data_9H7K
# 
_entry.id   9H7K 
# 
_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   9H7K         pdb_00009h7k 10.2210/pdb9h7k/pdb 
WWPDB D_1292142798 ?            ?                   
# 
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                        9H7K 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.wood@ucl.ac.uk 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Wood 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4106-775X 
# 
_audit_author.name               'Chen, W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8180-366X 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Plos One' ? ? 1932-6203 ? ? 20 ? e0323816 e0323816 
'Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.' 2025 ? 
10.1371/journal.pone.0323816 40367241 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv    ? ? 2692-8205 ? ? ?  ? ?        ?        
'Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method'  2025 ? 
10.1101/2025.02.22.639275    ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, W.' 1 0000-0002-8180-366X 
1       'Chen, W.' 2 0000-0002-8180-366X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Transthyretin                               13777.360 2  ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                               40.078    3  ? ? ? ? 
3 non-polymer syn '8-(3,5-dimethyl-1H-pyrazol-4-yl)quinoline' 223.273   2  ? ? ? ? 
4 water       nat water                                       18.015    59 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        ATTR,Prealbumin,TBPA 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'                               CA    
3 '8-(3,5-dimethyl-1H-pyrazol-4-yl)quinoline' A1IS2 
4 water                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   THR n 
1 4   GLY n 
1 5   THR n 
1 6   GLY n 
1 7   GLU n 
1 8   SER n 
1 9   LYS n 
1 10  CYS n 
1 11  PRO n 
1 12  LEU n 
1 13  MET n 
1 14  VAL n 
1 15  LYS n 
1 16  VAL n 
1 17  LEU n 
1 18  ASP n 
1 19  ALA n 
1 20  VAL n 
1 21  ARG n 
1 22  GLY n 
1 23  SER n 
1 24  PRO n 
1 25  ALA n 
1 26  ILE n 
1 27  ASN n 
1 28  VAL n 
1 29  ALA n 
1 30  VAL n 
1 31  HIS n 
1 32  VAL n 
1 33  PHE n 
1 34  ARG n 
1 35  LYS n 
1 36  ALA n 
1 37  ALA n 
1 38  ASP n 
1 39  ASP n 
1 40  THR n 
1 41  TRP n 
1 42  GLU n 
1 43  PRO n 
1 44  PHE n 
1 45  ALA n 
1 46  SER n 
1 47  GLY n 
1 48  LYS n 
1 49  THR n 
1 50  SER n 
1 51  GLU n 
1 52  SER n 
1 53  GLY n 
1 54  GLU n 
1 55  LEU n 
1 56  HIS n 
1 57  GLY n 
1 58  LEU n 
1 59  THR n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  GLU n 
1 64  PHE n 
1 65  VAL n 
1 66  GLU n 
1 67  GLY n 
1 68  ILE n 
1 69  TYR n 
1 70  LYS n 
1 71  VAL n 
1 72  GLU n 
1 73  ILE n 
1 74  ASP n 
1 75  THR n 
1 76  LYS n 
1 77  SER n 
1 78  TYR n 
1 79  TRP n 
1 80  LYS n 
1 81  ALA n 
1 82  LEU n 
1 83  GLY n 
1 84  ILE n 
1 85  SER n 
1 86  PRO n 
1 87  PHE n 
1 88  HIS n 
1 89  GLU n 
1 90  HIS n 
1 91  ALA n 
1 92  GLU n 
1 93  VAL n 
1 94  VAL n 
1 95  PHE n 
1 96  THR n 
1 97  ALA n 
1 98  ASN n 
1 99  ASP n 
1 100 SER n 
1 101 GLY n 
1 102 PRO n 
1 103 ARG n 
1 104 ARG n 
1 105 TYR n 
1 106 THR n 
1 107 ILE n 
1 108 ALA n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 SER n 
1 113 PRO n 
1 114 TYR n 
1 115 SER n 
1 116 TYR n 
1 117 SER n 
1 118 THR n 
1 119 THR n 
1 120 ALA n 
1 121 VAL n 
1 122 VAL n 
1 123 THR n 
1 124 ASN n 
1 125 PRO n 
1 126 LYS n 
1 127 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   127 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTR, PALB' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    Blood 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IS2 non-polymer         . '8-(3,5-dimethyl-1H-pyrazol-4-yl)quinoline' ? 'C14 H13 N3'     223.273 
ALA   'L-peptide linking' y ALANINE                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                             ? 'C4 H7 N O4'     133.103 
CA    non-polymer         . 'CALCIUM ION'                               ? 'Ca 2'           40.078  
CYS   'L-peptide linking' y CYSTEINE                                    ? 'C3 H7 N O2 S'   121.158 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                      ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                  ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                               ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                     ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                      ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                   ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                  ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                      ? 'C5 H11 N O2'    117.146 
# 
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  ?   ?   ?   A . n 
A 1 40  THR 40  40  ?   ?   ?   A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  CYS 10  10  10  CYS CYS B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  ?   ?   ?   B . n 
B 1 37  ALA 37  37  ?   ?   ?   B . n 
B 1 38  ASP 38  38  ?   ?   ?   B . n 
B 1 39  ASP 39  39  ?   ?   ?   B . n 
B 1 40  THR 40  40  ?   ?   ?   B . n 
B 1 41  TRP 41  41  ?   ?   ?   B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  PHE 44  44  44  PHE PHE B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  ?   ?   ?   B . n 
B 1 100 SER 100 100 ?   ?   ?   B . n 
B 1 101 GLY 101 101 ?   ?   ?   B . n 
B 1 102 PRO 102 102 ?   ?   ?   B . n 
B 1 103 ARG 103 103 ?   ?   ?   B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 THR 123 123 ?   ?   ?   B . n 
B 1 124 ASN 124 124 ?   ?   ?   B . n 
B 1 125 PRO 125 125 ?   ?   ?   B . n 
B 1 126 LYS 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IS2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IS2 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CA    1  201 1  CA    CA  A . 
D 3 A1IS2 1  202 1  A1IS2 297 A . 
E 2 CA    1  203 1  CA    CA  A . 
F 2 CA    1  201 1  CA    CA  B . 
G 3 A1IS2 1  202 1  A1IS2 297 B . 
H 4 HOH   1  301 22 HOH   HOH A . 
H 4 HOH   2  302 46 HOH   HOH A . 
H 4 HOH   3  303 23 HOH   HOH A . 
H 4 HOH   4  304 52 HOH   HOH A . 
H 4 HOH   5  305 33 HOH   HOH A . 
H 4 HOH   6  306 6  HOH   HOH A . 
H 4 HOH   7  307 30 HOH   HOH A . 
H 4 HOH   8  308 44 HOH   HOH A . 
H 4 HOH   9  309 57 HOH   HOH A . 
H 4 HOH   10 310 53 HOH   HOH A . 
H 4 HOH   11 311 39 HOH   HOH A . 
H 4 HOH   12 312 8  HOH   HOH A . 
H 4 HOH   13 313 18 HOH   HOH A . 
H 4 HOH   14 314 17 HOH   HOH A . 
H 4 HOH   15 315 38 HOH   HOH A . 
H 4 HOH   16 316 47 HOH   HOH A . 
H 4 HOH   17 317 11 HOH   HOH A . 
H 4 HOH   18 318 45 HOH   HOH A . 
H 4 HOH   19 319 10 HOH   HOH A . 
H 4 HOH   20 320 25 HOH   HOH A . 
H 4 HOH   21 321 37 HOH   HOH A . 
H 4 HOH   22 322 24 HOH   HOH A . 
H 4 HOH   23 323 12 HOH   HOH A . 
H 4 HOH   24 324 41 HOH   HOH A . 
H 4 HOH   25 325 32 HOH   HOH A . 
H 4 HOH   26 326 16 HOH   HOH A . 
H 4 HOH   27 327 14 HOH   HOH A . 
H 4 HOH   28 328 9  HOH   HOH A . 
H 4 HOH   29 329 48 HOH   HOH A . 
H 4 HOH   30 330 28 HOH   HOH A . 
H 4 HOH   31 331 55 HOH   HOH A . 
H 4 HOH   32 332 1  HOH   HOH A . 
H 4 HOH   33 333 56 HOH   HOH A . 
H 4 HOH   34 334 35 HOH   HOH A . 
H 4 HOH   35 335 4  HOH   HOH A . 
H 4 HOH   36 336 59 HOH   HOH A . 
H 4 HOH   37 337 27 HOH   HOH A . 
H 4 HOH   38 338 40 HOH   HOH A . 
H 4 HOH   39 339 43 HOH   HOH A . 
H 4 HOH   40 340 58 HOH   HOH A . 
H 4 HOH   41 341 34 HOH   HOH A . 
H 4 HOH   42 342 54 HOH   HOH A . 
H 4 HOH   43 343 26 HOH   HOH A . 
H 4 HOH   44 344 20 HOH   HOH A . 
I 4 HOH   1  301 42 HOH   HOH B . 
I 4 HOH   2  302 2  HOH   HOH B . 
I 4 HOH   3  303 51 HOH   HOH B . 
I 4 HOH   4  304 29 HOH   HOH B . 
I 4 HOH   5  305 21 HOH   HOH B . 
I 4 HOH   6  306 19 HOH   HOH B . 
I 4 HOH   7  307 7  HOH   HOH B . 
I 4 HOH   8  308 3  HOH   HOH B . 
I 4 HOH   9  309 5  HOH   HOH B . 
I 4 HOH   10 310 36 HOH   HOH B . 
I 4 HOH   11 311 15 HOH   HOH B . 
I 4 HOH   12 312 50 HOH   HOH B . 
I 4 HOH   13 313 31 HOH   HOH B . 
I 4 HOH   14 314 13 HOH   HOH B . 
I 4 HOH   15 315 49 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 LYS 15  ? CD  ? A LYS 15  CD  
2  1 Y 1 A LYS 15  ? CE  ? A LYS 15  CE  
3  1 Y 1 A LYS 15  ? NZ  ? A LYS 15  NZ  
4  1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
5  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
6  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
7  1 Y 1 A GLU 61  ? CG  ? A GLU 61  CG  
8  1 Y 1 A GLU 61  ? CD  ? A GLU 61  CD  
9  1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
10 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
11 1 Y 1 A LYS 76  ? CD  ? A LYS 76  CD  
12 1 Y 1 A LYS 76  ? CE  ? A LYS 76  CE  
13 1 Y 1 A LYS 76  ? NZ  ? A LYS 76  NZ  
14 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
15 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
16 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
17 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
18 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
19 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
20 1 Y 1 A ASN 124 ? ND2 ? A ASN 124 ND2 
21 1 Y 1 B CYS 10  ? CB  ? B CYS 10  CB  
22 1 Y 1 B CYS 10  ? SG  ? B CYS 10  SG  
23 1 Y 1 B ASN 27  ? ND2 ? B ASN 27  ND2 
24 1 Y 1 B ARG 34  ? CG  ? B ARG 34  CG  
25 1 Y 1 B ARG 34  ? CD  ? B ARG 34  CD  
26 1 Y 1 B ARG 34  ? NE  ? B ARG 34  NE  
27 1 Y 1 B ARG 34  ? CZ  ? B ARG 34  CZ  
28 1 Y 1 B ARG 34  ? NH1 ? B ARG 34  NH1 
29 1 Y 1 B ARG 34  ? NH2 ? B ARG 34  NH2 
30 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
31 1 Y 1 B GLU 42  ? CG  ? B GLU 42  CG  
32 1 Y 1 B GLU 42  ? CD  ? B GLU 42  CD  
33 1 Y 1 B GLU 42  ? OE1 ? B GLU 42  OE1 
34 1 Y 1 B GLU 42  ? OE2 ? B GLU 42  OE2 
35 1 Y 1 B LYS 48  ? NZ  ? B LYS 48  NZ  
36 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
37 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
38 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
39 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
40 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
41 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
42 1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
43 1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
44 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
45 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
46 1 Y 1 B LYS 70  ? CE  ? B LYS 70  CE  
47 1 Y 1 B LYS 70  ? NZ  ? B LYS 70  NZ  
48 1 Y 1 B LYS 80  ? NZ  ? B LYS 80  NZ  
49 1 Y 1 B LEU 82  ? CD1 ? B LEU 82  CD1 
50 1 Y 1 B THR 96  ? CG2 ? B THR 96  CG2 
51 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
52 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
53 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
54 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
55 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
56 1 Y 1 B ARG 104 ? NH2 ? B ARG 104 NH2 
57 1 Y 1 B VAL 122 ? CG1 ? B VAL 122 CG1 
58 1 Y 1 B VAL 122 ? CG2 ? B VAL 122 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC         ? ? ? 5.7.0029 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .        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                     9H7K 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.107 
_cell.length_a_esd                 ? 
_cell.length_b                     63.069 
_cell.length_b_esd                 ? 
_cell.length_c                     83.837 
_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                         9H7K 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 2 21' 
_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                   9H7K 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES, 200 mM CaCl2, 28% v/v PEG400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'APEX II CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-10-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.542 
_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                      'SEALED TUBE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER D8 QUEST' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.542 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7K 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               63.07 
_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                                     29346 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.07 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.78 
_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                                0.022 
_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                              0.043 
_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                                    1.6 
_reflns_shell.d_res_low                                     1.638 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1919 
_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                               0.145 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.176 
_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]                            0.59 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.37 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.22 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               15.248 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.919 
_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                                 9H7K 
_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                            1.60 
_refine.ls_d_res_low                             50.40 
_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                     27814 
_refine.ls_number_reflns_R_free                  1492 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.63 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17925 
_refine.ls_R_factor_R_free                       0.23552 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17631 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.109 
_refine.pdbx_overall_ESU_R_Free                  0.096 
_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                             4.133 
_refine.overall_SU_ML                            0.066 
_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                       1.60 
_refine_hist.d_res_low                        50.40 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               1710 
_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        1614 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.020  0.019  1728 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1551 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.962  1.963  2366 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.859  3.000  3573 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.408  5.000  220  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.108 23.667 60   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.366 15.000 241  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.734 15.000 4    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.107  0.200  269  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.021  1921 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  382  ? 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' ? 4.935  3.000  3279 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 21.215 5.000  17   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 14.026 5.000  3273 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.60 
_refine_ls_shell.d_res_low                        1.638 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             99 
_refine_ls_shell.number_reflns_R_work             1919 
_refine_ls_shell.percent_reflns_obs               92.65 
_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                  0.175 
_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   ? 
_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                  0.311 
# 
_struct.entry_id                     9H7K 
_struct.title                        'Human Transthyretin in Complex with 8-(3,5-dimethyl-1H-pyrazol-4-yl)quinoline' 
_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        9H7K 
_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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TTHY_HUMAN 
_struct_ref.pdbx_db_accession          P02766 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_struct_ref.pdbx_align_begin           21 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9H7K A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7K 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)' 8570  ? 
1 MORE         -73   ? 
1 'SSA (A^2)'  16760 ? 
# 
_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,F,G,H,I 
# 
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_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 41.1070000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 74 ? LEU A 82 ? ASP A 74 LEU A 82 1 ? 9 
HELX_P HELX_P2 AA2 ASP B 74 ? LEU B 82 ? ASP B 74 LEU B 82 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 66 OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 66  A CA  201 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc2  metalc ? ? A ASP 99 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc3  metalc ? ? A ASP 99 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc4  metalc ? ? C CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  201 A HOH 323 1_555 ? ? ? ? ? ? ? 2.537 ? ? 
metalc5  metalc ? ? C CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  201 A HOH 327 3_454 ? ? ? ? ? ? ? 2.295 ? ? 
metalc6  metalc ? ? C CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  201 A HOH 333 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc7  metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  203 A HOH 308 3_554 ? ? ? ? ? ? ? 2.380 ? ? 
metalc8  metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  203 A HOH 309 3_554 ? ? ? ? ? ? ? 2.416 ? ? 
metalc9  metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  203 A HOH 318 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc10 metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  203 A HOH 331 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc11 metalc ? ? B PHE 44 O   ? ? ? 1_555 F CA  . CA ? ? B PHE 44  B CA  201 1_555 ? ? ? ? ? ? ? 2.656 ? ? 
metalc12 metalc ? ? B GLU 66 OE2 ? ? ? 1_555 F CA  . CA ? ? B GLU 66  B CA  201 3_544 ? ? ? ? ? ? ? 2.190 ? ? 
metalc13 metalc ? ? B ASN 98 OD1 ? ? ? 1_555 F CA  . CA ? ? B ASN 98  B CA  201 3_544 ? ? ? ? ? ? ? 2.921 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? A ASP 99 ? A ASP 99  ? 1_555 91.0  ? 
2  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 86.8  ? 
3  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 72.4  ? 
4  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 323 ? 1_555 80.8  ? 
5  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 323 ? 1_555 136.1 ? 
6  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 323 ? 1_555 148.6 ? 
7  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 327 ? 3_454 156.0 ? 
8  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 327 ? 3_454 109.7 ? 
9  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 327 ? 3_454 87.9  ? 
10 O   ? H HOH .  ? A HOH 323 ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 327 ? 3_454 91.8  ? 
11 OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 333 ? 1_555 132.2 ? 
12 O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 333 ? 1_555 75.0  ? 
13 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 333 ? 1_555 128.9 ? 
14 O   ? H HOH .  ? A HOH 323 ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 333 ? 1_555 79.1  ? 
15 O   ? H HOH .  ? A HOH 327 ? 3_454 CA ? C CA . ? A CA 201 ? 1_555 O   ? H HOH .  ? A HOH 333 ? 1_555 67.4  ? 
16 O   ? H HOH .  ? A HOH 308 ? 3_554 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 309 ? 3_554 76.5  ? 
17 O   ? H HOH .  ? A HOH 308 ? 3_554 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 318 ? 1_555 89.3  ? 
18 O   ? H HOH .  ? A HOH 309 ? 3_554 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 318 ? 1_555 132.3 ? 
19 O   ? H HOH .  ? A HOH 308 ? 3_554 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 331 ? 1_555 133.1 ? 
20 O   ? H HOH .  ? A HOH 309 ? 3_554 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 331 ? 1_555 73.4  ? 
21 O   ? H HOH .  ? A HOH 318 ? 1_555 CA ? E CA . ? A CA 203 ? 1_555 O   ? H HOH .  ? A HOH 331 ? 1_555 85.2  ? 
22 O   ? B PHE 44 ? B PHE 44  ? 1_555 CA ? F CA . ? B CA 201 ? 1_555 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 43.1  ? 
23 O   ? B PHE 44 ? B PHE 44  ? 1_555 CA ? F CA . ? B CA 201 ? 1_555 OD1 ? B ASN 98 ? B ASN 98  ? 1_555 36.2  ? 
24 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? F CA . ? B CA 201 ? 1_555 OD1 ? B ASN 98 ? B ASN 98  ? 1_555 8.2   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? VAL B 121 ? SER B 115 VAL B 121 
AA1 6 TYR B 105 ? SER B 112 ? TYR B 105 SER B 112 
AA1 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA1 8 SER B 23  ? PRO B 24  ? SER B 23  PRO B 24  
AA2 1 GLU A 54  ? LEU A 55  ? GLU A 54  LEU A 55  
AA2 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA2 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA2 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA2 5 SER B 115 ? VAL B 121 ? SER B 115 VAL B 121 
AA2 6 TYR B 105 ? SER B 112 ? TYR B 105 SER B 112 
AA2 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA2 8 GLU B 54  ? LEU B 55  ? GLU B 54  LEU B 55  
AA3 1 GLU A 42  ? LYS A 48  ? GLU A 42  LYS A 48  
AA3 2 ALA A 29  ? LYS A 35  ? ALA A 29  LYS A 35  
AA3 3 GLY A 67  ? ILE A 73  ? GLY A 67  ILE A 73  
AA3 4 HIS A 88  ? ALA A 97  ? HIS A 88  ALA A 97  
AA3 5 ALA B 91  ? ALA B 97  ? ALA B 91  ALA B 97  
AA3 6 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA3 7 ALA B 29  ? ARG B 34  ? ALA B 29  ARG B 34  
AA3 8 PRO B 43  ? LYS B 48  ? PRO B 43  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 MET A 13  ? N MET A 13  O ILE A 107 ? O ILE A 107 
AA1 3 4 N ARG A 104 ? N ARG A 104 O THR A 123 ? O THR A 123 
AA1 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA1 5 6 O SER B 117 ? O SER B 117 N LEU B 110 ? N LEU B 110 
AA1 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N MET A 13  ? N MET A 13  O ILE A 107 ? O ILE A 107 
AA2 3 4 N ARG A 104 ? N ARG A 104 O THR A 123 ? O THR A 123 
AA2 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA2 5 6 O SER B 117 ? O SER B 117 N LEU B 110 ? N LEU B 110 
AA2 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N ILE A 73  ? N ILE A 73  O ALA A 91  ? O ALA A 91  
AA3 4 5 N GLU A 89  ? N GLU A 89  O VAL B 94  ? O VAL B 94  
AA3 5 6 O ALA B 97  ? O ALA B 97  N GLY B 67  ? N GLY B 67  
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                   9H7K 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 92 ? B OH A TYR 116 ? ? 1.51 
2 1 OE2 A GLU 92 ? B O  A HOH 301 ? ? 2.14 
3 1 OE1 A GLU 92 ? B O  B GLU 92  ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             35 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             35 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.356 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.127 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 34 ? ? CZ A ARG 34 ? ? NH1 A ARG 34 ? ? 124.83 120.30 4.53  0.50 N 
2 1 NE A ARG 34 ? ? CZ A ARG 34 ? ? NH2 A ARG 34 ? ? 115.81 120.30 -4.49 0.50 N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A A1IS2 202 ? D A1IS2 . 
2 1 A A1IS2 202 ? D A1IS2 . 
3 1 B A1IS2 202 ? G A1IS2 . 
4 1 B A1IS2 202 ? G A1IS2 . 
5 1 B HOH   315 ? I HOH   . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A GLY 4   ? A GLY 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A LYS 9   ? A LYS 9   
10 1 Y 1 A ASP 39  ? A ASP 39  
11 1 Y 1 A THR 40  ? A THR 40  
12 1 Y 1 A LYS 126 ? A LYS 126 
13 1 Y 1 A GLU 127 ? A GLU 127 
14 1 Y 1 B GLY 1   ? B GLY 1   
15 1 Y 1 B PRO 2   ? B PRO 2   
16 1 Y 1 B THR 3   ? B THR 3   
17 1 Y 1 B GLY 4   ? B GLY 4   
18 1 Y 1 B THR 5   ? B THR 5   
19 1 Y 1 B GLY 6   ? B GLY 6   
20 1 Y 1 B GLU 7   ? B GLU 7   
21 1 Y 1 B SER 8   ? B SER 8   
22 1 Y 1 B LYS 9   ? B LYS 9   
23 1 Y 1 B ALA 36  ? B ALA 36  
24 1 Y 1 B ALA 37  ? B ALA 37  
25 1 Y 1 B ASP 38  ? B ASP 38  
26 1 Y 1 B ASP 39  ? B ASP 39  
27 1 Y 1 B THR 40  ? B THR 40  
28 1 Y 1 B TRP 41  ? B TRP 41  
29 1 Y 1 B ASP 99  ? B ASP 99  
30 1 Y 1 B SER 100 ? B SER 100 
31 1 Y 1 B GLY 101 ? B GLY 101 
32 1 Y 1 B PRO 102 ? B PRO 102 
33 1 Y 1 B ARG 103 ? B ARG 103 
34 1 Y 1 B THR 123 ? B THR 123 
35 1 Y 1 B ASN 124 ? B ASN 124 
36 1 Y 1 B PRO 125 ? B PRO 125 
37 1 Y 1 B LYS 126 ? B LYS 126 
38 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 
A1IS2 N1   N  Y N 1   
A1IS2 C2   C  Y N 2   
A1IS2 C3   C  N N 3   
A1IS2 C4   C  N N 4   
A1IS2 C5   C  Y N 5   
A1IS2 C6   C  Y N 6   
A1IS2 C7   C  Y N 7   
A1IS2 C8   C  Y N 8   
A1IS2 C9   C  Y N 9   
A1IS2 C10  C  Y N 10  
A1IS2 C11  C  Y N 11  
A1IS2 C12  C  Y N 12  
A1IS2 C13  C  Y N 13  
A1IS2 C1   C  Y N 14  
A1IS2 N    N  Y N 15  
A1IS2 C    C  Y N 16  
A1IS2 N2   N  Y N 17  
A1IS2 H1   H  N N 18  
A1IS2 H2   H  N N 19  
A1IS2 H3   H  N N 20  
A1IS2 H4   H  N N 21  
A1IS2 H5   H  N N 22  
A1IS2 H6   H  N N 23  
A1IS2 H7   H  N N 24  
A1IS2 H8   H  N N 25  
A1IS2 H9   H  N N 26  
A1IS2 H10  H  N N 27  
A1IS2 H11  H  N N 28  
A1IS2 H12  H  N N 29  
A1IS2 H13  H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CA    CA   CA N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
GLU   N    N  N N 119 
GLU   CA   C  N S 120 
GLU   C    C  N N 121 
GLU   O    O  N N 122 
GLU   CB   C  N N 123 
GLU   CG   C  N N 124 
GLU   CD   C  N N 125 
GLU   OE1  O  N N 126 
GLU   OE2  O  N N 127 
GLU   OXT  O  N N 128 
GLU   H    H  N N 129 
GLU   H2   H  N N 130 
GLU   HA   H  N N 131 
GLU   HB2  H  N N 132 
GLU   HB3  H  N N 133 
GLU   HG2  H  N N 134 
GLU   HG3  H  N N 135 
GLU   HE2  H  N N 136 
GLU   HXT  H  N N 137 
GLY   N    N  N N 138 
GLY   CA   C  N N 139 
GLY   C    C  N N 140 
GLY   O    O  N N 141 
GLY   OXT  O  N N 142 
GLY   H    H  N N 143 
GLY   H2   H  N N 144 
GLY   HA2  H  N N 145 
GLY   HA3  H  N N 146 
GLY   HXT  H  N N 147 
HIS   N    N  N N 148 
HIS   CA   C  N S 149 
HIS   C    C  N N 150 
HIS   O    O  N N 151 
HIS   CB   C  N N 152 
HIS   CG   C  Y N 153 
HIS   ND1  N  Y N 154 
HIS   CD2  C  Y N 155 
HIS   CE1  C  Y N 156 
HIS   NE2  N  Y N 157 
HIS   OXT  O  N N 158 
HIS   H    H  N N 159 
HIS   H2   H  N N 160 
HIS   HA   H  N N 161 
HIS   HB2  H  N N 162 
HIS   HB3  H  N N 163 
HIS   HD1  H  N N 164 
HIS   HD2  H  N N 165 
HIS   HE1  H  N N 166 
HIS   HE2  H  N N 167 
HIS   HXT  H  N N 168 
HOH   O    O  N N 169 
HOH   H1   H  N N 170 
HOH   H2   H  N N 171 
ILE   N    N  N N 172 
ILE   CA   C  N S 173 
ILE   C    C  N N 174 
ILE   O    O  N N 175 
ILE   CB   C  N S 176 
ILE   CG1  C  N N 177 
ILE   CG2  C  N N 178 
ILE   CD1  C  N N 179 
ILE   OXT  O  N N 180 
ILE   H    H  N N 181 
ILE   H2   H  N N 182 
ILE   HA   H  N N 183 
ILE   HB   H  N N 184 
ILE   HG12 H  N N 185 
ILE   HG13 H  N N 186 
ILE   HG21 H  N N 187 
ILE   HG22 H  N N 188 
ILE   HG23 H  N N 189 
ILE   HD11 H  N N 190 
ILE   HD12 H  N N 191 
ILE   HD13 H  N N 192 
ILE   HXT  H  N N 193 
LEU   N    N  N N 194 
LEU   CA   C  N S 195 
LEU   C    C  N N 196 
LEU   O    O  N N 197 
LEU   CB   C  N N 198 
LEU   CG   C  N N 199 
LEU   CD1  C  N N 200 
LEU   CD2  C  N N 201 
LEU   OXT  O  N N 202 
LEU   H    H  N N 203 
LEU   H2   H  N N 204 
LEU   HA   H  N N 205 
LEU   HB2  H  N N 206 
LEU   HB3  H  N N 207 
LEU   HG   H  N N 208 
LEU   HD11 H  N N 209 
LEU   HD12 H  N N 210 
LEU   HD13 H  N N 211 
LEU   HD21 H  N N 212 
LEU   HD22 H  N N 213 
LEU   HD23 H  N N 214 
LEU   HXT  H  N N 215 
LYS   N    N  N N 216 
LYS   CA   C  N S 217 
LYS   C    C  N N 218 
LYS   O    O  N N 219 
LYS   CB   C  N N 220 
LYS   CG   C  N N 221 
LYS   CD   C  N N 222 
LYS   CE   C  N N 223 
LYS   NZ   N  N N 224 
LYS   OXT  O  N N 225 
LYS   H    H  N N 226 
LYS   H2   H  N N 227 
LYS   HA   H  N N 228 
LYS   HB2  H  N N 229 
LYS   HB3  H  N N 230 
LYS   HG2  H  N N 231 
LYS   HG3  H  N N 232 
LYS   HD2  H  N N 233 
LYS   HD3  H  N N 234 
LYS   HE2  H  N N 235 
LYS   HE3  H  N N 236 
LYS   HZ1  H  N N 237 
LYS   HZ2  H  N N 238 
LYS   HZ3  H  N N 239 
LYS   HXT  H  N N 240 
MET   N    N  N N 241 
MET   CA   C  N S 242 
MET   C    C  N N 243 
MET   O    O  N N 244 
MET   CB   C  N N 245 
MET   CG   C  N N 246 
MET   SD   S  N N 247 
MET   CE   C  N N 248 
MET   OXT  O  N N 249 
MET   H    H  N N 250 
MET   H2   H  N N 251 
MET   HA   H  N N 252 
MET   HB2  H  N N 253 
MET   HB3  H  N N 254 
MET   HG2  H  N N 255 
MET   HG3  H  N N 256 
MET   HE1  H  N N 257 
MET   HE2  H  N N 258 
MET   HE3  H  N N 259 
MET   HXT  H  N N 260 
PHE   N    N  N N 261 
PHE   CA   C  N S 262 
PHE   C    C  N N 263 
PHE   O    O  N N 264 
PHE   CB   C  N N 265 
PHE   CG   C  Y N 266 
PHE   CD1  C  Y N 267 
PHE   CD2  C  Y N 268 
PHE   CE1  C  Y N 269 
PHE   CE2  C  Y N 270 
PHE   CZ   C  Y N 271 
PHE   OXT  O  N N 272 
PHE   H    H  N N 273 
PHE   H2   H  N N 274 
PHE   HA   H  N N 275 
PHE   HB2  H  N N 276 
PHE   HB3  H  N N 277 
PHE   HD1  H  N N 278 
PHE   HD2  H  N N 279 
PHE   HE1  H  N N 280 
PHE   HE2  H  N N 281 
PHE   HZ   H  N N 282 
PHE   HXT  H  N N 283 
PRO   N    N  N N 284 
PRO   CA   C  N S 285 
PRO   C    C  N N 286 
PRO   O    O  N N 287 
PRO   CB   C  N N 288 
PRO   CG   C  N N 289 
PRO   CD   C  N N 290 
PRO   OXT  O  N N 291 
PRO   H    H  N N 292 
PRO   HA   H  N N 293 
PRO   HB2  H  N N 294 
PRO   HB3  H  N N 295 
PRO   HG2  H  N N 296 
PRO   HG3  H  N N 297 
PRO   HD2  H  N N 298 
PRO   HD3  H  N N 299 
PRO   HXT  H  N N 300 
SER   N    N  N N 301 
SER   CA   C  N S 302 
SER   C    C  N N 303 
SER   O    O  N N 304 
SER   CB   C  N N 305 
SER   OG   O  N N 306 
SER   OXT  O  N N 307 
SER   H    H  N N 308 
SER   H2   H  N N 309 
SER   HA   H  N N 310 
SER   HB2  H  N N 311 
SER   HB3  H  N N 312 
SER   HG   H  N N 313 
SER   HXT  H  N N 314 
THR   N    N  N N 315 
THR   CA   C  N S 316 
THR   C    C  N N 317 
THR   O    O  N N 318 
THR   CB   C  N R 319 
THR   OG1  O  N N 320 
THR   CG2  C  N N 321 
THR   OXT  O  N N 322 
THR   H    H  N N 323 
THR   H2   H  N N 324 
THR   HA   H  N N 325 
THR   HB   H  N N 326 
THR   HG1  H  N N 327 
THR   HG21 H  N N 328 
THR   HG22 H  N N 329 
THR   HG23 H  N N 330 
THR   HXT  H  N N 331 
TRP   N    N  N N 332 
TRP   CA   C  N S 333 
TRP   C    C  N N 334 
TRP   O    O  N N 335 
TRP   CB   C  N N 336 
TRP   CG   C  Y N 337 
TRP   CD1  C  Y N 338 
TRP   CD2  C  Y N 339 
TRP   NE1  N  Y N 340 
TRP   CE2  C  Y N 341 
TRP   CE3  C  Y N 342 
TRP   CZ2  C  Y N 343 
TRP   CZ3  C  Y N 344 
TRP   CH2  C  Y N 345 
TRP   OXT  O  N N 346 
TRP   H    H  N N 347 
TRP   H2   H  N N 348 
TRP   HA   H  N N 349 
TRP   HB2  H  N N 350 
TRP   HB3  H  N N 351 
TRP   HD1  H  N N 352 
TRP   HE1  H  N N 353 
TRP   HE3  H  N N 354 
TRP   HZ2  H  N N 355 
TRP   HZ3  H  N N 356 
TRP   HH2  H  N N 357 
TRP   HXT  H  N N 358 
TYR   N    N  N N 359 
TYR   CA   C  N S 360 
TYR   C    C  N N 361 
TYR   O    O  N N 362 
TYR   CB   C  N N 363 
TYR   CG   C  Y N 364 
TYR   CD1  C  Y N 365 
TYR   CD2  C  Y N 366 
TYR   CE1  C  Y N 367 
TYR   CE2  C  Y N 368 
TYR   CZ   C  Y N 369 
TYR   OH   O  N N 370 
TYR   OXT  O  N N 371 
TYR   H    H  N N 372 
TYR   H2   H  N N 373 
TYR   HA   H  N N 374 
TYR   HB2  H  N N 375 
TYR   HB3  H  N N 376 
TYR   HD1  H  N N 377 
TYR   HD2  H  N N 378 
TYR   HE1  H  N N 379 
TYR   HE2  H  N N 380 
TYR   HH   H  N N 381 
TYR   HXT  H  N N 382 
VAL   N    N  N N 383 
VAL   CA   C  N S 384 
VAL   C    C  N N 385 
VAL   O    O  N N 386 
VAL   CB   C  N N 387 
VAL   CG1  C  N N 388 
VAL   CG2  C  N N 389 
VAL   OXT  O  N N 390 
VAL   H    H  N N 391 
VAL   H2   H  N N 392 
VAL   HA   H  N N 393 
VAL   HB   H  N N 394 
VAL   HG11 H  N N 395 
VAL   HG12 H  N N 396 
VAL   HG13 H  N N 397 
VAL   HG21 H  N N 398 
VAL   HG22 H  N N 399 
VAL   HG23 H  N N 400 
VAL   HXT  H  N N 401 
# 
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 
A1IS2 C3  C2   sing N N 1   
A1IS2 C7  C6   sing Y N 2   
A1IS2 C7  C8   doub Y N 3   
A1IS2 C2  N1   sing Y N 4   
A1IS2 C2  C    doub Y N 5   
A1IS2 C6  C5   doub Y N 6   
A1IS2 C8  C9   sing Y N 7   
A1IS2 N1  N    sing Y N 8   
A1IS2 C5  C    sing N N 9   
A1IS2 C5  C10  sing Y N 10  
A1IS2 C   C1   sing Y N 11  
A1IS2 C9  C10  doub Y N 12  
A1IS2 C9  C13  sing Y N 13  
A1IS2 C10 N2   sing Y N 14  
A1IS2 C13 C12  doub Y N 15  
A1IS2 N   C1   doub Y N 16  
A1IS2 N2  C11  doub Y N 17  
A1IS2 C1  C4   sing N N 18  
A1IS2 C12 C11  sing Y N 19  
A1IS2 N1  H1   sing N N 20  
A1IS2 C3  H2   sing N N 21  
A1IS2 C3  H3   sing N N 22  
A1IS2 C3  H4   sing N N 23  
A1IS2 C4  H5   sing N N 24  
A1IS2 C4  H6   sing N N 25  
A1IS2 C4  H7   sing N N 26  
A1IS2 C6  H8   sing N N 27  
A1IS2 C7  H9   sing N N 28  
A1IS2 C8  H10  sing N N 29  
A1IS2 C11 H11  sing N N 30  
A1IS2 C12 H12  sing N N 31  
A1IS2 C13 H13  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLU   N   CA   sing N N 115 
GLU   N   H    sing N N 116 
GLU   N   H2   sing N N 117 
GLU   CA  C    sing N N 118 
GLU   CA  CB   sing N N 119 
GLU   CA  HA   sing N N 120 
GLU   C   O    doub N N 121 
GLU   C   OXT  sing N N 122 
GLU   CB  CG   sing N N 123 
GLU   CB  HB2  sing N N 124 
GLU   CB  HB3  sing N N 125 
GLU   CG  CD   sing N N 126 
GLU   CG  HG2  sing N N 127 
GLU   CG  HG3  sing N N 128 
GLU   CD  OE1  doub N N 129 
GLU   CD  OE2  sing N N 130 
GLU   OE2 HE2  sing N N 131 
GLU   OXT HXT  sing N N 132 
GLY   N   CA   sing N N 133 
GLY   N   H    sing N N 134 
GLY   N   H2   sing N N 135 
GLY   CA  C    sing N N 136 
GLY   CA  HA2  sing N N 137 
GLY   CA  HA3  sing N N 138 
GLY   C   O    doub N N 139 
GLY   C   OXT  sing N N 140 
GLY   OXT HXT  sing N N 141 
HIS   N   CA   sing N N 142 
HIS   N   H    sing N N 143 
HIS   N   H2   sing N N 144 
HIS   CA  C    sing N N 145 
HIS   CA  CB   sing N N 146 
HIS   CA  HA   sing N N 147 
HIS   C   O    doub N N 148 
HIS   C   OXT  sing N N 149 
HIS   CB  CG   sing N N 150 
HIS   CB  HB2  sing N N 151 
HIS   CB  HB3  sing N N 152 
HIS   CG  ND1  sing Y N 153 
HIS   CG  CD2  doub Y N 154 
HIS   ND1 CE1  doub Y N 155 
HIS   ND1 HD1  sing N N 156 
HIS   CD2 NE2  sing Y N 157 
HIS   CD2 HD2  sing N N 158 
HIS   CE1 NE2  sing Y N 159 
HIS   CE1 HE1  sing N N 160 
HIS   NE2 HE2  sing N N 161 
HIS   OXT HXT  sing N N 162 
HOH   O   H1   sing N N 163 
HOH   O   H2   sing N N 164 
ILE   N   CA   sing N N 165 
ILE   N   H    sing N N 166 
ILE   N   H2   sing N N 167 
ILE   CA  C    sing N N 168 
ILE   CA  CB   sing N N 169 
ILE   CA  HA   sing N N 170 
ILE   C   O    doub N N 171 
ILE   C   OXT  sing N N 172 
ILE   CB  CG1  sing N N 173 
ILE   CB  CG2  sing N N 174 
ILE   CB  HB   sing N N 175 
ILE   CG1 CD1  sing N N 176 
ILE   CG1 HG12 sing N N 177 
ILE   CG1 HG13 sing N N 178 
ILE   CG2 HG21 sing N N 179 
ILE   CG2 HG22 sing N N 180 
ILE   CG2 HG23 sing N N 181 
ILE   CD1 HD11 sing N N 182 
ILE   CD1 HD12 sing N N 183 
ILE   CD1 HD13 sing N N 184 
ILE   OXT HXT  sing N N 185 
LEU   N   CA   sing N N 186 
LEU   N   H    sing N N 187 
LEU   N   H2   sing N N 188 
LEU   CA  C    sing N N 189 
LEU   CA  CB   sing N N 190 
LEU   CA  HA   sing N N 191 
LEU   C   O    doub N N 192 
LEU   C   OXT  sing N N 193 
LEU   CB  CG   sing N N 194 
LEU   CB  HB2  sing N N 195 
LEU   CB  HB3  sing N N 196 
LEU   CG  CD1  sing N N 197 
LEU   CG  CD2  sing N N 198 
LEU   CG  HG   sing N N 199 
LEU   CD1 HD11 sing N N 200 
LEU   CD1 HD12 sing N N 201 
LEU   CD1 HD13 sing N N 202 
LEU   CD2 HD21 sing N N 203 
LEU   CD2 HD22 sing N N 204 
LEU   CD2 HD23 sing N N 205 
LEU   OXT HXT  sing N N 206 
LYS   N   CA   sing N N 207 
LYS   N   H    sing N N 208 
LYS   N   H2   sing N N 209 
LYS   CA  C    sing N N 210 
LYS   CA  CB   sing N N 211 
LYS   CA  HA   sing N N 212 
LYS   C   O    doub N N 213 
LYS   C   OXT  sing N N 214 
LYS   CB  CG   sing N N 215 
LYS   CB  HB2  sing N N 216 
LYS   CB  HB3  sing N N 217 
LYS   CG  CD   sing N N 218 
LYS   CG  HG2  sing N N 219 
LYS   CG  HG3  sing N N 220 
LYS   CD  CE   sing N N 221 
LYS   CD  HD2  sing N N 222 
LYS   CD  HD3  sing N N 223 
LYS   CE  NZ   sing N N 224 
LYS   CE  HE2  sing N N 225 
LYS   CE  HE3  sing N N 226 
LYS   NZ  HZ1  sing N N 227 
LYS   NZ  HZ2  sing N N 228 
LYS   NZ  HZ3  sing N N 229 
LYS   OXT HXT  sing N N 230 
MET   N   CA   sing N N 231 
MET   N   H    sing N N 232 
MET   N   H2   sing N N 233 
MET   CA  C    sing N N 234 
MET   CA  CB   sing N N 235 
MET   CA  HA   sing N N 236 
MET   C   O    doub N N 237 
MET   C   OXT  sing N N 238 
MET   CB  CG   sing N N 239 
MET   CB  HB2  sing N N 240 
MET   CB  HB3  sing N N 241 
MET   CG  SD   sing N N 242 
MET   CG  HG2  sing N N 243 
MET   CG  HG3  sing N N 244 
MET   SD  CE   sing N N 245 
MET   CE  HE1  sing N N 246 
MET   CE  HE2  sing N N 247 
MET   CE  HE3  sing N N 248 
MET   OXT HXT  sing N N 249 
PHE   N   CA   sing N N 250 
PHE   N   H    sing N N 251 
PHE   N   H2   sing N N 252 
PHE   CA  C    sing N N 253 
PHE   CA  CB   sing N N 254 
PHE   CA  HA   sing N N 255 
PHE   C   O    doub N N 256 
PHE   C   OXT  sing N N 257 
PHE   CB  CG   sing N N 258 
PHE   CB  HB2  sing N N 259 
PHE   CB  HB3  sing N N 260 
PHE   CG  CD1  doub Y N 261 
PHE   CG  CD2  sing Y N 262 
PHE   CD1 CE1  sing Y N 263 
PHE   CD1 HD1  sing N N 264 
PHE   CD2 CE2  doub Y N 265 
PHE   CD2 HD2  sing N N 266 
PHE   CE1 CZ   doub Y N 267 
PHE   CE1 HE1  sing N N 268 
PHE   CE2 CZ   sing Y N 269 
PHE   CE2 HE2  sing N N 270 
PHE   CZ  HZ   sing N N 271 
PHE   OXT HXT  sing N N 272 
PRO   N   CA   sing N N 273 
PRO   N   CD   sing N N 274 
PRO   N   H    sing N N 275 
PRO   CA  C    sing N N 276 
PRO   CA  CB   sing N N 277 
PRO   CA  HA   sing N N 278 
PRO   C   O    doub N N 279 
PRO   C   OXT  sing N N 280 
PRO   CB  CG   sing N N 281 
PRO   CB  HB2  sing N N 282 
PRO   CB  HB3  sing N N 283 
PRO   CG  CD   sing N N 284 
PRO   CG  HG2  sing N N 285 
PRO   CG  HG3  sing N N 286 
PRO   CD  HD2  sing N N 287 
PRO   CD  HD3  sing N N 288 
PRO   OXT HXT  sing N N 289 
SER   N   CA   sing N N 290 
SER   N   H    sing N N 291 
SER   N   H2   sing N N 292 
SER   CA  C    sing N N 293 
SER   CA  CB   sing N N 294 
SER   CA  HA   sing N N 295 
SER   C   O    doub N N 296 
SER   C   OXT  sing N N 297 
SER   CB  OG   sing N N 298 
SER   CB  HB2  sing N N 299 
SER   CB  HB3  sing N N 300 
SER   OG  HG   sing N N 301 
SER   OXT HXT  sing N N 302 
THR   N   CA   sing N N 303 
THR   N   H    sing N N 304 
THR   N   H2   sing N N 305 
THR   CA  C    sing N N 306 
THR   CA  CB   sing N N 307 
THR   CA  HA   sing N N 308 
THR   C   O    doub N N 309 
THR   C   OXT  sing N N 310 
THR   CB  OG1  sing N N 311 
THR   CB  CG2  sing N N 312 
THR   CB  HB   sing N N 313 
THR   OG1 HG1  sing N N 314 
THR   CG2 HG21 sing N N 315 
THR   CG2 HG22 sing N N 316 
THR   CG2 HG23 sing N N 317 
THR   OXT HXT  sing N N 318 
TRP   N   CA   sing N N 319 
TRP   N   H    sing N N 320 
TRP   N   H2   sing N N 321 
TRP   CA  C    sing N N 322 
TRP   CA  CB   sing N N 323 
TRP   CA  HA   sing N N 324 
TRP   C   O    doub N N 325 
TRP   C   OXT  sing N N 326 
TRP   CB  CG   sing N N 327 
TRP   CB  HB2  sing N N 328 
TRP   CB  HB3  sing N N 329 
TRP   CG  CD1  doub Y N 330 
TRP   CG  CD2  sing Y N 331 
TRP   CD1 NE1  sing Y N 332 
TRP   CD1 HD1  sing N N 333 
TRP   CD2 CE2  doub Y N 334 
TRP   CD2 CE3  sing Y N 335 
TRP   NE1 CE2  sing Y N 336 
TRP   NE1 HE1  sing N N 337 
TRP   CE2 CZ2  sing Y N 338 
TRP   CE3 CZ3  doub Y N 339 
TRP   CE3 HE3  sing N N 340 
TRP   CZ2 CH2  doub Y N 341 
TRP   CZ2 HZ2  sing N N 342 
TRP   CZ3 CH2  sing Y N 343 
TRP   CZ3 HZ3  sing N N 344 
TRP   CH2 HH2  sing N N 345 
TRP   OXT HXT  sing N N 346 
TYR   N   CA   sing N N 347 
TYR   N   H    sing N N 348 
TYR   N   H2   sing N N 349 
TYR   CA  C    sing N N 350 
TYR   CA  CB   sing N N 351 
TYR   CA  HA   sing N N 352 
TYR   C   O    doub N N 353 
TYR   C   OXT  sing N N 354 
TYR   CB  CG   sing N N 355 
TYR   CB  HB2  sing N N 356 
TYR   CB  HB3  sing N N 357 
TYR   CG  CD1  doub Y N 358 
TYR   CG  CD2  sing Y N 359 
TYR   CD1 CE1  sing Y N 360 
TYR   CD1 HD1  sing N N 361 
TYR   CD2 CE2  doub Y N 362 
TYR   CD2 HD2  sing N N 363 
TYR   CE1 CZ   doub Y N 364 
TYR   CE1 HE1  sing N N 365 
TYR   CE2 CZ   sing Y N 366 
TYR   CE2 HE2  sing N N 367 
TYR   CZ  OH   sing N N 368 
TYR   OH  HH   sing N N 369 
TYR   OXT HXT  sing N N 370 
VAL   N   CA   sing N N 371 
VAL   N   H    sing N N 372 
VAL   N   H2   sing N N 373 
VAL   CA  C    sing N N 374 
VAL   CA  CB   sing N N 375 
VAL   CA  HA   sing N N 376 
VAL   C   O    doub N N 377 
VAL   C   OXT  sing N N 378 
VAL   CB  CG1  sing N N 379 
VAL   CB  CG2  sing N N 380 
VAL   CB  HB   sing N N 381 
VAL   CG1 HG11 sing N N 382 
VAL   CG1 HG12 sing N N 383 
VAL   CG1 HG13 sing N N 384 
VAL   CG2 HG21 sing N N 385 
VAL   CG2 HG22 sing N N 386 
VAL   CG2 HG23 sing N N 387 
VAL   OXT HXT  sing N N 388 
# 
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                    9H7K 
_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]   0.024327 
_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]   0.015856 
_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]   0.011928 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS   A 1 10  ? 12.832 7.861   -10.408 1.00 34.22 ? 10  CYS   A N   1 
ATOM   2    C  CA  . CYS   A 1 10  ? 13.447 6.655   -11.052 1.00 26.04 ? 10  CYS   A CA  1 
ATOM   3    C  C   . CYS   A 1 10  ? 12.625 5.389   -10.879 1.00 21.09 ? 10  CYS   A C   1 
ATOM   4    O  O   . CYS   A 1 10  ? 12.430 4.901   -9.782  1.00 20.48 ? 10  CYS   A O   1 
ATOM   5    C  CB  . CYS   A 1 10  ? 14.832 6.380   -10.486 1.00 32.63 ? 10  CYS   A CB  1 
ATOM   6    S  SG  . CYS   A 1 10  ? 16.084 7.305   -11.352 1.00 45.34 ? 10  CYS   A SG  1 
ATOM   7    N  N   . PRO   A 1 11  ? 12.119 4.870   -11.963 1.00 16.13 ? 11  PRO   A N   1 
ATOM   8    C  CA  . PRO   A 1 11  ? 11.224 3.733   -11.753 1.00 12.99 ? 11  PRO   A CA  1 
ATOM   9    C  C   . PRO   A 1 11  ? 11.900 2.347   -11.724 1.00 11.05 ? 11  PRO   A C   1 
ATOM   10   O  O   . PRO   A 1 11  ? 11.279 1.353   -11.386 1.00 12.02 ? 11  PRO   A O   1 
ATOM   11   C  CB  . PRO   A 1 11  ? 10.316 3.797   -12.960 1.00 18.27 ? 11  PRO   A CB  1 
ATOM   12   C  CG  . PRO   A 1 11  ? 11.094 4.477   -13.988 1.00 19.11 ? 11  PRO   A CG  1 
ATOM   13   C  CD  . PRO   A 1 11  ? 11.944 5.484   -13.290 1.00 22.83 ? 11  PRO   A CD  1 
ATOM   14   N  N   . LEU   A 1 12  ? 13.192 2.299   -12.083 1.00 12.91 ? 12  LEU   A N   1 
ATOM   15   C  CA  . LEU   A 1 12  ? 13.870 1.055   -12.043 1.00 9.79  ? 12  LEU   A CA  1 
ATOM   16   C  C   . LEU   A 1 12  ? 15.306 1.281   -11.569 1.00 11.06 ? 12  LEU   A C   1 
ATOM   17   O  O   . LEU   A 1 12  ? 16.121 1.930   -12.260 1.00 15.52 ? 12  LEU   A O   1 
ATOM   18   C  CB  . LEU   A 1 12  ? 13.859 0.408   -13.441 1.00 9.93  ? 12  LEU   A CB  1 
ATOM   19   C  CG  . LEU   A 1 12  ? 14.552 -0.947  -13.517 1.00 14.20 ? 12  LEU   A CG  1 
ATOM   20   C  CD1 . LEU   A 1 12  ? 13.883 -2.017  -12.666 1.00 14.86 ? 12  LEU   A CD1 1 
ATOM   21   C  CD2 . LEU   A 1 12  ? 14.660 -1.405  -14.995 1.00 12.23 ? 12  LEU   A CD2 1 
ATOM   22   N  N   . MET   A 1 13  ? 15.578 0.762   -10.365 1.00 11.95 ? 13  MET   A N   1 
ATOM   23   C  CA  . MET   A 1 13  ? 16.866 0.924   -9.740  1.00 10.51 ? 13  MET   A CA  1 
ATOM   24   C  C   . MET   A 1 13  ? 17.434 -0.454  -9.458  1.00 9.40  ? 13  MET   A C   1 
ATOM   25   O  O   . MET   A 1 13  ? 16.749 -1.410  -9.161  1.00 9.33  ? 13  MET   A O   1 
ATOM   26   C  CB  . MET   A 1 13  ? 16.692 1.707   -8.413  1.00 14.50 ? 13  MET   A CB  1 
ATOM   27   C  CG  . MET   A 1 13  ? 16.068 3.099   -8.565  1.00 23.34 ? 13  MET   A CG  1 
ATOM   28   S  SD  . MET   A 1 13  ? 15.239 3.709   -7.073  1.00 31.79 ? 13  MET   A SD  1 
ATOM   29   C  CE  . MET   A 1 13  ? 13.668 2.804   -7.218  1.00 24.44 ? 13  MET   A CE  1 
ATOM   30   N  N   . VAL   A 1 14  ? 18.751 -0.559  -9.488  1.00 8.99  ? 14  VAL   A N   1 
ATOM   31   C  CA  . VAL   A 1 14  ? 19.425 -1.838  -9.252  1.00 8.46  ? 14  VAL   A CA  1 
ATOM   32   C  C   . VAL   A 1 14  ? 20.568 -1.542  -8.279  1.00 7.45  ? 14  VAL   A C   1 
ATOM   33   O  O   . VAL   A 1 14  ? 21.260 -0.486  -8.390  1.00 9.20  ? 14  VAL   A O   1 
ATOM   34   C  CB  . VAL   A 1 14  ? 19.990 -2.400  -10.539 1.00 8.99  ? 14  VAL   A CB  1 
ATOM   35   C  CG1 . VAL   A 1 14  ? 20.743 -3.680  -10.316 1.00 8.90  ? 14  VAL   A CG1 1 
ATOM   36   C  CG2 . VAL   A 1 14  ? 18.866 -2.567  -11.566 1.00 10.03 ? 14  VAL   A CG2 1 
ATOM   37   N  N   . LYS   A 1 15  ? 20.664 -2.412  -7.288  1.00 7.11  ? 15  LYS   A N   1 
ATOM   38   C  CA  . LYS   A 1 15  ? 21.698 -2.302  -6.236  1.00 7.84  ? 15  LYS   A CA  1 
ATOM   39   C  C   . LYS   A 1 15  ? 22.399 -3.641  -6.024  1.00 7.27  ? 15  LYS   A C   1 
ATOM   40   O  O   . LYS   A 1 15  ? 21.758 -4.635  -5.817  1.00 8.57  ? 15  LYS   A O   1 
ATOM   41   C  CB  . LYS   A 1 15  ? 21.110 -1.798  -4.895  1.00 11.04 ? 15  LYS   A CB  1 
ATOM   42   C  CG  . LYS   A 1 15  ? 22.175 -1.614  -3.813  1.00 18.68 ? 15  LYS   A CG  1 
ATOM   43   N  N   . VAL   A 1 16  ? 23.747 -3.644  -6.082  1.00 7.50  ? 16  VAL   A N   1 
ATOM   44   C  CA  . VAL   A 1 16  ? 24.509 -4.863  -6.135  1.00 6.65  ? 16  VAL   A CA  1 
ATOM   45   C  C   . VAL   A 1 16  ? 25.697 -4.813  -5.142  1.00 6.28  ? 16  VAL   A C   1 
ATOM   46   O  O   . VAL   A 1 16  ? 26.365 -3.797  -5.036  1.00 8.21  ? 16  VAL   A O   1 
ATOM   47   C  CB  . VAL   A 1 16  ? 25.053 -5.154  -7.525  1.00 7.43  ? 16  VAL   A CB  1 
ATOM   48   C  CG1 . VAL   A 1 16  ? 25.523 -6.599  -7.689  1.00 7.56  ? 16  VAL   A CG1 1 
ATOM   49   C  CG2 . VAL   A 1 16  ? 24.051 -4.796  -8.574  1.00 8.63  ? 16  VAL   A CG2 1 
ATOM   50   N  N   . LEU   A 1 17  ? 25.777 -5.836  -4.355  1.00 6.24  ? 17  LEU   A N   1 
ATOM   51   C  CA  . LEU   A 1 17  ? 26.792 -6.003  -3.308  1.00 4.94  ? 17  LEU   A CA  1 
ATOM   52   C  C   . LEU   A 1 17  ? 27.600 -7.278  -3.592  1.00 5.91  ? 17  LEU   A C   1 
ATOM   53   O  O   . LEU   A 1 17  ? 27.155 -8.244  -4.208  1.00 6.41  ? 17  LEU   A O   1 
ATOM   54   C  CB  . LEU   A 1 17  ? 26.120 -6.090  -1.912  1.00 6.42  ? 17  LEU   A CB  1 
ATOM   55   C  CG  . LEU   A 1 17  ? 25.352 -4.815  -1.454  1.00 5.55  ? 17  LEU   A CG  1 
ATOM   56   C  CD1 . LEU   A 1 17  ? 24.728 -5.085  -0.106  1.00 5.87  ? 17  LEU   A CD1 1 
ATOM   57   C  CD2 . LEU   A 1 17  ? 26.176 -3.551  -1.432  1.00 7.41  ? 17  LEU   A CD2 1 
ATOM   58   N  N   . ASP   A 1 18  ? 28.853 -7.234  -3.107  1.00 6.20  ? 18  ASP   A N   1 
ATOM   59   C  CA  . ASP   A 1 18  ? 29.853 -8.262  -3.312  1.00 4.78  ? 18  ASP   A CA  1 
ATOM   60   C  C   . ASP   A 1 18  ? 30.122 -8.992  -1.974  1.00 5.52  ? 18  ASP   A C   1 
ATOM   61   O  O   . ASP   A 1 18  ? 30.573 -8.350  -1.023  1.00 5.97  ? 18  ASP   A O   1 
ATOM   62   C  CB  . ASP   A 1 18  ? 31.106 -7.577  -3.881  1.00 5.64  ? 18  ASP   A CB  1 
ATOM   63   C  CG  . ASP   A 1 18  ? 32.313 -8.503  -4.028  1.00 7.16  ? 18  ASP   A CG  1 
ATOM   64   O  OD1 . ASP   A 1 18  ? 32.429 -9.526  -3.336  1.00 7.24  ? 18  ASP   A OD1 1 
ATOM   65   O  OD2 . ASP   A 1 18  ? 33.176 -8.145  -4.927  1.00 9.33  ? 18  ASP   A OD2 1 
ATOM   66   N  N   . ALA   A 1 19  ? 29.808 -10.307 -1.936  1.00 5.28  ? 19  ALA   A N   1 
ATOM   67   C  CA  . ALA   A 1 19  ? 29.901 -11.116 -0.697  1.00 6.15  ? 19  ALA   A CA  1 
ATOM   68   C  C   . ALA   A 1 19  ? 31.318 -11.617 -0.430  1.00 6.59  ? 19  ALA   A C   1 
ATOM   69   O  O   . ALA   A 1 19  ? 31.578 -12.214 0.616   1.00 7.91  ? 19  ALA   A O   1 
ATOM   70   C  CB  . ALA   A 1 19  ? 28.999 -12.287 -0.761  1.00 7.35  ? 19  ALA   A CB  1 
ATOM   71   N  N   . VAL   A 1 20  ? 32.192 -11.520 -1.431  1.00 8.18  ? 20  VAL   A N   1 
ATOM   72   C  CA  . VAL   A 1 20  ? 33.592 -11.931 -1.283  1.00 8.18  ? 20  VAL   A CA  1 
ATOM   73   C  C   . VAL   A 1 20  ? 34.479 -10.850 -0.733  1.00 9.74  ? 20  VAL   A C   1 
ATOM   74   O  O   . VAL   A 1 20  ? 35.432 -11.124 0.055   1.00 13.82 ? 20  VAL   A O   1 
ATOM   75   C  CB  . VAL   A 1 20  ? 34.154 -12.353 -2.660  1.00 8.12  ? 20  VAL   A CB  1 
ATOM   76   C  CG1 . VAL   A 1 20  ? 35.672 -12.634 -2.636  1.00 11.05 ? 20  VAL   A CG1 1 
ATOM   77   C  CG2 . VAL   A 1 20  ? 33.362 -13.555 -3.201  1.00 8.69  ? 20  VAL   A CG2 1 
ATOM   78   N  N   . ARG   A 1 21  ? 34.256 -9.638  -1.183  1.00 10.74 ? 21  ARG   A N   1 
ATOM   79   C  CA  . ARG   A 1 21  ? 35.044 -8.486  -0.756  1.00 10.79 ? 21  ARG   A CA  1 
ATOM   80   C  C   . ARG   A 1 21  ? 34.413 -7.664  0.353   1.00 8.81  ? 21  ARG   A C   1 
ATOM   81   O  O   . ARG   A 1 21  ? 35.117 -6.813  0.948   1.00 11.10 ? 21  ARG   A O   1 
ATOM   82   C  CB  . ARG   A 1 21  ? 35.324 -7.603  -1.939  1.00 14.22 ? 21  ARG   A CB  1 
ATOM   83   C  CG  . ARG   A 1 21  ? 36.018 -8.371  -3.071  1.00 19.30 ? 21  ARG   A CG  1 
ATOM   84   C  CD  . ARG   A 1 21  ? 36.911 -7.534  -3.989  1.00 27.53 ? 21  ARG   A CD  1 
ATOM   85   N  NE  . ARG   A 1 21  ? 36.305 -6.266  -4.404  1.00 33.20 ? 21  ARG   A NE  1 
ATOM   86   C  CZ  . ARG   A 1 21  ? 36.728 -5.066  -3.981  1.00 23.67 ? 21  ARG   A CZ  1 
ATOM   87   N  N   . GLY   A 1 22  ? 33.100 -7.846  0.629   1.00 10.94 ? 22  GLY   A N   1 
ATOM   88   C  CA  . GLY   A 1 22  ? 32.525 -7.023  1.659   1.00 7.45  ? 22  GLY   A CA  1 
ATOM   89   C  C   . GLY   A 1 22  ? 32.380 -5.602  1.238   1.00 6.27  ? 22  GLY   A C   1 
ATOM   90   O  O   . GLY   A 1 22  ? 32.698 -4.665  2.025   1.00 6.99  ? 22  GLY   A O   1 
ATOM   91   N  N   . SER   A 1 23  ? 31.927 -5.409  -0.013  1.00 6.44  ? 23  SER   A N   1 
ATOM   92   C  CA  . SER   A 1 23  ? 31.863 -4.098  -0.610  1.00 6.71  ? 23  SER   A CA  1 
ATOM   93   C  C   . SER   A 1 23  ? 30.692 -4.001  -1.563  1.00 6.40  ? 23  SER   A C   1 
ATOM   94   O  O   . SER   A 1 23  ? 30.171 -4.998  -2.024  1.00 6.24  ? 23  SER   A O   1 
ATOM   95   C  CB  . SER   A 1 23  ? 33.123 -3.801  -1.421  1.00 8.67  ? 23  SER   A CB  1 
ATOM   96   O  OG  . SER   A 1 23  ? 33.216 -4.630  -2.566  1.00 13.32 ? 23  SER   A OG  1 
ATOM   97   N  N   . PRO   A 1 24  ? 30.390 -2.763  -1.964  1.00 6.45  ? 24  PRO   A N   1 
ATOM   98   C  CA  . PRO   A 1 24  ? 29.528 -2.711  -3.110  1.00 7.29  ? 24  PRO   A CA  1 
ATOM   99   C  C   . PRO   A 1 24  ? 30.186 -3.341  -4.317  1.00 6.57  ? 24  PRO   A C   1 
ATOM   100  O  O   . PRO   A 1 24  ? 31.434 -3.412  -4.432  1.00 7.46  ? 24  PRO   A O   1 
ATOM   101  C  CB  . PRO   A 1 24  ? 29.295 -1.235  -3.335  1.00 9.47  ? 24  PRO   A CB  1 
ATOM   102  C  CG  . PRO   A 1 24  ? 30.364 -0.545  -2.581  1.00 15.40 ? 24  PRO   A CG  1 
ATOM   103  C  CD  . PRO   A 1 24  ? 30.961 -1.457  -1.589  1.00 10.45 ? 24  PRO   A CD  1 
ATOM   104  N  N   . ALA   A 1 25  ? 29.352 -3.773  -5.260  1.00 7.71  ? 25  ALA   A N   1 
ATOM   105  C  CA  . ALA   A 1 25  ? 29.859 -4.226  -6.526  1.00 7.11  ? 25  ALA   A CA  1 
ATOM   106  C  C   . ALA   A 1 25  ? 29.927 -3.047  -7.490  1.00 7.06  ? 25  ALA   A C   1 
ATOM   107  O  O   . ALA   A 1 25  ? 28.895 -2.584  -8.005  1.00 8.02  ? 25  ALA   A O   1 
ATOM   108  C  CB  . ALA   A 1 25  ? 29.049 -5.390  -7.122  1.00 8.92  ? 25  ALA   A CB  1 
ATOM   109  N  N   . ILE   A 1 26  ? 31.119 -2.549  -7.722  1.00 8.64  ? 26  ILE   A N   1 
ATOM   110  C  CA  . ILE   A 1 26  ? 31.335 -1.284  -8.446  1.00 9.83  ? 26  ILE   A CA  1 
ATOM   111  C  C   . ILE   A 1 26  ? 31.615 -1.566  -9.909  1.00 9.88  ? 26  ILE   A C   1 
ATOM   112  O  O   . ILE   A 1 26  ? 32.354 -2.498  -10.270 1.00 9.80  ? 26  ILE   A O   1 
ATOM   113  C  CB  . ILE   A 1 26  ? 32.507 -0.506  -7.793  1.00 11.64 ? 26  ILE   A CB  1 
ATOM   114  C  CG1 . ILE   A 1 26  ? 32.263 -0.222  -6.308  1.00 10.94 ? 26  ILE   A CG1 1 
ATOM   115  C  CG2 . ILE   A 1 26  ? 32.845 0.798   -8.521  1.00 15.93 ? 26  ILE   A CG2 1 
ATOM   116  C  CD1 . ILE   A 1 26  ? 33.557 0.076   -5.559  1.00 17.97 ? 26  ILE   A CD1 1 
ATOM   117  N  N   . ASN   A 1 27  ? 31.016 -0.731  -10.748 1.00 10.23 ? 27  ASN   A N   1 
ATOM   118  C  CA  . ASN   A 1 27  ? 31.227 -0.779  -12.187 1.00 10.91 ? 27  ASN   A CA  1 
ATOM   119  C  C   . ASN   A 1 27  ? 30.853 -2.089  -12.806 1.00 9.33  ? 27  ASN   A C   1 
ATOM   120  O  O   . ASN   A 1 27  ? 31.528 -2.523  -13.739 1.00 12.94 ? 27  ASN   A O   1 
ATOM   121  C  CB  . ASN   A 1 27  ? 32.701 -0.451  -12.484 1.00 10.55 ? 27  ASN   A CB  1 
ATOM   122  C  CG  . ASN   A 1 27  ? 33.063 0.993   -12.179 1.00 14.14 ? 27  ASN   A CG  1 
ATOM   123  O  OD1 . ASN   A 1 27  ? 34.236 1.272   -11.874 1.00 21.36 ? 27  ASN   A OD1 1 
ATOM   124  N  ND2 . ASN   A 1 27  ? 32.111 1.934   -12.337 1.00 15.65 ? 27  ASN   A ND2 1 
ATOM   125  N  N   . VAL   A 1 28  ? 29.751 -2.691  -12.326 1.00 7.89  ? 28  VAL   A N   1 
ATOM   126  C  CA  . VAL   A 1 28  ? 29.248 -3.923  -12.918 1.00 9.73  ? 28  VAL   A CA  1 
ATOM   127  C  C   . VAL   A 1 28  ? 28.201 -3.564  -13.962 1.00 7.79  ? 28  VAL   A C   1 
ATOM   128  O  O   . VAL   A 1 28  ? 27.349 -2.693  -13.705 1.00 7.82  ? 28  VAL   A O   1 
ATOM   129  C  CB  . VAL   A 1 28  ? 28.657 -4.920  -11.887 1.00 14.53 ? 28  VAL   A CB  1 
ATOM   130  C  CG1 . VAL   A 1 28  ? 28.371 -6.275  -12.557 1.00 17.42 ? 28  VAL   A CG1 1 
ATOM   131  C  CG2 . VAL   A 1 28  ? 29.589 -5.141  -10.752 1.00 16.93 ? 28  VAL   A CG2 1 
ATOM   132  N  N   . ALA   A 1 29  ? 28.331 -4.126  -15.162 1.00 8.39  ? 29  ALA   A N   1 
ATOM   133  C  CA  . ALA   A 1 29  ? 27.371 -3.823  -16.275 1.00 5.77  ? 29  ALA   A CA  1 
ATOM   134  C  C   . ALA   A 1 29  ? 26.003 -4.447  -15.973 1.00 6.20  ? 29  ALA   A C   1 
ATOM   135  O  O   . ALA   A 1 29  ? 25.900 -5.560  -15.527 1.00 6.08  ? 29  ALA   A O   1 
ATOM   136  C  CB  . ALA   A 1 29  ? 27.879 -4.366  -17.607 1.00 7.21  ? 29  ALA   A CB  1 
ATOM   137  N  N   . VAL   A 1 30  ? 24.930 -3.721  -16.277 1.00 7.07  ? 30  VAL   A N   1 
ATOM   138  C  CA  . VAL   A 1 30  ? 23.573 -4.211  -16.095 1.00 8.63  ? 30  VAL   A CA  1 
ATOM   139  C  C   . VAL   A 1 30  ? 22.841 -3.917  -17.388 1.00 7.15  ? 30  VAL   A C   1 
ATOM   140  O  O   . VAL   A 1 30  ? 22.823 -2.765  -17.833 1.00 7.21  ? 30  VAL   A O   1 
ATOM   141  C  CB  . VAL   A 1 30  ? 22.850 -3.543  -14.943 1.00 8.41  ? 30  VAL   A CB  1 
ATOM   142  C  CG1 . VAL   A 1 30  ? 21.447 -4.142  -14.859 1.00 8.67  ? 30  VAL   A CG1 1 
ATOM   143  C  CG2 . VAL   A 1 30  ? 23.613 -3.697  -13.596 1.00 9.14  ? 30  VAL   A CG2 1 
ATOM   144  N  N   . HIS   A 1 31  ? 22.260 -4.974  -17.972 1.00 7.57  ? 31  HIS   A N   1 
ATOM   145  C  CA  . HIS   A 1 31  ? 21.465 -4.838  -19.210 1.00 7.60  ? 31  HIS   A CA  1 
ATOM   146  C  C   . HIS   A 1 31  ? 20.033 -5.177  -18.904 1.00 7.28  ? 31  HIS   A C   1 
ATOM   147  O  O   . HIS   A 1 31  ? 19.748 -6.137  -18.172 1.00 12.73 ? 31  HIS   A O   1 
ATOM   148  C  CB  . HIS   A 1 31  ? 21.979 -5.819  -20.245 1.00 9.08  ? 31  HIS   A CB  1 
ATOM   149  C  CG  . HIS   A 1 31  ? 23.309 -5.457  -20.788 1.00 14.66 ? 31  HIS   A CG  1 
ATOM   150  N  ND1 . HIS   A 1 31  ? 24.495 -5.852  -20.204 1.00 21.60 ? 31  HIS   A ND1 1 
ATOM   151  C  CD2 . HIS   A 1 31  ? 23.640 -4.743  -21.880 1.00 12.80 ? 31  HIS   A CD2 1 
ATOM   152  C  CE1 . HIS   A 1 31  ? 25.494 -5.399  -20.925 1.00 21.81 ? 31  HIS   A CE1 1 
ATOM   153  N  NE2 . HIS   A 1 31  ? 25.006 -4.722  -21.943 1.00 18.43 ? 31  HIS   A NE2 1 
ATOM   154  N  N   . VAL   A 1 32  ? 19.138 -4.345  -19.441 1.00 7.20  ? 32  VAL   A N   1 
ATOM   155  C  CA  . VAL   A 1 32  ? 17.721 -4.640  -19.305 1.00 8.38  ? 32  VAL   A CA  1 
ATOM   156  C  C   . VAL   A 1 32  ? 17.151 -4.869  -20.693 1.00 8.59  ? 32  VAL   A C   1 
ATOM   157  O  O   . VAL   A 1 32  ? 17.386 -4.075  -21.611 1.00 10.09 ? 32  VAL   A O   1 
ATOM   158  C  CB  . VAL   A 1 32  ? 16.972 -3.511  -18.601 1.00 8.27  ? 32  VAL   A CB  1 
ATOM   159  C  CG1 . VAL   A 1 32  ? 15.552 -3.967  -18.264 1.00 8.65  ? 32  VAL   A CG1 1 
ATOM   160  C  CG2 . VAL   A 1 32  ? 17.658 -3.054  -17.316 1.00 8.48  ? 32  VAL   A CG2 1 
ATOM   161  N  N   . PHE   A 1 33  ? 16.308 -5.895  -20.795 1.00 8.00  ? 33  PHE   A N   1 
ATOM   162  C  CA  . PHE   A 1 33  ? 15.594 -6.244  -22.035 1.00 7.99  ? 33  PHE   A CA  1 
ATOM   163  C  C   . PHE   A 1 33  ? 14.126 -6.268  -21.717 1.00 9.07  ? 33  PHE   A C   1 
ATOM   164  O  O   . PHE   A 1 33  ? 13.766 -6.426  -20.534 1.00 8.78  ? 33  PHE   A O   1 
ATOM   165  C  CB  . PHE   A 1 33  ? 16.042 -7.588  -22.521 1.00 7.72  ? 33  PHE   A CB  1 
ATOM   166  C  CG  . PHE   A 1 33  ? 17.553 -7.633  -22.791 1.00 9.05  ? 33  PHE   A CG  1 
ATOM   167  C  CD1 . PHE   A 1 33  ? 18.412 -8.023  -21.788 1.00 9.52  ? 33  PHE   A CD1 1 
ATOM   168  C  CD2 . PHE   A 1 33  ? 18.043 -7.410  -24.060 1.00 10.93 ? 33  PHE   A CD2 1 
ATOM   169  C  CE1 . PHE   A 1 33  ? 19.787 -8.057  -21.995 1.00 11.00 ? 33  PHE   A CE1 1 
ATOM   170  C  CE2 . PHE   A 1 33  ? 19.446 -7.479  -24.277 1.00 12.91 ? 33  PHE   A CE2 1 
ATOM   171  C  CZ  . PHE   A 1 33  ? 20.269 -7.809  -23.249 1.00 11.75 ? 33  PHE   A CZ  1 
ATOM   172  N  N   . ARG   A 1 34  ? 13.340 -6.105  -22.772 1.00 8.48  ? 34  ARG   A N   1 
ATOM   173  C  CA  . ARG   A 1 34  ? 11.901 -6.191  -22.589 1.00 9.36  ? 34  ARG   A CA  1 
ATOM   174  C  C   . ARG   A 1 34  ? 11.333 -7.133  -23.625 1.00 8.67  ? 34  ARG   A C   1 
ATOM   175  O  O   . ARG   A 1 34  ? 11.721 -7.083  -24.808 1.00 10.78 ? 34  ARG   A O   1 
ATOM   176  C  CB  . ARG   A 1 34  ? 11.266 -4.776  -22.706 1.00 9.40  ? 34  ARG   A CB  1 
ATOM   177  C  CG  . ARG   A 1 34  ? 9.781  -4.731  -22.410 1.00 12.78 ? 34  ARG   A CG  1 
ATOM   178  C  CD  . ARG   A 1 34  ? 9.195  -3.434  -22.831 1.00 17.24 ? 34  ARG   A CD  1 
ATOM   179  N  NE  . ARG   A 1 34  ? 7.787  -3.670  -22.878 1.00 30.25 ? 34  ARG   A NE  1 
ATOM   180  C  CZ  . ARG   A 1 34  ? 7.046  -3.946  -23.957 1.00 21.43 ? 34  ARG   A CZ  1 
ATOM   181  N  NH1 . ARG   A 1 34  ? 7.504  -3.939  -25.234 1.00 21.22 ? 34  ARG   A NH1 1 
ATOM   182  N  NH2 . ARG   A 1 34  ? 5.789  -4.169  -23.736 1.00 24.48 ? 34  ARG   A NH2 1 
ATOM   183  N  N   . LYS   A 1 35  ? 10.425 -7.979  -23.175 1.00 10.39 ? 35  LYS   A N   1 
ATOM   184  C  CA  . LYS   A 1 35  ? 9.599  -8.789  -24.008 1.00 16.57 ? 35  LYS   A CA  1 
ATOM   185  C  C   . LYS   A 1 35  ? 8.199  -8.070  -24.150 1.00 17.14 ? 35  LYS   A C   1 
ATOM   186  O  O   . LYS   A 1 35  ? 7.323  -7.770  -23.160 1.00 22.69 ? 35  LYS   A O   1 
ATOM   187  C  CB  . LYS   A 1 35  ? 9.366  -10.199 -23.443 1.00 12.73 ? 35  LYS   A CB  1 
ATOM   188  C  CG  . LYS   A 1 35  ? 8.754  -11.172 -24.434 1.00 17.41 ? 35  LYS   A CG  1 
ATOM   189  C  CD  . LYS   A 1 35  ? 8.537  -12.605 -23.980 1.00 24.12 ? 35  LYS   A CD  1 
ATOM   190  C  CE  . LYS   A 1 35  ? 8.604  -12.813 -22.520 1.00 19.77 ? 35  LYS   A CE  1 
ATOM   191  N  N   . ALA   A 1 36  ? 7.939  -7.856  -25.382 1.00 14.51 ? 36  ALA   A N   1 
ATOM   192  C  CA  . ALA   A 1 36  ? 6.593  -7.300  -25.820 1.00 24.38 ? 36  ALA   A CA  1 
ATOM   193  C  C   . ALA   A 1 36  ? 5.436  -8.316  -25.831 1.00 30.47 ? 36  ALA   A C   1 
ATOM   194  O  O   . ALA   A 1 36  ? 5.629  -9.548  -25.791 1.00 27.68 ? 36  ALA   A O   1 
ATOM   195  C  CB  . ALA   A 1 36  ? 6.769  -6.669  -27.192 1.00 30.07 ? 36  ALA   A CB  1 
ATOM   196  N  N   . ALA   A 1 37  ? 4.215  -7.787  -25.899 1.00 27.28 ? 37  ALA   A N   1 
ATOM   197  C  CA  . ALA   A 1 37  ? 3.000  -8.627  -25.915 1.00 32.81 ? 37  ALA   A CA  1 
ATOM   198  C  C   . ALA   A 1 37  ? 3.029  -9.666  -27.041 1.00 33.91 ? 37  ALA   A C   1 
ATOM   199  O  O   . ALA   A 1 37  ? 2.374  -10.715 -26.990 1.00 28.82 ? 37  ALA   A O   1 
ATOM   200  C  CB  . ALA   A 1 37  ? 1.754  -7.746  -26.023 1.00 38.97 ? 37  ALA   A CB  1 
ATOM   201  N  N   . ASP   A 1 38  ? 3.799  -9.361  -28.075 1.00 31.76 ? 38  ASP   A N   1 
ATOM   202  C  CA  . ASP   A 1 38  ? 3.974  -10.275 -29.188 1.00 18.84 ? 38  ASP   A CA  1 
ATOM   203  C  C   . ASP   A 1 38  ? 5.204  -11.152 -29.010 1.00 25.77 ? 38  ASP   A C   1 
ATOM   204  O  O   . ASP   A 1 38  ? 5.672  -11.714 -29.991 1.00 32.47 ? 38  ASP   A O   1 
ATOM   205  C  CB  . ASP   A 1 38  ? 4.104  -9.455  -30.481 1.00 23.24 ? 38  ASP   A CB  1 
ATOM   206  C  CG  . ASP   A 1 38  ? 5.489  -8.709  -30.588 1.00 27.95 ? 38  ASP   A CG  1 
ATOM   207  O  OD1 . ASP   A 1 38  ? 6.431  -8.925  -29.738 1.00 29.72 ? 38  ASP   A OD1 1 
ATOM   208  O  OD2 . ASP   A 1 38  ? 5.625  -7.922  -31.564 1.00 25.51 ? 38  ASP   A OD2 1 
ATOM   209  N  N   A TRP   A 1 41  ? 12.002 -9.626  -27.382 0.50 25.00 ? 41  TRP   A N   1 
ATOM   210  N  N   B TRP   A 1 41  ? 13.401 -10.927 -27.163 0.50 28.25 ? 41  TRP   A N   1 
ATOM   211  C  CA  A TRP   A 1 41  ? 13.124 -9.529  -26.423 0.50 29.05 ? 41  TRP   A CA  1 
ATOM   212  C  CA  B TRP   A 1 41  ? 13.680 -9.730  -26.366 0.50 32.38 ? 41  TRP   A CA  1 
ATOM   213  C  C   A TRP   A 1 41  ? 14.198 -8.481  -26.742 0.50 27.64 ? 41  TRP   A C   1 
ATOM   214  C  C   B TRP   A 1 41  ? 13.629 -8.405  -27.258 0.50 30.26 ? 41  TRP   A C   1 
ATOM   215  O  O   A TRP   A 1 41  ? 15.400 -8.793  -26.861 0.50 26.14 ? 41  TRP   A O   1 
ATOM   216  O  O   B TRP   A 1 41  ? 13.277 -8.431  -28.469 0.50 22.48 ? 41  TRP   A O   1 
ATOM   217  C  CB  A TRP   A 1 41  ? 13.764 -10.876 -26.245 0.50 22.65 ? 41  TRP   A CB  1 
ATOM   218  C  CB  B TRP   A 1 41  ? 14.977 -9.967  -25.516 0.50 26.43 ? 41  TRP   A CB  1 
ATOM   219  C  CG  A TRP   A 1 41  ? 13.134 -11.629 -25.157 0.50 19.83 ? 41  TRP   A CG  1 
ATOM   220  C  CG  B TRP   A 1 41  ? 14.786 -11.078 -24.413 0.50 26.03 ? 41  TRP   A CG  1 
ATOM   221  C  CD1 A TRP   A 1 41  ? 12.591 -12.867 -25.238 0.50 25.89 ? 41  TRP   A CD1 1 
ATOM   222  C  CD1 B TRP   A 1 41  ? 15.314 -12.353 -24.384 0.50 26.93 ? 41  TRP   A CD1 1 
ATOM   223  C  CD2 A TRP   A 1 41  ? 12.995 -11.210 -23.789 0.50 19.74 ? 41  TRP   A CD2 1 
ATOM   224  C  CD2 B TRP   A 1 41  ? 13.974 -10.970 -23.232 0.50 25.28 ? 41  TRP   A CD2 1 
ATOM   225  N  NE1 A TRP   A 1 41  ? 12.116 -13.258 -24.009 0.50 30.03 ? 41  TRP   A NE1 1 
ATOM   226  N  NE1 B TRP   A 1 41  ? 14.882 -13.026 -23.267 0.50 25.39 ? 41  TRP   A NE1 1 
ATOM   227  C  CE2 A TRP   A 1 41  ? 12.369 -12.268 -23.097 0.50 20.86 ? 41  TRP   A CE2 1 
ATOM   228  C  CE2 B TRP   A 1 41  ? 14.053 -12.207 -22.546 0.50 22.59 ? 41  TRP   A CE2 1 
ATOM   229  C  CE3 A TRP   A 1 41  ? 13.375 -10.064 -23.077 0.50 18.56 ? 41  TRP   A CE3 1 
ATOM   230  C  CE3 B TRP   A 1 41  ? 13.193 -9.948  -22.692 0.50 20.32 ? 41  TRP   A CE3 1 
ATOM   231  C  CZ2 A TRP   A 1 41  ? 12.095 -12.204 -21.737 0.50 16.11 ? 41  TRP   A CZ2 1 
ATOM   232  C  CZ2 B TRP   A 1 41  ? 13.367 -12.441 -21.343 0.50 21.33 ? 41  TRP   A CZ2 1 
ATOM   233  C  CZ3 A TRP   A 1 41  ? 13.088 -9.993  -21.752 0.50 15.49 ? 41  TRP   A CZ3 1 
ATOM   234  C  CZ3 B TRP   A 1 41  ? 12.527 -10.176 -21.522 0.50 17.12 ? 41  TRP   A CZ3 1 
ATOM   235  C  CH2 A TRP   A 1 41  ? 12.459 -11.061 -21.082 0.50 15.59 ? 41  TRP   A CH2 1 
ATOM   236  C  CH2 B TRP   A 1 41  ? 12.609 -11.414 -20.853 0.50 17.53 ? 41  TRP   A CH2 1 
ATOM   237  N  N   . GLU   A 1 42  ? 13.743 -7.240  -26.632 1.00 26.07 ? 42  GLU   A N   1 
ATOM   238  C  CA  . GLU   A 1 42  ? 14.222 -6.038  -27.272 1.00 18.39 ? 42  GLU   A CA  1 
ATOM   239  C  C   . GLU   A 1 42  ? 15.193 -5.425  -26.258 1.00 16.19 ? 42  GLU   A C   1 
ATOM   240  O  O   . GLU   A 1 42  ? 14.901 -5.406  -25.109 1.00 12.71 ? 42  GLU   A O   1 
ATOM   241  C  CB  . GLU   A 1 42  ? 13.070 -5.016  -27.505 1.00 20.65 ? 42  GLU   A CB  1 
ATOM   242  C  CG  . GLU   A 1 42  ? 12.363 -4.450  -26.223 1.00 24.81 ? 42  GLU   A CG  1 
ATOM   243  C  CD  . GLU   A 1 42  ? 10.973 -3.718  -26.321 1.00 26.16 ? 42  GLU   A CD  1 
ATOM   244  O  OE1 . GLU   A 1 42  ? 10.860 -2.610  -25.762 1.00 21.03 ? 42  GLU   A OE1 1 
ATOM   245  O  OE2 . GLU   A 1 42  ? 9.952  -4.228  -26.815 1.00 24.10 ? 42  GLU   A OE2 1 
ATOM   246  N  N   . PRO   A 1 43  ? 16.358 -4.912  -26.688 1.00 14.54 ? 43  PRO   A N   1 
ATOM   247  C  CA  . PRO   A 1 43  ? 17.077 -4.092  -25.754 1.00 13.86 ? 43  PRO   A CA  1 
ATOM   248  C  C   . PRO   A 1 43  ? 16.191 -2.942  -25.217 1.00 11.71 ? 43  PRO   A C   1 
ATOM   249  O  O   . PRO   A 1 43  ? 15.420 -2.338  -25.965 1.00 14.67 ? 43  PRO   A O   1 
ATOM   250  C  CB  . PRO   A 1 43  ? 18.271 -3.618  -26.594 1.00 19.54 ? 43  PRO   A CB  1 
ATOM   251  C  CG  . PRO   A 1 43  ? 18.617 -4.908  -27.312 1.00 24.14 ? 43  PRO   A CG  1 
ATOM   252  C  CD  . PRO   A 1 43  ? 17.229 -5.328  -27.799 1.00 20.75 ? 43  PRO   A CD  1 
ATOM   253  N  N   . PHE   A 1 44  ? 16.332 -2.666  -23.917 1.00 10.22 ? 44  PHE   A N   1 
ATOM   254  C  CA  . PHE   A 1 44  ? 15.566 -1.607  -23.215 1.00 10.69 ? 44  PHE   A CA  1 
ATOM   255  C  C   . PHE   A 1 44  ? 16.401 -0.453  -22.612 1.00 10.69 ? 44  PHE   A C   1 
ATOM   256  O  O   . PHE   A 1 44  ? 16.152 0.722   -22.868 1.00 10.83 ? 44  PHE   A O   1 
ATOM   257  C  CB  . PHE   A 1 44  ? 14.619 -2.222  -22.160 1.00 9.89  ? 44  PHE   A CB  1 
ATOM   258  C  CG  . PHE   A 1 44  ? 13.807 -1.207  -21.444 1.00 7.70  ? 44  PHE   A CG  1 
ATOM   259  C  CD1 . PHE   A 1 44  ? 12.654 -0.642  -22.030 1.00 10.27 ? 44  PHE   A CD1 1 
ATOM   260  C  CD2 . PHE   A 1 44  ? 14.185 -0.764  -20.213 1.00 8.58  ? 44  PHE   A CD2 1 
ATOM   261  C  CE1 . PHE   A 1 44  ? 11.951 0.363   -21.369 1.00 9.75  ? 44  PHE   A CE1 1 
ATOM   262  C  CE2 . PHE   A 1 44  ? 13.518 0.241   -19.565 1.00 11.50 ? 44  PHE   A CE2 1 
ATOM   263  C  CZ  . PHE   A 1 44  ? 12.375 0.807   -20.124 1.00 8.06  ? 44  PHE   A CZ  1 
ATOM   264  N  N   . ALA   A 1 45  ? 17.392 -0.835  -21.818 1.00 9.21  ? 45  ALA   A N   1 
ATOM   265  C  CA  . ALA   A 1 45  ? 18.242 0.115   -21.149 1.00 13.77 ? 45  ALA   A CA  1 
ATOM   266  C  C   . ALA   A 1 45  ? 19.476 -0.660  -20.591 1.00 12.63 ? 45  ALA   A C   1 
ATOM   267  O  O   . ALA   A 1 45  ? 19.405 -1.817  -20.370 1.00 11.08 ? 45  ALA   A O   1 
ATOM   268  C  CB  . ALA   A 1 45  ? 17.520 0.764   -19.997 1.00 10.93 ? 45  ALA   A CB  1 
ATOM   269  N  N   . SER   A 1 46  ? 20.557 0.059   -20.284 1.00 11.09 ? 46  SER   A N   1 
ATOM   270  C  CA  . SER   A 1 46  ? 21.722 -0.538  -19.688 1.00 7.71  ? 46  SER   A CA  1 
ATOM   271  C  C   . SER   A 1 46  ? 22.546 0.548   -19.002 1.00 8.60  ? 46  SER   A C   1 
ATOM   272  O  O   . SER   A 1 46  ? 22.452 1.682   -19.348 1.00 9.99  ? 46  SER   A O   1 
ATOM   273  C  CB  . SER   A 1 46  ? 22.539 -1.321  -20.732 1.00 9.09  ? 46  SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 46  ? 22.923 -0.567  -21.852 1.00 9.66  ? 46  SER   A OG  1 
ATOM   275  N  N   . GLY   A 1 47  ? 23.449 0.151   -18.082 1.00 7.75  ? 47  GLY   A N   1 
ATOM   276  C  CA  . GLY   A 1 47  ? 24.198 1.089   -17.336 1.00 7.67  ? 47  GLY   A CA  1 
ATOM   277  C  C   . GLY   A 1 47  ? 25.242 0.283   -16.593 1.00 7.89  ? 47  GLY   A C   1 
ATOM   278  O  O   . GLY   A 1 47  ? 25.301 -0.949  -16.683 1.00 7.50  ? 47  GLY   A O   1 
ATOM   279  N  N   . LYS   A 1 48  ? 26.037 0.986   -15.791 1.00 8.60  ? 48  LYS   A N   1 
ATOM   280  C  CA  . LYS   A 1 48  ? 26.977 0.321   -14.885 1.00 8.04  ? 48  LYS   A CA  1 
ATOM   281  C  C   . LYS   A 1 48  ? 26.734 0.853   -13.465 1.00 7.11  ? 48  LYS   A C   1 
ATOM   282  O  O   . LYS   A 1 48  ? 26.383 2.051   -13.262 1.00 8.77  ? 48  LYS   A O   1 
ATOM   283  C  CB  . LYS   A 1 48  ? 28.436 0.628   -15.313 1.00 11.14 ? 48  LYS   A CB  1 
ATOM   284  C  CG  . LYS   A 1 48  ? 28.995 -0.364  -16.336 1.00 13.32 ? 48  LYS   A CG  1 
ATOM   285  C  CD  . LYS   A 1 48  ? 30.512 -0.477  -16.386 1.00 16.72 ? 48  LYS   A CD  1 
ATOM   286  C  CE  . LYS   A 1 48  ? 31.037 -1.736  -17.036 1.00 20.07 ? 48  LYS   A CE  1 
ATOM   287  N  NZ  . LYS   A 1 48  ? 32.436 -1.975  -16.567 1.00 24.79 ? 48  LYS   A NZ  1 
ATOM   288  N  N   . THR   A 1 49  ? 26.961 -0.002  -12.484 1.00 7.35  ? 49  THR   A N   1 
ATOM   289  C  CA  . THR   A 1 49  ? 26.823 0.404   -11.070 1.00 9.14  ? 49  THR   A CA  1 
ATOM   290  C  C   . THR   A 1 49  ? 27.887 1.419   -10.680 1.00 8.43  ? 49  THR   A C   1 
ATOM   291  O  O   . THR   A 1 49  ? 29.051 1.353   -11.179 1.00 10.31 ? 49  THR   A O   1 
ATOM   292  C  CB  . THR   A 1 49  ? 26.865 -0.800  -10.120 1.00 9.05  ? 49  THR   A CB  1 
ATOM   293  O  OG1 . THR   A 1 49  ? 28.124 -1.468  -10.270 1.00 8.67  ? 49  THR   A OG1 1 
ATOM   294  C  CG2 . THR   A 1 49  ? 25.718 -1.792  -10.426 1.00 10.21 ? 49  THR   A CG2 1 
ATOM   295  N  N   . SER   A 1 50  ? 27.501 2.315   -9.765  1.00 9.36  ? 50  SER   A N   1 
ATOM   296  C  CA  . SER   A 1 50  ? 28.351 3.355   -9.246  1.00 10.04 ? 50  SER   A CA  1 
ATOM   297  C  C   . SER   A 1 50  ? 29.304 2.803   -8.135  1.00 9.22  ? 50  SER   A C   1 
ATOM   298  O  O   . SER   A 1 50  ? 29.289 1.625   -7.793  1.00 8.41  ? 50  SER   A O   1 
ATOM   299  C  CB  . SER   A 1 50  ? 27.488 4.452   -8.623  1.00 11.16 ? 50  SER   A CB  1 
ATOM   300  O  OG  . SER   A 1 50  ? 27.003 3.970   -7.386  1.00 11.11 ? 50  SER   A OG  1 
ATOM   301  N  N   . GLU   A 1 51  ? 30.085 3.707   -7.560  1.00 10.22 ? 51  GLU   A N   1 
ATOM   302  C  CA  . GLU   A 1 51  ? 30.952 3.384   -6.420  1.00 13.59 ? 51  GLU   A CA  1 
ATOM   303  C  C   . GLU   A 1 51  ? 30.198 2.892   -5.161  1.00 12.24 ? 51  GLU   A C   1 
ATOM   304  O  O   . GLU   A 1 51  ? 30.796 2.285   -4.294  1.00 13.12 ? 51  GLU   A O   1 
ATOM   305  C  CB  . GLU   A 1 51  ? 31.858 4.574   -6.133  1.00 17.26 ? 51  GLU   A CB  1 
ATOM   306  C  CG  . GLU   A 1 51  ? 32.863 4.884   -7.236  1.00 22.03 ? 51  GLU   A CG  1 
ATOM   307  C  CD  . GLU   A 1 51  ? 33.302 6.333   -7.294  0.50 24.61 ? 51  GLU   A CD  1 
ATOM   308  O  OE1 . GLU   A 1 51  ? 34.031 6.795   -6.397  0.50 22.74 ? 51  GLU   A OE1 1 
ATOM   309  O  OE2 . GLU   A 1 51  ? 32.937 7.016   -8.271  0.50 30.61 ? 51  GLU   A OE2 1 
ATOM   310  N  N   . SER   A 1 52  ? 28.878 3.163   -5.074  1.00 12.29 ? 52  SER   A N   1 
ATOM   311  C  CA  . SER   A 1 52  ? 28.039 2.605   -4.002  1.00 12.89 ? 52  SER   A CA  1 
ATOM   312  C  C   . SER   A 1 52  ? 27.316 1.341   -4.413  1.00 8.54  ? 52  SER   A C   1 
ATOM   313  O  O   . SER   A 1 52  ? 26.488 0.780   -3.663  1.00 8.61  ? 52  SER   A O   1 
ATOM   314  C  CB  . SER   A 1 52  ? 27.066 3.652   -3.525  1.00 18.11 ? 52  SER   A CB  1 
ATOM   315  O  OG  . SER   A 1 52  ? 26.152 3.886   -4.565  1.00 22.10 ? 52  SER   A OG  1 
ATOM   316  N  N   . GLY   A 1 53  ? 27.618 0.863   -5.615  1.00 7.54  ? 53  GLY   A N   1 
ATOM   317  C  CA  . GLY   A 1 53  ? 26.976 -0.307  -6.145  1.00 7.31  ? 53  GLY   A CA  1 
ATOM   318  C  C   . GLY   A 1 53  ? 25.568 -0.110  -6.718  1.00 7.97  ? 53  GLY   A C   1 
ATOM   319  O  O   . GLY   A 1 53  ? 24.882 -1.117  -6.995  1.00 8.85  ? 53  GLY   A O   1 
ATOM   320  N  N   . GLU   A 1 54  ? 25.174 1.136   -6.931  1.00 9.35  ? 54  GLU   A N   1 
ATOM   321  C  CA  . GLU   A 1 54  ? 23.789 1.449   -7.323  1.00 9.48  ? 54  GLU   A CA  1 
ATOM   322  C  C   . GLU   A 1 54  ? 23.784 1.962   -8.748  1.00 9.53  ? 54  GLU   A C   1 
ATOM   323  O  O   . GLU   A 1 54  ? 24.724 2.556   -9.234  1.00 10.59 ? 54  GLU   A O   1 
ATOM   324  C  CB  . GLU   A 1 54  ? 23.247 2.480   -6.333  1.00 13.23 ? 54  GLU   A CB  1 
ATOM   325  C  CG  . GLU   A 1 54  ? 23.258 1.915   -4.896  1.00 15.46 ? 54  GLU   A CG  1 
ATOM   326  C  CD  . GLU   A 1 54  ? 22.361 2.637   -3.911  1.00 22.07 ? 54  GLU   A CD  1 
ATOM   327  O  OE1 . GLU   A 1 54  ? 21.750 3.634   -4.277  1.00 24.10 ? 54  GLU   A OE1 1 
ATOM   328  O  OE2 . GLU   A 1 54  ? 22.246 2.198   -2.748  1.00 28.07 ? 54  GLU   A OE2 1 
ATOM   329  N  N   . LEU   A 1 55  ? 22.652 1.763   -9.409  1.00 8.25  ? 55  LEU   A N   1 
ATOM   330  C  CA  . LEU   A 1 55  ? 22.463 2.126   -10.758 1.00 9.33  ? 55  LEU   A CA  1 
ATOM   331  C  C   . LEU   A 1 55  ? 21.070 2.752   -10.745 1.00 12.62 ? 55  LEU   A C   1 
ATOM   332  O  O   . LEU   A 1 55  ? 20.066 2.019   -10.620 1.00 11.51 ? 55  LEU   A O   1 
ATOM   333  C  CB  . LEU   A 1 55  ? 22.526 0.905   -11.660 1.00 10.62 ? 55  LEU   A CB  1 
ATOM   334  C  CG  . LEU   A 1 55  ? 22.252 1.100   -13.162 1.00 11.47 ? 55  LEU   A CG  1 
ATOM   335  C  CD1 . LEU   A 1 55  ? 22.898 2.318   -13.775 1.00 13.96 ? 55  LEU   A CD1 1 
ATOM   336  C  CD2 . LEU   A 1 55  ? 22.555 -0.161  -13.945 1.00 13.27 ? 55  LEU   A CD2 1 
ATOM   337  N  N   . HIS   A 1 56  ? 21.103 4.081   -10.860 1.00 15.24 ? 56  HIS   A N   1 
ATOM   338  C  CA  . HIS   A 1 56  ? 19.974 4.993   -10.999 1.00 18.32 ? 56  HIS   A CA  1 
ATOM   339  C  C   . HIS   A 1 56  ? 20.102 5.565   -12.443 1.00 22.54 ? 56  HIS   A C   1 
ATOM   340  O  O   . HIS   A 1 56  ? 21.169 5.627   -13.061 1.00 26.00 ? 56  HIS   A O   1 
ATOM   341  C  CB  . HIS   A 1 56  ? 19.991 6.126   -9.933  1.00 20.73 ? 56  HIS   A CB  1 
ATOM   342  C  CG  . HIS   A 1 56  ? 19.932 5.635   -8.517  1.00 25.74 ? 56  HIS   A CG  1 
ATOM   343  N  ND1 . HIS   A 1 56  ? 21.058 5.407   -7.754  1.00 31.34 ? 56  HIS   A ND1 1 
ATOM   344  C  CD2 . HIS   A 1 56  ? 18.875 5.367   -7.714  1.00 24.15 ? 56  HIS   A CD2 1 
ATOM   345  C  CE1 . HIS   A 1 56  ? 20.699 4.992   -6.552  1.00 27.20 ? 56  HIS   A CE1 1 
ATOM   346  N  NE2 . HIS   A 1 56  ? 19.379 4.950   -6.503  1.00 36.94 ? 56  HIS   A NE2 1 
ATOM   347  N  N   . GLY   A 1 57  ? 18.987 5.935   -12.988 1.00 21.69 ? 57  GLY   A N   1 
ATOM   348  C  CA  . GLY   A 1 57  ? 18.964 6.534   -14.280 1.00 18.62 ? 57  GLY   A CA  1 
ATOM   349  C  C   . GLY   A 1 57  ? 18.882 5.609   -15.468 1.00 16.35 ? 57  GLY   A C   1 
ATOM   350  O  O   . GLY   A 1 57  ? 19.034 6.076   -16.620 1.00 19.30 ? 57  GLY   A O   1 
ATOM   351  N  N   . LEU   A 1 58  ? 18.576 4.341   -15.241 1.00 14.96 ? 58  LEU   A N   1 
ATOM   352  C  CA  . LEU   A 1 58  ? 18.411 3.393   -16.349 1.00 17.85 ? 58  LEU   A CA  1 
ATOM   353  C  C   . LEU   A 1 58  ? 17.333 3.801   -17.322 1.00 17.24 ? 58  LEU   A C   1 
ATOM   354  O  O   . LEU   A 1 58  ? 17.473 3.585   -18.528 1.00 18.17 ? 58  LEU   A O   1 
ATOM   355  C  CB  . LEU   A 1 58  ? 18.060 2.000   -15.872 1.00 17.48 ? 58  LEU   A CB  1 
ATOM   356  C  CG  . LEU   A 1 58  ? 19.129 1.038   -15.466 1.00 19.13 ? 58  LEU   A CG  1 
ATOM   357  C  CD1 . LEU   A 1 58  ? 18.519 -0.226  -14.870 1.00 18.08 ? 58  LEU   A CD1 1 
ATOM   358  C  CD2 . LEU   A 1 58  ? 19.946 0.724   -16.694 1.00 15.35 ? 58  LEU   A CD2 1 
ATOM   359  N  N   . THR   A 1 59  ? 16.250 4.363   -16.794 1.00 15.65 ? 59  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 59  ? 15.091 4.606   -17.601 1.00 12.77 ? 59  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 59  ? 14.310 5.760   -17.005 1.00 16.39 ? 59  THR   A C   1 
ATOM   362  O  O   . THR   A 1 59  ? 14.707 6.339   -15.958 1.00 16.69 ? 59  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 59  ? 14.222 3.322   -17.771 1.00 10.86 ? 59  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 59  ? 13.278 3.517   -18.797 1.00 14.89 ? 59  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 59  ? 13.470 2.976   -16.461 1.00 13.44 ? 59  THR   A CG2 1 
ATOM   366  N  N   . THR   A 1 60  ? 13.132 6.003   -17.586 1.00 14.19 ? 60  THR   A N   1 
ATOM   367  C  CA  . THR   A 1 60  ? 12.266 7.114   -17.189 1.00 14.83 ? 60  THR   A CA  1 
ATOM   368  C  C   . THR   A 1 60  ? 10.845 6.604   -17.095 1.00 13.19 ? 60  THR   A C   1 
ATOM   369  O  O   . THR   A 1 60  ? 10.546 5.572   -17.687 1.00 12.79 ? 60  THR   A O   1 
ATOM   370  C  CB  . THR   A 1 60  ? 12.300 8.241   -18.221 1.00 16.39 ? 60  THR   A CB  1 
ATOM   371  O  OG1 . THR   A 1 60  ? 11.846 7.771   -19.481 1.00 20.01 ? 60  THR   A OG1 1 
ATOM   372  C  CG2 . THR   A 1 60  ? 13.679 8.737   -18.374 1.00 18.89 ? 60  THR   A CG2 1 
ATOM   373  N  N   . GLU   A 1 61  ? 9.992  7.303   -16.319 1.00 11.79 ? 61  GLU   A N   1 
ATOM   374  C  CA  . GLU   A 1 61  ? 8.519  6.984   -16.278 1.00 15.09 ? 61  GLU   A CA  1 
ATOM   375  C  C   . GLU   A 1 61  ? 7.922  6.812   -17.671 1.00 13.83 ? 61  GLU   A C   1 
ATOM   376  O  O   . GLU   A 1 61  ? 7.063  5.946   -17.911 1.00 16.54 ? 61  GLU   A O   1 
ATOM   377  C  CB  . GLU   A 1 61  ? 7.743  8.086   -15.545 1.00 18.36 ? 61  GLU   A CB  1 
ATOM   378  N  N   . GLU   A 1 62  ? 8.357  7.661   -18.591 1.00 13.35 ? 62  GLU   A N   1 
ATOM   379  C  CA  . GLU   A 1 62  ? 7.728  7.723   -19.891 1.00 16.49 ? 62  GLU   A CA  1 
ATOM   380  C  C   . GLU   A 1 62  ? 8.169  6.487   -20.730 1.00 12.53 ? 62  GLU   A C   1 
ATOM   381  O  O   . GLU   A 1 62  ? 7.455  6.050   -21.618 1.00 19.84 ? 62  GLU   A O   1 
ATOM   382  C  CB  . GLU   A 1 62  ? 8.044  9.065   -20.597 1.00 20.76 ? 62  GLU   A CB  1 
ATOM   383  C  CG  . GLU   A 1 62  ? 8.109  10.350  -19.747 1.00 22.63 ? 62  GLU   A CG  1 
ATOM   384  C  CD  . GLU   A 1 62  ? 9.514  10.540  -19.155 0.50 22.88 ? 62  GLU   A CD  1 
ATOM   385  O  OE1 . GLU   A 1 62  ? 10.517 10.491  -19.893 0.50 27.05 ? 62  GLU   A OE1 1 
ATOM   386  O  OE2 . GLU   A 1 62  ? 9.622  10.724  -17.955 0.50 22.74 ? 62  GLU   A OE2 1 
ATOM   387  N  N   . GLU   A 1 63  ? 9.345  5.899   -20.480 1.00 9.96  ? 63  GLU   A N   1 
ATOM   388  C  CA  . GLU   A 1 63  ? 9.814  4.832   -21.299 1.00 10.04 ? 63  GLU   A CA  1 
ATOM   389  C  C   . GLU   A 1 63  ? 9.441  3.490   -20.717 1.00 9.63  ? 63  GLU   A C   1 
ATOM   390  O  O   . GLU   A 1 63  ? 9.388  2.507   -21.423 1.00 10.90 ? 63  GLU   A O   1 
ATOM   391  C  CB  . GLU   A 1 63  ? 11.362 4.897   -21.450 1.00 9.52  ? 63  GLU   A CB  1 
ATOM   392  C  CG  . GLU   A 1 63  ? 11.843 6.103   -22.227 1.00 11.43 ? 63  GLU   A CG  1 
ATOM   393  C  CD  . GLU   A 1 63  ? 13.356 6.157   -22.235 1.00 15.73 ? 63  GLU   A CD  1 
ATOM   394  O  OE1 . GLU   A 1 63  ? 13.893 6.852   -21.353 1.00 22.33 ? 63  GLU   A OE1 1 
ATOM   395  O  OE2 . GLU   A 1 63  ? 14.021 5.516   -23.112 1.00 22.01 ? 63  GLU   A OE2 1 
ATOM   396  N  N   . PHE   A 1 64  ? 9.211  3.441   -19.392 1.00 9.79  ? 64  PHE   A N   1 
ATOM   397  C  CA  . PHE   A 1 64  ? 9.008  2.186   -18.680 1.00 9.62  ? 64  PHE   A CA  1 
ATOM   398  C  C   . PHE   A 1 64  ? 7.546  1.754   -18.656 1.00 10.89 ? 64  PHE   A C   1 
ATOM   399  O  O   . PHE   A 1 64  ? 6.807  2.086   -17.738 1.00 15.65 ? 64  PHE   A O   1 
ATOM   400  C  CB  . PHE   A 1 64  ? 9.568  2.397   -17.273 1.00 10.37 ? 64  PHE   A CB  1 
ATOM   401  C  CG  . PHE   A 1 64  ? 9.623  1.169   -16.421 1.00 9.56  ? 64  PHE   A CG  1 
ATOM   402  C  CD1 . PHE   A 1 64  ? 10.202 -0.007  -16.854 1.00 11.38 ? 64  PHE   A CD1 1 
ATOM   403  C  CD2 . PHE   A 1 64  ? 9.078  1.220   -15.128 1.00 14.12 ? 64  PHE   A CD2 1 
ATOM   404  C  CE1 . PHE   A 1 64  ? 10.305 -1.122  -15.991 1.00 10.89 ? 64  PHE   A CE1 1 
ATOM   405  C  CE2 . PHE   A 1 64  ? 9.188  0.149   -14.287 1.00 13.59 ? 64  PHE   A CE2 1 
ATOM   406  C  CZ  . PHE   A 1 64  ? 9.766  -1.041  -14.718 1.00 12.45 ? 64  PHE   A CZ  1 
ATOM   407  N  N   . VAL   A 1 65  ? 7.208  0.976   -19.658 1.00 8.13  ? 65  VAL   A N   1 
ATOM   408  C  CA  . VAL   A 1 65  ? 5.834  0.527   -19.950 1.00 6.26  ? 65  VAL   A CA  1 
ATOM   409  C  C   . VAL   A 1 65  ? 5.599  -0.855  -19.387 1.00 7.82  ? 65  VAL   A C   1 
ATOM   410  O  O   . VAL   A 1 65  ? 6.474  -1.491  -18.772 1.00 7.38  ? 65  VAL   A O   1 
ATOM   411  C  CB  . VAL   A 1 65  ? 5.642  0.614   -21.492 1.00 6.63  ? 65  VAL   A CB  1 
ATOM   412  C  CG1 . VAL   A 1 65  ? 5.677  2.076   -21.925 1.00 8.78  ? 65  VAL   A CG1 1 
ATOM   413  C  CG2 . VAL   A 1 65  ? 6.690  -0.219  -22.171 1.00 6.81  ? 65  VAL   A CG2 1 
ATOM   414  N  N   . GLU   A 1 66  ? 4.379  -1.299  -19.404 1.00 9.21  ? 66  GLU   A N   1 
ATOM   415  C  CA  . GLU   A 1 66  ? 4.048  -2.676  -19.065 1.00 8.93  ? 66  GLU   A CA  1 
ATOM   416  C  C   . GLU   A 1 66  ? 4.868  -3.595  -19.922 1.00 9.29  ? 66  GLU   A C   1 
ATOM   417  O  O   . GLU   A 1 66  ? 5.250  -3.265  -21.099 1.00 10.90 ? 66  GLU   A O   1 
ATOM   418  C  CB  . GLU   A 1 66  ? 2.565  -2.976  -19.414 1.00 13.46 ? 66  GLU   A CB  1 
ATOM   419  C  CG  . GLU   A 1 66  ? 1.604  -2.289  -18.610 1.00 15.51 ? 66  GLU   A CG  1 
ATOM   420  C  CD  . GLU   A 1 66  ? 0.248  -2.900  -19.003 1.00 13.28 ? 66  GLU   A CD  1 
ATOM   421  O  OE1 . GLU   A 1 66  ? -0.383 -2.565  -20.076 1.00 14.24 ? 66  GLU   A OE1 1 
ATOM   422  O  OE2 . GLU   A 1 66  ? -0.159 -3.750  -18.275 1.00 14.27 ? 66  GLU   A OE2 1 
ATOM   423  N  N   . GLY   A 1 67  ? 5.211  -4.731  -19.327 1.00 10.70 ? 67  GLY   A N   1 
ATOM   424  C  CA  . GLY   A 1 67  ? 5.889  -5.770  -20.048 1.00 10.58 ? 67  GLY   A CA  1 
ATOM   425  C  C   . GLY   A 1 67  ? 6.624  -6.767  -19.147 1.00 8.60  ? 67  GLY   A C   1 
ATOM   426  O  O   . GLY   A 1 67  ? 6.561  -6.694  -17.896 1.00 10.31 ? 67  GLY   A O   1 
ATOM   427  N  N   . ILE   A 1 68  ? 7.246  -7.747  -19.798 1.00 8.41  ? 68  ILE   A N   1 
ATOM   428  C  CA  . ILE   A 1 68  ? 8.131  -8.653  -19.114 1.00 6.69  ? 68  ILE   A CA  1 
ATOM   429  C  C   . ILE   A 1 68  ? 9.579  -8.148  -19.327 1.00 6.14  ? 68  ILE   A C   1 
ATOM   430  O  O   . ILE   A 1 68  ? 9.982  -8.003  -20.423 1.00 7.84  ? 68  ILE   A O   1 
ATOM   431  C  CB  . ILE   A 1 68  ? 8.003  -10.119 -19.589 1.00 8.13  ? 68  ILE   A CB  1 
ATOM   432  C  CG1 . ILE   A 1 68  ? 6.575  -10.601 -19.310 1.00 12.72 ? 68  ILE   A CG1 1 
ATOM   433  C  CG2 . ILE   A 1 68  ? 8.999  -10.980 -18.824 1.00 9.98  ? 68  ILE   A CG2 1 
ATOM   434  C  CD1 . ILE   A 1 68  ? 6.285  -11.983 -19.812 1.00 19.32 ? 68  ILE   A CD1 1 
ATOM   435  N  N   . TYR   A 1 69  ? 10.268 -7.853  -18.225 1.00 7.25  ? 69  TYR   A N   1 
ATOM   436  C  CA  . TYR   A 1 69  ? 11.608 -7.297  -18.239 1.00 6.22  ? 69  TYR   A CA  1 
ATOM   437  C  C   . TYR   A 1 69  ? 12.574 -8.305  -17.696 1.00 6.69  ? 69  TYR   A C   1 
ATOM   438  O  O   . TYR   A 1 69  ? 12.305 -9.066  -16.776 1.00 7.94  ? 69  TYR   A O   1 
ATOM   439  C  CB  . TYR   A 1 69  ? 11.680 -6.058  -17.430 1.00 7.54  ? 69  TYR   A CB  1 
ATOM   440  C  CG  . TYR   A 1 69  ? 10.984 -4.891  -18.040 1.00 7.65  ? 69  TYR   A CG  1 
ATOM   441  C  CD1 . TYR   A 1 69  ? 9.626  -4.690  -17.834 1.00 8.01  ? 69  TYR   A CD1 1 
ATOM   442  C  CD2 . TYR   A 1 69  ? 11.626 -3.987  -18.850 1.00 7.59  ? 69  TYR   A CD2 1 
ATOM   443  C  CE1 . TYR   A 1 69  ? 8.990  -3.615  -18.418 1.00 8.51  ? 69  TYR   A CE1 1 
ATOM   444  C  CE2 . TYR   A 1 69  ? 10.991 -2.914  -19.415 1.00 10.06 ? 69  TYR   A CE2 1 
ATOM   445  C  CZ  . TYR   A 1 69  ? 9.633  -2.720  -19.169 1.00 8.35  ? 69  TYR   A CZ  1 
ATOM   446  O  OH  . TYR   A 1 69  ? 9.040  -1.641  -19.738 1.00 9.74  ? 69  TYR   A OH  1 
ATOM   447  N  N   . LYS   A 1 70  ? 13.722 -8.336  -18.349 1.00 7.37  ? 70  LYS   A N   1 
ATOM   448  C  CA  . LYS   A 1 70  ? 14.886 -9.148  -17.892 1.00 8.32  ? 70  LYS   A CA  1 
ATOM   449  C  C   . LYS   A 1 70  ? 16.022 -8.169  -17.552 1.00 7.82  ? 70  LYS   A C   1 
ATOM   450  O  O   . LYS   A 1 70  ? 16.414 -7.335  -18.358 1.00 10.47 ? 70  LYS   A O   1 
ATOM   451  C  CB  . LYS   A 1 70  ? 15.323 -10.145 -19.011 1.00 8.22  ? 70  LYS   A CB  1 
ATOM   452  C  CG  . LYS   A 1 70  ? 16.660 -10.794 -18.755 1.00 12.69 ? 70  LYS   A CG  1 
ATOM   453  C  CD  . LYS   A 1 70  ? 16.907 -11.988 -19.633 1.00 16.44 ? 70  LYS   A CD  1 
ATOM   454  C  CE  . LYS   A 1 70  ? 17.044 -11.647 -21.116 1.00 23.52 ? 70  LYS   A CE  1 
ATOM   455  N  NZ  . LYS   A 1 70  ? 15.825 -11.965 -21.927 0.50 24.50 ? 70  LYS   A NZ  1 
ATOM   456  N  N   . VAL   A 1 71  ? 16.499 -8.280  -16.321 1.00 7.23  ? 71  VAL   A N   1 
ATOM   457  C  CA  . VAL   A 1 71  ? 17.664 -7.560  -15.876 1.00 8.72  ? 71  VAL   A CA  1 
ATOM   458  C  C   . VAL   A 1 71  ? 18.786 -8.567  -15.772 1.00 9.24  ? 71  VAL   A C   1 
ATOM   459  O  O   . VAL   A 1 71  ? 18.715 -9.520  -14.993 1.00 11.89 ? 71  VAL   A O   1 
ATOM   460  C  CB  . VAL   A 1 71  ? 17.437 -6.895  -14.503 1.00 9.44  ? 71  VAL   A CB  1 
ATOM   461  C  CG1 . VAL   A 1 71  ? 18.693 -6.236  -13.980 1.00 11.89 ? 71  VAL   A CG1 1 
ATOM   462  C  CG2 . VAL   A 1 71  ? 16.311 -5.846  -14.592 1.00 10.76 ? 71  VAL   A CG2 1 
ATOM   463  N  N   . GLU   A 1 72  ? 19.844 -8.335  -16.558 1.00 10.93 ? 72  GLU   A N   1 
ATOM   464  C  CA  . GLU   A 1 72  ? 20.986 -9.194  -16.531 1.00 10.08 ? 72  GLU   A CA  1 
ATOM   465  C  C   . GLU   A 1 72  ? 22.205 -8.418  -15.990 1.00 10.05 ? 72  GLU   A C   1 
ATOM   466  O  O   . GLU   A 1 72  ? 22.549 -7.389  -16.521 1.00 13.85 ? 72  GLU   A O   1 
ATOM   467  C  CB  . GLU   A 1 72  ? 21.403 -9.665  -17.949 1.00 13.26 ? 72  GLU   A CB  1 
ATOM   468  C  CG  . GLU   A 1 72  ? 20.552 -10.695 -18.665 1.00 19.23 ? 72  GLU   A CG  1 
ATOM   469  C  CD  . GLU   A 1 72  ? 21.216 -11.175 -19.958 1.00 21.89 ? 72  GLU   A CD  1 
ATOM   470  O  OE1 . GLU   A 1 72  ? 22.196 -10.574 -20.391 1.00 25.52 ? 72  GLU   A OE1 1 
ATOM   471  O  OE2 . GLU   A 1 72  ? 20.769 -12.144 -20.563 1.00 28.64 ? 72  GLU   A OE2 1 
ATOM   472  N  N   . ILE   A 1 73  ? 22.816 -8.948  -14.952 1.00 10.15 ? 73  ILE   A N   1 
ATOM   473  C  CA  . ILE   A 1 73  ? 23.984 -8.352  -14.324 1.00 7.84  ? 73  ILE   A CA  1 
ATOM   474  C  C   . ILE   A 1 73  ? 25.157 -9.182  -14.761 1.00 8.04  ? 73  ILE   A C   1 
ATOM   475  O  O   . ILE   A 1 73  ? 25.204 -10.391 -14.573 1.00 10.27 ? 73  ILE   A O   1 
ATOM   476  C  CB  . ILE   A 1 73  ? 23.796 -8.427  -12.810 1.00 7.99  ? 73  ILE   A CB  1 
ATOM   477  C  CG1 . ILE   A 1 73  ? 22.481 -7.756  -12.380 1.00 10.62 ? 73  ILE   A CG1 1 
ATOM   478  C  CG2 . ILE   A 1 73  ? 25.009 -7.902  -12.042 1.00 9.14  ? 73  ILE   A CG2 1 
ATOM   479  C  CD1 . ILE   A 1 73  ? 22.120 -7.878  -10.898 1.00 12.42 ? 73  ILE   A CD1 1 
ATOM   480  N  N   . ASP   A 1 74  ? 26.147 -8.501  -15.316 1.00 8.83  ? 74  ASP   A N   1 
ATOM   481  C  CA  . ASP   A 1 74  ? 27.343 -9.107  -15.889 1.00 11.75 ? 74  ASP   A CA  1 
ATOM   482  C  C   . ASP   A 1 74  ? 28.365 -9.553  -14.855 1.00 8.89  ? 74  ASP   A C   1 
ATOM   483  O  O   . ASP   A 1 74  ? 29.474 -8.964  -14.751 1.00 12.25 ? 74  ASP   A O   1 
ATOM   484  C  CB  . ASP   A 1 74  ? 27.998 -8.136  -16.894 1.00 12.43 ? 74  ASP   A CB  1 
ATOM   485  C  CG  . ASP   A 1 74  ? 29.304 -8.711  -17.510 1.00 16.23 ? 74  ASP   A CG  1 
ATOM   486  O  OD1 . ASP   A 1 74  ? 29.446 -9.963  -17.590 1.00 17.34 ? 74  ASP   A OD1 1 
ATOM   487  O  OD2 . ASP   A 1 74  ? 30.165 -7.894  -17.948 1.00 25.05 ? 74  ASP   A OD2 1 
ATOM   488  N  N   . THR   A 1 75  ? 27.994 -10.576 -14.114 1.00 10.93 ? 75  THR   A N   1 
ATOM   489  C  CA  . THR   A 1 75  ? 28.801 -11.102 -13.022 1.00 8.59  ? 75  THR   A CA  1 
ATOM   490  C  C   . THR   A 1 75  ? 30.103 -11.715 -13.541 1.00 8.65  ? 75  THR   A C   1 
ATOM   491  O  O   . THR   A 1 75  ? 31.094 -11.598 -12.871 1.00 9.23  ? 75  THR   A O   1 
ATOM   492  C  CB  . THR   A 1 75  ? 28.005 -12.086 -12.177 1.00 11.80 ? 75  THR   A CB  1 
ATOM   493  O  OG1 . THR   A 1 75  ? 27.578 -13.191 -12.999 1.00 10.77 ? 75  THR   A OG1 1 
ATOM   494  C  CG2 . THR   A 1 75  ? 26.801 -11.293 -11.517 1.00 7.36  ? 75  THR   A CG2 1 
ATOM   495  N  N   . LYS   A 1 76  ? 30.071 -12.346 -14.711 1.00 7.74  ? 76  LYS   A N   1 
ATOM   496  C  CA  . LYS   A 1 76  ? 31.250 -12.986 -15.242 1.00 10.14 ? 76  LYS   A CA  1 
ATOM   497  C  C   . LYS   A 1 76  ? 32.380 -11.935 -15.391 1.00 10.54 ? 76  LYS   A C   1 
ATOM   498  O  O   . LYS   A 1 76  ? 33.527 -12.167 -14.926 1.00 9.80  ? 76  LYS   A O   1 
ATOM   499  C  CB  . LYS   A 1 76  ? 31.002 -13.681 -16.562 1.00 12.79 ? 76  LYS   A CB  1 
ATOM   500  C  CG  . LYS   A 1 76  ? 32.031 -14.735 -17.003 1.00 18.50 ? 76  LYS   A CG  1 
ATOM   501  N  N   . SER   A 1 77  ? 32.109 -10.806 -16.047 1.00 8.76  ? 77  SER   A N   1 
ATOM   502  C  CA  . SER   A 1 77  ? 33.212 -9.772  -16.275 1.00 10.22 ? 77  SER   A CA  1 
ATOM   503  C  C   . SER   A 1 77  ? 33.720 -9.215  -14.973 1.00 8.56  ? 77  SER   A C   1 
ATOM   504  O  O   . SER   A 1 77  ? 34.901 -8.955  -14.776 1.00 11.18 ? 77  SER   A O   1 
ATOM   505  C  CB  . SER   A 1 77  ? 32.776 -8.582  -17.134 1.00 11.39 ? 77  SER   A CB  1 
ATOM   506  O  OG  . SER   A 1 77  ? 32.309 -9.075  -18.332 1.00 15.96 ? 77  SER   A OG  1 
ATOM   507  N  N   . TYR   A 1 78  ? 32.797 -9.067  -14.054 1.00 7.96  ? 78  TYR   A N   1 
ATOM   508  C  CA  . TYR   A 1 78  ? 33.096 -8.464  -12.761 1.00 7.58  ? 78  TYR   A CA  1 
ATOM   509  C  C   . TYR   A 1 78  ? 34.047 -9.363  -12.023 1.00 8.19  ? 78  TYR   A C   1 
ATOM   510  O  O   . TYR   A 1 78  ? 35.126 -8.905  -11.563 1.00 9.23  ? 78  TYR   A O   1 
ATOM   511  C  CB  . TYR   A 1 78  ? 31.794 -8.366  -11.943 1.00 7.13  ? 78  TYR   A CB  1 
ATOM   512  C  CG  . TYR   A 1 78  ? 31.963 -7.823  -10.554 1.00 6.82  ? 78  TYR   A CG  1 
ATOM   513  C  CD1 . TYR   A 1 78  ? 32.273 -6.473  -10.329 1.00 7.74  ? 78  TYR   A CD1 1 
ATOM   514  C  CD2 . TYR   A 1 78  ? 31.935 -8.684  -9.469  1.00 6.66  ? 78  TYR   A CD2 1 
ATOM   515  C  CE1 . TYR   A 1 78  ? 32.455 -5.989  -9.046  1.00 7.18  ? 78  TYR   A CE1 1 
ATOM   516  C  CE2 . TYR   A 1 78  ? 32.113 -8.221  -8.183  1.00 6.17  ? 78  TYR   A CE2 1 
ATOM   517  C  CZ  . TYR   A 1 78  ? 32.409 -6.852  -7.980  1.00 6.51  ? 78  TYR   A CZ  1 
ATOM   518  O  OH  . TYR   A 1 78  ? 32.616 -6.344  -6.700  1.00 6.89  ? 78  TYR   A OH  1 
ATOM   519  N  N   . TRP   A 1 79  ? 33.708 -10.631 -11.884 1.00 8.05  ? 79  TRP   A N   1 
ATOM   520  C  CA  . TRP   A 1 79  ? 34.624 -11.537 -11.192 1.00 7.83  ? 79  TRP   A CA  1 
ATOM   521  C  C   . TRP   A 1 79  ? 35.945 -11.740 -11.909 1.00 8.68  ? 79  TRP   A C   1 
ATOM   522  O  O   . TRP   A 1 79  ? 37.017 -11.713 -11.261 1.00 10.10 ? 79  TRP   A O   1 
ATOM   523  C  CB  . TRP   A 1 79  ? 34.009 -12.877 -10.933 1.00 9.12  ? 79  TRP   A CB  1 
ATOM   524  C  CG  . TRP   A 1 79  ? 32.823 -12.854 -9.981  1.00 7.84  ? 79  TRP   A CG  1 
ATOM   525  C  CD1 . TRP   A 1 79  ? 31.534 -13.296 -10.258 1.00 9.22  ? 79  TRP   A CD1 1 
ATOM   526  C  CD2 . TRP   A 1 79  ? 32.818 -12.433 -8.629  1.00 7.29  ? 79  TRP   A CD2 1 
ATOM   527  N  NE1 . TRP   A 1 79  ? 30.762 -13.129 -9.138  1.00 9.43  ? 79  TRP   A NE1 1 
ATOM   528  C  CE2 . TRP   A 1 79  ? 31.490 -12.547 -8.144  1.00 8.22  ? 79  TRP   A CE2 1 
ATOM   529  C  CE3 . TRP   A 1 79  ? 33.772 -11.857 -7.784  1.00 10.17 ? 79  TRP   A CE3 1 
ATOM   530  C  CZ2 . TRP   A 1 79  ? 31.145 -12.232 -6.836  1.00 8.11  ? 79  TRP   A CZ2 1 
ATOM   531  C  CZ3 . TRP   A 1 79  ? 33.420 -11.535 -6.446  1.00 8.74  ? 79  TRP   A CZ3 1 
ATOM   532  C  CH2 . TRP   A 1 79  ? 32.077 -11.705 -6.001  1.00 8.38  ? 79  TRP   A CH2 1 
ATOM   533  N  N   . LYS   A 1 80  ? 35.907 -11.875 -13.225 1.00 8.91  ? 80  LYS   A N   1 
ATOM   534  C  CA  . LYS   A 1 80  ? 37.155 -12.091 -13.959 1.00 9.05  ? 80  LYS   A CA  1 
ATOM   535  C  C   . LYS   A 1 80  ? 38.117 -10.859 -13.732 1.00 11.61 ? 80  LYS   A C   1 
ATOM   536  O  O   . LYS   A 1 80  ? 39.334 -11.065 -13.568 1.00 10.52 ? 80  LYS   A O   1 
ATOM   537  C  CB  . LYS   A 1 80  ? 36.900 -12.335 -15.461 1.00 12.02 ? 80  LYS   A CB  1 
ATOM   538  C  CG  . LYS   A 1 80  ? 36.309 -13.699 -15.818 1.00 18.33 ? 80  LYS   A CG  1 
ATOM   539  C  CD  . LYS   A 1 80  ? 37.271 -14.885 -15.644 1.00 26.75 ? 80  LYS   A CD  1 
ATOM   540  N  N   . ALA   A 1 81  ? 37.577 -9.634  -13.694 1.00 8.75  ? 81  ALA   A N   1 
ATOM   541  C  CA  . ALA   A 1 81  ? 38.404 -8.433  -13.522 1.00 9.96  ? 81  ALA   A CA  1 
ATOM   542  C  C   . ALA   A 1 81  ? 39.051 -8.327  -12.104 1.00 10.28 ? 81  ALA   A C   1 
ATOM   543  O  O   . ALA   A 1 81  ? 40.005 -7.611  -11.928 1.00 15.38 ? 81  ALA   A O   1 
ATOM   544  C  CB  . ALA   A 1 81  ? 37.636 -7.169  -13.882 1.00 11.76 ? 81  ALA   A CB  1 
ATOM   545  N  N   . LEU   A 1 82  ? 38.487 -9.062  -11.137 1.00 10.06 ? 82  LEU   A N   1 
ATOM   546  C  CA  . LEU   A 1 82  ? 38.978 -9.157  -9.791  1.00 11.99 ? 82  LEU   A CA  1 
ATOM   547  C  C   . LEU   A 1 82  ? 39.878 -10.367 -9.546  1.00 12.73 ? 82  LEU   A C   1 
ATOM   548  O  O   . LEU   A 1 82  ? 40.347 -10.561 -8.418  1.00 16.73 ? 82  LEU   A O   1 
ATOM   549  C  CB  . LEU   A 1 82  ? 37.806 -9.202  -8.824  1.00 12.12 ? 82  LEU   A CB  1 
ATOM   550  C  CG  . LEU   A 1 82  ? 36.974 -7.937  -8.749  1.00 14.14 ? 82  LEU   A CG  1 
ATOM   551  C  CD1 . LEU   A 1 82  ? 35.896 -8.238  -7.738  1.00 19.66 ? 82  LEU   A CD1 1 
ATOM   552  C  CD2 . LEU   A 1 82  ? 37.725 -6.663  -8.370  1.00 18.82 ? 82  LEU   A CD2 1 
ATOM   553  N  N   . GLY   A 1 83  ? 40.059 -11.197 -10.564 1.00 11.20 ? 83  GLY   A N   1 
ATOM   554  C  CA  . GLY   A 1 83  ? 40.963 -12.355 -10.519 1.00 13.41 ? 83  GLY   A CA  1 
ATOM   555  C  C   . GLY   A 1 83  ? 40.284 -13.533 -9.834  1.00 16.41 ? 83  GLY   A C   1 
ATOM   556  O  O   . GLY   A 1 83  ? 40.934 -14.390 -9.205  1.00 13.69 ? 83  GLY   A O   1 
ATOM   557  N  N   . ILE   A 1 84  ? 38.946 -13.582 -9.966  1.00 11.71 ? 84  ILE   A N   1 
ATOM   558  C  CA  . ILE   A 1 84  ? 38.162 -14.622 -9.322  1.00 10.56 ? 84  ILE   A CA  1 
ATOM   559  C  C   . ILE   A 1 84  ? 37.394 -15.434 -10.387 1.00 12.05 ? 84  ILE   A C   1 
ATOM   560  O  O   . ILE   A 1 84  ? 37.033 -14.900 -11.467 1.00 14.71 ? 84  ILE   A O   1 
ATOM   561  C  CB  . ILE   A 1 84  ? 37.184 -13.978 -8.281  1.00 13.73 ? 84  ILE   A CB  1 
ATOM   562  C  CG1 . ILE   A 1 84  ? 37.961 -13.452 -7.059  1.00 20.37 ? 84  ILE   A CG1 1 
ATOM   563  C  CG2 . ILE   A 1 84  ? 36.091 -14.968 -7.882  1.00 10.47 ? 84  ILE   A CG2 1 
ATOM   564  C  CD1 . ILE   A 1 84  ? 37.326 -12.274 -6.394  1.00 23.62 ? 84  ILE   A CD1 1 
ATOM   565  N  N   . SER   A 1 85  ? 37.272 -16.722 -10.100 1.00 12.27 ? 85  SER   A N   1 
ATOM   566  C  CA  A SER   A 1 85  ? 36.632 -17.691 -10.985 0.50 16.13 ? 85  SER   A CA  1 
ATOM   567  C  CA  B SER   A 1 85  ? 36.627 -17.674 -10.996 0.50 16.16 ? 85  SER   A CA  1 
ATOM   568  C  C   . SER   A 1 85  ? 35.115 -17.633 -10.818 1.00 18.83 ? 85  SER   A C   1 
ATOM   569  O  O   . SER   A 1 85  ? 34.584 -18.079 -9.777  1.00 21.79 ? 85  SER   A O   1 
ATOM   570  C  CB  A SER   A 1 85  ? 37.126 -19.114 -10.689 0.50 19.18 ? 85  SER   A CB  1 
ATOM   571  C  CB  B SER   A 1 85  ? 37.129 -19.095 -10.759 0.50 19.33 ? 85  SER   A CB  1 
ATOM   572  O  OG  A SER   A 1 85  ? 38.418 -19.345 -11.236 0.50 22.62 ? 85  SER   A OG  1 
ATOM   573  O  OG  B SER   A 1 85  ? 36.624 -19.961 -11.761 0.50 24.54 ? 85  SER   A OG  1 
ATOM   574  N  N   . PRO   A 1 86  ? 34.400 -17.094 -11.822 1.00 15.17 ? 86  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 86  ? 32.920 -17.021 -11.760 1.00 17.77 ? 86  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 86  ? 32.292 -18.305 -12.278 1.00 13.62 ? 86  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 86  ? 32.787 -18.871 -13.196 1.00 14.17 ? 86  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 86  ? 32.611 -15.893 -12.737 1.00 20.56 ? 86  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 86  ? 33.682 -15.995 -13.767 1.00 17.02 ? 86  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 86  ? 34.909 -16.426 -13.028 1.00 14.23 ? 86  PRO   A CD  1 
ATOM   581  N  N   . PHE   A 1 87  ? 31.230 -18.789 -11.649 1.00 17.34 ? 87  PHE   A N   1 
ATOM   582  C  CA  . PHE   A 1 87  ? 30.469 -19.912 -12.146 1.00 15.68 ? 87  PHE   A CA  1 
ATOM   583  C  C   . PHE   A 1 87  ? 29.443 -19.404 -13.116 1.00 18.30 ? 87  PHE   A C   1 
ATOM   584  O  O   . PHE   A 1 87  ? 29.335 -19.951 -14.203 1.00 12.06 ? 87  PHE   A O   1 
ATOM   585  C  CB  . PHE   A 1 87  ? 29.792 -20.655 -10.965 1.00 15.68 ? 87  PHE   A CB  1 
ATOM   586  C  CG  . PHE   A 1 87  ? 28.941 -21.794 -11.355 1.00 14.53 ? 87  PHE   A CG  1 
ATOM   587  C  CD1 . PHE   A 1 87  ? 29.496 -22.968 -11.856 1.00 16.82 ? 87  PHE   A CD1 1 
ATOM   588  C  CD2 . PHE   A 1 87  ? 27.554 -21.707 -11.221 1.00 21.35 ? 87  PHE   A CD2 1 
ATOM   589  C  CE1 . PHE   A 1 87  ? 28.700 -24.009 -12.238 1.00 19.50 ? 87  PHE   A CE1 1 
ATOM   590  C  CE2 . PHE   A 1 87  ? 26.746 -22.767 -11.619 1.00 21.59 ? 87  PHE   A CE2 1 
ATOM   591  C  CZ  . PHE   A 1 87  ? 27.330 -23.924 -12.092 1.00 24.02 ? 87  PHE   A CZ  1 
ATOM   592  N  N   . HIS   A 1 88  ? 28.660 -18.384 -12.702 1.00 17.17 ? 88  HIS   A N   1 
ATOM   593  C  CA  . HIS   A 1 88  ? 27.561 -17.907 -13.541 1.00 21.25 ? 88  HIS   A CA  1 
ATOM   594  C  C   . HIS   A 1 88  ? 28.070 -17.029 -14.655 1.00 15.26 ? 88  HIS   A C   1 
ATOM   595  O  O   . HIS   A 1 88  ? 29.000 -16.281 -14.473 1.00 23.83 ? 88  HIS   A O   1 
ATOM   596  C  CB  . HIS   A 1 88  ? 26.425 -17.214 -12.732 1.00 14.33 ? 88  HIS   A CB  1 
ATOM   597  C  CG  . HIS   A 1 88  ? 25.817 -18.110 -11.686 1.00 17.55 ? 88  HIS   A CG  1 
ATOM   598  N  ND1 . HIS   A 1 88  ? 26.240 -18.118 -10.368 1.00 22.39 ? 88  HIS   A ND1 1 
ATOM   599  C  CD2 . HIS   A 1 88  ? 24.837 -19.041 -11.767 1.00 21.15 ? 88  HIS   A CD2 1 
ATOM   600  C  CE1 . HIS   A 1 88  ? 25.534 -19.002 -9.687  1.00 24.02 ? 88  HIS   A CE1 1 
ATOM   601  N  NE2 . HIS   A 1 88  ? 24.691 -19.588 -10.515 1.00 25.55 ? 88  HIS   A NE2 1 
ATOM   602  N  N   . GLU   A 1 89  ? 27.383 -17.069 -15.785 1.00 17.49 ? 89  GLU   A N   1 
ATOM   603  C  CA  . GLU   A 1 89  ? 27.618 -16.161 -16.823 1.00 18.05 ? 89  GLU   A CA  1 
ATOM   604  C  C   . GLU   A 1 89  ? 27.136 -14.775 -16.378 1.00 17.20 ? 89  GLU   A C   1 
ATOM   605  O  O   . GLU   A 1 89  ? 27.730 -13.752 -16.671 1.00 16.63 ? 89  GLU   A O   1 
ATOM   606  C  CB  . GLU   A 1 89  ? 26.765 -16.580 -18.044 1.00 23.84 ? 89  GLU   A CB  1 
ATOM   607  C  CG  . GLU   A 1 89  ? 27.376 -17.723 -18.834 1.00 23.21 ? 89  GLU   A CG  1 
ATOM   608  C  CD  . GLU   A 1 89  ? 28.732 -17.289 -19.345 1.00 31.20 ? 89  GLU   A CD  1 
ATOM   609  O  OE1 . GLU   A 1 89  ? 28.786 -16.337 -20.175 1.00 27.30 ? 89  GLU   A OE1 1 
ATOM   610  O  OE2 . GLU   A 1 89  ? 29.756 -17.849 -18.872 1.00 36.34 ? 89  GLU   A OE2 1 
ATOM   611  N  N   . HIS   A 1 90  ? 25.968 -14.755 -15.762 1.00 11.05 ? 90  HIS   A N   1 
ATOM   612  C  CA  . HIS   A 1 90  ? 25.364 -13.519 -15.386 1.00 11.24 ? 90  HIS   A CA  1 
ATOM   613  C  C   . HIS   A 1 90  ? 24.271 -13.848 -14.381 1.00 14.83 ? 90  HIS   A C   1 
ATOM   614  O  O   . HIS   A 1 90  ? 23.998 -15.023 -14.198 1.00 19.91 ? 90  HIS   A O   1 
ATOM   615  C  CB  . HIS   A 1 90  ? 24.838 -12.746 -16.613 1.00 17.02 ? 90  HIS   A CB  1 
ATOM   616  C  CG  . HIS   A 1 90  ? 24.116 -13.575 -17.624 1.00 23.32 ? 90  HIS   A CG  1 
ATOM   617  N  ND1 . HIS   A 1 90  ? 22.783 -13.889 -17.514 1.00 28.33 ? 90  HIS   A ND1 1 
ATOM   618  C  CD2 . HIS   A 1 90  ? 24.523 -14.084 -18.802 1.00 32.64 ? 90  HIS   A CD2 1 
ATOM   619  C  CE1 . HIS   A 1 90  ? 22.397 -14.561 -18.574 1.00 28.05 ? 90  HIS   A CE1 1 
ATOM   620  N  NE2 . HIS   A 1 90  ? 23.441 -14.716 -19.363 1.00 36.18 ? 90  HIS   A NE2 1 
ATOM   621  N  N   . ALA   A 1 91  ? 23.811 -12.843 -13.624 1.00 13.84 ? 91  ALA   A N   1 
ATOM   622  C  CA  . ALA   A 1 91  ? 22.602 -12.967 -12.785 1.00 14.34 ? 91  ALA   A CA  1 
ATOM   623  C  C   . ALA   A 1 91  ? 21.442 -12.263 -13.485 1.00 18.56 ? 91  ALA   A C   1 
ATOM   624  O  O   . ALA   A 1 91  ? 21.584 -11.120 -13.839 1.00 21.93 ? 91  ALA   A O   1 
ATOM   625  C  CB  . ALA   A 1 91  ? 22.847 -12.394 -11.386 1.00 17.21 ? 91  ALA   A CB  1 
ATOM   626  N  N   . GLU   A 1 92  ? 20.283 -12.961 -13.571 1.00 25.92 ? 92  GLU   A N   1 
ATOM   627  C  CA  A GLU   A 1 92  ? 19.233 -12.686 -14.588 0.50 23.69 ? 92  GLU   A CA  1 
ATOM   628  C  CA  B GLU   A 1 92  ? 19.224 -12.726 -14.556 0.50 24.86 ? 92  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 92  ? 17.848 -12.726 -13.913 1.00 28.45 ? 92  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 92  ? 17.278 -13.783 -13.693 1.00 35.48 ? 92  GLU   A O   1 
ATOM   631  C  CB  A GLU   A 1 92  ? 19.368 -13.679 -15.791 0.50 26.50 ? 92  GLU   A CB  1 
ATOM   632  C  CB  B GLU   A 1 92  ? 19.234 -13.866 -15.572 0.50 33.82 ? 92  GLU   A CB  1 
ATOM   633  C  CG  A GLU   A 1 92  ? 18.144 -13.953 -16.681 0.50 22.00 ? 92  GLU   A CG  1 
ATOM   634  C  CG  B GLU   A 1 92  ? 19.596 -15.254 -15.009 0.50 35.18 ? 92  GLU   A CG  1 
ATOM   635  C  CD  A GLU   A 1 92  ? 18.391 -14.928 -17.858 0.50 26.85 ? 92  GLU   A CD  1 
ATOM   636  C  CD  B GLU   A 1 92  ? 19.468 -15.433 -13.479 0.50 30.64 ? 92  GLU   A CD  1 
ATOM   637  O  OE1 A GLU   A 1 92  ? 17.636 -15.916 -17.972 0.50 43.60 ? 92  GLU   A OE1 1 
ATOM   638  O  OE1 B GLU   A 1 92  ? 18.387 -15.455 -12.850 0.50 27.32 ? 92  GLU   A OE1 1 
ATOM   639  O  OE2 A GLU   A 1 92  ? 19.292 -14.718 -18.706 0.50 26.30 ? 92  GLU   A OE2 1 
ATOM   640  O  OE2 B GLU   A 1 92  ? 20.493 -15.616 -12.850 0.50 26.31 ? 92  GLU   A OE2 1 
ATOM   641  N  N   . VAL   A 1 93  ? 17.302 -11.544 -13.651 1.00 17.53 ? 93  VAL   A N   1 
ATOM   642  C  CA  . VAL   A 1 93  ? 16.073 -11.377 -12.932 1.00 13.12 ? 93  VAL   A CA  1 
ATOM   643  C  C   . VAL   A 1 93  ? 14.969 -11.061 -13.948 1.00 8.06  ? 93  VAL   A C   1 
ATOM   644  O  O   . VAL   A 1 93  ? 15.060 -10.078 -14.650 1.00 9.97  ? 93  VAL   A O   1 
ATOM   645  C  CB  . VAL   A 1 93  ? 16.275 -10.209 -11.966 1.00 20.13 ? 93  VAL   A CB  1 
ATOM   646  C  CG1 . VAL   A 1 93  ? 15.140 -10.123 -11.001 1.00 22.96 ? 93  VAL   A CG1 1 
ATOM   647  C  CG2 . VAL   A 1 93  ? 17.572 -10.385 -11.216 1.00 20.00 ? 93  VAL   A CG2 1 
ATOM   648  N  N   . VAL   A 1 94  ? 13.936 -11.896 -14.035 1.00 7.32  ? 94  VAL   A N   1 
ATOM   649  C  CA  . VAL   A 1 94  ? 12.863 -11.704 -15.011 1.00 7.31  ? 94  VAL   A CA  1 
ATOM   650  C  C   . VAL   A 1 94  ? 11.533 -11.533 -14.312 1.00 7.03  ? 94  VAL   A C   1 
ATOM   651  O  O   . VAL   A 1 94  ? 11.167 -12.379 -13.505 1.00 8.00  ? 94  VAL   A O   1 
ATOM   652  C  CB  . VAL   A 1 94  ? 12.807 -12.871 -16.008 1.00 8.72  ? 94  VAL   A CB  1 
ATOM   653  C  CG1 . VAL   A 1 94  ? 11.732 -12.652 -17.069 1.00 8.43  ? 94  VAL   A CG1 1 
ATOM   654  C  CG2 . VAL   A 1 94  ? 14.197 -13.085 -16.642 1.00 10.65 ? 94  VAL   A CG2 1 
ATOM   655  N  N   . PHE   A 1 95  ? 10.826 -10.458 -14.631 1.00 6.51  ? 95  PHE   A N   1 
ATOM   656  C  CA  . PHE   A 1 95  ? 9.558  -10.114 -13.924 1.00 6.82  ? 95  PHE   A CA  1 
ATOM   657  C  C   . PHE   A 1 95  ? 8.627  -9.339  -14.864 1.00 7.13  ? 95  PHE   A C   1 
ATOM   658  O  O   . PHE   A 1 95  ? 9.000  -8.666  -15.797 1.00 9.01  ? 95  PHE   A O   1 
ATOM   659  C  CB  . PHE   A 1 95  ? 9.867  -9.322  -12.655 1.00 8.47  ? 95  PHE   A CB  1 
ATOM   660  C  CG  . PHE   A 1 95  ? 10.505 -7.998  -12.893 1.00 7.70  ? 95  PHE   A CG  1 
ATOM   661  C  CD1 . PHE   A 1 95  ? 11.878 -7.923  -13.178 1.00 10.43 ? 95  PHE   A CD1 1 
ATOM   662  C  CD2 . PHE   A 1 95  ? 9.769  -6.827  -12.852 1.00 7.47  ? 95  PHE   A CD2 1 
ATOM   663  C  CE1 . PHE   A 1 95  ? 12.463 -6.725  -13.386 1.00 12.95 ? 95  PHE   A CE1 1 
ATOM   664  C  CE2 . PHE   A 1 95  ? 10.360 -5.614  -13.104 1.00 11.14 ? 95  PHE   A CE2 1 
ATOM   665  C  CZ  . PHE   A 1 95  ? 11.725 -5.566  -13.327 1.00 11.97 ? 95  PHE   A CZ  1 
ATOM   666  N  N   . THR   A 1 96  ? 7.343  -9.468  -14.593 1.00 8.23  ? 96  THR   A N   1 
ATOM   667  C  CA  . THR   A 1 96  ? 6.353  -8.609  -15.217 1.00 7.86  ? 96  THR   A CA  1 
ATOM   668  C  C   . THR   A 1 96  ? 6.243  -7.293  -14.454 1.00 7.56  ? 96  THR   A C   1 
ATOM   669  O  O   . THR   A 1 96  ? 6.053  -7.281  -13.232 1.00 10.93 ? 96  THR   A O   1 
ATOM   670  C  CB  . THR   A 1 96  ? 4.984  -9.381  -15.154 1.00 8.02  ? 96  THR   A CB  1 
ATOM   671  O  OG1 . THR   A 1 96  ? 5.039  -10.580 -15.975 1.00 11.58 ? 96  THR   A OG1 1 
ATOM   672  C  CG2 . THR   A 1 96  ? 3.777  -8.508  -15.635 1.00 10.74 ? 96  THR   A CG2 1 
ATOM   673  N  N   . ALA   A 1 97  ? 6.210  -6.206  -15.169 1.00 8.49  ? 97  ALA   A N   1 
ATOM   674  C  CA  . ALA   A 1 97  ? 6.193  -4.893  -14.578 1.00 7.79  ? 97  ALA   A CA  1 
ATOM   675  C  C   . ALA   A 1 97  ? 4.971  -4.115  -14.981 1.00 9.13  ? 97  ALA   A C   1 
ATOM   676  O  O   . ALA   A 1 97  ? 4.553  -4.209  -16.111 1.00 11.38 ? 97  ALA   A O   1 
ATOM   677  C  CB  . ALA   A 1 97  ? 7.409  -4.139  -14.989 1.00 7.42  ? 97  ALA   A CB  1 
ATOM   678  N  N   . ASN   A 1 98  ? 4.432  -3.356  -14.019 1.00 9.72  ? 98  ASN   A N   1 
ATOM   679  C  CA  . ASN   A 1 98  ? 3.427  -2.292  -14.289 1.00 9.43  ? 98  ASN   A CA  1 
ATOM   680  C  C   . ASN   A 1 98  ? 2.083  -2.813  -14.704 1.00 9.26  ? 98  ASN   A C   1 
ATOM   681  O  O   . ASN   A 1 98  ? 1.281  -2.054  -15.210 1.00 11.93 ? 98  ASN   A O   1 
ATOM   682  C  CB  . ASN   A 1 98  ? 3.926  -1.265  -15.295 1.00 8.72  ? 98  ASN   A CB  1 
ATOM   683  C  CG  . ASN   A 1 98  ? 5.287  -0.676  -14.935 1.00 9.71  ? 98  ASN   A CG  1 
ATOM   684  O  OD1 . ASN   A 1 98  ? 6.264  -0.648  -15.788 1.00 14.52 ? 98  ASN   A OD1 1 
ATOM   685  N  ND2 . ASN   A 1 98  ? 5.397  -0.209  -13.713 1.00 9.35  ? 98  ASN   A ND2 1 
ATOM   686  N  N   . ASP   A 1 99  ? 1.816  -4.065  -14.473 1.00 10.04 ? 99  ASP   A N   1 
ATOM   687  C  CA  . ASP   A 1 99  ? 0.639  -4.716  -15.112 1.00 10.06 ? 99  ASP   A CA  1 
ATOM   688  C  C   . ASP   A 1 99  ? -0.643 -4.166  -14.521 1.00 11.20 ? 99  ASP   A C   1 
ATOM   689  O  O   . ASP   A 1 99  ? -1.672 -4.180  -15.234 1.00 12.79 ? 99  ASP   A O   1 
ATOM   690  C  CB  . ASP   A 1 99  ? 0.653  -6.225  -14.908 1.00 12.79 ? 99  ASP   A CB  1 
ATOM   691  C  CG  . ASP   A 1 99  ? -0.168 -7.000  -15.934 1.00 11.58 ? 99  ASP   A CG  1 
ATOM   692  O  OD1 . ASP   A 1 99  ? -0.947 -6.435  -16.745 1.00 11.75 ? 99  ASP   A OD1 1 
ATOM   693  O  OD2 . ASP   A 1 99  ? 0.016  -8.248  -15.964 1.00 12.97 ? 99  ASP   A OD2 1 
ATOM   694  N  N   . SER   A 1 100 ? -0.631 -3.772  -13.243 1.00 12.38 ? 100 SER   A N   1 
ATOM   695  C  CA  . SER   A 1 100 ? -1.857 -3.203  -12.559 1.00 13.45 ? 100 SER   A CA  1 
ATOM   696  C  C   . SER   A 1 100 ? -1.719 -1.692  -12.377 1.00 12.16 ? 100 SER   A C   1 
ATOM   697  O  O   . SER   A 1 100 ? -2.524 -1.031  -11.653 1.00 18.23 ? 100 SER   A O   1 
ATOM   698  C  CB  . SER   A 1 100 ? -2.068 -3.853  -11.171 1.00 16.45 ? 100 SER   A CB  1 
ATOM   699  O  OG  . SER   A 1 100 ? -2.619 -5.153  -11.327 1.00 22.67 ? 100 SER   A OG  1 
ATOM   700  N  N   . GLY   A 1 101 ? -0.730 -1.119  -13.072 1.00 11.69 ? 101 GLY   A N   1 
ATOM   701  C  CA  . GLY   A 1 101 ? -0.436 0.309   -12.960 1.00 12.10 ? 101 GLY   A CA  1 
ATOM   702  C  C   . GLY   A 1 101 ? 1.053  0.557   -12.743 1.00 12.04 ? 101 GLY   A C   1 
ATOM   703  O  O   . GLY   A 1 101 ? 1.726  -0.344  -12.330 1.00 9.19  ? 101 GLY   A O   1 
ATOM   704  N  N   . PRO   A 1 102 ? 1.522  1.788   -12.991 1.00 10.21 ? 102 PRO   A N   1 
ATOM   705  C  CA  . PRO   A 1 102 ? 2.932  2.108   -12.810 1.00 9.16  ? 102 PRO   A CA  1 
ATOM   706  C  C   . PRO   A 1 102 ? 3.403  1.819   -11.352 1.00 10.05 ? 102 PRO   A C   1 
ATOM   707  O  O   . PRO   A 1 102 ? 2.749  2.204   -10.414 1.00 11.50 ? 102 PRO   A O   1 
ATOM   708  C  CB  . PRO   A 1 102 ? 3.005  3.582   -13.148 1.00 11.57 ? 102 PRO   A CB  1 
ATOM   709  C  CG  . PRO   A 1 102 ? 1.797  3.902   -13.972 1.00 14.38 ? 102 PRO   A CG  1 
ATOM   710  C  CD  . PRO   A 1 102 ? 0.755  2.968   -13.423 1.00 12.63 ? 102 PRO   A CD  1 
ATOM   711  N  N   . ARG   A 1 103 ? 4.589  1.209   -11.206 1.00 9.72  ? 103 ARG   A N   1 
ATOM   712  C  CA  . ARG   A 1 103 ? 5.207  1.027   -9.922  1.00 11.43 ? 103 ARG   A CA  1 
ATOM   713  C  C   . ARG   A 1 103 ? 6.677  1.365   -10.136 1.00 10.42 ? 103 ARG   A C   1 
ATOM   714  O  O   . ARG   A 1 103 ? 7.220  1.356   -11.242 1.00 9.93  ? 103 ARG   A O   1 
ATOM   715  C  CB  . ARG   A 1 103 ? 5.085  -0.392  -9.391  1.00 10.79 ? 103 ARG   A CB  1 
ATOM   716  C  CG  . ARG   A 1 103 ? 3.685  -0.920  -9.355  1.00 11.77 ? 103 ARG   A CG  1 
ATOM   717  C  CD  . ARG   A 1 103 ? 2.966  -0.288  -8.207  1.00 13.71 ? 103 ARG   A CD  1 
ATOM   718  N  NE  . ARG   A 1 103 ? 1.676  -0.922  -8.016  1.00 16.09 ? 103 ARG   A NE  1 
ATOM   719  C  CZ  . ARG   A 1 103 ? 0.527  -0.468  -8.529  1.00 22.66 ? 103 ARG   A CZ  1 
ATOM   720  N  NH1 . ARG   A 1 103 ? 0.517  0.585   -9.342  1.00 22.00 ? 103 ARG   A NH1 1 
ATOM   721  N  NH2 . ARG   A 1 103 ? -0.610 -1.107  -8.262  1.00 26.89 ? 103 ARG   A NH2 1 
ATOM   722  N  N   . ARG   A 1 104 ? 7.298  1.576   -9.019  1.00 9.29  ? 104 ARG   A N   1 
ATOM   723  C  CA  . ARG   A 1 104 ? 8.743  1.655   -8.910  1.00 9.58  ? 104 ARG   A CA  1 
ATOM   724  C  C   . ARG   A 1 104 ? 9.344  0.361   -8.348  1.00 8.53  ? 104 ARG   A C   1 
ATOM   725  O  O   . ARG   A 1 104 ? 8.898  -0.148  -7.323  1.00 11.31 ? 104 ARG   A O   1 
ATOM   726  C  CB  . ARG   A 1 104 ? 9.173  2.893   -8.007  1.00 17.38 ? 104 ARG   A CB  1 
ATOM   727  C  CG  . ARG   A 1 104 ? 8.715  4.319   -8.462  1.00 19.94 ? 104 ARG   A CG  1 
ATOM   728  C  CD  . ARG   A 1 104 ? 9.418  5.474   -7.717  1.00 25.62 ? 104 ARG   A CD  1 
ATOM   729  N  N   . TYR   A 1 105 ? 10.466 -0.041  -8.952  1.00 7.51  ? 105 TYR   A N   1 
ATOM   730  C  CA  . TYR   A 1 105 ? 11.120 -1.298  -8.715  1.00 8.14  ? 105 TYR   A CA  1 
ATOM   731  C  C   . TYR   A 1 105 ? 12.589 -1.115  -8.384  1.00 7.25  ? 105 TYR   A C   1 
ATOM   732  O  O   . TYR   A 1 105 ? 13.292 -0.434  -9.132  1.00 9.96  ? 105 TYR   A O   1 
ATOM   733  C  CB  . TYR   A 1 105 ? 11.037 -2.213  -9.956  1.00 6.62  ? 105 TYR   A CB  1 
ATOM   734  C  CG  . TYR   A 1 105 ? 9.620  -2.517  -10.353 1.00 7.39  ? 105 TYR   A CG  1 
ATOM   735  C  CD1 . TYR   A 1 105 ? 8.973  -1.707  -11.251 1.00 8.25  ? 105 TYR   A CD1 1 
ATOM   736  C  CD2 . TYR   A 1 105 ? 8.994  -3.662  -9.879  1.00 9.30  ? 105 TYR   A CD2 1 
ATOM   737  C  CE1 . TYR   A 1 105 ? 7.685  -2.023  -11.616 1.00 10.18 ? 105 TYR   A CE1 1 
ATOM   738  C  CE2 . TYR   A 1 105 ? 7.698  -3.983  -10.216 1.00 7.90  ? 105 TYR   A CE2 1 
ATOM   739  C  CZ  . TYR   A 1 105 ? 7.071  -3.138  -11.113 1.00 8.16  ? 105 TYR   A CZ  1 
ATOM   740  O  OH  . TYR   A 1 105 ? 5.726  -3.348  -11.473 1.00 9.29  ? 105 TYR   A OH  1 
ATOM   741  N  N   . THR   A 1 106 ? 12.976 -1.685  -7.265  1.00 8.64  ? 106 THR   A N   1 
ATOM   742  C  CA  . THR   A 1 106 ? 14.405 -1.837  -6.938  1.00 8.67  ? 106 THR   A CA  1 
ATOM   743  C  C   . THR   A 1 106 ? 14.745 -3.278  -6.998  1.00 7.70  ? 106 THR   A C   1 
ATOM   744  O  O   . THR   A 1 106 ? 14.161 -4.118  -6.332  1.00 7.52  ? 106 THR   A O   1 
ATOM   745  C  CB  . THR   A 1 106 ? 14.705 -1.264  -5.583  1.00 9.12  ? 106 THR   A CB  1 
ATOM   746  O  OG1 . THR   A 1 106 ? 14.438 0.131   -5.566  1.00 14.42 ? 106 THR   A OG1 1 
ATOM   747  C  CG2 . THR   A 1 106 ? 16.124 -1.442  -5.267  1.00 8.64  ? 106 THR   A CG2 1 
ATOM   748  N  N   . ILE   A 1 107 ? 15.757 -3.571  -7.837  1.00 7.14  ? 107 ILE   A N   1 
ATOM   749  C  CA  . ILE   A 1 107 ? 16.272 -4.934  -7.908  1.00 7.27  ? 107 ILE   A CA  1 
ATOM   750  C  C   . ILE   A 1 107 ? 17.626 -4.981  -7.156  1.00 6.90  ? 107 ILE   A C   1 
ATOM   751  O  O   . ILE   A 1 107 ? 18.533 -4.257  -7.541  1.00 8.07  ? 107 ILE   A O   1 
ATOM   752  C  CB  . ILE   A 1 107 ? 16.529 -5.373  -9.344  1.00 7.59  ? 107 ILE   A CB  1 
ATOM   753  C  CG1 . ILE   A 1 107 ? 15.237 -5.332  -10.174 1.00 9.59  ? 107 ILE   A CG1 1 
ATOM   754  C  CG2 . ILE   A 1 107 ? 17.048 -6.791  -9.421  1.00 9.62  ? 107 ILE   A CG2 1 
ATOM   755  C  CD1 . ILE   A 1 107 ? 14.114 -6.175  -9.671  1.00 12.11 ? 107 ILE   A CD1 1 
ATOM   756  N  N   . ALA   A 1 108 ? 17.656 -5.731  -6.068  1.00 7.11  ? 108 ALA   A N   1 
ATOM   757  C  CA  . ALA   A 1 108 ? 18.857 -5.903  -5.201  1.00 5.73  ? 108 ALA   A CA  1 
ATOM   758  C  C   . ALA   A 1 108 ? 19.461 -7.273  -5.449  1.00 5.74  ? 108 ALA   A C   1 
ATOM   759  O  O   . ALA   A 1 108 ? 18.745 -8.262  -5.581  1.00 5.37  ? 108 ALA   A O   1 
ATOM   760  C  CB  . ALA   A 1 108 ? 18.487 -5.703  -3.705  1.00 5.59  ? 108 ALA   A CB  1 
ATOM   761  N  N   . ALA   A 1 109 ? 20.821 -7.345  -5.586  1.00 6.68  ? 109 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 109 ? 21.513 -8.562  -5.865  1.00 5.16  ? 109 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 109 ? 22.780 -8.625  -5.017  1.00 6.45  ? 109 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 109 ? 23.451 -7.595  -4.832  1.00 6.40  ? 109 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 109 ? 21.875 -8.693  -7.366  1.00 6.45  ? 109 ALA   A CB  1 
ATOM   766  N  N   . LEU   A 1 110 ? 22.984 -9.823  -4.473  1.00 5.64  ? 110 LEU   A N   1 
ATOM   767  C  CA  . LEU   A 1 110 ? 24.152 -10.117 -3.646  1.00 5.10  ? 110 LEU   A CA  1 
ATOM   768  C  C   . LEU   A 1 110 ? 24.955 -11.166 -4.316  1.00 6.04  ? 110 LEU   A C   1 
ATOM   769  O  O   . LEU   A 1 110 ? 24.450 -12.288 -4.559  1.00 5.57  ? 110 LEU   A O   1 
ATOM   770  C  CB  . LEU   A 1 110 ? 23.689 -10.551 -2.263  1.00 5.17  ? 110 LEU   A CB  1 
ATOM   771  C  CG  . LEU   A 1 110 ? 24.825 -11.032 -1.353  1.00 6.67  ? 110 LEU   A CG  1 
ATOM   772  C  CD1 . LEU   A 1 110 ? 25.793 -9.917  -1.097  1.00 9.12  ? 110 LEU   A CD1 1 
ATOM   773  C  CD2 . LEU   A 1 110 ? 24.232 -11.543 -0.060  1.00 5.08  ? 110 LEU   A CD2 1 
ATOM   774  N  N   . LEU   A 1 111 ? 26.212 -10.862 -4.681  1.00 5.85  ? 111 LEU   A N   1 
ATOM   775  C  CA  . LEU   A 1 111 ? 26.971 -11.760 -5.523  1.00 5.39  ? 111 LEU   A CA  1 
ATOM   776  C  C   . LEU   A 1 111 ? 28.087 -12.553 -4.846  1.00 5.78  ? 111 LEU   A C   1 
ATOM   777  O  O   . LEU   A 1 111 ? 28.856 -11.975 -4.086  1.00 7.30  ? 111 LEU   A O   1 
ATOM   778  C  CB  . LEU   A 1 111 ? 27.700 -10.933 -6.624  1.00 6.31  ? 111 LEU   A CB  1 
ATOM   779  C  CG  . LEU   A 1 111 ? 26.813 -9.977  -7.448  1.00 6.92  ? 111 LEU   A CG  1 
ATOM   780  C  CD1 . LEU   A 1 111 ? 27.671 -9.361  -8.563  1.00 8.64  ? 111 LEU   A CD1 1 
ATOM   781  C  CD2 . LEU   A 1 111 ? 25.581 -10.711 -8.067  1.00 6.56  ? 111 LEU   A CD2 1 
ATOM   782  N  N   . SER   A 1 112 ? 28.152 -13.818 -5.159  1.00 5.29  ? 112 SER   A N   1 
ATOM   783  C  CA  . SER   A 1 112 ? 29.310 -14.667 -4.855  1.00 6.40  ? 112 SER   A CA  1 
ATOM   784  C  C   . SER   A 1 112 ? 29.702 -15.439 -6.124  1.00 8.38  ? 112 SER   A C   1 
ATOM   785  O  O   . SER   A 1 112 ? 28.928 -15.495 -7.114  1.00 8.21  ? 112 SER   A O   1 
ATOM   786  C  CB  . SER   A 1 112 ? 28.963 -15.686 -3.784  1.00 8.23  ? 112 SER   A CB  1 
ATOM   787  O  OG  . SER   A 1 112 ? 28.664 -15.064 -2.590  1.00 10.91 ? 112 SER   A OG  1 
ATOM   788  N  N   . PRO   A 1 113 ? 30.935 -16.031 -6.149  1.00 7.85  ? 113 PRO   A N   1 
ATOM   789  C  CA  . PRO   A 1 113 ? 31.368 -16.625 -7.416  1.00 9.99  ? 113 PRO   A CA  1 
ATOM   790  C  C   . PRO   A 1 113 ? 30.505 -17.813 -7.892  1.00 9.92  ? 113 PRO   A C   1 
ATOM   791  O  O   . PRO   A 1 113 ? 30.309 -17.975 -9.090  1.00 10.92 ? 113 PRO   A O   1 
ATOM   792  C  CB  . PRO   A 1 113 ? 32.843 -16.962 -7.170  1.00 11.56 ? 113 PRO   A CB  1 
ATOM   793  C  CG  . PRO   A 1 113 ? 33.235 -15.926 -6.175  1.00 9.56  ? 113 PRO   A CG  1 
ATOM   794  C  CD  . PRO   A 1 113 ? 32.041 -15.778 -5.248  1.00 9.53  ? 113 PRO   A CD  1 
ATOM   795  N  N   . TYR   A 1 114 ? 29.924 -18.565 -6.946  1.00 10.03 ? 114 TYR   A N   1 
ATOM   796  C  CA  . TYR   A 1 114 ? 29.109 -19.748 -7.279  1.00 10.21 ? 114 TYR   A CA  1 
ATOM   797  C  C   . TYR   A 1 114 ? 27.635 -19.601 -6.837  1.00 9.28  ? 114 TYR   A C   1 
ATOM   798  O  O   . TYR   A 1 114 ? 26.916 -20.556 -6.894  1.00 9.95  ? 114 TYR   A O   1 
ATOM   799  C  CB  . TYR   A 1 114 ? 29.692 -21.037 -6.699  1.00 9.47  ? 114 TYR   A CB  1 
ATOM   800  C  CG  . TYR   A 1 114 ? 30.806 -21.606 -7.485  1.00 10.49 ? 114 TYR   A CG  1 
ATOM   801  C  CD1 . TYR   A 1 114 ? 32.051 -21.084 -7.349  1.00 15.07 ? 114 TYR   A CD1 1 
ATOM   802  C  CD2 . TYR   A 1 114 ? 30.643 -22.730 -8.269  1.00 11.56 ? 114 TYR   A CD2 1 
ATOM   803  C  CE1 . TYR   A 1 114 ? 33.080 -21.608 -8.034  1.00 16.50 ? 114 TYR   A CE1 1 
ATOM   804  C  CE2 . TYR   A 1 114 ? 31.708 -23.282 -8.965  1.00 11.61 ? 114 TYR   A CE2 1 
ATOM   805  C  CZ  . TYR   A 1 114 ? 32.908 -22.673 -8.839  1.00 15.74 ? 114 TYR   A CZ  1 
ATOM   806  O  OH  . TYR   A 1 114 ? 34.023 -23.118 -9.500  1.00 26.00 ? 114 TYR   A OH  1 
ATOM   807  N  N   . SER   A 1 115 ? 27.231 -18.394 -6.463  1.00 6.75  ? 115 SER   A N   1 
ATOM   808  C  CA  . SER   A 1 115 ? 25.878 -18.152 -5.940  1.00 8.15  ? 115 SER   A CA  1 
ATOM   809  C  C   . SER   A 1 115 ? 25.491 -16.717 -6.124  1.00 7.87  ? 115 SER   A C   1 
ATOM   810  O  O   . SER   A 1 115 ? 26.317 -15.821 -6.044  1.00 9.40  ? 115 SER   A O   1 
ATOM   811  C  CB  . SER   A 1 115 ? 25.879 -18.462 -4.405  1.00 9.96  ? 115 SER   A CB  1 
ATOM   812  O  OG  . SER   A 1 115 ? 24.581 -18.356 -3.896  1.00 13.20 ? 115 SER   A OG  1 
ATOM   813  N  N   . TYR   A 1 116 ? 24.186 -16.465 -6.266  1.00 6.77  ? 116 TYR   A N   1 
ATOM   814  C  CA  . TYR   A 1 116 ? 23.689 -15.108 -6.073  1.00 6.71  ? 116 TYR   A CA  1 
ATOM   815  C  C   . TYR   A 1 116 ? 22.305 -15.181 -5.443  1.00 6.44  ? 116 TYR   A C   1 
ATOM   816  O  O   . TYR   A 1 116 ? 21.617 -16.180 -5.537  1.00 6.20  ? 116 TYR   A O   1 
ATOM   817  C  CB  . TYR   A 1 116 ? 23.716 -14.254 -7.351  1.00 9.31  ? 116 TYR   A CB  1 
ATOM   818  C  CG  . TYR   A 1 116 ? 22.858 -14.728 -8.457  1.00 9.50  ? 116 TYR   A CG  1 
ATOM   819  C  CD1 . TYR   A 1 116 ? 23.313 -15.707 -9.377  1.00 14.13 ? 116 TYR   A CD1 1 
ATOM   820  C  CD2 . TYR   A 1 116 ? 21.598 -14.273 -8.555  1.00 15.28 ? 116 TYR   A CD2 1 
ATOM   821  C  CE1 . TYR   A 1 116 ? 22.499 -16.124 -10.408 1.00 13.46 ? 116 TYR   A CE1 1 
ATOM   822  C  CE2 . TYR   A 1 116 ? 20.731 -14.699 -9.586  1.00 17.28 ? 116 TYR   A CE2 1 
ATOM   823  C  CZ  . TYR   A 1 116 ? 21.148 -15.660 -10.446 1.00 14.49 ? 116 TYR   A CZ  1 
ATOM   824  O  OH  . TYR   A 1 116 ? 20.247 -16.031 -11.424 1.00 29.81 ? 116 TYR   A OH  1 
ATOM   825  N  N   . SER   A 1 117 ? 21.968 -14.080 -4.804  1.00 6.08  ? 117 SER   A N   1 
ATOM   826  C  CA  A SER   A 1 117 ? 20.603 -13.899 -4.301  0.50 6.27  ? 117 SER   A CA  1 
ATOM   827  C  CA  B SER   A 1 117 ? 20.640 -13.837 -4.181  0.50 5.43  ? 117 SER   A CA  1 
ATOM   828  C  C   . SER   A 1 117 ? 20.068 -12.559 -4.773  1.00 7.14  ? 117 SER   A C   1 
ATOM   829  O  O   . SER   A 1 117 ? 20.775 -11.599 -4.956  1.00 7.48  ? 117 SER   A O   1 
ATOM   830  C  CB  A SER   A 1 117 ? 20.613 -14.038 -2.794  0.50 7.92  ? 117 SER   A CB  1 
ATOM   831  C  CB  B SER   A 1 117 ? 20.823 -13.691 -2.663  0.50 5.02  ? 117 SER   A CB  1 
ATOM   832  O  OG  A SER   A 1 117 ? 21.276 -12.956 -2.227  0.50 8.87  ? 117 SER   A OG  1 
ATOM   833  O  OG  B SER   A 1 117 ? 19.610 -13.283 -2.025  0.50 5.53  ? 117 SER   A OG  1 
ATOM   834  N  N   . THR   A 1 118 ? 18.747 -12.498 -5.058  1.00 7.33  ? 118 THR   A N   1 
ATOM   835  C  CA  . THR   A 1 118 ? 18.206 -11.293 -5.496  1.00 6.68  ? 118 THR   A CA  1 
ATOM   836  C  C   . THR   A 1 118 ? 16.814 -11.100 -4.885  1.00 5.60  ? 118 THR   A C   1 
ATOM   837  O  O   . THR   A 1 118 ? 16.111 -12.068 -4.572  1.00 7.20  ? 118 THR   A O   1 
ATOM   838  C  CB  . THR   A 1 118 ? 18.097 -11.257 -7.031  1.00 8.76  ? 118 THR   A CB  1 
ATOM   839  O  OG1 . THR   A 1 118 ? 17.575 -10.006 -7.449  1.00 11.19 ? 118 THR   A OG1 1 
ATOM   840  C  CG2 . THR   A 1 118 ? 17.198 -12.391 -7.616  1.00 12.16 ? 118 THR   A CG2 1 
ATOM   841  N  N   . THR   A 1 119 ? 16.474 -9.863  -4.646  1.00 5.80  ? 119 THR   A N   1 
ATOM   842  C  CA  . THR   A 1 119 ? 15.118 -9.539  -4.168  1.00 5.92  ? 119 THR   A CA  1 
ATOM   843  C  C   . THR   A 1 119 ? 14.626 -8.324  -4.845  1.00 6.43  ? 119 THR   A C   1 
ATOM   844  O  O   . THR   A 1 119 ? 15.327 -7.574  -5.491  1.00 8.38  ? 119 THR   A O   1 
ATOM   845  C  CB  . THR   A 1 119 ? 15.083 -9.322  -2.656  1.00 6.12  ? 119 THR   A CB  1 
ATOM   846  O  OG1 . THR   A 1 119 ? 13.717 -9.433  -2.194  1.00 7.32  ? 119 THR   A OG1 1 
ATOM   847  C  CG2 . THR   A 1 119 ? 15.687 -8.020  -2.206  1.00 8.30  ? 119 THR   A CG2 1 
ATOM   848  N  N   . ALA   A 1 120 ? 13.323 -8.138  -4.772  1.00 5.71  ? 120 ALA   A N   1 
ATOM   849  C  CA  . ALA   A 1 120 ? 12.714 -6.900  -5.302  1.00 6.67  ? 120 ALA   A CA  1 
ATOM   850  C  C   . ALA   A 1 120 ? 11.985 -6.085  -4.216  1.00 6.28  ? 120 ALA   A C   1 
ATOM   851  O  O   . ALA   A 1 120 ? 11.322 -6.649  -3.374  1.00 6.14  ? 120 ALA   A O   1 
ATOM   852  C  CB  . ALA   A 1 120 ? 11.685 -7.268  -6.361  1.00 7.45  ? 120 ALA   A CB  1 
ATOM   853  N  N   . VAL   A 1 121 ? 12.096 -4.777  -4.326  1.00 7.26  ? 121 VAL   A N   1 
ATOM   854  C  CA  . VAL   A 1 121 ? 11.288 -3.846  -3.574  1.00 9.01  ? 121 VAL   A CA  1 
ATOM   855  C  C   . VAL   A 1 121 ? 10.384 -3.159  -4.565  1.00 8.75  ? 121 VAL   A C   1 
ATOM   856  O  O   . VAL   A 1 121 ? 10.861 -2.537  -5.557  1.00 9.70  ? 121 VAL   A O   1 
ATOM   857  C  CB  . VAL   A 1 121 ? 12.167 -2.819  -2.804  1.00 11.51 ? 121 VAL   A CB  1 
ATOM   858  C  CG1 . VAL   A 1 121 ? 11.287 -1.880  -1.969  1.00 15.59 ? 121 VAL   A CG1 1 
ATOM   859  C  CG2 . VAL   A 1 121 ? 13.170 -3.550  -1.909  1.00 17.09 ? 121 VAL   A CG2 1 
ATOM   860  N  N   . VAL   A 1 122 ? 9.068  -3.176  -4.295  1.00 9.02  ? 122 VAL   A N   1 
ATOM   861  C  CA  . VAL   A 1 122 ? 8.109  -2.623  -5.244  1.00 10.40 ? 122 VAL   A CA  1 
ATOM   862  C  C   . VAL   A 1 122 ? 7.328  -1.611  -4.471  1.00 9.48  ? 122 VAL   A C   1 
ATOM   863  O  O   . VAL   A 1 122 ? 6.775  -1.968  -3.464  1.00 13.28 ? 122 VAL   A O   1 
ATOM   864  C  CB  . VAL   A 1 122 ? 7.128  -3.669  -5.797  1.00 13.03 ? 122 VAL   A CB  1 
ATOM   865  C  CG1 . VAL   A 1 122 ? 6.079  -3.067  -6.757  1.00 12.97 ? 122 VAL   A CG1 1 
ATOM   866  C  CG2 . VAL   A 1 122 ? 7.863  -4.800  -6.460  1.00 14.31 ? 122 VAL   A CG2 1 
ATOM   867  N  N   . THR   A 1 123 ? 7.270  -0.378  -4.995  1.00 10.84 ? 123 THR   A N   1 
ATOM   868  C  CA  . THR   A 1 123 ? 6.515  0.737   -4.389  1.00 15.25 ? 123 THR   A CA  1 
ATOM   869  C  C   . THR   A 1 123 ? 5.535  1.400   -5.369  1.00 15.27 ? 123 THR   A C   1 
ATOM   870  O  O   . THR   A 1 123 ? 5.747  1.411   -6.602  1.00 16.29 ? 123 THR   A O   1 
ATOM   871  C  CB  . THR   A 1 123 ? 7.422  1.806   -3.801  1.00 15.93 ? 123 THR   A CB  1 
ATOM   872  O  OG1 . THR   A 1 123 ? 8.158  2.442   -4.850  1.00 25.93 ? 123 THR   A OG1 1 
ATOM   873  C  CG2 . THR   A 1 123 ? 8.434  1.172   -2.836  1.00 20.91 ? 123 THR   A CG2 1 
ATOM   874  N  N   . ASN   A 1 124 ? 4.404  1.857   -4.839  1.00 19.81 ? 124 ASN   A N   1 
ATOM   875  C  CA  . ASN   A 1 124 ? 3.399  2.539   -5.669  1.00 24.87 ? 124 ASN   A CA  1 
ATOM   876  C  C   . ASN   A 1 124 ? 3.635  4.021   -5.504  1.00 28.38 ? 124 ASN   A C   1 
ATOM   877  O  O   . ASN   A 1 124 ? 3.323  4.560   -4.436  1.00 38.02 ? 124 ASN   A O   1 
ATOM   878  C  CB  . ASN   A 1 124 ? 1.947  2.165   -5.287  1.00 28.32 ? 124 ASN   A CB  1 
ATOM   879  C  CG  . ASN   A 1 124 ? 0.913  2.629   -6.321  1.00 34.99 ? 124 ASN   A CG  1 
ATOM   880  O  OD1 . ASN   A 1 124 ? 1.006  3.701   -6.946  1.00 34.59 ? 124 ASN   A OD1 1 
ATOM   881  N  N   . PRO   A 1 125 ? 4.189  4.670   -6.553  1.00 35.69 ? 125 PRO   A N   1 
ATOM   882  C  CA  . PRO   A 1 125 ? 4.843  5.994   -6.466  1.00 39.68 ? 125 PRO   A CA  1 
ATOM   883  C  C   . PRO   A 1 125 ? 4.102  7.015   -5.621  1.00 35.53 ? 125 PRO   A C   1 
ATOM   884  O  O   . PRO   A 1 125 ? 2.959  7.317   -5.911  1.00 37.02 ? 125 PRO   A O   1 
ATOM   885  C  CB  . PRO   A 1 125 ? 4.923  6.472   -7.929  1.00 43.74 ? 125 PRO   A CB  1 
ATOM   886  C  CG  . PRO   A 1 125 ? 4.693  5.271   -8.777  1.00 42.27 ? 125 PRO   A CG  1 
ATOM   887  C  CD  . PRO   A 1 125 ? 4.137  4.153   -7.936  1.00 35.58 ? 125 PRO   A CD  1 
ATOM   888  N  N   . CYS   B 1 10  ? 22.200 -38.173 -12.106 1.00 53.42 ? 10  CYS   B N   1 
ATOM   889  C  CA  . CYS   B 1 10  ? 23.636 -38.405 -12.459 1.00 41.16 ? 10  CYS   B CA  1 
ATOM   890  C  C   . CYS   B 1 10  ? 24.429 -37.105 -12.380 1.00 28.33 ? 10  CYS   B C   1 
ATOM   891  O  O   . CYS   B 1 10  ? 24.633 -36.547 -11.276 1.00 35.76 ? 10  CYS   B O   1 
ATOM   892  N  N   . PRO   B 1 11  ? 24.851 -36.583 -13.550 1.00 29.98 ? 11  PRO   B N   1 
ATOM   893  C  CA  . PRO   B 1 11  ? 25.729 -35.403 -13.565 1.00 24.16 ? 11  PRO   B CA  1 
ATOM   894  C  C   . PRO   B 1 11  ? 25.106 -34.079 -13.193 1.00 24.28 ? 11  PRO   B C   1 
ATOM   895  O  O   . PRO   B 1 11  ? 25.824 -33.182 -12.891 1.00 23.32 ? 11  PRO   B O   1 
ATOM   896  C  CB  . PRO   B 1 11  ? 26.191 -35.324 -15.020 1.00 27.27 ? 11  PRO   B CB  1 
ATOM   897  C  CG  . PRO   B 1 11  ? 25.095 -35.963 -15.811 1.00 28.17 ? 11  PRO   B CG  1 
ATOM   898  C  CD  . PRO   B 1 11  ? 24.493 -37.023 -14.918 1.00 26.41 ? 11  PRO   B CD  1 
ATOM   899  N  N   . LEU   B 1 12  ? 23.785 -33.978 -13.253 1.00 25.50 ? 12  LEU   B N   1 
ATOM   900  C  CA  . LEU   B 1 12  ? 23.111 -32.724 -12.997 1.00 18.25 ? 12  LEU   B CA  1 
ATOM   901  C  C   . LEU   B 1 12  ? 21.877 -32.951 -12.175 1.00 17.40 ? 12  LEU   B C   1 
ATOM   902  O  O   . LEU   B 1 12  ? 20.986 -33.728 -12.551 1.00 25.39 ? 12  LEU   B O   1 
ATOM   903  C  CB  . LEU   B 1 12  ? 22.760 -32.028 -14.308 1.00 21.27 ? 12  LEU   B CB  1 
ATOM   904  C  CG  . LEU   B 1 12  ? 22.161 -30.642 -14.268 1.00 28.28 ? 12  LEU   B CG  1 
ATOM   905  C  CD1 . LEU   B 1 12  ? 23.137 -29.640 -13.654 1.00 22.38 ? 12  LEU   B CD1 1 
ATOM   906  C  CD2 . LEU   B 1 12  ? 21.723 -30.250 -15.675 1.00 21.22 ? 12  LEU   B CD2 1 
ATOM   907  N  N   . MET   B 1 13  ? 21.817 -32.215 -11.060 1.00 19.25 ? 13  MET   B N   1 
ATOM   908  C  CA  . MET   B 1 13  ? 20.682 -32.352 -10.179 1.00 19.08 ? 13  MET   B CA  1 
ATOM   909  C  C   . MET   B 1 13  ? 20.201 -30.988 -9.786  1.00 16.35 ? 13  MET   B C   1 
ATOM   910  O  O   . MET   B 1 13  ? 20.985 -30.080 -9.602  1.00 16.88 ? 13  MET   B O   1 
ATOM   911  C  CB  . MET   B 1 13  ? 21.028 -33.150 -8.909  1.00 26.92 ? 13  MET   B CB  1 
ATOM   912  C  CG  . MET   B 1 13  ? 19.801 -33.573 -8.098  1.00 35.79 ? 13  MET   B CG  1 
ATOM   913  S  SD  . MET   B 1 13  ? 19.227 -32.359 -6.892  0.80 31.57 ? 13  MET   B SD  1 
ATOM   914  C  CE  . MET   B 1 13  ? 20.517 -32.602 -5.682  0.80 36.30 ? 13  MET   B CE  1 
ATOM   915  N  N   . VAL   B 1 14  ? 18.893 -30.854 -9.616  1.00 17.43 ? 14  VAL   B N   1 
ATOM   916  C  CA  . VAL   B 1 14  ? 18.352 -29.584 -9.143  1.00 14.49 ? 14  VAL   B CA  1 
ATOM   917  C  C   . VAL   B 1 14  ? 17.550 -29.853 -7.885  1.00 15.70 ? 14  VAL   B C   1 
ATOM   918  O  O   . VAL   B 1 14  ? 16.843 -30.879 -7.717  1.00 19.12 ? 14  VAL   B O   1 
ATOM   919  C  CB  . VAL   B 1 14  ? 17.509 -28.903 -10.236 1.00 17.48 ? 14  VAL   B CB  1 
ATOM   920  C  CG1 . VAL   B 1 14  ? 16.800 -27.617 -9.782  1.00 14.63 ? 14  VAL   B CG1 1 
ATOM   921  C  CG2 . VAL   B 1 14  ? 18.419 -28.604 -11.382 1.00 16.78 ? 14  VAL   B CG2 1 
ATOM   922  N  N   . LYS   B 1 15  ? 17.701 -28.917 -6.968  1.00 17.20 ? 15  LYS   B N   1 
ATOM   923  C  CA  . LYS   B 1 15  ? 16.971 -28.977 -5.735  1.00 15.93 ? 15  LYS   B CA  1 
ATOM   924  C  C   . LYS   B 1 15  ? 16.354 -27.599 -5.397  1.00 15.90 ? 15  LYS   B C   1 
ATOM   925  O  O   . LYS   B 1 15  ? 16.989 -26.561 -5.534  1.00 19.14 ? 15  LYS   B O   1 
ATOM   926  C  CB  . LYS   B 1 15  ? 17.851 -29.470 -4.621  1.00 22.27 ? 15  LYS   B CB  1 
ATOM   927  C  CG  . LYS   B 1 15  ? 17.077 -29.505 -3.313  1.00 23.81 ? 15  LYS   B CG  1 
ATOM   928  C  CD  . LYS   B 1 15  ? 17.633 -30.493 -2.353  1.00 30.96 ? 15  LYS   B CD  1 
ATOM   929  C  CE  . LYS   B 1 15  ? 16.625 -30.704 -1.260  1.00 28.20 ? 15  LYS   B CE  1 
ATOM   930  N  NZ  . LYS   B 1 15  ? 17.345 -31.376 -0.176  1.00 34.76 ? 15  LYS   B NZ  1 
ATOM   931  N  N   . VAL   B 1 16  ? 15.075 -27.617 -4.994  1.00 13.01 ? 16  VAL   B N   1 
ATOM   932  C  CA  . VAL   B 1 16  ? 14.346 -26.393 -4.789  1.00 10.79 ? 16  VAL   B CA  1 
ATOM   933  C  C   . VAL   B 1 16  ? 13.652 -26.434 -3.400  1.00 8.77  ? 16  VAL   B C   1 
ATOM   934  O  O   . VAL   B 1 16  ? 12.893 -27.398 -3.093  1.00 10.35 ? 16  VAL   B O   1 
ATOM   935  C  CB  . VAL   B 1 16  ? 13.302 -26.165 -5.902  1.00 12.89 ? 16  VAL   B CB  1 
ATOM   936  C  CG1 . VAL   B 1 16  ? 12.753 -24.729 -5.797  1.00 11.68 ? 16  VAL   B CG1 1 
ATOM   937  C  CG2 . VAL   B 1 16  ? 13.981 -26.414 -7.254  1.00 12.45 ? 16  VAL   B CG2 1 
ATOM   938  N  N   . LEU   B 1 17  ? 13.815 -25.351 -2.653  1.00 9.63  ? 17  LEU   B N   1 
ATOM   939  C  CA  . LEU   B 1 17  ? 13.238 -25.206 -1.305  1.00 9.67  ? 17  LEU   B CA  1 
ATOM   940  C  C   . LEU   B 1 17  ? 12.406 -23.891 -1.261  1.00 9.38  ? 17  LEU   B C   1 
ATOM   941  O  O   . LEU   B 1 17  ? 12.709 -22.904 -1.939  1.00 10.62 ? 17  LEU   B O   1 
ATOM   942  C  CB  . LEU   B 1 17  ? 14.337 -25.123 -0.237  1.00 9.70  ? 17  LEU   B CB  1 
ATOM   943  C  CG  . LEU   B 1 17  ? 15.305 -26.354 -0.053  1.00 12.35 ? 17  LEU   B CG  1 
ATOM   944  C  CD1 . LEU   B 1 17  ? 16.401 -26.064 0.969   1.00 13.89 ? 17  LEU   B CD1 1 
ATOM   945  C  CD2 . LEU   B 1 17  ? 14.566 -27.653 0.284   1.00 14.50 ? 17  LEU   B CD2 1 
ATOM   946  N  N   . ASP   B 1 18  ? 11.391 -23.926 -0.418  1.00 9.15  ? 18  ASP   B N   1 
ATOM   947  C  CA  . ASP   B 1 18  ? 10.470 -22.831 -0.174  1.00 6.28  ? 18  ASP   B CA  1 
ATOM   948  C  C   . ASP   B 1 18  ? 10.778 -22.229 1.240   1.00 5.83  ? 18  ASP   B C   1 
ATOM   949  O  O   . ASP   B 1 18  ? 10.584 -22.848 2.285   1.00 8.79  ? 18  ASP   B O   1 
ATOM   950  C  CB  . ASP   B 1 18  ? 9.082  -23.432 -0.293  1.00 7.45  ? 18  ASP   B CB  1 
ATOM   951  C  CG  . ASP   B 1 18  ? 7.945  -22.469 0.088   1.00 8.30  ? 18  ASP   B CG  1 
ATOM   952  O  OD1 . ASP   B 1 18  ? 8.101  -21.532 0.892   1.00 9.57  ? 18  ASP   B OD1 1 
ATOM   953  O  OD2 . ASP   B 1 18  ? 6.795  -22.781 -0.321  1.00 12.22 ? 18  ASP   B OD2 1 
ATOM   954  N  N   . ALA   B 1 19  ? 11.171 -20.980 1.218   1.00 6.63  ? 19  ALA   B N   1 
ATOM   955  C  CA  . ALA   B 1 19  ? 11.619 -20.210 2.348   1.00 6.25  ? 19  ALA   B CA  1 
ATOM   956  C  C   . ALA   B 1 19  ? 10.443 -19.578 3.148   1.00 7.72  ? 19  ALA   B C   1 
ATOM   957  O  O   . ALA   B 1 19  ? 10.696 -18.925 4.165   1.00 10.81 ? 19  ALA   B O   1 
ATOM   958  C  CB  . ALA   B 1 19  ? 12.519 -19.082 1.859   1.00 5.71  ? 19  ALA   B CB  1 
ATOM   959  N  N   . VAL   B 1 20  ? 9.210  -19.666 2.623   1.00 8.28  ? 20  VAL   B N   1 
ATOM   960  C  CA  . VAL   B 1 20  ? 8.069  -19.110 3.301   1.00 9.36  ? 20  VAL   B CA  1 
ATOM   961  C  C   . VAL   B 1 20  ? 7.384  -20.152 4.154   1.00 10.95 ? 20  VAL   B C   1 
ATOM   962  O  O   . VAL   B 1 20  ? 7.033  -19.889 5.330   1.00 17.65 ? 20  VAL   B O   1 
ATOM   963  C  CB  . VAL   B 1 20  ? 7.050  -18.544 2.267   1.00 11.21 ? 20  VAL   B CB  1 
ATOM   964  C  CG1 . VAL   B 1 20  ? 5.711  -18.195 2.891   1.00 14.88 ? 20  VAL   B CG1 1 
ATOM   965  C  CG2 . VAL   B 1 20  ? 7.637  -17.370 1.579   1.00 14.19 ? 20  VAL   B CG2 1 
ATOM   966  N  N   . ARG   B 1 21  ? 7.193  -21.326 3.577   1.00 12.45 ? 21  ARG   B N   1 
ATOM   967  C  CA  . ARG   B 1 21  ? 6.625  -22.446 4.264   1.00 11.13 ? 21  ARG   B CA  1 
ATOM   968  C  C   . ARG   B 1 21  ? 7.632  -23.406 4.891   1.00 12.39 ? 21  ARG   B C   1 
ATOM   969  O  O   . ARG   B 1 21  ? 7.179  -24.278 5.639   1.00 15.54 ? 21  ARG   B O   1 
ATOM   970  C  CB  . ARG   B 1 21  ? 5.750  -23.236 3.336   1.00 13.78 ? 21  ARG   B CB  1 
ATOM   971  C  CG  . ARG   B 1 21  ? 4.678  -22.400 2.702   1.00 17.37 ? 21  ARG   B CG  1 
ATOM   972  C  CD  . ARG   B 1 21  ? 3.696  -23.328 2.092   1.00 21.73 ? 21  ARG   B CD  1 
ATOM   973  N  NE  . ARG   B 1 21  ? 4.287  -24.013 0.984   1.00 17.80 ? 21  ARG   B NE  1 
ATOM   974  C  CZ  . ARG   B 1 21  ? 3.872  -25.204 0.541   1.00 25.67 ? 21  ARG   B CZ  1 
ATOM   975  N  NH1 . ARG   B 1 21  ? 2.847  -25.851 1.123   1.00 27.50 ? 21  ARG   B NH1 1 
ATOM   976  N  NH2 . ARG   B 1 21  ? 4.482  -25.748 -0.484  1.00 25.88 ? 21  ARG   B NH2 1 
ATOM   977  N  N   . GLY   B 1 22  ? 8.927  -23.261 4.583   1.00 14.52 ? 22  GLY   B N   1 
ATOM   978  C  CA  . GLY   B 1 22  ? 9.964  -24.137 5.135   1.00 12.95 ? 22  GLY   B CA  1 
ATOM   979  C  C   . GLY   B 1 22  ? 9.823  -25.585 4.670   1.00 12.47 ? 22  GLY   B C   1 
ATOM   980  O  O   . GLY   B 1 22  ? 9.819  -26.518 5.449   1.00 16.17 ? 22  GLY   B O   1 
ATOM   981  N  N   . SER   B 1 23  ? 9.682  -25.774 3.383   1.00 12.96 ? 23  SER   B N   1 
ATOM   982  C  CA  . SER   B 1 23  ? 9.389  -27.079 2.846   1.00 16.40 ? 23  SER   B CA  1 
ATOM   983  C  C   . SER   B 1 23  ? 10.114 -27.201 1.546   1.00 14.11 ? 23  SER   B C   1 
ATOM   984  O  O   . SER   B 1 23  ? 10.506 -26.172 0.927   1.00 13.33 ? 23  SER   B O   1 
ATOM   985  C  CB  . SER   B 1 23  ? 7.912  -27.180 2.558   1.00 20.82 ? 23  SER   B CB  1 
ATOM   986  O  OG  . SER   B 1 23  ? 7.580  -26.213 1.563   1.00 22.63 ? 23  SER   B OG  1 
ATOM   987  N  N   . PRO   B 1 24  ? 10.286 -28.449 1.095   1.00 14.92 ? 24  PRO   B N   1 
ATOM   988  C  CA  . PRO   B 1 24  ? 10.672 -28.614 -0.301  1.00 15.19 ? 24  PRO   B CA  1 
ATOM   989  C  C   . PRO   B 1 24  ? 9.614  -28.000 -1.225  1.00 12.62 ? 24  PRO   B C   1 
ATOM   990  O  O   . PRO   B 1 24  ? 8.436  -27.976 -0.856  1.00 15.08 ? 24  PRO   B O   1 
ATOM   991  C  CB  . PRO   B 1 24  ? 10.795 -30.132 -0.469  1.00 15.76 ? 24  PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 1 24  ? 10.110 -30.718 0.690   1.00 20.98 ? 24  PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 1 24  ? 9.973  -29.718 1.757   1.00 15.67 ? 24  PRO   B CD  1 
ATOM   994  N  N   . ALA   B 1 25  ? 10.042 -27.546 -2.409  1.00 13.89 ? 25  ALA   B N   1 
ATOM   995  C  CA  . ALA   B 1 25  ? 9.148  -27.059 -3.467  1.00 12.42 ? 25  ALA   B CA  1 
ATOM   996  C  C   . ALA   B 1 25  ? 8.882  -28.222 -4.429  1.00 11.14 ? 25  ALA   B C   1 
ATOM   997  O  O   . ALA   B 1 25  ? 9.706  -28.537 -5.269  1.00 14.56 ? 25  ALA   B O   1 
ATOM   998  C  CB  . ALA   B 1 25  ? 9.767  -25.860 -4.185  1.00 13.62 ? 25  ALA   B CB  1 
ATOM   999  N  N   . ILE   B 1 26  ? 7.692  -28.822 -4.253  1.00 12.06 ? 26  ILE   B N   1 
ATOM   1000 C  CA  . ILE   B 1 26  ? 7.235  -30.014 -4.921  1.00 12.09 ? 26  ILE   B CA  1 
ATOM   1001 C  C   . ILE   B 1 26  ? 6.509  -29.724 -6.256  1.00 12.16 ? 26  ILE   B C   1 
ATOM   1002 O  O   . ILE   B 1 26  ? 5.739  -28.770 -6.376  1.00 19.81 ? 26  ILE   B O   1 
ATOM   1003 C  CB  . ILE   B 1 26  ? 6.321  -30.840 -3.986  1.00 16.95 ? 26  ILE   B CB  1 
ATOM   1004 C  CG1 . ILE   B 1 26  ? 7.028  -31.168 -2.637  1.00 19.64 ? 26  ILE   B CG1 1 
ATOM   1005 C  CG2 . ILE   B 1 26  ? 5.821  -32.132 -4.671  1.00 20.86 ? 26  ILE   B CG2 1 
ATOM   1006 C  CD1 . ILE   B 1 26  ? 6.051  -31.519 -1.507  1.00 22.09 ? 26  ILE   B CD1 1 
ATOM   1007 N  N   . ASN   B 1 27  ? 6.745  -30.593 -7.235  1.00 14.06 ? 27  ASN   B N   1 
ATOM   1008 C  CA  . ASN   B 1 27  ? 6.126  -30.525 -8.581  1.00 16.35 ? 27  ASN   B CA  1 
ATOM   1009 C  C   . ASN   B 1 27  ? 6.416  -29.207 -9.285  1.00 19.42 ? 27  ASN   B C   1 
ATOM   1010 O  O   . ASN   B 1 27  ? 5.523  -28.631 -9.920  1.00 19.38 ? 27  ASN   B O   1 
ATOM   1011 C  CB  . ASN   B 1 27  ? 4.583  -30.738 -8.462  1.00 22.52 ? 27  ASN   B CB  1 
ATOM   1012 C  CG  . ASN   B 1 27  ? 3.940  -31.169 -9.765  1.00 29.83 ? 27  ASN   B CG  1 
ATOM   1013 O  OD1 . ASN   B 1 27  ? 4.486  -32.013 -10.465 1.00 34.96 ? 27  ASN   B OD1 1 
ATOM   1014 N  N   . VAL   B 1 28  ? 7.630  -28.683 -9.146  1.00 16.79 ? 28  VAL   B N   1 
ATOM   1015 C  CA  . VAL   B 1 28  ? 8.001  -27.491 -9.893  1.00 16.59 ? 28  VAL   B CA  1 
ATOM   1016 C  C   . VAL   B 1 28  ? 8.711  -27.839 -11.199 1.00 13.30 ? 28  VAL   B C   1 
ATOM   1017 O  O   . VAL   B 1 28  ? 9.620  -28.651 -11.233 1.00 18.71 ? 28  VAL   B O   1 
ATOM   1018 C  CB  . VAL   B 1 28  ? 8.878  -26.600 -9.024  1.00 16.52 ? 28  VAL   B CB  1 
ATOM   1019 C  CG1 . VAL   B 1 28  ? 9.311  -25.363 -9.734  1.00 14.04 ? 28  VAL   B CG1 1 
ATOM   1020 C  CG2 . VAL   B 1 28  ? 8.126  -26.263 -7.745  1.00 19.12 ? 28  VAL   B CG2 1 
ATOM   1021 N  N   . ALA   B 1 29  ? 8.244  -27.236 -12.279 1.00 9.92  ? 29  ALA   B N   1 
ATOM   1022 C  CA  . ALA   B 1 29  ? 8.829  -27.435 -13.598 1.00 11.53 ? 29  ALA   B CA  1 
ATOM   1023 C  C   . ALA   B 1 29  ? 10.227 -26.790 -13.663 1.00 12.82 ? 29  ALA   B C   1 
ATOM   1024 O  O   . ALA   B 1 29  ? 10.413 -25.669 -13.268 1.00 13.21 ? 29  ALA   B O   1 
ATOM   1025 C  CB  . ALA   B 1 29  ? 7.933  -26.879 -14.695 1.00 15.47 ? 29  ALA   B CB  1 
ATOM   1026 N  N   . VAL   B 1 30  ? 11.198 -27.557 -14.139 1.00 13.61 ? 30  VAL   B N   1 
ATOM   1027 C  CA  . VAL   B 1 30  ? 12.578 -27.114 -14.344 1.00 14.17 ? 30  VAL   B CA  1 
ATOM   1028 C  C   . VAL   B 1 30  ? 12.959 -27.460 -15.788 1.00 16.48 ? 30  VAL   B C   1 
ATOM   1029 O  O   . VAL   B 1 30  ? 12.804 -28.598 -16.224 1.00 16.62 ? 30  VAL   B O   1 
ATOM   1030 C  CB  . VAL   B 1 30  ? 13.485 -27.855 -13.358 1.00 15.61 ? 30  VAL   B CB  1 
ATOM   1031 C  CG1 . VAL   B 1 30  ? 14.939 -27.536 -13.571 1.00 14.76 ? 30  VAL   B CG1 1 
ATOM   1032 C  CG2 . VAL   B 1 30  ? 13.051 -27.539 -11.948 1.00 19.84 ? 30  VAL   B CG2 1 
ATOM   1033 N  N   . HIS   B 1 31  ? 13.405 -26.456 -16.531 1.00 18.95 ? 31  HIS   B N   1 
ATOM   1034 C  CA  . HIS   B 1 31  ? 13.870 -26.605 -17.893 1.00 19.97 ? 31  HIS   B CA  1 
ATOM   1035 C  C   . HIS   B 1 31  ? 15.319 -26.224 -17.974 1.00 16.35 ? 31  HIS   B C   1 
ATOM   1036 O  O   . HIS   B 1 31  ? 15.706 -25.137 -17.509 1.00 17.25 ? 31  HIS   B O   1 
ATOM   1037 C  CB  . HIS   B 1 31  ? 13.096 -25.697 -18.851 1.00 22.43 ? 31  HIS   B CB  1 
ATOM   1038 C  CG  . HIS   B 1 31  ? 11.705 -26.155 -19.092 1.00 22.77 ? 31  HIS   B CG  1 
ATOM   1039 N  ND1 . HIS   B 1 31  ? 10.740 -26.071 -18.112 1.00 29.84 ? 31  HIS   B ND1 1 
ATOM   1040 C  CD2 . HIS   B 1 31  ? 11.131 -26.772 -20.147 1.00 29.66 ? 31  HIS   B CD2 1 
ATOM   1041 C  CE1 . HIS   B 1 31  ? 9.613  -26.583 -18.575 1.00 31.20 ? 31  HIS   B CE1 1 
ATOM   1042 N  NE2 . HIS   B 1 31  ? 9.823  -27.010 -19.810 1.00 33.71 ? 31  HIS   B NE2 1 
ATOM   1043 N  N   . VAL   B 1 32  ? 16.070 -27.077 -18.644 1.00 19.13 ? 32  VAL   B N   1 
ATOM   1044 C  CA  . VAL   B 1 32  ? 17.503 -26.833 -18.868 1.00 15.93 ? 32  VAL   B CA  1 
ATOM   1045 C  C   . VAL   B 1 32  ? 17.775 -26.650 -20.363 1.00 17.35 ? 32  VAL   B C   1 
ATOM   1046 O  O   . VAL   B 1 32  ? 17.300 -27.436 -21.207 1.00 20.18 ? 32  VAL   B O   1 
ATOM   1047 C  CB  . VAL   B 1 32  ? 18.403 -27.951 -18.362 1.00 13.39 ? 32  VAL   B CB  1 
ATOM   1048 C  CG1 . VAL   B 1 32  ? 19.873 -27.493 -18.519 1.00 12.07 ? 32  VAL   B CG1 1 
ATOM   1049 C  CG2 . VAL   B 1 32  ? 18.054 -28.352 -16.928 1.00 13.59 ? 32  VAL   B CG2 1 
ATOM   1050 N  N   . PHE   B 1 33  ? 18.575 -25.628 -20.667 1.00 21.02 ? 33  PHE   B N   1 
ATOM   1051 C  CA  . PHE   B 1 33  ? 18.966 -25.271 -22.025 1.00 24.99 ? 33  PHE   B CA  1 
ATOM   1052 C  C   . PHE   B 1 33  ? 20.501 -25.201 -22.063 1.00 25.15 ? 33  PHE   B C   1 
ATOM   1053 O  O   . PHE   B 1 33  ? 21.134 -25.120 -21.018 1.00 24.62 ? 33  PHE   B O   1 
ATOM   1054 C  CB  . PHE   B 1 33  ? 18.335 -23.922 -22.444 1.00 27.32 ? 33  PHE   B CB  1 
ATOM   1055 C  CG  . PHE   B 1 33  ? 16.845 -23.827 -22.169 1.00 30.00 ? 33  PHE   B CG  1 
ATOM   1056 C  CD1 . PHE   B 1 33  ? 16.394 -23.326 -20.957 1.00 29.49 ? 33  PHE   B CD1 1 
ATOM   1057 C  CD2 . PHE   B 1 33  ? 15.901 -24.200 -23.134 1.00 38.16 ? 33  PHE   B CD2 1 
ATOM   1058 C  CE1 . PHE   B 1 33  ? 15.040 -23.231 -20.691 1.00 38.06 ? 33  PHE   B CE1 1 
ATOM   1059 C  CE2 . PHE   B 1 33  ? 14.523 -24.108 -22.878 1.00 36.15 ? 33  PHE   B CE2 1 
ATOM   1060 C  CZ  . PHE   B 1 33  ? 14.100 -23.625 -21.653 1.00 44.42 ? 33  PHE   B CZ  1 
ATOM   1061 N  N   . ARG   B 1 34  ? 21.058 -25.265 -23.272 1.00 31.05 ? 34  ARG   B N   1 
ATOM   1062 C  CA  . ARG   B 1 34  ? 22.494 -25.287 -23.542 1.00 26.96 ? 34  ARG   B CA  1 
ATOM   1063 C  C   . ARG   B 1 34  ? 22.664 -24.448 -24.758 1.00 32.69 ? 34  ARG   B C   1 
ATOM   1064 O  O   . ARG   B 1 34  ? 21.820 -24.512 -25.659 1.00 42.28 ? 34  ARG   B O   1 
ATOM   1065 C  CB  . ARG   B 1 34  ? 22.915 -26.708 -23.919 1.00 34.64 ? 34  ARG   B CB  1 
ATOM   1066 N  N   . LYS   B 1 35  ? 23.769 -23.739 -24.865 1.00 29.98 ? 35  LYS   B N   1 
ATOM   1067 C  CA  . LYS   B 1 35  ? 23.896 -22.752 -25.944 1.00 30.92 ? 35  LYS   B CA  1 
ATOM   1068 C  C   . LYS   B 1 35  ? 24.481 -23.351 -27.225 1.00 30.52 ? 35  LYS   B C   1 
ATOM   1069 O  O   . LYS   B 1 35  ? 25.435 -24.134 -27.180 1.00 51.12 ? 35  LYS   B O   1 
ATOM   1070 C  CB  . LYS   B 1 35  ? 24.691 -21.547 -25.458 1.00 29.28 ? 35  LYS   B CB  1 
ATOM   1071 C  CG  . LYS   B 1 35  ? 24.613 -20.351 -26.379 1.00 33.13 ? 35  LYS   B CG  1 
ATOM   1072 C  CD  . LYS   B 1 35  ? 25.214 -19.103 -25.728 1.00 35.47 ? 35  LYS   B CD  1 
ATOM   1073 C  CE  . LYS   B 1 35  ? 26.683 -19.294 -25.362 1.00 32.25 ? 35  LYS   B CE  1 
ATOM   1074 N  N   . GLU   B 1 42  ? 18.550 -23.384 -26.612 1.00 41.97 ? 42  GLU   B N   1 
ATOM   1075 C  CA  . GLU   B 1 42  ? 18.478 -24.783 -27.091 1.00 41.98 ? 42  GLU   B CA  1 
ATOM   1076 C  C   . GLU   B 1 42  ? 18.027 -25.802 -26.028 1.00 36.55 ? 42  GLU   B C   1 
ATOM   1077 O  O   . GLU   B 1 42  ? 18.811 -26.178 -25.127 1.00 37.43 ? 42  GLU   B O   1 
ATOM   1078 C  CB  . GLU   B 1 42  ? 19.831 -25.220 -27.625 1.00 28.31 ? 42  GLU   B CB  1 
ATOM   1079 N  N   . PRO   B 1 43  ? 16.773 -26.289 -26.121 1.00 43.69 ? 43  PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 1 43  ? 16.316 -27.189 -25.054 1.00 37.73 ? 43  PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 1 43  ? 17.232 -28.379 -24.843 1.00 28.40 ? 43  PRO   B C   1 
ATOM   1082 O  O   . PRO   B 1 43  ? 17.620 -29.017 -25.825 1.00 35.19 ? 43  PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 1 43  ? 14.949 -27.661 -25.565 1.00 33.54 ? 43  PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 1 43  ? 14.476 -26.522 -26.413 1.00 25.58 ? 43  PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 1 43  ? 15.723 -26.087 -27.139 1.00 33.83 ? 43  PRO   B CD  1 
ATOM   1086 N  N   . PHE   B 1 44  ? 17.581 -28.667 -23.583 1.00 32.67 ? 44  PHE   B N   1 
ATOM   1087 C  CA  . PHE   B 1 44  ? 18.525 -29.766 -23.264 1.00 26.78 ? 44  PHE   B CA  1 
ATOM   1088 C  C   . PHE   B 1 44  ? 17.987 -30.871 -22.310 1.00 26.69 ? 44  PHE   B C   1 
ATOM   1089 O  O   . PHE   B 1 44  ? 18.304 -32.047 -22.501 1.00 27.28 ? 44  PHE   B O   1 
ATOM   1090 C  CB  . PHE   B 1 44  ? 19.813 -29.152 -22.673 1.00 19.56 ? 44  PHE   B CB  1 
ATOM   1091 C  CG  . PHE   B 1 44  ? 20.790 -30.186 -22.115 1.00 22.24 ? 44  PHE   B CG  1 
ATOM   1092 C  CD1 . PHE   B 1 44  ? 21.652 -30.872 -22.965 1.00 25.28 ? 44  PHE   B CD1 1 
ATOM   1093 C  CD2 . PHE   B 1 44  ? 20.891 -30.403 -20.759 1.00 17.11 ? 44  PHE   B CD2 1 
ATOM   1094 C  CE1 . PHE   B 1 44  ? 22.573 -31.762 -22.480 1.00 19.22 ? 44  PHE   B CE1 1 
ATOM   1095 C  CE2 . PHE   B 1 44  ? 21.744 -31.331 -20.249 1.00 23.67 ? 44  PHE   B CE2 1 
ATOM   1096 C  CZ  . PHE   B 1 44  ? 22.619 -32.024 -21.130 1.00 30.12 ? 44  PHE   B CZ  1 
ATOM   1097 N  N   . ALA   B 1 45  ? 17.200 -30.513 -21.283 1.00 16.20 ? 45  ALA   B N   1 
ATOM   1098 C  CA  . ALA   B 1 45  ? 16.659 -31.477 -20.336 1.00 21.74 ? 45  ALA   B CA  1 
ATOM   1099 C  C   . ALA   B 1 45  ? 15.566 -30.787 -19.564 1.00 20.49 ? 45  ALA   B C   1 
ATOM   1100 O  O   . ALA   B 1 45  ? 15.560 -29.591 -19.547 1.00 20.48 ? 45  ALA   B O   1 
ATOM   1101 C  CB  . ALA   B 1 45  ? 17.736 -31.991 -19.425 1.00 20.61 ? 45  ALA   B CB  1 
ATOM   1102 N  N   . SER   B 1 46  ? 14.621 -31.529 -19.000 1.00 17.75 ? 46  SER   B N   1 
ATOM   1103 C  CA  . SER   B 1 46  ? 13.607 -30.912 -18.178 1.00 16.05 ? 46  SER   B CA  1 
ATOM   1104 C  C   . SER   B 1 46  ? 12.911 -31.950 -17.283 1.00 16.99 ? 46  SER   B C   1 
ATOM   1105 O  O   . SER   B 1 46  ? 13.075 -33.193 -17.444 1.00 18.40 ? 46  SER   B O   1 
ATOM   1106 C  CB  . SER   B 1 46  ? 12.601 -30.121 -19.062 1.00 19.69 ? 46  SER   B CB  1 
ATOM   1107 O  OG  . SER   B 1 46  ? 11.962 -30.929 -20.012 1.00 22.65 ? 46  SER   B OG  1 
ATOM   1108 N  N   . GLY   B 1 47  ? 12.182 -31.455 -16.293 1.00 15.80 ? 47  GLY   B N   1 
ATOM   1109 C  CA  . GLY   B 1 47  ? 11.411 -32.355 -15.431 1.00 16.52 ? 47  GLY   B CA  1 
ATOM   1110 C  C   . GLY   B 1 47  ? 10.672 -31.585 -14.380 1.00 14.77 ? 47  GLY   B C   1 
ATOM   1111 O  O   . GLY   B 1 47  ? 10.616 -30.377 -14.444 1.00 15.31 ? 47  GLY   B O   1 
ATOM   1112 N  N   . LYS   B 1 48  ? 10.088 -32.302 -13.427 1.00 16.88 ? 48  LYS   B N   1 
ATOM   1113 C  CA  . LYS   B 1 48  ? 9.425  -31.683 -12.293 1.00 17.89 ? 48  LYS   B CA  1 
ATOM   1114 C  C   . LYS   B 1 48  ? 10.079 -32.123 -11.007 1.00 17.01 ? 48  LYS   B C   1 
ATOM   1115 O  O   . LYS   B 1 48  ? 10.478 -33.292 -10.864 1.00 20.85 ? 48  LYS   B O   1 
ATOM   1116 C  CB  . LYS   B 1 48  ? 7.883  -31.970 -12.294 1.00 19.53 ? 48  LYS   B CB  1 
ATOM   1117 C  CG  . LYS   B 1 48  ? 7.218  -31.175 -13.417 1.00 22.79 ? 48  LYS   B CG  1 
ATOM   1118 C  CD  . LYS   B 1 48  ? 5.706  -31.088 -13.333 1.00 25.83 ? 48  LYS   B CD  1 
ATOM   1119 C  CE  . LYS   B 1 48  ? 5.186  -30.287 -14.511 1.00 28.40 ? 48  LYS   B CE  1 
ATOM   1120 N  N   . THR   B 1 49  ? 10.202 -31.227 -10.048 1.00 15.32 ? 49  THR   B N   1 
ATOM   1121 C  CA  . THR   B 1 49  ? 10.656 -31.687 -8.768  1.00 14.54 ? 49  THR   B CA  1 
ATOM   1122 C  C   . THR   B 1 49  ? 9.755  -32.725 -8.031  1.00 13.82 ? 49  THR   B C   1 
ATOM   1123 O  O   . THR   B 1 49  ? 8.496  -32.753 -8.141  1.00 17.00 ? 49  THR   B O   1 
ATOM   1124 C  CB  . THR   B 1 49  ? 10.923 -30.518 -7.822  1.00 11.93 ? 49  THR   B CB  1 
ATOM   1125 O  OG1 . THR   B 1 49  ? 9.702  -29.805 -7.615  1.00 13.94 ? 49  THR   B OG1 1 
ATOM   1126 C  CG2 . THR   B 1 49  ? 12.013 -29.597 -8.360  1.00 9.24  ? 49  THR   B CG2 1 
ATOM   1127 N  N   . SER   B 1 50  ? 10.445 -33.641 -7.349  1.00 18.01 ? 50  SER   B N   1 
ATOM   1128 C  CA  . SER   B 1 50  ? 9.854  -34.650 -6.476  1.00 18.66 ? 50  SER   B CA  1 
ATOM   1129 C  C   . SER   B 1 50  ? 9.270  -34.094 -5.146  1.00 20.86 ? 50  SER   B C   1 
ATOM   1130 O  O   . SER   B 1 50  ? 9.381  -32.926 -4.811  1.00 17.60 ? 50  SER   B O   1 
ATOM   1131 C  CB  . SER   B 1 50  ? 10.918 -35.712 -6.114  1.00 22.38 ? 50  SER   B CB  1 
ATOM   1132 O  OG  . SER   B 1 50  ? 11.818 -35.215 -5.099  1.00 23.67 ? 50  SER   B OG  1 
ATOM   1133 N  N   . GLU   B 1 51  ? 8.692  -34.982 -4.365  1.00 19.96 ? 51  GLU   B N   1 
ATOM   1134 C  CA  . GLU   B 1 51  ? 8.237  -34.708 -2.991  1.00 21.77 ? 51  GLU   B CA  1 
ATOM   1135 C  C   . GLU   B 1 51  ? 9.366  -34.157 -2.059  1.00 22.20 ? 51  GLU   B C   1 
ATOM   1136 O  O   . GLU   B 1 51  ? 9.107  -33.471 -1.063  1.00 22.93 ? 51  GLU   B O   1 
ATOM   1137 C  CB  . GLU   B 1 51  ? 7.520  -35.975 -2.443  1.00 21.06 ? 51  GLU   B CB  1 
ATOM   1138 C  CG  . GLU   B 1 51  ? 8.349  -37.269 -2.495  1.00 27.33 ? 51  GLU   B CG  1 
ATOM   1139 C  CD  . GLU   B 1 51  ? 8.525  -37.884 -3.907  1.00 26.30 ? 51  GLU   B CD  1 
ATOM   1140 N  N   . SER   B 1 52  ? 10.617 -34.427 -2.420  1.00 22.16 ? 52  SER   B N   1 
ATOM   1141 C  CA  . SER   B 1 52  ? 11.773 -33.931 -1.682  1.00 19.09 ? 52  SER   B CA  1 
ATOM   1142 C  C   . SER   B 1 52  ? 12.331 -32.625 -2.269  1.00 19.98 ? 52  SER   B C   1 
ATOM   1143 O  O   . SER   B 1 52  ? 13.342 -32.137 -1.812  1.00 23.18 ? 52  SER   B O   1 
ATOM   1144 C  CB  . SER   B 1 52  ? 12.876 -35.005 -1.729  1.00 25.97 ? 52  SER   B CB  1 
ATOM   1145 O  OG  . SER   B 1 52  ? 13.358 -35.173 -3.053  1.00 31.92 ? 52  SER   B OG  1 
ATOM   1146 N  N   . GLY   B 1 53  ? 11.676 -32.065 -3.283  1.00 18.05 ? 53  GLY   B N   1 
ATOM   1147 C  CA  . GLY   B 1 53  ? 12.176 -30.868 -3.919  1.00 18.12 ? 53  GLY   B CA  1 
ATOM   1148 C  C   . GLY   B 1 53  ? 13.293 -31.101 -4.909  1.00 16.48 ? 53  GLY   B C   1 
ATOM   1149 O  O   . GLY   B 1 53  ? 13.856 -30.144 -5.448  1.00 14.69 ? 53  GLY   B O   1 
ATOM   1150 N  N   . GLU   B 1 54  ? 13.580 -32.368 -5.168  1.00 14.71 ? 54  GLU   B N   1 
ATOM   1151 C  CA  . GLU   B 1 54  ? 14.752 -32.748 -5.940  1.00 16.85 ? 54  GLU   B CA  1 
ATOM   1152 C  C   . GLU   B 1 54  ? 14.318 -33.230 -7.296  1.00 16.43 ? 54  GLU   B C   1 
ATOM   1153 O  O   . GLU   B 1 54  ? 13.253 -33.843 -7.475  1.00 19.71 ? 54  GLU   B O   1 
ATOM   1154 C  CB  . GLU   B 1 54  ? 15.553 -33.836 -5.218  1.00 23.45 ? 54  GLU   B CB  1 
ATOM   1155 C  CG  . GLU   B 1 54  ? 16.116 -33.390 -3.894  1.00 29.00 ? 54  GLU   B CG  1 
ATOM   1156 C  CD  . GLU   B 1 54  ? 16.925 -34.456 -3.162  0.80 37.13 ? 54  GLU   B CD  1 
ATOM   1157 O  OE1 . GLU   B 1 54  ? 16.808 -35.652 -3.472  0.80 35.13 ? 54  GLU   B OE1 1 
ATOM   1158 O  OE2 . GLU   B 1 54  ? 17.681 -34.080 -2.239  0.80 40.48 ? 54  GLU   B OE2 1 
ATOM   1159 N  N   . LEU   B 1 55  ? 15.173 -32.965 -8.263  1.00 17.03 ? 55  LEU   B N   1 
ATOM   1160 C  CA  . LEU   B 1 55  ? 15.006 -33.462 -9.586  1.00 16.51 ? 55  LEU   B CA  1 
ATOM   1161 C  C   . LEU   B 1 55  ? 16.322 -34.098 -10.080 1.00 17.34 ? 55  LEU   B C   1 
ATOM   1162 O  O   . LEU   B 1 55  ? 17.301 -33.420 -10.257 1.00 15.62 ? 55  LEU   B O   1 
ATOM   1163 C  CB  . LEU   B 1 55  ? 14.548 -32.347 -10.497 1.00 17.83 ? 55  LEU   B CB  1 
ATOM   1164 C  CG  . LEU   B 1 55  ? 14.497 -32.679 -11.973 1.00 21.42 ? 55  LEU   B CG  1 
ATOM   1165 C  CD1 . LEU   B 1 55  ? 13.633 -33.883 -12.246 1.00 19.46 ? 55  LEU   B CD1 1 
ATOM   1166 C  CD2 . LEU   B 1 55  ? 14.063 -31.450 -12.717 1.00 22.54 ? 55  LEU   B CD2 1 
ATOM   1167 N  N   . HIS   B 1 56  ? 16.273 -35.410 -10.204 1.00 24.65 ? 56  HIS   B N   1 
ATOM   1168 C  CA  . HIS   B 1 56  ? 17.329 -36.248 -10.713 1.00 27.39 ? 56  HIS   B CA  1 
ATOM   1169 C  C   . HIS   B 1 56  ? 16.920 -36.780 -12.107 1.00 23.83 ? 56  HIS   B C   1 
ATOM   1170 O  O   . HIS   B 1 56  ? 15.775 -36.675 -12.512 1.00 29.84 ? 56  HIS   B O   1 
ATOM   1171 C  CB  . HIS   B 1 56  ? 17.493 -37.459 -9.797  1.00 24.44 ? 56  HIS   B CB  1 
ATOM   1172 C  CG  . HIS   B 1 56  ? 18.008 -37.132 -8.441  1.00 33.66 ? 56  HIS   B CG  1 
ATOM   1173 N  ND1 . HIS   B 1 56  ? 17.179 -36.893 -7.367  1.00 38.35 ? 56  HIS   B ND1 1 
ATOM   1174 C  CD2 . HIS   B 1 56  ? 19.274 -37.036 -7.974  1.00 34.27 ? 56  HIS   B CD2 1 
ATOM   1175 C  CE1 . HIS   B 1 56  ? 17.911 -36.644 -6.298  1.00 38.86 ? 56  HIS   B CE1 1 
ATOM   1176 N  NE2 . HIS   B 1 56  ? 19.187 -36.721 -6.639  1.00 40.25 ? 56  HIS   B NE2 1 
ATOM   1177 N  N   . GLY   B 1 57  ? 17.859 -37.364 -12.827 1.00 27.58 ? 57  GLY   B N   1 
ATOM   1178 C  CA  . GLY   B 1 57  ? 17.529 -38.038 -14.080 1.00 23.14 ? 57  GLY   B CA  1 
ATOM   1179 C  C   . GLY   B 1 57  ? 17.356 -37.101 -15.253 1.00 28.03 ? 57  GLY   B C   1 
ATOM   1180 O  O   . GLY   B 1 57  ? 16.784 -37.473 -16.305 1.00 40.16 ? 57  GLY   B O   1 
ATOM   1181 N  N   . LEU   B 1 58  ? 17.836 -35.869 -15.072 1.00 22.31 ? 58  LEU   B N   1 
ATOM   1182 C  CA  . LEU   B 1 58  ? 17.756 -34.826 -16.091 1.00 25.24 ? 58  LEU   B CA  1 
ATOM   1183 C  C   . LEU   B 1 58  ? 18.539 -35.138 -17.337 1.00 21.23 ? 58  LEU   B C   1 
ATOM   1184 O  O   . LEU   B 1 58  ? 18.034 -34.949 -18.453 1.00 23.42 ? 58  LEU   B O   1 
ATOM   1185 C  CB  . LEU   B 1 58  ? 18.277 -33.500 -15.542 1.00 19.40 ? 58  LEU   B CB  1 
ATOM   1186 C  CG  . LEU   B 1 58  ? 17.280 -32.628 -14.851 1.00 18.55 ? 58  LEU   B CG  1 
ATOM   1187 C  CD1 . LEU   B 1 58  ? 17.937 -31.403 -14.226 1.00 21.49 ? 58  LEU   B CD1 1 
ATOM   1188 C  CD2 . LEU   B 1 58  ? 16.180 -32.152 -15.754 1.00 14.60 ? 58  LEU   B CD2 1 
ATOM   1189 N  N   . THR   B 1 59  ? 19.786 -35.537 -17.158 1.00 21.41 ? 59  THR   B N   1 
ATOM   1190 C  CA  . THR   B 1 59  ? 20.639 -35.842 -18.282 1.00 25.28 ? 59  THR   B CA  1 
ATOM   1191 C  C   . THR   B 1 59  ? 21.529 -37.059 -17.978 1.00 28.29 ? 59  THR   B C   1 
ATOM   1192 O  O   . THR   B 1 59  ? 21.416 -37.716 -16.925 1.00 35.68 ? 59  THR   B O   1 
ATOM   1193 C  CB  . THR   B 1 59  ? 21.496 -34.605 -18.643 1.00 28.52 ? 59  THR   B CB  1 
ATOM   1194 O  OG1 . THR   B 1 59  ? 22.029 -34.737 -19.967 1.00 31.66 ? 59  THR   B OG1 1 
ATOM   1195 C  CG2 . THR   B 1 59  ? 22.646 -34.389 -17.634 1.00 29.40 ? 59  THR   B CG2 1 
ATOM   1196 N  N   . THR   B 1 60  ? 22.386 -37.356 -18.947 1.00 38.49 ? 60  THR   B N   1 
ATOM   1197 C  CA  . THR   B 1 60  ? 23.396 -38.407 -18.832 1.00 32.40 ? 60  THR   B CA  1 
ATOM   1198 C  C   . THR   B 1 60  ? 24.813 -37.813 -19.000 1.00 31.12 ? 60  THR   B C   1 
ATOM   1199 O  O   . THR   B 1 60  ? 24.974 -36.722 -19.535 1.00 34.06 ? 60  THR   B O   1 
ATOM   1200 C  CB  . THR   B 1 60  ? 23.171 -39.509 -19.875 1.00 27.52 ? 60  THR   B CB  1 
ATOM   1201 O  OG1 . THR   B 1 60  ? 23.156 -38.939 -21.206 1.00 34.50 ? 60  THR   B OG1 1 
ATOM   1202 C  CG2 . THR   B 1 60  ? 21.849 -40.206 -19.616 1.00 22.93 ? 60  THR   B CG2 1 
ATOM   1203 N  N   . GLU   B 1 61  ? 25.824 -38.521 -18.518 1.00 30.78 ? 61  GLU   B N   1 
ATOM   1204 C  CA  . GLU   B 1 61  ? 27.217 -38.106 -18.662 1.00 29.53 ? 61  GLU   B CA  1 
ATOM   1205 C  C   . GLU   B 1 61  ? 27.648 -37.974 -20.146 1.00 35.62 ? 61  GLU   B C   1 
ATOM   1206 O  O   . GLU   B 1 61  ? 28.480 -37.121 -20.477 1.00 44.99 ? 61  GLU   B O   1 
ATOM   1207 C  CB  . GLU   B 1 61  ? 28.118 -39.095 -17.895 1.00 29.19 ? 61  GLU   B CB  1 
ATOM   1208 N  N   . GLU   B 1 62  ? 27.082 -38.784 -21.041 1.00 32.54 ? 62  GLU   B N   1 
ATOM   1209 C  CA  . GLU   B 1 62  ? 27.429 -38.669 -22.470 1.00 35.45 ? 62  GLU   B CA  1 
ATOM   1210 C  C   . GLU   B 1 62  ? 26.870 -37.345 -23.006 1.00 30.97 ? 62  GLU   B C   1 
ATOM   1211 O  O   . GLU   B 1 62  ? 27.529 -36.648 -23.771 1.00 38.32 ? 62  GLU   B O   1 
ATOM   1212 C  CB  . GLU   B 1 62  ? 26.939 -39.872 -23.317 1.00 33.72 ? 62  GLU   B CB  1 
ATOM   1213 N  N   . GLU   B 1 63  ? 25.667 -36.984 -22.564 1.00 30.54 ? 63  GLU   B N   1 
ATOM   1214 C  CA  . GLU   B 1 63  ? 24.937 -35.864 -23.143 1.00 30.29 ? 63  GLU   B CA  1 
ATOM   1215 C  C   . GLU   B 1 63  ? 25.442 -34.529 -22.604 1.00 24.15 ? 63  GLU   B C   1 
ATOM   1216 O  O   . GLU   B 1 63  ? 25.388 -33.549 -23.288 1.00 22.49 ? 63  GLU   B O   1 
ATOM   1217 C  CB  . GLU   B 1 63  ? 23.446 -36.043 -22.816 1.00 30.72 ? 63  GLU   B CB  1 
ATOM   1218 C  CG  . GLU   B 1 63  ? 22.440 -35.350 -23.698 0.70 30.50 ? 63  GLU   B CG  1 
ATOM   1219 C  CD  . GLU   B 1 63  ? 21.042 -35.639 -23.193 0.70 32.14 ? 63  GLU   B CD  1 
ATOM   1220 O  OE1 . GLU   B 1 63  ? 20.677 -36.828 -23.098 0.70 39.13 ? 63  GLU   B OE1 1 
ATOM   1221 O  OE2 . GLU   B 1 63  ? 20.323 -34.697 -22.831 0.70 40.24 ? 63  GLU   B OE2 1 
ATOM   1222 N  N   . PHE   B 1 64  ? 25.981 -34.526 -21.390 1.00 24.58 ? 64  PHE   B N   1 
ATOM   1223 C  CA  . PHE   B 1 64  ? 26.209 -33.320 -20.641 1.00 23.79 ? 64  PHE   B CA  1 
ATOM   1224 C  C   . PHE   B 1 64  ? 27.657 -32.912 -20.856 1.00 14.88 ? 64  PHE   B C   1 
ATOM   1225 O  O   . PHE   B 1 64  ? 28.506 -33.200 -20.033 1.00 34.04 ? 64  PHE   B O   1 
ATOM   1226 C  CB  . PHE   B 1 64  ? 25.974 -33.612 -19.159 1.00 24.95 ? 64  PHE   B CB  1 
ATOM   1227 C  CG  . PHE   B 1 64  ? 26.118 -32.415 -18.283 1.00 27.60 ? 64  PHE   B CG  1 
ATOM   1228 C  CD1 . PHE   B 1 64  ? 25.410 -31.253 -18.568 1.00 26.07 ? 64  PHE   B CD1 1 
ATOM   1229 C  CD2 . PHE   B 1 64  ? 26.929 -32.442 -17.169 1.00 31.96 ? 64  PHE   B CD2 1 
ATOM   1230 C  CE1 . PHE   B 1 64  ? 25.496 -30.144 -17.757 1.00 28.65 ? 64  PHE   B CE1 1 
ATOM   1231 C  CE2 . PHE   B 1 64  ? 27.038 -31.326 -16.376 1.00 34.32 ? 64  PHE   B CE2 1 
ATOM   1232 C  CZ  . PHE   B 1 64  ? 26.310 -30.180 -16.670 1.00 28.09 ? 64  PHE   B CZ  1 
ATOM   1233 N  N   . VAL   B 1 65  ? 27.941 -32.233 -21.952 1.00 17.68 ? 65  VAL   B N   1 
ATOM   1234 C  CA  . VAL   B 1 65  ? 29.305 -31.880 -22.290 1.00 21.83 ? 65  VAL   B CA  1 
ATOM   1235 C  C   . VAL   B 1 65  ? 29.562 -30.521 -21.629 1.00 22.00 ? 65  VAL   B C   1 
ATOM   1236 O  O   . VAL   B 1 65  ? 28.637 -29.889 -21.137 1.00 29.05 ? 65  VAL   B O   1 
ATOM   1237 C  CB  . VAL   B 1 65  ? 29.442 -31.773 -23.809 1.00 25.16 ? 65  VAL   B CB  1 
ATOM   1238 C  CG1 . VAL   B 1 65  ? 29.331 -33.157 -24.444 1.00 24.24 ? 65  VAL   B CG1 1 
ATOM   1239 C  CG2 . VAL   B 1 65  ? 28.367 -30.851 -24.365 1.00 25.48 ? 65  VAL   B CG2 1 
ATOM   1240 N  N   . GLU   B 1 66  ? 30.820 -30.101 -21.590 1.00 21.48 ? 66  GLU   B N   1 
ATOM   1241 C  CA  . GLU   B 1 66  ? 31.159 -28.739 -21.296 1.00 26.28 ? 66  GLU   B CA  1 
ATOM   1242 C  C   . GLU   B 1 66  ? 30.374 -27.778 -22.193 1.00 23.38 ? 66  GLU   B C   1 
ATOM   1243 O  O   . GLU   B 1 66  ? 30.048 -28.107 -23.317 1.00 29.18 ? 66  GLU   B O   1 
ATOM   1244 C  CB  . GLU   B 1 66  ? 32.666 -28.516 -21.509 1.00 27.29 ? 66  GLU   B CB  1 
ATOM   1245 C  CG  . GLU   B 1 66  ? 33.501 -29.178 -20.447 1.00 23.34 ? 66  GLU   B CG  1 
ATOM   1246 C  CD  . GLU   B 1 66  ? 35.012 -28.997 -20.633 1.00 27.90 ? 66  GLU   B CD  1 
ATOM   1247 O  OE1 . GLU   B 1 66  ? 35.525 -28.697 -21.776 1.00 31.55 ? 66  GLU   B OE1 1 
ATOM   1248 O  OE2 . GLU   B 1 66  ? 35.666 -29.145 -19.581 1.00 41.88 ? 66  GLU   B OE2 1 
ATOM   1249 N  N   . GLY   B 1 67  ? 30.041 -26.599 -21.667 1.00 30.15 ? 67  GLY   B N   1 
ATOM   1250 C  CA  . GLY   B 1 67  ? 29.315 -25.593 -22.434 1.00 24.45 ? 67  GLY   B CA  1 
ATOM   1251 C  C   . GLY   B 1 67  ? 28.630 -24.642 -21.470 1.00 21.94 ? 67  GLY   B C   1 
ATOM   1252 O  O   . GLY   B 1 67  ? 28.904 -24.664 -20.265 1.00 22.42 ? 67  GLY   B O   1 
ATOM   1253 N  N   . ILE   B 1 68  ? 27.730 -23.824 -22.006 1.00 19.37 ? 68  ILE   B N   1 
ATOM   1254 C  CA  . ILE   B 1 68  ? 27.005 -22.875 -21.249 1.00 23.78 ? 68  ILE   B CA  1 
ATOM   1255 C  C   . ILE   B 1 68  ? 25.570 -23.369 -21.151 1.00 20.87 ? 68  ILE   B C   1 
ATOM   1256 O  O   . ILE   B 1 68  ? 24.927 -23.706 -22.172 1.00 22.42 ? 68  ILE   B O   1 
ATOM   1257 C  CB  . ILE   B 1 68  ? 27.043 -21.503 -21.913 1.00 26.95 ? 68  ILE   B CB  1 
ATOM   1258 C  CG1 . ILE   B 1 68  ? 28.489 -20.996 -21.926 1.00 25.52 ? 68  ILE   B CG1 1 
ATOM   1259 C  CG2 . ILE   B 1 68  ? 26.167 -20.554 -21.126 1.00 24.91 ? 68  ILE   B CG2 1 
ATOM   1260 C  CD1 . ILE   B 1 68  ? 28.735 -19.765 -22.747 1.00 28.68 ? 68  ILE   B CD1 1 
ATOM   1261 N  N   . TYR   B 1 69  ? 25.086 -23.463 -19.920 1.00 19.69 ? 69  TYR   B N   1 
ATOM   1262 C  CA  . TYR   B 1 69  ? 23.745 -23.958 -19.638 1.00 18.19 ? 69  TYR   B CA  1 
ATOM   1263 C  C   . TYR   B 1 69  ? 22.882 -22.907 -18.880 1.00 17.40 ? 69  TYR   B C   1 
ATOM   1264 O  O   . TYR   B 1 69  ? 23.398 -22.050 -18.158 1.00 18.32 ? 69  TYR   B O   1 
ATOM   1265 C  CB  . TYR   B 1 69  ? 23.903 -25.203 -18.781 1.00 16.54 ? 69  TYR   B CB  1 
ATOM   1266 C  CG  . TYR   B 1 69  ? 24.467 -26.366 -19.531 1.00 17.87 ? 69  TYR   B CG  1 
ATOM   1267 C  CD1 . TYR   B 1 69  ? 25.848 -26.566 -19.621 1.00 17.12 ? 69  TYR   B CD1 1 
ATOM   1268 C  CD2 . TYR   B 1 69  ? 23.644 -27.281 -20.096 1.00 16.42 ? 69  TYR   B CD2 1 
ATOM   1269 C  CE1 . TYR   B 1 69  ? 26.372 -27.649 -20.318 1.00 18.36 ? 69  TYR   B CE1 1 
ATOM   1270 C  CE2 . TYR   B 1 69  ? 24.131 -28.356 -20.808 1.00 18.89 ? 69  TYR   B CE2 1 
ATOM   1271 C  CZ  . TYR   B 1 69  ? 25.500 -28.526 -20.938 1.00 19.12 ? 69  TYR   B CZ  1 
ATOM   1272 O  OH  . TYR   B 1 69  ? 25.918 -29.633 -21.634 1.00 23.91 ? 69  TYR   B OH  1 
ATOM   1273 N  N   . LYS   B 1 70  ? 21.571 -23.000 -19.088 1.00 16.64 ? 70  LYS   B N   1 
ATOM   1274 C  CA  . LYS   B 1 70  ? 20.539 -22.187 -18.394 1.00 19.96 ? 70  LYS   B CA  1 
ATOM   1275 C  C   . LYS   B 1 70  ? 19.589 -23.166 -17.728 1.00 16.60 ? 70  LYS   B C   1 
ATOM   1276 O  O   . LYS   B 1 70  ? 19.003 -24.021 -18.414 1.00 21.13 ? 70  LYS   B O   1 
ATOM   1277 C  CB  . LYS   B 1 70  ? 19.800 -21.227 -19.366 1.00 21.57 ? 70  LYS   B CB  1 
ATOM   1278 C  CG  . LYS   B 1 70  ? 18.536 -20.517 -18.826 1.00 24.60 ? 70  LYS   B CG  1 
ATOM   1279 C  CD  . LYS   B 1 70  ? 17.968 -19.465 -19.780 1.00 23.64 ? 70  LYS   B CD  1 
ATOM   1280 N  N   . VAL   B 1 71  ? 19.486 -23.085 -16.405 1.00 17.61 ? 71  VAL   B N   1 
ATOM   1281 C  CA  . VAL   B 1 71  ? 18.449 -23.795 -15.675 1.00 14.63 ? 71  VAL   B CA  1 
ATOM   1282 C  C   . VAL   B 1 71  ? 17.350 -22.785 -15.357 1.00 17.37 ? 71  VAL   B C   1 
ATOM   1283 O  O   . VAL   B 1 71  ? 17.602 -21.739 -14.711 1.00 22.63 ? 71  VAL   B O   1 
ATOM   1284 C  CB  . VAL   B 1 71  ? 18.956 -24.477 -14.393 1.00 14.93 ? 71  VAL   B CB  1 
ATOM   1285 C  CG1 . VAL   B 1 71  ? 17.805 -25.129 -13.592 1.00 18.00 ? 71  VAL   B CG1 1 
ATOM   1286 C  CG2 . VAL   B 1 71  ? 20.021 -25.529 -14.705 1.00 17.25 ? 71  VAL   B CG2 1 
ATOM   1287 N  N   . GLU   B 1 72  ? 16.142 -23.071 -15.848 1.00 20.95 ? 72  GLU   B N   1 
ATOM   1288 C  CA  . GLU   B 1 72  ? 14.972 -22.198 -15.605 1.00 17.51 ? 72  GLU   B CA  1 
ATOM   1289 C  C   . GLU   B 1 72  ? 13.987 -22.903 -14.751 1.00 15.45 ? 72  GLU   B C   1 
ATOM   1290 O  O   . GLU   B 1 72  ? 13.458 -23.930 -15.149 1.00 16.69 ? 72  GLU   B O   1 
ATOM   1291 C  CB  . GLU   B 1 72  ? 14.290 -21.900 -16.958 1.00 24.07 ? 72  GLU   B CB  1 
ATOM   1292 C  CG  . GLU   B 1 72  ? 13.459 -20.653 -17.029 1.00 26.38 ? 72  GLU   B CG  1 
ATOM   1293 C  CD  . GLU   B 1 72  ? 13.277 -20.118 -18.426 0.50 27.20 ? 72  GLU   B CD  1 
ATOM   1294 O  OE1 . GLU   B 1 72  ? 12.252 -20.465 -19.043 0.50 31.01 ? 72  GLU   B OE1 1 
ATOM   1295 O  OE2 . GLU   B 1 72  ? 14.162 -19.371 -18.898 0.50 26.54 ? 72  GLU   B OE2 1 
ATOM   1296 N  N   . ILE   B 1 73  ? 13.725 -22.345 -13.586 1.00 10.53 ? 73  ILE   B N   1 
ATOM   1297 C  CA  . ILE   B 1 73  ? 12.761 -22.955 -12.636 1.00 10.94 ? 73  ILE   B CA  1 
ATOM   1298 C  C   . ILE   B 1 73  ? 11.452 -22.150 -12.672 1.00 9.53  ? 73  ILE   B C   1 
ATOM   1299 O  O   . ILE   B 1 73  ? 11.483 -20.933 -12.517 1.00 11.16 ? 73  ILE   B O   1 
ATOM   1300 C  CB  . ILE   B 1 73  ? 13.326 -22.988 -11.193 1.00 13.52 ? 73  ILE   B CB  1 
ATOM   1301 C  CG1 . ILE   B 1 73  ? 14.719 -23.681 -11.159 1.00 15.21 ? 73  ILE   B CG1 1 
ATOM   1302 C  CG2 . ILE   B 1 73  ? 12.328 -23.719 -10.270 1.00 18.31 ? 73  ILE   B CG2 1 
ATOM   1303 C  CD1 . ILE   B 1 73  ? 15.696 -23.092 -10.198 1.00 14.91 ? 73  ILE   B CD1 1 
ATOM   1304 N  N   . ASP   B 1 74  ? 10.336 -22.814 -12.893 1.00 10.56 ? 74  ASP   B N   1 
ATOM   1305 C  CA  . ASP   B 1 74  ? 9.052  -22.139 -13.040 1.00 10.80 ? 74  ASP   B CA  1 
ATOM   1306 C  C   . ASP   B 1 74  ? 8.414  -21.807 -11.687 1.00 9.56  ? 74  ASP   B C   1 
ATOM   1307 O  O   . ASP   B 1 74  ? 7.478  -22.458 -11.201 1.00 11.51 ? 74  ASP   B O   1 
ATOM   1308 C  CB  . ASP   B 1 74  ? 8.130  -22.944 -13.924 1.00 12.46 ? 74  ASP   B CB  1 
ATOM   1309 C  CG  . ASP   B 1 74  ? 6.840  -22.240 -14.193 1.00 13.59 ? 74  ASP   B CG  1 
ATOM   1310 O  OD1 . ASP   B 1 74  ? 6.714  -21.072 -13.774 1.00 14.48 ? 74  ASP   B OD1 1 
ATOM   1311 O  OD2 . ASP   B 1 74  ? 5.945  -22.884 -14.813 1.00 19.06 ? 74  ASP   B OD2 1 
ATOM   1312 N  N   . THR   B 1 75  ? 9.022  -20.836 -11.050 1.00 8.91  ? 75  THR   B N   1 
ATOM   1313 C  CA  . THR   B 1 75  ? 8.629  -20.362 -9.787  1.00 8.59  ? 75  THR   B CA  1 
ATOM   1314 C  C   . THR   B 1 75  ? 7.264  -19.651 -9.807  1.00 9.30  ? 75  THR   B C   1 
ATOM   1315 O  O   . THR   B 1 75  ? 6.519  -19.753 -8.825  1.00 9.46  ? 75  THR   B O   1 
ATOM   1316 C  CB  . THR   B 1 75  ? 9.697  -19.447 -9.206  1.00 7.92  ? 75  THR   B CB  1 
ATOM   1317 O  OG1 . THR   B 1 75  ? 9.815  -18.304 -10.012 1.00 9.90  ? 75  THR   B OG1 1 
ATOM   1318 C  CG2 . THR   B 1 75  ? 11.069 -20.215 -9.012  1.00 10.07 ? 75  THR   B CG2 1 
ATOM   1319 N  N   . LYS   B 1 76  ? 6.907  -19.045 -10.925 1.00 9.93  ? 76  LYS   B N   1 
ATOM   1320 C  CA  . LYS   B 1 76  ? 5.654  -18.318 -11.011 1.00 10.95 ? 76  LYS   B CA  1 
ATOM   1321 C  C   . LYS   B 1 76  ? 4.489  -19.305 -10.858 1.00 9.32  ? 76  LYS   B C   1 
ATOM   1322 O  O   . LYS   B 1 76  ? 3.582  -19.069 -10.048 1.00 7.71  ? 76  LYS   B O   1 
ATOM   1323 C  CB  . LYS   B 1 76  ? 5.558  -17.560 -12.335 1.00 15.00 ? 76  LYS   B CB  1 
ATOM   1324 C  CG  . LYS   B 1 76  ? 4.307  -16.735 -12.434 1.00 15.42 ? 76  LYS   B CG  1 
ATOM   1325 C  CD  . LYS   B 1 76  ? 4.299  -15.914 -13.691 1.00 21.90 ? 76  LYS   B CD  1 
ATOM   1326 C  CE  . LYS   B 1 76  ? 3.278  -14.777 -13.581 1.00 28.36 ? 76  LYS   B CE  1 
ATOM   1327 N  NZ  . LYS   B 1 76  ? 3.335  -13.965 -14.817 1.00 28.65 ? 76  LYS   B NZ  1 
ATOM   1328 N  N   . SER   B 1 77  ? 4.558  -20.432 -11.543 1.00 10.89 ? 77  SER   B N   1 
ATOM   1329 C  CA  . SER   B 1 77  ? 3.480  -21.428 -11.458 1.00 10.24 ? 77  SER   B CA  1 
ATOM   1330 C  C   . SER   B 1 77  ? 3.408  -22.035 -10.073 1.00 11.39 ? 77  SER   B C   1 
ATOM   1331 O  O   . SER   B 1 77  ? 2.332  -22.405 -9.623  1.00 12.80 ? 77  SER   B O   1 
ATOM   1332 C  CB  . SER   B 1 77  ? 3.730  -22.535 -12.423 1.00 12.90 ? 77  SER   B CB  1 
ATOM   1333 O  OG  . SER   B 1 77  ? 3.379  -22.110 -13.713 1.00 15.67 ? 77  SER   B OG  1 
ATOM   1334 N  N   . TYR   B 1 78  ? 4.575  -22.248 -9.437  1.00 9.38  ? 78  TYR   B N   1 
ATOM   1335 C  CA  . TYR   B 1 78  ? 4.629  -22.743 -8.060  1.00 10.06 ? 78  TYR   B CA  1 
ATOM   1336 C  C   . TYR   B 1 78  ? 3.833  -21.820 -7.092  1.00 10.22 ? 78  TYR   B C   1 
ATOM   1337 O  O   . TYR   B 1 78  ? 2.921  -22.273 -6.370  1.00 12.85 ? 78  TYR   B O   1 
ATOM   1338 C  CB  . TYR   B 1 78  ? 6.095  -22.874 -7.613  1.00 9.14  ? 78  TYR   B CB  1 
ATOM   1339 C  CG  . TYR   B 1 78  ? 6.271  -23.331 -6.170  1.00 9.00  ? 78  TYR   B CG  1 
ATOM   1340 C  CD1 . TYR   B 1 78  ? 6.013  -24.637 -5.805  1.00 11.18 ? 78  TYR   B CD1 1 
ATOM   1341 C  CD2 . TYR   B 1 78  ? 6.655  -22.432 -5.153  1.00 11.22 ? 78  TYR   B CD2 1 
ATOM   1342 C  CE1 . TYR   B 1 78  ? 6.165  -25.040 -4.481  1.00 11.98 ? 78  TYR   B CE1 1 
ATOM   1343 C  CE2 . TYR   B 1 78  ? 6.758  -22.830 -3.810  1.00 11.08 ? 78  TYR   B CE2 1 
ATOM   1344 C  CZ  . TYR   B 1 78  ? 6.492  -24.134 -3.493  1.00 13.31 ? 78  TYR   B CZ  1 
ATOM   1345 O  OH  . TYR   B 1 78  ? 6.589  -24.669 -2.257  1.00 14.69 ? 78  TYR   B OH  1 
ATOM   1346 N  N   . TRP   B 1 79  ? 4.164  -20.537 -7.066  1.00 8.46  ? 79  TRP   B N   1 
ATOM   1347 C  CA  . TRP   B 1 79  ? 3.546  -19.608 -6.081  1.00 8.03  ? 79  TRP   B CA  1 
ATOM   1348 C  C   . TRP   B 1 79  ? 2.022  -19.529 -6.372  1.00 10.11 ? 79  TRP   B C   1 
ATOM   1349 O  O   . TRP   B 1 79  ? 1.186  -19.468 -5.441  1.00 10.20 ? 79  TRP   B O   1 
ATOM   1350 C  CB  . TRP   B 1 79  ? 4.195  -18.234 -6.092  1.00 7.34  ? 79  TRP   B CB  1 
ATOM   1351 C  CG  . TRP   B 1 79  ? 5.615  -18.336 -5.565  1.00 7.84  ? 79  TRP   B CG  1 
ATOM   1352 C  CD1 . TRP   B 1 79  ? 6.779  -18.090 -6.241  1.00 8.53  ? 79  TRP   B CD1 1 
ATOM   1353 C  CD2 . TRP   B 1 79  ? 5.975  -18.630 -4.234  1.00 7.78  ? 79  TRP   B CD2 1 
ATOM   1354 N  NE1 . TRP   B 1 79  ? 7.864  -18.248 -5.396  1.00 8.48  ? 79  TRP   B NE1 1 
ATOM   1355 C  CE2 . TRP   B 1 79  ? 7.396  -18.611 -4.158  1.00 8.24  ? 79  TRP   B CE2 1 
ATOM   1356 C  CE3 . TRP   B 1 79  ? 5.245  -18.931 -3.088  1.00 10.14 ? 79  TRP   B CE3 1 
ATOM   1357 C  CZ2 . TRP   B 1 79  ? 8.058  -18.884 -2.982  1.00 9.59  ? 79  TRP   B CZ2 1 
ATOM   1358 C  CZ3 . TRP   B 1 79  ? 5.899  -19.275 -1.974  1.00 10.47 ? 79  TRP   B CZ3 1 
ATOM   1359 C  CH2 . TRP   B 1 79  ? 7.320  -19.198 -1.908  1.00 10.14 ? 79  TRP   B CH2 1 
ATOM   1360 N  N   . LYS   B 1 80  ? 1.703  -19.495 -7.661  1.00 10.38 ? 80  LYS   B N   1 
ATOM   1361 C  CA  . LYS   B 1 80  ? 0.316  -19.335 -8.050  1.00 11.02 ? 80  LYS   B CA  1 
ATOM   1362 C  C   . LYS   B 1 80  ? -0.545 -20.471 -7.559  1.00 10.15 ? 80  LYS   B C   1 
ATOM   1363 O  O   . LYS   B 1 80  ? -1.700 -20.268 -7.161  1.00 14.06 ? 80  LYS   B O   1 
ATOM   1364 C  CB  . LYS   B 1 80  ? 0.188  -19.070 -9.559  1.00 12.95 ? 80  LYS   B CB  1 
ATOM   1365 C  CG  . LYS   B 1 80  ? 0.686  -17.655 -9.856  1.00 15.05 ? 80  LYS   B CG  1 
ATOM   1366 C  CD  . LYS   B 1 80  ? 0.204  -17.024 -11.171 1.00 20.13 ? 80  LYS   B CD  1 
ATOM   1367 C  CE  . LYS   B 1 80  ? 0.041  -18.006 -12.310 1.00 26.28 ? 80  LYS   B CE  1 
ATOM   1368 N  N   . ALA   B 1 81  ? 0.004  -21.658 -7.603  1.00 12.04 ? 81  ALA   B N   1 
ATOM   1369 C  CA  . ALA   B 1 81  ? -0.666 -22.861 -7.115  1.00 11.84 ? 81  ALA   B CA  1 
ATOM   1370 C  C   . ALA   B 1 81  ? -0.975 -22.728 -5.611  1.00 15.37 ? 81  ALA   B C   1 
ATOM   1371 O  O   . ALA   B 1 81  ? -1.949 -23.296 -5.121  1.00 12.73 ? 81  ALA   B O   1 
ATOM   1372 C  CB  . ALA   B 1 81  ? 0.165  -24.104 -7.381  1.00 13.37 ? 81  ALA   B CB  1 
ATOM   1373 N  N   . LEU   B 1 82  ? -0.110 -22.012 -4.882  1.00 15.63 ? 82  LEU   B N   1 
ATOM   1374 C  CA  . LEU   B 1 82  ? -0.289 -21.820 -3.414  1.00 15.72 ? 82  LEU   B CA  1 
ATOM   1375 C  C   . LEU   B 1 82  ? -1.223 -20.665 -3.068  1.00 15.66 ? 82  LEU   B C   1 
ATOM   1376 O  O   . LEU   B 1 82  ? -1.517 -20.462 -1.894  1.00 19.76 ? 82  LEU   B O   1 
ATOM   1377 C  CB  . LEU   B 1 82  ? 1.063  -21.535 -2.783  1.00 17.85 ? 82  LEU   B CB  1 
ATOM   1378 C  CG  . LEU   B 1 82  ? 1.863  -22.785 -2.717  1.00 16.91 ? 82  LEU   B CG  1 
ATOM   1379 C  CD2 . LEU   B 1 82  ? 3.233  -22.381 -2.110  1.00 14.19 ? 82  LEU   B CD2 1 
ATOM   1380 N  N   . GLY   B 1 83  ? -1.592 -19.867 -4.070  1.00 10.16 ? 83  GLY   B N   1 
ATOM   1381 C  CA  . GLY   B 1 83  ? -2.431 -18.722 -3.845  1.00 10.99 ? 83  GLY   B CA  1 
ATOM   1382 C  C   . GLY   B 1 83  ? -1.672 -17.479 -3.501  1.00 12.30 ? 83  GLY   B C   1 
ATOM   1383 O  O   . GLY   B 1 83  ? -2.216 -16.515 -2.968  1.00 12.82 ? 83  GLY   B O   1 
ATOM   1384 N  N   . ILE   B 1 84  ? -0.392 -17.500 -3.820  1.00 10.30 ? 84  ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 1 84  ? 0.462  -16.370 -3.529  1.00 10.29 ? 84  ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 1 84  ? 0.923  -15.682 -4.838  1.00 11.24 ? 84  ILE   B C   1 
ATOM   1387 O  O   . ILE   B 1 84  ? 1.383  -16.316 -5.808  1.00 11.18 ? 84  ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 1 84  ? 1.694  -16.863 -2.749  1.00 11.41 ? 84  ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 1 84  ? 1.309  -17.381 -1.325  1.00 11.73 ? 84  ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 1 84  ? 2.737  -15.756 -2.675  1.00 11.50 ? 84  ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 1 84  ? 2.340  -18.347 -0.745  1.00 11.15 ? 84  ILE   B CD1 1 
ATOM   1392 N  N   . SER   B 1 85  ? 0.776  -14.367 -4.862  1.00 14.54 ? 85  SER   B N   1 
ATOM   1393 C  CA  . SER   B 1 85  ? 1.241  -13.565 -6.017  1.00 11.09 ? 85  SER   B CA  1 
ATOM   1394 C  C   . SER   B 1 85  ? 2.781  -13.407 -6.002  1.00 11.20 ? 85  SER   B C   1 
ATOM   1395 O  O   . SER   B 1 85  ? 3.306  -12.829 -5.060  1.00 11.35 ? 85  SER   B O   1 
ATOM   1396 C  CB  . SER   B 1 85  ? 0.600  -12.204 -6.008  1.00 16.25 ? 85  SER   B CB  1 
ATOM   1397 O  OG  . SER   B 1 85  ? 1.111  -11.414 -7.092  1.00 17.13 ? 85  SER   B OG  1 
ATOM   1398 N  N   . PRO   B 1 86  ? 3.469  -13.908 -7.039  1.00 10.79 ? 86  PRO   B N   1 
ATOM   1399 C  CA  . PRO   B 1 86  ? 4.948  -13.886 -7.081  1.00 9.33  ? 86  PRO   B CA  1 
ATOM   1400 C  C   . PRO   B 1 86  ? 5.467  -12.718 -7.921  1.00 10.59 ? 86  PRO   B C   1 
ATOM   1401 O  O   . PRO   B 1 86  ? 4.772  -12.237 -8.823  1.00 9.49  ? 86  PRO   B O   1 
ATOM   1402 C  CB  . PRO   B 1 86  ? 5.272  -15.180 -7.785  1.00 12.34 ? 86  PRO   B CB  1 
ATOM   1403 C  CG  . PRO   B 1 86  ? 4.169  -15.266 -8.829  1.00 14.32 ? 86  PRO   B CG  1 
ATOM   1404 C  CD  . PRO   B 1 86  ? 2.934  -14.746 -8.125  1.00 11.12 ? 86  PRO   B CD  1 
ATOM   1405 N  N   . PHE   B 1 87  ? 6.679  -12.314 -7.668  1.00 7.96  ? 87  PHE   B N   1 
ATOM   1406 C  CA  . PHE   B 1 87  ? 7.322  -11.244 -8.406  1.00 7.12  ? 87  PHE   B CA  1 
ATOM   1407 C  C   . PHE   B 1 87  ? 7.916  -11.729 -9.746  1.00 7.40  ? 87  PHE   B C   1 
ATOM   1408 O  O   . PHE   B 1 87  ? 7.737  -11.142 -10.769 1.00 8.31  ? 87  PHE   B O   1 
ATOM   1409 C  CB  . PHE   B 1 87  ? 8.449  -10.630 -7.557  1.00 7.99  ? 87  PHE   B CB  1 
ATOM   1410 C  CG  . PHE   B 1 87  ? 9.133  -9.537  -8.249  1.00 6.80  ? 87  PHE   B CG  1 
ATOM   1411 C  CD1 . PHE   B 1 87  ? 8.493  -8.320  -8.435  1.00 9.34  ? 87  PHE   B CD1 1 
ATOM   1412 C  CD2 . PHE   B 1 87  ? 10.391 -9.720  -8.728  1.00 7.74  ? 87  PHE   B CD2 1 
ATOM   1413 C  CE1 . PHE   B 1 87  ? 9.090  -7.311  -9.130  1.00 8.91  ? 87  PHE   B CE1 1 
ATOM   1414 C  CE2 . PHE   B 1 87  ? 11.016 -8.726  -9.453  1.00 8.54  ? 87  PHE   B CE2 1 
ATOM   1415 C  CZ  . PHE   B 1 87  ? 10.368 -7.520  -9.626  1.00 9.41  ? 87  PHE   B CZ  1 
ATOM   1416 N  N   . HIS   B 1 88  ? 8.657  -12.816 -9.678  1.00 7.05  ? 88  HIS   B N   1 
ATOM   1417 C  CA  . HIS   B 1 88  ? 9.420  -13.257 -10.799 1.00 7.73  ? 88  HIS   B CA  1 
ATOM   1418 C  C   . HIS   B 1 88  ? 8.705  -14.174 -11.757 1.00 7.93  ? 88  HIS   B C   1 
ATOM   1419 O  O   . HIS   B 1 88  ? 7.756  -14.935 -11.388 1.00 9.82  ? 88  HIS   B O   1 
ATOM   1420 C  CB  . HIS   B 1 88  ? 10.731 -13.944 -10.363 1.00 8.05  ? 88  HIS   B CB  1 
ATOM   1421 C  CG  . HIS   B 1 88  ? 11.600 -13.166 -9.464  1.00 7.77  ? 88  HIS   B CG  1 
ATOM   1422 N  ND1 . HIS   B 1 88  ? 11.545 -13.241 -8.097  1.00 9.77  ? 88  HIS   B ND1 1 
ATOM   1423 C  CD2 . HIS   B 1 88  ? 12.613 -12.338 -9.751  1.00 7.39  ? 88  HIS   B CD2 1 
ATOM   1424 C  CE1 . HIS   B 1 88  ? 12.457 -12.449 -7.580  1.00 9.75  ? 88  HIS   B CE1 1 
ATOM   1425 N  NE2 . HIS   B 1 88  ? 13.110 -11.870 -8.582  1.00 11.35 ? 88  HIS   B NE2 1 
ATOM   1426 N  N   . GLU   B 1 89  ? 9.124  -14.172 -13.021 1.00 7.90  ? 89  GLU   B N   1 
ATOM   1427 C  CA  . GLU   B 1 89  ? 8.526  -15.140 -13.975 1.00 10.21 ? 89  GLU   B CA  1 
ATOM   1428 C  C   . GLU   B 1 89  ? 9.086  -16.508 -13.738 1.00 13.03 ? 89  GLU   B C   1 
ATOM   1429 O  O   . GLU   B 1 89  ? 8.413  -17.498 -13.882 1.00 15.01 ? 89  GLU   B O   1 
ATOM   1430 C  CB  . GLU   B 1 89  ? 8.870  -14.747 -15.401 1.00 12.40 ? 89  GLU   B CB  1 
ATOM   1431 C  CG  . GLU   B 1 89  ? 8.124  -13.551 -15.877 1.00 12.67 ? 89  GLU   B CG  1 
ATOM   1432 C  CD  . GLU   B 1 89  ? 6.614  -13.833 -15.965 1.00 14.17 ? 89  GLU   B CD  1 
ATOM   1433 O  OE1 . GLU   B 1 89  ? 6.173  -14.691 -16.771 1.00 20.66 ? 89  GLU   B OE1 1 
ATOM   1434 O  OE2 . GLU   B 1 89  ? 5.849  -13.195 -15.240 1.00 19.86 ? 89  GLU   B OE2 1 
ATOM   1435 N  N   . HIS   B 1 90  ? 10.346 -16.550 -13.369 1.00 15.29 ? 90  HIS   B N   1 
ATOM   1436 C  CA  . HIS   B 1 90  ? 11.037 -17.785 -13.077 1.00 15.71 ? 90  HIS   B CA  1 
ATOM   1437 C  C   . HIS   B 1 90  ? 12.293 -17.431 -12.254 1.00 18.48 ? 90  HIS   B C   1 
ATOM   1438 O  O   . HIS   B 1 90  ? 12.606 -16.276 -12.093 1.00 22.47 ? 90  HIS   B O   1 
ATOM   1439 C  CB  . HIS   B 1 90  ? 11.425 -18.552 -14.369 1.00 20.77 ? 90  HIS   B CB  1 
ATOM   1440 C  CG  . HIS   B 1 90  ? 11.736 -17.702 -15.567 1.00 24.87 ? 90  HIS   B CG  1 
ATOM   1441 N  ND1 . HIS   B 1 90  ? 12.965 -17.112 -15.761 0.50 25.81 ? 90  HIS   B ND1 1 
ATOM   1442 C  CD2 . HIS   B 1 90  ? 11.012 -17.434 -16.687 0.50 27.60 ? 90  HIS   B CD2 1 
ATOM   1443 C  CE1 . HIS   B 1 90  ? 12.967 -16.469 -16.915 0.50 25.62 ? 90  HIS   B CE1 1 
ATOM   1444 N  NE2 . HIS   B 1 90  ? 11.796 -16.655 -17.499 0.50 26.97 ? 90  HIS   B NE2 1 
ATOM   1445 N  N   . ALA   B 1 91  ? 12.948 -18.445 -11.686 1.00 17.36 ? 91  ALA   B N   1 
ATOM   1446 C  CA  . ALA   B 1 91  ? 14.331 -18.360 -11.281 1.00 18.48 ? 91  ALA   B CA  1 
ATOM   1447 C  C   . ALA   B 1 91  ? 15.211 -19.008 -12.359 1.00 21.01 ? 91  ALA   B C   1 
ATOM   1448 O  O   . ALA   B 1 91  ? 15.070 -20.213 -12.594 1.00 24.15 ? 91  ALA   B O   1 
ATOM   1449 C  CB  . ALA   B 1 91  ? 14.489 -19.039 -9.945  1.00 25.25 ? 91  ALA   B CB  1 
ATOM   1450 N  N   . GLU   B 1 92  ? 16.029 -18.177 -13.054 1.00 23.95 ? 92  GLU   B N   1 
ATOM   1451 C  CA  . GLU   B 1 92  ? 16.854 -18.579 -14.211 1.00 21.11 ? 92  GLU   B CA  1 
ATOM   1452 C  C   . GLU   B 1 92  ? 18.300 -18.543 -13.859 1.00 29.12 ? 92  GLU   B C   1 
ATOM   1453 O  O   . GLU   B 1 92  ? 18.779 -17.572 -13.256 1.00 31.17 ? 92  GLU   B O   1 
ATOM   1454 C  CB  . GLU   B 1 92  ? 16.639 -17.708 -15.478 1.00 31.67 ? 92  GLU   B CB  1 
ATOM   1455 C  CG  . GLU   B 1 92  ? 15.869 -16.388 -15.371 0.50 27.48 ? 92  GLU   B CG  1 
ATOM   1456 C  CD  . GLU   B 1 92  ? 14.372 -16.538 -15.311 0.50 31.93 ? 92  GLU   B CD  1 
ATOM   1457 O  OE1 . GLU   B 1 92  ? 13.708 -16.580 -16.370 0.50 29.35 ? 92  GLU   B OE1 1 
ATOM   1458 O  OE2 . GLU   B 1 92  ? 13.853 -16.583 -14.179 0.50 31.74 ? 92  GLU   B OE2 1 
ATOM   1459 N  N   . VAL   B 1 93  ? 19.033 -19.572 -14.276 1.00 21.73 ? 93  VAL   B N   1 
ATOM   1460 C  CA  . VAL   B 1 93  ? 20.356 -19.718 -13.747 1.00 19.20 ? 93  VAL   B CA  1 
ATOM   1461 C  C   . VAL   B 1 93  ? 21.310 -20.174 -14.838 1.00 16.63 ? 93  VAL   B C   1 
ATOM   1462 O  O   . VAL   B 1 93  ? 21.135 -21.234 -15.382 1.00 19.59 ? 93  VAL   B O   1 
ATOM   1463 C  CB  . VAL   B 1 93  ? 20.280 -20.633 -12.517 1.00 18.13 ? 93  VAL   B CB  1 
ATOM   1464 C  CG1 . VAL   B 1 93  ? 21.678 -21.004 -11.981 1.00 18.91 ? 93  VAL   B CG1 1 
ATOM   1465 C  CG2 . VAL   B 1 93  ? 19.489 -19.908 -11.447 1.00 23.00 ? 93  VAL   B CG2 1 
ATOM   1466 N  N   . VAL   B 1 94  ? 22.294 -19.324 -15.149 1.00 15.83 ? 94  VAL   B N   1 
ATOM   1467 C  CA  . VAL   B 1 94  ? 23.092 -19.467 -16.402 1.00 17.83 ? 94  VAL   B CA  1 
ATOM   1468 C  C   . VAL   B 1 94  ? 24.574 -19.594 -16.032 1.00 15.61 ? 94  VAL   B C   1 
ATOM   1469 O  O   . VAL   B 1 94  ? 25.096 -18.797 -15.282 1.00 16.92 ? 94  VAL   B O   1 
ATOM   1470 C  CB  . VAL   B 1 94  ? 22.814 -18.281 -17.350 1.00 21.54 ? 94  VAL   B CB  1 
ATOM   1471 C  CG1 . VAL   B 1 94  ? 23.570 -18.433 -18.665 1.00 21.01 ? 94  VAL   B CG1 1 
ATOM   1472 C  CG2 . VAL   B 1 94  ? 21.311 -18.147 -17.630 1.00 23.71 ? 94  VAL   B CG2 1 
ATOM   1473 N  N   . PHE   B 1 95  ? 25.211 -20.682 -16.466 1.00 17.45 ? 95  PHE   B N   1 
ATOM   1474 C  CA  . PHE   B 1 95  ? 26.562 -21.016 -15.980 1.00 16.27 ? 95  PHE   B CA  1 
ATOM   1475 C  C   . PHE   B 1 95  ? 27.340 -21.805 -17.010 1.00 19.78 ? 95  PHE   B C   1 
ATOM   1476 O  O   . PHE   B 1 95  ? 26.761 -22.381 -17.910 1.00 19.44 ? 95  PHE   B O   1 
ATOM   1477 C  CB  . PHE   B 1 95  ? 26.460 -21.818 -14.683 1.00 14.21 ? 95  PHE   B CB  1 
ATOM   1478 C  CG  . PHE   B 1 95  ? 25.875 -23.207 -14.868 1.00 17.01 ? 95  PHE   B CG  1 
ATOM   1479 C  CD1 . PHE   B 1 95  ? 24.521 -23.408 -14.757 1.00 23.01 ? 95  PHE   B CD1 1 
ATOM   1480 C  CD2 . PHE   B 1 95  ? 26.692 -24.321 -15.115 1.00 20.70 ? 95  PHE   B CD2 1 
ATOM   1481 C  CE1 . PHE   B 1 95  ? 23.961 -24.673 -14.920 1.00 26.30 ? 95  PHE   B CE1 1 
ATOM   1482 C  CE2 . PHE   B 1 95  ? 26.151 -25.586 -15.263 1.00 17.89 ? 95  PHE   B CE2 1 
ATOM   1483 C  CZ  . PHE   B 1 95  ? 24.763 -25.771 -15.162 1.00 20.49 ? 95  PHE   B CZ  1 
ATOM   1484 N  N   . THR   B 1 96  ? 28.684 -21.729 -16.905 1.00 21.71 ? 96  THR   B N   1 
ATOM   1485 C  CA  . THR   B 1 96  ? 29.583 -22.512 -17.730 1.00 22.10 ? 96  THR   B CA  1 
ATOM   1486 C  C   . THR   B 1 96  ? 29.954 -23.787 -17.007 1.00 28.43 ? 96  THR   B C   1 
ATOM   1487 O  O   . THR   B 1 96  ? 30.352 -23.754 -15.847 1.00 29.62 ? 96  THR   B O   1 
ATOM   1488 C  CB  . THR   B 1 96  ? 30.867 -21.727 -18.022 1.00 31.76 ? 96  THR   B CB  1 
ATOM   1489 O  OG1 . THR   B 1 96  ? 30.559 -20.693 -18.967 1.00 33.14 ? 96  THR   B OG1 1 
ATOM   1490 N  N   . ALA   B 1 97  ? 29.797 -24.907 -17.714 1.00 29.23 ? 97  ALA   B N   1 
ATOM   1491 C  CA  . ALA   B 1 97  ? 30.185 -26.232 -17.250 1.00 25.55 ? 97  ALA   B CA  1 
ATOM   1492 C  C   . ALA   B 1 97  ? 31.605 -26.518 -17.675 1.00 29.59 ? 97  ALA   B C   1 
ATOM   1493 O  O   . ALA   B 1 97  ? 31.858 -26.708 -18.862 1.00 35.52 ? 97  ALA   B O   1 
ATOM   1494 C  CB  . ALA   B 1 97  ? 29.271 -27.295 -17.824 1.00 36.80 ? 97  ALA   B CB  1 
ATOM   1495 N  N   . ASN   B 1 98  ? 32.520 -26.534 -16.709 0.50 21.45 ? 98  ASN   B N   1 
ATOM   1496 C  CA  . ASN   B 1 98  ? 33.889 -26.921 -16.966 0.50 23.90 ? 98  ASN   B CA  1 
ATOM   1497 C  C   . ASN   B 1 98  ? 34.585 -27.366 -15.698 0.50 23.53 ? 98  ASN   B C   1 
ATOM   1498 O  O   . ASN   B 1 98  ? 34.990 -26.531 -14.897 0.50 30.91 ? 98  ASN   B O   1 
ATOM   1499 C  CB  . ASN   B 1 98  ? 34.663 -25.773 -17.607 0.50 25.68 ? 98  ASN   B CB  1 
ATOM   1500 C  CG  . ASN   B 1 98  ? 36.098 -26.152 -17.868 0.50 26.36 ? 98  ASN   B CG  1 
ATOM   1501 O  OD1 . ASN   B 1 98  ? 36.823 -26.539 -16.947 0.50 30.31 ? 98  ASN   B OD1 1 
ATOM   1502 N  ND2 . ASN   B 1 98  ? 36.503 -26.105 -19.127 0.50 31.45 ? 98  ASN   B ND2 1 
ATOM   1503 N  N   . ARG   B 1 104 ? 29.531 -33.627 -11.818 1.00 40.43 ? 104 ARG   B N   1 
ATOM   1504 C  CA  . ARG   B 1 104 ? 28.666 -33.683 -10.646 1.00 26.45 ? 104 ARG   B CA  1 
ATOM   1505 C  C   . ARG   B 1 104 ? 28.186 -32.299 -10.168 1.00 25.43 ? 104 ARG   B C   1 
ATOM   1506 O  O   . ARG   B 1 104 ? 28.805 -31.705 -9.286  1.00 27.69 ? 104 ARG   B O   1 
ATOM   1507 C  CB  . ARG   B 1 104 ? 29.449 -34.331 -9.512  1.00 40.20 ? 104 ARG   B CB  1 
ATOM   1508 N  N   . TYR   B 1 105 ? 27.082 -31.791 -10.723 1.00 22.66 ? 105 TYR   B N   1 
ATOM   1509 C  CA  . TYR   B 1 105 ? 26.622 -30.406 -10.474 1.00 17.60 ? 105 TYR   B CA  1 
ATOM   1510 C  C   . TYR   B 1 105 ? 25.296 -30.500 -9.805  1.00 18.12 ? 105 TYR   B C   1 
ATOM   1511 O  O   . TYR   B 1 105 ? 24.392 -31.204 -10.293 1.00 23.81 ? 105 TYR   B O   1 
ATOM   1512 C  CB  . TYR   B 1 105 ? 26.415 -29.586 -11.779 1.00 20.55 ? 105 TYR   B CB  1 
ATOM   1513 C  CG  . TYR   B 1 105 ? 27.688 -29.258 -12.522 1.00 19.30 ? 105 TYR   B CG  1 
ATOM   1514 C  CD1 . TYR   B 1 105 ? 28.398 -30.243 -13.185 1.00 20.48 ? 105 TYR   B CD1 1 
ATOM   1515 C  CD2 . TYR   B 1 105 ? 28.200 -27.968 -12.498 1.00 25.62 ? 105 TYR   B CD2 1 
ATOM   1516 C  CE1 . TYR   B 1 105 ? 29.578 -29.926 -13.865 1.00 22.12 ? 105 TYR   B CE1 1 
ATOM   1517 C  CE2 . TYR   B 1 105 ? 29.371 -27.652 -13.140 1.00 29.21 ? 105 TYR   B CE2 1 
ATOM   1518 C  CZ  . TYR   B 1 105 ? 30.055 -28.612 -13.821 1.00 21.65 ? 105 TYR   B CZ  1 
ATOM   1519 O  OH  . TYR   B 1 105 ? 31.233 -28.250 -14.448 1.00 32.85 ? 105 TYR   B OH  1 
ATOM   1520 N  N   . THR   B 1 106 ? 25.163 -29.783 -8.707  1.00 18.33 ? 106 THR   B N   1 
ATOM   1521 C  CA  . THR   B 1 106 ? 23.850 -29.556 -8.097  1.00 17.66 ? 106 THR   B CA  1 
ATOM   1522 C  C   . THR   B 1 106 ? 23.554 -28.080 -8.149  1.00 13.47 ? 106 THR   B C   1 
ATOM   1523 O  O   . THR   B 1 106 ? 24.342 -27.262 -7.721  1.00 13.60 ? 106 THR   B O   1 
ATOM   1524 C  CB  . THR   B 1 106 ? 23.869 -30.014 -6.638  1.00 18.21 ? 106 THR   B CB  1 
ATOM   1525 O  OG1 . THR   B 1 106 ? 24.172 -31.407 -6.599  1.00 22.74 ? 106 THR   B OG1 1 
ATOM   1526 C  CG2 . THR   B 1 106 ? 22.537 -29.711 -5.909  1.00 21.92 ? 106 THR   B CG2 1 
ATOM   1527 N  N   . ILE   B 1 107 ? 22.403 -27.758 -8.689  1.00 16.97 ? 107 ILE   B N   1 
ATOM   1528 C  CA  . ILE   B 1 107 ? 21.903 -26.415 -8.669  1.00 16.25 ? 107 ILE   B CA  1 
ATOM   1529 C  C   . ILE   B 1 107 ? 20.821 -26.392 -7.609  1.00 13.85 ? 107 ILE   B C   1 
ATOM   1530 O  O   . ILE   B 1 107 ? 19.800 -27.126 -7.746  1.00 19.24 ? 107 ILE   B O   1 
ATOM   1531 C  CB  . ILE   B 1 107 ? 21.294 -26.013 -10.058 1.00 15.73 ? 107 ILE   B CB  1 
ATOM   1532 C  CG1 . ILE   B 1 107 ? 22.318 -26.088 -11.226 1.00 17.34 ? 107 ILE   B CG1 1 
ATOM   1533 C  CG2 . ILE   B 1 107 ? 20.625 -24.668 -10.033 1.00 19.27 ? 107 ILE   B CG2 1 
ATOM   1534 C  CD1 . ILE   B 1 107 ? 23.651 -25.438 -10.999 1.00 17.41 ? 107 ILE   B CD1 1 
ATOM   1535 N  N   . ALA   B 1 108 ? 21.018 -25.537 -6.595  1.00 11.50 ? 108 ALA   B N   1 
ATOM   1536 C  CA  . ALA   B 1 108 ? 20.126 -25.375 -5.490  1.00 11.85 ? 108 ALA   B CA  1 
ATOM   1537 C  C   . ALA   B 1 108 ? 19.465 -24.048 -5.604  1.00 11.18 ? 108 ALA   B C   1 
ATOM   1538 O  O   . ALA   B 1 108 ? 20.092 -23.018 -5.879  1.00 11.87 ? 108 ALA   B O   1 
ATOM   1539 C  CB  . ALA   B 1 108 ? 20.900 -25.444 -4.172  1.00 15.16 ? 108 ALA   B CB  1 
ATOM   1540 N  N   . ALA   B 1 109 ? 18.161 -24.012 -5.295  1.00 12.58 ? 109 ALA   B N   1 
ATOM   1541 C  CA  . ALA   B 1 109 ? 17.435 -22.768 -5.365  1.00 10.24 ? 109 ALA   B CA  1 
ATOM   1542 C  C   . ALA   B 1 109 ? 16.509 -22.632 -4.183  1.00 9.29  ? 109 ALA   B C   1 
ATOM   1543 O  O   . ALA   B 1 109 ? 15.832 -23.576 -3.812  1.00 13.44 ? 109 ALA   B O   1 
ATOM   1544 C  CB  . ALA   B 1 109 ? 16.609 -22.681 -6.648  1.00 14.34 ? 109 ALA   B CB  1 
ATOM   1545 N  N   . LEU   B 1 110 ? 16.515 -21.462 -3.618  1.00 7.55  ? 110 LEU   B N   1 
ATOM   1546 C  CA  . LEU   B 1 110 ? 15.755 -21.160 -2.389  1.00 7.25  ? 110 LEU   B CA  1 
ATOM   1547 C  C   . LEU   B 1 110 ? 14.783 -20.024 -2.696  1.00 7.19  ? 110 LEU   B C   1 
ATOM   1548 O  O   . LEU   B 1 110 ? 15.162 -18.944 -3.087  1.00 7.46  ? 110 LEU   B O   1 
ATOM   1549 C  CB  . LEU   B 1 110 ? 16.684 -20.797 -1.242  1.00 8.75  ? 110 LEU   B CB  1 
ATOM   1550 C  CG  . LEU   B 1 110 ? 16.026 -20.352 0.047   1.00 9.02  ? 110 LEU   B CG  1 
ATOM   1551 C  CD1 . LEU   B 1 110 ? 15.158 -21.481 0.664   1.00 9.14  ? 110 LEU   B CD1 1 
ATOM   1552 C  CD2 . LEU   B 1 110 ? 17.078 -19.846 1.045   1.00 10.85 ? 110 LEU   B CD2 1 
ATOM   1553 N  N   . LEU   B 1 111 ? 13.456 -20.302 -2.576  1.00 7.92  ? 111 LEU   B N   1 
ATOM   1554 C  CA  . LEU   B 1 111 ? 12.455 -19.426 -3.135  1.00 6.36  ? 111 LEU   B CA  1 
ATOM   1555 C  C   . LEU   B 1 111 ? 11.640 -18.658 -2.099  1.00 5.27  ? 111 LEU   B C   1 
ATOM   1556 O  O   . LEU   B 1 111 ? 11.179 -19.237 -1.171  1.00 6.58  ? 111 LEU   B O   1 
ATOM   1557 C  CB  . LEU   B 1 111 ? 11.452 -20.303 -3.895  1.00 7.09  ? 111 LEU   B CB  1 
ATOM   1558 C  CG  . LEU   B 1 111 ? 12.004 -21.248 -4.972  1.00 7.85  ? 111 LEU   B CG  1 
ATOM   1559 C  CD1 . LEU   B 1 111 ? 10.863 -21.930 -5.760  1.00 9.34  ? 111 LEU   B CD1 1 
ATOM   1560 C  CD2 . LEU   B 1 111 ? 12.962 -20.495 -5.968  1.00 9.00  ? 111 LEU   B CD2 1 
ATOM   1561 N  N   . SER   B 1 112 ? 11.435 -17.384 -2.336  1.00 5.40  ? 112 SER   B N   1 
ATOM   1562 C  CA  . SER   B 1 112 ? 10.407 -16.560 -1.663  1.00 6.09  ? 112 SER   B CA  1 
ATOM   1563 C  C   . SER   B 1 112 ? 9.614  -15.770 -2.704  1.00 7.14  ? 112 SER   B C   1 
ATOM   1564 O  O   . SER   B 1 112 ? 9.959  -15.687 -3.857  1.00 6.62  ? 112 SER   B O   1 
ATOM   1565 C  CB  . SER   B 1 112 ? 11.082 -15.543 -0.738  1.00 8.76  ? 112 SER   B CB  1 
ATOM   1566 O  OG  . SER   B 1 112 ? 11.837 -16.211 0.214   1.00 10.83 ? 112 SER   B OG  1 
ATOM   1567 N  N   . PRO   B 1 113 ? 8.433  -15.202 -2.293  1.00 7.22  ? 113 PRO   B N   1 
ATOM   1568 C  CA  . PRO   B 1 113 ? 7.629  -14.626 -3.374  1.00 6.93  ? 113 PRO   B CA  1 
ATOM   1569 C  C   . PRO   B 1 113 ? 8.263  -13.465 -4.177  1.00 6.08  ? 113 PRO   B C   1 
ATOM   1570 O  O   . PRO   B 1 113 ? 8.028  -13.348 -5.410  1.00 5.87  ? 113 PRO   B O   1 
ATOM   1571 C  CB  . PRO   B 1 113 ? 6.342  -14.164 -2.603  1.00 6.85  ? 113 PRO   B CB  1 
ATOM   1572 C  CG  . PRO   B 1 113 ? 6.282  -15.216 -1.578  1.00 6.14  ? 113 PRO   B CG  1 
ATOM   1573 C  CD  . PRO   B 1 113 ? 7.687  -15.443 -1.079  1.00 7.01  ? 113 PRO   B CD  1 
ATOM   1574 N  N   . TYR   B 1 114 ? 9.158  -12.682 -3.516  1.00 6.49  ? 114 TYR   B N   1 
ATOM   1575 C  CA  . TYR   B 1 114 ? 9.825  -11.549 -4.135  1.00 6.17  ? 114 TYR   B CA  1 
ATOM   1576 C  C   . TYR   B 1 114 ? 11.338 -11.759 -4.196  1.00 7.08  ? 114 TYR   B C   1 
ATOM   1577 O  O   . TYR   B 1 114 ? 11.998 -10.810 -4.499  1.00 8.30  ? 114 TYR   B O   1 
ATOM   1578 C  CB  . TYR   B 1 114 ? 9.488  -10.216 -3.446  1.00 5.63  ? 114 TYR   B CB  1 
ATOM   1579 C  CG  . TYR   B 1 114 ? 8.093  -9.706  -3.732  1.00 6.46  ? 114 TYR   B CG  1 
ATOM   1580 C  CD1 . TYR   B 1 114 ? 6.982  -10.241 -3.050  1.00 8.83  ? 114 TYR   B CD1 1 
ATOM   1581 C  CD2 . TYR   B 1 114 ? 7.871  -8.707  -4.655  1.00 5.55  ? 114 TYR   B CD2 1 
ATOM   1582 C  CE1 . TYR   B 1 114 ? 5.720  -9.784  -3.320  1.00 9.95  ? 114 TYR   B CE1 1 
ATOM   1583 C  CE2 . TYR   B 1 114 ? 6.573  -8.323  -4.980  1.00 10.09 ? 114 TYR   B CE2 1 
ATOM   1584 C  CZ  . TYR   B 1 114 ? 5.540  -8.862  -4.294  1.00 10.33 ? 114 TYR   B CZ  1 
ATOM   1585 O  OH  . TYR   B 1 114 ? 4.250  -8.451  -4.540  1.00 14.39 ? 114 TYR   B OH  1 
ATOM   1586 N  N   . SER   B 1 115 ? 11.827 -12.969 -3.940  1.00 5.86  ? 115 SER   B N   1 
ATOM   1587 C  CA  . SER   B 1 115 ? 13.286 -13.205 -3.910  1.00 4.62  ? 115 SER   B CA  1 
ATOM   1588 C  C   . SER   B 1 115 ? 13.634 -14.648 -4.227  1.00 6.65  ? 115 SER   B C   1 
ATOM   1589 O  O   . SER   B 1 115 ? 12.822 -15.554 -4.033  1.00 7.35  ? 115 SER   B O   1 
ATOM   1590 C  CB  . SER   B 1 115 ? 13.757 -12.855 -2.512  1.00 5.55  ? 115 SER   B CB  1 
ATOM   1591 O  OG  . SER   B 1 115 ? 15.145 -13.088 -2.323  1.00 11.20 ? 115 SER   B OG  1 
ATOM   1592 N  N   . TYR   B 1 116 ? 14.874 -14.861 -4.719  1.00 5.07  ? 116 TYR   B N   1 
ATOM   1593 C  CA  . TYR   B 1 116 ? 15.381 -16.162 -4.767  1.00 6.25  ? 116 TYR   B CA  1 
ATOM   1594 C  C   . TYR   B 1 116 ? 16.892 -16.085 -4.667  1.00 6.87  ? 116 TYR   B C   1 
ATOM   1595 O  O   . TYR   B 1 116 ? 17.499 -15.058 -5.009  1.00 7.10  ? 116 TYR   B O   1 
ATOM   1596 C  CB  . TYR   B 1 116 ? 14.961 -16.949 -6.039  1.00 6.95  ? 116 TYR   B CB  1 
ATOM   1597 C  CG  . TYR   B 1 116 ? 15.502 -16.432 -7.321  1.00 8.94  ? 116 TYR   B CG  1 
ATOM   1598 C  CD1 . TYR   B 1 116 ? 16.737 -16.857 -7.810  1.00 11.77 ? 116 TYR   B CD1 1 
ATOM   1599 C  CD2 . TYR   B 1 116 ? 14.773 -15.470 -8.053  1.00 10.97 ? 116 TYR   B CD2 1 
ATOM   1600 C  CE1 . TYR   B 1 116 ? 17.241 -16.325 -8.985  1.00 12.53 ? 116 TYR   B CE1 1 
ATOM   1601 C  CE2 . TYR   B 1 116 ? 15.225 -14.997 -9.243  1.00 15.35 ? 116 TYR   B CE2 1 
ATOM   1602 C  CZ  . TYR   B 1 116 ? 16.449 -15.406 -9.696  1.00 13.79 ? 116 TYR   B CZ  1 
ATOM   1603 O  OH  . TYR   B 1 116 ? 16.863 -14.866 -10.880 1.00 27.40 ? 116 TYR   B OH  1 
ATOM   1604 N  N   . SER   B 1 117 ? 17.423 -17.141 -4.122  1.00 7.52  ? 117 SER   B N   1 
ATOM   1605 C  CA  A SER   B 1 117 ? 18.853 -17.377 -4.221  0.50 8.84  ? 117 SER   B CA  1 
ATOM   1606 C  CA  B SER   B 1 117 ? 18.862 -17.417 -4.092  0.50 8.92  ? 117 SER   B CA  1 
ATOM   1607 C  C   . SER   B 1 117 ? 19.151 -18.731 -4.810  1.00 7.83  ? 117 SER   B C   1 
ATOM   1608 O  O   . SER   B 1 117 ? 18.411 -19.720 -4.743  1.00 8.91  ? 117 SER   B O   1 
ATOM   1609 C  CB  A SER   B 1 117 ? 19.500 -17.246 -2.859  0.50 11.27 ? 117 SER   B CB  1 
ATOM   1610 C  CB  B SER   B 1 117 ? 19.306 -17.465 -2.612  0.50 11.72 ? 117 SER   B CB  1 
ATOM   1611 O  OG  A SER   B 1 117 ? 19.100 -18.313 -2.058  0.50 13.40 ? 117 SER   B OG  1 
ATOM   1612 O  OG  B SER   B 1 117 ? 20.662 -17.874 -2.410  0.50 14.86 ? 117 SER   B OG  1 
ATOM   1613 N  N   . THR   B 1 118 ? 20.310 -18.744 -5.442  1.00 10.32 ? 118 THR   B N   1 
ATOM   1614 C  CA  . THR   B 1 118 ? 20.711 -19.941 -6.077  1.00 8.58  ? 118 THR   B CA  1 
ATOM   1615 C  C   . THR   B 1 118 ? 22.199 -20.144 -5.940  1.00 9.95  ? 118 THR   B C   1 
ATOM   1616 O  O   . THR   B 1 118 ? 22.968 -19.187 -5.903  1.00 13.27 ? 118 THR   B O   1 
ATOM   1617 C  CB  . THR   B 1 118 ? 20.295 -19.988 -7.555  1.00 11.09 ? 118 THR   B CB  1 
ATOM   1618 O  OG1 . THR   B 1 118 ? 20.719 -21.245 -8.067  1.00 16.87 ? 118 THR   B OG1 1 
ATOM   1619 C  CG2 . THR   B 1 118 ? 20.853 -18.807 -8.399  1.00 10.03 ? 118 THR   B CG2 1 
ATOM   1620 N  N   . THR   B 1 119 ? 22.583 -21.384 -5.813  1.00 10.04 ? 119 THR   B N   1 
ATOM   1621 C  CA  . THR   B 1 119 ? 24.063 -21.716 -5.735  1.00 9.55  ? 119 THR   B CA  1 
ATOM   1622 C  C   . THR   B 1 119 ? 24.314 -22.972 -6.544  1.00 11.25 ? 119 THR   B C   1 
ATOM   1623 O  O   . THR   B 1 119 ? 23.388 -23.749 -6.893  1.00 12.80 ? 119 THR   B O   1 
ATOM   1624 C  CB  . THR   B 1 119 ? 24.567 -21.960 -4.255  1.00 11.25 ? 119 THR   B CB  1 
ATOM   1625 O  OG1 . THR   B 1 119 ? 26.015 -21.888 -4.189  1.00 13.88 ? 119 THR   B OG1 1 
ATOM   1626 C  CG2 . THR   B 1 119 ? 24.161 -23.277 -3.728  1.00 13.07 ? 119 THR   B CG2 1 
ATOM   1627 N  N   . ALA   B 1 120 ? 25.590 -23.238 -6.792  1.00 10.84 ? 120 ALA   B N   1 
ATOM   1628 C  CA  . ALA   B 1 120 ? 26.007 -24.440 -7.500  1.00 14.38 ? 120 ALA   B CA  1 
ATOM   1629 C  C   . ALA   B 1 120 ? 26.986 -25.179 -6.619  1.00 12.88 ? 120 ALA   B C   1 
ATOM   1630 O  O   . ALA   B 1 120 ? 27.849 -24.554 -5.947  1.00 14.26 ? 120 ALA   B O   1 
ATOM   1631 C  CB  . ALA   B 1 120 ? 26.641 -24.098 -8.830  1.00 16.55 ? 120 ALA   B CB  1 
ATOM   1632 N  N   . VAL   B 1 121 ? 26.834 -26.488 -6.601  1.00 15.54 ? 121 VAL   B N   1 
ATOM   1633 C  CA  . VAL   B 1 121 ? 27.818 -27.319 -5.907  1.00 16.38 ? 121 VAL   B CA  1 
ATOM   1634 C  C   . VAL   B 1 121 ? 28.427 -28.229 -6.946  1.00 20.13 ? 121 VAL   B C   1 
ATOM   1635 O  O   . VAL   B 1 121 ? 27.683 -28.941 -7.602  1.00 21.31 ? 121 VAL   B O   1 
ATOM   1636 C  CB  . VAL   B 1 121 ? 27.147 -28.161 -4.809  1.00 21.10 ? 121 VAL   B CB  1 
ATOM   1637 C  CG1 . VAL   B 1 121 ? 28.249 -28.915 -4.123  1.00 25.78 ? 121 VAL   B CG1 1 
ATOM   1638 C  CG2 . VAL   B 1 121 ? 26.362 -27.254 -3.850  1.00 19.26 ? 121 VAL   B CG2 1 
ATOM   1639 N  N   . VAL   B 1 122 ? 29.766 -28.209 -7.092  1.00 18.06 ? 122 VAL   B N   1 
ATOM   1640 C  CA  . VAL   B 1 122 ? 30.380 -28.825 -8.238  1.00 18.84 ? 122 VAL   B CA  1 
ATOM   1641 C  C   . VAL   B 1 122 ? 31.511 -29.735 -7.857  1.00 27.94 ? 122 VAL   B C   1 
ATOM   1642 O  O   . VAL   B 1 122 ? 32.264 -29.377 -6.958  1.00 31.14 ? 122 VAL   B O   1 
ATOM   1643 C  CB  . VAL   B 1 122 ? 30.912 -27.732 -9.187  1.00 33.25 ? 122 VAL   B CB  1 
HETATM 1644 CA CA  . CA    C 2 .   ? -2.191 -4.694  -17.577 1.00 12.68 ? 201 CA    A CA  1 
HETATM 1645 N  N1  . A1IS2 D 3 .   ? 20.196 -11.138 -0.591  0.50 8.68  ? 202 A1IS2 A N1  1 
HETATM 1646 C  C2  . A1IS2 D 3 .   ? 20.164 -9.911  -1.124  0.50 10.05 ? 202 A1IS2 A C2  1 
HETATM 1647 C  C3  . A1IS2 D 3 .   ? 19.659 -9.492  -2.481  0.50 12.09 ? 202 A1IS2 A C3  1 
HETATM 1648 C  C4  . A1IS2 D 3 .   ? 21.625 -9.339  2.366   0.50 12.03 ? 202 A1IS2 A C4  1 
HETATM 1649 C  C5  . A1IS2 D 3 .   ? 20.828 -7.543  -0.402  0.50 8.97  ? 202 A1IS2 A C5  1 
HETATM 1650 C  C6  . A1IS2 D 3 .   ? 21.543 -7.136  -1.542  0.50 9.62  ? 202 A1IS2 A C6  1 
HETATM 1651 C  C7  . A1IS2 D 3 .   ? 21.751 -5.786  -1.866  0.50 7.79  ? 202 A1IS2 A C7  1 
HETATM 1652 C  C8  . A1IS2 D 3 .   ? 21.234 -4.781  -1.082  0.50 9.87  ? 202 A1IS2 A C8  1 
HETATM 1653 C  C9  . A1IS2 D 3 .   ? 20.547 -5.155  0.013   0.50 10.14 ? 202 A1IS2 A C9  1 
HETATM 1654 C  C10 . A1IS2 D 3 .   ? 20.298 -6.554  0.441   0.50 9.83  ? 202 A1IS2 A C10 1 
HETATM 1655 C  C11 . A1IS2 D 3 .   ? 19.124 -6.017  2.285   0.50 11.33 ? 202 A1IS2 A C11 1 
HETATM 1656 C  C12 . A1IS2 D 3 .   ? 19.301 -4.677  1.997   0.50 12.22 ? 202 A1IS2 A C12 1 
HETATM 1657 C  C13 . A1IS2 D 3 .   ? 20.012 -4.222  0.913   0.50 11.69 ? 202 A1IS2 A C13 1 
HETATM 1658 C  C1  . A1IS2 D 3 .   ? 21.024 -9.809  1.070   0.50 10.00 ? 202 A1IS2 A C1  1 
HETATM 1659 N  N   . A1IS2 D 3 .   ? 20.734 -11.055 0.704   0.50 8.31  ? 202 A1IS2 A N   1 
HETATM 1660 C  C   . A1IS2 D 3 .   ? 20.575 -8.979  -0.023  0.50 9.80  ? 202 A1IS2 A C   1 
HETATM 1661 N  N2  . A1IS2 D 3 .   ? 19.614 -6.963  1.509   0.50 11.41 ? 202 A1IS2 A N2  1 
HETATM 1662 CA CA  . CA    E 2 .   ? 30.284 6.035   -11.333 0.80 21.91 ? 203 CA    A CA  1 
HETATM 1663 CA CA  . CA    F 2 .   ? 17.020 -34.201 -23.377 1.00 68.43 ? 201 CA    B CA  1 
HETATM 1664 N  N1  . A1IS2 G 3 .   ? 20.666 -20.043 -0.647  0.50 13.65 ? 202 A1IS2 B N1  1 
HETATM 1665 C  C2  . A1IS2 G 3 .   ? 20.487 -21.263 -1.176  0.50 12.02 ? 202 A1IS2 B C2  1 
HETATM 1666 C  C3  . A1IS2 G 3 .   ? 20.388 -21.634 -2.633  0.50 14.17 ? 202 A1IS2 B C3  1 
HETATM 1667 C  C4  . A1IS2 G 3 .   ? 20.561 -21.853 2.629   0.50 14.99 ? 202 A1IS2 B C4  1 
HETATM 1668 C  C5  . A1IS2 G 3 .   ? 20.193 -23.634 -0.280  0.50 15.46 ? 202 A1IS2 B C5  1 
HETATM 1669 C  C6  . A1IS2 G 3 .   ? 19.137 -24.039 -1.103  0.50 15.16 ? 202 A1IS2 B C6  1 
HETATM 1670 C  C7  . A1IS2 G 3 .   ? 18.852 -25.387 -1.322  0.50 14.19 ? 202 A1IS2 B C7  1 
HETATM 1671 C  C8  . A1IS2 G 3 .   ? 19.593 -26.411 -0.758  0.50 15.57 ? 202 A1IS2 B C8  1 
HETATM 1672 C  C9  . A1IS2 G 3 .   ? 20.577 -26.073 0.019   0.50 15.83 ? 202 A1IS2 B C9  1 
HETATM 1673 C  C10 . A1IS2 G 3 .   ? 20.992 -24.661 0.347   0.50 18.00 ? 202 A1IS2 B C10 1 
HETATM 1674 C  C11 . A1IS2 G 3 .   ? 22.741 -25.210 1.699   0.50 18.54 ? 202 A1IS2 B C11 1 
HETATM 1675 C  C12 . A1IS2 G 3 .   ? 22.465 -26.562 1.501   0.50 16.63 ? 202 A1IS2 B C12 1 
HETATM 1676 C  C13 . A1IS2 G 3 .   ? 21.437 -27.021 0.685   0.50 15.81 ? 202 A1IS2 B C13 1 
HETATM 1677 C  C1  . A1IS2 G 3 .   ? 20.561 -21.407 1.194   0.50 11.94 ? 202 A1IS2 B C1  1 
HETATM 1678 N  N   . A1IS2 G 3 .   ? 20.684 -20.160 0.763   0.50 13.21 ? 202 A1IS2 B N   1 
HETATM 1679 C  C   . A1IS2 G 3 .   ? 20.530 -22.223 -0.012  0.50 11.84 ? 202 A1IS2 B C   1 
HETATM 1680 N  N2  . A1IS2 G 3 .   ? 22.001 -24.277 1.139   0.50 17.35 ? 202 A1IS2 B N2  1 
HETATM 1681 O  O   . HOH   H 4 .   ? 22.171 -16.682 -13.648 1.00 17.49 ? 301 HOH   A O   1 
HETATM 1682 O  O   . HOH   H 4 .   ? 18.349 2.682   -12.599 1.00 22.60 ? 302 HOH   A O   1 
HETATM 1683 O  O   . HOH   H 4 .   ? 29.450 -14.875 -12.422 1.00 18.70 ? 303 HOH   A O   1 
HETATM 1684 O  O   . HOH   H 4 .   ? 22.433 3.920   -18.047 1.00 26.54 ? 304 HOH   A O   1 
HETATM 1685 O  O   . HOH   H 4 .   ? 4.141  -5.003  -10.189 1.00 18.82 ? 305 HOH   A O   1 
HETATM 1686 O  O   . HOH   H 4 .   ? 27.887 -13.799 -8.846  1.00 10.19 ? 306 HOH   A O   1 
HETATM 1687 O  O   . HOH   H 4 .   ? 37.415 -12.836 0.425   1.00 16.39 ? 307 HOH   A O   1 
HETATM 1688 O  O   . HOH   H 4 .   ? 7.353  -6.140  -30.614 1.00 26.69 ? 308 HOH   A O   1 
HETATM 1689 O  O   . HOH   H 4 .   ? 9.065  -4.085  -29.323 1.00 24.48 ? 309 HOH   A O   1 
HETATM 1690 O  O   . HOH   H 4 .   ? 34.785 -3.448  -9.701  1.00 24.83 ? 310 HOH   A O   1 
HETATM 1691 O  O   . HOH   H 4 .   ? 25.164 5.691   -6.450  1.00 23.72 ? 311 HOH   A O   1 
HETATM 1692 O  O   . HOH   H 4 .   ? 14.881 -9.787  -7.717  1.00 15.29 ? 312 HOH   A O   1 
HETATM 1693 O  O   . HOH   H 4 .   ? 28.622 -16.347 -10.493 1.00 22.72 ? 313 HOH   A O   1 
HETATM 1694 O  O   . HOH   H 4 .   ? 4.285  -4.243  -26.018 1.00 11.51 ? 314 HOH   A O   1 
HETATM 1695 O  O   . HOH   H 4 .   ? 41.826 -10.076 -14.118 1.00 25.31 ? 315 HOH   A O   1 
HETATM 1696 O  O   . HOH   H 4 .   ? 35.578 -19.192 -7.458  1.00 21.72 ? 316 HOH   A O   1 
HETATM 1697 O  O   . HOH   H 4 .   ? 14.351 -14.182 -12.546 1.00 12.39 ? 317 HOH   A O   1 
HETATM 1698 O  O   . HOH   H 4 .   ? 30.306 6.512   -8.937  1.00 22.32 ? 318 HOH   A O   1 
HETATM 1699 O  O   . HOH   H 4 .   ? 5.911  -8.922  -11.001 1.00 9.59  ? 319 HOH   A O   1 
HETATM 1700 O  O   . HOH   H 4 .   ? 1.423  -2.900  -11.286 1.00 15.43 ? 320 HOH   A O   1 
HETATM 1701 O  O   . HOH   H 4 .   ? 6.635  2.913   -13.476 1.00 19.74 ? 321 HOH   A O   1 
HETATM 1702 O  O   . HOH   H 4 .   ? 33.675 -3.747  -6.686  1.00 15.92 ? 322 HOH   A O   1 
HETATM 1703 O  O   . HOH   H 4 .   ? -3.020 -3.395  -19.593 1.00 17.56 ? 323 HOH   A O   1 
HETATM 1704 O  O   . HOH   H 4 .   ? 25.768 4.514   -12.047 1.00 15.27 ? 324 HOH   A O   1 
HETATM 1705 O  O   . HOH   H 4 .   ? 23.341 -21.717 -9.240  1.00 26.94 ? 325 HOH   A O   1 
HETATM 1706 O  O   . HOH   H 4 .   ? 15.280 4.239   -13.661 1.00 15.74 ? 326 HOH   A O   1 
HETATM 1707 O  O   . HOH   H 4 .   ? 16.573 6.128   -24.244 1.00 24.12 ? 327 HOH   A O   1 
HETATM 1708 O  O   . HOH   H 4 .   ? 36.609 -8.743  -17.066 1.00 16.98 ? 328 HOH   A O   1 
HETATM 1709 O  O   . HOH   H 4 .   ? 30.549 -5.859  -15.699 1.00 26.55 ? 329 HOH   A O   1 
HETATM 1710 O  O   . HOH   H 4 .   ? 25.866 -14.441 -2.606  1.00 16.57 ? 330 HOH   A O   1 
HETATM 1711 O  O   . HOH   H 4 .   ? 31.791 4.372   -10.821 1.00 26.55 ? 331 HOH   A O   1 
HETATM 1712 O  O   . HOH   H 4 .   ? 28.638 -7.390  0.901   1.00 8.56  ? 332 HOH   A O   1 
HETATM 1713 O  O   . HOH   H 4 .   ? -4.135 -3.753  -16.724 1.00 28.14 ? 333 HOH   A O   1 
HETATM 1714 O  O   . HOH   H 4 .   ? 11.402 0.415   -5.397  1.00 24.27 ? 334 HOH   A O   1 
HETATM 1715 O  O   . HOH   H 4 .   ? 3.246  -6.082  -12.761 1.00 11.28 ? 335 HOH   A O   1 
HETATM 1716 O  O   . HOH   H 4 .   ? 19.953 -3.535  -23.128 1.00 29.19 ? 336 HOH   A O   1 
HETATM 1717 O  O   . HOH   H 4 .   ? 33.438 1.165   -16.252 1.00 21.18 ? 337 HOH   A O   1 
HETATM 1718 O  O   . HOH   H 4 .   ? 22.063 -4.470  -24.036 1.00 18.73 ? 338 HOH   A O   1 
HETATM 1719 O  O   . HOH   H 4 .   ? -4.687 -1.820  -14.537 1.00 24.49 ? 339 HOH   A O   1 
HETATM 1720 O  O   . HOH   H 4 .   ? 34.858 4.685   -10.584 1.00 26.59 ? 340 HOH   A O   1 
HETATM 1721 O  O   . HOH   H 4 .   ? 39.267 -9.754  -17.256 1.00 19.34 ? 341 HOH   A O   1 
HETATM 1722 O  O   . HOH   H 4 .   ? 25.868 -5.267  -25.841 1.00 25.01 ? 342 HOH   A O   1 
HETATM 1723 O  O   . HOH   H 4 .   ? 5.260  -7.261  -8.964  1.00 18.40 ? 343 HOH   A O   1 
HETATM 1724 O  O   . HOH   H 4 .   ? -5.494 -3.597  -20.822 1.00 17.34 ? 344 HOH   A O   1 
HETATM 1725 O  O   . HOH   I 4 .   ? 37.256 -26.919 -21.881 1.00 35.76 ? 301 HOH   B O   1 
HETATM 1726 O  O   . HOH   I 4 .   ? 8.192  -16.551 -9.162  1.00 10.74 ? 302 HOH   B O   1 
HETATM 1727 O  O   . HOH   I 4 .   ? 11.152 -35.830 -10.435 1.00 28.84 ? 303 HOH   B O   1 
HETATM 1728 O  O   . HOH   I 4 .   ? 2.381  -12.026 -2.679  1.00 12.78 ? 304 HOH   B O   1 
HETATM 1729 O  O   . HOH   I 4 .   ? 27.750 -23.762 -3.325  1.00 17.32 ? 305 HOH   B O   1 
HETATM 1730 O  O   . HOH   I 4 .   ? 6.211  -11.611 -13.065 1.00 12.15 ? 306 HOH   B O   1 
HETATM 1731 O  O   . HOH   I 4 .   ? 9.296  -14.757 -7.372  1.00 11.23 ? 307 HOH   B O   1 
HETATM 1732 O  O   . HOH   I 4 .   ? -3.014 -17.805 -7.544  1.00 13.39 ? 308 HOH   B O   1 
HETATM 1733 O  O   . HOH   I 4 .   ? 10.699 -17.416 -5.982  1.00 8.02  ? 309 HOH   B O   1 
HETATM 1734 O  O   . HOH   I 4 .   ? 6.453  -25.037 -11.815 1.00 19.50 ? 310 HOH   B O   1 
HETATM 1735 O  O   . HOH   I 4 .   ? 11.784 -16.986 -8.432  1.00 16.58 ? 311 HOH   B O   1 
HETATM 1736 O  O   . HOH   I 4 .   ? 21.157 -35.675 -14.637 1.00 27.62 ? 312 HOH   B O   1 
HETATM 1737 O  O   . HOH   I 4 .   ? -1.968 -14.152 -1.288  1.00 22.39 ? 313 HOH   B O   1 
HETATM 1738 O  O   . HOH   I 4 .   ? 14.448 -16.949 -0.953  1.00 14.07 ? 314 HOH   B O   1 
HETATM 1739 O  O   . HOH   I 4 .   ? 20.553 -30.386 0.000   0.50 26.00 ? 315 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    N  N   . CYS   A 10  ? 0.4500 0.2268 0.6233 -0.0672 0.1151  -0.0080 10  CYS   A N   
2    C  CA  . CYS   A 10  ? 0.2612 0.2272 0.5008 -0.0112 -0.0588 -0.0013 10  CYS   A CA  
3    C  C   . CYS   A 10  ? 0.2574 0.2677 0.2760 -0.0392 -0.0608 0.0019  10  CYS   A C   
4    O  O   . CYS   A 10  ? 0.2159 0.3673 0.1946 0.1479  -0.0840 -0.0484 10  CYS   A O   
5    C  CB  . CYS   A 10  ? 0.3011 0.4390 0.4995 -0.0374 -0.1553 -0.0133 10  CYS   A CB  
6    S  SG  . CYS   A 10  ? 0.2721 0.6159 0.8344 -0.0365 0.0019  0.0789  10  CYS   A SG  
7    N  N   . PRO   A 11  ? 0.1710 0.2684 0.1735 0.0334  0.0007  0.0209  11  PRO   A N   
8    C  CA  . PRO   A 11  ? 0.1211 0.2386 0.1336 0.0665  0.0041  0.1304  11  PRO   A CA  
9    C  C   . PRO   A 11  ? 0.0514 0.2178 0.1503 0.0132  -0.0354 0.1017  11  PRO   A C   
10   O  O   . PRO   A 11  ? 0.0524 0.2595 0.1444 -0.0160 -0.0126 0.0837  11  PRO   A O   
11   C  CB  . PRO   A 11  ? 0.2137 0.2873 0.1931 0.0169  -0.0660 0.0506  11  PRO   A CB  
12   C  CG  . PRO   A 11  ? 0.1388 0.4818 0.1053 0.1390  -0.0420 0.0843  11  PRO   A CG  
13   C  CD  . PRO   A 11  ? 0.3021 0.3270 0.2380 0.0317  -0.0103 0.0904  11  PRO   A CD  
14   N  N   . LEU   A 12  ? 0.0589 0.2319 0.1995 -0.0508 0.0006  0.0703  12  LEU   A N   
15   C  CA  . LEU   A 12  ? 0.0732 0.1731 0.1256 -0.0669 0.0003  0.0637  12  LEU   A CA  
16   C  C   . LEU   A 12  ? 0.0599 0.2045 0.1555 -0.0611 0.0126  0.0352  12  LEU   A C   
17   O  O   . LEU   A 12  ? 0.0806 0.2927 0.2164 -0.0895 -0.0155 0.1190  12  LEU   A O   
18   C  CB  . LEU   A 12  ? 0.0843 0.1598 0.1330 -0.0519 0.0433  0.0429  12  LEU   A CB  
19   C  CG  . LEU   A 12  ? 0.1545 0.2063 0.1786 -0.0050 0.0227  0.0184  12  LEU   A CG  
20   C  CD1 . LEU   A 12  ? 0.1828 0.2031 0.1785 -0.0148 0.0750  -0.0099 12  LEU   A CD1 
21   C  CD2 . LEU   A 12  ? 0.0913 0.2124 0.1607 -0.0059 0.0764  0.0480  12  LEU   A CD2 
22   N  N   . MET   A 13  ? 0.0516 0.2195 0.1829 -0.0636 0.0078  0.0601  13  MET   A N   
23   C  CA  . MET   A 13  ? 0.0750 0.1550 0.1692 -0.0192 -0.0164 0.0433  13  MET   A CA  
24   C  C   . MET   A 13  ? 0.0446 0.1702 0.1421 0.0016  0.0217  0.0354  13  MET   A C   
25   O  O   . MET   A 13  ? 0.0772 0.1687 0.1083 0.0051  0.0307  0.0485  13  MET   A O   
26   C  CB  . MET   A 13  ? 0.2006 0.1502 0.2000 -0.0476 -0.0366 0.0214  13  MET   A CB  
27   C  CG  . MET   A 13  ? 0.2774 0.2222 0.3869 0.0295  -0.0399 -0.0049 13  MET   A CG  
28   S  SD  . MET   A 13  ? 0.3090 0.3712 0.5275 -0.0213 -0.0469 -0.1351 13  MET   A SD  
29   C  CE  . MET   A 13  ? 0.2597 0.2696 0.3991 0.0587  -0.1003 0.0156  13  MET   A CE  
30   N  N   . VAL   A 14  ? 0.0407 0.1560 0.1449 -0.0111 0.0245  0.0102  14  VAL   A N   
31   C  CA  . VAL   A 14  ? 0.0784 0.1515 0.0915 -0.0515 -0.0252 0.0602  14  VAL   A CA  
32   C  C   . VAL   A 14  ? 0.0312 0.1349 0.1169 -0.0248 -0.0178 0.0595  14  VAL   A C   
33   O  O   . VAL   A 14  ? 0.0381 0.1298 0.1817 -0.0225 -0.0269 0.0698  14  VAL   A O   
34   C  CB  . VAL   A 14  ? 0.0625 0.1508 0.1283 -0.0140 -0.0141 0.0280  14  VAL   A CB  
35   C  CG1 . VAL   A 14  ? 0.0594 0.1514 0.1270 -0.0347 0.0024  0.0749  14  VAL   A CG1 
36   C  CG2 . VAL   A 14  ? 0.0900 0.1927 0.0982 -0.0166 -0.0158 0.0379  14  VAL   A CG2 
37   N  N   . LYS   A 15  ? 0.0351 0.1311 0.1040 -0.0193 -0.0277 0.0508  15  LYS   A N   
38   C  CA  . LYS   A 15  ? 0.0467 0.1328 0.1184 -0.0098 -0.0426 0.0486  15  LYS   A CA  
39   C  C   . LYS   A 15  ? 0.0421 0.1188 0.1150 -0.0068 -0.0099 0.0302  15  LYS   A C   
40   O  O   . LYS   A 15  ? 0.0259 0.1488 0.1506 -0.0076 -0.0074 0.0588  15  LYS   A O   
41   C  CB  . LYS   A 15  ? 0.1200 0.1738 0.1256 0.0087  -0.0426 0.0400  15  LYS   A CB  
42   C  CG  . LYS   A 15  ? 0.2066 0.2873 0.2159 -0.0055 -0.1125 -0.0229 15  LYS   A CG  
43   N  N   . VAL   A 16  ? 0.0414 0.1068 0.1365 0.0007  -0.0025 0.0327  16  VAL   A N   
44   C  CA  . VAL   A 16  ? 0.0641 0.0991 0.0893 -0.0021 -0.0296 0.0298  16  VAL   A CA  
45   C  C   . VAL   A 16  ? 0.0273 0.1056 0.1058 -0.0027 -0.0126 0.0114  16  VAL   A C   
46   O  O   . VAL   A 16  ? 0.0401 0.1268 0.1450 -0.0176 -0.0405 0.0224  16  VAL   A O   
47   C  CB  . VAL   A 16  ? 0.0539 0.1328 0.0956 -0.0009 -0.0240 0.0016  16  VAL   A CB  
48   C  CG1 . VAL   A 16  ? 0.0514 0.1372 0.0985 -0.0031 -0.0373 0.0055  16  VAL   A CG1 
49   C  CG2 . VAL   A 16  ? 0.0466 0.1573 0.1238 -0.0337 -0.0315 0.0424  16  VAL   A CG2 
50   N  N   . LEU   A 17  ? 0.0346 0.1184 0.0840 0.0109  -0.0202 0.0108  17  LEU   A N   
51   C  CA  . LEU   A 17  ? 0.0328 0.0924 0.0623 -0.0143 -0.0134 0.0112  17  LEU   A CA  
52   C  C   . LEU   A 17  ? 0.0339 0.1152 0.0752 -0.0085 -0.0163 -0.0093 17  LEU   A C   
53   O  O   . LEU   A 17  ? 0.0303 0.1185 0.0945 -0.0085 -0.0008 -0.0161 17  LEU   A O   
54   C  CB  . LEU   A 17  ? 0.0525 0.1203 0.0709 -0.0073 0.0011  -0.0110 17  LEU   A CB  
55   C  CG  . LEU   A 17  ? 0.0380 0.1107 0.0621 -0.0049 0.0104  0.0102  17  LEU   A CG  
56   C  CD1 . LEU   A 17  ? 0.0424 0.1169 0.0636 0.0022  0.0188  -0.0004 17  LEU   A CD1 
57   C  CD2 . LEU   A 17  ? 0.0915 0.1098 0.0800 -0.0075 -0.0133 -0.0052 17  LEU   A CD2 
58   N  N   . ASP   A 18  ? 0.0295 0.1019 0.1041 0.0065  -0.0175 -0.0085 18  ASP   A N   
59   C  CA  . ASP   A 18  ? 0.0256 0.0843 0.0715 -0.0034 0.0025  0.0023  18  ASP   A CA  
60   C  C   . ASP   A 18  ? 0.0284 0.1064 0.0748 0.0157  0.0031  0.0063  18  ASP   A C   
61   O  O   . ASP   A 18  ? 0.0255 0.1220 0.0790 0.0042  0.0018  0.0041  18  ASP   A O   
62   C  CB  . ASP   A 18  ? 0.0271 0.1153 0.0718 -0.0074 0.0069  0.0066  18  ASP   A CB  
63   C  CG  . ASP   A 18  ? 0.0289 0.1545 0.0887 0.0050  0.0151  0.0243  18  ASP   A CG  
64   O  OD1 . ASP   A 18  ? 0.0360 0.1858 0.0531 -0.0310 0.0043  0.0303  18  ASP   A OD1 
65   O  OD2 . ASP   A 18  ? 0.0409 0.2477 0.0657 -0.0100 0.0148  0.0225  18  ASP   A OD2 
66   N  N   . ALA   A 19  ? 0.0332 0.1038 0.0634 0.0247  -0.0006 0.0020  19  ALA   A N   
67   C  CA  . ALA   A 19  ? 0.0518 0.1105 0.0711 0.0441  0.0045  0.0065  19  ALA   A CA  
68   C  C   . ALA   A 19  ? 0.0634 0.1284 0.0586 0.0575  -0.0080 0.0056  19  ALA   A C   
69   O  O   . ALA   A 19  ? 0.0878 0.1385 0.0742 0.0548  0.0024  0.0279  19  ALA   A O   
70   C  CB  . ALA   A 19  ? 0.0806 0.1194 0.0792 0.0350  0.0324  0.0260  19  ALA   A CB  
71   N  N   . VAL   A 20  ? 0.0527 0.1626 0.0955 0.0063  -0.0047 0.0281  20  VAL   A N   
72   C  CA  . VAL   A 20  ? 0.0833 0.1112 0.1162 0.0572  -0.0122 0.0001  20  VAL   A CA  
73   C  C   . VAL   A 20  ? 0.0489 0.1936 0.1275 0.0452  -0.0080 -0.0239 20  VAL   A C   
74   O  O   . VAL   A 20  ? 0.0383 0.2968 0.1899 0.0259  -0.0454 -0.0521 20  VAL   A O   
75   C  CB  . VAL   A 20  ? 0.0422 0.1453 0.1210 0.0419  -0.0102 -0.0072 20  VAL   A CB  
76   C  CG1 . VAL   A 20  ? 0.0477 0.1911 0.1809 0.0595  -0.0150 -0.0147 20  VAL   A CG1 
77   C  CG2 . VAL   A 20  ? 0.0894 0.1172 0.1235 0.0432  -0.0013 -0.0169 20  VAL   A CG2 
78   N  N   . ARG   A 21  ? 0.0722 0.1882 0.1474 0.0249  -0.0660 -0.0485 21  ARG   A N   
79   C  CA  . ARG   A 21  ? 0.0292 0.2052 0.1755 0.0045  -0.0126 -0.0515 21  ARG   A CA  
80   C  C   . ARG   A 21  ? 0.0350 0.1728 0.1270 -0.0129 -0.0182 -0.0280 21  ARG   A C   
81   O  O   . ARG   A 21  ? 0.0528 0.2459 0.1227 -0.0141 -0.0121 -0.0810 21  ARG   A O   
82   C  CB  . ARG   A 21  ? 0.1160 0.2592 0.1650 -0.0678 -0.0020 -0.0598 21  ARG   A CB  
83   C  CG  . ARG   A 21  ? 0.2133 0.2921 0.2277 -0.0258 -0.0059 -0.1062 21  ARG   A CG  
84   C  CD  . ARG   A 21  ? 0.4806 0.2564 0.3089 -0.1050 0.0251  -0.0564 21  ARG   A CD  
85   N  NE  . ARG   A 21  ? 0.6054 0.3624 0.2934 0.0931  0.0765  -0.0789 21  ARG   A NE  
86   C  CZ  . ARG   A 21  ? 0.3967 0.3340 0.1683 -0.0840 0.0417  0.1597  21  ARG   A CZ  
87   N  N   . GLY   A 22  ? 0.0424 0.2149 0.1581 0.0059  0.0078  0.0179  22  GLY   A N   
88   C  CA  . GLY   A 22  ? 0.0433 0.1517 0.0881 -0.0305 -0.0278 0.0089  22  GLY   A CA  
89   C  C   . GLY   A 22  ? 0.0273 0.1386 0.0721 0.0002  -0.0096 -0.0132 22  GLY   A C   
90   O  O   . GLY   A 22  ? 0.0426 0.0989 0.1239 0.0227  0.0036  -0.0226 22  GLY   A O   
91   N  N   . SER   A 23  ? 0.0432 0.1124 0.0889 0.0140  -0.0314 -0.0146 23  SER   A N   
92   C  CA  . SER   A 23  ? 0.0499 0.1324 0.0725 0.0002  -0.0336 0.0059  23  SER   A CA  
93   C  C   . SER   A 23  ? 0.0557 0.1128 0.0747 -0.0064 -0.0384 0.0058  23  SER   A C   
94   O  O   . SER   A 23  ? 0.0328 0.1295 0.0747 -0.0141 -0.0139 -0.0053 23  SER   A O   
95   C  CB  . SER   A 23  ? 0.0498 0.1562 0.1234 -0.0449 -0.0356 0.0175  23  SER   A CB  
96   O  OG  . SER   A 23  ? 0.0516 0.2474 0.2070 -0.0296 -0.0296 -0.0238 23  SER   A OG  
97   N  N   . PRO   A 24  ? 0.0315 0.1215 0.0918 0.0236  -0.0042 0.0044  24  PRO   A N   
98   C  CA  . PRO   A 24  ? 0.0757 0.1316 0.0696 -0.0038 -0.0110 -0.0212 24  PRO   A CA  
99   C  C   . PRO   A 24  ? 0.0339 0.1818 0.0336 -0.0131 -0.0083 0.0078  24  PRO   A C   
100  O  O   . PRO   A 24  ? 0.0330 0.1798 0.0704 -0.0216 0.0079  0.0361  24  PRO   A O   
101  C  CB  . PRO   A 24  ? 0.0853 0.1402 0.1341 -0.0063 0.0000  -0.0040 24  PRO   A CB  
102  C  CG  . PRO   A 24  ? 0.2718 0.1027 0.2104 -0.0579 -0.0898 -0.0046 24  PRO   A CG  
103  C  CD  . PRO   A 24  ? 0.1087 0.1360 0.1523 0.0115  -0.0035 -0.0151 24  PRO   A CD  
104  N  N   . ALA   A 25  ? 0.0509 0.1650 0.0768 -0.0169 -0.0315 -0.0088 25  ALA   A N   
105  C  CA  . ALA   A 25  ? 0.0535 0.1527 0.0637 0.0045  -0.0318 0.0126  25  ALA   A CA  
106  C  C   . ALA   A 25  ? 0.0439 0.1425 0.0816 0.0088  -0.0305 0.0118  25  ALA   A C   
107  O  O   . ALA   A 25  ? 0.0569 0.1757 0.0722 0.0294  -0.0127 0.0597  25  ALA   A O   
108  C  CB  . ALA   A 25  ? 0.0469 0.1673 0.1247 -0.0182 -0.0136 0.0208  25  ALA   A CB  
109  N  N   . ILE   A 26  ? 0.0445 0.1706 0.1130 0.0011  -0.0178 0.0042  26  ILE   A N   
110  C  CA  . ILE   A 26  ? 0.0748 0.2031 0.0955 -0.0143 -0.0282 0.0099  26  ILE   A CA  
111  C  C   . ILE   A 26  ? 0.0682 0.2062 0.1006 -0.0468 -0.0363 -0.0116 26  ILE   A C   
112  O  O   . ILE   A 26  ? 0.1066 0.2100 0.0556 -0.0339 0.0007  0.0423  26  ILE   A O   
113  C  CB  . ILE   A 26  ? 0.1121 0.2265 0.1037 -0.0371 -0.0378 -0.0064 26  ILE   A CB  
114  C  CG1 . ILE   A 26  ? 0.1242 0.1875 0.1039 -0.0486 -0.0146 0.0245  26  ILE   A CG1 
115  C  CG2 . ILE   A 26  ? 0.1880 0.2467 0.1704 -0.0173 -0.0317 0.0040  26  ILE   A CG2 
116  C  CD1 . ILE   A 26  ? 0.2299 0.3164 0.1364 -0.0344 -0.1038 -0.0300 26  ILE   A CD1 
117  N  N   . ASN   A 27  ? 0.0674 0.2325 0.0889 -0.0222 -0.0202 -0.0122 27  ASN   A N   
118  C  CA  . ASN   A 27  ? 0.0701 0.2438 0.1004 -0.0490 0.0011  0.0456  27  ASN   A CA  
119  C  C   . ASN   A 27  ? 0.0524 0.2608 0.0412 -0.0351 -0.0181 0.0503  27  ASN   A C   
120  O  O   . ASN   A 27  ? 0.0953 0.2942 0.1022 -0.0340 0.0068  -0.0053 27  ASN   A O   
121  C  CB  . ASN   A 27  ? 0.0633 0.2332 0.1040 -0.0381 -0.0071 0.0710  27  ASN   A CB  
122  C  CG  . ASN   A 27  ? 0.0846 0.2507 0.2018 -0.1083 -0.0147 0.0961  27  ASN   A CG  
123  O  OD1 . ASN   A 27  ? 0.1075 0.4516 0.2523 -0.1744 -0.0167 0.0278  27  ASN   A OD1 
124  N  ND2 . ASN   A 27  ? 0.1069 0.2910 0.1966 -0.1105 -0.0431 0.0905  27  ASN   A ND2 
125  N  N   . VAL   A 28  ? 0.0279 0.1846 0.0873 -0.0024 -0.0119 0.0457  28  VAL   A N   
126  C  CA  . VAL   A 28  ? 0.0469 0.2265 0.0963 0.0030  -0.0117 -0.0119 28  VAL   A CA  
127  C  C   . VAL   A 28  ? 0.0532 0.1473 0.0953 -0.0164 -0.0028 0.0270  28  VAL   A C   
128  O  O   . VAL   A 28  ? 0.0270 0.1782 0.0916 -0.0146 0.0000  0.0421  28  VAL   A O   
129  C  CB  . VAL   A 28  ? 0.1595 0.1934 0.1989 -0.0379 -0.0752 0.0453  28  VAL   A CB  
130  C  CG1 . VAL   A 28  ? 0.3507 0.2052 0.1060 -0.1526 0.0303  0.0721  28  VAL   A CG1 
131  C  CG2 . VAL   A 28  ? 0.1990 0.2137 0.2306 -0.0463 -0.1080 0.0024  28  VAL   A CG2 
132  N  N   . ALA   A 29  ? 0.0321 0.1786 0.1078 0.0086  -0.0221 0.0115  29  ALA   A N   
133  C  CA  . ALA   A 29  ? 0.0496 0.1006 0.0689 -0.0227 -0.0082 0.0347  29  ALA   A CA  
134  C  C   . ALA   A 29  ? 0.0458 0.0925 0.0970 -0.0127 0.0005  0.0363  29  ALA   A C   
135  O  O   . ALA   A 29  ? 0.0387 0.0854 0.1068 0.0037  -0.0158 0.0306  29  ALA   A O   
136  C  CB  . ALA   A 29  ? 0.0339 0.1419 0.0979 -0.0114 0.0147  0.0264  29  ALA   A CB  
137  N  N   . VAL   A 30  ? 0.0604 0.1191 0.0889 -0.0047 0.0005  0.0683  30  VAL   A N   
138  C  CA  . VAL   A 30  ? 0.0589 0.1504 0.1185 -0.0187 -0.0254 0.0416  30  VAL   A CA  
139  C  C   . VAL   A 30  ? 0.0254 0.1404 0.1056 0.0032  0.0016  0.0477  30  VAL   A C   
140  O  O   . VAL   A 30  ? 0.0315 0.1536 0.0889 -0.0207 -0.0197 0.0620  30  VAL   A O   
141  C  CB  . VAL   A 30  ? 0.0542 0.1518 0.1135 -0.0088 -0.0234 0.0513  30  VAL   A CB  
142  C  CG1 . VAL   A 30  ? 0.0662 0.1361 0.1269 -0.0143 0.0219  0.0334  30  VAL   A CG1 
143  C  CG2 . VAL   A 30  ? 0.0554 0.1868 0.1050 -0.0368 -0.0222 0.0329  30  VAL   A CG2 
144  N  N   . HIS   A 31  ? 0.0374 0.1391 0.1109 -0.0057 -0.0249 0.0726  31  HIS   A N   
145  C  CA  . HIS   A 31  ? 0.0274 0.1690 0.0920 -0.0079 -0.0120 0.0452  31  HIS   A CA  
146  C  C   . HIS   A 31  ? 0.0291 0.1513 0.0961 -0.0122 -0.0114 0.0263  31  HIS   A C   
147  O  O   . HIS   A 31  ? 0.0531 0.2069 0.2237 0.0166  0.0005  0.0970  31  HIS   A O   
148  C  CB  . HIS   A 31  ? 0.0639 0.1703 0.1108 -0.0590 -0.0273 0.0220  31  HIS   A CB  
149  C  CG  . HIS   A 31  ? 0.0545 0.2877 0.2144 -0.0357 0.0190  -0.0194 31  HIS   A CG  
150  N  ND1 . HIS   A 31  ? 0.1699 0.3999 0.2509 -0.0268 -0.0443 0.0026  31  HIS   A ND1 
151  C  CD2 . HIS   A 31  ? 0.0475 0.2698 0.1689 -0.0724 0.0108  -0.0694 31  HIS   A CD2 
152  C  CE1 . HIS   A 31  ? 0.1983 0.3894 0.2407 -0.0825 -0.0076 -0.0861 31  HIS   A CE1 
153  N  NE2 . HIS   A 31  ? 0.0467 0.3997 0.2539 -0.0540 0.0150  -0.0907 31  HIS   A NE2 
154  N  N   . VAL   A 32  ? 0.0362 0.1460 0.0911 -0.0184 -0.0012 0.0601  32  VAL   A N   
155  C  CA  . VAL   A 32  ? 0.0367 0.1668 0.1147 -0.0261 -0.0123 0.0403  32  VAL   A CA  
156  C  C   . VAL   A 32  ? 0.0423 0.1932 0.0909 -0.0023 0.0066  0.0303  32  VAL   A C   
157  O  O   . VAL   A 32  ? 0.0281 0.2704 0.0848 -0.0104 0.0086  0.0508  32  VAL   A O   
158  C  CB  . VAL   A 32  ? 0.0341 0.1786 0.1014 -0.0263 0.0140  0.0215  32  VAL   A CB  
159  C  CG1 . VAL   A 32  ? 0.0457 0.1592 0.1236 -0.0327 0.0237  0.0357  32  VAL   A CG1 
160  C  CG2 . VAL   A 32  ? 0.0540 0.1716 0.0965 -0.0185 0.0178  0.0315  32  VAL   A CG2 
161  N  N   . PHE   A 33  ? 0.0722 0.1762 0.0553 0.0000  0.0159  0.0388  33  PHE   A N   
162  C  CA  . PHE   A 33  ? 0.0566 0.1665 0.0802 -0.0504 0.0232  0.0101  33  PHE   A CA  
163  C  C   . PHE   A 33  ? 0.0460 0.2091 0.0893 -0.0272 0.0133  0.0257  33  PHE   A C   
164  O  O   . PHE   A 33  ? 0.0536 0.2104 0.0693 -0.0020 -0.0182 0.0279  33  PHE   A O   
165  C  CB  . PHE   A 33  ? 0.0393 0.1793 0.0747 -0.0441 0.0012  0.0237  33  PHE   A CB  
166  C  CG  . PHE   A 33  ? 0.0468 0.1829 0.1138 -0.0063 0.0276  0.0420  33  PHE   A CG  
167  C  CD1 . PHE   A 33  ? 0.0479 0.2006 0.1132 0.0098  0.0216  0.0073  33  PHE   A CD1 
168  C  CD2 . PHE   A 33  ? 0.0562 0.2188 0.1403 -0.0238 0.0427  0.0660  33  PHE   A CD2 
169  C  CE1 . PHE   A 33  ? 0.0396 0.2134 0.1648 -0.0518 -0.0046 0.0222  33  PHE   A CE1 
170  C  CE2 . PHE   A 33  ? 0.0560 0.2723 0.1621 -0.0425 0.0477  0.0424  33  PHE   A CE2 
171  C  CZ  . PHE   A 33  ? 0.0759 0.1863 0.1841 -0.0476 0.0294  0.0291  33  PHE   A CZ  
172  N  N   . ARG   A 34  ? 0.0491 0.1780 0.0949 -0.0286 0.0218  0.0501  34  ARG   A N   
173  C  CA  . ARG   A 34  ? 0.0402 0.1924 0.1227 -0.0319 0.0046  0.0224  34  ARG   A CA  
174  C  C   . ARG   A 34  ? 0.0639 0.1697 0.0959 0.0088  0.0174  0.0265  34  ARG   A C   
175  O  O   . ARG   A 34  ? 0.0459 0.2578 0.1060 -0.0414 0.0328  -0.0011 34  ARG   A O   
176  C  CB  . ARG   A 34  ? 0.0623 0.1525 0.1421 -0.0683 -0.0170 0.0207  34  ARG   A CB  
177  C  CG  . ARG   A 34  ? 0.0960 0.2069 0.1825 -0.0073 0.0434  0.0527  34  ARG   A CG  
178  C  CD  . ARG   A 34  ? 0.2070 0.1646 0.2832 0.0371  0.0453  0.0187  34  ARG   A CD  
179  N  NE  . ARG   A 34  ? 0.3305 0.4279 0.3907 -0.0095 -0.0879 0.0000  34  ARG   A NE  
180  C  CZ  . ARG   A 34  ? 0.2562 0.2635 0.2943 0.1169  -0.1313 0.0711  34  ARG   A CZ  
181  N  NH1 . ARG   A 34  ? 0.1472 0.3557 0.3031 0.0731  -0.1776 -0.0328 34  ARG   A NH1 
182  N  NH2 . ARG   A 34  ? 0.3169 0.3591 0.2538 0.1371  0.0694  -0.0660 34  ARG   A NH2 
183  N  N   . LYS   A 35  ? 0.0755 0.1940 0.1251 0.0008  -0.0148 0.1015  35  LYS   A N   
184  C  CA  . LYS   A 35  ? 0.1624 0.2401 0.2268 0.0047  0.0045  0.0116  35  LYS   A CA  
185  C  C   . LYS   A 35  ? 0.0933 0.1932 0.3645 -0.0629 -0.0414 0.0186  35  LYS   A C   
186  O  O   . LYS   A 35  ? 0.0632 0.4092 0.3896 -0.0274 -0.0524 0.0387  35  LYS   A O   
187  C  CB  . LYS   A 35  ? 0.0809 0.2351 0.1676 0.0651  -0.0018 0.0259  35  LYS   A CB  
188  C  CG  . LYS   A 35  ? 0.1741 0.2182 0.2691 0.0456  0.0327  -0.0242 35  LYS   A CG  
189  C  CD  . LYS   A 35  ? 0.3605 0.2833 0.2724 0.0670  -0.0485 0.0423  35  LYS   A CD  
190  C  CE  . LYS   A 35  ? 0.1335 0.3279 0.2896 -0.0370 -0.0943 0.0831  35  LYS   A CE  
191  N  N   . ALA   A 36  ? 0.1278 0.1831 0.2403 0.0219  0.1457  0.0655  36  ALA   A N   
192  C  CA  . ALA   A 36  ? 0.1818 0.3979 0.3466 0.1021  0.0706  0.0176  36  ALA   A CA  
193  C  C   . ALA   A 36  ? 0.2394 0.4529 0.4652 0.0888  0.0433  -0.0367 36  ALA   A C   
194  O  O   . ALA   A 36  ? 0.2739 0.4317 0.3459 0.0462  -0.1152 -0.0641 36  ALA   A O   
195  C  CB  . ALA   A 36  ? 0.3241 0.4900 0.3283 0.0022  -0.0385 0.0526  36  ALA   A CB  
196  N  N   . ALA   A 37  ? 0.2371 0.3989 0.4003 0.0597  0.0442  -0.0254 37  ALA   A N   
197  C  CA  . ALA   A 37  ? 0.2623 0.5982 0.3860 -0.0180 -0.0355 0.0016  37  ALA   A CA  
198  C  C   . ALA   A 37  ? 0.3449 0.4446 0.4990 -0.1281 0.0783  -0.0105 37  ALA   A C   
199  O  O   . ALA   A 37  ? 0.1718 0.5676 0.3555 -0.1844 -0.0985 0.0996  37  ALA   A O   
200  C  CB  . ALA   A 37  ? 0.2267 0.7052 0.5485 0.0296  0.0002  0.0265  37  ALA   A CB  
201  N  N   . ASP   A 38  ? 0.3804 0.4406 0.3854 -0.0218 0.0404  -0.0468 38  ASP   A N   
202  C  CA  . ASP   A 38  ? 0.1036 0.3417 0.2704 0.0383  -0.0039 0.0313  38  ASP   A CA  
203  C  C   . ASP   A 38  ? 0.0742 0.2934 0.6113 0.0589  0.1347  -0.0434 38  ASP   A C   
204  O  O   . ASP   A 38  ? 0.4203 0.4788 0.3345 0.0454  -0.0635 -0.0909 38  ASP   A O   
205  C  CB  . ASP   A 38  ? 0.2607 0.3610 0.2611 -0.0514 0.0543  0.0069  38  ASP   A CB  
206  C  CG  . ASP   A 38  ? 0.3284 0.4039 0.3293 -0.1454 0.0284  0.1343  38  ASP   A CG  
207  O  OD1 . ASP   A 38  ? 0.3172 0.4836 0.3285 0.0745  0.0591  0.1211  38  ASP   A OD1 
208  O  OD2 . ASP   A 38  ? 0.2622 0.4714 0.2353 -0.0587 -0.0047 0.1109  38  ASP   A OD2 
209  N  N   A TRP   A 41  ? 0.1366 0.4885 0.3246 0.1739  0.1276  0.0281  41  TRP   A N   
210  N  N   B TRP   A 41  ? 0.5016 0.3878 0.1837 -0.0899 0.1976  0.1251  41  TRP   A N   
211  C  CA  A TRP   A 41  ? 0.3697 0.3670 0.3667 0.0144  0.0527  0.0446  41  TRP   A CA  
212  C  CA  B TRP   A 41  ? 0.3825 0.4265 0.4212 -0.0315 0.0995  0.0236  41  TRP   A CA  
213  C  C   A TRP   A 41  ? 0.4227 0.4157 0.2116 -0.0380 0.1560  -0.0889 41  TRP   A C   
214  C  C   B TRP   A 41  ? 0.4648 0.3552 0.3297 -0.0645 0.0768  -0.0808 41  TRP   A C   
215  O  O   A TRP   A 41  ? 0.4404 0.2818 0.2708 0.0249  -0.1327 0.0291  41  TRP   A O   
216  O  O   B TRP   A 41  ? 0.0772 0.2898 0.4870 0.0614  -0.1507 -0.1110 41  TRP   A O   
217  C  CB  A TRP   A 41  ? 0.2139 0.4013 0.2453 0.0398  -0.0220 0.0715  41  TRP   A CB  
218  C  CB  B TRP   A 41  ? 0.3320 0.4256 0.2465 -0.0573 0.2022  -0.0262 41  TRP   A CB  
219  C  CG  A TRP   A 41  ? 0.1118 0.3411 0.3002 0.0406  0.0220  0.0198  41  TRP   A CG  
220  C  CG  B TRP   A 41  ? 0.3521 0.3500 0.2867 -0.0169 0.0598  -0.0334 41  TRP   A CG  
221  C  CD1 A TRP   A 41  ? 0.2602 0.3347 0.3889 0.0150  0.0018  -0.0653 41  TRP   A CD1 
222  C  CD1 B TRP   A 41  ? 0.2649 0.4036 0.3545 -0.0095 0.0516  -0.0387 41  TRP   A CD1 
223  C  CD2 A TRP   A 41  ? 0.1415 0.3094 0.2990 0.0647  0.0722  0.0134  41  TRP   A CD2 
224  C  CD2 B TRP   A 41  ? 0.3608 0.3172 0.2823 -0.0302 0.0713  0.0084  41  TRP   A CD2 
225  N  NE1 A TRP   A 41  ? 0.3605 0.3796 0.4006 0.0310  0.0013  -0.0429 41  TRP   A NE1 
226  N  NE1 B TRP   A 41  ? 0.2974 0.4034 0.2639 0.0693  -0.0853 -0.0043 41  TRP   A NE1 
227  C  CE2 A TRP   A 41  ? 0.2051 0.2485 0.3387 0.0710  0.0746  -0.0121 41  TRP   A CE2 
228  C  CE2 B TRP   A 41  ? 0.3175 0.3401 0.2006 0.0144  -0.0433 -0.0068 41  TRP   A CE2 
229  C  CE3 A TRP   A 41  ? 0.1372 0.3203 0.2476 0.0565  0.0319  0.0331  41  TRP   A CE3 
230  C  CE3 B TRP   A 41  ? 0.1747 0.3594 0.2376 -0.0034 -0.0146 0.0333  41  TRP   A CE3 
231  C  CZ2 A TRP   A 41  ? 0.1171 0.1953 0.2996 -0.0755 0.0734  0.0919  41  TRP   A CZ2 
232  C  CZ2 B TRP   A 41  ? 0.2098 0.2830 0.3175 -0.0106 0.0085  -0.0166 41  TRP   A CZ2 
233  C  CZ3 A TRP   A 41  ? 0.0855 0.3166 0.1863 0.0384  -0.0838 0.0548  41  TRP   A CZ3 
234  C  CZ3 B TRP   A 41  ? 0.0866 0.3844 0.1795 0.0190  -0.0934 0.0354  41  TRP   A CZ3 
235  C  CH2 A TRP   A 41  ? 0.0270 0.2952 0.2700 0.0183  -0.0108 -0.0006 41  TRP   A CH2 
236  C  CH2 B TRP   A 41  ? 0.0663 0.3204 0.2791 -0.0094 -0.0067 0.0000  41  TRP   A CH2 
237  N  N   . GLU   A 42  ? 0.4324 0.3473 0.2106 -0.1057 0.2137  -0.0637 42  GLU   A N   
238  C  CA  . GLU   A 42  ? 0.1873 0.3811 0.1302 -0.1189 0.1046  -0.0366 42  GLU   A CA  
239  C  C   . GLU   A 42  ? 0.1248 0.3636 0.1264 -0.0721 0.0739  0.0121  42  GLU   A C   
240  O  O   . GLU   A 42  ? 0.0496 0.3428 0.0904 0.0097  -0.0114 0.0789  42  GLU   A O   
241  C  CB  . GLU   A 42  ? 0.1685 0.4391 0.1770 -0.1535 -0.0755 -0.0724 42  GLU   A CB  
242  C  CG  . GLU   A 42  ? 0.2707 0.3719 0.3000 -0.0013 0.0197  -0.0116 42  GLU   A CG  
243  C  CD  . GLU   A 42  ? 0.1977 0.3531 0.4432 -0.0833 -0.0789 -0.0789 42  GLU   A CD  
244  O  OE1 . GLU   A 42  ? 0.1668 0.2558 0.3762 0.0510  -0.0218 0.0519  42  GLU   A OE1 
245  O  OE2 . GLU   A 42  ? 0.0967 0.4290 0.3900 -0.0062 -0.0352 -0.1424 42  GLU   A OE2 
246  N  N   . PRO   A 43  ? 0.0952 0.2977 0.1594 -0.0403 0.0713  -0.0137 43  PRO   A N   
247  C  CA  . PRO   A 43  ? 0.1311 0.2966 0.0990 -0.0494 0.0873  -0.0212 43  PRO   A CA  
248  C  C   . PRO   A 43  ? 0.0652 0.2331 0.1464 -0.0368 0.0232  0.0375  43  PRO   A C   
249  O  O   . PRO   A 43  ? 0.1320 0.2693 0.1561 0.0002  0.0285  0.0319  43  PRO   A O   
250  C  CB  . PRO   A 43  ? 0.1293 0.4111 0.2020 -0.0636 0.1255  -0.0215 43  PRO   A CB  
251  C  CG  . PRO   A 43  ? 0.2697 0.3006 0.3467 -0.1293 0.0617  -0.0133 43  PRO   A CG  
252  C  CD  . PRO   A 43  ? 0.2016 0.3758 0.2106 -0.1292 0.1670  -0.0391 43  PRO   A CD  
253  N  N   . PHE   A 44  ? 0.0564 0.1993 0.1326 0.0028  -0.0300 0.0587  44  PHE   A N   
254  C  CA  . PHE   A 44  ? 0.0599 0.2205 0.1256 0.0157  -0.0468 0.0618  44  PHE   A CA  
255  C  C   . PHE   A 44  ? 0.0469 0.2212 0.1379 0.0120  0.0055  0.0514  44  PHE   A C   
256  O  O   . PHE   A 44  ? 0.0276 0.2242 0.1595 -0.0113 0.0133  0.0278  44  PHE   A O   
257  C  CB  . PHE   A 44  ? 0.0775 0.2087 0.0893 0.0512  -0.0274 0.0499  44  PHE   A CB  
258  C  CG  . PHE   A 44  ? 0.0651 0.1317 0.0958 -0.0015 -0.0204 0.0278  44  PHE   A CG  
259  C  CD1 . PHE   A 44  ? 0.0628 0.2018 0.1256 0.0259  -0.0224 0.0138  44  PHE   A CD1 
260  C  CD2 . PHE   A 44  ? 0.0263 0.2240 0.0754 0.0038  -0.0055 0.0359  44  PHE   A CD2 
261  C  CE1 . PHE   A 44  ? 0.0319 0.2284 0.1098 0.0261  0.0038  0.0316  44  PHE   A CE1 
262  C  CE2 . PHE   A 44  ? 0.0382 0.2363 0.1621 0.0103  -0.0272 0.0082  44  PHE   A CE2 
263  C  CZ  . PHE   A 44  ? 0.0323 0.1535 0.1203 0.0208  0.0214  0.0196  44  PHE   A CZ  
264  N  N   . ALA   A 45  ? 0.0319 0.1894 0.1286 0.0238  0.0241  0.0518  45  ALA   A N   
265  C  CA  . ALA   A 45  ? 0.0507 0.2764 0.1959 0.0122  0.0045  0.0335  45  ALA   A CA  
266  C  C   . ALA   A 45  ? 0.0320 0.2278 0.2198 -0.0132 0.0244  0.0886  45  ALA   A C   
267  O  O   . ALA   A 45  ? 0.0293 0.2501 0.1415 0.0077  -0.0164 0.0708  45  ALA   A O   
268  C  CB  . ALA   A 45  ? 0.1158 0.1714 0.1278 -0.0365 0.0362  0.0710  45  ALA   A CB  
269  N  N   . SER   A 46  ? 0.0748 0.2442 0.1022 -0.0243 -0.0199 0.1281  46  SER   A N   
270  C  CA  . SER   A 46  ? 0.0545 0.1620 0.0763 -0.0064 0.0075  0.0742  46  SER   A CA  
271  C  C   . SER   A 46  ? 0.0367 0.1478 0.1421 -0.0057 -0.0063 0.0838  46  SER   A C   
272  O  O   . SER   A 46  ? 0.0344 0.1459 0.1992 0.0031  -0.0322 0.0733  46  SER   A O   
273  C  CB  . SER   A 46  ? 0.0594 0.1614 0.1243 0.0018  -0.0026 0.0670  46  SER   A CB  
274  O  OG  . SER   A 46  ? 0.0372 0.2474 0.0825 -0.0116 -0.0231 0.0730  46  SER   A OG  
275  N  N   . GLY   A 47  ? 0.0275 0.1457 0.1213 -0.0154 -0.0101 0.0467  47  GLY   A N   
276  C  CA  . GLY   A 47  ? 0.0258 0.1452 0.1201 0.0007  0.0005  0.0148  47  GLY   A CA  
277  C  C   . GLY   A 47  ? 0.0265 0.1309 0.1423 0.0052  -0.0108 -0.0049 47  GLY   A C   
278  O  O   . GLY   A 47  ? 0.0263 0.1564 0.1019 -0.0045 0.0084  -0.0056 47  GLY   A O   
279  N  N   . LYS   A 48  ? 0.0681 0.1266 0.1318 0.0134  -0.0521 0.0169  48  LYS   A N   
280  C  CA  . LYS   A 48  ? 0.0367 0.1418 0.1268 -0.0053 -0.0330 0.0411  48  LYS   A CA  
281  C  C   . LYS   A 48  ? 0.0335 0.1122 0.1244 -0.0198 -0.0248 0.0297  48  LYS   A C   
282  O  O   . LYS   A 48  ? 0.0538 0.1587 0.1205 0.0204  -0.0042 0.0205  48  LYS   A O   
283  C  CB  . LYS   A 48  ? 0.0435 0.2185 0.1613 -0.0391 -0.0284 0.0241  48  LYS   A CB  
284  C  CG  . LYS   A 48  ? 0.1108 0.2568 0.1383 -0.0625 -0.0398 -0.0250 48  LYS   A CG  
285  C  CD  . LYS   A 48  ? 0.1319 0.2469 0.2564 -0.0082 -0.0669 0.0287  48  LYS   A CD  
286  C  CE  . LYS   A 48  ? 0.1882 0.3419 0.2322 -0.0419 -0.0034 -0.0320 48  LYS   A CE  
287  N  NZ  . LYS   A 48  ? 0.2559 0.3928 0.2932 -0.0050 -0.0745 -0.0637 48  LYS   A NZ  
288  N  N   . THR   A 49  ? 0.0390 0.1196 0.1206 0.0232  -0.0223 0.0190  49  THR   A N   
289  C  CA  . THR   A 49  ? 0.0709 0.1467 0.1294 0.0377  -0.0431 0.0101  49  THR   A CA  
290  C  C   . THR   A 49  ? 0.0632 0.1663 0.0906 0.0205  -0.0174 0.0113  49  THR   A C   
291  O  O   . THR   A 49  ? 0.0645 0.2472 0.0800 0.0218  -0.0210 0.0354  49  THR   A O   
292  C  CB  . THR   A 49  ? 0.0574 0.1686 0.1177 0.0296  -0.0158 0.0100  49  THR   A CB  
293  O  OG1 . THR   A 49  ? 0.0476 0.1845 0.0972 0.0309  -0.0270 0.0296  49  THR   A OG1 
294  C  CG2 . THR   A 49  ? 0.0890 0.1807 0.1181 0.0068  -0.0215 0.0095  49  THR   A CG2 
295  N  N   . SER   A 50  ? 0.0455 0.1559 0.1540 -0.0022 -0.0226 -0.0204 50  SER   A N   
296  C  CA  . SER   A 50  ? 0.1003 0.1937 0.0872 -0.0299 -0.0416 -0.0086 50  SER   A CA  
297  C  C   . SER   A 50  ? 0.0494 0.1580 0.1429 -0.0340 -0.0312 0.0280  50  SER   A C   
298  O  O   . SER   A 50  ? 0.0388 0.1569 0.1239 -0.0256 -0.0341 0.0333  50  SER   A O   
299  C  CB  . SER   A 50  ? 0.0889 0.2043 0.1309 -0.0204 -0.0182 -0.0006 50  SER   A CB  
300  O  OG  . SER   A 50  ? 0.0989 0.2136 0.1094 0.0084  -0.0037 -0.0155 50  SER   A OG  
301  N  N   . GLU   A 51  ? 0.0843 0.1742 0.1295 -0.0443 -0.0060 -0.0049 51  GLU   A N   
302  C  CA  . GLU   A 51  ? 0.1258 0.2473 0.1431 -0.0074 -0.0274 -0.0258 51  GLU   A CA  
303  C  C   . GLU   A 51  ? 0.1131 0.2186 0.1334 -0.0157 -0.0730 0.0088  51  GLU   A C   
304  O  O   . GLU   A 51  ? 0.0851 0.2499 0.1632 -0.0059 -0.0904 -0.0068 51  GLU   A O   
305  C  CB  . GLU   A 51  ? 0.2078 0.2315 0.2165 -0.0204 -0.0619 -0.0329 51  GLU   A CB  
306  C  CG  . GLU   A 51  ? 0.2775 0.3255 0.2339 0.0000  -0.0133 -0.0287 51  GLU   A CG  
307  C  CD  . GLU   A 51  ? 0.3011 0.3305 0.3032 -0.0365 -0.0727 -0.0785 51  GLU   A CD  
308  O  OE1 . GLU   A 51  ? 0.0952 0.3332 0.4357 -0.0137 -0.1691 0.0483  51  GLU   A OE1 
309  O  OE2 . GLU   A 51  ? 0.3770 0.4419 0.3441 -0.0763 -0.0043 0.0074  51  GLU   A OE2 
310  N  N   . SER   A 52  ? 0.1415 0.2014 0.1239 0.0546  -0.0606 0.0356  52  SER   A N   
311  C  CA  . SER   A 52  ? 0.1632 0.1674 0.1591 -0.0226 -0.0351 -0.0155 52  SER   A CA  
312  C  C   . SER   A 52  ? 0.0564 0.1662 0.1015 -0.0182 -0.0040 0.0008  52  SER   A C   
313  O  O   . SER   A 52  ? 0.0274 0.1813 0.1184 -0.0170 0.0072  -0.0261 52  SER   A O   
314  C  CB  . SER   A 52  ? 0.1750 0.2401 0.2728 0.0015  0.0206  0.0042  52  SER   A CB  
315  O  OG  . SER   A 52  ? 0.2749 0.2913 0.2736 0.0958  0.0738  0.0943  52  SER   A OG  
316  N  N   . GLY   A 53  ? 0.0327 0.1470 0.1064 -0.0273 0.0089  0.0056  53  GLY   A N   
317  C  CA  . GLY   A 53  ? 0.0471 0.1507 0.0797 -0.0256 -0.0176 0.0091  53  GLY   A CA  
318  C  C   . GLY   A 53  ? 0.0504 0.1314 0.1210 0.0063  -0.0140 0.0367  53  GLY   A C   
319  O  O   . GLY   A 53  ? 0.0318 0.1850 0.1191 -0.0252 -0.0218 0.0489  53  GLY   A O   
320  N  N   . GLU   A 54  ? 0.0704 0.1169 0.1680 -0.0186 -0.0791 0.0149  54  GLU   A N   
321  C  CA  . GLU   A 54  ? 0.0536 0.1633 0.1433 -0.0031 -0.0395 0.0306  54  GLU   A CA  
322  C  C   . GLU   A 54  ? 0.0589 0.1408 0.1623 -0.0369 -0.0308 0.0483  54  GLU   A C   
323  O  O   . GLU   A 54  ? 0.0604 0.1835 0.1585 0.0015  0.0204  0.0661  54  GLU   A O   
324  C  CB  . GLU   A 54  ? 0.0967 0.2429 0.1631 0.0085  -0.0709 -0.0165 54  GLU   A CB  
325  C  CG  . GLU   A 54  ? 0.1531 0.2703 0.1639 -0.0191 -0.0366 -0.0132 54  GLU   A CG  
326  C  CD  . GLU   A 54  ? 0.2803 0.3405 0.2174 0.0952  -0.0231 -0.0065 54  GLU   A CD  
327  O  OE1 . GLU   A 54  ? 0.2421 0.2367 0.4367 0.0437  0.0684  0.0192  54  GLU   A OE1 
328  O  OE2 . GLU   A 54  ? 0.4395 0.4697 0.1572 0.1309  -0.0597 -0.0336 54  GLU   A OE2 
329  N  N   . LEU   A 55  ? 0.0579 0.1430 0.1124 -0.0465 -0.0093 0.0304  55  LEU   A N   
330  C  CA  . LEU   A 55  ? 0.0563 0.1540 0.1439 -0.0450 -0.0143 0.0806  55  LEU   A CA  
331  C  C   . LEU   A 55  ? 0.0838 0.2029 0.1925 -0.0041 0.0244  0.0288  55  LEU   A C   
332  O  O   . LEU   A 55  ? 0.0597 0.2056 0.1717 0.0157  0.0158  0.0479  55  LEU   A O   
333  C  CB  . LEU   A 55  ? 0.0584 0.1945 0.1506 -0.0698 -0.0126 0.0490  55  LEU   A CB  
334  C  CG  . LEU   A 55  ? 0.1023 0.1959 0.1375 -0.0061 -0.0166 -0.0018 55  LEU   A CG  
335  C  CD1 . LEU   A 55  ? 0.1745 0.1983 0.1573 -0.0312 -0.0540 -0.0138 55  LEU   A CD1 
336  C  CD2 . LEU   A 55  ? 0.1478 0.2272 0.1292 -0.0041 -0.0482 -0.0344 55  LEU   A CD2 
337  N  N   . HIS   A 56  ? 0.1377 0.2137 0.2276 0.0124  -0.0616 0.0431  56  HIS   A N   
338  C  CA  . HIS   A 56  ? 0.2708 0.2319 0.1931 0.0927  -0.0602 0.0239  56  HIS   A CA  
339  C  C   . HIS   A 56  ? 0.2673 0.3374 0.2517 0.0274  -0.1060 0.1182  56  HIS   A C   
340  O  O   . HIS   A 56  ? 0.3216 0.4050 0.2612 0.0256  -0.0858 0.0415  56  HIS   A O   
341  C  CB  . HIS   A 56  ? 0.2591 0.2790 0.2493 0.1864  -0.0250 0.0007  56  HIS   A CB  
342  C  CG  . HIS   A 56  ? 0.2987 0.4271 0.2520 0.1417  0.1337  0.0095  56  HIS   A CG  
343  N  ND1 . HIS   A 56  ? 0.4681 0.4776 0.2450 0.1430  0.0620  0.0095  56  HIS   A ND1 
344  C  CD2 . HIS   A 56  ? 0.2911 0.4186 0.2076 0.1173  0.0924  0.0923  56  HIS   A CD2 
345  C  CE1 . HIS   A 56  ? 0.2508 0.5136 0.2690 0.2213  0.1672  -0.0059 56  HIS   A CE1 
346  N  NE2 . HIS   A 56  ? 0.3257 0.8776 0.2000 0.0768  0.1410  0.2018  56  HIS   A NE2 
347  N  N   . GLY   A 57  ? 0.1901 0.3956 0.2382 -0.0772 -0.1380 0.0468  57  GLY   A N   
348  C  CA  . GLY   A 57  ? 0.1257 0.3389 0.2429 -0.0496 -0.0612 0.0590  57  GLY   A CA  
349  C  C   . GLY   A 57  ? 0.1218 0.3095 0.1898 -0.0037 -0.0247 0.0757  57  GLY   A C   
350  O  O   . GLY   A 57  ? 0.1531 0.3581 0.2221 -0.0783 -0.0208 0.1094  57  GLY   A O   
351  N  N   . LEU   A 58  ? 0.1014 0.3003 0.1666 0.0720  -0.0269 0.0894  58  LEU   A N   
352  C  CA  . LEU   A 58  ? 0.1718 0.2943 0.2121 0.0169  0.0231  0.0684  58  LEU   A CA  
353  C  C   . LEU   A 58  ? 0.1634 0.2967 0.1948 0.0002  0.0341  0.0863  58  LEU   A C   
354  O  O   . LEU   A 58  ? 0.2039 0.3125 0.1736 0.0204  0.0034  0.1347  58  LEU   A O   
355  C  CB  . LEU   A 58  ? 0.0858 0.3132 0.2651 -0.0246 0.0579  0.0575  58  LEU   A CB  
356  C  CG  . LEU   A 58  ? 0.1727 0.3261 0.2280 0.0250  0.0262  0.0034  58  LEU   A CG  
357  C  CD1 . LEU   A 58  ? 0.1043 0.3328 0.2495 0.0191  0.0169  0.0217  58  LEU   A CD1 
358  C  CD2 . LEU   A 58  ? 0.0447 0.3411 0.1972 0.0702  -0.0114 0.0592  58  LEU   A CD2 
359  N  N   . THR   A 59  ? 0.1365 0.2002 0.2580 0.0146  -0.0499 0.1092  59  THR   A N   
360  C  CA  . THR   A 59  ? 0.1332 0.2109 0.1411 -0.0271 -0.0326 0.1020  59  THR   A CA  
361  C  C   . THR   A 59  ? 0.1709 0.2464 0.2054 -0.0073 -0.1383 0.0027  59  THR   A C   
362  O  O   . THR   A 59  ? 0.1270 0.3127 0.1941 -0.0449 -0.1020 -0.0017 59  THR   A O   
363  C  CB  . THR   A 59  ? 0.0852 0.1717 0.1555 0.0329  -0.0473 0.0831  59  THR   A CB  
364  O  OG1 . THR   A 59  ? 0.1717 0.2056 0.1883 0.0238  -0.1122 0.0569  59  THR   A OG1 
365  C  CG2 . THR   A 59  ? 0.1471 0.1743 0.1890 -0.0070 -0.0354 0.1051  59  THR   A CG2 
366  N  N   . THR   A 60  ? 0.1296 0.2541 0.1552 -0.0137 -0.0773 0.0411  60  THR   A N   
367  C  CA  . THR   A 60  ? 0.1128 0.2316 0.2189 -0.0159 -0.0645 0.0166  60  THR   A CA  
368  C  C   . THR   A 60  ? 0.1161 0.2295 0.1553 -0.0086 -0.0287 0.0104  60  THR   A C   
369  O  O   . THR   A 60  ? 0.1309 0.2175 0.1376 -0.0072 -0.0704 0.0104  60  THR   A O   
370  C  CB  . THR   A 60  ? 0.1532 0.2246 0.2448 -0.0459 0.0111  0.0044  60  THR   A CB  
371  O  OG1 . THR   A 60  ? 0.2001 0.3181 0.2419 -0.0187 -0.0681 0.0620  60  THR   A OG1 
372  C  CG2 . THR   A 60  ? 0.1922 0.2064 0.3190 -0.1049 0.0102  -0.0202 60  THR   A CG2 
373  N  N   . GLU   A 61  ? 0.1118 0.2318 0.1043 0.0554  -0.0670 0.0250  61  GLU   A N   
374  C  CA  . GLU   A 61  ? 0.1171 0.3106 0.1456 0.0655  -0.0537 0.0283  61  GLU   A CA  
375  C  C   . GLU   A 61  ? 0.1102 0.2550 0.1600 0.0066  -0.0398 -0.0235 61  GLU   A C   
376  O  O   . GLU   A 61  ? 0.0845 0.3809 0.1630 -0.0659 -0.0541 0.0712  61  GLU   A O   
377  C  CB  . GLU   A 61  ? 0.2785 0.3407 0.0785 0.0270  -0.0169 -0.0758 61  GLU   A CB  
378  N  N   . GLU   A 62  ? 0.0402 0.3224 0.1444 0.0187  -0.0402 0.0032  62  GLU   A N   
379  C  CA  . GLU   A 62  ? 0.2063 0.3094 0.1109 0.0466  -0.0385 0.0374  62  GLU   A CA  
380  C  C   . GLU   A 62  ? 0.0862 0.2816 0.1080 0.0114  0.0068  0.0502  62  GLU   A C   
381  O  O   . GLU   A 62  ? 0.1026 0.4258 0.2253 0.0592  -0.0613 -0.0306 62  GLU   A O   
382  C  CB  . GLU   A 62  ? 0.3000 0.3444 0.1443 0.0194  -0.1480 0.0465  62  GLU   A CB  
383  C  CG  . GLU   A 62  ? 0.3459 0.1628 0.3510 0.0435  -0.0916 0.1246  62  GLU   A CG  
384  C  CD  . GLU   A 62  ? 0.3175 0.2983 0.2536 0.0474  -0.0554 -0.0197 62  GLU   A CD  
385  O  OE1 . GLU   A 62  ? 0.3845 0.2849 0.3583 0.2598  0.0208  -0.0436 62  GLU   A OE1 
386  O  OE2 . GLU   A 62  ? 0.2672 0.3872 0.2096 0.0330  0.0144  0.1080  62  GLU   A OE2 
387  N  N   . GLU   A 63  ? 0.0681 0.2313 0.0788 -0.0335 -0.0478 0.0331  63  GLU   A N   
388  C  CA  . GLU   A 63  ? 0.0314 0.2335 0.1164 -0.0108 -0.0235 0.0403  63  GLU   A CA  
389  C  C   . GLU   A 63  ? 0.0307 0.2387 0.0964 -0.0087 0.0021  0.0241  63  GLU   A C   
390  O  O   . GLU   A 63  ? 0.0470 0.2443 0.1229 -0.0322 -0.0121 0.0164  63  GLU   A O   
391  C  CB  . GLU   A 63  ? 0.0310 0.2062 0.1243 -0.0217 -0.0195 0.0176  63  GLU   A CB  
392  C  CG  . GLU   A 63  ? 0.0601 0.2280 0.1459 -0.0269 -0.0647 0.0442  63  GLU   A CG  
393  C  CD  . GLU   A 63  ? 0.0609 0.2726 0.2640 -0.0669 -0.0214 0.0356  63  GLU   A CD  
394  O  OE1 . GLU   A 63  ? 0.1484 0.4349 0.2651 -0.1493 -0.1342 0.0840  63  GLU   A OE1 
395  O  OE2 . GLU   A 63  ? 0.1026 0.4424 0.2912 0.1030  0.0050  0.0772  63  GLU   A OE2 
396  N  N   . PHE   A 64  ? 0.0657 0.2129 0.0934 0.0251  0.0000  0.0003  64  PHE   A N   
397  C  CA  . PHE   A 64  ? 0.0341 0.2231 0.1081 -0.0375 -0.0163 0.0245  64  PHE   A CA  
398  C  C   . PHE   A 64  ? 0.0358 0.2652 0.1124 -0.0464 -0.0065 -0.0258 64  PHE   A C   
399  O  O   . PHE   A 64  ? 0.0597 0.3690 0.1658 -0.0463 0.0121  -0.0497 64  PHE   A O   
400  C  CB  . PHE   A 64  ? 0.1162 0.2006 0.0769 -0.0402 0.0048  0.0413  64  PHE   A CB  
401  C  CG  . PHE   A 64  ? 0.0656 0.1915 0.1060 -0.0575 -0.0516 0.0389  64  PHE   A CG  
402  C  CD1 . PHE   A 64  ? 0.0640 0.2124 0.1560 -0.0325 0.0079  0.0545  64  PHE   A CD1 
403  C  CD2 . PHE   A 64  ? 0.1388 0.2507 0.1469 -0.0553 0.0040  0.0275  64  PHE   A CD2 
404  C  CE1 . PHE   A 64  ? 0.1069 0.1947 0.1121 -0.0254 0.0293  0.0313  64  PHE   A CE1 
405  C  CE2 . PHE   A 64  ? 0.1213 0.2346 0.1604 -0.0644 0.0399  0.0315  64  PHE   A CE2 
406  C  CZ  . PHE   A 64  ? 0.0801 0.2590 0.1339 -0.0460 0.0410  0.0052  64  PHE   A CZ  
407  N  N   . VAL   A 65  ? 0.0316 0.1573 0.1199 -0.0179 -0.0005 0.0107  65  VAL   A N   
408  C  CA  . VAL   A 65  ? 0.0329 0.1458 0.0589 0.0035  -0.0158 0.0010  65  VAL   A CA  
409  C  C   . VAL   A 65  ? 0.0329 0.1682 0.0961 0.0174  -0.0129 0.0407  65  VAL   A C   
410  O  O   . VAL   A 65  ? 0.0271 0.1663 0.0870 0.0073  -0.0036 0.0630  65  VAL   A O   
411  C  CB  . VAL   A 65  ? 0.0496 0.1457 0.0566 -0.0055 0.0074  0.0243  65  VAL   A CB  
412  C  CG1 . VAL   A 65  ? 0.0722 0.1503 0.1110 0.0256  0.0222  0.0222  65  VAL   A CG1 
413  C  CG2 . VAL   A 65  ? 0.0479 0.1457 0.0650 -0.0104 0.0180  0.0273  65  VAL   A CG2 
414  N  N   . GLU   A 66  ? 0.0274 0.1956 0.1267 0.0189  0.0027  0.0028  66  GLU   A N   
415  C  CA  . GLU   A 66  ? 0.0350 0.1870 0.1172 0.0286  -0.0147 0.0301  66  GLU   A CA  
416  C  C   . GLU   A 66  ? 0.0485 0.1890 0.1155 0.0175  -0.0249 0.0119  66  GLU   A C   
417  O  O   . GLU   A 66  ? 0.0352 0.2384 0.1403 0.0243  0.0051  0.0158  66  GLU   A O   
418  C  CB  . GLU   A 66  ? 0.0271 0.2243 0.2597 -0.0118 0.0108  0.0704  66  GLU   A CB  
419  C  CG  . GLU   A 66  ? 0.0987 0.2470 0.2433 -0.0372 0.0412  0.0812  66  GLU   A CG  
420  C  CD  . GLU   A 66  ? 0.0292 0.2574 0.2179 0.0060  0.0248  0.1266  66  GLU   A CD  
421  O  OE1 . GLU   A 66  ? 0.0532 0.2812 0.2063 -0.0219 0.0401  0.1050  66  GLU   A OE1 
422  O  OE2 . GLU   A 66  ? 0.1138 0.2811 0.1470 0.0141  -0.0028 0.1274  66  GLU   A OE2 
423  N  N   . GLY   A 67  ? 0.0696 0.2075 0.1293 0.0347  -0.0120 0.0280  67  GLY   A N   
424  C  CA  . GLY   A 67  ? 0.1049 0.1811 0.1160 0.0240  -0.0125 0.0314  67  GLY   A CA  
425  C  C   . GLY   A 67  ? 0.0275 0.1804 0.1187 0.0072  -0.0112 0.0304  67  GLY   A C   
426  O  O   . GLY   A 67  ? 0.0314 0.2325 0.1277 0.0071  -0.0235 0.0189  67  GLY   A O   
427  N  N   . ILE   A 68  ? 0.0488 0.1494 0.1213 -0.0132 -0.0309 0.0282  68  ILE   A N   
428  C  CA  . ILE   A 68  ? 0.0266 0.1511 0.0764 -0.0097 0.0022  0.0329  68  ILE   A CA  
429  C  C   . ILE   A 68  ? 0.0267 0.1576 0.0488 -0.0075 0.0017  0.0353  68  ILE   A C   
430  O  O   . ILE   A 68  ? 0.0309 0.2263 0.0404 0.0077  -0.0072 0.0230  68  ILE   A O   
431  C  CB  . ILE   A 68  ? 0.0435 0.1496 0.1157 -0.0089 -0.0149 0.0156  68  ILE   A CB  
432  C  CG1 . ILE   A 68  ? 0.0675 0.2261 0.1897 -0.0368 0.0157  0.0173  68  ILE   A CG1 
433  C  CG2 . ILE   A 68  ? 0.0764 0.1317 0.1710 0.0135  -0.0097 0.0176  68  ILE   A CG2 
434  C  CD1 . ILE   A 68  ? 0.1778 0.2516 0.3044 -0.0161 -0.0573 -0.0221 68  ILE   A CD1 
435  N  N   . TYR   A 69  ? 0.0289 0.1753 0.0713 -0.0211 0.0041  0.0073  69  TYR   A N   
436  C  CA  . TYR   A 69  ? 0.0274 0.1396 0.0693 -0.0120 -0.0089 0.0335  69  TYR   A CA  
437  C  C   . TYR   A 69  ? 0.0253 0.1503 0.0786 -0.0013 0.0001  0.0402  69  TYR   A C   
438  O  O   . TYR   A 69  ? 0.0306 0.1787 0.0922 0.0069  0.0179  0.0534  69  TYR   A O   
439  C  CB  . TYR   A 69  ? 0.0456 0.1477 0.0930 0.0149  0.0073  0.0134  69  TYR   A CB  
440  C  CG  . TYR   A 69  ? 0.0584 0.1331 0.0989 0.0098  0.0157  0.0259  69  TYR   A CG  
441  C  CD1 . TYR   A 69  ? 0.0596 0.1268 0.1177 -0.0095 0.0450  0.0448  69  TYR   A CD1 
442  C  CD2 . TYR   A 69  ? 0.0543 0.1282 0.1058 -0.0113 -0.0100 0.0247  69  TYR   A CD2 
443  C  CE1 . TYR   A 69  ? 0.0930 0.1318 0.0983 0.0240  0.0545  0.0088  69  TYR   A CE1 
444  C  CE2 . TYR   A 69  ? 0.0689 0.1460 0.1671 0.0069  0.0666  0.0756  69  TYR   A CE2 
445  C  CZ  . TYR   A 69  ? 0.0722 0.1258 0.1192 0.0424  0.0346  0.0385  69  TYR   A CZ  
446  O  OH  . TYR   A 69  ? 0.0343 0.1754 0.1602 0.0349  0.0105  0.0824  69  TYR   A OH  
447  N  N   . LYS   A 70  ? 0.0395 0.1897 0.0505 0.0359  0.0064  0.0408  70  LYS   A N   
448  C  CA  . LYS   A 70  ? 0.0401 0.1579 0.1179 0.0110  -0.0310 0.0353  70  LYS   A CA  
449  C  C   . LYS   A 70  ? 0.0342 0.1791 0.0838 0.0089  -0.0206 0.0177  70  LYS   A C   
450  O  O   . LYS   A 70  ? 0.0359 0.2392 0.1225 -0.0005 -0.0300 0.0527  70  LYS   A O   
451  C  CB  . LYS   A 70  ? 0.0377 0.1632 0.1112 0.0021  -0.0306 0.0326  70  LYS   A CB  
452  C  CG  . LYS   A 70  ? 0.0654 0.2400 0.1767 0.0467  -0.0450 0.0355  70  LYS   A CG  
453  C  CD  . LYS   A 70  ? 0.0871 0.2773 0.2601 0.0872  -0.0195 0.0000  70  LYS   A CD  
454  C  CE  . LYS   A 70  ? 0.2445 0.3328 0.3161 0.0089  -0.0188 0.0691  70  LYS   A CE  
455  N  NZ  . LYS   A 70  ? 0.2292 0.3238 0.3778 -0.0191 -0.0085 0.0765  70  LYS   A NZ  
456  N  N   . VAL   A 71  ? 0.0258 0.1707 0.0783 -0.0078 -0.0019 0.0610  71  VAL   A N   
457  C  CA  . VAL   A 71  ? 0.0583 0.1433 0.1297 -0.0317 -0.0035 0.0571  71  VAL   A CA  
458  C  C   . VAL   A 71  ? 0.0718 0.1476 0.1318 -0.0168 0.0146  0.0532  71  VAL   A C   
459  O  O   . VAL   A 71  ? 0.0358 0.2038 0.2121 -0.0424 -0.0223 0.1224  71  VAL   A O   
460  C  CB  . VAL   A 71  ? 0.0768 0.1341 0.1475 -0.0507 0.0204  0.0418  71  VAL   A CB  
461  C  CG1 . VAL   A 71  ? 0.0853 0.1811 0.1853 -0.0703 0.0129  0.0492  71  VAL   A CG1 
462  C  CG2 . VAL   A 71  ? 0.0708 0.1816 0.1563 -0.0289 0.0157  0.0191  71  VAL   A CG2 
463  N  N   . GLU   A 72  ? 0.0410 0.1705 0.2038 -0.0236 0.0202  0.0607  72  GLU   A N   
464  C  CA  . GLU   A 72  ? 0.0445 0.1581 0.1802 -0.0148 -0.0015 0.0205  72  GLU   A CA  
465  C  C   . GLU   A 72  ? 0.0287 0.1866 0.1662 0.0016  -0.0213 0.0222  72  GLU   A C   
466  O  O   . GLU   A 72  ? 0.0432 0.2523 0.2305 -0.0065 -0.0575 0.0887  72  GLU   A O   
467  C  CB  . GLU   A 72  ? 0.1266 0.2482 0.1291 -0.0219 -0.0557 0.0234  72  GLU   A CB  
468  C  CG  . GLU   A 72  ? 0.2462 0.2633 0.2208 -0.0588 -0.0199 -0.0295 72  GLU   A CG  
469  C  CD  . GLU   A 72  ? 0.2580 0.3047 0.2687 0.0739  0.0261  0.0287  72  GLU   A CD  
470  O  OE1 . GLU   A 72  ? 0.2782 0.4086 0.2825 0.0792  0.0765  0.0490  72  GLU   A OE1 
471  O  OE2 . GLU   A 72  ? 0.3488 0.2613 0.4778 0.1002  0.0214  0.0280  72  GLU   A OE2 
472  N  N   . ILE   A 73  ? 0.0322 0.1929 0.1603 -0.0340 -0.0066 0.0407  73  ILE   A N   
473  C  CA  . ILE   A 73  ? 0.0462 0.1385 0.1130 0.0121  -0.0347 0.0361  73  ILE   A CA  
474  C  C   . ILE   A 73  ? 0.0691 0.1168 0.1194 0.0004  -0.0097 0.0212  73  ILE   A C   
475  O  O   . ILE   A 73  ? 0.0644 0.1291 0.1965 -0.0248 -0.0182 0.0394  73  ILE   A O   
476  C  CB  . ILE   A 73  ? 0.0713 0.1235 0.1086 0.0235  -0.0141 0.0321  73  ILE   A CB  
477  C  CG1 . ILE   A 73  ? 0.1047 0.1741 0.1245 0.0443  0.0061  0.0086  73  ILE   A CG1 
478  C  CG2 . ILE   A 73  ? 0.0998 0.1519 0.0953 0.0083  -0.0199 0.0302  73  ILE   A CG2 
479  C  CD1 . ILE   A 73  ? 0.1255 0.2222 0.1241 0.0241  -0.0133 0.0382  73  ILE   A CD1 
480  N  N   . ASP   A 74  ? 0.0315 0.1468 0.1570 0.0031  -0.0270 0.0260  74  ASP   A N   
481  C  CA  . ASP   A 74  ? 0.0641 0.2083 0.1741 0.0505  -0.0139 0.0297  74  ASP   A CA  
482  C  C   . ASP   A 74  ? 0.0665 0.1623 0.1089 -0.0174 -0.0126 0.0203  74  ASP   A C   
483  O  O   . ASP   A 74  ? 0.0522 0.2227 0.1903 -0.0171 -0.0646 0.0847  74  ASP   A O   
484  C  CB  . ASP   A 74  ? 0.0508 0.2214 0.1998 0.0584  -0.0264 0.0352  74  ASP   A CB  
485  C  CG  . ASP   A 74  ? 0.0614 0.3341 0.2209 0.0688  0.0082  0.0462  74  ASP   A CG  
486  O  OD1 . ASP   A 74  ? 0.1699 0.2662 0.2226 -0.0740 0.0353  -0.0375 74  ASP   A OD1 
487  O  OD2 . ASP   A 74  ? 0.0952 0.6856 0.1708 -0.0109 0.0176  0.1728  74  ASP   A OD2 
488  N  N   . THR   A 75  ? 0.0959 0.1756 0.1439 0.0042  -0.0198 0.0467  75  THR   A N   
489  C  CA  . THR   A 75  ? 0.0446 0.1537 0.1278 0.0005  -0.0151 0.0124  75  THR   A CA  
490  C  C   . THR   A 75  ? 0.0630 0.1988 0.0666 0.0319  -0.0300 0.0160  75  THR   A C   
491  O  O   . THR   A 75  ? 0.0641 0.1432 0.1431 0.0128  -0.0523 0.0235  75  THR   A O   
492  C  CB  . THR   A 75  ? 0.1291 0.2007 0.1186 0.0089  0.0068  0.0306  75  THR   A CB  
493  O  OG1 . THR   A 75  ? 0.0309 0.2163 0.1620 -0.0136 -0.0076 0.0492  75  THR   A OG1 
494  C  CG2 . THR   A 75  ? 0.0422 0.1853 0.0519 -0.0373 -0.0108 0.0537  75  THR   A CG2 
495  N  N   . LYS   A 76  ? 0.0376 0.1612 0.0951 0.0005  -0.0099 0.0009  76  LYS   A N   
496  C  CA  . LYS   A 76  ? 0.0713 0.1909 0.1229 0.0208  0.0161  0.0045  76  LYS   A CA  
497  C  C   . LYS   A 76  ? 0.0729 0.1941 0.1334 0.0044  -0.0291 0.0174  76  LYS   A C   
498  O  O   . LYS   A 76  ? 0.0429 0.1960 0.1333 0.0303  0.0052  0.0108  76  LYS   A O   
499  C  CB  . LYS   A 76  ? 0.1208 0.1848 0.1802 -0.0228 -0.0861 -0.0044 76  LYS   A CB  
500  C  CG  . LYS   A 76  ? 0.1510 0.2770 0.2746 0.0036  0.0167  0.0286  76  LYS   A CG  
501  N  N   . SER   A 77  ? 0.0422 0.1678 0.1225 -0.0007 0.0133  0.0114  77  SER   A N   
502  C  CA  . SER   A 77  ? 0.0621 0.2023 0.1237 -0.0303 0.0275  -0.0017 77  SER   A CA  
503  C  C   . SER   A 77  ? 0.0409 0.1702 0.1142 -0.0161 0.0175  0.0128  77  SER   A C   
504  O  O   . SER   A 77  ? 0.0400 0.2079 0.1766 -0.0304 0.0139  0.0052  77  SER   A O   
505  C  CB  . SER   A 77  ? 0.0795 0.2013 0.1518 -0.0081 0.0264  -0.0035 77  SER   A CB  
506  O  OG  . SER   A 77  ? 0.1688 0.3039 0.1335 0.0173  0.0240  0.0090  77  SER   A OG  
507  N  N   . TYR   A 78  ? 0.0509 0.1524 0.0988 0.0203  0.0072  -0.0186 78  TYR   A N   
508  C  CA  . TYR   A 78  ? 0.0520 0.1501 0.0856 0.0286  0.0163  -0.0187 78  TYR   A CA  
509  C  C   . TYR   A 78  ? 0.0418 0.1903 0.0790 0.0179  -0.0067 -0.0235 78  TYR   A C   
510  O  O   . TYR   A 78  ? 0.0291 0.2061 0.1154 -0.0087 0.0185  -0.0279 78  TYR   A O   
511  C  CB  . TYR   A 78  ? 0.0290 0.1541 0.0877 0.0216  -0.0002 0.0110  78  TYR   A CB  
512  C  CG  . TYR   A 78  ? 0.0335 0.1344 0.0911 0.0084  0.0100  0.0043  78  TYR   A CG  
513  C  CD1 . TYR   A 78  ? 0.0464 0.1535 0.0941 -0.0053 -0.0130 -0.0211 78  TYR   A CD1 
514  C  CD2 . TYR   A 78  ? 0.0382 0.1091 0.1056 -0.0099 0.0308  -0.0009 78  TYR   A CD2 
515  C  CE1 . TYR   A 78  ? 0.0793 0.1060 0.0874 -0.0110 -0.0149 -0.0026 78  TYR   A CE1 
516  C  CE2 . TYR   A 78  ? 0.0280 0.1090 0.0972 -0.0136 0.0053  0.0034  78  TYR   A CE2 
517  C  CZ  . TYR   A 78  ? 0.0527 0.1085 0.0861 -0.0130 0.0133  -0.0019 78  TYR   A CZ  
518  O  OH  . TYR   A 78  ? 0.0506 0.1332 0.0777 -0.0216 0.0018  0.0095  78  TYR   A OH  
519  N  N   . TRP   A 79  ? 0.0347 0.1913 0.0797 0.0227  0.0132  0.0054  79  TRP   A N   
520  C  CA  . TRP   A 79  ? 0.0390 0.2000 0.0584 0.0136  -0.0060 0.0058  79  TRP   A CA  
521  C  C   . TRP   A 79  ? 0.0447 0.1951 0.0897 0.0233  0.0046  0.0227  79  TRP   A C   
522  O  O   . TRP   A 79  ? 0.0455 0.2176 0.1207 -0.0024 -0.0055 -0.0161 79  TRP   A O   
523  C  CB  . TRP   A 79  ? 0.0599 0.1937 0.0928 0.0059  0.0263  -0.0301 79  TRP   A CB  
524  C  CG  . TRP   A 79  ? 0.0404 0.1594 0.0980 -0.0347 0.0170  -0.0698 79  TRP   A CG  
525  C  CD1 . TRP   A 79  ? 0.0284 0.1825 0.1390 -0.0222 0.0089  -0.0536 79  TRP   A CD1 
526  C  CD2 . TRP   A 79  ? 0.0261 0.1898 0.0609 -0.0071 0.0048  -0.0191 79  TRP   A CD2 
527  N  NE1 . TRP   A 79  ? 0.0444 0.2033 0.1103 0.0005  -0.0003 -0.0060 79  TRP   A NE1 
528  C  CE2 . TRP   A 79  ? 0.0336 0.1854 0.0933 -0.0095 0.0160  0.0182  79  TRP   A CE2 
529  C  CE3 . TRP   A 79  ? 0.0323 0.2580 0.0958 0.0044  -0.0215 -0.0458 79  TRP   A CE3 
530  C  CZ2 . TRP   A 79  ? 0.0410 0.1880 0.0790 0.0134  -0.0094 0.0203  79  TRP   A CZ2 
531  C  CZ3 . TRP   A 79  ? 0.0421 0.2241 0.0658 -0.0571 -0.0066 0.0106  79  TRP   A CZ3 
532  C  CH2 . TRP   A 79  ? 0.0466 0.1992 0.0725 -0.0199 0.0182  0.0067  79  TRP   A CH2 
533  N  N   . LYS   A 80  ? 0.0265 0.2104 0.1016 -0.0037 0.0084  -0.0112 80  LYS   A N   
534  C  CA  . LYS   A 80  ? 0.0319 0.1942 0.1176 -0.0147 0.0215  0.0068  80  LYS   A CA  
535  C  C   . LYS   A 80  ? 0.0596 0.2020 0.1795 -0.0235 -0.0145 0.0114  80  LYS   A C   
536  O  O   . LYS   A 80  ? 0.0597 0.2110 0.1287 -0.0023 -0.0021 -0.0010 80  LYS   A O   
537  C  CB  . LYS   A 80  ? 0.0408 0.2840 0.1318 0.0088  0.0138  0.0292  80  LYS   A CB  
538  C  CG  . LYS   A 80  ? 0.1296 0.3196 0.2473 0.0185  0.0071  -0.0176 80  LYS   A CG  
539  C  CD  . LYS   A 80  ? 0.2770 0.3743 0.3650 0.0777  -0.0427 0.0226  80  LYS   A CD  
540  N  N   . ALA   A 81  ? 0.0619 0.1755 0.0948 -0.0527 0.0085  0.0268  81  ALA   A N   
541  C  CA  . ALA   A 81  ? 0.0759 0.1943 0.1080 -0.0570 0.0228  0.0363  81  ALA   A CA  
542  C  C   . ALA   A 81  ? 0.0526 0.1765 0.1616 -0.0540 -0.0347 0.0049  81  ALA   A C   
543  O  O   . ALA   A 81  ? 0.0782 0.2652 0.2408 -0.1120 0.0257  -0.0631 81  ALA   A O   
544  C  CB  . ALA   A 81  ? 0.0688 0.2273 0.1507 -0.0261 0.0398  0.0595  81  ALA   A CB  
545  N  N   . LEU   A 82  ? 0.0376 0.2361 0.1085 -0.0341 -0.0010 -0.0122 82  LEU   A N   
546  C  CA  . LEU   A 82  ? 0.0714 0.2528 0.1310 -0.0017 -0.0348 -0.0099 82  LEU   A CA  
547  C  C   . LEU   A 82  ? 0.0656 0.2332 0.1849 -0.0286 0.0033  0.0056  82  LEU   A C   
548  O  O   . LEU   A 82  ? 0.0271 0.3818 0.2265 -0.0125 -0.0173 0.0127  82  LEU   A O   
549  C  CB  . LEU   A 82  ? 0.0853 0.2263 0.1489 -0.0390 -0.0377 -0.0016 82  LEU   A CB  
550  C  CG  . LEU   A 82  ? 0.1354 0.2470 0.1548 -0.0172 -0.0095 -0.0252 82  LEU   A CG  
551  C  CD1 . LEU   A 82  ? 0.1450 0.3186 0.2832 -0.0382 0.0592  -0.0628 82  LEU   A CD1 
552  C  CD2 . LEU   A 82  ? 0.1904 0.2606 0.2640 -0.0236 0.0088  -0.0364 82  LEU   A CD2 
553  N  N   . GLY   A 83  ? 0.0417 0.2402 0.1433 -0.0469 -0.0274 0.0023  83  GLY   A N   
554  C  CA  . GLY   A 83  ? 0.0523 0.2473 0.2097 -0.0212 -0.0530 0.0500  83  GLY   A CA  
555  C  C   . GLY   A 83  ? 0.0937 0.2295 0.3000 -0.0109 -0.0372 0.0674  83  GLY   A C   
556  O  O   . GLY   A 83  ? 0.0260 0.2116 0.2823 -0.0064 0.0087  0.0643  83  GLY   A O   
557  N  N   . ILE   A 84  ? 0.1009 0.2029 0.1410 0.0094  -0.0818 0.0589  84  ILE   A N   
558  C  CA  . ILE   A 84  ? 0.0961 0.1574 0.1473 0.0295  -0.0624 0.0414  84  ILE   A CA  
559  C  C   . ILE   A 84  ? 0.0374 0.2059 0.2146 -0.0246 -0.0427 0.0168  84  ILE   A C   
560  O  O   . ILE   A 84  ? 0.0777 0.2457 0.2354 -0.0039 -0.0203 0.0465  84  ILE   A O   
561  C  CB  . ILE   A 84  ? 0.0552 0.2413 0.2251 -0.0286 0.0007  0.0165  84  ILE   A CB  
562  C  CG1 . ILE   A 84  ? 0.2298 0.3043 0.2398 -0.0195 -0.0182 -0.0580 84  ILE   A CG1 
563  C  CG2 . ILE   A 84  ? 0.0275 0.2238 0.1464 0.0070  0.0120  0.0206  84  ILE   A CG2 
564  C  CD1 . ILE   A 84  ? 0.2291 0.3101 0.3582 0.0816  -0.0504 0.0029  84  ILE   A CD1 
565  N  N   . SER   A 85  ? 0.0460 0.2123 0.2076 0.0427  -0.0154 0.0344  85  SER   A N   
566  C  CA  A SER   A 85  ? 0.1176 0.2606 0.2347 0.0032  -0.0279 0.0176  85  SER   A CA  
567  C  CA  B SER   A 85  ? 0.1181 0.2509 0.2447 -0.0147 -0.0170 0.0231  85  SER   A CA  
568  C  C   . SER   A 85  ? 0.1039 0.3135 0.2978 -0.0666 -0.0559 -0.0164 85  SER   A C   
569  O  O   . SER   A 85  ? 0.1109 0.3804 0.3366 -0.0587 -0.0352 -0.0489 85  SER   A O   
570  C  CB  A SER   A 85  ? 0.2084 0.2516 0.2687 0.0123  -0.0658 -0.0206 85  SER   A CB  
571  C  CB  B SER   A 85  ? 0.1936 0.2370 0.3036 -0.0195 -0.0088 0.0034  85  SER   A CB  
572  O  OG  A SER   A 85  ? 0.2375 0.4154 0.2062 0.0629  -0.0834 -0.0082 85  SER   A OG  
573  O  OG  B SER   A 85  ? 0.2999 0.2840 0.3485 -0.1860 -0.0048 0.0377  85  SER   A OG  
574  N  N   . PRO   A 86  ? 0.0909 0.2112 0.2740 -0.0723 -0.0255 0.0033  86  PRO   A N   
575  C  CA  . PRO   A 86  ? 0.0934 0.2971 0.2846 -0.0874 -0.0564 -0.0818 86  PRO   A CA  
576  C  C   . PRO   A 86  ? 0.1458 0.2059 0.1658 -0.0431 0.0079  -0.0614 86  PRO   A C   
577  O  O   . PRO   A 86  ? 0.0745 0.2945 0.1694 -0.0702 0.0027  -0.0757 86  PRO   A O   
578  C  CB  . PRO   A 86  ? 0.1502 0.2764 0.3543 -0.0220 0.0309  -0.0932 86  PRO   A CB  
579  C  CG  . PRO   A 86  ? 0.1703 0.2142 0.2620 0.0156  -0.0016 -0.0475 86  PRO   A CG  
580  C  CD  . PRO   A 86  ? 0.0994 0.1540 0.2872 -0.0667 0.0036  -0.0740 86  PRO   A CD  
581  N  N   . PHE   A 87  ? 0.1560 0.2289 0.2739 -0.0530 0.0217  -0.0508 87  PHE   A N   
582  C  CA  . PHE   A 87  ? 0.2093 0.2328 0.1535 -0.0251 -0.0099 -0.0792 87  PHE   A CA  
583  C  C   . PHE   A 87  ? 0.2156 0.3204 0.1591 0.0243  0.0070  -0.0947 87  PHE   A C   
584  O  O   . PHE   A 87  ? 0.0293 0.3131 0.1158 0.0244  -0.0167 -0.0489 87  PHE   A O   
585  C  CB  . PHE   A 87  ? 0.1802 0.2645 0.1507 -0.0235 -0.0231 -0.0530 87  PHE   A CB  
586  C  CG  . PHE   A 87  ? 0.1475 0.2921 0.1124 -0.0186 0.0230  -0.0754 87  PHE   A CG  
587  C  CD1 . PHE   A 87  ? 0.2247 0.2147 0.1995 -0.0418 -0.0119 -0.0449 87  PHE   A CD1 
588  C  CD2 . PHE   A 87  ? 0.1448 0.2648 0.4014 -0.1262 -0.0087 -0.1300 87  PHE   A CD2 
589  C  CE1 . PHE   A 87  ? 0.2981 0.2455 0.1970 -0.0625 -0.0390 -0.0329 87  PHE   A CE1 
590  C  CE2 . PHE   A 87  ? 0.3397 0.1542 0.3265 -0.1308 -0.0031 -0.1111 87  PHE   A CE2 
591  C  CZ  . PHE   A 87  ? 0.2891 0.2204 0.4029 -0.1320 -0.0245 -0.2077 87  PHE   A CZ  
592  N  N   . HIS   A 88  ? 0.1976 0.2707 0.1840 -0.0283 0.0657  -0.0474 88  HIS   A N   
593  C  CA  . HIS   A 88  ? 0.2253 0.2774 0.3046 0.0182  0.0416  -0.0370 88  HIS   A CA  
594  C  C   . HIS   A 88  ? 0.1235 0.1606 0.2956 0.0335  -0.0063 -0.0484 88  HIS   A C   
595  O  O   . HIS   A 88  ? 0.0284 0.3466 0.5302 0.0113  -0.0335 0.0765  88  HIS   A O   
596  C  CB  . HIS   A 88  ? 0.1274 0.0895 0.3276 -0.0235 -0.0385 -0.0560 88  HIS   A CB  
597  C  CG  . HIS   A 88  ? 0.1068 0.2326 0.3272 -0.0077 0.0196  -0.0679 88  HIS   A CG  
598  N  ND1 . HIS   A 88  ? 0.1781 0.2883 0.3841 -0.1538 -0.0895 -0.0763 88  HIS   A ND1 
599  C  CD2 . HIS   A 88  ? 0.0609 0.3908 0.3519 -0.0694 0.0757  0.0269  88  HIS   A CD2 
600  C  CE1 . HIS   A 88  ? 0.2690 0.3281 0.3152 -0.0319 0.0105  0.0399  88  HIS   A CE1 
601  N  NE2 . HIS   A 88  ? 0.2319 0.4268 0.3118 -0.0042 0.0591  0.0275  88  HIS   A NE2 
602  N  N   . GLU   A 89  ? 0.1650 0.2392 0.2603 0.0015  0.0128  0.0466  89  GLU   A N   
603  C  CA  . GLU   A 89  ? 0.1844 0.2477 0.2535 -0.0159 -0.0051 0.0520  89  GLU   A CA  
604  C  C   . GLU   A 89  ? 0.0805 0.2671 0.3056 -0.0431 -0.0122 -0.0154 89  GLU   A C   
605  O  O   . GLU   A 89  ? 0.1291 0.2288 0.2738 -0.0450 -0.0413 -0.0218 89  GLU   A O   
606  C  CB  . GLU   A 89  ? 0.2922 0.2816 0.3320 -0.0857 0.0202  -0.0968 89  GLU   A CB  
607  C  CG  . GLU   A 89  ? 0.2506 0.2915 0.3396 -0.0572 -0.0267 -0.1232 89  GLU   A CG  
608  C  CD  . GLU   A 89  ? 0.3085 0.3836 0.4931 0.0305  0.1189  0.0068  89  GLU   A CD  
609  O  OE1 . GLU   A 89  ? 0.2335 0.3363 0.4674 -0.0617 0.1133  -0.0792 89  GLU   A OE1 
610  O  OE2 . GLU   A 89  ? 0.3466 0.4542 0.5799 0.0393  0.0521  -0.0940 89  GLU   A OE2 
611  N  N   . HIS   A 90  ? 0.0808 0.1592 0.1799 -0.0479 -0.0326 -0.0176 90  HIS   A N   
612  C  CA  . HIS   A 90  ? 0.0672 0.1290 0.2306 -0.0307 -0.0726 0.0157  90  HIS   A CA  
613  C  C   . HIS   A 90  ? 0.0651 0.1815 0.3168 -0.0514 -0.0390 0.0342  90  HIS   A C   
614  O  O   . HIS   A 90  ? 0.0645 0.1897 0.5021 -0.0193 0.0415  0.0587  90  HIS   A O   
615  C  CB  . HIS   A 90  ? 0.1653 0.2523 0.2290 0.0144  -0.0816 0.0225  90  HIS   A CB  
616  C  CG  . HIS   A 90  ? 0.3046 0.2367 0.3445 0.0423  -0.0952 -0.0724 90  HIS   A CG  
617  N  ND1 . HIS   A 90  ? 0.3536 0.2276 0.4952 0.0650  -0.0871 -0.1008 90  HIS   A ND1 
618  C  CD2 . HIS   A 90  ? 0.4776 0.4268 0.3355 0.0129  -0.1206 -0.0876 90  HIS   A CD2 
619  C  CE1 . HIS   A 90  ? 0.3206 0.2704 0.4748 0.0456  -0.2073 -0.0393 90  HIS   A CE1 
620  N  NE2 . HIS   A 90  ? 0.4426 0.4683 0.4638 -0.0230 -0.1470 0.0270  90  HIS   A NE2 
621  N  N   . ALA   A 91  ? 0.0406 0.1717 0.3133 -0.0342 0.0238  0.0789  91  ALA   A N   
622  C  CA  . ALA   A 91  ? 0.0725 0.2053 0.2669 -0.0346 0.0299  0.0690  91  ALA   A CA  
623  C  C   . ALA   A 91  ? 0.0296 0.2423 0.4333 -0.0233 0.0046  0.0717  91  ALA   A C   
624  O  O   . ALA   A 91  ? 0.1113 0.3295 0.3922 -0.0469 0.0015  0.1437  91  ALA   A O   
625  C  CB  . ALA   A 91  ? 0.1646 0.1936 0.2954 -0.0378 0.0396  0.0483  91  ALA   A CB  
626  N  N   . GLU   A 92  ? 0.0567 0.3649 0.5629 -0.0861 0.0510  0.0768  92  GLU   A N   
627  C  CA  A GLU   A 92  ? 0.1324 0.2764 0.4910 -0.0090 0.0584  0.0925  92  GLU   A CA  
628  C  CA  B GLU   A 92  ? 0.1268 0.3021 0.5154 0.0138  0.0537  0.0813  92  GLU   A CA  
629  C  C   . GLU   A 92  ? 0.1489 0.3475 0.5842 -0.0206 0.0893  0.0455  92  GLU   A C   
630  O  O   . GLU   A 92  ? 0.3361 0.2894 0.7224 0.1428  0.2281  0.2165  92  GLU   A O   
631  C  CB  A GLU   A 92  ? 0.1954 0.3784 0.4330 -0.0695 0.0026  0.0643  92  GLU   A CB  
632  C  CB  B GLU   A 92  ? 0.3272 0.3986 0.5591 -0.0069 0.0283  0.0138  92  GLU   A CB  
633  C  CG  A GLU   A 92  ? 0.1478 0.4295 0.2584 -0.0861 0.0717  0.1510  92  GLU   A CG  
634  C  CG  B GLU   A 92  ? 0.4458 0.3776 0.5132 -0.0693 0.0351  0.0485  92  GLU   A CG  
635  C  CD  A GLU   A 92  ? 0.2701 0.3069 0.4429 -0.0403 -0.0650 0.0881  92  GLU   A CD  
636  C  CD  B GLU   A 92  ? 0.3599 0.3728 0.4313 -0.0874 -0.1087 -0.1016 92  GLU   A CD  
637  O  OE1 A GLU   A 92  ? 0.5546 0.4445 0.6572 -0.1735 -0.2742 -0.0725 92  GLU   A OE1 
638  O  OE1 B GLU   A 92  ? 0.5044 0.3795 0.1539 0.0966  -0.0653 -0.1330 92  GLU   A OE1 
639  O  OE2 A GLU   A 92  ? 0.3121 0.4046 0.2824 0.0370  -0.1799 0.1691  92  GLU   A OE2 
640  O  OE2 B GLU   A 92  ? 0.3947 0.2378 0.3669 -0.0044 -0.0456 0.0908  92  GLU   A OE2 
641  N  N   . VAL   A 93  ? 0.1025 0.2255 0.3380 -0.0804 -0.0030 0.1252  93  VAL   A N   
642  C  CA  . VAL   A 93  ? 0.1437 0.1988 0.1560 0.0090  -0.0645 0.1028  93  VAL   A CA  
643  C  C   . VAL   A 93  ? 0.0274 0.1247 0.1541 -0.0026 -0.0156 0.0525  93  VAL   A C   
644  O  O   . VAL   A 93  ? 0.0624 0.1973 0.1188 -0.0362 -0.0081 0.0807  93  VAL   A O   
645  C  CB  . VAL   A 93  ? 0.2340 0.2402 0.2904 -0.0001 -0.0348 0.0589  93  VAL   A CB  
646  C  CG1 . VAL   A 93  ? 0.2066 0.3381 0.3276 -0.1440 0.0042  0.0344  93  VAL   A CG1 
647  C  CG2 . VAL   A 93  ? 0.2798 0.1940 0.2859 -0.0400 -0.0564 0.1438  93  VAL   A CG2 
648  N  N   . VAL   A 94  ? 0.0421 0.1300 0.1059 -0.0142 0.0011  0.0303  94  VAL   A N   
649  C  CA  . VAL   A 94  ? 0.0338 0.1267 0.1170 0.0200  0.0128  0.0312  94  VAL   A CA  
650  C  C   . VAL   A 94  ? 0.0298 0.1319 0.1054 -0.0154 0.0116  0.0131  94  VAL   A C   
651  O  O   . VAL   A 94  ? 0.0406 0.1523 0.1109 -0.0016 0.0187  0.0228  94  VAL   A O   
652  C  CB  . VAL   A 94  ? 0.0286 0.1643 0.1381 0.0122  -0.0162 -0.0029 94  VAL   A CB  
653  C  CG1 . VAL   A 94  ? 0.0698 0.1479 0.1024 0.0115  -0.0187 0.0006  94  VAL   A CG1 
654  C  CG2 . VAL   A 94  ? 0.0622 0.1797 0.1627 0.0270  0.0205  -0.0054 94  VAL   A CG2 
655  N  N   . PHE   A 95  ? 0.0494 0.1221 0.0757 -0.0172 0.0255  0.0151  95  PHE   A N   
656  C  CA  . PHE   A 95  ? 0.0416 0.1229 0.0944 0.0006  0.0138  0.0179  95  PHE   A CA  
657  C  C   . PHE   A 95  ? 0.0387 0.1278 0.1043 0.0071  0.0164  0.0193  95  PHE   A C   
658  O  O   . PHE   A 95  ? 0.0283 0.2111 0.1029 0.0125  0.0151  0.0497  95  PHE   A O   
659  C  CB  . PHE   A 95  ? 0.0856 0.1263 0.1098 0.0314  0.0137  0.0015  95  PHE   A CB  
660  C  CG  . PHE   A 95  ? 0.0841 0.1501 0.0582 0.0120  0.0208  -0.0378 95  PHE   A CG  
661  C  CD1 . PHE   A 95  ? 0.0868 0.1776 0.1316 -0.0517 0.0141  -0.0357 95  PHE   A CD1 
662  C  CD2 . PHE   A 95  ? 0.0629 0.1302 0.0908 -0.0008 -0.0261 -0.0032 95  PHE   A CD2 
663  C  CE1 . PHE   A 95  ? 0.1383 0.1837 0.1699 -0.0714 -0.0336 0.0050  95  PHE   A CE1 
664  C  CE2 . PHE   A 95  ? 0.1319 0.1639 0.1274 -0.0126 -0.0030 0.0372  95  PHE   A CE2 
665  C  CZ  . PHE   A 95  ? 0.1259 0.2069 0.1219 -0.0525 -0.0077 0.0096  95  PHE   A CZ  
666  N  N   . THR   A 96  ? 0.0405 0.1890 0.0830 -0.0272 0.0074  0.0404  96  THR   A N   
667  C  CA  . THR   A 96  ? 0.0598 0.1404 0.0985 -0.0220 0.0351  0.0389  96  THR   A CA  
668  C  C   . THR   A 96  ? 0.0272 0.1675 0.0922 -0.0132 0.0047  0.0215  96  THR   A C   
669  O  O   . THR   A 96  ? 0.1085 0.2066 0.0998 -0.0060 0.0387  0.0044  96  THR   A O   
670  C  CB  . THR   A 96  ? 0.0302 0.1632 0.1113 -0.0070 0.0121  0.0446  96  THR   A CB  
671  O  OG1 . THR   A 96  ? 0.0624 0.2053 0.1722 -0.0399 -0.0295 0.0053  96  THR   A OG1 
672  C  CG2 . THR   A 96  ? 0.0679 0.1879 0.1520 0.0366  0.0102  0.0265  96  THR   A CG2 
673  N  N   . ALA   A 97  ? 0.0410 0.1759 0.1056 -0.0005 0.0340  0.0300  97  ALA   A N   
674  C  CA  . ALA   A 97  ? 0.0387 0.1604 0.0969 0.0056  0.0281  0.0526  97  ALA   A CA  
675  C  C   . ALA   A 97  ? 0.0564 0.1786 0.1119 0.0208  0.0117  0.0461  97  ALA   A C   
676  O  O   . ALA   A 97  ? 0.0269 0.2793 0.1262 0.0064  0.0125  0.0729  97  ALA   A O   
677  C  CB  . ALA   A 97  ? 0.0443 0.1402 0.0971 -0.0002 0.0363  0.0159  97  ALA   A CB  
678  N  N   . ASN   A 98  ? 0.0312 0.2263 0.1118 0.0330  0.0155  0.0569  98  ASN   A N   
679  C  CA  . ASN   A 98  ? 0.0784 0.1770 0.1027 0.0298  -0.0162 0.0176  98  ASN   A CA  
680  C  C   . ASN   A 98  ? 0.0821 0.1584 0.1112 0.0292  -0.0205 0.0173  98  ASN   A C   
681  O  O   . ASN   A 98  ? 0.0481 0.2087 0.1962 0.0344  -0.0422 0.0270  98  ASN   A O   
682  C  CB  . ASN   A 98  ? 0.0704 0.1705 0.0903 0.0273  -0.0193 0.0151  98  ASN   A CB  
683  C  CG  . ASN   A 98  ? 0.0799 0.1838 0.1053 -0.0251 0.0296  0.0417  98  ASN   A CG  
684  O  OD1 . ASN   A 98  ? 0.0932 0.3578 0.1007 0.0460  0.0367  0.0457  98  ASN   A OD1 
685  N  ND2 . ASN   A 98  ? 0.0288 0.1988 0.1274 0.0025  -0.0183 0.0202  98  ASN   A ND2 
686  N  N   . ASP   A 99  ? 0.0562 0.1923 0.1330 0.0177  -0.0262 0.0370  99  ASP   A N   
687  C  CA  . ASP   A 99  ? 0.0562 0.2076 0.1183 0.0488  -0.0423 -0.0065 99  ASP   A CA  
688  C  C   . ASP   A 99  ? 0.0271 0.2401 0.1583 -0.0197 0.0012  -0.0302 99  ASP   A C   
689  O  O   . ASP   A 99  ? 0.0278 0.2888 0.1693 0.0015  -0.0033 0.0164  99  ASP   A O   
690  C  CB  . ASP   A 99  ? 0.1258 0.2089 0.1510 0.0310  -0.0502 0.0239  99  ASP   A CB  
691  C  CG  . ASP   A 99  ? 0.0688 0.1932 0.1780 0.0321  -0.0358 0.0220  99  ASP   A CG  
692  O  OD1 . ASP   A 99  ? 0.0749 0.2078 0.1637 -0.0022 -0.0558 0.0301  99  ASP   A OD1 
693  O  OD2 . ASP   A 99  ? 0.0630 0.2228 0.2067 0.0163  0.0584  0.0449  99  ASP   A OD2 
694  N  N   . SER   A 100 ? 0.0284 0.2877 0.1540 0.0221  0.0104  -0.0256 100 SER   A N   
695  C  CA  . SER   A 100 ? 0.0397 0.2660 0.2054 0.0383  0.0443  0.0397  100 SER   A CA  
696  C  C   . SER   A 100 ? 0.0585 0.2461 0.1571 0.0805  0.0423  0.0578  100 SER   A C   
697  O  O   . SER   A 100 ? 0.1283 0.4067 0.1575 0.0199  0.0756  -0.0858 100 SER   A O   
698  C  CB  . SER   A 100 ? 0.1212 0.2535 0.2502 0.0128  0.0995  0.0624  100 SER   A CB  
699  O  OG  . SER   A 100 ? 0.2697 0.2695 0.3220 0.0184  0.0483  0.0399  100 SER   A OG  
700  N  N   . GLY   A 101 ? 0.0700 0.2309 0.1430 0.0118  -0.0088 0.0452  101 GLY   A N   
701  C  CA  . GLY   A 101 ? 0.0867 0.1968 0.1762 0.0073  -0.0316 0.0511  101 GLY   A CA  
702  C  C   . GLY   A 101 ? 0.0848 0.2120 0.1604 0.0155  -0.0244 0.0521  101 GLY   A C   
703  O  O   . GLY   A 101 ? 0.0265 0.1869 0.1356 0.0138  0.0031  0.0025  101 GLY   A O   
704  N  N   . PRO   A 102 ? 0.0370 0.2149 0.1359 -0.0046 -0.0355 0.0361  102 PRO   A N   
705  C  CA  . PRO   A 102 ? 0.0308 0.1921 0.1251 -0.0046 -0.0021 0.0025  102 PRO   A CA  
706  C  C   . PRO   A 102 ? 0.0578 0.1973 0.1264 0.0406  -0.0003 -0.0032 102 PRO   A C   
707  O  O   . PRO   A 102 ? 0.0598 0.2673 0.1100 0.0193  -0.0019 -0.0177 102 PRO   A O   
708  C  CB  . PRO   A 102 ? 0.0978 0.2175 0.1244 0.0080  -0.0184 0.0313  102 PRO   A CB  
709  C  CG  . PRO   A 102 ? 0.0898 0.2285 0.2281 -0.0015 -0.0382 0.0570  102 PRO   A CG  
710  C  CD  . PRO   A 102 ? 0.0276 0.2256 0.2266 0.0191  -0.0075 0.0280  102 PRO   A CD  
711  N  N   . ARG   A 103 ? 0.0395 0.2148 0.1147 0.0289  0.0051  0.0030  103 ARG   A N   
712  C  CA  . ARG   A 103 ? 0.0560 0.2198 0.1583 0.0277  -0.0337 0.0176  103 ARG   A CA  
713  C  C   . ARG   A 103 ? 0.0674 0.2432 0.0853 0.0424  0.0140  0.0250  103 ARG   A C   
714  O  O   . ARG   A 103 ? 0.0570 0.2452 0.0748 0.0476  0.0001  0.0349  103 ARG   A O   
715  C  CB  . ARG   A 103 ? 0.0512 0.2210 0.1376 0.0282  0.0037  0.0344  103 ARG   A CB  
716  C  CG  . ARG   A 103 ? 0.0937 0.2218 0.1316 -0.0119 -0.0438 0.0194  103 ARG   A CG  
717  C  CD  . ARG   A 103 ? 0.0967 0.2420 0.1819 0.0165  0.0113  0.0666  103 ARG   A CD  
718  N  NE  . ARG   A 103 ? 0.1086 0.2743 0.2282 -0.0060 0.0640  0.0431  103 ARG   A NE  
719  C  CZ  . ARG   A 103 ? 0.1398 0.3339 0.3872 0.0115  0.0006  0.0466  103 ARG   A CZ  
720  N  NH1 . ARG   A 103 ? 0.0719 0.4152 0.3485 -0.0839 -0.0388 0.0877  103 ARG   A NH1 
721  N  NH2 . ARG   A 103 ? 0.0872 0.4680 0.4663 0.0699  0.1134  0.0305  103 ARG   A NH2 
722  N  N   . ARG   A 104 ? 0.0329 0.2162 0.1038 0.0114  0.0090  -0.0298 104 ARG   A N   
723  C  CA  . ARG   A 104 ? 0.0318 0.1916 0.1405 0.0008  0.0267  0.0322  104 ARG   A CA  
724  C  C   . ARG   A 104 ? 0.0302 0.1800 0.1139 -0.0276 -0.0034 0.0206  104 ARG   A C   
725  O  O   . ARG   A 104 ? 0.1008 0.2191 0.1098 0.0962  0.0380  0.0460  104 ARG   A O   
726  C  CB  . ARG   A 104 ? 0.2377 0.1924 0.2303 0.0199  0.0005  -0.0092 104 ARG   A CB  
727  C  CG  . ARG   A 104 ? 0.1925 0.2102 0.3548 0.0084  0.0518  0.0160  104 ARG   A CG  
728  C  CD  . ARG   A 104 ? 0.4513 0.1683 0.3535 -0.0021 0.1570  -0.0518 104 ARG   A CD  
729  N  N   . TYR   A 105 ? 0.0572 0.1616 0.0665 -0.0173 -0.0021 0.0096  105 TYR   A N   
730  C  CA  . TYR   A 105 ? 0.0351 0.1664 0.1076 -0.0212 -0.0227 0.0172  105 TYR   A CA  
731  C  C   . TYR   A 105 ? 0.0329 0.1567 0.0857 -0.0315 -0.0080 0.0391  105 TYR   A C   
732  O  O   . TYR   A 105 ? 0.0376 0.2264 0.1144 -0.0479 -0.0289 0.0944  105 TYR   A O   
733  C  CB  . TYR   A 105 ? 0.0268 0.1317 0.0931 -0.0004 0.0027  0.0315  105 TYR   A CB  
734  C  CG  . TYR   A 105 ? 0.0328 0.1546 0.0933 0.0139  -0.0152 0.0333  105 TYR   A CG  
735  C  CD1 . TYR   A 105 ? 0.0593 0.1722 0.0819 -0.0096 -0.0079 0.0661  105 TYR   A CD1 
736  C  CD2 . TYR   A 105 ? 0.0695 0.1445 0.1393 0.0244  -0.0462 0.0576  105 TYR   A CD2 
737  C  CE1 . TYR   A 105 ? 0.0721 0.1816 0.1329 0.0020  -0.0528 0.0841  105 TYR   A CE1 
738  C  CE2 . TYR   A 105 ? 0.0632 0.1534 0.0833 -0.0071 -0.0008 0.0352  105 TYR   A CE2 
739  C  CZ  . TYR   A 105 ? 0.0354 0.1735 0.1011 0.0026  -0.0222 0.0304  105 TYR   A CZ  
740  O  OH  . TYR   A 105 ? 0.0286 0.2575 0.0668 0.0129  -0.0100 0.0046  105 TYR   A OH  
741  N  N   . THR   A 106 ? 0.0317 0.1928 0.1037 -0.0241 -0.0209 0.0517  106 THR   A N   
742  C  CA  . THR   A 106 ? 0.0370 0.1626 0.1295 0.0210  -0.0179 0.0376  106 THR   A CA  
743  C  C   . THR   A 106 ? 0.0254 0.1573 0.1097 0.0007  -0.0023 0.0353  106 THR   A C   
744  O  O   . THR   A 106 ? 0.0264 0.1441 0.1149 0.0057  -0.0059 0.0401  106 THR   A O   
745  C  CB  . THR   A 106 ? 0.0577 0.1675 0.1213 0.0000  -0.0148 0.0444  106 THR   A CB  
746  O  OG1 . THR   A 106 ? 0.1295 0.1837 0.2344 -0.0228 0.0001  0.0213  106 THR   A OG1 
747  C  CG2 . THR   A 106 ? 0.0594 0.1445 0.1243 0.0320  -0.0052 0.0009  106 THR   A CG2 
748  N  N   . ILE   A 107 ? 0.0551 0.1175 0.0985 -0.0179 0.0190  0.0131  107 ILE   A N   
749  C  CA  . ILE   A 107 ? 0.0343 0.1236 0.1180 -0.0081 -0.0289 0.0288  107 ILE   A CA  
750  C  C   . ILE   A 107 ? 0.0358 0.1205 0.1056 -0.0018 -0.0262 0.0423  107 ILE   A C   
751  O  O   . ILE   A 107 ? 0.0314 0.1500 0.1251 0.0079  -0.0082 0.0900  107 ILE   A O   
752  C  CB  . ILE   A 107 ? 0.0405 0.1656 0.0821 -0.0317 -0.0086 0.0635  107 ILE   A CB  
753  C  CG1 . ILE   A 107 ? 0.0830 0.1812 0.1000 -0.0543 -0.0517 0.0039  107 ILE   A CG1 
754  C  CG2 . ILE   A 107 ? 0.0922 0.1669 0.1064 -0.0594 0.0306  0.0499  107 ILE   A CG2 
755  C  CD1 . ILE   A 107 ? 0.0919 0.2294 0.1386 -0.0113 0.0171  0.0403  107 ILE   A CD1 
756  N  N   . ALA   A 108 ? 0.0275 0.1428 0.0996 0.0162  0.0046  0.0433  108 ALA   A N   
757  C  CA  . ALA   A 108 ? 0.0444 0.1002 0.0731 -0.0160 -0.0092 0.0202  108 ALA   A CA  
758  C  C   . ALA   A 108 ? 0.0393 0.0953 0.0833 -0.0271 0.0096  0.0035  108 ALA   A C   
759  O  O   . ALA   A 108 ? 0.0274 0.0732 0.1033 -0.0099 0.0022  0.0025  108 ALA   A O   
760  C  CB  . ALA   A 108 ? 0.0424 0.0932 0.0768 -0.0045 -0.0143 0.0097  108 ALA   A CB  
761  N  N   . ALA   A 109 ? 0.0427 0.1073 0.1035 -0.0330 0.0192  -0.0032 109 ALA   A N   
762  C  CA  . ALA   A 109 ? 0.0370 0.0920 0.0667 -0.0178 -0.0100 0.0427  109 ALA   A CA  
763  C  C   . ALA   A 109 ? 0.0470 0.1073 0.0906 -0.0123 -0.0244 0.0059  109 ALA   A C   
764  O  O   . ALA   A 109 ? 0.0344 0.1212 0.0876 -0.0278 -0.0153 0.0272  109 ALA   A O   
765  C  CB  . ALA   A 109 ? 0.0306 0.1196 0.0946 0.0034  0.0183  -0.0100 109 ALA   A CB  
766  N  N   . LEU   A 110 ? 0.0332 0.1201 0.0607 -0.0195 -0.0123 0.0185  110 LEU   A N   
767  C  CA  . LEU   A 110 ? 0.0506 0.0870 0.0560 -0.0175 -0.0247 -0.0007 110 LEU   A CA  
768  C  C   . LEU   A 110 ? 0.0381 0.1037 0.0877 -0.0178 -0.0200 -0.0128 110 LEU   A C   
769  O  O   . LEU   A 110 ? 0.0337 0.0821 0.0958 0.0083  -0.0156 -0.0193 110 LEU   A O   
770  C  CB  . LEU   A 110 ? 0.0438 0.0918 0.0605 -0.0279 -0.0108 -0.0075 110 LEU   A CB  
771  C  CG  . LEU   A 110 ? 0.0854 0.1186 0.0493 0.0091  0.0011  0.0276  110 LEU   A CG  
772  C  CD1 . LEU   A 110 ? 0.0890 0.1670 0.0903 0.0102  -0.0528 0.0121  110 LEU   A CD1 
773  C  CD2 . LEU   A 110 ? 0.0315 0.1095 0.0517 -0.0089 -0.0076 0.0192  110 LEU   A CD2 
774  N  N   . LEU   A 111 ? 0.0482 0.1172 0.0568 -0.0309 -0.0206 0.0025  111 LEU   A N   
775  C  CA  . LEU   A 111 ? 0.0381 0.0960 0.0707 -0.0192 -0.0200 0.0059  111 LEU   A CA  
776  C  C   . LEU   A 111 ? 0.0372 0.1049 0.0775 0.0010  -0.0020 0.0078  111 LEU   A C   
777  O  O   . LEU   A 111 ? 0.0296 0.1637 0.0839 0.0076  -0.0072 -0.0082 111 LEU   A O   
778  C  CB  . LEU   A 111 ? 0.0707 0.0939 0.0749 -0.0087 -0.0022 0.0109  111 LEU   A CB  
779  C  CG  . LEU   A 111 ? 0.0701 0.1163 0.0763 -0.0191 -0.0067 0.0291  111 LEU   A CG  
780  C  CD1 . LEU   A 111 ? 0.0913 0.1806 0.0561 0.0027  0.0150  0.0262  111 LEU   A CD1 
781  C  CD2 . LEU   A 111 ? 0.0429 0.1194 0.0869 0.0016  0.0001  0.0197  111 LEU   A CD2 
782  N  N   . SER   A 112 ? 0.0271 0.1184 0.0553 0.0114  -0.0037 -0.0025 112 SER   A N   
783  C  CA  . SER   A 112 ? 0.0501 0.1190 0.0738 0.0238  -0.0113 0.0122  112 SER   A CA  
784  C  C   . SER   A 112 ? 0.0487 0.1596 0.1100 0.0217  0.0044  -0.0259 112 SER   A C   
785  O  O   . SER   A 112 ? 0.0538 0.1700 0.0882 0.0320  0.0181  -0.0079 112 SER   A O   
786  C  CB  . SER   A 112 ? 0.0770 0.1537 0.0816 0.0004  -0.0134 0.0249  112 SER   A CB  
787  O  OG  . SER   A 112 ? 0.1192 0.1736 0.1217 0.0061  0.0059  -0.0073 112 SER   A OG  
788  N  N   . PRO   A 113 ? 0.0658 0.1276 0.1049 0.0327  0.0022  -0.0192 113 PRO   A N   
789  C  CA  . PRO   A 113 ? 0.0661 0.1789 0.1342 0.0436  0.0501  -0.0101 113 PRO   A CA  
790  C  C   . PRO   A 113 ? 0.0929 0.1609 0.1229 0.0283  0.0643  0.0058  113 PRO   A C   
791  O  O   . PRO   A 113 ? 0.0761 0.2175 0.1211 0.0249  0.0693  0.0192  113 PRO   A O   
792  C  CB  . PRO   A 113 ? 0.0685 0.1878 0.1830 0.0392  0.0266  -0.0190 113 PRO   A CB  
793  C  CG  . PRO   A 113 ? 0.0348 0.1669 0.1614 0.0151  -0.0032 0.0250  113 PRO   A CG  
794  C  CD  . PRO   A 113 ? 0.0591 0.1478 0.1551 0.0403  -0.0031 -0.0270 113 PRO   A CD  
795  N  N   . TYR   A 114 ? 0.0787 0.1947 0.1075 -0.0109 0.0397  0.0143  114 TYR   A N   
796  C  CA  . TYR   A 114 ? 0.0677 0.2031 0.1170 -0.0022 0.0039  0.0032  114 TYR   A CA  
797  C  C   . TYR   A 114 ? 0.1083 0.1589 0.0850 -0.0055 0.0593  0.0037  114 TYR   A C   
798  O  O   . TYR   A 114 ? 0.0866 0.1733 0.1178 -0.0060 0.0489  -0.0357 114 TYR   A O   
799  C  CB  . TYR   A 114 ? 0.0906 0.1973 0.0716 -0.0249 0.0011  -0.0041 114 TYR   A CB  
800  C  CG  . TYR   A 114 ? 0.0548 0.1780 0.1656 -0.0024 -0.0360 -0.0204 114 TYR   A CG  
801  C  CD1 . TYR   A 114 ? 0.0447 0.2073 0.3205 -0.0021 -0.0080 -0.0661 114 TYR   A CD1 
802  C  CD2 . TYR   A 114 ? 0.0827 0.1784 0.1779 0.0599  -0.0303 -0.0240 114 TYR   A CD2 
803  C  CE1 . TYR   A 114 ? 0.0862 0.2326 0.3081 -0.0041 0.0647  0.0050  114 TYR   A CE1 
804  C  CE2 . TYR   A 114 ? 0.0834 0.1507 0.2069 0.0379  0.0015  -0.0037 114 TYR   A CE2 
805  C  CZ  . TYR   A 114 ? 0.0331 0.2735 0.2914 0.0430  0.0065  -0.0187 114 TYR   A CZ  
806  O  OH  . TYR   A 114 ? 0.1821 0.3824 0.4231 0.2336  0.0935  0.0836  114 TYR   A OH  
807  N  N   . SER   A 115 ? 0.0358 0.1455 0.0749 0.0095  -0.0021 0.0131  115 SER   A N   
808  C  CA  . SER   A 115 ? 0.0584 0.1400 0.1111 0.0083  0.0284  -0.0002 115 SER   A CA  
809  C  C   . SER   A 115 ? 0.0432 0.1443 0.1114 0.0139  0.0117  0.0011  115 SER   A C   
810  O  O   . SER   A 115 ? 0.0378 0.1807 0.1384 -0.0040 -0.0005 -0.0020 115 SER   A O   
811  C  CB  . SER   A 115 ? 0.0658 0.1888 0.1239 0.0329  0.0107  0.0363  115 SER   A CB  
812  O  OG  . SER   A 115 ? 0.0525 0.2483 0.2006 0.0396  0.0009  0.0305  115 SER   A OG  
813  N  N   . TYR   A 116 ? 0.0326 0.0992 0.1252 -0.0210 -0.0030 -0.0273 116 TYR   A N   
814  C  CA  . TYR   A 116 ? 0.0324 0.1025 0.1199 -0.0227 -0.0008 -0.0185 116 TYR   A CA  
815  C  C   . TYR   A 116 ? 0.0405 0.0947 0.1092 -0.0014 0.0081  -0.0031 116 TYR   A C   
816  O  O   . TYR   A 116 ? 0.0327 0.1029 0.0999 0.0015  0.0072  -0.0098 116 TYR   A O   
817  C  CB  . TYR   A 116 ? 0.0733 0.1555 0.1250 -0.0107 0.0056  -0.0048 116 TYR   A CB  
818  C  CG  . TYR   A 116 ? 0.1199 0.2022 0.0387 -0.0194 0.0257  0.0280  116 TYR   A CG  
819  C  CD1 . TYR   A 116 ? 0.2269 0.2260 0.0840 -0.0180 -0.0334 -0.0267 116 TYR   A CD1 
820  C  CD2 . TYR   A 116 ? 0.1357 0.2852 0.1593 -0.0103 -0.0392 0.0178  116 TYR   A CD2 
821  C  CE1 . TYR   A 116 ? 0.0777 0.3025 0.1311 0.0375  -0.0650 0.0326  116 TYR   A CE1 
822  C  CE2 . TYR   A 116 ? 0.1328 0.4248 0.0989 -0.0192 -0.0453 0.0627  116 TYR   A CE2 
823  C  CZ  . TYR   A 116 ? 0.0288 0.3397 0.1820 -0.0151 -0.0229 0.0604  116 TYR   A CZ  
824  O  OH  . TYR   A 116 ? 0.3770 0.5688 0.1867 -0.2657 -0.1130 0.1104  116 TYR   A OH  
825  N  N   . SER   A 117 ? 0.0272 0.1114 0.0924 -0.0037 0.0110  -0.0111 117 SER   A N   
826  C  CA  A SER   A 117 ? 0.0280 0.1070 0.1031 -0.0015 0.0144  0.0000  117 SER   A CA  
827  C  CA  B SER   A 117 ? 0.0277 0.1007 0.0779 -0.0036 0.0107  0.0008  117 SER   A CA  
828  C  C   . SER   A 117 ? 0.0371 0.1256 0.1084 -0.0129 -0.0077 0.0295  117 SER   A C   
829  O  O   . SER   A 117 ? 0.0276 0.1262 0.1305 -0.0143 -0.0064 0.0089  117 SER   A O   
830  C  CB  A SER   A 117 ? 0.0841 0.1087 0.1080 0.0033  0.0042  -0.0023 117 SER   A CB  
831  C  CB  B SER   A 117 ? 0.0265 0.0855 0.0788 0.0029  0.0075  -0.0003 117 SER   A CB  
832  O  OG  A SER   A 117 ? 0.1195 0.1264 0.0910 0.0164  -0.0258 -0.0205 117 SER   A OG  
833  O  OG  B SER   A 117 ? 0.0378 0.1297 0.0426 0.0337  0.0014  0.0190  117 SER   A OG  
834  N  N   . THR   A 118 ? 0.0374 0.1534 0.0877 -0.0378 -0.0114 0.0128  118 THR   A N   
835  C  CA  . THR   A 118 ? 0.0411 0.1308 0.0819 -0.0406 0.0025  -0.0135 118 THR   A CA  
836  C  C   . THR   A 118 ? 0.0342 0.1120 0.0663 -0.0100 -0.0158 -0.0131 118 THR   A C   
837  O  O   . THR   A 118 ? 0.0349 0.1199 0.1187 -0.0131 -0.0178 -0.0097 118 THR   A O   
838  C  CB  . THR   A 118 ? 0.0876 0.1632 0.0817 -0.0235 0.0279  -0.0188 118 THR   A CB  
839  O  OG1 . THR   A 118 ? 0.1398 0.1948 0.0904 -0.0187 0.0093  0.0257  118 THR   A OG1 
840  C  CG2 . THR   A 118 ? 0.0963 0.2388 0.1266 -0.0483 -0.0532 0.0008  118 THR   A CG2 
841  N  N   . THR   A 119 ? 0.0266 0.1300 0.0638 -0.0112 0.0034  -0.0160 119 THR   A N   
842  C  CA  . THR   A 119 ? 0.0313 0.1346 0.0590 -0.0067 0.0137  -0.0011 119 THR   A CA  
843  C  C   . THR   A 119 ? 0.0255 0.1388 0.0800 -0.0027 0.0025  -0.0042 119 THR   A C   
844  O  O   . THR   A 119 ? 0.0279 0.1859 0.1044 -0.0043 -0.0143 0.0382  119 THR   A O   
845  C  CB  . THR   A 119 ? 0.0319 0.1404 0.0600 -0.0053 0.0111  0.0016  119 THR   A CB  
846  O  OG1 . THR   A 119 ? 0.0390 0.1770 0.0620 -0.0209 0.0145  0.0282  119 THR   A OG1 
847  C  CG2 . THR   A 119 ? 0.0882 0.1458 0.0811 0.0117  0.0001  -0.0280 119 THR   A CG2 
848  N  N   . ALA   A 120 ? 0.0253 0.1121 0.0795 0.0009  0.0005  0.0004  120 ALA   A N   
849  C  CA  . ALA   A 120 ? 0.0721 0.1148 0.0665 -0.0001 -0.0030 0.0071  120 ALA   A CA  
850  C  C   . ALA   A 120 ? 0.0393 0.1277 0.0715 0.0103  0.0109  0.0349  120 ALA   A C   
851  O  O   . ALA   A 120 ? 0.0258 0.0980 0.1092 0.0057  0.0057  0.0564  120 ALA   A O   
852  C  CB  . ALA   A 120 ? 0.0472 0.1248 0.1107 0.0029  -0.0111 -0.0074 120 ALA   A CB  
853  N  N   . VAL   A 121 ? 0.0330 0.1313 0.1114 -0.0228 0.0111  0.0190  121 VAL   A N   
854  C  CA  . VAL   A 121 ? 0.1142 0.1280 0.0999 0.0112  0.0349  0.0502  121 VAL   A CA  
855  C  C   . VAL   A 121 ? 0.0922 0.1520 0.0882 -0.0009 0.0121  0.0236  121 VAL   A C   
856  O  O   . VAL   A 121 ? 0.0331 0.2152 0.1202 0.0377  0.0187  0.0723  121 VAL   A O   
857  C  CB  . VAL   A 121 ? 0.1184 0.1422 0.1765 0.0138  0.0021  0.0419  121 VAL   A CB  
858  C  CG1 . VAL   A 121 ? 0.1926 0.1740 0.2255 0.0441  0.0253  0.0270  121 VAL   A CG1 
859  C  CG2 . VAL   A 121 ? 0.1455 0.2607 0.2429 0.0187  -0.0791 0.0309  121 VAL   A CG2 
860  N  N   . VAL   A 122 ? 0.0935 0.2161 0.0328 0.0451  0.0159  0.0259  122 VAL   A N   
861  C  CA  . VAL   A 122 ? 0.0952 0.1810 0.1186 0.0422  -0.0132 0.0438  122 VAL   A CA  
862  C  C   . VAL   A 122 ? 0.0472 0.2288 0.0842 0.0429  -0.0184 0.0355  122 VAL   A C   
863  O  O   . VAL   A 122 ? 0.1405 0.2728 0.0911 0.0740  0.0195  0.0440  122 VAL   A O   
864  C  CB  . VAL   A 122 ? 0.1431 0.2395 0.1124 0.0127  -0.0412 0.0254  122 VAL   A CB  
865  C  CG1 . VAL   A 122 ? 0.1347 0.2379 0.1199 0.0590  -0.0058 0.0330  122 VAL   A CG1 
866  C  CG2 . VAL   A 122 ? 0.1149 0.3384 0.0900 0.0758  -0.0448 0.0628  122 VAL   A CG2 
867  N  N   . THR   A 123 ? 0.0949 0.2136 0.1032 0.0690  0.0385  0.0079  123 THR   A N   
868  C  CA  . THR   A 123 ? 0.2105 0.2045 0.1643 0.1109  0.0347  0.0020  123 THR   A CA  
869  C  C   . THR   A 123 ? 0.2102 0.2372 0.1328 0.1140  0.0325  -0.0012 123 THR   A C   
870  O  O   . THR   A 123 ? 0.2231 0.2717 0.1239 0.1074  -0.0118 0.0523  123 THR   A O   
871  C  CB  . THR   A 123 ? 0.2293 0.2301 0.1459 0.1713  0.0113  -0.0732 123 THR   A CB  
872  O  OG1 . THR   A 123 ? 0.2570 0.4686 0.2595 0.0229  0.0557  -0.0556 123 THR   A OG1 
873  C  CG2 . THR   A 123 ? 0.2631 0.2510 0.2802 0.1025  -0.0497 0.0173  123 THR   A CG2 
874  N  N   . ASN   A 124 ? 0.2553 0.2701 0.2271 0.1742  0.0807  0.0624  124 ASN   A N   
875  C  CA  . ASN   A 124 ? 0.2418 0.4108 0.2923 0.0581  -0.0856 0.0318  124 ASN   A CA  
876  C  C   . ASN   A 124 ? 0.4447 0.3580 0.2756 0.1808  0.0448  -0.0149 124 ASN   A C   
877  O  O   . ASN   A 124 ? 0.4859 0.5158 0.4427 0.2351  0.0353  -0.1909 124 ASN   A O   
878  C  CB  . ASN   A 124 ? 0.2648 0.4891 0.3220 0.0900  0.0395  0.0013  124 ASN   A CB  
879  C  CG  . ASN   A 124 ? 0.4864 0.3954 0.4476 0.2067  -0.0719 0.0140  124 ASN   A CG  
880  O  OD1 . ASN   A 124 ? 0.5452 0.4196 0.3492 0.0490  0.0079  -0.0451 124 ASN   A OD1 
881  N  N   . PRO   A 125 ? 0.4490 0.4113 0.4956 0.0833  0.1099  0.0820  125 PRO   A N   
882  C  CA  . PRO   A 125 ? 0.3817 0.4983 0.6274 0.0865  0.0700  -0.0231 125 PRO   A CA  
883  C  C   . PRO   A 125 ? 0.5457 0.3393 0.4649 0.1205  -0.0302 0.0071  125 PRO   A C   
884  O  O   . PRO   A 125 ? 0.4431 0.5299 0.4335 0.0941  0.1358  0.1000  125 PRO   A O   
885  C  CB  . PRO   A 125 ? 0.5526 0.4877 0.6214 0.0213  0.1478  0.0151  125 PRO   A CB  
886  C  CG  . PRO   A 125 ? 0.6319 0.5035 0.4706 -0.0096 0.1545  0.0548  125 PRO   A CG  
887  C  CD  . PRO   A 125 ? 0.4542 0.3888 0.5086 0.0109  0.1129  0.0241  125 PRO   A CD  
888  N  N   . CYS   B 10  ? 0.6904 0.7146 0.6247 0.2204  -0.0737 0.0714  10  CYS   B N   
889  C  CA  . CYS   B 10  ? 0.5066 0.6042 0.4530 -0.1224 0.0011  -0.0044 10  CYS   B CA  
890  C  C   . CYS   B 10  ? 0.2303 0.5417 0.3042 0.0527  0.0941  -0.2216 10  CYS   B C   
891  O  O   . CYS   B 10  ? 0.4361 0.5857 0.3366 0.1219  -0.0384 -0.2159 10  CYS   B O   
892  N  N   . PRO   B 11  ? 0.2614 0.4558 0.4218 -0.0508 0.0323  -0.1674 11  PRO   B N   
893  C  CA  . PRO   B 11  ? 0.2814 0.2917 0.3449 0.0197  -0.0202 -0.2455 11  PRO   B CA  
894  C  C   . PRO   B 11  ? 0.3075 0.1941 0.4207 -0.0074 -0.0607 -0.1348 11  PRO   B C   
895  O  O   . PRO   B 11  ? 0.2145 0.2589 0.4125 -0.0441 0.0466  -0.1398 11  PRO   B O   
896  C  CB  . PRO   B 11  ? 0.4411 0.2007 0.3944 0.0264  0.0472  -0.2160 11  PRO   B CB  
897  C  CG  . PRO   B 11  ? 0.3177 0.5677 0.1846 -0.0044 0.1133  -0.2060 11  PRO   B CG  
898  C  CD  . PRO   B 11  ? 0.3212 0.2599 0.4222 0.1371  0.0107  -0.1432 11  PRO   B CD  
899  N  N   . LEU   B 12  ? 0.2766 0.1967 0.4955 -0.1243 -0.0157 -0.2193 12  LEU   B N   
900  C  CA  . LEU   B 12  ? 0.1361 0.2613 0.2958 -0.1225 0.0006  -0.1657 12  LEU   B CA  
901  C  C   . LEU   B 12  ? 0.0598 0.2164 0.3847 -0.0511 -0.0080 -0.1554 12  LEU   B C   
902  O  O   . LEU   B 12  ? 0.1085 0.3375 0.5186 -0.1203 -0.0361 -0.2029 12  LEU   B O   
903  C  CB  . LEU   B 12  ? 0.1426 0.3459 0.3194 0.0497  0.0211  -0.1302 12  LEU   B CB  
904  C  CG  . LEU   B 12  ? 0.3369 0.2865 0.4509 -0.0377 -0.0069 -0.1316 12  LEU   B CG  
905  C  CD1 . LEU   B 12  ? 0.1486 0.3301 0.3714 0.0041  -0.0817 -0.0435 12  LEU   B CD1 
906  C  CD2 . LEU   B 12  ? 0.1037 0.2708 0.4316 -0.0859 -0.0616 -0.1651 12  LEU   B CD2 
907  N  N   . MET   B 13  ? 0.1230 0.2257 0.3827 -0.1323 0.0925  -0.1435 13  MET   B N   
908  C  CA  . MET   B 13  ? 0.1283 0.1066 0.4900 -0.0674 0.1302  -0.0879 13  MET   B CA  
909  C  C   . MET   B 13  ? 0.0676 0.0953 0.4583 -0.0362 0.0439  -0.0510 13  MET   B C   
910  O  O   . MET   B 13  ? 0.0466 0.1688 0.4257 -0.0548 0.0591  -0.1285 13  MET   B O   
911  C  CB  . MET   B 13  ? 0.3249 0.1113 0.5867 0.0456  0.0737  -0.0834 13  MET   B CB  
912  C  CG  . MET   B 13  ? 0.4098 0.3525 0.5974 0.0572  0.1176  -0.0468 13  MET   B CG  
913  S  SD  . MET   B 13  ? 0.2934 0.5080 0.3981 -0.0228 0.1265  -0.0454 13  MET   B SD  
914  C  CE  . MET   B 13  ? 0.4481 0.4602 0.4707 -0.0323 -0.0464 0.0326  13  MET   B CE  
915  N  N   . VAL   B 14  ? 0.0732 0.2138 0.3751 -0.0603 0.0833  -0.0941 14  VAL   B N   
916  C  CA  . VAL   B 14  ? 0.1120 0.1614 0.2770 -0.0711 -0.0128 -0.0757 14  VAL   B CA  
917  C  C   . VAL   B 14  ? 0.0870 0.1820 0.3273 -0.0181 0.0505  -0.0867 14  VAL   B C   
918  O  O   . VAL   B 14  ? 0.1245 0.2591 0.3429 -0.0779 0.0984  -0.1267 14  VAL   B O   
919  C  CB  . VAL   B 14  ? 0.1949 0.1835 0.2857 0.0035  -0.0347 -0.0512 14  VAL   B CB  
920  C  CG1 . VAL   B 14  ? 0.1194 0.1667 0.2695 -0.0553 -0.0844 -0.0840 14  VAL   B CG1 
921  C  CG2 . VAL   B 14  ? 0.1022 0.1613 0.3739 -0.0805 -0.0797 -0.0327 14  VAL   B CG2 
922  N  N   . LYS   B 15  ? 0.1280 0.2770 0.2483 -0.0167 0.1046  -0.1056 15  LYS   B N   
923  C  CA  . LYS   B 15  ? 0.1779 0.2077 0.2196 -0.0339 0.1009  -0.1008 15  LYS   B CA  
924  C  C   . LYS   B 15  ? 0.0846 0.2148 0.3044 -0.0405 0.1148  -0.0985 15  LYS   B C   
925  O  O   . LYS   B 15  ? 0.2054 0.1758 0.3458 -0.0534 0.1108  -0.1423 15  LYS   B O   
926  C  CB  . LYS   B 15  ? 0.2195 0.2811 0.3453 -0.0158 0.0412  -0.0472 15  LYS   B CB  
927  C  CG  . LYS   B 15  ? 0.2712 0.3489 0.2844 0.0702  0.0029  -0.0320 15  LYS   B CG  
928  C  CD  . LYS   B 15  ? 0.4889 0.4664 0.2207 0.0221  -0.0967 -0.0309 15  LYS   B CD  
929  C  CE  . LYS   B 15  ? 0.4121 0.3371 0.3220 0.0390  -0.0420 -0.0382 15  LYS   B CE  
930  N  NZ  . LYS   B 15  ? 0.4674 0.5880 0.2651 0.0552  -0.1037 -0.0770 15  LYS   B NZ  
931  N  N   . VAL   B 16  ? 0.0530 0.1986 0.2426 -0.0636 0.0558  -0.1338 16  VAL   B N   
932  C  CA  . VAL   B 16  ? 0.0860 0.1669 0.1570 -0.0359 0.0067  -0.0438 16  VAL   B CA  
933  C  C   . VAL   B 16  ? 0.0364 0.1470 0.1495 -0.0340 -0.0027 -0.0341 16  VAL   B C   
934  O  O   . VAL   B 16  ? 0.0973 0.1416 0.1541 -0.0471 0.0484  -0.0450 16  VAL   B O   
935  C  CB  . VAL   B 16  ? 0.1324 0.1798 0.1776 -0.0254 -0.0169 -0.0594 16  VAL   B CB  
936  C  CG1 . VAL   B 16  ? 0.0395 0.1938 0.2104 -0.0186 0.0015  -0.0074 16  VAL   B CG1 
937  C  CG2 . VAL   B 16  ? 0.1069 0.1869 0.1790 -0.0933 -0.0057 -0.0408 16  VAL   B CG2 
938  N  N   . LEU   B 17  ? 0.0369 0.1424 0.1865 -0.0196 0.0277  -0.0408 17  LEU   B N   
939  C  CA  . LEU   B 17  ? 0.1069 0.0853 0.1751 -0.0054 0.0249  -0.0370 17  LEU   B CA  
940  C  C   . LEU   B 17  ? 0.0353 0.1250 0.1958 0.0071  0.0111  0.0185  17  LEU   B C   
941  O  O   . LEU   B 17  ? 0.0509 0.1254 0.2272 -0.0168 0.0266  0.0180  17  LEU   B O   
942  C  CB  . LEU   B 17  ? 0.0446 0.1349 0.1888 0.0233  0.0461  0.0120  17  LEU   B CB  
943  C  CG  . LEU   B 17  ? 0.1014 0.1571 0.2105 0.0400  -0.0319 0.0580  17  LEU   B CG  
944  C  CD1 . LEU   B 17  ? 0.1657 0.1838 0.1780 0.0146  -0.0247 0.0139  17  LEU   B CD1 
945  C  CD2 . LEU   B 17  ? 0.1757 0.1723 0.2030 0.0018  0.0304  -0.0084 17  LEU   B CD2 
946  N  N   . ASP   B 18  ? 0.1056 0.1012 0.1407 -0.0007 0.0369  0.0099  18  ASP   B N   
947  C  CA  . ASP   B 18  ? 0.0467 0.0891 0.1026 -0.0314 0.0195  0.0033  18  ASP   B CA  
948  C  C   . ASP   B 18  ? 0.0303 0.0980 0.0931 0.0117  0.0157  0.0080  18  ASP   B C   
949  O  O   . ASP   B 18  ? 0.1156 0.1342 0.0842 -0.0144 0.0048  0.0067  18  ASP   B O   
950  C  CB  . ASP   B 18  ? 0.0523 0.1188 0.1119 -0.0428 0.0100  -0.0062 18  ASP   B CB  
951  C  CG  . ASP   B 18  ? 0.0454 0.1191 0.1505 -0.0266 -0.0012 0.0000  18  ASP   B CG  
952  O  OD1 . ASP   B 18  ? 0.0301 0.1855 0.1480 -0.0234 0.0164  -0.0226 18  ASP   B OD1 
953  O  OD2 . ASP   B 18  ? 0.0614 0.2126 0.1902 -0.0710 -0.0014 -0.0120 18  ASP   B OD2 
954  N  N   . ALA   B 19  ? 0.0282 0.1024 0.1211 0.0142  -0.0068 -0.0078 19  ALA   B N   
955  C  CA  . ALA   B 19  ? 0.0898 0.0606 0.0870 0.0250  -0.0118 0.0189  19  ALA   B CA  
956  C  C   . ALA   B 19  ? 0.0786 0.1034 0.1113 0.0036  0.0099  0.0052  19  ALA   B C   
957  O  O   . ALA   B 19  ? 0.1300 0.1730 0.1077 0.0108  0.0150  -0.0161 19  ALA   B O   
958  C  CB  . ALA   B 19  ? 0.0293 0.1026 0.0850 0.0024  -0.0154 -0.0099 19  ALA   B CB  
959  N  N   . VAL   B 20  ? 0.0827 0.1109 0.1209 0.0012  0.0089  -0.0036 20  VAL   B N   
960  C  CA  . VAL   B 20  ? 0.1006 0.1085 0.1465 0.0472  0.0230  0.0311  20  VAL   B CA  
961  C  C   . VAL   B 20  ? 0.1215 0.1365 0.1577 0.0266  0.0251  0.0269  20  VAL   B C   
962  O  O   . VAL   B 20  ? 0.2394 0.2484 0.1825 0.0196  0.0996  0.0481  20  VAL   B O   
963  C  CB  . VAL   B 20  ? 0.0846 0.1794 0.1617 0.0572  0.0312  0.0306  20  VAL   B CB  
964  C  CG1 . VAL   B 20  ? 0.1349 0.2086 0.2216 0.0335  0.1269  0.0777  20  VAL   B CG1 
965  C  CG2 . VAL   B 20  ? 0.1776 0.1850 0.1763 0.0343  0.0169  0.0477  20  VAL   B CG2 
966  N  N   . ARG   B 21  ? 0.1226 0.1766 0.1737 -0.0275 0.0482  0.0180  21  ARG   B N   
967  C  CA  . ARG   B 21  ? 0.2064 0.1503 0.0660 0.0180  0.0818  0.0110  21  ARG   B CA  
968  C  C   . ARG   B 21  ? 0.1987 0.1754 0.0964 -0.0069 0.0786  0.0504  21  ARG   B C   
969  O  O   . ARG   B 21  ? 0.2737 0.2102 0.1062 -0.0712 0.0285  0.0744  21  ARG   B O   
970  C  CB  . ARG   B 21  ? 0.1387 0.1773 0.2072 -0.0082 0.0318  0.0207  21  ARG   B CB  
971  C  CG  . ARG   B 21  ? 0.1768 0.2692 0.2138 0.0696  0.0621  -0.0103 21  ARG   B CG  
972  C  CD  . ARG   B 21  ? 0.2428 0.2638 0.3188 0.0541  0.0635  -0.0527 21  ARG   B CD  
973  N  NE  . ARG   B 21  ? 0.0863 0.2957 0.2942 -0.0001 0.0456  -0.0337 21  ARG   B NE  
974  C  CZ  . ARG   B 21  ? 0.2500 0.3019 0.4232 -0.0233 0.0451  -0.0773 21  ARG   B CZ  
975  N  NH1 . ARG   B 21  ? 0.2743 0.3670 0.4033 -0.1165 -0.0206 -0.0697 21  ARG   B NH1 
976  N  NH2 . ARG   B 21  ? 0.3557 0.3653 0.2621 0.0176  0.0363  0.0436  21  ARG   B NH2 
977  N  N   . GLY   B 22  ? 0.1980 0.1408 0.2127 -0.0157 0.0592  0.1194  22  GLY   B N   
978  C  CA  . GLY   B 22  ? 0.1058 0.1821 0.2039 -0.0347 0.0457  0.0816  22  GLY   B CA  
979  C  C   . GLY   B 22  ? 0.0658 0.2167 0.1912 -0.0012 0.0416  0.0229  22  GLY   B C   
980  O  O   . GLY   B 22  ? 0.1720 0.2148 0.2272 -0.0732 -0.0029 0.0366  22  GLY   B O   
981  N  N   . SER   B 23  ? 0.1253 0.1842 0.1828 -0.0481 0.0748  0.0086  23  SER   B N   
982  C  CA  . SER   B 23  ? 0.1684 0.2132 0.2415 -0.0104 0.0285  -0.0394 23  SER   B CA  
983  C  C   . SER   B 23  ? 0.1544 0.1756 0.2059 -0.0692 0.0170  -0.0101 23  SER   B C   
984  O  O   . SER   B 23  ? 0.1354 0.1365 0.2346 -0.0206 -0.0207 0.0178  23  SER   B O   
985  C  CB  . SER   B 23  ? 0.1608 0.2958 0.3343 -0.0295 0.0315  -0.0279 23  SER   B CB  
986  O  OG  . SER   B 23  ? 0.1792 0.3201 0.3603 0.0241  -0.0277 -0.0507 23  SER   B OG  
987  N  N   . PRO   B 24  ? 0.0800 0.2048 0.2821 -0.0369 0.0096  -0.0127 24  PRO   B N   
988  C  CA  . PRO   B 24  ? 0.1302 0.1762 0.2706 -0.0484 -0.0119 -0.0623 24  PRO   B CA  
989  C  C   . PRO   B 24  ? 0.0585 0.1925 0.2285 -0.0247 0.0804  -0.0359 24  PRO   B C   
990  O  O   . PRO   B 24  ? 0.0662 0.1580 0.3485 0.0036  0.1096  -0.0525 24  PRO   B O   
991  C  CB  . PRO   B 24  ? 0.1694 0.1805 0.2486 -0.0307 0.1132  -0.0661 24  PRO   B CB  
992  C  CG  . PRO   B 24  ? 0.3760 0.2448 0.1763 -0.0435 0.0514  -0.0023 24  PRO   B CG  
993  C  CD  . PRO   B 24  ? 0.1435 0.2032 0.2488 -0.0552 0.0077  -0.0367 24  PRO   B CD  
994  N  N   . ALA   B 25  ? 0.1164 0.2431 0.1682 -0.0196 0.0505  -0.0482 25  ALA   B N   
995  C  CA  . ALA   B 25  ? 0.0716 0.2086 0.1914 0.0043  0.0457  -0.0577 25  ALA   B CA  
996  C  C   . ALA   B 25  ? 0.0455 0.2384 0.1394 -0.0009 0.0224  -0.0429 25  ALA   B C   
997  O  O   . ALA   B 25  ? 0.0700 0.2368 0.2464 -0.0238 0.0520  -0.1447 25  ALA   B O   
998  C  CB  . ALA   B 25  ? 0.1661 0.2643 0.0870 0.0127  0.0587  -0.0618 25  ALA   B CB  
999  N  N   . ILE   B 26  ? 0.0756 0.2169 0.1657 -0.0174 0.0590  -0.0624 26  ILE   B N   
1000 C  CA  . ILE   B 26  ? 0.0873 0.1702 0.2016 0.0472  0.0440  -0.0574 26  ILE   B CA  
1001 C  C   . ILE   B 26  ? 0.0795 0.1385 0.2437 -0.0386 -0.0035 -0.0366 26  ILE   B C   
1002 O  O   . ILE   B 26  ? 0.0966 0.2177 0.4382 -0.0048 0.0164  0.0254  26  ILE   B O   
1003 C  CB  . ILE   B 26  ? 0.1750 0.2018 0.2673 0.0070  0.0775  -0.0244 26  ILE   B CB  
1004 C  CG1 . ILE   B 26  ? 0.1976 0.2684 0.2800 -0.0400 0.0580  -0.0461 26  ILE   B CG1 
1005 C  CG2 . ILE   B 26  ? 0.1378 0.3298 0.3247 -0.0292 0.0235  -0.0708 26  ILE   B CG2 
1006 C  CD1 . ILE   B 26  ? 0.2355 0.3075 0.2963 -0.0363 0.0361  0.0264  26  ILE   B CD1 
1007 N  N   . ASN   B 27  ? 0.0941 0.2132 0.2268 -0.0005 0.0490  -0.0421 27  ASN   B N   
1008 C  CA  . ASN   B 27  ? 0.0881 0.2897 0.2432 -0.0455 0.0569  -0.0200 27  ASN   B CA  
1009 C  C   . ASN   B 27  ? 0.1650 0.2608 0.3119 -0.0409 0.0364  -0.0264 27  ASN   B C   
1010 O  O   . ASN   B 27  ? 0.1974 0.3138 0.2250 -0.0483 0.0202  -0.0773 27  ASN   B O   
1011 C  CB  . ASN   B 27  ? 0.0845 0.4011 0.3700 -0.0434 0.0549  -0.0131 27  ASN   B CB  
1012 C  CG  . ASN   B 27  ? 0.3743 0.3941 0.3646 -0.1198 0.0047  -0.0182 27  ASN   B CG  
1013 O  OD1 . ASN   B 27  ? 0.1753 0.4688 0.6839 -0.1853 0.0210  -0.1633 27  ASN   B OD1 
1014 N  N   . VAL   B 28  ? 0.1793 0.1892 0.2693 -0.0553 0.0824  -0.0364 28  VAL   B N   
1015 C  CA  . VAL   B 28  ? 0.2133 0.1947 0.2221 0.0072  0.0998  -0.0567 28  VAL   B CA  
1016 C  C   . VAL   B 28  ? 0.1747 0.1726 0.1578 -0.0160 0.0504  -0.0341 28  VAL   B C   
1017 O  O   . VAL   B 28  ? 0.0889 0.2959 0.3258 0.0074  0.0067  -0.0376 28  VAL   B O   
1018 C  CB  . VAL   B 28  ? 0.2362 0.2257 0.1654 -0.0148 0.0410  -0.0159 28  VAL   B CB  
1019 C  CG1 . VAL   B 28  ? 0.2032 0.1707 0.1595 -0.0657 -0.0685 -0.0707 28  VAL   B CG1 
1020 C  CG2 . VAL   B 28  ? 0.3219 0.2209 0.1835 0.0097  0.0549  -0.0511 28  VAL   B CG2 
1021 N  N   . ALA   B 29  ? 0.0774 0.1658 0.1336 -0.0165 0.0268  -0.0823 29  ALA   B N   
1022 C  CA  . ALA   B 29  ? 0.0933 0.1773 0.1672 0.0053  0.0663  -0.0929 29  ALA   B CA  
1023 C  C   . ALA   B 29  ? 0.1270 0.1689 0.1913 -0.0369 0.0560  -0.0502 29  ALA   B C   
1024 O  O   . ALA   B 29  ? 0.0990 0.1658 0.2368 0.0196  0.0634  -0.0578 29  ALA   B O   
1025 C  CB  . ALA   B 29  ? 0.1651 0.2586 0.1638 -0.0133 0.0556  -0.0352 29  ALA   B CB  
1026 N  N   . VAL   B 30  ? 0.1077 0.1369 0.2724 -0.0719 0.0828  -0.0531 30  VAL   B N   
1027 C  CA  . VAL   B 30  ? 0.0722 0.1618 0.3043 -0.0514 0.0243  -0.0563 30  VAL   B CA  
1028 C  C   . VAL   B 30  ? 0.1262 0.1882 0.3115 -0.0368 -0.0034 -0.0542 30  VAL   B C   
1029 O  O   . VAL   B 30  ? 0.0608 0.2632 0.3072 -0.0769 0.0752  -0.1394 30  VAL   B O   
1030 C  CB  . VAL   B 30  ? 0.0894 0.2224 0.2813 -0.0556 0.0421  -0.0522 30  VAL   B CB  
1031 C  CG1 . VAL   B 30  ? 0.0969 0.1954 0.2682 -0.0549 0.0543  0.0026  30  VAL   B CG1 
1032 C  CG2 . VAL   B 30  ? 0.1985 0.2594 0.2960 -0.0669 0.0358  -0.1051 30  VAL   B CG2 
1033 N  N   . HIS   B 31  ? 0.1129 0.3037 0.3032 -0.0357 0.0572  -0.0421 31  HIS   B N   
1034 C  CA  . HIS   B 31  ? 0.1340 0.3306 0.2940 -0.0630 0.0768  -0.0159 31  HIS   B CA  
1035 C  C   . HIS   B 31  ? 0.0948 0.1943 0.3319 0.0030  -0.0081 -0.0425 31  HIS   B C   
1036 O  O   . HIS   B 31  ? 0.0554 0.2905 0.3094 -0.0705 0.0691  -0.1019 31  HIS   B O   
1037 C  CB  . HIS   B 31  ? 0.1574 0.4035 0.2912 -0.0919 0.0597  0.0324  31  HIS   B CB  
1038 C  CG  . HIS   B 31  ? 0.1842 0.5104 0.1702 -0.1022 -0.0164 0.0041  31  HIS   B CG  
1039 N  ND1 . HIS   B 31  ? 0.3111 0.6022 0.2202 -0.1090 0.0679  0.0450  31  HIS   B ND1 
1040 C  CD2 . HIS   B 31  ? 0.3015 0.5880 0.2374 -0.3039 -0.0391 0.0176  31  HIS   B CD2 
1041 C  CE1 . HIS   B 31  ? 0.4044 0.5762 0.2045 -0.1073 -0.0383 0.0512  31  HIS   B CE1 
1042 N  NE2 . HIS   B 31  ? 0.3353 0.7976 0.1477 -0.4187 -0.0905 -0.0035 31  HIS   B NE2 
1043 N  N   . VAL   B 32  ? 0.0774 0.3176 0.3315 -0.0465 0.0836  -0.0931 32  VAL   B N   
1044 C  CA  . VAL   B 32  ? 0.0846 0.2505 0.2702 -0.0737 0.0494  -0.0329 32  VAL   B CA  
1045 C  C   . VAL   B 32  ? 0.1033 0.3511 0.2048 -0.0394 -0.0632 -0.1010 32  VAL   B C   
1046 O  O   . VAL   B 32  ? 0.1628 0.4361 0.1676 -0.1182 0.0300  -0.1483 32  VAL   B O   
1047 C  CB  . VAL   B 32  ? 0.0898 0.2322 0.1867 -0.1088 0.0144  -0.0424 32  VAL   B CB  
1048 C  CG1 . VAL   B 32  ? 0.0628 0.2053 0.1905 -0.0587 0.0210  -0.0374 32  VAL   B CG1 
1049 C  CG2 . VAL   B 32  ? 0.1146 0.1937 0.2078 -0.0444 0.0033  0.0102  32  VAL   B CG2 
1050 N  N   . PHE   B 33  ? 0.1607 0.3571 0.2806 -0.0029 0.0320  -0.0265 33  PHE   B N   
1051 C  CA  . PHE   B 33  ? 0.1591 0.5255 0.2649 -0.0676 0.0130  -0.0715 33  PHE   B CA  
1052 C  C   . PHE   B 33  ? 0.1518 0.5415 0.2621 0.0066  0.0190  -0.0530 33  PHE   B C   
1053 O  O   . PHE   B 33  ? 0.1525 0.5265 0.2563 -0.0547 0.0361  -0.0629 33  PHE   B O   
1054 C  CB  . PHE   B 33  ? 0.0890 0.5892 0.3597 -0.0285 0.0778  0.0330  33  PHE   B CB  
1055 C  CG  . PHE   B 33  ? 0.0953 0.7080 0.3366 -0.0288 0.0899  0.0350  33  PHE   B CG  
1056 C  CD1 . PHE   B 33  ? 0.1195 0.6385 0.3624 0.0490  0.1302  0.0593  33  PHE   B CD1 
1057 C  CD2 . PHE   B 33  ? 0.1566 0.8099 0.4834 0.0517  -0.0036 0.0319  33  PHE   B CD2 
1058 C  CE1 . PHE   B 33  ? 0.1266 0.8105 0.5090 0.0577  0.1599  0.1107  33  PHE   B CE1 
1059 C  CE2 . PHE   B 33  ? 0.1540 0.7669 0.4526 -0.0448 0.0157  0.0534  33  PHE   B CE2 
1060 C  CZ  . PHE   B 33  ? 0.3354 0.8982 0.4538 0.0756  0.1001  0.1055  33  PHE   B CZ  
1061 N  N   . ARG   B 34  ? 0.1639 0.7037 0.3119 -0.0232 0.0572  -0.0406 34  ARG   B N   
1062 C  CA  . ARG   B 34  ? 0.1700 0.5086 0.3456 -0.1908 0.1054  0.0257  34  ARG   B CA  
1063 C  C   . ARG   B 34  ? 0.4173 0.4616 0.3630 -0.1020 0.0823  0.0130  34  ARG   B C   
1064 O  O   . ARG   B 34  ? 0.2990 0.6263 0.6811 -0.2552 0.0308  -0.0343 34  ARG   B O   
1065 C  CB  . ARG   B 34  ? 0.3703 0.6702 0.2757 0.0436  -0.1000 -0.0212 34  ARG   B CB  
1066 N  N   . LYS   B 35  ? 0.2237 0.4783 0.4369 0.0145  -0.0479 -0.0538 35  LYS   B N   
1067 C  CA  . LYS   B 35  ? 0.2795 0.5116 0.3835 -0.0147 0.0945  -0.0877 35  LYS   B CA  
1068 C  C   . LYS   B 35  ? 0.3353 0.3960 0.4283 -0.1235 0.2494  -0.0765 35  LYS   B C   
1069 O  O   . LYS   B 35  ? 0.4049 0.7388 0.7986 -0.0072 0.2117  -0.0161 35  LYS   B O   
1070 C  CB  . LYS   B 35  ? 0.3271 0.4463 0.3390 -0.0139 0.0253  0.0158  35  LYS   B CB  
1071 C  CG  . LYS   B 35  ? 0.3420 0.4358 0.4809 -0.0128 0.0334  0.0515  35  LYS   B CG  
1072 C  CD  . LYS   B 35  ? 0.3998 0.4205 0.5273 0.0124  0.0022  -0.0021 35  LYS   B CD  
1073 C  CE  . LYS   B 35  ? 0.4422 0.3210 0.4621 -0.0385 -0.0435 0.1667  35  LYS   B CE  
1074 N  N   . GLU   B 42  ? 0.4512 0.9075 0.2358 0.1863  0.1089  0.0281  42  GLU   B N   
1075 C  CA  . GLU   B 42  ? 0.4880 0.8728 0.2341 -0.0409 0.0236  0.0190  42  GLU   B CA  
1076 C  C   . GLU   B 42  ? 0.2800 0.7106 0.3980 -0.0448 -0.1262 0.0619  42  GLU   B C   
1077 O  O   . GLU   B 42  ? 0.3573 0.8092 0.2556 0.0709  -0.0519 0.0381  42  GLU   B O   
1078 C  CB  . GLU   B 42  ? 0.3825 0.5028 0.1903 -0.1851 0.0257  0.2300  42  GLU   B CB  
1079 N  N   . PRO   B 43  ? 0.2917 0.8237 0.5443 -0.0546 -0.0457 0.0499  43  PRO   B N   
1080 C  CA  . PRO   B 43  ? 0.2637 0.5608 0.6087 0.0331  -0.0013 0.0013  43  PRO   B CA  
1081 C  C   . PRO   B 43  ? 0.2087 0.5859 0.2843 0.0833  0.0005  -0.1122 43  PRO   B C   
1082 O  O   . PRO   B 43  ? 0.3113 0.7274 0.2981 -0.0651 -0.0016 -0.2562 43  PRO   B O   
1083 C  CB  . PRO   B 43  ? 0.2762 0.6616 0.3364 0.0617  -0.0210 -0.0622 43  PRO   B CB  
1084 C  CG  . PRO   B 43  ? 0.1801 0.5593 0.2325 -0.2067 -0.1053 -0.0462 43  PRO   B CG  
1085 C  CD  . PRO   B 43  ? 0.1585 0.5745 0.5523 -0.0527 0.0251  0.0311  43  PRO   B CD  
1086 N  N   . PHE   B 44  ? 0.1833 0.7940 0.2637 0.0364  0.1155  -0.0325 44  PHE   B N   
1087 C  CA  . PHE   B 44  ? 0.4192 0.4746 0.1234 -0.0288 0.0553  -0.1637 44  PHE   B CA  
1088 C  C   . PHE   B 44  ? 0.3285 0.3863 0.2993 0.0231  0.1456  -0.1538 44  PHE   B C   
1089 O  O   . PHE   B 44  ? 0.2155 0.4227 0.3981 0.0371  0.0948  -0.1719 44  PHE   B O   
1090 C  CB  . PHE   B 44  ? 0.3756 0.2324 0.1352 0.0135  0.0636  -0.1401 44  PHE   B CB  
1091 C  CG  . PHE   B 44  ? 0.2176 0.3196 0.3076 -0.0989 0.0504  -0.0781 44  PHE   B CG  
1092 C  CD1 . PHE   B 44  ? 0.3362 0.1979 0.4263 0.0475  -0.0056 -0.0954 44  PHE   B CD1 
1093 C  CD2 . PHE   B 44  ? 0.1252 0.2474 0.2774 0.0354  0.0848  -0.1507 44  PHE   B CD2 
1094 C  CE1 . PHE   B 44  ? 0.1580 0.2895 0.2826 0.0814  0.0450  -0.1988 44  PHE   B CE1 
1095 C  CE2 . PHE   B 44  ? 0.1368 0.4449 0.3175 0.0529  0.0243  -0.1737 44  PHE   B CE2 
1096 C  CZ  . PHE   B 44  ? 0.3606 0.4544 0.3291 0.1005  0.1299  -0.1466 44  PHE   B CZ  
1097 N  N   . ALA   B 45  ? 0.1482 0.1606 0.3064 -0.0451 0.0822  -0.1683 45  ALA   B N   
1098 C  CA  . ALA   B 45  ? 0.3933 0.2164 0.2163 -0.1611 0.0421  -0.1682 45  ALA   B CA  
1099 C  C   . ALA   B 45  ? 0.1982 0.2460 0.3344 -0.0945 -0.0315 -0.1043 45  ALA   B C   
1100 O  O   . ALA   B 45  ? 0.1122 0.2585 0.4075 -0.0309 0.1822  -0.0715 45  ALA   B O   
1101 C  CB  . ALA   B 45  ? 0.4210 0.1595 0.2026 -0.1990 0.0453  -0.0993 45  ALA   B CB  
1102 N  N   . SER   B 46  ? 0.1228 0.2701 0.2811 -0.0628 -0.0257 -0.1668 46  SER   B N   
1103 C  CA  . SER   B 46  ? 0.2256 0.2144 0.1699 -0.0829 -0.0050 -0.1474 46  SER   B CA  
1104 C  C   . SER   B 46  ? 0.1133 0.2534 0.2786 -0.0198 0.0395  -0.0988 46  SER   B C   
1105 O  O   . SER   B 46  ? 0.1139 0.2860 0.2992 -0.0206 0.0286  -0.1314 46  SER   B O   
1106 C  CB  . SER   B 46  ? 0.1583 0.3610 0.2287 -0.0003 0.0976  -0.1743 46  SER   B CB  
1107 O  OG  . SER   B 46  ? 0.1606 0.3880 0.3118 0.0018  0.0405  -0.2265 46  SER   B OG  
1108 N  N   . GLY   B 47  ? 0.1077 0.2096 0.2830 -0.0920 0.0391  -0.1462 47  GLY   B N   
1109 C  CA  . GLY   B 47  ? 0.1537 0.1847 0.2892 -0.0129 0.0250  -0.0602 47  GLY   B CA  
1110 C  C   . GLY   B 47  ? 0.0891 0.2150 0.2571 -0.0764 0.0172  -0.0793 47  GLY   B C   
1111 O  O   . GLY   B 47  ? 0.0557 0.2332 0.2927 -0.0665 0.0324  -0.0887 47  GLY   B O   
1112 N  N   . LYS   B 48  ? 0.1369 0.2306 0.2738 -0.0217 0.0337  -0.0470 48  LYS   B N   
1113 C  CA  . LYS   B 48  ? 0.0890 0.2596 0.3308 -0.0430 0.0950  -0.0390 48  LYS   B CA  
1114 C  C   . LYS   B 48  ? 0.0534 0.2639 0.3288 -0.0110 0.0657  -0.0837 48  LYS   B C   
1115 O  O   . LYS   B 48  ? 0.1388 0.2874 0.3659 0.0072  -0.0263 -0.1891 48  LYS   B O   
1116 C  CB  . LYS   B 48  ? 0.0961 0.2741 0.3717 -0.0656 0.1204  0.0295  48  LYS   B CB  
1117 C  CG  . LYS   B 48  ? 0.1699 0.3418 0.3542 -0.0116 0.0756  -0.0325 48  LYS   B CG  
1118 C  CD  . LYS   B 48  ? 0.1838 0.3875 0.4100 0.0522  0.0268  -0.0097 48  LYS   B CD  
1119 C  CE  . LYS   B 48  ? 0.2657 0.3061 0.5071 0.0291  0.0146  0.0967  48  LYS   B CE  
1120 N  N   . THR   B 49  ? 0.0954 0.1859 0.3005 -0.0373 0.0140  -0.0223 49  THR   B N   
1121 C  CA  . THR   B 49  ? 0.0878 0.2333 0.2314 -0.0636 0.0259  -0.0612 49  THR   B CA  
1122 C  C   . THR   B 49  ? 0.0884 0.1748 0.2615 -0.0674 -0.0118 -0.0549 49  THR   B C   
1123 O  O   . THR   B 49  ? 0.0700 0.2090 0.3668 0.0054  0.0883  -0.0842 49  THR   B O   
1124 C  CB  . THR   B 49  ? 0.1386 0.1380 0.1764 -0.0114 0.0362  -0.0148 49  THR   B CB  
1125 O  OG1 . THR   B 49  ? 0.1032 0.1426 0.2838 -0.0357 0.0238  -0.0489 49  THR   B OG1 
1126 C  CG2 . THR   B 49  ? 0.0325 0.1416 0.1769 0.0160  -0.0193 -0.0291 49  THR   B CG2 
1127 N  N   . SER   B 50  ? 0.1914 0.2052 0.2875 -0.0297 0.0332  -0.0174 50  SER   B N   
1128 C  CA  . SER   B 50  ? 0.2141 0.1767 0.3179 -0.0019 0.0629  -0.0056 50  SER   B CA  
1129 C  C   . SER   B 50  ? 0.2751 0.2131 0.3042 -0.0314 0.0806  -0.0188 50  SER   B C   
1130 O  O   . SER   B 50  ? 0.1538 0.2473 0.2673 -0.0798 0.0978  -0.0419 50  SER   B O   
1131 C  CB  . SER   B 50  ? 0.2979 0.2268 0.3256 0.0652  0.0537  -0.0022 50  SER   B CB  
1132 O  OG  . SER   B 50  ? 0.2889 0.3519 0.2583 0.1124  0.0871  -0.0085 50  SER   B OG  
1133 N  N   . GLU   B 51  ? 0.2858 0.2007 0.2717 -0.0405 0.0212  -0.0220 51  GLU   B N   
1134 C  CA  . GLU   B 51  ? 0.3101 0.2361 0.2807 -0.0155 0.0210  -0.0081 51  GLU   B CA  
1135 C  C   . GLU   B 51  ? 0.2881 0.2575 0.2977 -0.0430 0.0624  -0.0316 51  GLU   B C   
1136 O  O   . GLU   B 51  ? 0.2390 0.3012 0.3308 -0.0830 0.0570  -0.0843 51  GLU   B O   
1137 C  CB  . GLU   B 51  ? 0.3729 0.2114 0.2156 -0.0435 0.0306  -0.0534 51  GLU   B CB  
1138 C  CG  . GLU   B 51  ? 0.3772 0.2823 0.3789 -0.0039 0.0460  -0.0171 51  GLU   B CG  
1139 C  CD  . GLU   B 51  ? 0.2048 0.4154 0.3791 0.0105  0.0510  -0.0110 51  GLU   B CD  
1140 N  N   . SER   B 52  ? 0.2562 0.1999 0.3858 0.0187  -0.0135 0.0068  52  SER   B N   
1141 C  CA  . SER   B 52  ? 0.2182 0.1963 0.3108 0.0206  0.0057  0.0380  52  SER   B CA  
1142 C  C   . SER   B 52  ? 0.2017 0.2035 0.3539 -0.0237 -0.0027 0.0018  52  SER   B C   
1143 O  O   . SER   B 52  ? 0.1742 0.1760 0.5305 0.0196  -0.0418 -0.0153 52  SER   B O   
1144 C  CB  . SER   B 52  ? 0.3017 0.2294 0.4556 0.0682  0.0180  -0.0399 52  SER   B CB  
1145 O  OG  . SER   B 52  ? 0.1607 0.4037 0.6484 -0.0604 0.1977  -0.1326 52  SER   B OG  
1146 N  N   . GLY   B 53  ? 0.1351 0.1467 0.4037 -0.0093 0.0289  0.0133  53  GLY   B N   
1147 C  CA  . GLY   B 53  ? 0.1495 0.1884 0.3504 0.0021  0.0593  0.0124  53  GLY   B CA  
1148 C  C   . GLY   B 53  ? 0.1090 0.1540 0.3631 -0.0145 0.0426  -0.0327 53  GLY   B C   
1149 O  O   . GLY   B 53  ? 0.1057 0.1124 0.3397 -0.0130 0.0373  -0.0778 53  GLY   B O   
1150 N  N   . GLU   B 54  ? 0.0798 0.1859 0.2929 0.0244  0.0449  -0.0316 54  GLU   B N   
1151 C  CA  . GLU   B 54  ? 0.2105 0.1761 0.2534 0.0621  0.1074  -0.0585 54  GLU   B CA  
1152 C  C   . GLU   B 54  ? 0.1793 0.1375 0.3074 0.0211  0.0601  -0.0349 54  GLU   B C   
1153 O  O   . GLU   B 54  ? 0.1915 0.2384 0.3190 -0.0098 0.0698  -0.0804 54  GLU   B O   
1154 C  CB  . GLU   B 54  ? 0.2761 0.2678 0.3469 0.0214  -0.0088 -0.0263 54  GLU   B CB  
1155 C  CG  . GLU   B 54  ? 0.3463 0.4074 0.3480 -0.0319 -0.0610 -0.0077 54  GLU   B CG  
1156 C  CD  . GLU   B 54  ? 0.5068 0.3360 0.5677 0.0797  -0.0970 -0.0472 54  GLU   B CD  
1157 O  OE1 . GLU   B 54  ? 0.4871 0.2529 0.5947 0.2755  -0.0676 0.0224  54  GLU   B OE1 
1158 O  OE2 . GLU   B 54  ? 0.4157 0.5436 0.5785 -0.0495 -0.1276 0.1960  54  GLU   B OE2 
1159 N  N   . LEU   B 55  ? 0.0660 0.2299 0.3510 -0.0754 0.0161  -0.0267 55  LEU   B N   
1160 C  CA  . LEU   B 55  ? 0.1192 0.1613 0.3466 -0.0054 0.0758  -0.0867 55  LEU   B CA  
1161 C  C   . LEU   B 55  ? 0.1079 0.2017 0.3492 -0.0494 0.1014  -0.1204 55  LEU   B C   
1162 O  O   . LEU   B 55  ? 0.0459 0.1651 0.3822 -0.0011 0.0505  -0.0866 55  LEU   B O   
1163 C  CB  . LEU   B 55  ? 0.1832 0.2039 0.2903 -0.0176 0.1058  -0.0753 55  LEU   B CB  
1164 C  CG  . LEU   B 55  ? 0.2096 0.3040 0.3002 -0.0452 0.0659  -0.0493 55  LEU   B CG  
1165 C  CD1 . LEU   B 55  ? 0.2000 0.2814 0.2577 -0.0011 -0.0057 -0.0542 55  LEU   B CD1 
1166 C  CD2 . LEU   B 55  ? 0.1590 0.2287 0.4685 -0.1474 0.0709  -0.0370 55  LEU   B CD2 
1167 N  N   . HIS   B 56  ? 0.2831 0.2003 0.4531 -0.0596 0.0098  -0.1661 56  HIS   B N   
1168 C  CA  . HIS   B 56  ? 0.2955 0.2874 0.4576 -0.0208 0.0410  -0.1218 56  HIS   B CA  
1169 C  C   . HIS   B 56  ? 0.2041 0.2758 0.4254 0.0912  -0.0121 -0.1287 56  HIS   B C   
1170 O  O   . HIS   B 56  ? 0.2053 0.4850 0.4433 0.0534  -0.0373 -0.1855 56  HIS   B O   
1171 C  CB  . HIS   B 56  ? 0.1700 0.2027 0.5555 0.0710  0.1318  -0.1707 56  HIS   B CB  
1172 C  CG  . HIS   B 56  ? 0.3841 0.3174 0.5770 0.0668  -0.0238 -0.1389 56  HIS   B CG  
1173 N  ND1 . HIS   B 56  ? 0.4718 0.5098 0.4754 0.0486  -0.0512 0.0795  56  HIS   B ND1 
1174 C  CD2 . HIS   B 56  ? 0.4281 0.2475 0.6265 -0.0493 -0.0804 -0.0933 56  HIS   B CD2 
1175 C  CE1 . HIS   B 56  ? 0.3103 0.5185 0.6477 -0.1467 -0.0877 0.0541  56  HIS   B CE1 
1176 N  NE2 . HIS   B 56  ? 0.3770 0.6367 0.5154 0.1982  -0.0919 0.1880  56  HIS   B NE2 
1177 N  N   . GLY   B 57  ? 0.3371 0.3393 0.3714 0.0636  0.0709  -0.1491 57  GLY   B N   
1178 C  CA  . GLY   B 57  ? 0.2355 0.3165 0.3272 0.0233  0.0589  -0.1053 57  GLY   B CA  
1179 C  C   . GLY   B 57  ? 0.2371 0.3312 0.4964 -0.0056 -0.0648 -0.0705 57  GLY   B C   
1180 O  O   . GLY   B 57  ? 0.2927 0.6978 0.5354 -0.1852 -0.0486 -0.1481 57  GLY   B O   
1181 N  N   . LEU   B 58  ? 0.0295 0.3847 0.4331 -0.0194 -0.0257 -0.1423 58  LEU   B N   
1182 C  CA  . LEU   B 58  ? 0.2449 0.2956 0.4184 -0.0251 0.0334  -0.1571 58  LEU   B CA  
1183 C  C   . LEU   B 58  ? 0.1546 0.2805 0.3714 -0.0076 -0.0488 -0.1817 58  LEU   B C   
1184 O  O   . LEU   B 58  ? 0.1441 0.4338 0.3117 -0.0236 0.0139  -0.2330 58  LEU   B O   
1185 C  CB  . LEU   B 58  ? 0.1407 0.2927 0.3036 -0.0437 0.0368  -0.1087 58  LEU   B CB  
1186 C  CG  . LEU   B 58  ? 0.2040 0.2899 0.2108 -0.0113 0.0457  -0.0765 58  LEU   B CG  
1187 C  CD1 . LEU   B 58  ? 0.1026 0.2675 0.4464 0.0283  0.1276  -0.1740 58  LEU   B CD1 
1188 C  CD2 . LEU   B 58  ? 0.1384 0.1824 0.2337 -0.0166 0.0295  -0.1676 58  LEU   B CD2 
1189 N  N   . THR   B 59  ? 0.0868 0.2923 0.4343 -0.0699 -0.0014 -0.1532 59  THR   B N   
1190 C  CA  . THR   B 59  ? 0.2582 0.3390 0.3632 -0.0094 -0.0358 -0.1904 59  THR   B CA  
1191 C  C   . THR   B 59  ? 0.2257 0.4975 0.3516 0.0828  -0.1104 -0.1582 59  THR   B C   
1192 O  O   . THR   B 59  ? 0.3384 0.4932 0.5239 -0.1869 -0.1089 -0.1401 59  THR   B O   
1193 C  CB  . THR   B 59  ? 0.2636 0.3589 0.4612 -0.0276 -0.1129 -0.1445 59  THR   B CB  
1194 O  OG1 . THR   B 59  ? 0.3645 0.4383 0.3998 -0.1118 -0.1846 -0.1892 59  THR   B OG1 
1195 C  CG2 . THR   B 59  ? 0.3099 0.4280 0.3792 -0.0508 -0.0997 -0.1787 59  THR   B CG2 
1196 N  N   . THR   B 60  ? 0.2596 0.5907 0.6120 0.0474  0.1010  -0.1188 60  THR   B N   
1197 C  CA  . THR   B 60  ? 0.3136 0.4276 0.4897 -0.0293 0.0205  -0.1390 60  THR   B CA  
1198 C  C   . THR   B 60  ? 0.2932 0.4497 0.4392 0.0039  0.1915  -0.1836 60  THR   B C   
1199 O  O   . THR   B 60  ? 0.1820 0.4323 0.6796 -0.0744 0.0486  -0.2923 60  THR   B O   
1200 C  CB  . THR   B 60  ? 0.2086 0.4185 0.4185 -0.1235 0.0309  -0.1104 60  THR   B CB  
1201 O  OG1 . THR   B 60  ? 0.1541 0.7902 0.3662 0.1942  0.0164  -0.1584 60  THR   B OG1 
1202 C  CG2 . THR   B 60  ? 0.1517 0.4455 0.2740 -0.0825 0.0183  -0.0930 60  THR   B CG2 
1203 N  N   . GLU   B 61  ? 0.3013 0.3910 0.4771 -0.0337 0.1572  -0.1608 61  GLU   B N   
1204 C  CA  . GLU   B 61  ? 0.2458 0.5244 0.3515 -0.0079 0.0131  -0.1359 61  GLU   B CA  
1205 C  C   . GLU   B 61  ? 0.2969 0.6297 0.4267 0.0332  0.0882  -0.1032 61  GLU   B C   
1206 O  O   . GLU   B 61  ? 0.3193 0.8165 0.5733 -0.0808 0.0038  -0.1928 61  GLU   B O   
1207 C  CB  . GLU   B 61  ? 0.1401 0.4672 0.5017 -0.0289 0.1364  -0.0783 61  GLU   B CB  
1208 N  N   . GLU   B 62  ? 0.2677 0.4895 0.4790 0.0819  0.1470  -0.1374 62  GLU   B N   
1209 C  CA  . GLU   B 62  ? 0.3966 0.4922 0.4579 -0.0823 -0.0348 -0.0221 62  GLU   B CA  
1210 C  C   . GLU   B 62  ? 0.2077 0.5883 0.3807 0.0548  0.0691  -0.0763 62  GLU   B C   
1211 O  O   . GLU   B 62  ? 0.2933 0.7632 0.3993 -0.0644 0.0697  -0.0744 62  GLU   B O   
1212 C  CB  . GLU   B 62  ? 0.2857 0.4067 0.5888 -0.1629 -0.0869 0.0337  62  GLU   B CB  
1213 N  N   . GLU   B 63  ? 0.1005 0.5399 0.5198 0.0037  -0.0236 -0.1323 63  GLU   B N   
1214 C  CA  . GLU   B 63  ? 0.2496 0.4709 0.4303 -0.0590 0.0127  -0.0339 63  GLU   B CA  
1215 C  C   . GLU   B 63  ? 0.2004 0.4279 0.2890 0.0509  0.0366  -0.0572 63  GLU   B C   
1216 O  O   . GLU   B 63  ? 0.1132 0.4457 0.2956 -0.0048 -0.0481 -0.0958 63  GLU   B O   
1217 C  CB  . GLU   B 63  ? 0.2008 0.5174 0.4487 -0.0702 -0.0672 -0.1844 63  GLU   B CB  
1218 C  CG  . GLU   B 63  ? 0.3299 0.4543 0.3746 -0.0509 0.0128  0.0088  63  GLU   B CG  
1219 C  CD  . GLU   B 63  ? 0.1195 0.4344 0.6671 -0.0868 -0.1880 -0.1227 63  GLU   B CD  
1220 O  OE1 . GLU   B 63  ? 0.1908 0.5929 0.7030 -0.1503 0.0158  0.1593  63  GLU   B OE1 
1221 O  OE2 . GLU   B 63  ? 0.2960 0.4010 0.8318 -0.0285 0.0244  0.0531  63  GLU   B OE2 
1222 N  N   . PHE   B 64  ? 0.1833 0.4195 0.3311 -0.0381 0.0047  -0.1482 64  PHE   B N   
1223 C  CA  . PHE   B 64  ? 0.1284 0.3653 0.4101 -0.0845 0.0076  -0.1092 64  PHE   B CA  
1224 C  C   . PHE   B 64  ? 0.0960 0.2806 0.1888 0.0141  0.0472  -0.1046 64  PHE   B C   
1225 O  O   . PHE   B 64  ? 0.1788 0.4973 0.6171 0.1463  -0.1834 -0.1492 64  PHE   B O   
1226 C  CB  . PHE   B 64  ? 0.1465 0.3793 0.4219 -0.0077 -0.0031 -0.1137 64  PHE   B CB  
1227 C  CG  . PHE   B 64  ? 0.1879 0.4632 0.3976 -0.0270 -0.0324 -0.1403 64  PHE   B CG  
1228 C  CD1 . PHE   B 64  ? 0.4433 0.2651 0.2819 -0.1471 0.0186  -0.0436 64  PHE   B CD1 
1229 C  CD2 . PHE   B 64  ? 0.4845 0.4382 0.2916 -0.0367 -0.0322 -0.0243 64  PHE   B CD2 
1230 C  CE1 . PHE   B 64  ? 0.3881 0.2899 0.4103 -0.0691 -0.0110 -0.1028 64  PHE   B CE1 
1231 C  CE2 . PHE   B 64  ? 0.5658 0.3724 0.3655 0.0174  0.0468  -0.0493 64  PHE   B CE2 
1232 C  CZ  . PHE   B 64  ? 0.6969 0.1565 0.2138 -0.0969 -0.0263 -0.1046 64  PHE   B CZ  
1233 N  N   . VAL   B 65  ? 0.0649 0.3797 0.2268 -0.0610 0.0857  -0.1362 65  VAL   B N   
1234 C  CA  . VAL   B 65  ? 0.0625 0.4047 0.3619 -0.0879 0.0638  -0.1046 65  VAL   B CA  
1235 C  C   . VAL   B 65  ? 0.1540 0.3468 0.3347 -0.0361 0.0719  -0.0704 65  VAL   B C   
1236 O  O   . VAL   B 65  ? 0.0315 0.5330 0.5391 -0.0381 -0.0089 -0.1910 65  VAL   B O   
1237 C  CB  . VAL   B 65  ? 0.2045 0.4109 0.3403 -0.0399 -0.0308 -0.1087 65  VAL   B CB  
1238 C  CG1 . VAL   B 65  ? 0.0743 0.4326 0.4139 -0.0787 0.0755  -0.1257 65  VAL   B CG1 
1239 C  CG2 . VAL   B 65  ? 0.2133 0.3477 0.4068 0.0178  0.0540  -0.0846 65  VAL   B CG2 
1240 N  N   . GLU   B 66  ? 0.1256 0.3044 0.3861 0.0090  0.0084  -0.1554 66  GLU   B N   
1241 C  CA  . GLU   B 66  ? 0.1842 0.3457 0.4683 -0.0190 0.0034  -0.1606 66  GLU   B CA  
1242 C  C   . GLU   B 66  ? 0.1678 0.4126 0.3077 -0.0401 0.0067  -0.1386 66  GLU   B C   
1243 O  O   . GLU   B 66  ? 0.0655 0.7279 0.3152 -0.1424 0.0993  -0.2586 66  GLU   B O   
1244 C  CB  . GLU   B 66  ? 0.1804 0.4056 0.4506 0.0225  0.0676  -0.1271 66  GLU   B CB  
1245 C  CG  . GLU   B 66  ? 0.1194 0.3701 0.3970 -0.0132 0.0408  -0.1177 66  GLU   B CG  
1246 C  CD  . GLU   B 66  ? 0.0739 0.4419 0.5440 0.0999  -0.0024 -0.2507 66  GLU   B CD  
1247 O  OE1 . GLU   B 66  ? 0.1105 0.4997 0.5884 -0.0964 0.0408  -0.3242 66  GLU   B OE1 
1248 O  OE2 . GLU   B 66  ? 0.2450 0.7986 0.5477 0.0474  -0.0610 -0.2885 66  GLU   B OE2 
1249 N  N   . GLY   B 67  ? 0.2448 0.4192 0.4813 0.0979  0.0488  -0.0925 67  GLY   B N   
1250 C  CA  . GLY   B 67  ? 0.2477 0.2916 0.3896 0.0194  0.0536  -0.0876 67  GLY   B CA  
1251 C  C   . GLY   B 67  ? 0.2475 0.3082 0.2777 -0.0154 0.0973  -0.0277 67  GLY   B C   
1252 O  O   . GLY   B 67  ? 0.1935 0.3291 0.3290 0.1365  0.0882  -0.0670 67  GLY   B O   
1253 N  N   . ILE   B 68  ? 0.1256 0.3585 0.2518 -0.0441 0.0960  -0.0505 68  ILE   B N   
1254 C  CA  . ILE   B 68  ? 0.2411 0.2911 0.3712 -0.0256 0.0833  -0.0678 68  ILE   B CA  
1255 C  C   . ILE   B 68  ? 0.2296 0.3063 0.2568 -0.0415 0.0536  -0.0290 68  ILE   B C   
1256 O  O   . ILE   B 68  ? 0.1117 0.4619 0.2780 -0.0800 0.1134  -0.0178 68  ILE   B O   
1257 C  CB  . ILE   B 68  ? 0.2657 0.3774 0.3806 -0.0576 0.0994  0.0046  68  ILE   B CB  
1258 C  CG1 . ILE   B 68  ? 0.2318 0.3714 0.3664 -0.0133 0.1337  0.0211  68  ILE   B CG1 
1259 C  CG2 . ILE   B 68  ? 0.3253 0.2530 0.3682 -0.0809 0.0391  -0.0411 68  ILE   B CG2 
1260 C  CD1 . ILE   B 68  ? 0.3164 0.3903 0.3829 0.0222  0.1632  0.0177  68  ILE   B CD1 
1261 N  N   . TYR   B 69  ? 0.0909 0.3483 0.3087 -0.0497 0.0706  -0.0748 69  TYR   B N   
1262 C  CA  . TYR   B 69  ? 0.0914 0.2966 0.3030 -0.0347 0.0917  -0.0964 69  TYR   B CA  
1263 C  C   . TYR   B 69  ? 0.1081 0.2471 0.3059 -0.0474 0.0659  -0.1054 69  TYR   B C   
1264 O  O   . TYR   B 69  ? 0.0920 0.2781 0.3256 -0.1081 0.1158  -0.1000 69  TYR   B O   
1265 C  CB  . TYR   B 69  ? 0.0439 0.2427 0.3418 -0.0440 0.0609  -0.1203 69  TYR   B CB  
1266 C  CG  . TYR   B 69  ? 0.0747 0.2767 0.3273 -0.0350 0.0657  -0.1309 69  TYR   B CG  
1267 C  CD1 . TYR   B 69  ? 0.0760 0.2587 0.3157 0.0012  0.0337  -0.0823 69  TYR   B CD1 
1268 C  CD2 . TYR   B 69  ? 0.1461 0.2382 0.2395 -0.0551 0.0762  -0.1180 69  TYR   B CD2 
1269 C  CE1 . TYR   B 69  ? 0.1376 0.2667 0.2933 -0.0590 0.0509  -0.1331 69  TYR   B CE1 
1270 C  CE2 . TYR   B 69  ? 0.1227 0.1931 0.4016 -0.0573 -0.0334 -0.2009 69  TYR   B CE2 
1271 C  CZ  . TYR   B 69  ? 0.1340 0.2588 0.3337 -0.0092 -0.0494 -0.1140 69  TYR   B CZ  
1272 O  OH  . TYR   B 69  ? 0.1009 0.4196 0.3877 0.0416  -0.0713 -0.2168 69  TYR   B OH  
1273 N  N   . LYS   B 70  ? 0.0748 0.2260 0.3311 -0.0124 0.1131  -0.0477 70  LYS   B N   
1274 C  CA  . LYS   B 70  ? 0.1678 0.2640 0.3263 -0.0115 0.1726  -0.0676 70  LYS   B CA  
1275 C  C   . LYS   B 70  ? 0.0876 0.2611 0.2818 -0.0357 0.0342  -0.0463 70  LYS   B C   
1276 O  O   . LYS   B 70  ? 0.2164 0.2411 0.3453 -0.1004 0.1176  -0.1036 70  LYS   B O   
1277 C  CB  . LYS   B 70  ? 0.2084 0.1672 0.4437 -0.0873 0.2017  0.0348  70  LYS   B CB  
1278 C  CG  . LYS   B 70  ? 0.1652 0.2699 0.4993 -0.1247 0.1953  -0.0103 70  LYS   B CG  
1279 C  CD  . LYS   B 70  ? 0.0641 0.2495 0.5844 -0.0907 0.0435  -0.0231 70  LYS   B CD  
1280 N  N   . VAL   B 71  ? 0.1617 0.2148 0.2923 -0.0380 0.1031  -0.0616 71  VAL   B N   
1281 C  CA  . VAL   B 71  ? 0.1229 0.2406 0.1922 -0.0325 0.0980  -0.1025 71  VAL   B CA  
1282 C  C   . VAL   B 71  ? 0.1637 0.1671 0.3292 -0.0176 0.0769  -0.0514 71  VAL   B C   
1283 O  O   . VAL   B 71  ? 0.1402 0.2538 0.4656 -0.0437 0.2165  -0.1540 71  VAL   B O   
1284 C  CB  . VAL   B 71  ? 0.1738 0.1673 0.2262 -0.1112 0.0123  -0.1143 71  VAL   B CB  
1285 C  CG1 . VAL   B 71  ? 0.2061 0.2419 0.2359 -0.0479 0.0567  -0.0297 71  VAL   B CG1 
1286 C  CG2 . VAL   B 71  ? 0.1021 0.2739 0.2792 -0.0962 0.1125  -0.0342 71  VAL   B CG2 
1287 N  N   . GLU   B 72  ? 0.1347 0.3014 0.3596 0.0077  0.1296  -0.1517 72  GLU   B N   
1288 C  CA  . GLU   B 72  ? 0.2052 0.1699 0.2901 0.0023  0.1696  -0.0967 72  GLU   B CA  
1289 C  C   . GLU   B 72  ? 0.1790 0.2038 0.2040 -0.0098 0.0810  -0.0662 72  GLU   B C   
1290 O  O   . GLU   B 72  ? 0.1440 0.2594 0.2307 -0.0725 0.0836  -0.0402 72  GLU   B O   
1291 C  CB  . GLU   B 72  ? 0.2418 0.4049 0.2678 -0.0008 0.2063  -0.0287 72  GLU   B CB  
1292 C  CG  . GLU   B 72  ? 0.3683 0.3722 0.2617 0.0210  0.2154  -0.1134 72  GLU   B CG  
1293 C  CD  . GLU   B 72  ? 0.3626 0.4030 0.2676 -0.0436 0.0218  -0.1106 72  GLU   B CD  
1294 O  OE1 . GLU   B 72  ? 0.4250 0.5926 0.1603 0.0525  -0.1346 -0.0114 72  GLU   B OE1 
1295 O  OE2 . GLU   B 72  ? 0.4280 0.2234 0.3569 0.0075  0.0029  -0.0087 72  GLU   B OE2 
1296 N  N   . ILE   B 73  ? 0.0729 0.1623 0.1646 -0.0547 0.0162  -0.0571 73  ILE   B N   
1297 C  CA  . ILE   B 73  ? 0.1068 0.1357 0.1729 -0.0015 0.0613  -0.0390 73  ILE   B CA  
1298 C  C   . ILE   B 73  ? 0.0469 0.1728 0.1424 -0.0454 0.0097  -0.0153 73  ILE   B C   
1299 O  O   . ILE   B 73  ? 0.0486 0.1928 0.1824 0.0141  0.0575  -0.0147 73  ILE   B O   
1300 C  CB  . ILE   B 73  ? 0.1279 0.1737 0.2121 0.0101  0.0151  -0.0386 73  ILE   B CB  
1301 C  CG1 . ILE   B 73  ? 0.1043 0.2487 0.2247 0.0007  -0.0732 -0.0329 73  ILE   B CG1 
1302 C  CG2 . ILE   B 73  ? 0.2130 0.2584 0.2242 0.0011  0.0388  -0.0109 73  ILE   B CG2 
1303 C  CD1 . ILE   B 73  ? 0.1122 0.2809 0.1731 0.0058  -0.0635 -0.0273 73  ILE   B CD1 
1304 N  N   . ASP   B 74  ? 0.0586 0.1479 0.1946 -0.0407 0.0068  -0.0578 74  ASP   B N   
1305 C  CA  . ASP   B 74  ? 0.0938 0.1504 0.1659 -0.0134 -0.0006 -0.0719 74  ASP   B CA  
1306 C  C   . ASP   B 74  ? 0.0712 0.1595 0.1326 -0.0407 -0.0035 -0.0112 74  ASP   B C   
1307 O  O   . ASP   B 74  ? 0.0699 0.2100 0.1574 -0.0834 0.0012  -0.0639 74  ASP   B O   
1308 C  CB  . ASP   B 74  ? 0.0818 0.2403 0.1510 -0.0128 -0.0098 -0.0858 74  ASP   B CB  
1309 C  CG  . ASP   B 74  ? 0.1096 0.2727 0.1340 0.0173  -0.0451 -0.1136 74  ASP   B CG  
1310 O  OD1 . ASP   B 74  ? 0.0849 0.2483 0.2168 0.0071  -0.0580 -0.0697 74  ASP   B OD1 
1311 O  OD2 . ASP   B 74  ? 0.0714 0.3992 0.2534 0.0360  -0.0591 -0.1981 74  ASP   B OD2 
1312 N  N   . THR   B 75  ? 0.0629 0.1563 0.1192 -0.0555 0.0170  -0.0018 75  THR   B N   
1313 C  CA  . THR   B 75  ? 0.0586 0.1574 0.1103 -0.0182 -0.0019 0.0027  75  THR   B CA  
1314 C  C   . THR   B 75  ? 0.0676 0.1838 0.1018 -0.0075 0.0131  -0.0131 75  THR   B C   
1315 O  O   . THR   B 75  ? 0.0342 0.2139 0.1111 -0.0272 0.0086  -0.0436 75  THR   B O   
1316 C  CB  . THR   B 75  ? 0.0887 0.1094 0.1025 0.0086  -0.0031 -0.0333 75  THR   B CB  
1317 O  OG1 . THR   B 75  ? 0.0620 0.1726 0.1412 -0.0118 0.0162  0.0113  75  THR   B OG1 
1318 C  CG2 . THR   B 75  ? 0.0721 0.1789 0.1314 0.0066  0.0065  -0.0038 75  THR   B CG2 
1319 N  N   . LYS   B 76  ? 0.0491 0.2138 0.1144 -0.0125 0.0418  0.0307  76  LYS   B N   
1320 C  CA  . LYS   B 76  ? 0.0455 0.2449 0.1255 -0.0164 0.0392  0.0132  76  LYS   B CA  
1321 C  C   . LYS   B 76  ? 0.0778 0.2034 0.0729 -0.0290 0.0288  -0.0196 76  LYS   B C   
1322 O  O   . LYS   B 76  ? 0.0317 0.1685 0.0925 0.0302  -0.0026 -0.0122 76  LYS   B O   
1323 C  CB  . LYS   B 76  ? 0.1326 0.2508 0.1864 0.0518  -0.0323 0.0481  76  LYS   B CB  
1324 C  CG  . LYS   B 76  ? 0.1107 0.2662 0.2090 0.0518  0.0148  0.0125  76  LYS   B CG  
1325 C  CD  . LYS   B 76  ? 0.2115 0.3611 0.2594 -0.0073 0.0435  0.0758  76  LYS   B CD  
1326 C  CE  . LYS   B 76  ? 0.2973 0.3901 0.3900 0.0150  0.0171  0.0864  76  LYS   B CE  
1327 N  NZ  . LYS   B 76  ? 0.2099 0.5572 0.3214 -0.0111 -0.0527 0.0826  76  LYS   B NZ  
1328 N  N   . SER   B 77  ? 0.0982 0.2009 0.1144 -0.0362 -0.0134 -0.0137 77  SER   B N   
1329 C  CA  . SER   B 77  ? 0.0637 0.1932 0.1322 -0.0287 -0.0356 -0.0213 77  SER   B CA  
1330 C  C   . SER   B 77  ? 0.0434 0.2144 0.1747 -0.0529 -0.0306 0.0319  77  SER   B C   
1331 O  O   . SER   B 77  ? 0.0281 0.2337 0.2243 -0.0233 0.0073  -0.0080 77  SER   B O   
1332 C  CB  . SER   B 77  ? 0.0833 0.2394 0.1674 -0.0385 -0.0330 -0.0544 77  SER   B CB  
1333 O  OG  . SER   B 77  ? 0.1111 0.3055 0.1787 -0.0340 -0.0583 -0.0493 77  SER   B OG  
1334 N  N   . TYR   B 78  ? 0.0447 0.1828 0.1286 0.0150  -0.0077 -0.0068 78  TYR   B N   
1335 C  CA  . TYR   B 78  ? 0.0565 0.1574 0.1680 0.0096  0.0011  0.0263  78  TYR   B CA  
1336 C  C   . TYR   B 78  ? 0.0780 0.1569 0.1531 -0.0212 0.0010  0.0037  78  TYR   B C   
1337 O  O   . TYR   B 78  ? 0.0524 0.1749 0.2608 -0.0631 0.0019  0.0183  78  TYR   B O   
1338 C  CB  . TYR   B 78  ? 0.0464 0.1369 0.1637 -0.0175 0.0088  0.0075  78  TYR   B CB  
1339 C  CG  . TYR   B 78  ? 0.0290 0.1357 0.1772 0.0201  0.0055  0.0312  78  TYR   B CG  
1340 C  CD1 . TYR   B 78  ? 0.1019 0.1343 0.1884 -0.0023 -0.0322 0.0326  78  TYR   B CD1 
1341 C  CD2 . TYR   B 78  ? 0.0326 0.1844 0.2092 -0.0339 -0.0073 0.0204  78  TYR   B CD2 
1342 C  CE1 . TYR   B 78  ? 0.0517 0.2005 0.2027 -0.0180 -0.0608 0.0342  78  TYR   B CE1 
1343 C  CE2 . TYR   B 78  ? 0.0317 0.1919 0.1973 -0.0121 -0.0295 -0.0163 78  TYR   B CE2 
1344 C  CZ  . TYR   B 78  ? 0.1347 0.2050 0.1660 0.0088  0.0227  0.0220  78  TYR   B CZ  
1345 O  OH  . TYR   B 78  ? 0.1406 0.2312 0.1861 0.0076  0.0016  0.0419  78  TYR   B OH  
1346 N  N   . TRP   B 79  ? 0.0319 0.1375 0.1519 0.0051  0.0288  0.0340  79  TRP   B N   
1347 C  CA  . TRP   B 79  ? 0.0522 0.1503 0.1023 -0.0087 -0.0187 0.0086  79  TRP   B CA  
1348 C  C   . TRP   B 79  ? 0.0412 0.2071 0.1357 -0.0073 0.0085  0.0000  79  TRP   B C   
1349 O  O   . TRP   B 79  ? 0.0266 0.1992 0.1616 -0.0125 0.0076  -0.0026 79  TRP   B O   
1350 C  CB  . TRP   B 79  ? 0.0418 0.1470 0.0900 0.0068  0.0055  0.0146  79  TRP   B CB  
1351 C  CG  . TRP   B 79  ? 0.0380 0.1634 0.0963 -0.0072 0.0094  0.0296  79  TRP   B CG  
1352 C  CD1 . TRP   B 79  ? 0.0436 0.2022 0.0780 -0.0313 0.0084  0.0014  79  TRP   B CD1 
1353 C  CD2 . TRP   B 79  ? 0.0440 0.1573 0.0943 -0.0215 0.0028  0.0212  79  TRP   B CD2 
1354 N  NE1 . TRP   B 79  ? 0.0573 0.1693 0.0955 0.0205  0.0053  0.0142  79  TRP   B NE1 
1355 C  CE2 . TRP   B 79  ? 0.0459 0.1889 0.0780 0.0074  -0.0056 -0.0081 79  TRP   B CE2 
1356 C  CE3 . TRP   B 79  ? 0.0929 0.1988 0.0935 -0.0185 0.0117  0.0371  79  TRP   B CE3 
1357 C  CZ2 . TRP   B 79  ? 0.0939 0.2126 0.0575 -0.0569 -0.0150 0.0030  79  TRP   B CZ2 
1358 C  CZ3 . TRP   B 79  ? 0.0572 0.2438 0.0968 -0.0616 -0.0030 0.0260  79  TRP   B CZ3 
1359 C  CH2 . TRP   B 79  ? 0.0522 0.2566 0.0761 -0.0260 -0.0136 0.0261  79  TRP   B CH2 
1360 N  N   . LYS   B 80  ? 0.0439 0.2238 0.1267 -0.0203 0.0264  -0.0155 80  LYS   B N   
1361 C  CA  . LYS   B 80  ? 0.0418 0.2199 0.1567 -0.0134 0.0377  0.0101  80  LYS   B CA  
1362 C  C   . LYS   B 80  ? 0.0643 0.1965 0.1247 -0.0021 0.0622  0.0004  80  LYS   B C   
1363 O  O   . LYS   B 80  ? 0.0295 0.3043 0.2003 0.0224  0.0203  -0.0041 80  LYS   B O   
1364 C  CB  . LYS   B 80  ? 0.0935 0.2444 0.1539 0.0083  0.0473  0.0291  80  LYS   B CB  
1365 C  CG  . LYS   B 80  ? 0.1489 0.2251 0.1976 0.0183  0.0643  0.0232  80  LYS   B CG  
1366 C  CD  . LYS   B 80  ? 0.2678 0.2885 0.2084 0.0499  0.0411  0.0195  80  LYS   B CD  
1367 C  CE  . LYS   B 80  ? 0.3491 0.4143 0.2350 -0.0249 0.0765  -0.0582 80  LYS   B CE  
1368 N  N   . ALA   B 81  ? 0.0447 0.1505 0.2621 -0.0461 0.0408  -0.0489 81  ALA   B N   
1369 C  CA  . ALA   B 81  ? 0.0817 0.1734 0.1948 -0.0530 0.0530  -0.0309 81  ALA   B CA  
1370 C  C   . ALA   B 81  ? 0.1243 0.2753 0.1841 -0.1108 0.0420  0.0245  81  ALA   B C   
1371 O  O   . ALA   B 81  ? 0.0441 0.2428 0.1968 -0.0498 0.0073  0.0604  81  ALA   B O   
1372 C  CB  . ALA   B 81  ? 0.1296 0.1272 0.2509 -0.0533 0.0382  0.0299  81  ALA   B CB  
1373 N  N   . LEU   B 82  ? 0.0895 0.2429 0.2614 0.0067  -0.0149 -0.0628 82  LEU   B N   
1374 C  CA  . LEU   B 82  ? 0.0702 0.2518 0.2751 -0.0907 0.0298  -0.0010 82  LEU   B CA  
1375 C  C   . LEU   B 82  ? 0.1206 0.2876 0.1866 -0.0487 0.0525  0.0602  82  LEU   B C   
1376 O  O   . LEU   B 82  ? 0.1146 0.4144 0.2216 -0.1176 0.0989  0.0119  82  LEU   B O   
1377 C  CB  . LEU   B 82  ? 0.1240 0.3334 0.2206 -0.0529 -0.0328 0.0270  82  LEU   B CB  
1378 C  CG  . LEU   B 82  ? 0.0531 0.3281 0.2609 -0.0587 -0.0202 0.0539  82  LEU   B CG  
1379 C  CD2 . LEU   B 82  ? 0.0310 0.2582 0.2499 -0.0361 -0.0074 0.0791  82  LEU   B CD2 
1380 N  N   . GLY   B 83  ? 0.0413 0.2146 0.1301 -0.0326 0.0181  -0.0081 83  GLY   B N   
1381 C  CA  . GLY   B 83  ? 0.0543 0.2645 0.0985 0.0167  0.0431  0.0405  83  GLY   B CA  
1382 C  C   . GLY   B 83  ? 0.0906 0.2450 0.1315 0.0115  0.0327  0.0236  83  GLY   B C   
1383 O  O   . GLY   B 83  ? 0.0352 0.2613 0.1906 -0.0364 0.0293  -0.0179 83  GLY   B O   
1384 N  N   . ILE   B 84  ? 0.0894 0.2400 0.0618 -0.0205 0.0289  0.0168  84  ILE   B N   
1385 C  CA  . ILE   B 84  ? 0.0757 0.2150 0.1000 0.0036  -0.0091 0.0233  84  ILE   B CA  
1386 C  C   . ILE   B 84  ? 0.0550 0.2284 0.1435 -0.0151 -0.0120 0.0524  84  ILE   B C   
1387 O  O   . ILE   B 84  ? 0.0285 0.2382 0.1581 0.0019  0.0204  0.0367  84  ILE   B O   
1388 C  CB  . ILE   B 84  ? 0.1011 0.1883 0.1441 -0.0200 -0.0391 0.0622  84  ILE   B CB  
1389 C  CG1 . ILE   B 84  ? 0.0963 0.2242 0.1252 -0.0522 -0.0303 0.0111  84  ILE   B CG1 
1390 C  CG2 . ILE   B 84  ? 0.0972 0.2024 0.1372 -0.0171 -0.0022 -0.0253 84  ILE   B CG2 
1391 C  CD1 . ILE   B 84  ? 0.1455 0.2166 0.0616 -0.0501 -0.0258 0.0409  84  ILE   B CD1 
1392 N  N   . SER   B 85  ? 0.1349 0.2231 0.1941 -0.0373 0.0079  0.0800  85  SER   B N   
1393 C  CA  . SER   B 85  ? 0.0395 0.2608 0.1208 -0.0548 -0.0204 0.0498  85  SER   B CA  
1394 C  C   . SER   B 85  ? 0.0354 0.2151 0.1751 -0.0314 -0.0141 0.0249  85  SER   B C   
1395 O  O   . SER   B 85  ? 0.0436 0.1877 0.1999 -0.0048 0.0180  -0.0052 85  SER   B O   
1396 C  CB  . SER   B 85  ? 0.1745 0.1956 0.2471 -0.0792 0.0103  0.0078  85  SER   B CB  
1397 O  OG  . SER   B 85  ? 0.0877 0.3148 0.2484 -0.0499 -0.0598 0.0414  85  SER   B OG  
1398 N  N   . PRO   B 86  ? 0.0495 0.2191 0.1414 -0.0298 -0.0321 0.0402  86  PRO   B N   
1399 C  CA  . PRO   B 86  ? 0.0510 0.1779 0.1253 0.0104  0.0082  0.0455  86  PRO   B CA  
1400 C  C   . PRO   B 86  ? 0.0907 0.1833 0.1282 -0.0076 -0.0266 0.0612  86  PRO   B C   
1401 O  O   . PRO   B 86  ? 0.0325 0.1822 0.1457 -0.0167 -0.0161 0.0675  86  PRO   B O   
1402 C  CB  . PRO   B 86  ? 0.1196 0.1946 0.1545 -0.0179 0.0383  0.0182  86  PRO   B CB  
1403 C  CG  . PRO   B 86  ? 0.1244 0.2335 0.1860 0.0331  0.0469  0.0215  86  PRO   B CG  
1404 C  CD  . PRO   B 86  ? 0.0814 0.2048 0.1363 -0.0021 0.0173  0.0119  86  PRO   B CD  
1405 N  N   . PHE   B 87  ? 0.0827 0.1393 0.0802 0.0345  -0.0300 0.0101  87  PHE   B N   
1406 C  CA  . PHE   B 87  ? 0.0663 0.1455 0.0588 0.0125  -0.0235 -0.0049 87  PHE   B CA  
1407 C  C   . PHE   B 87  ? 0.0588 0.1442 0.0780 0.0119  -0.0051 -0.0019 87  PHE   B C   
1408 O  O   . PHE   B 87  ? 0.0493 0.1767 0.0894 0.0225  0.0386  0.0210  87  PHE   B O   
1409 C  CB  . PHE   B 87  ? 0.0396 0.1497 0.1142 0.0060  -0.0154 -0.0162 87  PHE   B CB  
1410 C  CG  . PHE   B 87  ? 0.0661 0.1124 0.0797 0.0053  -0.0464 -0.0174 87  PHE   B CG  
1411 C  CD1 . PHE   B 87  ? 0.0698 0.1298 0.1549 0.0157  -0.0131 0.0014  87  PHE   B CD1 
1412 C  CD2 . PHE   B 87  ? 0.1011 0.1344 0.0585 0.0066  0.0066  0.0216  87  PHE   B CD2 
1413 C  CE1 . PHE   B 87  ? 0.1010 0.1243 0.1131 0.0555  -0.0224 0.0357  87  PHE   B CE1 
1414 C  CE2 . PHE   B 87  ? 0.1289 0.1346 0.0607 -0.0191 -0.0437 0.0369  87  PHE   B CE2 
1415 C  CZ  . PHE   B 87  ? 0.1156 0.1490 0.0928 -0.0122 0.0195  0.0686  87  PHE   B CZ  
1416 N  N   . HIS   B 88  ? 0.1039 0.1060 0.0578 -0.0070 0.0111  -0.0123 88  HIS   B N   
1417 C  CA  . HIS   B 88  ? 0.0477 0.1383 0.1074 -0.0041 0.0426  0.0033  88  HIS   B CA  
1418 C  C   . HIS   B 88  ? 0.0639 0.1438 0.0935 -0.0193 0.0477  0.0016  88  HIS   B C   
1419 O  O   . HIS   B 88  ? 0.0578 0.1949 0.1204 -0.0512 0.0477  -0.0280 88  HIS   B O   
1420 C  CB  . HIS   B 88  ? 0.0718 0.1411 0.0928 0.0061  0.0353  0.0268  88  HIS   B CB  
1421 C  CG  . HIS   B 88  ? 0.0671 0.1493 0.0788 -0.0049 0.0292  0.0545  88  HIS   B CG  
1422 N  ND1 . HIS   B 88  ? 0.1002 0.1838 0.0871 -0.0339 0.0401  0.0473  88  HIS   B ND1 
1423 C  CD2 . HIS   B 88  ? 0.0317 0.1950 0.0541 -0.0236 -0.0124 0.0258  88  HIS   B CD2 
1424 C  CE1 . HIS   B 88  ? 0.0724 0.1833 0.1144 -0.0122 0.0075  0.0254  88  HIS   B CE1 
1425 N  NE2 . HIS   B 88  ? 0.0806 0.2997 0.0507 -0.0420 -0.0372 0.0295  88  HIS   B NE2 
1426 N  N   . GLU   B 89  ? 0.0665 0.1396 0.0940 -0.0460 0.0457  -0.0176 89  GLU   B N   
1427 C  CA  . GLU   B 89  ? 0.1209 0.1715 0.0955 -0.0689 0.0441  -0.0218 89  GLU   B CA  
1428 C  C   . GLU   B 89  ? 0.1604 0.1694 0.1653 -0.0704 0.0786  -0.0134 89  GLU   B C   
1429 O  O   . GLU   B 89  ? 0.2165 0.2135 0.1401 -0.1114 0.1161  -0.0547 89  GLU   B O   
1430 C  CB  . GLU   B 89  ? 0.1247 0.2305 0.1159 -0.0623 0.0782  -0.0055 89  GLU   B CB  
1431 C  CG  . GLU   B 89  ? 0.1023 0.2530 0.1260 -0.0663 0.0175  0.0133  89  GLU   B CG  
1432 C  CD  . GLU   B 89  ? 0.0918 0.2657 0.1807 -0.0213 -0.0705 0.0133  89  GLU   B CD  
1433 O  OE1 . GLU   B 89  ? 0.1854 0.2662 0.3332 -0.0871 -0.0137 -0.0428 89  GLU   B OE1 
1434 O  OE2 . GLU   B 89  ? 0.1674 0.3656 0.2216 -0.0186 0.0210  0.0491  89  GLU   B OE2 
1435 N  N   . HIS   B 90  ? 0.1460 0.2440 0.1908 -0.0289 0.0940  0.0253  90  HIS   B N   
1436 C  CA  . HIS   B 90  ? 0.1755 0.1405 0.2806 -0.0803 0.1567  -0.0101 90  HIS   B CA  
1437 C  C   . HIS   B 90  ? 0.1422 0.2090 0.3507 -0.0084 0.1298  -0.0064 90  HIS   B C   
1438 O  O   . HIS   B 90  ? 0.0532 0.2506 0.5497 -0.0366 0.0849  -0.0647 90  HIS   B O   
1439 C  CB  . HIS   B 90  ? 0.3176 0.1940 0.2775 0.0262  0.0833  -0.0333 90  HIS   B CB  
1440 C  CG  . HIS   B 90  ? 0.3804 0.2345 0.3298 0.0726  0.0479  -0.0272 90  HIS   B CG  
1441 N  ND1 . HIS   B 90  ? 0.3877 0.2869 0.3059 0.0346  0.0594  -0.0775 90  HIS   B ND1 
1442 C  CD2 . HIS   B 90  ? 0.3553 0.3228 0.3706 0.1020  0.0088  -0.0020 90  HIS   B CD2 
1443 C  CE1 . HIS   B 90  ? 0.3309 0.2532 0.3893 0.0503  0.0172  -0.0049 90  HIS   B CE1 
1444 N  NE2 . HIS   B 90  ? 0.3465 0.3324 0.3458 0.1220  -0.0217 0.0299  90  HIS   B NE2 
1445 N  N   . ALA   B 91  ? 0.0624 0.1777 0.4193 -0.0650 -0.0002 -0.0187 91  ALA   B N   
1446 C  CA  . ALA   B 91  ? 0.0324 0.1527 0.5170 -0.0272 0.0443  -0.0984 91  ALA   B CA  
1447 C  C   . ALA   B 91  ? 0.0801 0.1349 0.5833 0.0321  0.0676  -0.1089 91  ALA   B C   
1448 O  O   . ALA   B 91  ? 0.0399 0.1815 0.6960 -0.0476 0.0421  -0.1541 91  ALA   B O   
1449 C  CB  . ALA   B 91  ? 0.2019 0.1700 0.5875 -0.0038 -0.0074 -0.0947 91  ALA   B CB  
1450 N  N   . GLU   B 92  ? 0.1822 0.3014 0.4261 0.0042  0.0000  -0.0130 92  GLU   B N   
1451 C  CA  . GLU   B 92  ? 0.1276 0.2272 0.4472 -0.0137 0.0373  0.0118  92  GLU   B CA  
1452 C  C   . GLU   B 92  ? 0.2136 0.4102 0.4825 0.1133  -0.1253 -0.0733 92  GLU   B C   
1453 O  O   . GLU   B 92  ? 0.1060 0.5001 0.5781 0.0518  0.0933  -0.1721 92  GLU   B O   
1454 C  CB  . GLU   B 92  ? 0.2669 0.4334 0.5028 -0.0424 0.0460  0.0657  92  GLU   B CB  
1455 C  CG  . GLU   B 92  ? 0.4448 0.2115 0.3876 -0.1531 0.0997  0.1084  92  GLU   B CG  
1456 C  CD  . GLU   B 92  ? 0.4004 0.4061 0.4068 -0.0438 -0.0131 0.0511  92  GLU   B CD  
1457 O  OE1 . GLU   B 92  ? 0.6074 0.2989 0.2087 -0.0009 0.0908  0.0341  92  GLU   B OE1 
1458 O  OE2 . GLU   B 92  ? 0.4405 0.3515 0.4140 -0.2025 -0.0139 -0.0556 92  GLU   B OE2 
1459 N  N   . VAL   B 93  ? 0.1511 0.3359 0.3384 -0.0425 0.0320  -0.0126 93  VAL   B N   
1460 C  CA  . VAL   B 93  ? 0.1506 0.2922 0.2867 0.0212  0.0595  -0.0412 93  VAL   B CA  
1461 C  C   . VAL   B 93  ? 0.0882 0.2185 0.3248 -0.0560 0.0824  -0.0525 93  VAL   B C   
1462 O  O   . VAL   B 93  ? 0.1202 0.2468 0.3771 -0.1026 0.0763  -0.0783 93  VAL   B O   
1463 C  CB  . VAL   B 93  ? 0.1139 0.2942 0.2806 -0.1254 -0.0070 -0.0472 93  VAL   B CB  
1464 C  CG1 . VAL   B 93  ? 0.0538 0.3679 0.2967 -0.0881 0.0565  -0.0685 93  VAL   B CG1 
1465 C  CG2 . VAL   B 93  ? 0.0837 0.5240 0.2659 -0.0706 0.0723  0.0116  93  VAL   B CG2 
1466 N  N   . VAL   B 94  ? 0.1908 0.1647 0.2458 -0.1152 0.0850  -0.1370 94  VAL   B N   
1467 C  CA  . VAL   B 94  ? 0.1589 0.2527 0.2658 -0.0658 0.1029  -0.0342 94  VAL   B CA  
1468 C  C   . VAL   B 94  ? 0.1702 0.1501 0.2725 -0.0525 0.1072  -0.0680 94  VAL   B C   
1469 O  O   . VAL   B 94  ? 0.1420 0.2175 0.2832 -0.0761 0.1067  -0.1114 94  VAL   B O   
1470 C  CB  . VAL   B 94  ? 0.1619 0.3047 0.3515 -0.0524 0.1197  0.0207  94  VAL   B CB  
1471 C  CG1 . VAL   B 94  ? 0.2914 0.2167 0.2901 0.0020  0.0733  -0.0528 94  VAL   B CG1 
1472 C  CG2 . VAL   B 94  ? 0.2246 0.4009 0.2753 -0.0306 -0.0004 0.0275  94  VAL   B CG2 
1473 N  N   . PHE   B 95  ? 0.0810 0.2581 0.3239 -0.0092 0.1231  -0.0988 95  PHE   B N   
1474 C  CA  . PHE   B 95  ? 0.1066 0.1822 0.3292 -0.0926 0.0391  -0.0408 95  PHE   B CA  
1475 C  C   . PHE   B 95  ? 0.0743 0.2678 0.4095 -0.0634 0.0353  -0.0824 95  PHE   B C   
1476 O  O   . PHE   B 95  ? 0.1040 0.2804 0.3540 -0.0447 0.1323  -0.1324 95  PHE   B O   
1477 C  CB  . PHE   B 95  ? 0.0851 0.1745 0.2801 -0.0528 0.1050  -0.0529 95  PHE   B CB  
1478 C  CG  . PHE   B 95  ? 0.2016 0.1924 0.2523 -0.0756 -0.0250 -0.0871 95  PHE   B CG  
1479 C  CD1 . PHE   B 95  ? 0.2383 0.2684 0.3672 -0.0788 0.0715  -0.0478 95  PHE   B CD1 
1480 C  CD2 . PHE   B 95  ? 0.2511 0.2273 0.3080 -0.0767 0.0956  -0.0853 95  PHE   B CD2 
1481 C  CE1 . PHE   B 95  ? 0.2222 0.3138 0.4631 -0.1454 0.1206  -0.0239 95  PHE   B CE1 
1482 C  CE2 . PHE   B 95  ? 0.1793 0.2652 0.2350 -0.1055 0.1320  -0.0622 95  PHE   B CE2 
1483 C  CZ  . PHE   B 95  ? 0.1955 0.2830 0.2997 -0.1724 0.0866  -0.1019 95  PHE   B CZ  
1484 N  N   . THR   B 96  ? 0.0593 0.3931 0.3725 -0.0171 0.1070  -0.1157 96  THR   B N   
1485 C  CA  . THR   B 96  ? 0.1694 0.3815 0.2887 0.0015  0.1168  -0.1035 96  THR   B CA  
1486 C  C   . THR   B 96  ? 0.2971 0.4730 0.3099 -0.0452 0.0434  0.0040  96  THR   B C   
1487 O  O   . THR   B 96  ? 0.2386 0.5603 0.3266 0.0805  0.0653  -0.0362 96  THR   B O   
1488 C  CB  . THR   B 96  ? 0.3527 0.2783 0.5754 -0.1611 0.0177  -0.0901 96  THR   B CB  
1489 O  OG1 . THR   B 96  ? 0.1570 0.2443 0.8577 -0.0417 0.1698  -0.0330 96  THR   B OG1 
1490 N  N   . ALA   B 97  ? 0.2429 0.5010 0.3664 0.0055  0.0712  0.0052  97  ALA   B N   
1491 C  CA  . ALA   B 97  ? 0.1191 0.5488 0.3030 -0.0197 0.0930  0.0818  97  ALA   B CA  
1492 C  C   . ALA   B 97  ? 0.1569 0.5708 0.3965 0.1176  0.0480  -0.0551 97  ALA   B C   
1493 O  O   . ALA   B 97  ? 0.1376 0.7731 0.4388 0.0589  0.0069  -0.1682 97  ALA   B O   
1494 C  CB  . ALA   B 97  ? 0.4328 0.5305 0.4348 -0.0186 0.0124  -0.0333 97  ALA   B CB  
1495 N  N   . ASN   B 98  ? 0.2398 0.2933 0.2816 0.1324  0.0491  -0.1558 98  ASN   B N   
1496 C  CA  . ASN   B 98  ? 0.1582 0.4230 0.3267 0.0222  0.0493  -0.0667 98  ASN   B CA  
1497 C  C   . ASN   B 98  ? 0.0282 0.4525 0.4130 0.0355  -0.0070 -0.0785 98  ASN   B C   
1498 O  O   . ASN   B 98  ? 0.0694 0.4005 0.7043 -0.0037 0.1562  -0.2302 98  ASN   B O   
1499 C  CB  . ASN   B 98  ? 0.2420 0.3482 0.3855 0.0204  -0.0056 -0.0593 98  ASN   B CB  
1500 C  CG  . ASN   B 98  ? 0.1228 0.4510 0.4275 -0.1499 -0.0541 -0.0078 98  ASN   B CG  
1501 O  OD1 . ASN   B 98  ? 0.2870 0.4150 0.4494 -0.0183 -0.1032 -0.0438 98  ASN   B OD1 
1502 N  ND2 . ASN   B 98  ? 0.3130 0.4375 0.4442 -0.1428 -0.0442 -0.0829 98  ASN   B ND2 
1503 N  N   . ARG   B 104 ? 0.5865 0.4820 0.4674 -0.0562 0.0896  -0.2474 104 ARG   B N   
1504 C  CA  . ARG   B 104 ? 0.3761 0.2295 0.3994 -0.0433 0.0141  -0.1207 104 ARG   B CA  
1505 C  C   . ARG   B 104 ? 0.2883 0.3034 0.3744 0.0252  -0.0174 -0.1428 104 ARG   B C   
1506 O  O   . ARG   B 104 ? 0.2011 0.3933 0.4575 0.0941  -0.1206 -0.1591 104 ARG   B O   
1507 C  CB  . ARG   B 104 ? 0.6236 0.3136 0.5900 0.2311  -0.0054 -0.0893 104 ARG   B CB  
1508 N  N   . TYR   B 105 ? 0.2710 0.2310 0.3587 -0.0104 0.0199  -0.1206 105 TYR   B N   
1509 C  CA  . TYR   B 105 ? 0.0980 0.2682 0.3023 0.0363  0.0715  -0.1185 105 TYR   B CA  
1510 C  C   . TYR   B 105 ? 0.0683 0.2062 0.4139 -0.0276 0.0591  -0.1403 105 TYR   B C   
1511 O  O   . TYR   B 105 ? 0.1941 0.2705 0.4398 -0.1141 0.0626  -0.2010 105 TYR   B O   
1512 C  CB  . TYR   B 105 ? 0.2127 0.3005 0.2675 -0.0139 0.1018  -0.1173 105 TYR   B CB  
1513 C  CG  . TYR   B 105 ? 0.0559 0.2924 0.3848 -0.0565 -0.0093 -0.1880 105 TYR   B CG  
1514 C  CD1 . TYR   B 105 ? 0.0915 0.2943 0.3923 -0.0280 0.0318  -0.1475 105 TYR   B CD1 
1515 C  CD2 . TYR   B 105 ? 0.2454 0.2017 0.5262 0.0265  0.2274  -0.1749 105 TYR   B CD2 
1516 C  CE1 . TYR   B 105 ? 0.2340 0.2184 0.3879 0.0406  0.1671  -0.1678 105 TYR   B CE1 
1517 C  CE2 . TYR   B 105 ? 0.2943 0.3070 0.5083 -0.0848 0.1820  -0.1204 105 TYR   B CE2 
1518 C  CZ  . TYR   B 105 ? 0.1482 0.2836 0.3905 -0.0442 0.1080  -0.0582 105 TYR   B CZ  
1519 O  OH  . TYR   B 105 ? 0.2842 0.4506 0.5134 -0.1078 0.2305  -0.0256 105 TYR   B OH  
1520 N  N   . THR   B 106 ? 0.1511 0.2109 0.3345 -0.0045 0.0464  -0.0900 106 THR   B N   
1521 C  CA  . THR   B 106 ? 0.1362 0.1514 0.3833 0.0101  0.0344  -0.0707 106 THR   B CA  
1522 C  C   . THR   B 106 ? 0.1027 0.1305 0.2785 -0.0352 0.0458  -0.1212 106 THR   B C   
1523 O  O   . THR   B 106 ? 0.0291 0.1922 0.2953 -0.0045 0.0257  -0.1558 106 THR   B O   
1524 C  CB  . THR   B 106 ? 0.1183 0.2356 0.3379 -0.0761 -0.0823 -0.1106 106 THR   B CB  
1525 O  OG1 . THR   B 106 ? 0.2235 0.2586 0.3818 0.0440  0.0513  -0.0492 106 THR   B OG1 
1526 C  CG2 . THR   B 106 ? 0.2103 0.3084 0.3141 -0.0500 0.0125  -0.0464 106 THR   B CG2 
1527 N  N   . ILE   B 107 ? 0.1267 0.1761 0.3418 -0.0951 -0.0381 -0.1006 107 ILE   B N   
1528 C  CA  . ILE   B 107 ? 0.0998 0.1840 0.3334 -0.1077 0.0743  -0.1145 107 ILE   B CA  
1529 C  C   . ILE   B 107 ? 0.0924 0.1716 0.2619 -0.0450 0.0346  -0.1095 107 ILE   B C   
1530 O  O   . ILE   B 107 ? 0.1311 0.2781 0.3216 -0.0888 0.0219  -0.2336 107 ILE   B O   
1531 C  CB  . ILE   B 107 ? 0.1234 0.1944 0.2796 -0.1199 0.0557  -0.1228 107 ILE   B CB  
1532 C  CG1 . ILE   B 107 ? 0.1829 0.2597 0.2161 -0.0807 0.0384  -0.0506 107 ILE   B CG1 
1533 C  CG2 . ILE   B 107 ? 0.0947 0.2049 0.4325 -0.0912 -0.0117 -0.1402 107 ILE   B CG2 
1534 C  CD1 . ILE   B 107 ? 0.1727 0.2528 0.2357 -0.0640 0.0542  -0.0886 107 ILE   B CD1 
1535 N  N   . ALA   B 108 ? 0.0284 0.1985 0.2101 0.0189  0.0023  -0.0873 108 ALA   B N   
1536 C  CA  . ALA   B 108 ? 0.0429 0.1567 0.2506 -0.0429 0.0427  -0.0766 108 ALA   B CA  
1537 C  C   . ALA   B 108 ? 0.0321 0.1617 0.2310 -0.0287 0.0207  -0.0424 108 ALA   B C   
1538 O  O   . ALA   B 108 ? 0.0341 0.1389 0.2780 -0.0047 0.0449  -0.0756 108 ALA   B O   
1539 C  CB  . ALA   B 108 ? 0.1176 0.1746 0.2837 -0.0172 0.0300  -0.0084 108 ALA   B CB  
1540 N  N   . ALA   B 109 ? 0.0320 0.1751 0.2709 -0.0193 0.0270  -0.0099 109 ALA   B N   
1541 C  CA  . ALA   B 109 ? 0.0620 0.1590 0.1678 -0.0106 0.0135  -0.0119 109 ALA   B CA  
1542 C  C   . ALA   B 109 ? 0.0664 0.1088 0.1777 -0.0167 0.0206  0.0096  109 ALA   B C   
1543 O  O   . ALA   B 109 ? 0.1241 0.1355 0.2510 -0.0514 0.0871  0.0014  109 ALA   B O   
1544 C  CB  . ALA   B 109 ? 0.1580 0.2098 0.1770 0.0255  -0.0134 -0.0698 109 ALA   B CB  
1545 N  N   . LEU   B 110 ? 0.0266 0.1210 0.1390 -0.0100 0.0069  -0.0133 110 LEU   B N   
1546 C  CA  . LEU   B 110 ? 0.0397 0.1010 0.1345 -0.0188 0.0213  -0.0153 110 LEU   B CA  
1547 C  C   . LEU   B 110 ? 0.0280 0.1239 0.1211 -0.0143 0.0093  -0.0113 110 LEU   B C   
1548 O  O   . LEU   B 110 ? 0.0264 0.1122 0.1447 0.0063  0.0069  -0.0192 110 LEU   B O   
1549 C  CB  . LEU   B 110 ? 0.0891 0.1103 0.1330 0.0002  0.0062  -0.0214 110 LEU   B CB  
1550 C  CG  . LEU   B 110 ? 0.0926 0.1473 0.1025 -0.0117 -0.0120 -0.0166 110 LEU   B CG  
1551 C  CD1 . LEU   B 110 ? 0.0651 0.1596 0.1222 0.0305  0.0056  0.0141  110 LEU   B CD1 
1552 C  CD2 . LEU   B 110 ? 0.0918 0.1569 0.1634 -0.0438 -0.0006 -0.0564 110 LEU   B CD2 
1553 N  N   . LEU   B 111 ? 0.0370 0.1311 0.1326 -0.0318 0.0219  -0.0237 111 LEU   B N   
1554 C  CA  . LEU   B 111 ? 0.0784 0.0944 0.0686 -0.0277 0.0172  -0.0218 111 LEU   B CA  
1555 C  C   . LEU   B 111 ? 0.0297 0.1017 0.0686 -0.0184 0.0020  -0.0118 111 LEU   B C   
1556 O  O   . LEU   B 111 ? 0.0372 0.1299 0.0827 0.0045  -0.0041 0.0278  111 LEU   B O   
1557 C  CB  . LEU   B 111 ? 0.0436 0.1143 0.1114 -0.0216 -0.0024 -0.0087 111 LEU   B CB  
1558 C  CG  . LEU   B 111 ? 0.0717 0.1230 0.1032 -0.0097 -0.0062 -0.0120 111 LEU   B CG  
1559 C  CD1 . LEU   B 111 ? 0.0838 0.1692 0.1018 -0.0009 0.0133  -0.0881 111 LEU   B CD1 
1560 C  CD2 . LEU   B 111 ? 0.0780 0.1578 0.1059 0.0008  0.0340  -0.0272 111 LEU   B CD2 
1561 N  N   . SER   B 112 ? 0.0358 0.0988 0.0705 -0.0161 0.0187  -0.0051 112 SER   B N   
1562 C  CA  . SER   B 112 ? 0.0385 0.1016 0.0914 -0.0052 0.0269  0.0092  112 SER   B CA  
1563 C  C   . SER   B 112 ? 0.0258 0.1344 0.1108 0.0065  0.0029  -0.0049 112 SER   B C   
1564 O  O   . SER   B 112 ? 0.0319 0.1149 0.1046 -0.0208 -0.0165 0.0219  112 SER   B O   
1565 C  CB  . SER   B 112 ? 0.1100 0.1674 0.0552 0.0102  -0.0021 -0.0053 112 SER   B CB  
1566 O  OG  . SER   B 112 ? 0.0536 0.2277 0.1300 -0.0002 -0.0218 0.0308  112 SER   B OG  
1567 N  N   . PRO   B 113 ? 0.0268 0.1355 0.1120 -0.0020 0.0115  -0.0143 113 PRO   B N   
1568 C  CA  . PRO   B 113 ? 0.0293 0.1459 0.0878 0.0007  0.0156  -0.0098 113 PRO   B CA  
1569 C  C   . PRO   B 113 ? 0.0303 0.1450 0.0554 -0.0002 -0.0121 -0.0093 113 PRO   B C   
1570 O  O   . PRO   B 113 ? 0.0301 0.1438 0.0491 0.0231  -0.0013 -0.0195 113 PRO   B O   
1571 C  CB  . PRO   B 113 ? 0.0361 0.1347 0.0894 -0.0157 0.0256  -0.0200 113 PRO   B CB  
1572 C  CG  . PRO   B 113 ? 0.0323 0.1216 0.0793 -0.0253 0.0094  -0.0186 113 PRO   B CG  
1573 C  CD  . PRO   B 113 ? 0.0480 0.1136 0.1048 0.0070  0.0033  -0.0038 113 PRO   B CD  
1574 N  N   . TYR   B 114 ? 0.0646 0.1106 0.0712 0.0031  -0.0295 -0.0103 114 TYR   B N   
1575 C  CA  . TYR   B 114 ? 0.0401 0.1096 0.0848 0.0027  -0.0278 -0.0144 114 TYR   B CA  
1576 C  C   . TYR   B 114 ? 0.0417 0.1089 0.1182 0.0037  -0.0112 0.0008  114 TYR   B C   
1577 O  O   . TYR   B 114 ? 0.0565 0.1156 0.1432 -0.0148 -0.0566 -0.0086 114 TYR   B O   
1578 C  CB  . TYR   B 114 ? 0.0557 0.0943 0.0636 0.0129  -0.0182 0.0089  114 TYR   B CB  
1579 C  CG  . TYR   B 114 ? 0.0394 0.1073 0.0986 -0.0023 -0.0098 0.0127  114 TYR   B CG  
1580 C  CD1 . TYR   B 114 ? 0.0828 0.1556 0.0968 0.0000  0.0133  0.0476  114 TYR   B CD1 
1581 C  CD2 . TYR   B 114 ? 0.0647 0.1105 0.0355 0.0006  -0.0104 -0.0169 114 TYR   B CD2 
1582 C  CE1 . TYR   B 114 ? 0.0940 0.1343 0.1497 0.0091  -0.0087 0.0300  114 TYR   B CE1 
1583 C  CE2 . TYR   B 114 ? 0.1046 0.1370 0.1415 0.0495  -0.0169 0.0665  114 TYR   B CE2 
1584 C  CZ  . TYR   B 114 ? 0.0638 0.1879 0.1407 0.0036  -0.0633 0.0373  114 TYR   B CZ  
1585 O  OH  . TYR   B 114 ? 0.0326 0.2821 0.2321 0.0370  0.0043  -0.0520 114 TYR   B OH  
1586 N  N   . SER   B 115 ? 0.0268 0.1141 0.0816 -0.0011 -0.0092 -0.0011 115 SER   B N   
1587 C  CA  . SER   B 115 ? 0.0282 0.1004 0.0469 0.0041  0.0070  -0.0075 115 SER   B CA  
1588 C  C   . SER   B 115 ? 0.0570 0.1147 0.0808 0.0004  0.0185  -0.0316 115 SER   B C   
1589 O  O   . SER   B 115 ? 0.0433 0.1476 0.0882 -0.0056 -0.0039 -0.0184 115 SER   B O   
1590 C  CB  . SER   B 115 ? 0.0438 0.1043 0.0627 0.0009  0.0094  -0.0486 115 SER   B CB  
1591 O  OG  . SER   B 115 ? 0.0590 0.1942 0.1720 0.0213  -0.0102 -0.0268 115 SER   B OG  
1592 N  N   . TYR   B 116 ? 0.0419 0.1002 0.0502 -0.0213 0.0082  -0.0139 116 TYR   B N   
1593 C  CA  . TYR   B 116 ? 0.0447 0.1130 0.0797 -0.0147 0.0232  -0.0046 116 TYR   B CA  
1594 C  C   . TYR   B 116 ? 0.0474 0.1184 0.0952 -0.0310 0.0083  0.0130  116 TYR   B C   
1595 O  O   . TYR   B 116 ? 0.0281 0.1050 0.1366 -0.0139 0.0018  0.0236  116 TYR   B O   
1596 C  CB  . TYR   B 116 ? 0.0682 0.1149 0.0807 0.0024  -0.0257 0.0149  116 TYR   B CB  
1597 C  CG  . TYR   B 116 ? 0.1219 0.1374 0.0803 -0.0386 -0.0275 0.0018  116 TYR   B CG  
1598 C  CD1 . TYR   B 116 ? 0.1442 0.2188 0.0841 -0.0175 -0.0129 0.0370  116 TYR   B CD1 
1599 C  CD2 . TYR   B 116 ? 0.1163 0.1542 0.1459 -0.0306 -0.0423 0.0132  116 TYR   B CD2 
1600 C  CE1 . TYR   B 116 ? 0.1283 0.3151 0.0327 -0.0472 -0.0192 0.0008  116 TYR   B CE1 
1601 C  CE2 . TYR   B 116 ? 0.1884 0.2913 0.1033 -0.0295 -0.0386 -0.0165 116 TYR   B CE2 
1602 C  CZ  . TYR   B 116 ? 0.1353 0.2794 0.1090 -0.0494 -0.0212 0.0180  116 TYR   B CZ  
1603 O  OH  . TYR   B 116 ? 0.3937 0.4781 0.1691 -0.1978 -0.0775 0.1356  116 TYR   B OH  
1604 N  N   . SER   B 117 ? 0.0382 0.1477 0.0998 -0.0162 0.0249  0.0204  117 SER   B N   
1605 C  CA  A SER   B 117 ? 0.0474 0.1385 0.1499 0.0049  0.0459  -0.0062 117 SER   B CA  
1606 C  CA  B SER   B 117 ? 0.0445 0.1385 0.1556 0.0049  0.0468  -0.0084 117 SER   B CA  
1607 C  C   . SER   B 117 ? 0.0283 0.1370 0.1320 -0.0011 0.0180  -0.0081 117 SER   B C   
1608 O  O   . SER   B 117 ? 0.0559 0.1254 0.1570 0.0025  0.0541  -0.0038 117 SER   B O   
1609 C  CB  A SER   B 117 ? 0.1482 0.1133 0.1666 0.0127  0.0246  -0.0750 117 SER   B CB  
1610 C  CB  B SER   B 117 ? 0.1507 0.1330 0.1615 -0.0093 0.0209  -0.0508 117 SER   B CB  
1611 O  OG  A SER   B 117 ? 0.1167 0.2671 0.1251 0.0464  0.0186  0.0302  117 SER   B OG  
1612 O  OG  B SER   B 117 ? 0.2102 0.2191 0.1352 0.0467  -0.0538 -0.0207 117 SER   B OG  
1613 N  N   . THR   B 118 ? 0.0504 0.1279 0.2135 -0.0167 0.0627  0.0012  118 THR   B N   
1614 C  CA  . THR   B 118 ? 0.0329 0.1058 0.1869 -0.0012 0.0197  0.0165  118 THR   B CA  
1615 C  C   . THR   B 118 ? 0.0333 0.1271 0.2173 0.0100  0.0389  0.0339  118 THR   B C   
1616 O  O   . THR   B 118 ? 0.1054 0.0948 0.3038 0.0129  0.0282  0.0293  118 THR   B O   
1617 C  CB  . THR   B 118 ? 0.0719 0.1649 0.1845 -0.0211 0.0141  0.0149  118 THR   B CB  
1618 O  OG1 . THR   B 118 ? 0.1778 0.2331 0.2298 -0.0091 -0.0272 -0.0413 118 THR   B OG1 
1619 C  CG2 . THR   B 118 ? 0.1073 0.1343 0.1393 0.0529  0.0105  0.0190  118 THR   B CG2 
1620 N  N   . THR   B 119 ? 0.0481 0.1322 0.2009 0.0150  0.0623  0.0181  119 THR   B N   
1621 C  CA  . THR   B 119 ? 0.0318 0.1520 0.1789 -0.0149 0.0206  -0.0086 119 THR   B CA  
1622 C  C   . THR   B 119 ? 0.0842 0.1534 0.1898 -0.0236 0.0281  -0.0163 119 THR   B C   
1623 O  O   . THR   B 119 ? 0.0446 0.1691 0.2725 0.0252  0.0083  -0.0799 119 THR   B O   
1624 C  CB  . THR   B 119 ? 0.0920 0.1560 0.1791 -0.0368 0.0428  -0.0137 119 THR   B CB  
1625 O  OG1 . THR   B 119 ? 0.0890 0.2293 0.2088 -0.0518 -0.0087 -0.0428 119 THR   B OG1 
1626 C  CG2 . THR   B 119 ? 0.1455 0.1626 0.1885 -0.0392 0.0618  -0.0065 119 THR   B CG2 
1627 N  N   . ALA   B 120 ? 0.0767 0.1747 0.1603 -0.0141 -0.0074 0.0187  120 ALA   B N   
1628 C  CA  . ALA   B 120 ? 0.1305 0.1977 0.2182 0.0153  -0.0015 0.0003  120 ALA   B CA  
1629 C  C   . ALA   B 120 ? 0.0259 0.2084 0.2548 -0.0010 0.0039  -0.0263 120 ALA   B C   
1630 O  O   . ALA   B 120 ? 0.0711 0.1827 0.2876 0.0126  -0.0268 -0.0476 120 ALA   B O   
1631 C  CB  . ALA   B 120 ? 0.1328 0.2197 0.2761 0.1213  0.0680  -0.0326 120 ALA   B CB  
1632 N  N   . VAL   B 121 ? 0.0375 0.2229 0.3299 0.0158  -0.0390 -0.1039 121 VAL   B N   
1633 C  CA  . VAL   B 121 ? 0.0843 0.1519 0.3860 -0.0342 -0.0961 -0.0903 121 VAL   B CA  
1634 C  C   . VAL   B 121 ? 0.1109 0.2493 0.4045 0.0286  -0.0451 -0.0847 121 VAL   B C   
1635 O  O   . VAL   B 121 ? 0.1059 0.3235 0.3803 0.0325  0.0161  -0.1605 121 VAL   B O   
1636 C  CB  . VAL   B 121 ? 0.2493 0.1882 0.3641 0.0353  -0.0468 -0.0302 121 VAL   B CB  
1637 C  CG1 . VAL   B 121 ? 0.3272 0.3289 0.3232 -0.0210 -0.0378 0.1820  121 VAL   B CG1 
1638 C  CG2 . VAL   B 121 ? 0.1082 0.1082 0.5153 -0.0007 -0.1492 -0.1313 121 VAL   B CG2 
1639 N  N   . VAL   B 122 ? 0.1217 0.2645 0.2998 0.0270  0.0034  -0.0657 122 VAL   B N   
1640 C  CA  . VAL   B 122 ? 0.0858 0.2510 0.3789 -0.0758 -0.0193 -0.1888 122 VAL   B CA  
1641 C  C   . VAL   B 122 ? 0.2918 0.3552 0.4143 0.0541  -0.0690 -0.0917 122 VAL   B C   
1642 O  O   . VAL   B 122 ? 0.4364 0.3230 0.4236 0.1713  -0.0543 -0.1806 122 VAL   B O   
1643 C  CB  . VAL   B 122 ? 0.3661 0.4285 0.4685 -0.3416 0.0753  -0.1578 122 VAL   B CB  
1644 CA CA  . CA    C .   ? 0.0260 0.2902 0.1655 0.0120  -0.0013 0.0789  201 CA    A CA  
1645 N  N1  . A1IS2 D .   ? 0.0269 0.2020 0.1009 0.0164  0.0049  0.0224  202 A1IS2 A N1  
1646 C  C2  . A1IS2 D .   ? 0.0465 0.1936 0.1416 0.0085  0.0098  0.0048  202 A1IS2 A C2  
1647 C  C3  . A1IS2 D .   ? 0.0908 0.2043 0.1640 0.0085  -0.0072 0.0340  202 A1IS2 A C3  
1648 C  C4  . A1IS2 D .   ? 0.1009 0.1899 0.1662 0.0146  -0.0006 -0.0413 202 A1IS2 A C4  
1649 C  C5  . A1IS2 D .   ? 0.0423 0.1898 0.1084 -0.0140 -0.0148 0.0075  202 A1IS2 A C5  
1650 C  C6  . A1IS2 D .   ? 0.0416 0.1769 0.1469 -0.0214 0.0026  0.0265  202 A1IS2 A C6  
1651 C  C7  . A1IS2 D .   ? 0.0298 0.1560 0.1099 -0.0043 -0.0192 0.0011  202 A1IS2 A C7  
1652 C  C8  . A1IS2 D .   ? 0.1118 0.1622 0.1010 -0.0195 -0.0175 -0.0230 202 A1IS2 A C8  
1653 C  C9  . A1IS2 D .   ? 0.0605 0.1705 0.1542 0.0000  0.0056  -0.0115 202 A1IS2 A C9  
1654 C  C10 . A1IS2 D .   ? 0.0444 0.1830 0.1461 0.0042  -0.0181 0.0075  202 A1IS2 A C10 
1655 C  C11 . A1IS2 D .   ? 0.0899 0.1749 0.1656 0.0295  -0.0014 -0.0384 202 A1IS2 A C11 
1656 C  C12 . A1IS2 D .   ? 0.1164 0.1993 0.1483 -0.0032 0.0201  -0.0009 202 A1IS2 A C12 
1657 C  C13 . A1IS2 D .   ? 0.1531 0.1705 0.1203 0.0016  0.0152  -0.0066 202 A1IS2 A C13 
1658 C  C1  . A1IS2 D .   ? 0.0493 0.1832 0.1472 -0.0015 0.0073  0.0014  202 A1IS2 A C1  
1659 N  N   . A1IS2 D .   ? 0.0256 0.1749 0.1150 0.0007  -0.0052 -0.0032 202 A1IS2 A N   
1660 C  C   . A1IS2 D .   ? 0.0263 0.1815 0.1643 -0.0009 -0.0121 0.0040  202 A1IS2 A C   
1661 N  N2  . A1IS2 D .   ? 0.0490 0.2356 0.1487 0.0325  0.0283  -0.0450 202 A1IS2 A N2  
1662 CA CA  . CA    E .   ? 0.1448 0.3785 0.3088 -0.0422 -0.0327 -0.0249 203 CA    A CA  
1663 CA CA  . CA    F .   ? 0.5512 0.8428 1.2059 -0.1049 0.2366  -0.2874 201 CA    B CA  
1664 N  N1  . A1IS2 G .   ? 0.0677 0.2856 0.1652 0.0098  0.0243  0.0188  202 A1IS2 B N1  
1665 C  C2  . A1IS2 G .   ? 0.0425 0.2629 0.1511 -0.0181 0.0438  0.0094  202 A1IS2 B C2  
1666 C  C3  . A1IS2 G .   ? 0.1215 0.2309 0.1860 -0.0029 0.0079  -0.0559 202 A1IS2 B C3  
1667 C  C4  . A1IS2 G .   ? 0.1679 0.2251 0.1763 0.0182  -0.0001 0.0467  202 A1IS2 B C4  
1668 C  C5  . A1IS2 G .   ? 0.1189 0.2698 0.1985 0.0161  0.0005  0.0059  202 A1IS2 B C5  
1669 C  C6  . A1IS2 G .   ? 0.1199 0.2608 0.1951 0.0075  0.0215  -0.0271 202 A1IS2 B C6  
1670 C  C7  . A1IS2 G .   ? 0.1156 0.2452 0.1781 0.0130  0.0089  -0.0059 202 A1IS2 B C7  
1671 C  C8  . A1IS2 G .   ? 0.1565 0.2410 0.1941 0.0001  0.0165  0.0334  202 A1IS2 B C8  
1672 C  C9  . A1IS2 G .   ? 0.1508 0.2361 0.2143 0.0065  0.0174  0.0171  202 A1IS2 B C9  
1673 C  C10 . A1IS2 G .   ? 0.1929 0.2480 0.2430 0.0104  -0.0127 0.0192  202 A1IS2 B C10 
1674 C  C11 . A1IS2 G .   ? 0.2777 0.2435 0.1830 0.0154  0.0312  0.0306  202 A1IS2 B C11 
1675 C  C12 . A1IS2 G .   ? 0.2041 0.2559 0.1717 0.0228  0.0362  -0.0495 202 A1IS2 B C12 
1676 C  C13 . A1IS2 G .   ? 0.1536 0.2249 0.2222 -0.0139 0.0213  0.0348  202 A1IS2 B C13 
1677 C  C1  . A1IS2 G .   ? 0.0538 0.2483 0.1515 0.0374  0.0393  0.0025  202 A1IS2 B C1  
1678 N  N   . A1IS2 G .   ? 0.0766 0.2648 0.1603 -0.0109 0.0680  -0.0150 202 A1IS2 B N   
1679 C  C   . A1IS2 G .   ? 0.0316 0.2799 0.1381 0.0064  0.0263  0.0035  202 A1IS2 B C   
1680 N  N2  . A1IS2 G .   ? 0.1510 0.3225 0.1854 0.0011  0.0291  0.0555  202 A1IS2 B N2  
1681 O  O   . HOH   H .   ? 0.0435 0.2868 0.3341 0.0073  0.0723  -0.0463 301 HOH   A O   
1682 O  O   . HOH   H .   ? 0.1311 0.5419 0.1855 -0.0141 -0.0110 0.1490  302 HOH   A O   
1683 O  O   . HOH   H .   ? 0.1213 0.2124 0.3768 0.0359  -0.0331 -0.0453 303 HOH   A O   
1684 O  O   . HOH   H .   ? 0.3507 0.3844 0.2734 0.0199  -0.0902 -0.1256 304 HOH   A O   
1685 O  O   . HOH   H .   ? 0.1479 0.3677 0.1992 -0.1784 0.0619  0.0183  305 HOH   A O   
1686 O  O   . HOH   H .   ? 0.0291 0.2483 0.1094 -0.0282 0.0040  0.0051  306 HOH   A O   
1687 O  O   . HOH   H .   ? 0.1000 0.3338 0.1886 0.0290  -0.0105 -0.0212 307 HOH   A O   
1688 O  O   . HOH   H .   ? 0.2020 0.4330 0.3789 0.0675  -0.0424 0.2190  308 HOH   A O   
1689 O  O   . HOH   H .   ? 0.1711 0.3463 0.4126 0.1228  -0.0665 -0.0297 309 HOH   A O   
1690 O  O   . HOH   H .   ? 0.2283 0.4262 0.2888 -0.0059 0.0321  -0.0625 310 HOH   A O   
1691 O  O   . HOH   H .   ? 0.3172 0.2097 0.3742 0.0927  0.1489  0.0009  311 HOH   A O   
1692 O  O   . HOH   H .   ? 0.2072 0.2829 0.0908 0.0269  -0.0434 -0.0359 312 HOH   A O   
1693 O  O   . HOH   H .   ? 0.1964 0.4416 0.2250 -0.0222 0.0060  -0.1074 313 HOH   A O   
1694 O  O   . HOH   H .   ? 0.0651 0.2097 0.1622 -0.0181 -0.0738 0.0348  314 HOH   A O   
1695 O  O   . HOH   H .   ? 0.0506 0.4515 0.4595 0.0790  0.0896  0.1352  315 HOH   A O   
1696 O  O   . HOH   H .   ? 0.0935 0.3332 0.3986 0.0662  0.1153  0.1111  316 HOH   A O   
1697 O  O   . HOH   H .   ? 0.0950 0.1702 0.2054 -0.0021 -0.1067 0.0523  317 HOH   A O   
1698 O  O   . HOH   H .   ? 0.0989 0.4366 0.3123 -0.1018 -0.0517 -0.0033 318 HOH   A O   
1699 O  O   . HOH   H .   ? 0.0316 0.2199 0.1127 0.0238  0.0211  0.0370  319 HOH   A O   
1700 O  O   . HOH   H .   ? 0.1722 0.2427 0.1712 -0.0119 -0.0579 0.0550  320 HOH   A O   
1701 O  O   . HOH   H .   ? 0.1546 0.4141 0.1812 -0.0156 0.0436  0.1033  321 HOH   A O   
1702 O  O   . HOH   H .   ? 0.0254 0.2860 0.2935 -0.0043 0.0007  0.1217  322 HOH   A O   
1703 O  O   . HOH   H .   ? 0.1377 0.3424 0.1869 -0.0695 -0.0475 0.0772  323 HOH   A O   
1704 O  O   . HOH   H .   ? 0.1533 0.1675 0.2592 -0.0363 0.0063  -0.0151 324 HOH   A O   
1705 O  O   . HOH   H .   ? 0.4024 0.3954 0.2257 0.1466  0.0156  -0.0134 325 HOH   A O   
1706 O  O   . HOH   H .   ? 0.1071 0.2664 0.2245 0.0091  0.0346  0.0533  326 HOH   A O   
1707 O  O   . HOH   H .   ? 0.0460 0.4417 0.4285 0.0104  0.0900  0.1138  327 HOH   A O   
1708 O  O   . HOH   H .   ? 0.1000 0.3731 0.1718 0.0286  -0.0123 0.0857  328 HOH   A O   
1709 O  O   . HOH   H .   ? 0.0664 0.4598 0.4823 0.0970  -0.0125 -0.2662 329 HOH   A O   
1710 O  O   . HOH   H .   ? 0.1267 0.3095 0.1931 0.0415  0.0329  0.0154  330 HOH   A O   
1711 O  O   . HOH   H .   ? 0.1121 0.5149 0.3815 -0.0226 0.0052  0.0500  331 HOH   A O   
1712 O  O   . HOH   H .   ? 0.0395 0.2299 0.0556 -0.0522 0.0047  -0.0365 332 HOH   A O   
1713 O  O   . HOH   H .   ? 0.2681 0.4579 0.3431 0.0214  -0.0910 -0.0698 333 HOH   A O   
1714 O  O   . HOH   H .   ? 0.2650 0.2795 0.3774 -0.0391 -0.0979 0.0379  334 HOH   A O   
1715 O  O   . HOH   H .   ? 0.0467 0.2327 0.1490 -0.0050 -0.0485 0.0650  335 HOH   A O   
1716 O  O   . HOH   H .   ? 0.2849 0.4391 0.3850 -0.1846 0.1035  0.0225  336 HOH   A O   
1717 O  O   . HOH   H .   ? 0.0982 0.4548 0.2517 -0.0287 0.0235  -0.1378 337 HOH   A O   
1718 O  O   . HOH   H .   ? 0.1696 0.2971 0.2447 0.0104  0.0762  0.0297  338 HOH   A O   
1719 O  O   . HOH   H .   ? 0.1889 0.3781 0.3632 -0.0593 -0.1704 0.1376  339 HOH   A O   
1720 O  O   . HOH   H .   ? 0.1684 0.3350 0.5070 -0.0823 -0.0315 -0.1449 340 HOH   A O   
1721 O  O   . HOH   H .   ? 0.0380 0.4609 0.2359 -0.0005 0.0288  -0.0282 341 HOH   A O   
1722 O  O   . HOH   H .   ? 0.3232 0.2485 0.3786 0.0408  -0.0555 -0.0534 342 HOH   A O   
1723 O  O   . HOH   H .   ? 0.1541 0.4131 0.1318 0.0837  -0.0156 -0.0244 343 HOH   A O   
1724 O  O   . HOH   H .   ? 0.1603 0.3163 0.1820 0.0040  0.0046  0.1074  344 HOH   A O   
1725 O  O   . HOH   I .   ? 0.1305 0.6072 0.6206 -0.0266 0.0716  -0.5402 301 HOH   B O   
1726 O  O   . HOH   I .   ? 0.0448 0.2243 0.1389 -0.0092 0.0470  -0.0175 302 HOH   B O   
1727 O  O   . HOH   I .   ? 0.1715 0.3376 0.5867 -0.0856 0.0340  -0.0775 303 HOH   B O   
1728 O  O   . HOH   I .   ? 0.0677 0.2978 0.1200 -0.0213 0.0099  -0.0141 304 HOH   B O   
1729 O  O   . HOH   I .   ? 0.1089 0.3027 0.2463 -0.0094 -0.0286 -0.0435 305 HOH   B O   
1730 O  O   . HOH   I .   ? 0.0683 0.2577 0.1356 -0.0454 0.0372  0.0599  306 HOH   B O   
1731 O  O   . HOH   I .   ? 0.0776 0.2178 0.1310 0.0247  0.0160  0.0254  307 HOH   B O   
1732 O  O   . HOH   I .   ? 0.0342 0.2424 0.2320 0.0329  0.0319  0.0227  308 HOH   B O   
1733 O  O   . HOH   I .   ? 0.0341 0.1430 0.1273 -0.0269 0.0219  -0.0261 309 HOH   B O   
1734 O  O   . HOH   I .   ? 0.1618 0.2679 0.3110 0.0655  0.0305  0.0766  310 HOH   B O   
1735 O  O   . HOH   I .   ? 0.0658 0.3550 0.2091 0.0239  -0.0158 -0.0832 311 HOH   B O   
1736 O  O   . HOH   I .   ? 0.1989 0.4213 0.4289 -0.0812 0.0655  -0.1699 312 HOH   B O   
1737 O  O   . HOH   I .   ? 0.0972 0.3413 0.4120 -0.0614 0.0926  -0.0369 313 HOH   B O   
1738 O  O   . HOH   I .   ? 0.0493 0.2434 0.2418 0.0592  0.0079  -0.0823 314 HOH   B O   
1739 O  O   . HOH   I .   ? 0.1302 0.2286 0.6289 0.0000  0.0030  0.0000  315 HOH   B O   
# 
