   
789  C CB  . SER A 115 ? 0.3471 0.3296 0.3051 -0.0266 0.0014  0.0185  115 SER A CB  
790  O OG  . SER A 115 ? 0.4257 0.4126 0.3833 -0.0248 0.0061  0.0146  115 SER A OG  
791  N N   . TYR A 116 ? 0.3036 0.2796 0.2704 -0.0200 0.0020  0.0083  116 TYR A N   
792  C CA  . TYR A 116 ? 0.2951 0.2701 0.2661 -0.0184 0.0041  0.0059  116 TYR A CA  
793  C C   . TYR A 116 ? 0.3014 0.2796 0.2727 -0.0170 0.0083  0.0036  116 TYR A C   
794  O O   . TYR A 116 ? 0.2944 0.2739 0.2631 -0.0169 0.0095  0.0018  116 TYR A O   
795  C CB  . TYR A 116 ? 0.3274 0.2985 0.3022 -0.0166 0.0026  0.0034  116 TYR A CB  
796  C CG  . TYR A 116 ? 0.3296 0.3016 0.3056 -0.0154 0.0024  0.0007  116 TYR A CG  
797  C CD1 . TYR A 116 ? 0.3485 0.3216 0.3263 -0.0143 0.0056  -0.0025 116 TYR A CD1 
798  C CD2 . TYR A 116 ? 0.3757 0.3477 0.3511 -0.0158 -0.0013 0.0019  116 TYR A CD2 
799  C CE1 . TYR A 116 ? 0.4299 0.4036 0.4091 -0.0142 0.0052  -0.0052 116 TYR A CE1 
800  C CE2 . TYR A 116 ? 0.4191 0.3933 0.3962 -0.0154 -0.0022 -0.0006 116 TYR A CE2 
801  C CZ  . TYR A 116 ? 0.4137 0.3886 0.3925 -0.0150 0.0010  -0.0044 116 TYR A CZ  
802  O OH  . TYR A 116 ? 0.5538 0.5308 0.5340 -0.0158 -0.0003 -0.0070 116 TYR A OH  
803  N N   . SER A 117 ? 0.3033 0.2823 0.2777 -0.0158 0.0105  0.0035  117 SER A N   
804  C CA  A SER A 117 ? 0.3082 0.2889 0.2846 -0.0138 0.0147  0.0020  117 SER A CA  
805  C CA  B SER A 117 ? 0.3087 0.2895 0.2851 -0.0138 0.0147  0.0020  117 SER A CA  
806  C C   . SER A 117 ? 0.3440 0.3228 0.3240 -0.0124 0.0150  0.0009  117 SER A C   
807  O O   . SER A 117 ? 0.3070 0.2849 0.2873 -0.0132 0.0129  0.0016  117 SER A O   
808  C CB  A SER A 117 ? 0.3385 0.3246 0.3162 -0.0135 0.0173  0.0052  117 SER A CB  
809  C CB  B SER A 117 ? 0.3384 0.3245 0.3160 -0.0135 0.0174  0.0051  117 SER A CB  
810  O OG  A SER A 117 ? 0.3742 0.3620 0.3546 -0.0138 0.0163  0.0076  117 SER A OG  
811  O OG  B SER A 117 ? 0.3856 0.3748 0.3600 -0.0154 0.0170  0.0071  117 SER A OG  
812  N N   . THR A 118 ? 0.3308 0.3083 0.3130 -0.0108 0.0179  -0.0013 118 THR A N   
813  C CA  . THR A 118 ? 0.3566 0.3329 0.3421 -0.0098 0.0189  -0.0015 118 THR A CA  
814  C C   . THR A 118 ? 0.3413 0.3178 0.3301 -0.0078 0.0230  -0.0005 118 THR A C   
815  O O   . THR A 118 ? 0.3255 0.3007 0.3142 -0.0070 0.0254  -0.0022 118 THR A O   
816  C CB  . THR A 118 ? 0.3508 0.3243 0.3377 -0.0102 0.0178  -0.0047 118 THR A CB  
817  O OG1 . THR A 118 ? 0.4438 0.4173 0.4337 -0.0095 0.0194  -0.0042 118 THR A OG1 
818  C CG2 . THR A 118 ? 0.3546 0.3261 0.3416 -0.0106 0.0191  -0.0080 118 THR A CG2 
819  N N   . THR A 119 ? 0.3705 0.3487 0.3618 -0.0069 0.0239  0.0025  119 THR A N   
820  C CA  . THR A 119 ? 0.3332 0.3119 0.3289 -0.0044 0.0275  0.0054  119 THR A CA  
821  C C   . THR A 119 ? 0.3309 0.3086 0.3285 -0.0044 0.0281  0.0069  119 THR A C   
822  O O   . THR A 119 ? 0.3254 0.3044 0.3205 -0.0062 0.0259  0.0064  119 THR A O   
823  C CB  . THR A 119 ? 0.4005 0.3859 0.3980 -0.0032 0.0276  0.0106  119 THR A CB  
824  O OG1 . THR A 119 ? 0.4638 0.4517 0.4589 -0.0042 0.0266  0.0099  119 THR A OG1 
825  C CG2 . THR A 119 ? 0.3830 0.3680 0.3868 0.0006  0.0319  0.0135  119 THR A CG2 
826  N N   . ALA A 120 ? 0.3009 0.2757 0.3030 -0.0026 0.0315  0.0082  120 ALA A N   
827  C CA  . ALA A 120 ? 0.3227 0.2974 0.3270 -0.0028 0.0325  0.0113  120 ALA A CA  
828  C C   . ALA A 120 ? 0.3004 0.2778 0.3088 -0.0001 0.0343  0.0181  120 ALA A C   
829  O O   . ALA A 120 ? 0.3712 0.3465 0.3840 0.0028  0.0369  0.0192  120 ALA A O   
830  C CB  . ALA A 120 ? 0.3459 0.3143 0.3527 -0.0039 0.0345  0.0077  120 ALA A CB  
831  N N   . VAL A 121 ? 0.3093 0.2919 0.3162 -0.0010 0.0329  0.0229  121 VAL A N   
832  C CA  . VAL A 121 ? 0.3155 0.3016 0.3263 0.0011  0.0340  0.0308  121 VAL A CA  
833  C C   . VAL A 121 ? 0.3303 0.3133 0.3422 0.0001  0.0361  0.0330  121 VAL A C   
834  O O   . VAL A 121 ? 0.3241 0.3092 0.3310 -0.0029 0.0350  0.0315  121 VAL A O   
835  C CB  . VAL A 121 ? 0.3476 0.3437 0.3546 -0.0002 0.0303  0.0353  121 VAL A CB  
836  C CG1 . VAL A 121 ? 0.3789 0.3802 0.3911 0.0023  0.0309  0.0449  121 VAL A CG1 
837  C CG2 . VAL A 121 ? 0.3764 0.3755 0.3818 -0.0007 0.0280  0.0323  121 VAL A CG2 
838  N N   . VAL A 122 ? 0.3028 0.2804 0.3217 0.0027  0.0395  0.0367  122 VAL A N   
839  C CA  . VAL A 122 ? 0.3289 0.3016 0.3505 0.0015  0.0422  0.0391  122 VAL A CA  
840  C C   . VAL A 122 ? 0.3616 0.3376 0.3875 0.0039  0.0429  0.0498  122 VAL A C   
841  O O   . VAL A 122 ? 0.3895 0.3642 0.4219 0.0082  0.0442  0.0539  122 VAL A O   
842  C CB  . VAL A 122 ? 0.3591 0.3204 0.3859 0.0016  0.0456  0.0337  122 VAL A CB  
843  C CG1 . VAL A 122 ? 0.3783 0.3353 0.4082 -0.0009 0.0481  0.0363  122 VAL A CG1 
844  C CG2 . VAL A 122 ? 0.3606 0.3208 0.3830 -0.0008 0.0439  0.0241  122 VAL A CG2 
845  N N   . THR A 123 ? 0.3497 0.3312 0.3715 0.0014  0.0420  0.0549  123 THR A N   
846  C CA  . THR A 123 ? 0.4335 0.4193 0.4589 0.0034  0.0422  0.0668  123 THR A CA  
847  C C   . THR A 123 ? 0.4658 0.4489 0.4920 0.0012  0.0448  0.0722  123 THR A C   
848  O O   . THR A 123 ? 0.3831 0.3643 0.4056 -0.0027 0.0461  0.0667  123 THR A O   
849  C CB  . THR A 123 ? 0.4885 0.4878 0.5070 0.0022  0.0375  0.0710  123 THR A CB  
850  O OG1 . THR A 123 ? 0.4851 0.4895 0.4934 -0.0028 0.0363  0.0682  123 THR A OG1 
851  C CG2 . THR A 123 ? 0.4552 0.4575 0.4730 0.0034  0.0349  0.0657  123 THR A CG2 
852  N N   . ASN A 124 ? 0.4900 0.4738 0.5220 0.0038  0.0456  0.0838  124 ASN A N   
853  C CA  . ASN A 124 ? 0.6323 0.6158 0.6645 0.0014  0.0476  0.0921  124 ASN A CA  
854  C C   . ASN A 124 ? 0.6321 0.6289 0.6539 -0.0024 0.0450  0.0982  124 ASN A C   
855  O O   . ASN A 124 ? 0.6284 0.6260 0.6453 -0.0068 0.0471  0.0971  124 ASN A O   
856  C CB  . ASN A 124 ? 0.6798 0.6565 0.7235 0.0058  0.0500  0.1026  124 ASN A CB  
857  C CG  . ASN A 124 ? 0.7685 0.7302 0.8193 0.0047  0.0551  0.0999  124 ASN A CG  
858  O OD1 . ASN A 124 ? 0.6587 0.6191 0.7086 0.0008  0.0571  0.1043  124 ASN A OD1 
859  N ND2 . ASN A 124 ? 0.7936 0.7443 0.8509 0.0075  0.0572  0.0921  124 ASN A ND2 
860  N N   . PRO B 11  ? 0.5249 0.5786 0.4441 -0.0391 -0.1032 0.0386  11  PRO B N   
861  C CA  . PRO B 11  ? 0.4913 0.5334 0.4242 -0.0348 -0.1017 0.0432  11  PRO B CA  
862  C C   . PRO B 11  ? 0.4659 0.4985 0.4072 -0.0318 -0.0934 0.0341  11  PRO B C   
863  O O   . PRO B 11  ? 0.4681 0.4901 0.4162 -0.0286 -0.0916 0.0370  11  PRO B O   
864  C CB  . PRO B 11  ? 0.5291 0.5732 0.4753 -0.0318 -0.1100 0.0481  11  PRO B CB  
865  C CG  . PRO B 11  ? 0.5514 0.6069 0.4953 -0.0346 -0.1141 0.0426  11  PRO B CG  
866  C CD  . PRO B 11  ? 0.5716 0.6334 0.4950 -0.0398 -0.1125 0.0396  11  PRO B CD  
867  N N   . LEU B 12  ? 0.4278 0.4634 0.3685 -0.0327 -0.0893 0.0235  12  LEU B N   
868  C CA  . LEU B 12  ? 0.4102 0.4383 0.3583 -0.0303 -0.0816 0.0158  12  LEU B CA  
869  C C   . LEU B 12  ? 0.4196 0.4504 0.3582 -0.0332 -0.0759 0.0073  12  LEU B C   
870  O O   . LEU B 12  ? 0.4244 0.4623 0.3570 -0.0361 -0.0790 0.0024  12  LEU B O   
871  C CB  . LEU B 12  ? 0.4186 0.4476 0.3821 -0.0274 -0.0832 0.0125  12  LEU B CB  
872  C CG  . LEU B 12  ? 0.3936 0.4165 0.3657 -0.0249 -0.0754 0.0055  12  LEU B CG  
873  C CD1 . LEU B 12  ? 0.4025 0.4141 0.3742 -0.0216 -0.0703 0.0077  12  LEU B CD1 
874  C CD2 . LEU B 12  ? 0.4504 0.4781 0.4387 -0.0223 -0.0778 0.0049  12  LEU B CD2 
875  N N   . MET B 13  ? 0.3980 0.4228 0.3346 -0.0325 -0.0685 0.0057  13  MET B N   
876  C CA  A MET B 13  ? 0.4157 0.4415 0.3451 -0.0338 -0.0615 -0.0017 13  MET B CA  
877  C CA  B MET B 13  ? 0.3996 0.4254 0.3295 -0.0338 -0.0616 -0.0023 13  MET B CA  
878  C C   . MET B 13  ? 0.3763 0.3939 0.3156 -0.0314 -0.0550 -0.0061 13  MET B C   
879  O O   . MET B 13  ? 0.3669 0.3780 0.3121 -0.0293 -0.0544 -0.0015 13  MET B O   
880  C CB  A MET B 13  ? 0.4605 0.4895 0.3784 -0.0353 -0.0587 0.0041  13  MET B CB  
881  C CB  B MET B 13  ? 0.4188 0.4488 0.3355 -0.0355 -0.0584 0.0017  13  MET B CB  
882  C CG  A MET B 13  ? 0.5342 0.5663 0.4437 -0.0355 -0.0510 -0.0027 13  MET B CG  
883  C CG  B MET B 13  ? 0.4646 0.4975 0.3727 -0.0357 -0.0516 -0.0071 13  MET B CG  
884  S SD  A MET B 13  ? 0.6487 0.6884 0.5472 -0.0367 -0.0466 0.0062  13  MET B SD  
885  S SD  B MET B 13  ? 0.4896 0.5167 0.4036 -0.0333 -0.0413 -0.0096 13  MET B SD  
886  C CE  A MET B 13  ? 0.5809 0.6144 0.4893 -0.0349 -0.0385 0.0064  13  MET B CE  
887  C CE  B MET B 13  ? 0.4597 0.4942 0.3653 -0.0344 -0.0379 0.0008  13  MET B CE  
888  N N   . VAL B 14  ? 0.3585 0.3756 0.2988 -0.0316 -0.0505 -0.0147 14  VAL B N   
889  C CA  . VAL B 14  ? 0.3574 0.3676 0.3067 -0.0295 -0.0442 -0.0177 14  VAL B CA  
890  C C   . VAL B 14  ? 0.3676 0.3781 0.3101 -0.0299 -0.0377 -0.0216 14  VAL B C   
891  O O   . VAL B 14  ? 0.3928 0.4069 0.3279 -0.0311 -0.0374 -0.0275 14  VAL B O   
892  C CB  . VAL B 14  ? 0.3678 0.3770 0.3286 -0.0292 -0.0445 -0.0235 14  VAL B CB  
893  C CG1 . VAL B 14  ? 0.3542 0.3572 0.3228 -0.0273 -0.0376 -0.0256 14  VAL B CG1 
894  C CG2 . VAL B 14  ? 0.3600 0.3712 0.3295 -0.0279 -0.0502 -0.0191 14  VAL B CG2 
895  N N   . LYS B 15  ? 0.3345 0.3414 0.2795 -0.0285 -0.0328 -0.0186 15  LYS B N   
896  C CA  . LYS B 15  ? 0.3497 0.3575 0.2918 -0.0278 -0.0258 -0.0213 15  LYS B CA  
897  C C   . LYS B 15  ? 0.3549 0.3564 0.3070 -0.0261 -0.0212 -0.0229 15  LYS B C   
898  O O   . LYS B 15  ? 0.3202 0.3176 0.2771 -0.0257 -0.0224 -0.0181 15  LYS B O   
899  C CB  . LYS B 15  ? 0.3797 0.3924 0.3152 -0.0285 -0.0246 -0.0134 15  LYS B CB  
900  C CG  . LYS B 15  ? 0.4563 0.4721 0.3914 -0.0270 -0.0167 -0.0140 15  LYS B CG  
901  N N   . VAL B 16  ? 0.3143 0.3144 0.2689 -0.0250 -0.0163 -0.0295 16  VAL B N   
902  C CA  . VAL B 16  ? 0.3071 0.3017 0.2719 -0.0236 -0.0122 -0.0300 16  VAL B CA  
903  C C   . VAL B 16  ? 0.3316 0.3271 0.2963 -0.0215 -0.0053 -0.0310 16  VAL B C   
904  O O   . VAL B 16  ? 0.3233 0.3205 0.2828 -0.0203 -0.0027 -0.0373 16  VAL B O   
905  C CB  . VAL B 16  ? 0.3027 0.2933 0.2755 -0.0241 -0.0131 -0.0365 16  VAL B CB  
906  C CG1 . VAL B 16  ? 0.2864 0.2722 0.2701 -0.0228 -0.0092 -0.0346 16  VAL B CG1 
907  C CG2 . VAL B 16  ? 0.3157 0.3084 0.2895 -0.0258 -0.0196 -0.0360 16  VAL B CG2 
908  N N   . LEU B 17  ? 0.3182 0.3124 0.2891 -0.0206 -0.0027 -0.0253 17  LEU B N   
909  C CA  . LEU B 17  ? 0.3200 0.3165 0.2941 -0.0182 0.0034  -0.0237 17  LEU B CA  
910  C C   . LEU B 17  ? 0.3291 0.3197 0.3139 -0.0169 0.0060  -0.0237 17  LEU B C   
911  O O   . LEU B 17  ? 0.3256 0.3121 0.3140 -0.0182 0.0033  -0.0217 17  LEU B O   
912  C CB  . LEU B 17  ? 0.3364 0.3387 0.3084 -0.0192 0.0030  -0.0144 17  LEU B CB  
913  C CG  . LEU B 17  ? 0.3790 0.3888 0.3414 -0.0207 0.0011  -0.0114 17  LEU B CG  
914  C CD1 . LEU B 17  ? 0.4532 0.4688 0.4175 -0.0224 0.0009  -0.0008 17  LEU B CD1 
915  C CD2 . LEU B 17  ? 0.4143 0.4290 0.3698 -0.0181 0.0058  -0.0184 17  LEU B CD2 
916  N N   . ASP B 18  ? 0.2951 0.2860 0.2850 -0.0139 0.0117  -0.0252 18  ASP B N   
917  C CA  . ASP B 18  ? 0.2896 0.2752 0.2906 -0.0124 0.0145  -0.0247 18  ASP B CA  
918  C C   . ASP B 18  ? 0.2675 0.2579 0.2736 -0.0110 0.0171  -0.0160 18  ASP B C   
919  O O   . ASP B 18  ? 0.3161 0.3122 0.3226 -0.0081 0.0214  -0.0153 18  ASP B O   
920  C CB  . ASP B 18  ? 0.3076 0.2880 0.3116 -0.0099 0.0181  -0.0336 18  ASP B CB  
921  C CG  . ASP B 18  ? 0.3582 0.3329 0.3750 -0.0078 0.0215  -0.0325 18  ASP B CG  
922  O OD1 . ASP B 18  ? 0.3591 0.3361 0.3823 -0.0072 0.0226  -0.0241 18  ASP B OD1 
923  O OD2 . ASP B 18  ? 0.3930 0.3601 0.4134 -0.0067 0.0229  -0.0404 18  ASP B OD2 
924  N N   . ALA B 19  ? 0.2765 0.2656 0.2855 -0.0130 0.0142  -0.0092 19  ALA B N   
925  C CA  . ALA B 19  ? 0.2752 0.2691 0.2886 -0.0130 0.0143  0.0000  19  ALA B CA  
926  C C   . ALA B 19  ? 0.2983 0.2919 0.3240 -0.0095 0.0193  0.0020  19  ALA B C   
927  O O   . ALA B 19  ? 0.3296 0.3290 0.3612 -0.0089 0.0199  0.0100  19  ALA B O   
928  C CB  . ALA B 19  ? 0.2904 0.2808 0.2998 -0.0166 0.0084  0.0053  19  ALA B CB  
929  N N   . VAL B 20  ? 0.2855 0.2724 0.3162 -0.0074 0.0222  -0.0043 20  VAL B N   
930  C CA  . VAL B 20  ? 0.3022 0.2868 0.3455 -0.0037 0.0265  -0.0023 20  VAL B CA  
931  C C   . VAL B 20  ? 0.3412 0.3289 0.3874 0.0016  0.0325  -0.0063 20  VAL B C   
932  O O   . VAL B 20  ? 0.3954 0.3876 0.4511 0.0053  0.0362  -0.0005 20  VAL B O   
933  C CB  . VAL B 20  ? 0.3472 0.3222 0.3957 -0.0044 0.0264  -0.0063 20  VAL B CB  
934  C CG1 . VAL B 20  ? 0.3676 0.3375 0.4298 0.0000  0.0313  -0.0067 20  VAL B CG1 
935  C CG2 . VAL B 20  ? 0.3376 0.3121 0.3842 -0.0082 0.0223  -0.0001 20  VAL B CG2 
936  N N   . ARG B 21  ? 0.3421 0.3279 0.3795 0.0022  0.0336  -0.0159 21  ARG B N   
937  C CA  . ARG B 21  ? 0.3673 0.3549 0.4037 0.0081  0.0401  -0.0221 21  ARG B CA  
938  C C   . ARG B 21  ? 0.3586 0.3588 0.3861 0.0085  0.0416  -0.0191 21  ARG B C   
939  O O   . ARG B 21  ? 0.3426 0.3476 0.3691 0.0143  0.0484  -0.0223 21  ARG B O   
940  C CB  . ARG B 21  ? 0.3953 0.3723 0.4252 0.0083  0.0397  -0.0353 21  ARG B CB  
941  C CG  . ARG B 21  ? 0.4407 0.4046 0.4808 0.0078  0.0387  -0.0389 21  ARG B CG  
942  C CD  . ARG B 21  ? 0.4558 0.4103 0.4885 0.0050  0.0352  -0.0508 21  ARG B CD  
943  N NE  . ARG B 21  ? 0.5275 0.4744 0.5566 0.0101  0.0392  -0.0622 21  ARG B NE  
944  N N   . GLY B 22  ? 0.3114 0.3167 0.3326 0.0029  0.0358  -0.0132 22  GLY B N   
945  C CA  . GLY B 22  ? 0.3237 0.3408 0.3370 0.0018  0.0359  -0.0089 22  GLY B CA  
946  C C   . GLY B 22  ? 0.3473 0.3645 0.3477 0.0037  0.0384  -0.0186 22  GLY B C   
947  O O   . GLY B 22  ? 0.3432 0.3697 0.3400 0.0078  0.0445  -0.0187 22  GLY B O   
948  N N   . SER B 23  ? 0.3399 0.3480 0.3332 0.0006  0.0334  -0.0264 23  SER B N   
949  C CA  . SER B 23  ? 0.3809 0.3875 0.3613 0.0014  0.0338  -0.0363 23  SER B CA  
950  C C   . SER B 23  ? 0.3524 0.3555 0.3252 -0.0045 0.0254  -0.0381 23  SER B C   
951  O O   . SER B 23  ? 0.3400 0.3392 0.3183 -0.0083 0.0202  -0.0339 23  SER B O   
952  C CB  . SER B 23  ? 0.4446 0.4405 0.4273 0.0060  0.0379  -0.0478 23  SER B CB  
953  O OG  . SER B 23  ? 0.5034 0.4884 0.4920 0.0020  0.0322  -0.0506 23  SER B OG  
954  N N   . PRO B 24  ? 0.3751 0.3807 0.3343 -0.0051 0.0240  -0.0437 24  PRO B N   
955  C CA  . PRO B 24  ? 0.3787 0.3797 0.3327 -0.0099 0.0159  -0.0473 24  PRO B CA  
956  C C   . PRO B 24  ? 0.3820 0.3717 0.3452 -0.0108 0.0138  -0.0536 24  PRO B C   
957  O O   . PRO B 24  ? 0.3773 0.3608 0.3450 -0.0075 0.0183  -0.0596 24  PRO B O   
958  C CB  . PRO B 24  ? 0.4285 0.4327 0.3665 -0.0092 0.0158  -0.0547 24  PRO B CB  
959  C CG  . PRO B 24  ? 0.4652 0.4707 0.4008 -0.0027 0.0252  -0.0594 24  PRO B CG  
960  C CD  . PRO B 24  ? 0.4258 0.4380 0.3735 -0.0009 0.0299  -0.0480 24  PRO B CD  
961  N N   . ALA B 25  ? 0.3524 0.3398 0.3188 -0.0151 0.0072  -0.0519 25  ALA B N   
962  C CA  . ALA B 25  ? 0.3514 0.3303 0.3271 -0.0169 0.0047  -0.0565 25  ALA B CA  
963  C C   . ALA B 25  ? 0.3706 0.3475 0.3383 -0.0195 -0.0006 -0.0655 25  ALA B C   
964  O O   . ALA B 25  ? 0.3517 0.3333 0.3146 -0.0226 -0.0066 -0.0635 25  ALA B O   
965  C CB  . ALA B 25  ? 0.3358 0.3154 0.3198 -0.0193 0.0014  -0.0488 25  ALA B CB  
966  N N   . ILE B 26  ? 0.3733 0.3424 0.3399 -0.0183 0.0010  -0.0754 26  ILE B N   
967  C CA  . ILE B 26  ? 0.4175 0.3839 0.3727 -0.0208 -0.0044 -0.0855 26  ILE B CA  
968  C C   . ILE B 26  ? 0.4304 0.3898 0.3969 -0.0260 -0.0111 -0.0889 26  ILE B C   
969  O O   . ILE B 26  ? 0.4129 0.3664 0.3945 -0.0261 -0.0090 -0.0869 26  ILE B O   
970  C CB  . ILE B 26  ? 0.4831 0.4439 0.4266 -0.0163 0.0007  -0.0962 26  ILE B CB  
971  C CG1 . ILE B 26  ? 0.5264 0.4728 0.4801 -0.0148 0.0029  -0.1039 26  ILE B CG1 
972  C CG2 . ILE B 26  ? 0.4675 0.4372 0.4053 -0.0104 0.0094  -0.0905 26  ILE B CG2 
973  C CD1 . ILE B 26  ? 0.6030 0.5408 0.5433 -0.0104 0.0062  -0.1173 26  ILE B CD1 
974  N N   . ASN B 27  ? 0.4389 0.4009 0.3990 -0.0305 -0.0194 -0.0923 27  ASN B N   
975  C CA  . ASN B 27  ? 0.4629 0.4209 0.4339 -0.0364 -0.0270 -0.0949 27  ASN B CA  
976  C C   . ASN B 27  ? 0.4288 0.3910 0.4182 -0.0381 -0.0274 -0.0849 27  ASN B C   
977  O O   . ASN B 27  ? 0.4039 0.3613 0.4077 -0.0415 -0.0298 -0.0855 27  ASN B O   
978  C CB  . ASN B 27  ? 0.4975 0.4414 0.4718 -0.0369 -0.0266 -0.1051 27  ASN B CB  
979  C CG  . ASN B 27  ? 0.6107 0.5498 0.5718 -0.0405 -0.0341 -0.1164 27  ASN B CG  
980  O OD1 . ASN B 27  ? 0.6171 0.5569 0.5582 -0.0373 -0.0324 -0.1227 27  ASN B OD1 
981  N ND2 . ASN B 27  ? 0.6498 0.5866 0.6212 -0.0476 -0.0434 -0.1180 27  ASN B ND2 
982  N N   . VAL B 28  ? 0.4047 0.3755 0.3930 -0.0356 -0.0250 -0.0758 28  VAL B N   
983  C CA  . VAL B 28  ? 0.3988 0.3741 0.4013 -0.0362 -0.0251 -0.0667 28  VAL B CA  
984  C C   . VAL B 28  ? 0.3691 0.3519 0.3738 -0.0398 -0.0334 -0.0649 28  VAL B C   
985  O O   . VAL B 28  ? 0.3262 0.3140 0.3191 -0.0398 -0.0371 -0.0649 28  VAL B O   
986  C CB  . VAL B 28  ? 0.3935 0.3726 0.3930 -0.0320 -0.0200 -0.0586 28  VAL B CB  
987  C CG1 . VAL B 28  ? 0.3669 0.3495 0.3789 -0.0318 -0.0197 -0.0507 28  VAL B CG1 
988  C CG2 . VAL B 28  ? 0.3950 0.3689 0.3933 -0.0285 -0.0125 -0.0590 28  VAL B CG2 
989  N N   . ALA B 29  ? 0.3316 0.3163 0.3528 -0.0429 -0.0361 -0.0623 29  ALA B N   
990  C CA  . ALA B 29  ? 0.3232 0.3170 0.3500 -0.0457 -0.0436 -0.0591 29  ALA B CA  
991  C C   . ALA B 29  ? 0.3090 0.3101 0.3364 -0.0413 -0.0414 -0.0501 29  ALA B C   
992  O O   . ALA B 29  ? 0.3148 0.3144 0.3459 -0.0375 -0.0347 -0.0453 29  ALA B O   
993  C CB  . ALA B 29  ? 0.3401 0.3351 0.3863 -0.0506 -0.0470 -0.0583 29  ALA B CB  
994  N N   . VAL B 30  ? 0.2963 0.3042 0.3180 -0.0416 -0.0476 -0.0482 30  VAL B N   
995  C CA  . VAL B 30  ? 0.2869 0.2999 0.3082 -0.0373 -0.0470 -0.0404 30  VAL B CA  
996  C C   . VAL B 30  ? 0.3032 0.3262 0.3354 -0.0388 -0.0546 -0.0365 30  VAL B C   
997  O O   . VAL B 30  ? 0.3280 0.3546 0.3559 -0.0433 -0.0628 -0.0396 30  VAL B O   
998  C CB  . VAL B 30  ? 0.2858 0.2976 0.2891 -0.0356 -0.0476 -0.0400 30  VAL B CB  
999  C CG1 . VAL B 30  ? 0.3238 0.3384 0.3280 -0.0315 -0.0481 -0.0320 30  VAL B CG1 
1000 C CG2 . VAL B 30  ? 0.3079 0.3122 0.3028 -0.0337 -0.0400 -0.0424 30  VAL B CG2 
1001 N N   . HIS B 31  ? 0.3143 0.3422 0.3599 -0.0351 -0.0519 -0.0298 31  HIS B N   
1002 C CA  . HIS B 31  ? 0.3141 0.3529 0.3718 -0.0345 -0.0576 -0.0242 31  HIS B CA  
1003 C C   . HIS B 31  ? 0.3097 0.3497 0.3652 -0.0278 -0.0563 -0.0180 31  HIS B C   
1004 O O   . HIS B 31  ? 0.3375 0.3712 0.3895 -0.0225 -0.0490 -0.0163 31  HIS B O   
1005 C CB  . HIS B 31  ? 0.3444 0.3897 0.4233 -0.0352 -0.0551 -0.0212 31  HIS B CB  
1006 C CG  . HIS B 31  ? 0.3938 0.4392 0.4793 -0.0432 -0.0598 -0.0260 31  HIS B CG  
1007 N ND1 . HIS B 31  ? 0.4432 0.4790 0.5258 -0.0455 -0.0553 -0.0312 31  HIS B ND1 
1008 C CD2 . HIS B 31  ? 0.4262 0.4794 0.5218 -0.0497 -0.0696 -0.0264 31  HIS B CD2 
1009 C CE1 . HIS B 31  ? 0.4313 0.4670 0.5214 -0.0531 -0.0618 -0.0355 31  HIS B CE1 
1010 N NE2 . HIS B 31  ? 0.4960 0.5424 0.5936 -0.0562 -0.0709 -0.0328 31  HIS B NE2 
1011 N N   . VAL B 32  ? 0.2995 0.3466 0.3563 -0.0278 -0.0641 -0.0144 32  VAL B N   
1012 C CA  . VAL B 32  ? 0.2947 0.3415 0.3500 -0.0213 -0.0642 -0.0083 32  VAL B CA  
1013 C C   . VAL B 32  ? 0.3131 0.3722 0.3886 -0.0183 -0.0671 -0.0019 32  VAL B C   
1014 O O   . VAL B 32  ? 0.3313 0.4008 0.4170 -0.0235 -0.0743 -0.0012 32  VAL B O   
1015 C CB  . VAL B 32  ? 0.3138 0.3588 0.3533 -0.0230 -0.0710 -0.0072 32  VAL B CB  
1016 C CG1 . VAL B 32  ? 0.3066 0.3487 0.3452 -0.0164 -0.0715 -0.0003 32  VAL B CG1 
1017 C CG2 . VAL B 32  ? 0.3221 0.3586 0.3436 -0.0265 -0.0681 -0.0131 32  VAL B CG2 
1018 N N   . PHE B 33  ? 0.2896 0.3472 0.3703 -0.0098 -0.0621 0.0027  33  PHE B N   
1019 C CA  . PHE B 33  ? 0.3143 0.3834 0.4149 -0.0042 -0.0623 0.0093  33  PHE B CA  
1020 C C   . PHE B 33  ? 0.3290 0.3936 0.4267 0.0042  -0.0632 0.0141  33  PHE B C   
1021 O O   . PHE B 33  ? 0.3090 0.3598 0.3907 0.0065  -0.0611 0.0121  33  PHE B O   
1022 C CB  . PHE B 33  ? 0.3248 0.3966 0.4375 0.0001  -0.0520 0.0097  33  PHE B CB  
1023 C CG  . PHE B 33  ? 0.3501 0.4234 0.4659 -0.0074 -0.0498 0.0057  33  PHE B CG  
1024 C CD1 . PHE B 33  ? 0.3961 0.4564 0.4961 -0.0098 -0.0451 -0.0003 33  PHE B CD1 
1025 C CD2 . PHE B 33  ? 0.4123 0.4996 0.5481 -0.0124 -0.0531 0.0086  33  PHE B CD2 
1026 C CE1 . PHE B 33  ? 0.4152 0.4754 0.5190 -0.0161 -0.0431 -0.0037 33  PHE B CE1 
1027 C CE2 . PHE B 33  ? 0.4402 0.5265 0.5794 -0.0198 -0.0519 0.0050  33  PHE B CE2 
1028 C CZ  . PHE B 33  ? 0.4843 0.5564 0.6072 -0.0212 -0.0466 -0.0013 33  PHE B CZ  
1029 N N   . ARG B 34  ? 0.3307 0.4069 0.4454 0.0086  -0.0668 0.0208  34  ARG B N   
1030 C CA  A ARG B 34  ? 0.3454 0.4171 0.4612 0.0180  -0.0672 0.0258  34  ARG B CA  
1031 C CA  B ARG B 34  ? 0.3578 0.4295 0.4735 0.0180  -0.0671 0.0258  34  ARG B CA  
1032 C C   . ARG B 34  ? 0.3552 0.4347 0.4898 0.0277  -0.0592 0.0292  34  ARG B C   
1033 O O   . ARG B 34  ? 0.3822 0.4783 0.5358 0.0256  -0.0586 0.0320  34  ARG B O   
1034 C CB  A ARG B 34  ? 0.3551 0.4344 0.4743 0.0157  -0.0794 0.0323  34  ARG B CB  
1035 C CB  B ARG B 34  ? 0.3856 0.4650 0.5050 0.0156  -0.0793 0.0322  34  ARG B CB  
1036 C CG  A ARG B 34  ? 0.3645 0.4341 0.4794 0.0235  -0.0817 0.0372  34  ARG B CG  
1037 C CG  B ARG B 34  ? 0.4182 0.4988 0.5493 0.0264  -0.0803 0.0398  34  ARG B CG  
1038 C CD  A ARG B 34  ? 0.3931 0.4693 0.5079 0.0196  -0.0946 0.0443  34  ARG B CD  
1039 C CD  B ARG B 34  ? 0.4587 0.5440 0.5899 0.0240  -0.0929 0.0471  34  ARG B CD  
1040 N NE  A ARG B 34  ? 0.4160 0.4836 0.5321 0.0284  -0.0967 0.0507  34  ARG B NE  
1041 N NE  B ARG B 34  ? 0.4683 0.5688 0.6034 0.0136  -0.1025 0.0484  34  ARG B NE  
1042 C CZ  A ARG B 34  ? 0.4426 0.5128 0.5763 0.0396  -0.0934 0.0552  34  ARG B CZ  
1043 C CZ  B ARG B 34  ? 0.4975 0.5977 0.6184 0.0061  -0.1124 0.0496  34  ARG B CZ  
1044 N NH1 A ARG B 34  ? 0.4732 0.5572 0.6254 0.0430  -0.0876 0.0550  34  ARG B NH1 
1045 N NH1 B ARG B 34  ? 0.4963 0.5826 0.5999 0.0075  -0.1132 0.0507  34  ARG B NH1 
1046 N NH2 A ARG B 34  ? 0.4735 0.5331 0.6074 0.0477  -0.0956 0.0603  34  ARG B NH2 
1047 N NH2 B ARG B 34  ? 0.4869 0.6000 0.6097 -0.0030 -0.1214 0.0497  34  ARG B NH2 
1048 N N   . LYS B 35  ? 0.3705 0.4386 0.5004 0.0381  -0.0531 0.0290  35  LYS B N   
1049 C CA  . LYS B 35  ? 0.4021 0.4769 0.5478 0.0495  -0.0439 0.0317  35  LYS B CA  
1050 C C   . LYS B 35  ? 0.3987 0.4885 0.5655 0.0541  -0.0501 0.0406  35  LYS B C   
1051 O O   . LYS B 35  ? 0.3919 0.4755 0.5545 0.0556  -0.0582 0.0437  35  LYS B O   
1052 C CB  . LYS B 35  ? 0.4155 0.4706 0.5464 0.0598  -0.0362 0.0272  35  LYS B CB  
1053 C CG  . LYS B 35  ? 0.4620 0.5219 0.6027 0.0718  -0.0234 0.0273  35  LYS B CG  
1054 C CD  . LYS B 35  ? 0.4965 0.5363 0.6156 0.0768  -0.0150 0.0194  35  LYS B CD  
1055 N N   . ALA B 36  ? 0.4236 0.5342 0.6144 0.0556  -0.0471 0.0458  36  ALA B N   
1056 C CA  . ALA B 36  ? 0.4689 0.5967 0.6838 0.0611  -0.0521 0.0555  36  ALA B CA  
1057 C C   . ALA B 36  ? 0.5062 0.6319 0.7298 0.0783  -0.0422 0.0580  36  ALA B C   
1058 O O   . ALA B 36  ? 0.4991 0.6125 0.7110 0.0853  -0.0308 0.0518  36  ALA B O   
1059 C CB  . ALA B 36  ? 0.4502 0.6031 0.6894 0.0539  -0.0546 0.0612  36  ALA B CB  
1060 N N   . ALA B 37  ? 0.5080 0.6456 0.7517 0.0853  -0.0470 0.0669  37  ALA B N   
1061 C CA  . ALA B 37  ? 0.5732 0.7089 0.8270 0.1034  -0.0382 0.0696  37  ALA B CA  
1062 C C   . ALA B 37  ? 0.5866 0.7319 0.8500 0.1122  -0.0217 0.0683  37  ALA B C   
1063 O O   . ALA B 37  ? 0.6478 0.7808 0.9038 0.1263  -0.0108 0.0641  37  ALA B O   
1064 C CB  . ALA B 37  ? 0.5496 0.7022 0.8293 0.1085  -0.0466 0.0816  37  ALA B CB  
1065 N N   . ASP B 38  ? 0.5643 0.7304 0.8424 0.1033  -0.0205 0.0718  38  ASP B N   
1066 C CA  . ASP B 38  ? 0.5687 0.7461 0.8551 0.1077  -0.0057 0.0718  38  ASP B CA  
1067 C C   . ASP B 38  ? 0.5687 0.7263 0.8267 0.1054  0.0030  0.0608  38  ASP B C   
1068 O O   . ASP B 38  ? 0.5588 0.7257 0.8214 0.1074  0.0146  0.0613  38  ASP B O   
1069 C CB  . ASP B 38  ? 0.5614 0.7663 0.8733 0.0958  -0.0099 0.0800  38  ASP B CB  
1070 C CG  . ASP B 38  ? 0.5967 0.8282 0.9392 0.1058  0.0013  0.0899  38  ASP B CG  
1071 N N   . THR B 40  ? 0.4634 0.6038 0.6877 0.0736  -0.0058 0.0485  40  THR B N   
1072 C CA  . THR B 40  ? 0.4473 0.5930 0.6728 0.0586  -0.0098 0.0476  40  THR B CA  
1073 C C   . THR B 40  ? 0.4393 0.5697 0.6453 0.0477  -0.0223 0.0414  40  THR B C   
1074 O O   . THR B 40  ? 0.4182 0.5417 0.6181 0.0500  -0.0298 0.0417  40  THR B O   
1075 C CB  . THR B 40  ? 0.4407 0.6136 0.6982 0.0532  -0.0144 0.0574  40  THR B CB  
1076 N N   . TRP B 41  ? 0.4456 0.5716 0.6430 0.0363  -0.0239 0.0368  41  TRP B N   
1077 C CA  . TRP B 41  ? 0.4432 0.5562 0.6218 0.0263  -0.0337 0.0307  41  TRP B CA  
1078 C C   . TRP B 41  ? 0.4813 0.6069 0.6724 0.0154  -0.0453 0.0333  41  TRP B C   
1079 O O   . TRP B 41  ? 0.5489 0.6861 0.7555 0.0091  -0.0449 0.0354  41  TRP B O   
1080 C CB  . TRP B 41  ? 0.4500 0.5495 0.6112 0.0212  -0.0282 0.0235  41  TRP B CB  
1081 C CG  . TRP B 41  ? 0.4614 0.5452 0.6046 0.0298  -0.0196 0.0195  41  TRP B CG  
1082 C CD1 . TRP B 41  ? 0.4999 0.5819 0.6410 0.0355  -0.0079 0.0190  41  TRP B CD1 
1083 C CD2 . TRP B 41  ? 0.4570 0.5234 0.5803 0.0332  -0.0228 0.0158  41  TRP B CD2 
1084 N NE1 . TRP B 41  ? 0.4820 0.5466 0.6029 0.0420  -0.0043 0.0143  41  TRP B NE1 
1085 C CE2 . TRP B 41  ? 0.4658 0.5200 0.5762 0.0407  -0.0131 0.0124  41  TRP B CE2 
1086 C CE3 . TRP B 41  ? 0.4516 0.5119 0.5668 0.0304  -0.0326 0.0156  41  TRP B CE3 
1087 C CZ2 . TRP B 41  ? 0.4835 0.5191 0.5747 0.0446  -0.0143 0.0085  41  TRP B CZ2 
1088 C CZ3 . TRP B 41  ? 0.4359 0.4786 0.5331 0.0347  -0.0330 0.0130  41  TRP B CZ3 
1089 C CH2 . TRP B 41  ? 0.4723 0.5023 0.5583 0.0413  -0.0244 0.0092  41  TRP B CH2 
1090 N N   . GLU B 42  ? 0.4666 0.5904 0.6516 0.0128  -0.0563 0.0337  42  GLU B N   
1091 C CA  . GLU B 42  ? 0.4716 0.6065 0.6650 0.0024  -0.0691 0.0356  42  GLU B CA  
1092 C C   . GLU B 42  ? 0.4816 0.6020 0.6505 -0.0069 -0.0744 0.0267  42  GLU B C   
1093 O O   . GLU B 42  ? 0.4400 0.5467 0.5887 -0.0043 -0.0743 0.0236  42  GLU B O   
1094 C CB  . GLU B 42  ? 0.4529 0.5976 0.6560 0.0061  -0.0784 0.0433  42  GLU B CB  
1095 N N   . PRO B 43  ? 0.5148 0.6377 0.6859 -0.0175 -0.0786 0.0227  43  PRO B N   
1096 C CA  . PRO B 43  ? 0.4770 0.5882 0.6261 -0.0260 -0.0847 0.0142  43  PRO B CA  
1097 C C   . PRO B 43  ? 0.4509 0.5624 0.5880 -0.0277 -0.0954 0.0152  43  PRO B C   
1098 O O   . PRO B 43  ? 0.4732 0.5981 0.6238 -0.0281 -0.1040 0.0221  43  PRO B O   
1099 C CB  . PRO B 43  ? 0.5356 0.6532 0.6961 -0.0365 -0.0902 0.0117  43  PRO B CB  
1100 C CG  . PRO B 43  ? 0.4954 0.6285 0.6849 -0.0341 -0.0860 0.0200  43  PRO B CG  
1101 C CD  . PRO B 43  ? 0.5299 0.6629 0.7215 -0.0211 -0.0749 0.0249  43  PRO B CD  
1102 N N   . PHE B 44  ? 0.4180 0.5159 0.5304 -0.0289 -0.0950 0.0092  44  PHE B N   
1103 C CA  . PHE B 44  ? 0.4687 0.5644 0.5658 -0.0287 -0.1021 0.0113  44  PHE B CA  
1104 C C   . PHE B 44  ? 0.4536 0.5430 0.5291 -0.0371 -0.1070 0.0031  44  PHE B C   
1105 O O   . PHE B 44  ? 0.4651 0.5601 0.5332 -0.0419 -0.1177 0.0041  44  PHE B O   
1106 C CB  . PHE B 44  ? 0.4512 0.5360 0.5392 -0.0198 -0.0946 0.0138  44  PHE B CB  
1107 C CG  . PHE B 44  ? 0.5051 0.5865 0.5775 -0.0199 -0.1013 0.0171  44  PHE B CG  
1108 C CD1 . PHE B 44  ? 0.5054 0.5963 0.5865 -0.0178 -0.1100 0.0259  44  PHE B CD1 
1109 C CD2 . PHE B 44  ? 0.4732 0.5430 0.5237 -0.0218 -0.0985 0.0129  44  PHE B CD2 
1110 C CE1 . PHE B 44  ? 0.5142 0.6018 0.5810 -0.0181 -0.1161 0.0305  44  PHE B CE1 
1111 C CE2 . PHE B 44  ? 0.4920 0.5599 0.5288 -0.0224 -0.1042 0.0174  44  PHE B CE2 
1112 C CZ  . PHE B 44  ? 0.5040 0.5805 0.5486 -0.0207 -0.1131 0.0263  44  PHE B CZ  
1113 N N   . ALA B 45  ? 0.4031 0.4814 0.4683 -0.0385 -0.0993 -0.0048 45  ALA B N   
1114 C CA  . ALA B 45  ? 0.4147 0.4860 0.4590 -0.0445 -0.1016 -0.0132 45  ALA B CA  
1115 C C   . ALA B 45  ? 0.3972 0.4588 0.4403 -0.0455 -0.0928 -0.0210 45  ALA B C   
1116 O O   . ALA B 45  ? 0.3900 0.4492 0.4444 -0.0408 -0.0839 -0.0187 45  ALA B O   
1117 C CB  . ALA B 45  ? 0.3850 0.4509 0.4087 -0.0419 -0.1008 -0.0116 45  ALA B CB  
1118 N N   . SER B 46  ? 0.3702 0.4260 0.3993 -0.0511 -0.0949 -0.0299 46  SER B N   
1119 C CA  . SER B 46  ? 0.3571 0.4021 0.3831 -0.0513 -0.0864 -0.0372 46  SER B CA  
1120 C C   . SER B 46  ? 0.3923 0.4298 0.3974 -0.0548 -0.0878 -0.0469 46  SER B C   
1121 O O   . SER B 46  ? 0.3879 0.4292 0.3814 -0.0586 -0.0967 -0.0491 46  SER B O   
1122 C CB  . SER B 46  ? 0.3314 0.3782 0.3785 -0.0544 -0.0861 -0.0377 46  SER B CB  
1123 O OG  . SER B 46  ? 0.3166 0.3674 0.3674 -0.0623 -0.0970 -0.0416 46  SER B OG  
1124 N N   . GLY B 47  ? 0.3809 0.4082 0.3816 -0.0534 -0.0793 -0.0526 47  GLY B N   
1125 C CA  . GLY B 47  ? 0.4003 0.4194 0.3832 -0.0555 -0.0788 -0.0629 47  GLY B CA  
1126 C C   . GLY B 47  ? 0.4157 0.4246 0.3992 -0.0521 -0.0680 -0.0665 47  GLY B C   
1127 O O   . GLY B 47  ? 0.3836 0.3917 0.3823 -0.0498 -0.0622 -0.0615 47  GLY B O   
1128 N N   . LYS B 48  ? 0.4126 0.4141 0.3799 -0.0519 -0.0654 -0.0754 48  LYS B N   
1129 C CA  . LYS B 48  ? 0.4216 0.4140 0.3893 -0.0482 -0.0554 -0.0785 48  LYS B CA  
1130 C C   . LYS B 48  ? 0.3939 0.3874 0.3436 -0.0435 -0.0493 -0.0781 48  LYS B C   
1131 O O   . LYS B 48  ? 0.4086 0.4053 0.3408 -0.0443 -0.0528 -0.0814 48  LYS B O   
1132 C CB  . LYS B 48  ? 0.4706 0.4519 0.4396 -0.0513 -0.0567 -0.0897 48  LYS B CB  
1133 C CG  . LYS B 48  ? 0.4624 0.4414 0.4545 -0.0549 -0.0584 -0.0872 48  LYS B CG  
1134 C CD  . LYS B 48  ? 0.5089 0.4779 0.5033 -0.0607 -0.0648 -0.0976 48  LYS B CD  
1135 C CE  . LYS B 48  ? 0.4909 0.4559 0.5089 -0.0631 -0.0630 -0.0938 48  LYS B CE  
1136 N NZ  . LYS B 48  ? 0.4885 0.4526 0.5113 -0.0566 -0.0513 -0.0873 48  LYS B NZ  
1137 N N   . THR B 49  ? 0.3664 0.3574 0.3200 -0.0391 -0.0403 -0.0741 49  THR B N   
1138 C CA  . THR B 49  ? 0.3421 0.3355 0.2816 -0.0351 -0.0342 -0.0723 49  THR B CA  
1139 C C   . THR B 49  ? 0.3872 0.3759 0.3120 -0.0338 -0.0314 -0.0833 49  THR B C   
1140 O O   . THR B 49  ? 0.3675 0.3467 0.2962 -0.0343 -0.0309 -0.0920 49  THR B O   
1141 C CB  . THR B 49  ? 0.3436 0.3357 0.2913 -0.0312 -0.0259 -0.0657 49  THR B CB  
1142 O OG1 . THR B 49  ? 0.3366 0.3201 0.2946 -0.0303 -0.0217 -0.0706 49  THR B OG1 
1143 C CG2 . THR B 49  ? 0.3224 0.3184 0.2793 -0.0314 -0.0281 -0.0556 49  THR B CG2 
1144 N N   . SER B 50  ? 0.4006 0.3959 0.3080 -0.0320 -0.0299 -0.0825 50  SER B N   
1145 C CA  . SER B 50  ? 0.4846 0.4776 0.3748 -0.0290 -0.0254 -0.0920 50  SER B CA  
1146 C C   . SER B 50  ? 0.4693 0.4585 0.3636 -0.0229 -0.0140 -0.0928 50  SER B C   
1147 O O   . SER B 50  ? 0.3998 0.3875 0.3107 -0.0220 -0.0106 -0.0860 50  SER B O   
1148 C CB  . SER B 50  ? 0.5065 0.5109 0.3782 -0.0286 -0.0261 -0.0876 50  SER B CB  
1149 O OG  . SER B 50  ? 0.4698 0.4813 0.3462 -0.0255 -0.0192 -0.0763 50  SER B OG  
1150 N N   . GLU B 51  ? 0.4961 0.4832 0.3753 -0.0186 -0.0084 -0.1019 51  GLU B N   
1151 C CA  . GLU B 51  ? 0.5212 0.5073 0.4028 -0.0114 0.0035  -0.1023 51  GLU B CA  
1152 C C   . GLU B 51  ? 0.4994 0.4979 0.3874 -0.0096 0.0088  -0.0877 51  GLU B C   
1153 O O   . GLU B 51  ? 0.4964 0.4951 0.3947 -0.0052 0.0166  -0.0841 51  GLU B O   
1154 C CB  . GLU B 51  ? 0.5293 0.5142 0.3899 -0.0060 0.0091  -0.1138 51  GLU B CB  
1155 N N   . SER B 52  ? 0.5165 0.5251 0.3995 -0.0133 0.0038  -0.0786 52  SER B N   
1156 C CA  . SER B 52  ? 0.4775 0.4964 0.3662 -0.0130 0.0068  -0.0647 52  SER B CA  
1157 C C   . SER B 52  ? 0.4404 0.4560 0.3455 -0.0168 0.0014  -0.0565 52  SER B C   
1158 O O   . SER B 52  ? 0.3934 0.4152 0.3029 -0.0178 0.0016  -0.0452 52  SER B O   
1159 C CB  . SER B 52  ? 0.5295 0.5603 0.4022 -0.0149 0.0043  -0.0589 52  SER B CB  
1160 O OG  . SER B 52  ? 0.5572 0.5870 0.4279 -0.0204 -0.0066 -0.0577 52  SER B OG  
1161 N N   . GLY B 53  ? 0.3923 0.3983 0.3061 -0.0190 -0.0033 -0.0622 53  GLY B N   
1162 C CA  . GLY B 53  ? 0.3885 0.3915 0.3168 -0.0216 -0.0073 -0.0558 53  GLY B CA  
1163 C C   . GLY B 53  ? 0.3608 0.3686 0.2864 -0.0252 -0.0153 -0.0494 53  GLY B C   
1164 O O   . GLY B 53  ? 0.3729 0.3796 0.3079 -0.0260 -0.0173 -0.0425 53  GLY B O   
1165 N N   . GLU B 54  ? 0.3706 0.3833 0.2831 -0.0269 -0.0197 -0.0517 54  GLU B N   
1166 C CA  . GLU B 54  ? 0.3770 0.3953 0.2865 -0.0298 -0.0273 -0.0445 54  GLU B CA  
1167 C C   . GLU B 54  ? 0.3891 0.4060 0.2989 -0.0329 -0.0356 -0.0503 54  GLU B C   
1168 O O   . GLU B 54  ? 0.3864 0.4002 0.2900 -0.0337 -0.0364 -0.0606 54  GLU B O   
1169 C CB  . GLU B 54  ? 0.4181 0.4460 0.3123 -0.0298 -0.0268 -0.0393 54  GLU B CB  
1170 C CG  . GLU B 54  ? 0.4196 0.4522 0.3146 -0.0279 -0.0200 -0.0305 54  GLU B CG  
1171 C CD  . GLU B 54  ? 0.4779 0.5219 0.3581 -0.0284 -0.0195 -0.0245 54  GLU B CD  
1172 O OE1 . GLU B 54  ? 0.4986 0.5464 0.3640 -0.0274 -0.0181 -0.0316 54  GLU B OE1 
1173 O OE2 . GLU B 54  ? 0.4891 0.5380 0.3715 -0.0301 -0.0209 -0.0123 54  GLU B OE2 
1174 N N   . LEU B 55  ? 0.3820 0.4011 0.2988 -0.0346 -0.0422 -0.0437 55  LEU B N   
1175 C CA  . LEU B 55  ? 0.4141 0.4354 0.3323 -0.0379 -0.0512 -0.0461 55  LEU B CA  
1176 C C   . LEU B 55  ? 0.4392 0.4684 0.3519 -0.0389 -0.0578 -0.0367 55  LEU B C   
1177 O O   . LEU B 55  ? 0.4481 0.4772 0.3689 -0.0374 -0.0582 -0.0277 55  LEU B O   
1178 C CB  . LEU B 55  ? 0.4099 0.4271 0.3469 -0.0382 -0.0525 -0.0465 55  LEU B CB  
1179 C CG  . LEU B 55  ? 0.3940 0.4150 0.3381 -0.0416 -0.0617 -0.0475 55  LEU B CG  
1180 C CD1 . LEU B 55  ? 0.4557 0.4760 0.3897 -0.0459 -0.0668 -0.0579 55  LEU B CD1 
1181 C CD2 . LEU B 55  ? 0.4221 0.4400 0.3862 -0.0408 -0.0596 -0.0465 55  LEU B CD2 
1182 N N   . HIS B 56  ? 0.4561 0.4909 0.3539 -0.0413 -0.0627 -0.0392 56  HIS B N   
1183 C CA  . HIS B 56  ? 0.5285 0.5719 0.4187 -0.0429 -0.0700 -0.0301 56  HIS B CA  
1184 C C   . HIS B 56  ? 0.5293 0.5763 0.4231 -0.0464 -0.0808 -0.0317 56  HIS B C   
1185 O O   . HIS B 56  ? 0.5083 0.5519 0.4074 -0.0484 -0.0830 -0.0408 56  HIS B O   
1186 C CB  . HIS B 56  ? 0.5500 0.5997 0.4178 -0.0434 -0.0678 -0.0305 56  HIS B CB  
1187 C CG  . HIS B 56  ? 0.6083 0.6579 0.4726 -0.0403 -0.0574 -0.0271 56  HIS B CG  
1188 N ND1 . HIS B 56  ? 0.6385 0.6910 0.5068 -0.0398 -0.0563 -0.0145 56  HIS B ND1 
1189 C CD2 . HIS B 56  ? 0.6572 0.7043 0.5157 -0.0375 -0.0476 -0.0346 56  HIS B CD2 
1190 C CE1 . HIS B 56  ? 0.6152 0.6681 0.4814 -0.0375 -0.0469 -0.0135 56  HIS B CE1 
1191 N NE2 . HIS B 56  ? 0.6555 0.7058 0.5162 -0.0356 -0.0411 -0.0256 56  HIS B NE2 
1192 N N   . GLY B 57  ? 0.5656 0.6201 0.4576 -0.0475 -0.0886 -0.0223 57  GLY B N   
1193 C CA  . GLY B 57  ? 0.5598 0.6205 0.4532 -0.0513 -0.1002 -0.0226 57  GLY B CA  
1194 C C   . GLY B 57  ? 0.5430 0.6028 0.4601 -0.0511 -0.1039 -0.0218 57  GLY B C   
1195 O O   . GLY B 57  ? 0.5668 0.6318 0.4884 -0.0548 -0.1130 -0.0235 57  GLY B O   
1196 N N   . LEU B 58  ? 0.5045 0.5588 0.4369 -0.0468 -0.0971 -0.0185 58  LEU B N   
1197 C CA  . LEU B 58  ? 0.5063 0.5613 0.4609 -0.0456 -0.0992 -0.0168 58  LEU B CA  
1198 C C   . LEU B 58  ? 0.5384 0.6028 0.5023 -0.0454 -0.1092 -0.0073 58  LEU B C   
1199 O O   . LEU B 58  ? 0.5092 0.5797 0.4877 -0.0473 -0.1150 -0.0076 58  LEU B O   
1200 C CB  . LEU B 58  ? 0.4697 0.5169 0.4358 -0.0404 -0.0896 -0.0153 58  LEU B CB  
1201 C CG  . LEU B 58  ? 0.4589 0.4983 0.4232 -0.0406 -0.0808 -0.0242 58  LEU B CG  
1202 C CD1 . LEU B 58  ? 0.4789 0.5110 0.4471 -0.0359 -0.0722 -0.0208 58  LEU B CD1 
1203 C CD2 . LEU B 58  ? 0.4379 0.4780 0.4166 -0.0431 -0.0822 -0.0297 58  LEU B CD2 
1204 N N   . THR B 59  ? 0.5125 0.5789 0.4689 -0.0436 -0.1117 0.0018  59  THR B N   
1205 C CA  . THR B 59  ? 0.5436 0.6177 0.5100 -0.0423 -0.1207 0.0122  59  THR B CA  
1206 C C   . THR B 59  ? 0.5548 0.6326 0.5053 -0.0436 -0.1258 0.0206  59  THR B C   
1207 O O   . THR B 59  ? 0.5639 0.6391 0.4959 -0.0453 -0.1215 0.0183  59  THR B O   
1208 C CB  . THR B 59  ? 0.5501 0.6193 0.5361 -0.0351 -0.1161 0.0178  59  THR B CB  
1209 O OG1 . THR B 59  ? 0.5691 0.6460 0.5683 -0.0325 -0.1244 0.0277  59  THR B OG1 
1210 C CG2 . THR B 59  ? 0.5391 0.5972 0.5175 -0.0315 -0.1087 0.0205  59  THR B CG2 
1211 N N   . THR B 60  ? 0.5985 0.6837 0.5571 -0.0426 -0.1351 0.0309  60  THR B N   
1212 C CA  . THR B 60  ? 0.5738 0.6637 0.5195 -0.0440 -0.1414 0.0412  60  THR B CA  
1213 C C   . THR B 60  ? 0.5378 0.6224 0.4971 -0.0379 -0.1414 0.0527  60  THR B C   
1214 O O   . THR B 60  ? 0.4619 0.5420 0.4409 -0.0324 -0.1386 0.0525  60  THR B O   
1215 C CB  . THR B 60  ? 0.6238 0.7274 0.5670 -0.0486 -0.1548 0.0452  60  THR B CB  
1216 O OG1 . THR B 60  ? 0.5784 0.6870 0.5468 -0.0455 -0.1604 0.0501  60  THR B OG1 
1217 C CG2 . THR B 60  ? 0.6562 0.7636 0.5829 -0.0554 -0.1568 0.0324  60  THR B CG2 
1218 N N   . GLU B 61  ? 0.5518 0.6369 0.5001 -0.0389 -0.1446 0.0629  61  GLU B N   
1219 C CA  . GLU B 61  ? 0.5983 0.6766 0.5571 -0.0339 -0.1463 0.0749  61  GLU B CA  
1220 C C   . GLU B 61  ? 0.6037 0.6861 0.5844 -0.0289 -0.1536 0.0810  61  GLU B C   
1221 O O   . GLU B 61  ? 0.5929 0.6656 0.5891 -0.0218 -0.1508 0.0840  61  GLU B O   
1222 C CB  . GLU B 61  ? 0.6295 0.7117 0.5728 -0.0376 -0.1514 0.0868  61  GLU B CB  
1223 N N   . GLU B 62  ? 0.5889 0.6859 0.5708 -0.0325 -0.1630 0.0825  62  GLU B N   
1224 C CA  . GLU B 62  ? 0.6195 0.7245 0.6232 -0.0283 -0.1713 0.0903  62  GLU B CA  
1225 C C   . GLU B 62  ? 0.5755 0.6782 0.6003 -0.0229 -0.1646 0.0825  62  GLU B C   
1226 O O   . GLU B 62  ? 0.5779 0.6790 0.6234 -0.0148 -0.1646 0.0887  62  GLU B O   
1227 C CB  . GLU B 62  ? 0.6277 0.7502 0.6263 -0.0350 -0.1844 0.0943  62  GLU B CB  
1228 C CG  . GLU B 62  ? 0.6716 0.7995 0.6508 -0.0395 -0.1924 0.1050  62  GLU B CG  
1229 C CD  . GLU B 62  ? 0.7175 0.8632 0.6933 -0.0454 -0.2069 0.1099  62  GLU B CD  
1230 O OE1 . GLU B 62  ? 0.7250 0.8777 0.6927 -0.0473 -0.2160 0.1230  62  GLU B OE1 
1231 O OE2 . GLU B 62  ? 0.7476 0.9005 0.7289 -0.0487 -0.2101 0.1012  62  GLU B OE2 
1232 N N   . GLU B 63  ? 0.5305 0.6319 0.5499 -0.0265 -0.1578 0.0695  63  GLU B N   
1233 C CA  . GLU B 63  ? 0.5128 0.6148 0.5521 -0.0227 -0.1519 0.0630  63  GLU B CA  
1234 C C   . GLU B 63  ? 0.4831 0.5698 0.5278 -0.0148 -0.1396 0.0599  63  GLU B C   
1235 O O   . GLU B 63  ? 0.4612 0.5485 0.5245 -0.0087 -0.1348 0.0587  63  GLU B O   
1237 N N   . PHE B 64  ? 0.4639 0.5382 0.4917 -0.0155 -0.1349 0.0587  64  PHE B N   
1238 C CA  . PHE B 64  ? 0.4351 0.4940 0.4627 -0.0104 -0.1243 0.0542  64  PHE B CA  
1239 C C   . PHE B 64  ? 0.4301 0.4790 0.4660 -0.0023 -0.1250 0.0625  64  PHE B C   
1240 O O   . PHE B 64  ? 0.4781 0.5150 0.5035 -0.0024 -0.1244 0.0657  64  PHE B O   
1241 C CB  . PHE B 64  ? 0.4260 0.4777 0.4325 -0.0160 -0.1195 0.0490  64  PHE B CB  
1242 C CG  . PHE B 64  ? 0.4317 0.4697 0.4368 -0.0128 -0.1091 0.0428  64  PHE B CG  
1243 C CD1 . PHE B 64  ? 0.4119 0.4490 0.4276 -0.0096 -0.1022 0.0353  64  PHE B CD1 
1244 C CD2 . PHE B 64  ? 0.4569 0.4841 0.4495 -0.0141 -0.1065 0.0448  64  PHE B CD2 
1245 C CE1 . PHE B 64  ? 0.4484 0.4732 0.4608 -0.0071 -0.0932 0.0301  64  PHE B CE1 
1246 C CE2 . PHE B 64  ? 0.4369 0.4519 0.4275 -0.0120 -0.0982 0.0393  64  PHE B CE2 
1247 C CZ  . PHE B 64  ? 0.4313 0.4450 0.4310 -0.0084 -0.0917 0.0317  64  PHE B CZ  
1248 N N   . VAL B 65  ? 0.4001 0.4532 0.4559 0.0051  -0.1258 0.0655  65  VAL B N   
1249 C CA  . VAL B 65  ? 0.4164 0.4601 0.4824 0.0144  -0.1269 0.0729  65  VAL B CA  
1250 C C   . VAL B 65  ? 0.4009 0.4279 0.4667 0.0213  -0.1160 0.0654  65  VAL B C   
1251 O O   . VAL B 65  ? 0.4125 0.4395 0.4750 0.0195  -0.1080 0.0561  65  VAL B O   
1252 C CB  . VAL B 65  ? 0.4069 0.4642 0.4963 0.0208  -0.1318 0.0798  65  VAL B CB  
1253 C CG1 . VAL B 65  ? 0.4308 0.5056 0.5208 0.0137  -0.1442 0.0877  65  VAL B CG1 
1254 C CG2 . VAL B 65  ? 0.4080 0.4736 0.5119 0.0242  -0.1240 0.0727  65  VAL B CG2 
1255 N N   . GLU B 66  ? 0.4111 0.4231 0.4802 0.0292  -0.1162 0.0696  66  GLU B N   
1256 C CA  . GLU B 66  ? 0.4366 0.4311 0.5049 0.0372  -0.1069 0.0624  66  GLU B CA  
1257 C C   . GLU B 66  ? 0.4144 0.4188 0.4953 0.0426  -0.0986 0.0561  66  GLU B C   
1258 O O   . GLU B 66  ? 0.4430 0.4631 0.5413 0.0460  -0.1008 0.0606  66  GLU B O   
1259 C CB  . GLU B 66  ? 0.4942 0.4735 0.5695 0.0473  -0.1097 0.0681  66  GLU B CB  
1260 C CG  . GLU B 66  ? 0.5279 0.4921 0.5908 0.0425  -0.1169 0.0744  66  GLU B CG  
1261 C CD  . GLU B 66  ? 0.5930 0.5364 0.6619 0.0528  -0.1192 0.0781  66  GLU B CD  
1262 O OE1 . GLU B 66  ? 0.5678 0.5154 0.6508 0.0585  -0.1255 0.0875  66  GLU B OE1 
1263 O OE2 . GLU B 66  ? 0.6577 0.5798 0.7167 0.0549  -0.1152 0.0716  66  GLU B OE2 
1264 N N   . GLY B 67  ? 0.4031 0.3991 0.4764 0.0435  -0.0891 0.0468  67  GLY B N   
1265 C CA  . GLY B 67  ? 0.3938 0.3989 0.4781 0.0483  -0.0803 0.0417  67  GLY B CA  
1266 C C   . GLY B 67  ? 0.3700 0.3658 0.4404 0.0456  -0.0718 0.0324  67  GLY B C   
1267 O O   . GLY B 67  ? 0.3593 0.3422 0.4132 0.0402  -0.0733 0.0302  67  GLY B O   
1268 N N   . ILE B 68  ? 0.3574 0.3613 0.4357 0.0486  -0.0632 0.0281  68  ILE B N   
1269 C CA  . ILE B 68  ? 0.3520 0.3490 0.4183 0.0459  -0.0552 0.0202  68  ILE B CA  
1270 C C   . ILE B 68  ? 0.3451 0.3572 0.4147 0.0363  -0.0553 0.0189  68  ILE B C   
1271 O O   . ILE B 68  ? 0.3566 0.3858 0.4431 0.0362  -0.0561 0.0220  68  ILE B O   
1272 C CB  . ILE B 68  ? 0.3762 0.3699 0.4466 0.0565  -0.0444 0.0164  68  ILE B CB  
1273 C CG1 . ILE B 68  ? 0.4282 0.4038 0.4938 0.0670  -0.0446 0.0162  68  ILE B CG1 
1274 C CG2 . ILE B 68  ? 0.3559 0.3444 0.4136 0.0521  -0.0373 0.0095  68  ILE B CG2 
1275 C CD1 . ILE B 68  ? 0.4621 0.4322 0.5283 0.0793  -0.0338 0.0115  68  ILE B CD1 
1276 N N   . TYR B 69  ? 0.3147 0.3204 0.3691 0.0282  -0.0553 0.0147  69  TYR B N   
1277 C CA  . TYR B 69  ? 0.3000 0.3161 0.3546 0.0190  -0.0559 0.0122  69  TYR B CA  
1278 C C   . TYR B 69  ? 0.2879 0.2987 0.3356 0.0173  -0.0476 0.0061  69  TYR B C   
1279 O O   . TYR B 69  ? 0.3053 0.3025 0.3419 0.0203  -0.0437 0.0037  69  TYR B O   
1280 C CB  . TYR B 69  ? 0.3368 0.3520 0.3795 0.0108  -0.0639 0.0134  69  TYR B CB  
1281 C CG  . TYR B 69  ? 0.3093 0.3324 0.3577 0.0104  -0.0733 0.0201  69  TYR B CG  
1282 C CD1 . TYR B 69  ? 0.3645 0.3793 0.4118 0.0158  -0.0772 0.0258  69  TYR B CD1 
1283 C CD2 . TYR B 69  ? 0.3334 0.3721 0.3893 0.0047  -0.0793 0.0213  69  TYR B CD2 
1284 C CE1 . TYR B 69  ? 0.3491 0.3717 0.4026 0.0156  -0.0863 0.0335  69  TYR B CE1 
1285 C CE2 . TYR B 69  ? 0.3441 0.3907 0.4045 0.0042  -0.0889 0.0284  69  TYR B CE2 
1286 C CZ  . TYR B 69  ? 0.3439 0.3831 0.4036 0.0098  -0.0923 0.0351  69  TYR B CZ  
1287 O OH  . TYR B 69  ? 0.3643 0.4120 0.4300 0.0098  -0.1026 0.0441  69  TYR B OH  
1288 N N   . LYS B 70  ? 0.2905 0.3116 0.3452 0.0121  -0.0458 0.0040  70  LYS B N   
1289 C CA  . LYS B 70  ? 0.2943 0.3126 0.3453 0.0096  -0.0385 -0.0006 70  LYS B CA  
1290 C C   . LYS B 70  ? 0.2944 0.3153 0.3405 0.0003  -0.0423 -0.0037 70  LYS B C   
1291 O O   . LYS B 70  ? 0.3122 0.3431 0.3656 -0.0041 -0.0482 -0.0030 70  LYS B O   
1292 C CB  . LYS B 70  ? 0.3058 0.3349 0.3737 0.0126  -0.0321 0.0006  70  LYS B CB  
1293 C CG  . LYS B 70  ? 0.3647 0.3906 0.4290 0.0102  -0.0249 -0.0026 70  LYS B CG  
1294 C CD  . LYS B 70  ? 0.3838 0.4184 0.4618 0.0147  -0.0167 0.0000  70  LYS B CD  
1295 C CE  . LYS B 70  ? 0.4339 0.4851 0.5328 0.0107  -0.0191 0.0035  70  LYS B CE  
1296 N NZ  . LYS B 70  ? 0.4863 0.5477 0.5997 0.0148  -0.0099 0.0077  70  LYS B NZ  
1297 N N   . VAL B 71  ? 0.2740 0.2861 0.3074 -0.0026 -0.0392 -0.0073 71  VAL B N   
1298 C CA  . VAL B 71  ? 0.2978 0.3111 0.3263 -0.0100 -0.0405 -0.0114 71  VAL B CA  
1299 C C   . VAL B 71  ? 0.3111 0.3225 0.3429 -0.0108 -0.0333 -0.0142 71  VAL B C   
1300 O O   . VAL B 71  ? 0.3127 0.3162 0.3380 -0.0081 -0.0281 -0.0142 71  VAL B O   
1301 C CB  . VAL B 71  ? 0.3244 0.3303 0.3364 -0.0124 -0.0426 -0.0120 71  VAL B CB  
1302 C CG1 . VAL B 71  ? 0.3450 0.3522 0.3516 -0.0184 -0.0422 -0.0170 71  VAL B CG1 
1303 C CG2 . VAL B 71  ? 0.3517 0.3590 0.3602 -0.0117 -0.0499 -0.0074 71  VAL B CG2 
1304 N N   . GLU B 72  ? 0.3124 0.3307 0.3551 -0.0147 -0.0335 -0.0160 72  GLU B N   
1305 C CA  . GLU B 72  ? 0.3295 0.3460 0.3773 -0.0161 -0.0271 -0.0176 72  GLU B CA  
1306 C C   . GLU B 72  ? 0.3098 0.3223 0.3518 -0.0218 -0.0284 -0.0230 72  GLU B C   
1307 O O   . GLU B 72  ? 0.3243 0.3401 0.3679 -0.0264 -0.0341 -0.0261 72  GLU B O   
1308 C CB  . GLU B 72  ? 0.3454 0.3721 0.4126 -0.0164 -0.0258 -0.0146 72  GLU B CB  
1309 C CG  . GLU B 72  ? 0.3569 0.3829 0.4318 -0.0195 -0.0207 -0.0152 72  GLU B CG  
1310 C CD  . GLU B 72  ? 0.3975 0.4352 0.4930 -0.0196 -0.0188 -0.0099 72  GLU B CD  
1311 O OE1 . GLU B 72  ? 0.3994 0.4459 0.5026 -0.0152 -0.0192 -0.0056 72  GLU B OE1 
1312 O OE2 . GLU B 72  ? 0.3962 0.4347 0.5015 -0.0240 -0.0167 -0.0094 72  GLU B OE2 
1313 N N   . ILE B 73  ? 0.3177 0.3225 0.3522 -0.0212 -0.0232 -0.0242 73  ILE B N   
1314 C CA  . ILE B 73  ? 0.3262 0.3262 0.3550 -0.0248 -0.0228 -0.0292 73  ILE B CA  
1315 C C   . ILE B 73  ? 0.3431 0.3412 0.3824 -0.0262 -0.0180 -0.0296 73  ILE B C   
1316 O O   . ILE B 73  ? 0.3280 0.3252 0.3704 -0.0232 -0.0125 -0.0252 73  ILE B O   
1317 C CB  . ILE B 73  ? 0.3256 0.3198 0.3408 -0.0228 -0.0204 -0.0285 73  ILE B CB  
1318 C CG1 . ILE B 73  ? 0.3398 0.3355 0.3455 -0.0220 -0.0255 -0.0266 73  ILE B CG1 
1319 C CG2 . ILE B 73  ? 0.3108 0.3010 0.3222 -0.0250 -0.0181 -0.0330 73  ILE B CG2 
1320 C CD1 . ILE B 73  ? 0.3388 0.3294 0.3337 -0.0205 -0.0239 -0.0237 73  ILE B CD1 
1321 N N   . ASP B 74  ? 0.3300 0.3271 0.3745 -0.0307 -0.0205 -0.0344 74  ASP B N   
1322 C CA  . ASP B 74  ? 0.3590 0.3546 0.4171 -0.0328 -0.0173 -0.0335 74  ASP B CA  
1323 C C   . ASP B 74  ? 0.3589 0.3461 0.4124 -0.0317 -0.0120 -0.0348 74  ASP B C   
1324 O O   . ASP B 74  ? 0.3758 0.3569 0.4294 -0.0340 -0.0128 -0.0402 74  ASP B O   
1325 C CB  . ASP B 74  ? 0.4188 0.4153 0.4868 -0.0388 -0.0232 -0.0376 74  ASP B CB  
1326 C CG  . ASP B 74  ? 0.4756 0.4701 0.5598 -0.0418 -0.0204 -0.0353 74  ASP B CG  
1327 O OD1 . ASP B 74  ? 0.5602 0.5523 0.6471 -0.0390 -0.0134 -0.0305 74  ASP B OD1 
1328 O OD2 . ASP B 74  ? 0.5373 0.5327 0.6320 -0.0474 -0.0261 -0.0376 74  ASP B OD2 
1329 N N   . THR B 75  ? 0.3416 0.3283 0.3908 -0.0276 -0.0070 -0.0296 75  THR B N   
1330 C CA  . THR B 75  ? 0.3246 0.3048 0.3690 -0.0261 -0.0025 -0.0293 75  THR B CA  
1331 C C   . THR B 75  ? 0.3031 0.2800 0.3603 -0.0278 0.0006  -0.0278 75  THR B C   
1332 O O   . THR B 75  ? 0.3186 0.2891 0.3759 -0.0277 0.0025  -0.0301 75  THR B O   
1333 C CB  . THR B 75  ? 0.3189 0.2997 0.3553 -0.0223 0.0003  -0.0236 75  THR B CB  
1334 O OG1 . THR B 75  ? 0.3088 0.2934 0.3517 -0.0208 0.0027  -0.0184 75  THR B OG1 
1335 C CG2 . THR B 75  ? 0.3383 0.3203 0.3624 -0.0210 -0.0036 -0.0246 75  THR B CG2 
1336 N N   . LYS B 76  ? 0.3119 0.2935 0.3813 -0.0293 0.0012  -0.0233 76  LYS B N   
1337 C CA  . LYS B 76  ? 0.3101 0.2892 0.3929 -0.0313 0.0042  -0.0196 76  LYS B CA  
1338 C C   . LYS B 76  ? 0.3405 0.3114 0.4302 -0.0355 0.0009  -0.0264 76  LYS B C   
1339 O O   . LYS B 76  ? 0.3573 0.3208 0.4515 -0.0355 0.0035  -0.0259 76  LYS B O   
1340 C CB  . LYS B 76  ? 0.3401 0.3280 0.4361 -0.0324 0.0059  -0.0123 76  LYS B CB  
1341 C CG  . LYS B 76  ? 0.3177 0.3041 0.4278 -0.0347 0.0095  -0.0060 76  LYS B CG  
1342 C CD  . LYS B 76  ? 0.3416 0.3396 0.4629 -0.0346 0.0132  0.0033  76  LYS B CD  
1343 C CE  . LYS B 76  ? 0.3626 0.3605 0.4972 -0.0368 0.0175  0.0120  76  LYS B CE  
1344 N N   . SER B 77  ? 0.3787 0.3501 0.4678 -0.0389 -0.0053 -0.0330 77  SER B N   
1345 C CA  . SER B 77  ? 0.3904 0.3519 0.4824 -0.0429 -0.0096 -0.0417 77  SER B CA  
1346 C C   . SER B 77  ? 0.3616 0.3144 0.4402 -0.0392 -0.0074 -0.0485 77  SER B C   
1347 O O   . SER B 77  ? 0.3588 0.3010 0.4404 -0.0399 -0.0074 -0.0539 77  SER B O   
1348 C CB  . SER B 77  ? 0.4249 0.3895 0.5158 -0.0474 -0.0179 -0.0476 77  SER B CB  
1349 O OG  . SER B 77  ? 0.4429 0.4172 0.5488 -0.0508 -0.0202 -0.0409 77  SER B OG  
1350 N N   . TYR B 78  ? 0.3674 0.3250 0.4316 -0.0351 -0.0057 -0.0481 78  TYR B N   
1351 C CA  . TYR B 78  ? 0.3647 0.3174 0.4169 -0.0311 -0.0027 -0.0529 78  TYR B CA  
1352 C C   . TYR B 78  ? 0.3551 0.3023 0.4152 -0.0282 0.0034  -0.0484 78  TYR B C   
1353 O O   . TYR B 78  ? 0.3762 0.3148 0.4373 -0.0268 0.0050  -0.0537 78  TYR B O   
1354 C CB  . TYR B 78  ? 0.3665 0.3270 0.4052 -0.0284 -0.0023 -0.0503 78  TYR B CB  
1355 C CG  . TYR B 78  ? 0.3611 0.3198 0.3895 -0.0243 0.0015  -0.0526 78  TYR B CG  
1356 C CD1 . TYR B 78  ? 0.3632 0.3191 0.3819 -0.0238 0.0004  -0.0616 78  TYR B CD1 
1357 C CD2 . TYR B 78  ? 0.3392 0.2999 0.3678 -0.0210 0.0063  -0.0455 78  TYR B CD2 
1358 C CE1 . TYR B 78  ? 0.3622 0.3183 0.3727 -0.0194 0.0053  -0.0631 78  TYR B CE1 
1359 C CE2 . TYR B 78  ? 0.3488 0.3098 0.3712 -0.0174 0.0101  -0.0464 78  TYR B CE2 
1360 C CZ  . TYR B 78  ? 0.3542 0.3137 0.3679 -0.0162 0.0102  -0.0548 78  TYR B CZ  
1361 O OH  . TYR B 78  ? 0.3704 0.3325 0.3780 -0.0117 0.0152  -0.0553 78  TYR B OH  
1362 N N   . TRP B 79  ? 0.2931 0.2452 0.3585 -0.0272 0.0065  -0.0384 79  TRP B N   
1363 C CA  . TRP B 79  ? 0.3097 0.2585 0.3818 -0.0248 0.0113  -0.0326 79  TRP B CA  
1364 C C   . TRP B 79  ? 0.3248 0.2648 0.4122 -0.0273 0.0111  -0.0333 79  TRP B C   
1365 O O   . TRP B 79  ? 0.3891 0.3219 0.4816 -0.0249 0.0141  -0.0330 79  TRP B O   
1366 C CB  . TRP B 79  ? 0.2857 0.2416 0.3578 -0.0239 0.0134  -0.0223 79  TRP B CB  
1367 C CG  . TRP B 79  ? 0.2670 0.2282 0.3248 -0.0213 0.0133  -0.0211 79  TRP B CG  
1368 C CD1 . TRP B 79  ? 0.3102 0.2772 0.3604 -0.0213 0.0114  -0.0191 79  TRP B CD1 
1369 C CD2 . TRP B 79  ? 0.2757 0.2365 0.3257 -0.0183 0.0147  -0.0221 79  TRP B CD2 
1370 N NE1 . TRP B 79  ? 0.2518 0.2204 0.2903 -0.0194 0.0108  -0.0185 79  TRP B NE1 
1371 C CE2 . TRP B 79  ? 0.2978 0.2640 0.3364 -0.0179 0.0128  -0.0196 79  TRP B CE2 
1372 C CE3 . TRP B 79  ? 0.3156 0.2725 0.3682 -0.0158 0.0175  -0.0242 79  TRP B CE3 
1373 C CZ2 . TRP B 79  ? 0.2782 0.2467 0.3090 -0.0162 0.0131  -0.0184 79  TRP B CZ2 
1374 C CZ3 . TRP B 79  ? 0.3078 0.2687 0.3528 -0.0130 0.0189  -0.0229 79  TRP B CZ3 
1375 C CH2 . TRP B 79  ? 0.3101 0.2773 0.3446 -0.0139 0.0164  -0.0196 79  TRP B CH2 
1376 N N   . LYS B 80  ? 0.3548 0.2961 0.4510 -0.0324 0.0075  -0.0331 80  LYS B N   
1377 C CA  A LYS B 80  ? 0.4013 0.3340 0.5137 -0.0363 0.0061  -0.0329 80  LYS B CA  
1378 C CA  B LYS B 80  ? 0.3900 0.3229 0.5025 -0.0364 0.0059  -0.0330 80  LYS B CA  
1379 C C   . LYS B 80  ? 0.4149 0.3335 0.5251 -0.0359 0.0040  -0.0448 80  LYS B C   
1380 O O   . LYS B 80  ? 0.4237 0.3307 0.5444 -0.0355 0.0053  -0.0450 80  LYS B O   
1381 C CB  A LYS B 80  ? 0.4230 0.3617 0.5460 -0.0426 0.0016  -0.0304 80  LYS B CB  
1382 C CB  B LYS B 80  ? 0.3936 0.3322 0.5157 -0.0428 0.0009  -0.0317 80  LYS B CB  
1383 C CG  A LYS B 80  ? 0.4495 0.4001 0.5798 -0.0425 0.0055  -0.0176 80  LYS B CG  
1384 C CG  B LYS B 80  ? 0.4004 0.3516 0.5306 -0.0435 0.0039  -0.0194 80  LYS B CG  
1385 C CD  A LYS B 80  ? 0.4351 0.3952 0.5762 -0.0476 0.0019  -0.0146 80  LYS B CD  
1386 C CD  B LYS B 80  ? 0.3745 0.3263 0.5061 -0.0397 0.0105  -0.0098 80  LYS B CD  
1387 C CE  A LYS B 80  ? 0.4739 0.4290 0.6355 -0.0545 -0.0012 -0.0121 80  LYS B CE  
1388 C CE  B LYS B 80  ? 0.3694 0.3277 0.5166 -0.0426 0.0132  0.0023  80  LYS B CE  
1389 N NZ  A LYS B 80  ? 0.4914 0.4611 0.6670 -0.0572 0.0005  -0.0006 80  LYS B NZ  
1390 N NZ  B LYS B 80  ? 0.3026 0.2616 0.4490 -0.0390 0.0190  0.0120  80  LYS B NZ  
1391 N N   . ALA B 81  ? 0.4650 0.3840 0.5609 -0.0354 0.0008  -0.0548 81  ALA B N   
1392 C CA  . ALA B 81  ? 0.5293 0.4352 0.6184 -0.0340 -0.0007 -0.0677 81  ALA B CA  
1393 C C   . ALA B 81  ? 0.5493 0.4502 0.6353 -0.0263 0.0066  -0.0677 81  ALA B C   
1394 O O   . ALA B 81  ? 0.5548 0.4424 0.6417 -0.0236 0.0077  -0.0757 81  ALA B O   
1395 C CB  . ALA B 81  ? 0.5226 0.4326 0.5946 -0.0350 -0.0053 -0.0767 81  ALA B CB  
1396 N N   . LEU B 82  ? 0.5115 0.4228 0.5944 -0.0224 0.0115  -0.0588 82  LEU B N   
1397 C CA  . LEU B 82  ? 0.5220 0.4313 0.6048 -0.0154 0.0179  -0.0568 82  LEU B CA  
1398 C C   . LEU B 82  ? 0.5059 0.4115 0.6054 -0.0147 0.0207  -0.0469 82  LEU B C   
1399 O O   . LEU B 82  ? 0.5247 0.4289 0.6277 -0.0090 0.0255  -0.0435 82  LEU B O   
1400 C CB  . LEU B 82  ? 0.5030 0.4258 0.5743 -0.0123 0.0206  -0.0515 82  LEU B CB  
1401 C CG  . LEU B 82  ? 0.5337 0.4613 0.5881 -0.0123 0.0185  -0.0595 82  LEU B CG  
1402 C CD1 . LEU B 82  ? 0.5071 0.4474 0.5533 -0.0110 0.0198  -0.0518 82  LEU B CD1 
1403 C CD2 . LEU B 82  ? 0.5569 0.4766 0.6047 -0.0074 0.0216  -0.0706 82  LEU B CD2 
1404 N N   . GLY B 83  ? 0.4677 0.3734 0.5783 -0.0203 0.0178  -0.0407 83  GLY B N   
1405 C CA  . GLY B 83  ? 0.4580 0.3611 0.5845 -0.0203 0.0202  -0.0296 83  GLY B CA  
1406 C C   . GLY B 83  ? 0.4460 0.3613 0.5707 -0.0184 0.0234  -0.0169 83  GLY B C   
1407 O O   . GLY B 83  ? 0.4386 0.3522 0.5729 -0.0164 0.0261  -0.0082 83  GLY B O   
1408 N N   . ILE B 84  ? 0.4476 0.3744 0.5600 -0.0194 0.0224  -0.0157 84  ILE B N   
1409 C CA  . ILE B 84  ? 0.4113 0.3481 0.5181 -0.0178 0.0244  -0.0058 84  ILE B CA  
1410 C C   . ILE B 84  ? 0.4266 0.3712 0.5323 -0.0216 0.0230  -0.0007 84  ILE B C   
1411 O O   . ILE B 84  ? 0.3925 0.3389 0.4956 -0.0244 0.0202  -0.0064 84  ILE B O   
1412 C CB  . ILE B 84  ? 0.4874 0.4299 0.5791 -0.0147 0.0245  -0.0095 84  ILE B CB  
1413 C CG1 . ILE B 84  ? 0.5291 0.4666 0.6219 -0.0099 0.0271  -0.0143 84  ILE B CG1 
1414 C CG2 . ILE B 84  ? 0.4804 0.4313 0.5660 -0.0139 0.0250  0.0003  84  ILE B CG2 
1415 C CD1 . ILE B 84  ? 0.5253 0.4697 0.6053 -0.0071 0.0278  -0.0169 84  ILE B CD1 
1416 N N   . SER B 85  ? 0.3927 0.3422 0.5010 -0.0215 0.0251  0.0104  85  SER B N   
1417 C CA  . SER B 85  ? 0.4276 0.3845 0.5364 -0.0239 0.0257  0.0165  85  SER B CA  
1418 C C   . SER B 85  ? 0.4023 0.3662 0.4940 -0.0220 0.0250  0.0150  85  SER B C   
1419 O O   . SER B 85  ? 0.3878 0.3528 0.4697 -0.0194 0.0251  0.0175  85  SER B O   
1420 C CB  . SER B 85  ? 0.4951 0.4540 0.6113 -0.0239 0.0287  0.0291  85  SER B CB  
1421 O OG  . SER B 85  ? 0.5811 0.5455 0.7047 -0.0270 0.0300  0.0345  85  SER B OG  
1422 N N   . PRO B 86  ? 0.3305 0.2980 0.4194 -0.0233 0.0233  0.0103  86  PRO B N   
1423 C CA  . PRO B 86  ? 0.3318 0.3038 0.4050 -0.0210 0.0222  0.0085  86  PRO B CA  
1424 C C   . PRO B 86  ? 0.3067 0.2855 0.3764 -0.0198 0.0248  0.0147  86  PRO B C   
1425 O O   . PRO B 86  ? 0.3507 0.3336 0.4314 -0.0213 0.0274  0.0197  86  PRO B O   
1426 C CB  . PRO B 86  ? 0.3379 0.3097 0.4110 -0.0226 0.0187  -0.0004 86  PRO B CB  
1427 C CG  . PRO B 86  ? 0.3708 0.3428 0.4595 -0.0262 0.0185  0.0000  86  PRO B CG  
1428 C CD  . PRO B 86  ? 0.3429 0.3094 0.4419 -0.0269 0.0210  0.0051  86  PRO B CD  
1429 N N   . PHE B 87  ? 0.3026 0.2827 0.3573 -0.0171 0.0239  0.0137  87  PHE B N   
1430 C CA  . PHE B 87  ? 0.2998 0.2851 0.3481 -0.0145 0.0267  0.0176  87  PHE B CA  
1431 C C   . PHE B 87  ? 0.2886 0.2787 0.3396 -0.0137 0.0263  0.0136  87  PHE B C   
1432 O O   . PHE B 87  ? 0.2859 0.2832 0.3438 -0.0127 0.0302  0.0179  87  PHE B O   
1433 C CB  . PHE B 87  ? 0.3024 0.2845 0.3323 -0.0118 0.0252  0.0177  87  PHE B CB  
1434 C CG  . PHE B 87  ? 0.3057 0.2906 0.3254 -0.0080 0.0280  0.0196  87  PHE B CG  
1435 C CD1 . PHE B 87  ? 0.3438 0.3334 0.3642 -0.0070 0.0331  0.0271  87  PHE B CD1 
1436 C CD2 . PHE B 87  ? 0.3269 0.3097 0.3360 -0.0050 0.0260  0.0141  87  PHE B CD2 
1437 C CE1 . PHE B 87  ? 0.3415 0.3336 0.3499 -0.0025 0.0366  0.0284  87  PHE B CE1 
1438 C CE2 . PHE B 87  ? 0.3727 0.3571 0.3716 -0.0001 0.0295  0.0151  87  PHE B CE2 
1439 C CZ  . PHE B 87  ? 0.3503 0.3395 0.3483 0.0013  0.0352  0.0219  87  PHE B CZ  
1440 N N   . HIS B 88  ? 0.3068 0.2942 0.3526 -0.0137 0.0218  0.0065  88  HIS B N   
1441 C CA  . HIS B 88  ? 0.2853 0.2773 0.3318 -0.0119 0.0207  0.0037  88  HIS B CA  
1442 C C   . HIS B 88  ? 0.2896 0.2864 0.3525 -0.0157 0.0192  0.0025  88  HIS B C   
1443 O O   . HIS B 88  ? 0.2995 0.2924 0.3683 -0.0196 0.0167  -0.0004 88  HIS B O   
1444 C CB  . HIS B 88  ? 0.3048 0.2920 0.3390 -0.0108 0.0156  -0.0019 88  HIS B CB  
1445 C CG  . HIS B 88  ? 0.3248 0.3057 0.3429 -0.0085 0.0151  -0.0010 88  HIS B CG  
1446 N ND1 . HIS B 88  ? 0.3585 0.3349 0.3723 -0.0105 0.0137  -0.0003 88  HIS B ND1 
1447 C CD2 . HIS B 88  ? 0.3903 0.3684 0.3958 -0.0042 0.0153  -0.0008 88  HIS B CD2 
1448 C CE1 . HIS B 88  ? 0.3675 0.3392 0.3676 -0.0088 0.0122  0.0011  88  HIS B CE1 
1449 N NE2 . HIS B 88  ? 0.4304 0.4017 0.4241 -0.0051 0.0129  0.0000  88  HIS B NE2 
1450 N N   . GLU B 89  ? 0.2847 0.2897 0.3548 -0.0142 0.0203  0.0042  89  GLU B N   
1451 C CA  . GLU B 89  ? 0.3100 0.3206 0.3952 -0.0182 0.0166  0.0026  89  GLU B CA  
1452 C C   . GLU B 89  ? 0.3069 0.3134 0.3858 -0.0199 0.0095  -0.0051 89  GLU B C   
1453 O O   . GLU B 89  ? 0.3902 0.3960 0.4771 -0.0250 0.0050  -0.0088 89  GLU B O   
1454 C CB  . GLU B 89  ? 0.3315 0.3542 0.4266 -0.0153 0.0198  0.0077  89  GLU B CB  
1455 C CG  . GLU B 89  ? 0.3610 0.3904 0.4655 -0.0149 0.0271  0.0164  89  GLU B CG  
1456 C CD  . GLU B 89  ? 0.4183 0.4485 0.5411 -0.0225 0.0255  0.0193  89  GLU B CD  
1457 O OE1 . GLU B 89  ? 0.4567 0.4914 0.5937 -0.0271 0.0206  0.0181  89  GLU B OE1 
1458 O OE2 . GLU B 89  ? 0.4626 0.4881 0.5857 -0.0240 0.0283  0.0230  89  GLU B OE2 
1459 N N   . HIS B 90  ? 0.3262 0.3298 0.3906 -0.0159 0.0081  -0.0074 90  HIS B N   
1460 C CA  . HIS B 90  ? 0.3472 0.3483 0.4042 -0.0170 0.0019  -0.0128 90  HIS B CA  
1461 C C   . HIS B 90  ? 0.3756 0.3718 0.4173 -0.0125 0.0020  -0.0127 90  HIS B C   
1462 O O   . HIS B 90  ? 0.3656 0.3601 0.4020 -0.0084 0.0063  -0.0095 90  HIS B O   
1463 C CB  . HIS B 90  ? 0.3667 0.3762 0.4339 -0.0183 -0.0028 -0.0134 90  HIS B CB  
1464 C CG  . HIS B 90  ? 0.4309 0.4490 0.5059 -0.0136 0.0006  -0.0080 90  HIS B CG  
1465 N ND1 . HIS B 90  ? 0.5576 0.5741 0.6229 -0.0071 0.0022  -0.0071 90  HIS B ND1 
1466 C CD2 . HIS B 90  ? 0.5025 0.5315 0.5953 -0.0141 0.0033  -0.0029 90  HIS B CD2 
1467 C CE1 . HIS B 90  ? 0.5131 0.5388 0.5884 -0.0026 0.0064  -0.0025 90  HIS B CE1 
1468 N NE2 . HIS B 90  ? 0.5874 0.6221 0.6803 -0.0070 0.0074  0.0008  90  HIS B NE2 
1469 N N   . ALA B 91  ? 0.3349 0.3279 0.3678 -0.0134 -0.0031 -0.0161 91  ALA B N   
1470 C CA  . ALA B 91  ? 0.3692 0.3572 0.3894 -0.0101 -0.0048 -0.0155 91  ALA B CA  
1471 C C   . ALA B 91  ? 0.4477 0.4400 0.4705 -0.0083 -0.0092 -0.0156 91  ALA B C   
1472 O O   . ALA B 91  ? 0.4312 0.4280 0.4583 -0.0118 -0.0137 -0.0177 91  ALA B O   
1473 C CB  . ALA B 91  ? 0.3911 0.3735 0.4008 -0.0126 -0.0071 -0.0171 91  ALA B CB  
1474 N N   . GLU B 92  ? 0.4374 0.4282 0.4576 -0.0026 -0.0080 -0.0136 92  GLU B N   
1475 C CA  . GLU B 92  ? 0.4275 0.4222 0.4518 0.0008  -0.0115 -0.0125 92  GLU B CA  
1476 C C   . GLU B 92  ? 0.4743 0.4589 0.4852 0.0034  -0.0150 -0.0125 92  GLU B C   
1477 O O   . GLU B 92  ? 0.5515 0.5274 0.5529 0.0061  -0.0124 -0.0128 92  GLU B O   
1478 C CB  . GLU B 92  ? 0.4876 0.4892 0.5226 0.0067  -0.0063 -0.0097 92  GLU B CB  
1479 N N   . VAL B 93  ? 0.3528 0.3379 0.3625 0.0020  -0.0216 -0.0119 93  VAL B N   
1480 C CA  . VAL B 93  ? 0.3532 0.3286 0.3524 0.0040  -0.0258 -0.0106 93  VAL B CA  
1481 C C   . VAL B 93  ? 0.3220 0.3005 0.3286 0.0092  -0.0289 -0.0083 93  VAL B C   
1482 O O   . VAL B 93  ? 0.3315 0.3200 0.3468 0.0071  -0.0327 -0.0068 93  VAL B O   
1483 C CB  . VAL B 93  ? 0.4347 0.4092 0.4264 -0.0024 -0.0305 -0.0102 93  VAL B CB  
1484 C CG1 . VAL B 93  ? 0.4231 0.3880 0.4057 -0.0015 -0.0355 -0.0073 93  VAL B CG1 
1485 C CG2 . VAL B 93  ? 0.4727 0.4462 0.4606 -0.0063 -0.0265 -0.0122 93  VAL B CG2 
1486 N N   . VAL B 94  ? 0.3164 0.2865 0.3200 0.0164  -0.0275 -0.0080 94  VAL B N   
1487 C CA  . VAL B 94  ? 0.3084 0.2808 0.3202 0.0228  -0.0297 -0.0054 94  VAL B CA  
1488 C C   . VAL B 94  ? 0.3478 0.3058 0.3501 0.0251  -0.0355 -0.0041 94  VAL B C   
1489 O O   . VAL B 94  ? 0.3418 0.2853 0.3320 0.0266  -0.0347 -0.0064 94  VAL B O   
1490 C CB  . VAL B 94  ? 0.3280 0.3036 0.3472 0.0315  -0.0216 -0.0063 94  VAL B CB  
1491 C CG1 . VAL B 94  ? 0.3165 0.2967 0.3474 0.0392  -0.0232 -0.0030 94  VAL B CG1 
1492 C CG2 . VAL B 94  ? 0.3493 0.3389 0.3792 0.0284  -0.0161 -0.0061 94  VAL B CG2 
1493 N N   . PHE B 95  ? 0.3020 0.2635 0.3099 0.0249  -0.0424 0.0003  95  PHE B N   
1494 C CA  . PHE B 95  ? 0.3438 0.2919 0.3437 0.0253  -0.0492 0.0032  95  PHE B CA  
1495 C C   . PHE B 95  ? 0.3467 0.2991 0.3572 0.0298  -0.0543 0.0084  95  PHE B C   
1496 O O   . PHE B 95  ? 0.3506 0.3187 0.3731 0.0293  -0.0548 0.0106  95  PHE B O   
1497 C CB  . PHE B 95  ? 0.3478 0.2952 0.3381 0.0155  -0.0536 0.0050  95  PHE B CB  
1498 C CG  . PHE B 95  ? 0.3563 0.3188 0.3516 0.0097  -0.0573 0.0080  95  PHE B CG  
1499 C CD1 . PHE B 95  ? 0.3559 0.3300 0.3544 0.0057  -0.0535 0.0045  95  PHE B CD1 
1500 C CD2 . PHE B 95  ? 0.3627 0.3269 0.3583 0.0080  -0.0651 0.0143  95  PHE B CD2 
1501 C CE1 . PHE B 95  ? 0.3625 0.3485 0.3630 0.0003  -0.0577 0.0059  95  PHE B CE1 
1502 C CE2 . PHE B 95  ? 0.3837 0.3616 0.3804 0.0023  -0.0690 0.0166  95  PHE B CE2 
1503 C CZ  . PHE B 95  ? 0.3343 0.3225 0.3329 -0.0013 -0.0653 0.0116  95  PHE B CZ  
1504 N N   . THR B 96  ? 0.3906 0.3283 0.3977 0.0345  -0.0586 0.0107  96  THR B N   
1505 C CA  . THR B 96  ? 0.4036 0.3445 0.4208 0.0382  -0.0649 0.0173  96  THR B CA  
1506 C C   . THR B 96  ? 0.4585 0.4002 0.4702 0.0294  -0.0738 0.0238  96  THR B C   
1507 O O   . THR B 96  ? 0.4476 0.3767 0.4473 0.0247  -0.0762 0.0241  96  THR B O   
1508 C CB  . THR B 96  ? 0.4569 0.3791 0.4735 0.0484  -0.0658 0.0171  96  THR B CB  
1509 O OG1 . THR B 96  ? 0.4716 0.3929 0.4917 0.0582  -0.0564 0.0110  96  THR B OG1 
1510 C CG2 . THR B 96  ? 0.4641 0.3895 0.4929 0.0522  -0.0733 0.0257  96  THR B CG2 
1511 N N   . ALA B 97  ? 0.4303 0.3866 0.4510 0.0276  -0.0790 0.0298  97  ALA B N   
1512 C CA  . ALA B 97  ? 0.4503 0.4112 0.4652 0.0193  -0.0870 0.0366  97  ALA B CA  
1513 C C   . ALA B 97  ? 0.5422 0.4966 0.5617 0.0229  -0.0950 0.0456  97  ALA B C   
1514 O O   . ALA B 97  ? 0.4901 0.4443 0.5224 0.0318  -0.0959 0.0478  97  ALA B O   
1515 C CB  . ALA B 97  ? 0.5012 0.4826 0.5197 0.0135  -0.0884 0.0369  97  ALA B CB  
1516 N N   . ASN B 98  ? 0.5638 0.5118 0.5731 0.0162  -0.1005 0.0513  98  ASN B N   
1517 C CA  . ASN B 98  ? 0.6053 0.5535 0.6170 0.0149  -0.1101 0.0629  98  ASN B CA  
1518 C C   . ASN B 98  ? 0.6070 0.5365 0.6251 0.0233  -0.1132 0.0661  98  ASN B C   
1519 O O   . ASN B 98  ? 0.5834 0.5115 0.6076 0.0248  -0.1214 0.0765  98  ASN B O   
1520 C CB  . ASN B 98  ? 0.5952 0.5641 0.6154 0.0142  -0.1142 0.0674  98  ASN B CB  
1521 C CG  . ASN B 98  ? 0.6161 0.6007 0.6265 0.0049  -0.1130 0.0646  98  ASN B CG  
1522 O OD1 . ASN B 98  ? 0.5301 0.5121 0.5269 -0.0021 -0.1118 0.0645  98  ASN B OD1 
1523 N ND2 . ASN B 98  ? 0.5599 0.5608 0.5775 0.0047  -0.1136 0.0624  98  ASN B ND2 
1524 N N   . ASP B 99  ? 0.6191 0.5343 0.6353 0.0292  -0.1067 0.0569  99  ASP B N   
1525 C CA  . ASP B 99  ? 0.6764 0.5697 0.6959 0.0389  -0.1075 0.0556  99  ASP B CA  
1526 C C   . ASP B 99  ? 0.7125 0.5913 0.7312 0.0365  -0.1178 0.0661  99  ASP B C   
1527 O O   . ASP B 99  ? 0.8019 0.6686 0.8296 0.0456  -0.1214 0.0695  99  ASP B O   
1528 C CB  . ASP B 99  ? 0.6293 0.5068 0.6381 0.0408  -0.1005 0.0444  99  ASP B CB  
1529 N N   . GLY B 101 ? 0.6740 0.5843 0.6902 0.0155  -0.1360 0.0960  101 GLY B N   
1530 C CA  . GLY B 101 ? 0.6939 0.6252 0.7062 0.0073  -0.1402 0.1047  101 GLY B CA  
1531 C C   . GLY B 101 ? 0.7049 0.6527 0.7062 0.0000  -0.1335 0.0971  101 GLY B C   
1532 O O   . GLY B 101 ? 0.6935 0.6348 0.6891 -0.0007 -0.1262 0.0871  101 GLY B O   
1533 N N   . PRO B 102 ? 0.7258 0.6947 0.7240 -0.0049 -0.1362 0.1013  102 PRO B N   
1534 C CA  . PRO B 102 ? 0.7274 0.7114 0.7135 -0.0121 -0.1312 0.0952  102 PRO B CA  
1535 C C   . PRO B 102 ? 0.7379 0.7186 0.7107 -0.0192 -0.1266 0.0943  102 PRO B C   
1536 O O   . PRO B 102 ? 0.7298 0.7068 0.6980 -0.0238 -0.1306 0.1048  102 PRO B O   
1537 C CB  . PRO B 102 ? 0.7735 0.7759 0.7571 -0.0157 -0.1383 0.1032  102 PRO B CB  
1538 C CG  . PRO B 102 ? 0.7993 0.8015 0.8000 -0.0077 -0.1433 0.1060  102 PRO B CG  
1539 C CD  . PRO B 102 ? 0.8072 0.7873 0.8173 0.0000  -0.1418 0.1058  102 PRO B CD  
1540 N N   . ARG B 103 ? 0.7293 0.7126 0.6976 -0.0201 -0.1181 0.0825  103 ARG B N   
1541 C CA  . ARG B 103 ? 0.7221 0.7043 0.6801 -0.0259 -0.1128 0.0810  103 ARG B CA  
1542 C C   . ARG B 103 ? 0.6774 0.6744 0.6280 -0.0286 -0.1064 0.0718  103 ARG B C   
1543 O O   . ARG B 103 ? 0.6694 0.6729 0.6245 -0.0257 -0.1058 0.0649  103 ARG B O   
1544 C CB  . ARG B 103 ? 0.7547 0.7192 0.7160 -0.0231 -0.1087 0.0749  103 ARG B CB  
1545 C CG  . ARG B 103 ? 0.7659 0.7114 0.7345 -0.0187 -0.1145 0.0798  103 ARG B CG  
1546 C CD  . ARG B 103 ? 0.7761 0.7125 0.7411 -0.0248 -0.1195 0.0905  103 ARG B CD  
1547 N NE  . ARG B 103 ? 0.8486 0.7645 0.8208 -0.0201 -0.1262 0.0945  103 ARG B NE  
1548 C CZ  . ARG B 103 ? 0.8689 0.7831 0.8486 -0.0162 -0.1331 0.1025  103 ARG B CZ  
1549 N NH1 . ARG B 103 ? 0.8535 0.7866 0.8338 -0.0172 -0.1353 0.1081  103 ARG B NH1 
1550 N NH2 . ARG B 103 ? 0.9053 0.7979 0.8915 -0.0110 -0.1384 0.1047  103 ARG B NH2 
1551 N N   . ARG B 104 ? 0.5495 0.5513 0.4900 -0.0338 -0.1016 0.0718  104 ARG B N   
1552 C CA  . ARG B 104 ? 0.4949 0.5060 0.4294 -0.0348 -0.0941 0.0609  104 ARG B CA  
1553 C C   . ARG B 104 ? 0.4661 0.4661 0.4058 -0.0324 -0.0877 0.0527  104 ARG B C   
1554 O O   . ARG B 104 ? 0.4206 0.4101 0.3614 -0.0333 -0.0876 0.0569  104 ARG B O   
1555 C CB  . ARG B 104 ? 0.4972 0.5202 0.4186 -0.0401 -0.0910 0.0642  104 ARG B CB  
1556 N N   . TYR B 105 ? 0.4168 0.4185 0.3602 -0.0296 -0.0834 0.0421  105 TYR B N   
1557 C CA  . TYR B 105 ? 0.4130 0.4066 0.3608 -0.0272 -0.0770 0.0343  105 TYR B CA  
1558 C C   . TYR B 105 ? 0.3890 0.3899 0.3318 -0.0293 -0.0701 0.0266  105 TYR B C   
1559 O O   . TYR B 105 ? 0.4133 0.4231 0.3546 -0.0299 -0.0704 0.0219  105 TYR B O   
1560 C CB  . TYR B 105 ? 0.4409 0.4313 0.3992 -0.0216 -0.0771 0.0289  105 TYR B CB  
1561 C CG  . TYR B 105 ? 0.4422 0.4229 0.4071 -0.0171 -0.0822 0.0343  105 TYR B CG  
1562 C CD1 . TYR B 105 ? 0.4978 0.4634 0.4644 -0.0136 -0.0803 0.0329  105 TYR B CD1 
1563 C CD2 . TYR B 105 ? 0.4950 0.4810 0.4643 -0.0158 -0.0893 0.0405  105 TYR B CD2 
1564 C CE1 . TYR B 105 ? 0.4887 0.4432 0.4607 -0.0084 -0.0850 0.0369  105 TYR B CE1 
1565 C CE2 . TYR B 105 ? 0.5383 0.5145 0.5149 -0.0106 -0.0939 0.0458  105 TYR B CE2 
1566 C CZ  . TYR B 105 ? 0.4850 0.4448 0.4629 -0.0065 -0.0914 0.0432  105 TYR B CZ  
1567 O OH  . TYR B 105 ? 0.5561 0.5047 0.5407 -0.0004 -0.0960 0.0476  105 TYR B OH  
1568 N N   . THR B 106 ? 0.3851 0.3820 0.3258 -0.0306 -0.0647 0.0257  106 THR B N   
1569 C CA  . THR B 106 ? 0.3853 0.3864 0.3243 -0.0311 -0.0573 0.0180  106 THR B CA  
1570 C C   . THR B 106 ? 0.3669 0.3586 0.3130 -0.0281 -0.0536 0.0132  106 THR B C   
1571 O O   . THR B 106 ? 0.3627 0.3450 0.3099 -0.0278 -0.0545 0.0168  106 THR B O   
1572 C CB  . THR B 106 ? 0.3864 0.3934 0.3182 -0.0344 -0.0534 0.0219  106 THR B CB  
1573 O OG1 . THR B 106 ? 0.4480 0.4649 0.3715 -0.0367 -0.0564 0.0268  106 THR B OG1 
1574 C CG2 . THR B 106 ? 0.4878 0.4986 0.4187 -0.0337 -0.0454 0.0139  106 THR B CG2 
1575 N N   . ILE B 107 ? 0.3583 0.3519 0.3090 -0.0262 -0.0503 0.0054  107 ILE B N   
1576 C CA  . ILE B 107 ? 0.3461 0.3324 0.3034 -0.0233 -0.0462 0.0013  107 ILE B CA  
1577 C C   . ILE B 107 ? 0.3643 0.3536 0.3199 -0.0250 -0.0400 -0.0025 107 ILE B C   
1578 O O   . ILE B 107 ? 0.3864 0.3819 0.3416 -0.0259 -0.0380 -0.0077 107 ILE B O   
1579 C CB  . ILE B 107 ? 0.3703 0.3579 0.3365 -0.0202 -0.0461 -0.0031 107 ILE B CB  
1580 C CG1 . ILE B 107 ? 0.4164 0.4023 0.3864 -0.0171 -0.0520 0.0011  107 ILE B CG1 
1581 C CG2 . ILE B 107 ? 0.3800 0.3629 0.3515 -0.0178 -0.0401 -0.0071 107 ILE B CG2 
1582 C CD1 . ILE B 107 ? 0.4455 0.4197 0.4129 -0.0148 -0.0537 0.0055  107 ILE B CD1 
1583 N N   . ALA B 108 ? 0.3548 0.3393 0.3095 -0.0254 -0.0375 -0.0001 108 ALA B N   
1584 C CA  . ALA B 108 ? 0.3433 0.3310 0.2983 -0.0262 -0.0313 -0.0027 108 ALA B CA  
1585 C C   . ALA B 108 ? 0.3542 0.3362 0.3150 -0.0242 -0.0276 -0.0056 108 ALA B C   
1586 O O   . ALA B 108 ? 0.3619 0.3367 0.3229 -0.0230 -0.0296 -0.0035 108 ALA B O   
1587 C CB  . ALA B 108 ? 0.3826 0.3726 0.3336 -0.0289 -0.0313 0.0041  108 ALA B CB  
1588 N N   . ALA B 109 ? 0.3126 0.2972 0.2773 -0.0237 -0.0225 -0.0103 109 ALA B N   
1589 C CA  . ALA B 109 ? 0.3072 0.2875 0.2781 -0.0220 -0.0188 -0.0120 109 ALA B CA  
1590 C C   . ALA B 109 ? 0.3146 0.2972 0.2874 -0.0224 -0.0138 -0.0120 109 ALA B C   
1591 O O   . ALA B 109 ? 0.3194 0.3067 0.2921 -0.0225 -0.0112 -0.0156 109 ALA B O   
1592 C CB  . ALA B 109 ? 0.3356 0.3163 0.3135 -0.0206 -0.0176 -0.0168 109 ALA B CB  
1593 N N   . LEU B 110 ? 0.3050 0.2842 0.2795 -0.0222 -0.0124 -0.0084 110 LEU B N   
1594 C CA  . LEU B 110 ? 0.2875 0.2691 0.2664 -0.0219 -0.0079 -0.0071 110 LEU B CA  
1595 C C   . LEU B 110 ? 0.2946 0.2726 0.2800 -0.0203 -0.0050 -0.0087 110 LEU B C   
1596 O O   . LEU B 110 ? 0.2919 0.2653 0.2755 -0.0200 -0.0066 -0.0063 110 LEU B O   
1597 C CB  . LEU B 110 ? 0.2992 0.2809 0.2758 -0.0238 -0.0102 0.0001  110 LEU B CB  
1598 C CG  . LEU B 110 ? 0.3302 0.3161 0.3129 -0.0235 -0.0064 0.0040  110 LEU B CG  
1599 C CD1 . LEU B 110 ? 0.3116 0.3050 0.2973 -0.0218 -0.0011 0.0017  110 LEU B CD1 
1600 C CD2 . LEU B 110 ? 0.4129 0.3989 0.3937 -0.0268 -0.0110 0.0122  110 LEU B CD2 
1601 N N   . LEU B 111 ? 0.2561 0.2356 0.2481 -0.0193 -0.0006 -0.0123 111 LEU B N   
1602 C CA  . LEU B 111 ? 0.2696 0.2459 0.2693 -0.0183 0.0020  -0.0134 111 LEU B CA  
1603 C C   . LEU B 111 ? 0.2648 0.2409 0.2709 -0.0174 0.0057  -0.0097 111 LEU B C   
1604 O O   . LEU B 111 ? 0.2774 0.2558 0.2867 -0.0162 0.0086  -0.0103 111 LEU B O   
1605 C CB  . LEU B 111 ? 0.2794 0.2556 0.2843 -0.0185 0.0030  -0.0202 111 LEU B CB  
1606 C CG  . LEU B 111 ? 0.3131 0.2910 0.3140 -0.0197 -0.0011 -0.0237 111 LEU B CG  
1607 C CD1 . LEU B 111 ? 0.3105 0.2875 0.3179 -0.0209 -0.0010 -0.0301 111 LEU B CD1 
1608 C CD2 . LEU B 111 ? 0.2961 0.2734 0.2953 -0.0192 -0.0038 -0.0205 111 LEU B CD2 
1609 N N   . SER B 112 ? 0.2825 0.2562 0.2904 -0.0172 0.0060  -0.0054 112 SER B N   
1610 C CA  . SER B 112 ? 0.2870 0.2602 0.3034 -0.0162 0.0094  -0.0014 112 SER B CA  
1611 C C   . SER B 112 ? 0.3249 0.2959 0.3473 -0.0161 0.0114  -0.0014 112 SER B C   
1612 O O   . SER B 112 ? 0.3007 0.2717 0.3205 -0.0164 0.0102  -0.0034 112 SER B O   
1613 C CB  . SER B 112 ? 0.3035 0.2779 0.3165 -0.0167 0.0076  0.0062  112 SER B CB  
1614 O OG  . SER B 112 ? 0.3440 0.3218 0.3523 -0.0178 0.0050  0.0078  112 SER B OG  
1615 N N   . PRO B 113 ? 0.3081 0.2781 0.3403 -0.0156 0.0145  0.0017  113 PRO B N   
1616 C CA  . PRO B 113 ? 0.3101 0.2792 0.3497 -0.0161 0.0165  0.0031  113 PRO B CA  
1617 C C   . PRO B 113 ? 0.2958 0.2668 0.3285 -0.0159 0.0163  0.0074  113 PRO B C   
1618 O O   . PRO B 113 ? 0.2936 0.2662 0.3303 -0.0161 0.0177  0.0067  113 PRO B O   
1619 C CB  . PRO B 113 ? 0.2969 0.2642 0.3476 -0.0155 0.0194  0.0080  113 PRO B CB  
1620 C CG  . PRO B 113 ? 0.3176 0.2839 0.3697 -0.0140 0.0197  0.0044  113 PRO B CG  
1621 C CD  . PRO B 113 ? 0.2980 0.2680 0.3376 -0.0141 0.0168  0.0040  113 PRO B CD  
1622 N N   . TYR B 114 ? 0.2676 0.2384 0.2903 -0.0153 0.0146  0.0118  114 TYR B N   
1623 C CA  . TYR B 114 ? 0.2802 0.2509 0.2925 -0.0143 0.0141  0.0146  114 TYR B CA  
1624 C C   . TYR B 114 ? 0.2954 0.2633 0.2936 -0.0138 0.0099  0.0115  114 TYR B C   
1625 O O   . TYR B 114 ? 0.3167 0.2821 0.3034 -0.0125 0.0090  0.0131  114 TYR B O   
1626 C CB  . TYR B 114 ? 0.2967 0.2681 0.3079 -0.0143 0.0150  0.0226  114 TYR B CB  
1627 C CG  . TYR B 114 ? 0.3102 0.2843 0.3334 -0.0143 0.0199  0.0272  114 TYR B CG  
1628 C CD1 . TYR B 114 ? 0.3956 0.3692 0.4343 -0.0153 0.0216  0.0273  114 TYR B CD1 
1629 C CD2 . TYR B 114 ? 0.3380 0.3148 0.3564 -0.0131 0.0228  0.0319  114 TYR B CD2 
1630 C CE1 . TYR B 114 ? 0.4604 0.4353 0.5114 -0.0160 0.0252  0.0325  114 TYR B CE1 
1631 C CE2 . TYR B 114 ? 0.3587 0.3392 0.3896 -0.0137 0.0274  0.0378  114 TYR B CE2 
1632 C CZ  . TYR B 114 ? 0.4102 0.3893 0.4577 -0.0155 0.0279  0.0383  114 TYR B CZ  
1633 O OH  . TYR B 114 ? 0.5820 0.5634 0.6430 -0.0169 0.0315  0.0450  114 TYR B OH  
1634 N N   . SER B 115 ? 0.3006 0.2679 0.2986 -0.0147 0.0073  0.0068  115 SER B N   
1635 C CA  . SER B 115 ? 0.3022 0.2659 0.2880 -0.0148 0.0024  0.0050  115 SER B CA  
1636 C C   . SER B 115 ? 0.3076 0.2727 0.2958 -0.0155 0.0008  0.0002  115 SER B C   
1637 O O   . SER B 115 ? 0.3160 0.2845 0.3120 -0.0165 0.0023  -0.0011 115 SER B O   
1638 C CB  . SER B 115 ? 0.3442 0.3065 0.3250 -0.0171 -0.0016 0.0095  115 SER B CB  
1639 O OG  . SER B 115 ? 0.4007 0.3575 0.3697 -0.0179 -0.0072 0.0082  115 SER B OG  
1640 N N   . TYR B 116 ? 0.3076 0.2697 0.2883 -0.0147 -0.0025 -0.0022 116 TYR B N   
1641 C CA  . TYR B 116 ? 0.2962 0.2600 0.2769 -0.0159 -0.0055 -0.0049 116 TYR B CA  
1642 C C   . TYR B 116 ? 0.2922 0.2503 0.2626 -0.0162 -0.0109 -0.0040 116 TYR B C   
1643 O O   . TYR B 116 ? 0.3021 0.2535 0.2649 -0.0142 -0.0124 -0.0038 116 TYR B O   
1644 C CB  . TYR B 116 ? 0.3202 0.2879 0.3079 -0.0151 -0.0041 -0.0093 116 TYR B CB  
1645 C CG  . TYR B 116 ? 0.3259 0.2926 0.3127 -0.0121 -0.0043 -0.0103 116 TYR B CG  
1646 C CD1 . TYR B 116 ? 0.3814 0.3450 0.3618 -0.0108 -0.0087 -0.0110 116 TYR B CD1 
1647 C CD2 . TYR B 116 ? 0.4210 0.3902 0.4142 -0.0100 0.0002  -0.0096 116 TYR B CD2 
1648 C CE1 . TYR B 116 ? 0.3998 0.3629 0.3810 -0.0067 -0.0081 -0.0119 116 TYR B CE1 
1649 C CE2 . TYR B 116 ? 0.3943 0.3643 0.3876 -0.0062 0.0013  -0.0099 116 TYR B CE2 
1650 C CZ  . TYR B 116 ? 0.4566 0.4233 0.4438 -0.0040 -0.0026 -0.0113 116 TYR B CZ  
1651 O OH  . TYR B 116 ? 0.4880 0.4557 0.4766 0.0011  -0.0009 -0.0116 116 TYR B OH  
1652 N N   . SER B 117 ? 0.3041 0.2640 0.2733 -0.0185 -0.0142 -0.0034 117 SER B N   
1653 C CA  . SER B 117 ? 0.3200 0.2742 0.2813 -0.0195 -0.0202 -0.0018 117 SER B CA  
1654 C C   . SER B 117 ? 0.3020 0.2598 0.2649 -0.0192 -0.0217 -0.0038 117 SER B C   
1655 O O   . SER B 117 ? 0.3011 0.2664 0.2690 -0.0199 -0.0192 -0.0056 117 SER B O   
1656 C CB  . SER B 117 ? 0.3658 0.3195 0.3242 -0.0236 -0.0239 0.0037  117 SER B CB  
1657 O OG  . SER B 117 ? 0.4697 0.4326 0.4331 -0.0256 -0.0222 0.0054  117 SER B OG  
1658 N N   . THR B 118 ? 0.3264 0.2782 0.2849 -0.0176 -0.0260 -0.0038 118 THR B N   
1659 C CA  . THR B 118 ? 0.3299 0.2853 0.2897 -0.0178 -0.0288 -0.0040 118 THR B CA  
1660 C C   . THR B 118 ? 0.3707 0.3189 0.3242 -0.0192 -0.0353 0.0001  118 THR B C   
1661 O O   . THR B 118 ? 0.4064 0.3435 0.3546 -0.0180 -0.0381 0.0005  118 THR B O   
1662 C CB  . THR B 118 ? 0.3770 0.3350 0.3423 -0.0139 -0.0272 -0.0076 118 THR B CB  
1663 O OG1 . THR B 118 ? 0.4885 0.4513 0.4547 -0.0149 -0.0311 -0.0067 118 THR B OG1 
1664 C CG2 . THR B 118 ? 0.3641 0.3137 0.3271 -0.0089 -0.0275 -0.0085 118 THR B CG2 
1665 N N   . THR B 119 ? 0.3338 0.2875 0.2873 -0.0220 -0.0382 0.0034  119 THR B N   
1666 C CA  . THR B 119 ? 0.3471 0.2949 0.2963 -0.0242 -0.0449 0.0090  119 THR B CA  
1667 C C   . THR B 119 ? 0.3417 0.2952 0.2921 -0.0240 -0.0477 0.0106  119 THR B C   
1668 O O   . THR B 119 ? 0.3690 0.3324 0.3216 -0.0240 -0.0449 0.0082  119 THR B O   
1669 C CB  . THR B 119 ? 0.4250 0.3751 0.3725 -0.0298 -0.0464 0.0153  119 THR B CB  
1670 O OG1 . THR B 119 ? 0.5139 0.4558 0.4583 -0.0327 -0.0539 0.0215  119 THR B OG1 
1671 C CG2 . THR B 119 ? 0.3957 0.3593 0.3450 -0.0318 -0.0431 0.0170  119 THR B CG2 
1672 N N   . ALA B 120 ? 0.3350 0.2808 0.2834 -0.0237 -0.0540 0.0148  120 ALA B N   
1673 C CA  . ALA B 120 ? 0.3378 0.2886 0.2872 -0.0239 -0.0581 0.0185  120 ALA B CA  
1674 C C   . ALA B 120 ? 0.3630 0.3138 0.3089 -0.0293 -0.0631 0.0277  120 ALA B C   
1675 O O   . ALA B 120 ? 0.3738 0.3134 0.3181 -0.0314 -0.0672 0.0314  120 ALA B O   
1676 C CB  . ALA B 120 ? 0.3599 0.3018 0.3121 -0.0183 -0.0616 0.0174  120 ALA B CB  
1677 N N   . VAL B 121 ? 0.3533 0.3171 0.2978 -0.0320 -0.0629 0.0313  121 VAL B N   
1678 C CA  . VAL B 121 ? 0.3751 0.3427 0.3168 -0.0372 -0.0673 0.0418  121 VAL B CA  
1679 C C   . VAL B 121 ? 0.3862 0.3550 0.3280 -0.0357 -0.0728 0.0454  121 VAL B C   
1680 O O   . VAL B 121 ? 0.3833 0.3626 0.3239 -0.0342 -0.0714 0.0422  121 VAL B O   
1681 C CB  . VAL B 121 ? 0.4025 0.3854 0.3409 -0.0405 -0.0616 0.0435  121 VAL B CB  
1682 C CG1 . VAL B 121 ? 0.4337 0.4227 0.3698 -0.0459 -0.0650 0.0561  121 VAL B CG1 
1683 C CG2 . VAL B 121 ? 0.4794 0.4617 0.4202 -0.0403 -0.0555 0.0387  121 VAL B CG2 
1684 N N   . VAL B 122 ? 0.3878 0.3448 0.3315 -0.0359 -0.0799 0.0519  122 VAL B N   
1685 C CA  . VAL B 122 ? 0.4349 0.3914 0.3806 -0.0338 -0.0859 0.0564  122 VAL B CA  
1686 C C   . VAL B 122 ? 0.4667 0.4265 0.4100 -0.0397 -0.0916 0.0699  122 VAL B C   
1687 O O   . VAL B 122 ? 0.4400 0.3887 0.3847 -0.0429 -0.0956 0.0759  122 VAL B O   
1688 C CB  . VAL B 122 ? 0.4514 0.3900 0.4022 -0.0278 -0.0896 0.0533  122 VAL B CB  
1689 C CG1 . VAL B 122 ? 0.5067 0.4455 0.4621 -0.0244 -0.0956 0.0584  122 VAL B CG1 
1690 C CG2 . VAL B 122 ? 0.4465 0.3836 0.3994 -0.0222 -0.0828 0.0413  122 VAL B CG2 
1691 N N   . THR B 123 ? 0.4974 0.4726 0.4368 -0.0415 -0.0921 0.0747  123 THR B N   
1692 C CA  . THR B 123 ? 0.5542 0.5363 0.4903 -0.0475 -0.0962 0.0888  123 THR B CA  
1693 C C   . THR B 123 ? 0.6388 0.6282 0.5734 -0.0466 -0.1020 0.0952  123 THR B C   
1694 O O   . THR B 123 ? 0.6469 0.6283 0.5874 -0.0417 -0.1066 0.0931  123 THR B O   
1695 C CB  . THR B 123 ? 0.6073 0.6062 0.5363 -0.0518 -0.0889 0.0904  123 THR B CB  
1696 O OG1 . THR B 123 ? 0.6964 0.7083 0.6186 -0.0492 -0.0841 0.0819  123 THR B OG1 
1697 C CG2 . THR B 123 ? 0.6255 0.6200 0.5573 -0.0531 -0.0833 0.0859  123 THR B CG2 
# 
