data_9H7C
# 
_entry.id   9H7C 
# 
_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   9H7C         pdb_00009h7c 10.2210/pdb9h7c/pdb 
WWPDB D_1292142780 ?            ?                   
# 
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                        9H7C 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.wood@ucl.ac.uk 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Wood 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4106-775X 
# 
_audit_author.name               'Chen, W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8180-366X 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Plos One' ? ? 1932-6203 ? ? 20 ? e0323816 e0323816 
'Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.' 2025 ? 
10.1371/journal.pone.0323816 40367241 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv    ? ? 2692-8205 ? ? ?  ? ?        ?        
'Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method'  2025 ? 
10.1101/2025.02.22.639275    ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, W.' 1 0000-0002-8180-366X 
1       'Chen, W.' 2 0000-0002-8180-366X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Transthyretin                13777.360 2  ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                40.078    2  ? ? ? ? 
3 non-polymer syn '4-(1H-IMIDAZOL-1-YL)PHENOL' 160.173   2  ? ? ? ? 
4 water       nat water                        18.015    97 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        ATTR,Prealbumin,TBPA 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'                CA  
3 '4-(1H-IMIDAZOL-1-YL)PHENOL' MSR 
4 water                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   THR n 
1 4   GLY n 
1 5   THR n 
1 6   GLY n 
1 7   GLU n 
1 8   SER n 
1 9   LYS n 
1 10  CYS n 
1 11  PRO n 
1 12  LEU n 
1 13  MET n 
1 14  VAL n 
1 15  LYS n 
1 16  VAL n 
1 17  LEU n 
1 18  ASP n 
1 19  ALA n 
1 20  VAL n 
1 21  ARG n 
1 22  GLY n 
1 23  SER n 
1 24  PRO n 
1 25  ALA n 
1 26  ILE n 
1 27  ASN n 
1 28  VAL n 
1 29  ALA n 
1 30  VAL n 
1 31  HIS n 
1 32  VAL n 
1 33  PHE n 
1 34  ARG n 
1 35  LYS n 
1 36  ALA n 
1 37  ALA n 
1 38  ASP n 
1 39  ASP n 
1 40  THR n 
1 41  TRP n 
1 42  GLU n 
1 43  PRO n 
1 44  PHE n 
1 45  ALA n 
1 46  SER n 
1 47  GLY n 
1 48  LYS n 
1 49  THR n 
1 50  SER n 
1 51  GLU n 
1 52  SER n 
1 53  GLY n 
1 54  GLU n 
1 55  LEU n 
1 56  HIS n 
1 57  GLY n 
1 58  LEU n 
1 59  THR n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  GLU n 
1 64  PHE n 
1 65  VAL n 
1 66  GLU n 
1 67  GLY n 
1 68  ILE n 
1 69  TYR n 
1 70  LYS n 
1 71  VAL n 
1 72  GLU n 
1 73  ILE n 
1 74  ASP n 
1 75  THR n 
1 76  LYS n 
1 77  SER n 
1 78  TYR n 
1 79  TRP n 
1 80  LYS n 
1 81  ALA n 
1 82  LEU n 
1 83  GLY n 
1 84  ILE n 
1 85  SER n 
1 86  PRO n 
1 87  PHE n 
1 88  HIS n 
1 89  GLU n 
1 90  HIS n 
1 91  ALA n 
1 92  GLU n 
1 93  VAL n 
1 94  VAL n 
1 95  PHE n 
1 96  THR n 
1 97  ALA n 
1 98  ASN n 
1 99  ASP n 
1 100 SER n 
1 101 GLY n 
1 102 PRO n 
1 103 ARG n 
1 104 ARG n 
1 105 TYR n 
1 106 THR n 
1 107 ILE n 
1 108 ALA n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 SER n 
1 113 PRO n 
1 114 TYR n 
1 115 SER n 
1 116 TYR n 
1 117 SER n 
1 118 THR n 
1 119 THR n 
1 120 ALA n 
1 121 VAL n 
1 122 VAL n 
1 123 THR n 
1 124 ASN n 
1 125 PRO n 
1 126 LYS n 
1 127 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   127 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTR, PALB' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    Blood 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                      ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                     ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                   ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'              ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'                ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE                     ? 'C3 H7 N O2 S'   121.158 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'              ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                      ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                    ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                        ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                   ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                      ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                       ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                   ? 'C5 H11 N O2 S'  149.211 
MSR non-polymer         . '4-(1H-IMIDAZOL-1-YL)PHENOL' ? 'C9 H8 N2 O'     160.173 
PHE 'L-peptide linking' y PHENYLALANINE                ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                      ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                       ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                    ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                   ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                     ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                       ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  CYS 10  10  ?   ?   ?   B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  TRP 41  41  41  TRP TRP B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  PHE 44  44  44  PHE PHE B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  ?   ?   ?   B . n 
B 1 100 SER 100 100 ?   ?   ?   B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ASN 124 124 ?   ?   ?   B . n 
B 1 125 PRO 125 125 ?   ?   ?   B . n 
B 1 126 LYS 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MSR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MSR 
_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 MSR 1  202 1  MSR 004 A . 
E 2 CA  1  201 1  CA  CA  B . 
F 3 MSR 1  202 2  MSR 004 B . 
G 4 HOH 1  301 62 HOH HOH A . 
G 4 HOH 2  302 33 HOH HOH A . 
G 4 HOH 3  303 11 HOH HOH A . 
G 4 HOH 4  304 44 HOH HOH A . 
G 4 HOH 5  305 18 HOH HOH A . 
G 4 HOH 6  306 70 HOH HOH A . 
G 4 HOH 7  307 32 HOH HOH A . 
G 4 HOH 8  308 3  HOH HOH A . 
G 4 HOH 9  309 37 HOH HOH A . 
G 4 HOH 10 310 31 HOH HOH A . 
G 4 HOH 11 311 30 HOH HOH A . 
G 4 HOH 12 312 66 HOH HOH A . 
G 4 HOH 13 313 60 HOH HOH A . 
G 4 HOH 14 314 53 HOH HOH A . 
G 4 HOH 15 315 13 HOH HOH A . 
G 4 HOH 16 316 85 HOH HOH A . 
G 4 HOH 17 317 48 HOH HOH A . 
G 4 HOH 18 318 22 HOH HOH A . 
G 4 HOH 19 319 59 HOH HOH A . 
G 4 HOH 20 320 29 HOH HOH A . 
G 4 HOH 21 321 55 HOH HOH A . 
G 4 HOH 22 322 2  HOH HOH A . 
G 4 HOH 23 323 12 HOH HOH A . 
G 4 HOH 24 324 25 HOH HOH A . 
G 4 HOH 25 325 10 HOH HOH A . 
G 4 HOH 26 326 54 HOH HOH A . 
G 4 HOH 27 327 94 HOH HOH A . 
G 4 HOH 28 328 88 HOH HOH A . 
G 4 HOH 29 329 35 HOH HOH A . 
G 4 HOH 30 330 4  HOH HOH A . 
G 4 HOH 31 331 58 HOH HOH A . 
G 4 HOH 32 332 15 HOH HOH A . 
G 4 HOH 33 333 69 HOH HOH A . 
G 4 HOH 34 334 57 HOH HOH A . 
G 4 HOH 35 335 39 HOH HOH A . 
G 4 HOH 36 336 20 HOH HOH A . 
G 4 HOH 37 337 34 HOH HOH A . 
G 4 HOH 38 338 87 HOH HOH A . 
G 4 HOH 39 339 42 HOH HOH A . 
G 4 HOH 40 340 47 HOH HOH A . 
G 4 HOH 41 341 14 HOH HOH A . 
G 4 HOH 42 342 28 HOH HOH A . 
G 4 HOH 43 343 52 HOH HOH A . 
G 4 HOH 44 344 74 HOH HOH A . 
G 4 HOH 45 345 50 HOH HOH A . 
G 4 HOH 46 346 16 HOH HOH A . 
G 4 HOH 47 347 36 HOH HOH A . 
G 4 HOH 48 348 6  HOH HOH A . 
G 4 HOH 49 349 49 HOH HOH A . 
G 4 HOH 50 350 63 HOH HOH A . 
G 4 HOH 51 351 89 HOH HOH A . 
G 4 HOH 52 352 71 HOH HOH A . 
G 4 HOH 53 353 46 HOH HOH A . 
G 4 HOH 54 354 75 HOH HOH A . 
G 4 HOH 55 355 65 HOH HOH A . 
G 4 HOH 56 356 17 HOH HOH A . 
G 4 HOH 57 357 79 HOH HOH A . 
G 4 HOH 58 358 41 HOH HOH A . 
G 4 HOH 59 359 96 HOH HOH A . 
G 4 HOH 60 360 77 HOH HOH A . 
G 4 HOH 61 361 78 HOH HOH A . 
H 4 HOH 1  301 97 HOH HOH B . 
H 4 HOH 2  302 68 HOH HOH B . 
H 4 HOH 3  303 26 HOH HOH B . 
H 4 HOH 4  304 5  HOH HOH B . 
H 4 HOH 5  305 76 HOH HOH B . 
H 4 HOH 6  306 21 HOH HOH B . 
H 4 HOH 7  307 7  HOH HOH B . 
H 4 HOH 8  308 23 HOH HOH B . 
H 4 HOH 9  309 40 HOH HOH B . 
H 4 HOH 10 310 73 HOH HOH B . 
H 4 HOH 11 311 83 HOH HOH B . 
H 4 HOH 12 312 1  HOH HOH B . 
H 4 HOH 13 313 8  HOH HOH B . 
H 4 HOH 14 314 72 HOH HOH B . 
H 4 HOH 15 315 67 HOH HOH B . 
H 4 HOH 16 316 19 HOH HOH B . 
H 4 HOH 17 317 9  HOH HOH B . 
H 4 HOH 18 318 81 HOH HOH B . 
H 4 HOH 19 319 90 HOH HOH B . 
H 4 HOH 20 320 93 HOH HOH B . 
H 4 HOH 21 321 24 HOH HOH B . 
H 4 HOH 22 322 56 HOH HOH B . 
H 4 HOH 23 323 80 HOH HOH B . 
H 4 HOH 24 324 38 HOH HOH B . 
H 4 HOH 25 325 64 HOH HOH B . 
H 4 HOH 26 326 45 HOH HOH B . 
H 4 HOH 27 327 27 HOH HOH B . 
H 4 HOH 28 328 82 HOH HOH B . 
H 4 HOH 29 329 51 HOH HOH B . 
H 4 HOH 30 330 84 HOH HOH B . 
H 4 HOH 31 331 43 HOH HOH B . 
H 4 HOH 32 332 91 HOH HOH B . 
H 4 HOH 33 333 92 HOH HOH B . 
H 4 HOH 34 334 95 HOH HOH B . 
H 4 HOH 35 335 61 HOH HOH B . 
H 4 HOH 36 336 86 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A CYS 10  ? CB  ? A CYS 10  CB  
2  1 Y 1 A CYS 10  ? SG  ? A CYS 10  SG  
3  1 Y 1 A MET 13  ? CE  ? A MET 13  CE  
4  1 Y 1 A ARG 21  ? CZ  ? A ARG 21  CZ  
5  1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
6  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
7  1 Y 1 A LYS 35  ? CG  ? A LYS 35  CG  
8  1 Y 1 A LYS 35  ? CD  ? A LYS 35  CD  
9  1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
10 1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
11 1 Y 1 A ASP 39  ? CG  ? A ASP 39  CG  
12 1 Y 1 A ASP 39  ? OD1 ? A ASP 39  OD1 
13 1 Y 1 A ASP 39  ? OD2 ? A ASP 39  OD2 
14 1 Y 1 A GLU 42  ? CG  ? A GLU 42  CG  
15 1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
16 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
17 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
18 1 Y 1 A LYS 48  ? CG  ? A LYS 48  CG  
19 1 Y 1 A LYS 48  ? CD  ? A LYS 48  CD  
20 1 Y 1 A LYS 48  ? CE  ? A LYS 48  CE  
21 1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
22 1 Y 1 A GLU 51  ? CG  ? A GLU 51  CG  
23 1 Y 1 A GLU 51  ? CD  ? A GLU 51  CD  
24 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
25 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
26 1 Y 1 A GLU 54  ? OE2 ? A GLU 54  OE2 
27 1 Y 1 A GLU 61  ? CG  ? A GLU 61  CG  
28 1 Y 1 A GLU 61  ? CD  ? A GLU 61  CD  
29 1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
30 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
31 1 Y 1 A GLU 72  ? OE2 ? A GLU 72  OE2 
32 1 Y 1 A LYS 76  ? CE  ? A LYS 76  CE  
33 1 Y 1 A LYS 76  ? NZ  ? A LYS 76  NZ  
34 1 Y 1 A LYS 80  ? CG  ? A LYS 80  CG  
35 1 Y 1 A LYS 80  ? CD  ? A LYS 80  CD  
36 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
37 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
38 1 Y 1 A ARG 104 ? CG  ? A ARG 104 CG  
39 1 Y 1 A ARG 104 ? CD  ? A ARG 104 CD  
40 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
41 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
42 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
43 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
44 1 Y 1 A PRO 125 ? C   ? A PRO 125 C   
45 1 Y 1 A PRO 125 ? O   ? A PRO 125 O   
46 1 Y 1 B MET 13  ? CE  ? B MET 13  CE  
47 1 Y 1 B ARG 21  ? CG  ? B ARG 21  CG  
48 1 Y 1 B ARG 21  ? CD  ? B ARG 21  CD  
49 1 Y 1 B ARG 21  ? NE  ? B ARG 21  NE  
50 1 Y 1 B ARG 21  ? CZ  ? B ARG 21  CZ  
51 1 Y 1 B ARG 21  ? NH1 ? B ARG 21  NH1 
52 1 Y 1 B ARG 21  ? NH2 ? B ARG 21  NH2 
53 1 Y 1 B ARG 34  ? NE  ? B ARG 34  NE  
54 1 Y 1 B ARG 34  ? CZ  ? B ARG 34  CZ  
55 1 Y 1 B ARG 34  ? NH1 ? B ARG 34  NH1 
56 1 Y 1 B ARG 34  ? NH2 ? B ARG 34  NH2 
57 1 Y 1 B LYS 35  ? CG  ? B LYS 35  CG  
58 1 Y 1 B LYS 35  ? CD  ? B LYS 35  CD  
59 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
60 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
61 1 Y 1 B ASP 39  ? CG  ? B ASP 39  CG  
62 1 Y 1 B ASP 39  ? OD1 ? B ASP 39  OD1 
63 1 Y 1 B ASP 39  ? OD2 ? B ASP 39  OD2 
64 1 Y 1 B GLU 42  ? CG  ? B GLU 42  CG  
65 1 Y 1 B GLU 42  ? CD  ? B GLU 42  CD  
66 1 Y 1 B GLU 42  ? OE1 ? B GLU 42  OE1 
67 1 Y 1 B GLU 42  ? OE2 ? B GLU 42  OE2 
68 1 Y 1 B LYS 48  ? NZ  ? B LYS 48  NZ  
69 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
70 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
71 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
72 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
73 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
74 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
75 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
76 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
77 1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
78 1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
79 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
80 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
81 1 Y 1 B GLU 72  ? OE1 ? B GLU 72  OE1 
82 1 Y 1 B GLU 72  ? OE2 ? B GLU 72  OE2 
83 1 Y 1 B LYS 80  ? NZ  ? B LYS 80  NZ  
84 1 Y 1 B ASN 98  ? CG  ? B ASN 98  CG  
85 1 Y 1 B ASN 98  ? OD1 ? B ASN 98  OD1 
86 1 Y 1 B ASN 98  ? ND2 ? B ASN 98  ND2 
87 1 Y 1 B ARG 103 ? CG  ? B ARG 103 CG  
88 1 Y 1 B ARG 103 ? CD  ? B ARG 103 CD  
89 1 Y 1 B ARG 103 ? NE  ? B ARG 103 NE  
90 1 Y 1 B ARG 103 ? CZ  ? B ARG 103 CZ  
91 1 Y 1 B ARG 103 ? NH1 ? B ARG 103 NH1 
92 1 Y 1 B ARG 103 ? NH2 ? B ARG 103 NH2 
93 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
94 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
95 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
96 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
97 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
98 1 Y 1 B ARG 104 ? NH2 ? B ARG 104 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.7.0032 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .        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                     9H7C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.034 
_cell.length_a_esd                 ? 
_cell.length_b                     85.040 
_cell.length_b_esd                 ? 
_cell.length_c                     63.639 
_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                         9H7C 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H7C 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.40 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES, 200 mM CaCl2, 28% v/v PEG400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-02-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.27 
_reflns.d_resolution_low                               50 
_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                                     59970 
_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                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_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                                0.026 
_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                              0.05 
_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                                    1.27 
_reflns_shell.d_res_low                                     1.303 
_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                             3748 
_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                               0.338 
_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                          89.36 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.609 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.01 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.02 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.708 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_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                                 9H7C 
_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                            1.27 
_refine.ls_d_res_low                             35.35 
_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                     56888 
_refine.ls_number_reflns_R_free                  3038 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.31 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16778 
_refine.ls_R_factor_R_free                       0.20869 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16572 
_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                       0.045 
_refine.pdbx_overall_ESU_R_Free                  0.048 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.533 
_refine.overall_SU_ML                            0.030 
_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                       1.27 
_refine_hist.d_res_low                        35.35 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1782 
_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        1659 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_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' ? 0.022  0.019  1765 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1575 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.156  1.952  2428 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.942  3.000  3617 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.265  5.000  233  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.007 23.509 57   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.488 15.000 228  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.600  15.000 2    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.155  0.200  286  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.021  1999 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  397  ? 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' ? 2.914  1.548  916  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.914  1.549  917  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.332  2.330  1144 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.337  2.329  1143 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.512  1.826  849  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.510  1.827  850  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.075  2.639  1281 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.232  13.797 1929 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.232  13.802 1930 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 7.849  3.000  3339 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 16.291 5.000  23   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 9.586  5.000  3362 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.270 
_refine_ls_shell.d_res_low                        1.303 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             200 
_refine_ls_shell.number_reflns_R_work             3748 
_refine_ls_shell.percent_reflns_obs               89.36 
_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                  0.236 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.284 
# 
_struct.entry_id                     9H7C 
_struct.title                        'Human Transthyretin in Complex with 4-(1H-imidazol-1-yl)phenol' 
_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        9H7C 
_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 3 ? 
G N N 4 ? 
H 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 9H7C A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7C 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)' 8200  ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  17830 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 74 ? LEU A 82 ? ASP A 74 LEU A 82 1 ? 9 
HELX_P HELX_P2 AA2 ASP B 74 ? LEU B 82 ? ASP B 74 LEU B 82 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_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 ? ? ? ? ? ? ? 2.383 ? ? 
metalc2 metalc ? ? A ASP 99 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.517 ? ? 
metalc3 metalc ? ? A ASP 99 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.402 ? ? 
metalc4 metalc ? ? C CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? A CA  201 A HOH 319 4_557 ? ? ? ? ? ? ? 2.308 ? ? 
metalc5 metalc ? ? C CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? A CA  201 A HOH 333 4_557 ? ? ? ? ? ? ? 2.427 ? ? 
metalc6 metalc ? ? C CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? A CA  201 A HOH 350 1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc7 metalc ? ? B GLU 66 OE2 ? ? ? 1_555 E CA  . CA ? ? B GLU 66  B CA  201 1_555 ? ? ? ? ? ? ? 2.559 ? ? 
metalc8 metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? B CA  201 B HOH 302 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc9 metalc ? ? E CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? B CA  201 B HOH 305 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
# 
_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_555 100.2 ? 
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 77.4  ? 
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 71.4  ? 
4  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 319 ? 4_557 164.0 ? 
5  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 319 ? 4_557 83.7  ? 
6  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 319 ? 4_557 89.3  ? 
7  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 333 ? 4_557 110.4 ? 
8  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 333 ? 4_557 127.4 ? 
9  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 333 ? 4_557 155.1 ? 
10 O   ? G HOH .  ? A HOH 319 ? 4_557 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 333 ? 4_557 78.3  ? 
11 OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 85.0  ? 
12 O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 149.4 ? 
13 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 80.5  ? 
14 O   ? G HOH .  ? A HOH 319 ? 4_557 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 84.0  ? 
15 O   ? G HOH .  ? A HOH 333 ? 4_557 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 76.8  ? 
16 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? E CA . ? B CA 201 ? 1_555 O   ? H HOH .  ? B HOH 302 ? 1_555 72.5  ? 
17 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? E CA . ? B CA 201 ? 1_555 O   ? H HOH .  ? B HOH 305 ? 1_555 66.0  ? 
18 O   ? H HOH .  ? B HOH 302 ? 1_555 CA ? E CA . ? B CA 201 ? 1_555 O   ? H HOH .  ? B HOH 305 ? 1_555 94.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA1 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 
AA1 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA1 8 SER B 23  ? PRO B 24  ? SER B 23  PRO B 24  
AA2 1 GLU A 54  ? LEU A 55  ? GLU A 54  LEU A 55  
AA2 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA2 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA2 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA2 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA2 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 
AA2 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA2 8 GLU B 54  ? LEU B 55  ? GLU B 54  LEU B 55  
AA3 1 TRP A 41  ? LYS A 48  ? TRP A 41  LYS A 48  
AA3 2 ALA A 29  ? LYS A 35  ? ALA A 29  LYS A 35  
AA3 3 GLY A 67  ? ILE A 73  ? GLY A 67  ILE A 73  
AA3 4 ALA A 91  ? ALA A 97  ? ALA A 91  ALA A 97  
AA3 5 HIS B 88  ? ALA B 97  ? HIS B 88  ALA B 97  
AA3 6 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA3 7 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA3 8 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA1 3 4 N ALA A 108 ? N ALA A 108 O THR A 119 ? O THR A 119 
AA1 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA1 5 6 O THR B 123 ? O THR B 123 N ARG B 104 ? N ARG B 104 
AA1 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA2 3 4 N ALA A 108 ? N ALA A 108 O THR A 119 ? O THR A 119 
AA2 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA2 5 6 O THR B 123 ? O THR B 123 N ARG B 104 ? N ARG B 104 
AA2 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N ILE A 73  ? N ILE A 73  O ALA A 91  ? O ALA A 91  
AA3 4 5 N VAL A 94  ? N VAL A 94  O GLU B 89  ? O GLU B 89  
AA3 5 6 O ALA B 91  ? O ALA B 91  N ILE B 73  ? N ILE B 73  
AA3 6 7 O GLU B 72  ? O GLU B 72  N HIS B 31  ? N HIS B 31  
AA3 7 8 N VAL B 32  ? N VAL B 32  O ALA B 45  ? O ALA B 45  
# 
_pdbx_entry_details.entry_id                   9H7C 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A MSR 202 ? D MSR . 
2 1 A MSR 202 ? D MSR . 
3 1 B HOH 301 ? H HOH . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       336 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.09 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A GLY 4   ? A GLY 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A LYS 9   ? A LYS 9   
10 1 Y 1 A LYS 126 ? A LYS 126 
11 1 Y 1 A GLU 127 ? A GLU 127 
12 1 Y 1 B GLY 1   ? B GLY 1   
13 1 Y 1 B PRO 2   ? B PRO 2   
14 1 Y 1 B THR 3   ? B THR 3   
15 1 Y 1 B GLY 4   ? B GLY 4   
16 1 Y 1 B THR 5   ? B THR 5   
17 1 Y 1 B GLY 6   ? B GLY 6   
18 1 Y 1 B GLU 7   ? B GLU 7   
19 1 Y 1 B SER 8   ? B SER 8   
20 1 Y 1 B LYS 9   ? B LYS 9   
21 1 Y 1 B CYS 10  ? B CYS 10  
22 1 Y 1 B ASP 99  ? B ASP 99  
23 1 Y 1 B SER 100 ? B SER 100 
24 1 Y 1 B ASN 124 ? B ASN 124 
25 1 Y 1 B PRO 125 ? B PRO 125 
26 1 Y 1 B LYS 126 ? B LYS 126 
27 1 Y 1 B GLU 127 ? B GLU 127 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLU N    N  N N 89  
GLU CA   C  N S 90  
GLU C    C  N N 91  
GLU O    O  N N 92  
GLU CB   C  N N 93  
GLU CG   C  N N 94  
GLU CD   C  N N 95  
GLU OE1  O  N N 96  
GLU OE2  O  N N 97  
GLU OXT  O  N N 98  
GLU H    H  N N 99  
GLU H2   H  N N 100 
GLU HA   H  N N 101 
GLU HB2  H  N N 102 
GLU HB3  H  N N 103 
GLU HG2  H  N N 104 
GLU HG3  H  N N 105 
GLU HE2  H  N N 106 
GLU HXT  H  N N 107 
GLY N    N  N N 108 
GLY CA   C  N N 109 
GLY C    C  N N 110 
GLY O    O  N N 111 
GLY OXT  O  N N 112 
GLY H    H  N N 113 
GLY H2   H  N N 114 
GLY HA2  H  N N 115 
GLY HA3  H  N N 116 
GLY HXT  H  N N 117 
HIS N    N  N N 118 
HIS CA   C  N S 119 
HIS C    C  N N 120 
HIS O    O  N N 121 
HIS CB   C  N N 122 
HIS CG   C  Y N 123 
HIS ND1  N  Y N 124 
HIS CD2  C  Y N 125 
HIS CE1  C  Y N 126 
HIS NE2  N  Y N 127 
HIS OXT  O  N N 128 
HIS H    H  N N 129 
HIS H2   H  N N 130 
HIS HA   H  N N 131 
HIS HB2  H  N N 132 
HIS HB3  H  N N 133 
HIS HD1  H  N N 134 
HIS HD2  H  N N 135 
HIS HE1  H  N N 136 
HIS HE2  H  N N 137 
HIS HXT  H  N N 138 
HOH O    O  N N 139 
HOH H1   H  N N 140 
HOH H2   H  N N 141 
ILE N    N  N N 142 
ILE CA   C  N S 143 
ILE C    C  N N 144 
ILE O    O  N N 145 
ILE CB   C  N S 146 
ILE CG1  C  N N 147 
ILE CG2  C  N N 148 
ILE CD1  C  N N 149 
ILE OXT  O  N N 150 
ILE H    H  N N 151 
ILE H2   H  N N 152 
ILE HA   H  N N 153 
ILE HB   H  N N 154 
ILE HG12 H  N N 155 
ILE HG13 H  N N 156 
ILE HG21 H  N N 157 
ILE HG22 H  N N 158 
ILE HG23 H  N N 159 
ILE HD11 H  N N 160 
ILE HD12 H  N N 161 
ILE HD13 H  N N 162 
ILE HXT  H  N N 163 
LEU N    N  N N 164 
LEU CA   C  N S 165 
LEU C    C  N N 166 
LEU O    O  N N 167 
LEU CB   C  N N 168 
LEU CG   C  N N 169 
LEU CD1  C  N N 170 
LEU CD2  C  N N 171 
LEU OXT  O  N N 172 
LEU H    H  N N 173 
LEU H2   H  N N 174 
LEU HA   H  N N 175 
LEU HB2  H  N N 176 
LEU HB3  H  N N 177 
LEU HG   H  N N 178 
LEU HD11 H  N N 179 
LEU HD12 H  N N 180 
LEU HD13 H  N N 181 
LEU HD21 H  N N 182 
LEU HD22 H  N N 183 
LEU HD23 H  N N 184 
LEU HXT  H  N N 185 
LYS N    N  N N 186 
LYS CA   C  N S 187 
LYS C    C  N N 188 
LYS O    O  N N 189 
LYS CB   C  N N 190 
LYS CG   C  N N 191 
LYS CD   C  N N 192 
LYS CE   C  N N 193 
LYS NZ   N  N N 194 
LYS OXT  O  N N 195 
LYS H    H  N N 196 
LYS H2   H  N N 197 
LYS HA   H  N N 198 
LYS HB2  H  N N 199 
LYS HB3  H  N N 200 
LYS HG2  H  N N 201 
LYS HG3  H  N N 202 
LYS HD2  H  N N 203 
LYS HD3  H  N N 204 
LYS HE2  H  N N 205 
LYS HE3  H  N N 206 
LYS HZ1  H  N N 207 
LYS HZ2  H  N N 208 
LYS HZ3  H  N N 209 
LYS HXT  H  N N 210 
MET N    N  N N 211 
MET CA   C  N S 212 
MET C    C  N N 213 
MET O    O  N N 214 
MET CB   C  N N 215 
MET CG   C  N N 216 
MET SD   S  N N 217 
MET CE   C  N N 218 
MET OXT  O  N N 219 
MET H    H  N N 220 
MET H2   H  N N 221 
MET HA   H  N N 222 
MET HB2  H  N N 223 
MET HB3  H  N N 224 
MET HG2  H  N N 225 
MET HG3  H  N N 226 
MET HE1  H  N N 227 
MET HE2  H  N N 228 
MET HE3  H  N N 229 
MET HXT  H  N N 230 
MSR C12  C  Y N 231 
MSR C13  C  Y N 232 
MSR C14  C  Y N 233 
MSR O17  O  N N 234 
MSR C15  C  Y N 235 
MSR C16  C  Y N 236 
MSR C11  C  Y N 237 
MSR N3   N  Y N 238 
MSR C4   C  Y N 239 
MSR C5   C  Y N 240 
MSR NFE  N  Y N 241 
MSR C2   C  Y N 242 
MSR H12  H  N N 243 
MSR H13  H  N N 244 
MSR HO17 H  N N 245 
MSR H15  H  N N 246 
MSR H16  H  N N 247 
MSR H4   H  N N 248 
MSR H5   H  N N 249 
MSR H2   H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLU N   CA   sing N N 83  
GLU N   H    sing N N 84  
GLU N   H2   sing N N 85  
GLU CA  C    sing N N 86  
GLU CA  CB   sing N N 87  
GLU CA  HA   sing N N 88  
GLU C   O    doub N N 89  
GLU C   OXT  sing N N 90  
GLU CB  CG   sing N N 91  
GLU CB  HB2  sing N N 92  
GLU CB  HB3  sing N N 93  
GLU CG  CD   sing N N 94  
GLU CG  HG2  sing N N 95  
GLU CG  HG3  sing N N 96  
GLU CD  OE1  doub N N 97  
GLU CD  OE2  sing N N 98  
GLU OE2 HE2  sing N N 99  
GLU OXT HXT  sing N N 100 
GLY N   CA   sing N N 101 
GLY N   H    sing N N 102 
GLY N   H2   sing N N 103 
GLY CA  C    sing N N 104 
GLY CA  HA2  sing N N 105 
GLY CA  HA3  sing N N 106 
GLY C   O    doub N N 107 
GLY C   OXT  sing N N 108 
GLY OXT HXT  sing N N 109 
HIS N   CA   sing N N 110 
HIS N   H    sing N N 111 
HIS N   H2   sing N N 112 
HIS CA  C    sing N N 113 
HIS CA  CB   sing N N 114 
HIS CA  HA   sing N N 115 
HIS C   O    doub N N 116 
HIS C   OXT  sing N N 117 
HIS CB  CG   sing N N 118 
HIS CB  HB2  sing N N 119 
HIS CB  HB3  sing N N 120 
HIS CG  ND1  sing Y N 121 
HIS CG  CD2  doub Y N 122 
HIS ND1 CE1  doub Y N 123 
HIS ND1 HD1  sing N N 124 
HIS CD2 NE2  sing Y N 125 
HIS CD2 HD2  sing N N 126 
HIS CE1 NE2  sing Y N 127 
HIS CE1 HE1  sing N N 128 
HIS NE2 HE2  sing N N 129 
HIS OXT HXT  sing N N 130 
HOH O   H1   sing N N 131 
HOH O   H2   sing N N 132 
ILE N   CA   sing N N 133 
ILE N   H    sing N N 134 
ILE N   H2   sing N N 135 
ILE CA  C    sing N N 136 
ILE CA  CB   sing N N 137 
ILE CA  HA   sing N N 138 
ILE C   O    doub N N 139 
ILE C   OXT  sing N N 140 
ILE CB  CG1  sing N N 141 
ILE CB  CG2  sing N N 142 
ILE CB  HB   sing N N 143 
ILE CG1 CD1  sing N N 144 
ILE CG1 HG12 sing N N 145 
ILE CG1 HG13 sing N N 146 
ILE CG2 HG21 sing N N 147 
ILE CG2 HG22 sing N N 148 
ILE CG2 HG23 sing N N 149 
ILE CD1 HD11 sing N N 150 
ILE CD1 HD12 sing N N 151 
ILE CD1 HD13 sing N N 152 
ILE OXT HXT  sing N N 153 
LEU N   CA   sing N N 154 
LEU N   H    sing N N 155 
LEU N   H2   sing N N 156 
LEU CA  C    sing N N 157 
LEU CA  CB   sing N N 158 
LEU CA  HA   sing N N 159 
LEU C   O    doub N N 160 
LEU C   OXT  sing N N 161 
LEU CB  CG   sing N N 162 
LEU CB  HB2  sing N N 163 
LEU CB  HB3  sing N N 164 
LEU CG  CD1  sing N N 165 
LEU CG  CD2  sing N N 166 
LEU CG  HG   sing N N 167 
LEU CD1 HD11 sing N N 168 
LEU CD1 HD12 sing N N 169 
LEU CD1 HD13 sing N N 170 
LEU CD2 HD21 sing N N 171 
LEU CD2 HD22 sing N N 172 
LEU CD2 HD23 sing N N 173 
LEU OXT HXT  sing N N 174 
LYS N   CA   sing N N 175 
LYS N   H    sing N N 176 
LYS N   H2   sing N N 177 
LYS CA  C    sing N N 178 
LYS CA  CB   sing N N 179 
LYS CA  HA   sing N N 180 
LYS C   O    doub N N 181 
LYS C   OXT  sing N N 182 
LYS CB  CG   sing N N 183 
LYS CB  HB2  sing N N 184 
LYS CB  HB3  sing N N 185 
LYS CG  CD   sing N N 186 
LYS CG  HG2  sing N N 187 
LYS CG  HG3  sing N N 188 
LYS CD  CE   sing N N 189 
LYS CD  HD2  sing N N 190 
LYS CD  HD3  sing N N 191 
LYS CE  NZ   sing N N 192 
LYS CE  HE2  sing N N 193 
LYS CE  HE3  sing N N 194 
LYS NZ  HZ1  sing N N 195 
LYS NZ  HZ2  sing N N 196 
LYS NZ  HZ3  sing N N 197 
LYS OXT HXT  sing N N 198 
MET N   CA   sing N N 199 
MET N   H    sing N N 200 
MET N   H2   sing N N 201 
MET CA  C    sing N N 202 
MET CA  CB   sing N N 203 
MET CA  HA   sing N N 204 
MET C   O    doub N N 205 
MET C   OXT  sing N N 206 
MET CB  CG   sing N N 207 
MET CB  HB2  sing N N 208 
MET CB  HB3  sing N N 209 
MET CG  SD   sing N N 210 
MET CG  HG2  sing N N 211 
MET CG  HG3  sing N N 212 
MET SD  CE   sing N N 213 
MET CE  HE1  sing N N 214 
MET CE  HE2  sing N N 215 
MET CE  HE3  sing N N 216 
MET OXT HXT  sing N N 217 
MSR C12 C13  doub Y N 218 
MSR C12 C11  sing Y N 219 
MSR C12 H12  sing N N 220 
MSR C13 C14  sing Y N 221 
MSR C13 H13  sing N N 222 
MSR C14 O17  sing N N 223 
MSR C14 C15  doub Y N 224 
MSR O17 HO17 sing N N 225 
MSR C15 C16  sing Y N 226 
MSR C15 H15  sing N N 227 
MSR C16 C11  doub Y N 228 
MSR C16 H16  sing N N 229 
MSR C11 N3   sing Y N 230 
MSR N3  C4   sing Y N 231 
MSR N3  C2   sing Y N 232 
MSR C4  C5   doub Y N 233 
MSR C4  H4   sing N N 234 
MSR C5  NFE  sing Y N 235 
MSR C5  H5   sing N N 236 
MSR NFE C2   doub Y N 237 
MSR C2  H2   sing N N 238 
PHE N   CA   sing N N 239 
PHE N   H    sing N N 240 
PHE N   H2   sing N N 241 
PHE CA  C    sing N N 242 
PHE CA  CB   sing N N 243 
PHE CA  HA   sing N N 244 
PHE C   O    doub N N 245 
PHE C   OXT  sing N N 246 
PHE CB  CG   sing N N 247 
PHE CB  HB2  sing N N 248 
PHE CB  HB3  sing N N 249 
PHE CG  CD1  doub Y N 250 
PHE CG  CD2  sing Y N 251 
PHE CD1 CE1  sing Y N 252 
PHE CD1 HD1  sing N N 253 
PHE CD2 CE2  doub Y N 254 
PHE CD2 HD2  sing N N 255 
PHE CE1 CZ   doub Y N 256 
PHE CE1 HE1  sing N N 257 
PHE CE2 CZ   sing Y N 258 
PHE CE2 HE2  sing N N 259 
PHE CZ  HZ   sing N N 260 
PHE OXT HXT  sing N N 261 
PRO N   CA   sing N N 262 
PRO N   CD   sing N N 263 
PRO N   H    sing N N 264 
PRO CA  C    sing N N 265 
PRO CA  CB   sing N N 266 
PRO CA  HA   sing N N 267 
PRO C   O    doub N N 268 
PRO C   OXT  sing N N 269 
PRO CB  CG   sing N N 270 
PRO CB  HB2  sing N N 271 
PRO CB  HB3  sing N N 272 
PRO CG  CD   sing N N 273 
PRO CG  HG2  sing N N 274 
PRO CG  HG3  sing N N 275 
PRO CD  HD2  sing N N 276 
PRO CD  HD3  sing N N 277 
PRO OXT HXT  sing N N 278 
SER N   CA   sing N N 279 
SER N   H    sing N N 280 
SER N   H2   sing N N 281 
SER CA  C    sing N N 282 
SER CA  CB   sing N N 283 
SER CA  HA   sing N N 284 
SER C   O    doub N N 285 
SER C   OXT  sing N N 286 
SER CB  OG   sing N N 287 
SER CB  HB2  sing N N 288 
SER CB  HB3  sing N N 289 
SER OG  HG   sing N N 290 
SER OXT HXT  sing N N 291 
THR N   CA   sing N N 292 
THR N   H    sing N N 293 
THR N   H2   sing N N 294 
THR CA  C    sing N N 295 
THR CA  CB   sing N N 296 
THR CA  HA   sing N N 297 
THR C   O    doub N N 298 
THR C   OXT  sing N N 299 
THR CB  OG1  sing N N 300 
THR CB  CG2  sing N N 301 
THR CB  HB   sing N N 302 
THR OG1 HG1  sing N N 303 
THR CG2 HG21 sing N N 304 
THR CG2 HG22 sing N N 305 
THR CG2 HG23 sing N N 306 
THR OXT HXT  sing N N 307 
TRP N   CA   sing N N 308 
TRP N   H    sing N N 309 
TRP N   H2   sing N N 310 
TRP CA  C    sing N N 311 
TRP CA  CB   sing N N 312 
TRP CA  HA   sing N N 313 
TRP C   O    doub N N 314 
TRP C   OXT  sing N N 315 
TRP CB  CG   sing N N 316 
TRP CB  HB2  sing N N 317 
TRP CB  HB3  sing N N 318 
TRP CG  CD1  doub Y N 319 
TRP CG  CD2  sing Y N 320 
TRP CD1 NE1  sing Y N 321 
TRP CD1 HD1  sing N N 322 
TRP CD2 CE2  doub Y N 323 
TRP CD2 CE3  sing Y N 324 
TRP NE1 CE2  sing Y N 325 
TRP NE1 HE1  sing N N 326 
TRP CE2 CZ2  sing Y N 327 
TRP CE3 CZ3  doub Y N 328 
TRP CE3 HE3  sing N N 329 
TRP CZ2 CH2  doub Y N 330 
TRP CZ2 HZ2  sing N N 331 
TRP CZ3 CH2  sing Y N 332 
TRP CZ3 HZ3  sing N N 333 
TRP CH2 HH2  sing N N 334 
TRP OXT HXT  sing N N 335 
TYR N   CA   sing N N 336 
TYR N   H    sing N N 337 
TYR N   H2   sing N N 338 
TYR CA  C    sing N N 339 
TYR CA  CB   sing N N 340 
TYR CA  HA   sing N N 341 
TYR C   O    doub N N 342 
TYR C   OXT  sing N N 343 
TYR CB  CG   sing N N 344 
TYR CB  HB2  sing N N 345 
TYR CB  HB3  sing N N 346 
TYR CG  CD1  doub Y N 347 
TYR CG  CD2  sing Y N 348 
TYR CD1 CE1  sing Y N 349 
TYR CD1 HD1  sing N N 350 
TYR CD2 CE2  doub Y N 351 
TYR CD2 HD2  sing N N 352 
TYR CE1 CZ   doub Y N 353 
TYR CE1 HE1  sing N N 354 
TYR CE2 CZ   sing Y N 355 
TYR CE2 HE2  sing N N 356 
TYR CZ  OH   sing N N 357 
TYR OH  HH   sing N N 358 
TYR OXT HXT  sing N N 359 
VAL N   CA   sing N N 360 
VAL N   H    sing N N 361 
VAL N   H2   sing N N 362 
VAL CA  C    sing N N 363 
VAL CA  CB   sing N N 364 
VAL CA  HA   sing N N 365 
VAL C   O    doub N N 366 
VAL C   OXT  sing N N 367 
VAL CB  CG1  sing N N 368 
VAL CB  CG2  sing N N 369 
VAL CB  HB   sing N N 370 
VAL CG1 HG11 sing N N 371 
VAL CG1 HG12 sing N N 372 
VAL CG1 HG13 sing N N 373 
VAL CG2 HG21 sing N N 374 
VAL CG2 HG22 sing N N 375 
VAL CG2 HG23 sing N N 376 
VAL OXT HXT  sing N N 377 
# 
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                    9H7C 
_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]   0.023790 
_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]   0.011759 
_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]   0.015714 
_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  ? 6.313   11.802 56.087  1.00 48.48 ? 10  CYS A N   1 
ATOM   2    C  CA  . CYS A 1 10  ? 5.686   11.425 57.384  1.00 48.68 ? 10  CYS A CA  1 
ATOM   3    C  C   . CYS A 1 10  ? 6.723   11.339 58.500  1.00 29.95 ? 10  CYS A C   1 
ATOM   4    O  O   . CYS A 1 10  ? 7.071   10.298 58.929  1.00 36.51 ? 10  CYS A O   1 
ATOM   5    N  N   . PRO A 1 11  ? 7.301   12.469 58.919  1.00 18.34 ? 11  PRO A N   1 
ATOM   6    C  CA  . PRO A 1 11  ? 8.146   12.322 60.077  1.00 15.58 ? 11  PRO A CA  1 
ATOM   7    C  C   . PRO A 1 11  ? 7.493   12.227 61.462  1.00 13.32 ? 11  PRO A C   1 
ATOM   8    O  O   . PRO A 1 11  ? 8.152   11.872 62.406  1.00 14.91 ? 11  PRO A O   1 
ATOM   9    C  CB  . PRO A 1 11  ? 9.073   13.467 60.005  1.00 20.84 ? 11  PRO A CB  1 
ATOM   10   C  CG  . PRO A 1 11  ? 8.343   14.459 59.338  1.00 24.37 ? 11  PRO A CG  1 
ATOM   11   C  CD  . PRO A 1 11  ? 7.426   13.809 58.363  1.00 24.21 ? 11  PRO A CD  1 
ATOM   12   N  N   . LEU A 1 12  ? 6.217   12.521 61.554  1.00 13.19 ? 12  LEU A N   1 
ATOM   13   C  CA  . LEU A 1 12  ? 5.501   12.463 62.837  1.00 12.96 ? 12  LEU A CA  1 
ATOM   14   C  C   . LEU A 1 12  ? 4.120   11.863 62.498  1.00 14.10 ? 12  LEU A C   1 
ATOM   15   O  O   . LEU A 1 12  ? 3.404   12.457 61.750  1.00 20.78 ? 12  LEU A O   1 
ATOM   16   C  CB  . LEU A 1 12  ? 5.378   13.844 63.465  1.00 15.41 ? 12  LEU A CB  1 
ATOM   17   C  CG  . LEU A 1 12  ? 4.612   13.934 64.780  1.00 17.09 ? 12  LEU A CG  1 
ATOM   18   C  CD1 . LEU A 1 12  ? 5.266   13.074 65.835  1.00 17.14 ? 12  LEU A CD1 1 
ATOM   19   C  CD2 . LEU A 1 12  ? 4.525   15.403 65.183  1.00 19.80 ? 12  LEU A CD2 1 
ATOM   20   N  N   . MET A 1 13  ? 3.786   10.750 63.116  1.00 11.87 ? 13  MET A N   1 
ATOM   21   C  CA  . MET A 1 13  ? 2.501   10.101 62.976  1.00 12.37 ? 13  MET A CA  1 
ATOM   22   C  C   . MET A 1 13  ? 1.951   9.824  64.346  1.00 10.94 ? 13  MET A C   1 
ATOM   23   O  O   . MET A 1 13  ? 2.723   9.554  65.263  1.00 12.55 ? 13  MET A O   1 
ATOM   24   C  CB  . MET A 1 13  ? 2.595   8.837  62.111  1.00 16.34 ? 13  MET A CB  1 
ATOM   25   C  CG  . MET A 1 13  ? 1.240   8.160  61.731  1.00 22.50 ? 13  MET A CG  1 
ATOM   26   S  SD  . MET A 1 13  ? 0.537   7.013  62.904  0.50 17.02 ? 13  MET A SD  1 
ATOM   27   N  N   . VAL A 1 14  ? 0.665   9.881  64.494  1.00 10.19 ? 14  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 14  ? 0.002   9.650  65.767  1.00 10.68 ? 14  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 14  ? -1.074  8.566  65.550  1.00 11.79 ? 14  VAL A C   1 
ATOM   30   O  O   . VAL A 1 14  ? -1.808  8.643  64.574  1.00 14.27 ? 14  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 14  ? -0.585  10.889 66.400  1.00 12.37 ? 14  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 14  ? -1.301  10.573 67.714  1.00 13.40 ? 14  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 14  ? 0.490   11.925 66.639  1.00 11.76 ? 14  VAL A CG2 1 
ATOM   34   N  N   . LYS A 1 15  ? -1.116  7.535  66.372  1.00 11.12 ? 15  LYS A N   1 
ATOM   35   C  CA  . LYS A 1 15  ? -2.120  6.457  66.300  1.00 11.74 ? 15  LYS A CA  1 
ATOM   36   C  C   . LYS A 1 15  ? -2.781  6.319  67.654  1.00 10.96 ? 15  LYS A C   1 
ATOM   37   O  O   . LYS A 1 15  ? -2.076  6.287  68.672  1.00 13.23 ? 15  LYS A O   1 
ATOM   38   C  CB  . LYS A 1 15  ? -1.452  5.169  65.913  0.50 10.42 ? 15  LYS A CB  1 
ATOM   39   C  CG  . LYS A 1 15  ? -2.466  4.059  65.892  0.50 17.44 ? 15  LYS A CG  1 
ATOM   40   C  CD  . LYS A 1 15  ? -2.095  2.970  64.893  0.50 19.59 ? 15  LYS A CD  1 
ATOM   41   C  CE  . LYS A 1 15  ? -3.203  1.932  64.794  0.50 20.62 ? 15  LYS A CE  1 
ATOM   42   N  NZ  . LYS A 1 15  ? -2.969  1.061  63.625  0.50 28.96 ? 15  LYS A NZ  1 
ATOM   43   N  N   . VAL A 1 16  ? -4.102  6.263  67.683  1.00 10.88 ? 16  VAL A N   1 
ATOM   44   C  CA  . VAL A 1 16  ? -4.887  6.186  68.901  1.00 10.51 ? 16  VAL A CA  1 
ATOM   45   C  C   . VAL A 1 16  ? -5.839  5.043  68.859  1.00 11.16 ? 16  VAL A C   1 
ATOM   46   O  O   . VAL A 1 16  ? -6.582  4.879  67.927  1.00 11.89 ? 16  VAL A O   1 
ATOM   47   C  CB  . VAL A 1 16  ? -5.616  7.539  69.172  1.00 11.49 ? 16  VAL A CB  1 
ATOM   48   C  CG1 . VAL A 1 16  ? -6.179  7.587  70.600  1.00 12.58 ? 16  VAL A CG1 1 
ATOM   49   C  CG2 . VAL A 1 16  ? -4.680  8.722  68.949  1.00 11.19 ? 16  VAL A CG2 1 
ATOM   50   N  N   . LEU A 1 17  ? -5.818  4.265  69.947  1.00 11.53 ? 17  LEU A N   1 
ATOM   51   C  CA  . LEU A 1 17  ? -6.674  3.090  70.147  1.00 11.03 ? 17  LEU A CA  1 
ATOM   52   C  C   . LEU A 1 17  ? -7.546  3.246  71.374  1.00 10.37 ? 17  LEU A C   1 
ATOM   53   O  O   . LEU A 1 17  ? -7.126  3.859  72.350  1.00 11.14 ? 17  LEU A O   1 
ATOM   54   C  CB  . LEU A 1 17  ? -5.857  1.822  70.237  1.00 11.72 ? 17  LEU A CB  1 
ATOM   55   C  CG  . LEU A 1 17  ? -4.978  1.462  69.006  1.00 14.13 ? 17  LEU A CG  1 
ATOM   56   C  CD1 . LEU A 1 17  ? -4.243  0.133  69.307  1.00 16.43 ? 17  LEU A CD1 1 
ATOM   57   C  CD2 . LEU A 1 17  ? -5.872  1.259  67.772  1.00 17.63 ? 17  LEU A CD2 1 
ATOM   58   N  N   . ASP A 1 18  ? -8.720  2.639  71.339  1.00 11.15 ? 18  ASP A N   1 
ATOM   59   C  CA  . ASP A 1 18  ? -9.702  2.653  72.416  1.00 10.02 ? 18  ASP A CA  1 
ATOM   60   C  C   . ASP A 1 18  ? -9.730  1.274  73.095  1.00 9.91  ? 18  ASP A C   1 
ATOM   61   O  O   . ASP A 1 18  ? -10.057 0.270  72.437  1.00 11.06 ? 18  ASP A O   1 
ATOM   62   C  CB  . ASP A 1 18  ? -11.056 3.044  71.822  1.00 11.61 ? 18  ASP A CB  1 
ATOM   63   C  CG  . ASP A 1 18  ? -12.206 3.034  72.782  1.00 12.94 ? 18  ASP A CG  1 
ATOM   64   O  OD1 . ASP A 1 18  ? -12.231 2.253  73.707  1.00 12.37 ? 18  ASP A OD1 1 
ATOM   65   O  OD2 . ASP A 1 18  ? -13.147 3.833  72.551  1.00 14.84 ? 18  ASP A OD2 1 
ATOM   66   N  N   . ALA A 1 19  ? -9.314  1.221  74.342  1.00 9.20  ? 19  ALA A N   1 
ATOM   67   C  CA  . ALA A 1 19  ? -9.211  -0.006 75.133  1.00 10.34 ? 19  ALA A CA  1 
ATOM   68   C  C   . ALA A 1 19  ? -10.519 -0.482 75.718  1.00 10.56 ? 19  ALA A C   1 
ATOM   69   O  O   . ALA A 1 19  ? -10.555 -1.593 76.274  1.00 12.68 ? 19  ALA A O   1 
ATOM   70   C  CB  . ALA A 1 19  ? -8.178  0.157  76.213  1.00 12.04 ? 19  ALA A CB  1 
ATOM   71   N  N   . VAL A 1 20  ? -11.578 0.289  75.607  1.00 11.44 ? 20  VAL A N   1 
ATOM   72   C  CA  . VAL A 1 20  ? -12.897 -0.149 76.057  1.00 12.87 ? 20  VAL A CA  1 
ATOM   73   C  C   . VAL A 1 20  ? -13.655 -0.885 74.963  1.00 12.34 ? 20  VAL A C   1 
ATOM   74   O  O   . VAL A 1 20  ? -14.203 -1.933 75.197  1.00 15.54 ? 20  VAL A O   1 
ATOM   75   C  CB  . VAL A 1 20  ? -13.736 1.065  76.511  1.00 13.04 ? 20  VAL A CB  1 
ATOM   76   C  CG1 . VAL A 1 20  ? -15.193 0.650  76.768  1.00 16.26 ? 20  VAL A CG1 1 
ATOM   77   C  CG2 . VAL A 1 20  ? -13.179 1.696  77.705  1.00 15.50 ? 20  VAL A CG2 1 
ATOM   78   N  N   . ARG A 1 21  ? -13.602 -0.354 73.766  1.00 11.81 ? 21  ARG A N   1 
ATOM   79   C  CA  . ARG A 1 21  ? -14.307 -0.886 72.615  1.00 13.99 ? 21  ARG A CA  1 
ATOM   80   C  C   . ARG A 1 21  ? -13.466 -1.785 71.779  1.00 11.52 ? 21  ARG A C   1 
ATOM   81   O  O   . ARG A 1 21  ? -13.954 -2.530 70.973  1.00 15.85 ? 21  ARG A O   1 
ATOM   82   C  CB  . ARG A 1 21  ? -14.819 0.292  71.671  1.00 18.38 ? 21  ARG A CB  1 
ATOM   83   C  CG  . ARG A 1 21  ? -15.850 1.215  72.303  1.00 28.98 ? 21  ARG A CG  1 
ATOM   84   C  CD  . ARG A 1 21  ? -16.031 2.604  71.590  1.00 35.32 ? 21  ARG A CD  1 
ATOM   85   N  NE  . ARG A 1 21  ? -17.312 2.782  70.918  1.00 46.12 ? 21  ARG A NE  1 
ATOM   86   N  N   . GLY A 1 22  ? -12.161 -1.783 71.922  1.00 10.85 ? 22  GLY A N   1 
ATOM   87   C  CA  . GLY A 1 22  ? -11.296 -2.584 71.054  1.00 12.03 ? 22  GLY A CA  1 
ATOM   88   C  C   . GLY A 1 22  ? -11.280 -2.119 69.643  1.00 9.92  ? 22  GLY A C   1 
ATOM   89   O  O   . GLY A 1 22  ? -11.497 -2.872 68.712  1.00 11.65 ? 22  GLY A O   1 
ATOM   90   N  N   . SER A 1 23  ? -11.045 -0.809 69.473  1.00 11.51 ? 23  SER A N   1 
ATOM   91   C  CA  . SER A 1 23  ? -11.213 -0.190 68.166  1.00 12.27 ? 23  SER A CA  1 
ATOM   92   C  C   . SER A 1 23  ? -10.231 0.956  68.086  1.00 11.85 ? 23  SER A C   1 
ATOM   93   O  O   . SER A 1 23  ? -9.719  1.443  69.042  1.00 12.60 ? 23  SER A O   1 
ATOM   94   C  CB  . SER A 1 23  ? -12.589 0.404  67.987  1.00 14.25 ? 23  SER A CB  1 
ATOM   95   O  OG  . SER A 1 23  ? -12.795 1.457  68.882  1.00 20.63 ? 23  SER A OG  1 
ATOM   96   N  N   . PRO A 1 24  ? -9.993  1.360  66.819  1.00 12.16 ? 24  PRO A N   1 
ATOM   97   C  CA  . PRO A 1 24  ? -9.365  2.664  66.626  1.00 11.74 ? 24  PRO A CA  1 
ATOM   98   C  C   . PRO A 1 24  ? -10.161 3.742  67.297  1.00 12.06 ? 24  PRO A C   1 
ATOM   99   O  O   . PRO A 1 24  ? -11.378 3.657  67.343  1.00 13.48 ? 24  PRO A O   1 
ATOM   100  C  CB  . PRO A 1 24  ? -9.378  2.863  65.118  1.00 14.63 ? 24  PRO A CB  1 
ATOM   101  C  CG  . PRO A 1 24  ? -10.429 1.996  64.607  1.00 21.59 ? 24  PRO A CG  1 
ATOM   102  C  CD  . PRO A 1 24  ? -10.440 0.831  65.521  1.00 13.19 ? 24  PRO A CD  1 
ATOM   103  N  N   . ALA A 1 25  ? -9.509  4.780  67.788  1.00 11.77 ? 25  ALA A N   1 
ATOM   104  C  CA  . ALA A 1 25  ? -10.144 5.963  68.343  1.00 11.30 ? 25  ALA A CA  1 
ATOM   105  C  C   . ALA A 1 25  ? -10.220 7.002  67.214  1.00 12.43 ? 25  ALA A C   1 
ATOM   106  O  O   . ALA A 1 25  ? -9.214  7.539  66.815  1.00 12.86 ? 25  ALA A O   1 
ATOM   107  C  CB  . ALA A 1 25  ? -9.376  6.490  69.530  1.00 11.60 ? 25  ALA A CB  1 
ATOM   108  N  N   . ILE A 1 26  ? -11.434 7.175  66.681  1.00 12.84 ? 26  ILE A N   1 
ATOM   109  C  CA  . ILE A 1 26  ? -11.676 7.921  65.455  1.00 13.08 ? 26  ILE A CA  1 
ATOM   110  C  C   . ILE A 1 26  ? -12.043 9.356  65.786  1.00 13.71 ? 26  ILE A C   1 
ATOM   111  O  O   . ILE A 1 26  ? -12.612 9.627  66.834  1.00 14.58 ? 26  ILE A O   1 
ATOM   112  C  CB  . ILE A 1 26  ? -12.791 7.268  64.583  1.00 16.11 ? 26  ILE A CB  1 
ATOM   113  C  CG1 . ILE A 1 26  ? -12.387 5.813  64.299  1.00 18.15 ? 26  ILE A CG1 1 
ATOM   114  C  CG2 . ILE A 1 26  ? -13.118 8.017  63.338  1.00 24.65 ? 26  ILE A CG2 1 
ATOM   115  C  CD1 . ILE A 1 26  ? -13.506 4.857  63.823  1.00 30.43 ? 26  ILE A CD1 1 
ATOM   116  N  N   . ASN A 1 27  ? -11.660 10.311 64.943  1.00 12.92 ? 27  ASN A N   1 
ATOM   117  C  CA  . ASN A 1 27  ? -12.037 11.720 65.150  1.00 13.33 ? 27  ASN A CA  1 
ATOM   118  C  C   . ASN A 1 27  ? -11.505 12.331 66.411  1.00 13.53 ? 27  ASN A C   1 
ATOM   119  O  O   . ASN A 1 27  ? -12.078 13.224 66.951  1.00 15.24 ? 27  ASN A O   1 
ATOM   120  C  CB  . ASN A 1 27  ? -13.566 11.919 65.133  1.00 17.12 ? 27  ASN A CB  1 
ATOM   121  C  CG  . ASN A 1 27  ? -14.171 11.513 63.821  1.00 23.18 ? 27  ASN A CG  1 
ATOM   122  O  OD1 . ASN A 1 27  ? -13.543 11.723 62.803  1.00 24.83 ? 27  ASN A OD1 1 
ATOM   123  N  ND2 . ASN A 1 27  ? -15.347 10.803 63.836  1.00 30.15 ? 27  ASN A ND2 1 
ATOM   124  N  N   . VAL A 1 28  ? -10.303 11.911 66.784  1.00 11.98 ? 28  VAL A N   1 
ATOM   125  C  CA  . VAL A 1 28  ? -9.657  12.451 67.983  1.00 11.32 ? 28  VAL A CA  1 
ATOM   126  C  C   . VAL A 1 28  ? -8.767  13.623 67.580  1.00 10.13 ? 28  VAL A C   1 
ATOM   127  O  O   . VAL A 1 28  ? -7.917  13.484 66.701  1.00 11.20 ? 28  VAL A O   1 
ATOM   128  C  CB  . VAL A 1 28  ? -8.772  11.378 68.703  1.00 11.59 ? 28  VAL A CB  1 
ATOM   129  C  CG1 . VAL A 1 28  ? -7.998  11.979 69.887  1.00 14.20 ? 28  VAL A CG1 1 
ATOM   130  C  CG2 . VAL A 1 28  ? -9.606  10.182 69.119  1.00 14.64 ? 28  VAL A CG2 1 
ATOM   131  N  N   . ALA A 1 29  ? -8.955  14.757 68.189  1.00 10.18 ? 29  ALA A N   1 
ATOM   132  C  CA  . ALA A 1 29  ? -8.133  15.959 67.867  1.00 10.30 ? 29  ALA A CA  1 
ATOM   133  C  C   . ALA A 1 29  ? -6.791  15.799 68.520  1.00 9.89  ? 29  ALA A C   1 
ATOM   134  O  O   . ALA A 1 29  ? -6.681  15.344 69.645  1.00 10.39 ? 29  ALA A O   1 
ATOM   135  C  CB  . ALA A 1 29  ? -8.816  17.218 68.372  1.00 11.81 ? 29  ALA A CB  1 
ATOM   136  N  N   . VAL A 1 30  ? -5.764  16.207 67.803  1.00 10.78 ? 30  VAL A N   1 
ATOM   137  C  CA  . VAL A 1 30  ? -4.369  16.166 68.245  1.00 10.86 ? 30  VAL A CA  1 
ATOM   138  C  C   . VAL A 1 30  ? -3.747  17.503 67.946  1.00 10.10 ? 30  VAL A C   1 
ATOM   139  O  O   . VAL A 1 30  ? -3.784  17.955 66.807  1.00 11.17 ? 30  VAL A O   1 
ATOM   140  C  CB  . VAL A 1 30  ? -3.602  15.047 67.527  1.00 10.54 ? 30  VAL A CB  1 
ATOM   141  C  CG1 . VAL A 1 30  ? -2.161  15.041 67.982  1.00 13.03 ? 30  VAL A CG1 1 
ATOM   142  C  CG2 . VAL A 1 30  ? -4.257  13.685 67.784  1.00 11.40 ? 30  VAL A CG2 1 
ATOM   143  N  N   . HIS A 1 31  ? -3.141  18.110 68.976  1.00 10.65 ? 31  HIS A N   1 
ATOM   144  C  CA  . HIS A 1 31  ? -2.455  19.400 68.846  1.00 11.09 ? 31  HIS A CA  1 
ATOM   145  C  C   . HIS A 1 31  ? -1.017  19.227 69.212  1.00 10.53 ? 31  HIS A C   1 
ATOM   146  O  O   . HIS A 1 31  ? -0.687  18.619 70.247  1.00 12.94 ? 31  HIS A O   1 
ATOM   147  C  CB  . HIS A 1 31  ? -3.053  20.401 69.784  1.00 12.66 ? 31  HIS A CB  1 
ATOM   148  C  CG  . HIS A 1 31  ? -4.427  20.802 69.415  1.00 13.76 ? 31  HIS A CG  1 
ATOM   149  N  ND1 . HIS A 1 31  ? -5.604  20.108 69.642  1.00 17.22 ? 31  HIS A ND1 1 
ATOM   150  C  CD2 . HIS A 1 31  ? -4.787  21.924 68.774  1.00 12.34 ? 31  HIS A CD2 1 
ATOM   151  C  CE1 . HIS A 1 31  ? -6.624  20.830 69.197  1.00 13.11 ? 31  HIS A CE1 1 
ATOM   152  N  NE2 . HIS A 1 31  ? -6.142  21.896 68.640  1.00 18.77 ? 31  HIS A NE2 1 
ATOM   153  N  N   . VAL A 1 32  ? -0.122  19.700 68.353  1.00 10.07 ? 32  VAL A N   1 
ATOM   154  C  CA  . VAL A 1 32  ? 1.314   19.624 68.572  1.00 10.76 ? 32  VAL A CA  1 
ATOM   155  C  C   . VAL A 1 32  ? 1.855   21.035 68.766  1.00 11.04 ? 32  VAL A C   1 
ATOM   156  O  O   . VAL A 1 32  ? 1.503   21.939 67.982  1.00 11.28 ? 32  VAL A O   1 
ATOM   157  C  CB  . VAL A 1 32  ? 2.042   18.959 67.365  1.00 11.34 ? 32  VAL A CB  1 
ATOM   158  C  CG1 . VAL A 1 32  ? 3.534   18.740 67.672  1.00 11.99 ? 32  VAL A CG1 1 
ATOM   159  C  CG2 . VAL A 1 32  ? 1.359   17.643 67.003  1.00 12.18 ? 32  VAL A CG2 1 
ATOM   160  N  N   . PHE A 1 33  ? 2.684   21.181 69.795  1.00 11.22 ? 33  PHE A N   1 
ATOM   161  C  CA  . PHE A 1 33  ? 3.338   22.434 70.119  1.00 11.98 ? 33  PHE A CA  1 
ATOM   162  C  C   . PHE A 1 33  ? 4.855   22.225 70.095  1.00 11.27 ? 33  PHE A C   1 
ATOM   163  O  O   . PHE A 1 33  ? 5.311   21.106 70.276  1.00 11.05 ? 33  PHE A O   1 
ATOM   164  C  CB  . PHE A 1 33  ? 2.885   22.957 71.465  1.00 13.29 ? 33  PHE A CB  1 
ATOM   165  C  CG  . PHE A 1 33  ? 1.409   23.088 71.599  1.00 14.82 ? 33  PHE A CG  1 
ATOM   166  C  CD1 . PHE A 1 33  ? 0.634   21.996 71.966  1.00 16.46 ? 33  PHE A CD1 1 
ATOM   167  C  CD2 . PHE A 1 33  ? 0.780   24.278 71.290  1.00 15.89 ? 33  PHE A CD2 1 
ATOM   168  C  CE1 . PHE A 1 33  ? -0.764  22.128 72.024  1.00 16.05 ? 33  PHE A CE1 1 
ATOM   169  C  CE2 . PHE A 1 33  ? -0.574  24.407 71.350  1.00 17.71 ? 33  PHE A CE2 1 
ATOM   170  C  CZ  . PHE A 1 33  ? -1.326  23.335 71.718  1.00 16.85 ? 33  PHE A CZ  1 
ATOM   171  N  N   . ARG A 1 34  ? 5.587   23.299 69.941  1.00 12.71 ? 34  ARG A N   1 
ATOM   172  C  CA  . ARG A 1 34  ? 7.040   23.285 70.010  1.00 12.66 ? 34  ARG A CA  1 
ATOM   173  C  C   . ARG A 1 34  ? 7.511   24.400 70.887  1.00 12.08 ? 34  ARG A C   1 
ATOM   174  O  O   . ARG A 1 34  ? 7.064   25.548 70.756  1.00 13.56 ? 34  ARG A O   1 
ATOM   175  C  CB  . ARG A 1 34  ? 7.624   23.456 68.599  1.00 12.16 ? 34  ARG A CB  1 
ATOM   176  C  CG  . ARG A 1 34  ? 9.158   23.349 68.528  1.00 13.09 ? 34  ARG A CG  1 
ATOM   177  C  CD  . ARG A 1 34  ? 9.644   23.677 67.149  1.00 13.45 ? 34  ARG A CD  1 
ATOM   178  N  NE  . ARG A 1 34  ? 11.102  23.700 67.105  1.00 14.75 ? 34  ARG A NE  1 
ATOM   179  C  CZ  . ARG A 1 34  ? 11.843  24.735 67.414  1.00 13.47 ? 34  ARG A CZ  1 
ATOM   180  N  NH1 . ARG A 1 34  ? 11.276  25.860 67.769  1.00 14.89 ? 34  ARG A NH1 1 
ATOM   181  N  NH2 . ARG A 1 34  ? 13.167  24.616 67.337  1.00 15.28 ? 34  ARG A NH2 1 
ATOM   182  N  N   . LYS A 1 35  ? 8.479   24.112 71.731  1.00 11.63 ? 35  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 35  ? 8.994   25.127 72.707  1.00 13.38 ? 35  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 35  ? 9.728   26.198 71.944  1.00 12.58 ? 35  LYS A C   1 
ATOM   185  O  O   . LYS A 1 35  ? 10.621  25.911 71.162  1.00 14.55 ? 35  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 35  ? 9.898   24.500 73.742  1.00 15.70 ? 35  LYS A CB  1 
ATOM   187  N  N   . ALA A 1 36  ? 9.393   27.448 72.175  1.00 15.02 ? 36  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 36  ? 10.032  28.592 71.570  1.00 16.97 ? 36  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 36  ? 11.275  29.021 72.335  1.00 15.94 ? 36  ALA A C   1 
ATOM   190  O  O   . ALA A 1 36  ? 11.493  28.547 73.428  1.00 19.78 ? 36  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 36  ? 9.037   29.734 71.489  1.00 19.07 ? 36  ALA A CB  1 
ATOM   192  N  N   . ALA A 1 37  ? 12.024  29.972 71.760  1.00 23.19 ? 37  ALA A N   1 
ATOM   193  C  CA  . ALA A 1 37  ? 13.239  30.417 72.387  1.00 25.07 ? 37  ALA A CA  1 
ATOM   194  C  C   . ALA A 1 37  ? 12.993  31.083 73.737  1.00 24.03 ? 37  ALA A C   1 
ATOM   195  O  O   . ALA A 1 37  ? 13.885  31.103 74.615  1.00 36.60 ? 37  ALA A O   1 
ATOM   196  C  CB  . ALA A 1 37  ? 13.983  31.390 71.465  1.00 29.54 ? 37  ALA A CB  1 
ATOM   197  N  N   . ASP A 1 38  ? 11.798  31.613 73.923  1.00 25.77 ? 38  ASP A N   1 
ATOM   198  C  CA  . ASP A 1 38  ? 11.491  32.261 75.168  1.00 30.75 ? 38  ASP A CA  1 
ATOM   199  C  C   . ASP A 1 38  ? 10.873  31.274 76.120  1.00 26.43 ? 38  ASP A C   1 
ATOM   200  O  O   . ASP A 1 38  ? 10.355  31.687 77.136  1.00 33.90 ? 38  ASP A O   1 
ATOM   201  C  CB  . ASP A 1 38  ? 10.546  33.441 74.959  1.00 28.79 ? 38  ASP A CB  1 
ATOM   202  C  CG  . ASP A 1 38  ? 9.169   33.029 74.615  1.00 35.63 ? 38  ASP A CG  1 
ATOM   203  O  OD1 . ASP A 1 38  ? 8.961   31.854 74.257  1.00 30.18 ? 38  ASP A OD1 1 
ATOM   204  O  OD2 . ASP A 1 38  ? 8.300   33.916 74.633  1.00 41.55 ? 38  ASP A OD2 1 
ATOM   205  N  N   . ASP A 1 39  ? 10.929  29.984 75.801  1.00 27.09 ? 39  ASP A N   1 
ATOM   206  C  CA  . ASP A 1 39  ? 10.510  28.896 76.731  1.00 26.87 ? 39  ASP A CA  1 
ATOM   207  C  C   . ASP A 1 39  ? 9.025   28.715 76.845  1.00 30.32 ? 39  ASP A C   1 
ATOM   208  O  O   . ASP A 1 39  ? 8.566   27.985 77.747  1.00 36.80 ? 39  ASP A O   1 
ATOM   209  C  CB  . ASP A 1 39  ? 11.114  29.048 78.143  1.00 39.20 ? 39  ASP A CB  1 
ATOM   210  N  N   . THR A 1 40  ? 8.247   29.319 75.948  1.00 25.91 ? 40  THR A N   1 
ATOM   211  C  CA  . THR A 1 40  ? 6.797   29.012 75.894  1.00 27.30 ? 40  THR A CA  1 
ATOM   212  C  C   . THR A 1 40  ? 6.459   28.055 74.733  1.00 20.50 ? 40  THR A C   1 
ATOM   213  O  O   . THR A 1 40  ? 7.262   27.852 73.848  1.00 20.35 ? 40  THR A O   1 
ATOM   214  C  CB  . THR A 1 40  ? 6.005   30.280 75.756  1.00 28.74 ? 40  THR A CB  1 
ATOM   215  O  OG1 . THR A 1 40  ? 6.186   30.837 74.455  1.00 29.53 ? 40  THR A OG1 1 
ATOM   216  C  CG2 . THR A 1 40  ? 6.427   31.278 76.866  1.00 30.62 ? 40  THR A CG2 1 
ATOM   217  N  N   . TRP A 1 41  ? 5.263   27.528 74.758  1.00 28.21 ? 41  TRP A N   1 
ATOM   218  C  CA  . TRP A 1 41  ? 4.847   26.549 73.787  1.00 21.48 ? 41  TRP A CA  1 
ATOM   219  C  C   . TRP A 1 41  ? 4.214   27.315 72.699  1.00 26.15 ? 41  TRP A C   1 
ATOM   220  O  O   . TRP A 1 41  ? 3.367   28.126 72.946  1.00 36.30 ? 41  TRP A O   1 
ATOM   221  C  CB  . TRP A 1 41  ? 3.757   25.695 74.441  1.00 20.53 ? 41  TRP A CB  1 
ATOM   222  C  CG  . TRP A 1 41  ? 4.334   24.646 75.396  1.00 20.27 ? 41  TRP A CG  1 
ATOM   223  C  CD1 . TRP A 1 41  ? 4.054   24.563 76.766  1.00 25.58 ? 41  TRP A CD1 1 
ATOM   224  C  CD2 . TRP A 1 41  ? 5.212   23.573 75.085  1.00 16.01 ? 41  TRP A CD2 1 
ATOM   225  N  NE1 . TRP A 1 41  ? 4.724   23.451 77.247  1.00 27.47 ? 41  TRP A NE1 1 
ATOM   226  C  CE2 . TRP A 1 41  ? 5.432   22.847 76.248  1.00 20.22 ? 41  TRP A CE2 1 
ATOM   227  C  CE3 . TRP A 1 41  ? 5.773   23.136 73.916  1.00 13.68 ? 41  TRP A CE3 1 
ATOM   228  C  CZ2 . TRP A 1 41  ? 6.280   21.737 76.267  1.00 20.49 ? 41  TRP A CZ2 1 
ATOM   229  C  CZ3 . TRP A 1 41  ? 6.615   22.053 73.958  1.00 14.19 ? 41  TRP A CZ3 1 
ATOM   230  C  CH2 . TRP A 1 41  ? 6.856   21.375 75.113  1.00 18.75 ? 41  TRP A CH2 1 
ATOM   231  N  N   . GLU A 1 42  ? 4.677   27.117 71.504  1.00 15.59 ? 42  GLU A N   1 
ATOM   232  C  CA  . GLU A 1 42  ? 4.143   27.733 70.338  1.00 17.05 ? 42  GLU A CA  1 
ATOM   233  C  C   . GLU A 1 42  ? 3.408   26.641 69.528  1.00 17.75 ? 42  GLU A C   1 
ATOM   234  O  O   . GLU A 1 42  ? 3.816   25.504 69.478  1.00 18.23 ? 42  GLU A O   1 
ATOM   235  C  CB  . GLU A 1 42  ? 5.241   28.246 69.410  1.00 22.63 ? 42  GLU A CB  1 
ATOM   236  N  N   . PRO A 1 43  ? 2.352   27.023 68.845  1.00 15.14 ? 43  PRO A N   1 
ATOM   237  C  CA  . PRO A 1 43  ? 1.675   26.053 67.992  1.00 14.81 ? 43  PRO A CA  1 
ATOM   238  C  C   . PRO A 1 43  ? 2.546   25.554 66.893  1.00 17.47 ? 43  PRO A C   1 
ATOM   239  O  O   . PRO A 1 43  ? 3.423   26.281 66.397  1.00 22.63 ? 43  PRO A O   1 
ATOM   240  C  CB  . PRO A 1 43  ? 0.429   26.819 67.472  1.00 18.72 ? 43  PRO A CB  1 
ATOM   241  C  CG  . PRO A 1 43  ? 0.263   27.965 68.409  1.00 24.14 ? 43  PRO A CG  1 
ATOM   242  C  CD  . PRO A 1 43  ? 1.653   28.317 68.900  1.00 18.23 ? 43  PRO A CD  1 
ATOM   243  N  N   . PHE A 1 44  ? 2.444   24.273 66.586  1.00 12.70 ? 44  PHE A N   1 
ATOM   244  C  CA  . PHE A 1 44  ? 3.242   23.685 65.551  1.00 13.28 ? 44  PHE A CA  1 
ATOM   245  C  C   . PHE A 1 44  ? 2.397   22.987 64.477  1.00 11.78 ? 44  PHE A C   1 
ATOM   246  O  O   . PHE A 1 44  ? 2.567   23.271 63.337  1.00 13.21 ? 44  PHE A O   1 
ATOM   247  C  CB  . PHE A 1 44  ? 4.273   22.721 66.174  1.00 12.82 ? 44  PHE A CB  1 
ATOM   248  C  CG  . PHE A 1 44  ? 5.147   22.036 65.195  1.00 13.07 ? 44  PHE A CG  1 
ATOM   249  C  CD1 . PHE A 1 44  ? 6.234   22.739 64.644  1.00 15.93 ? 44  PHE A CD1 1 
ATOM   250  C  CD2 . PHE A 1 44  ? 4.863   20.794 64.689  1.00 12.33 ? 44  PHE A CD2 1 
ATOM   251  C  CE1 . PHE A 1 44  ? 7.009   22.126 63.647  1.00 14.00 ? 44  PHE A CE1 1 
ATOM   252  C  CE2 . PHE A 1 44  ? 5.616   20.222 63.719  1.00 14.91 ? 44  PHE A CE2 1 
ATOM   253  C  CZ  . PHE A 1 44  ? 6.704   20.862 63.136  1.00 13.75 ? 44  PHE A CZ  1 
ATOM   254  N  N   . ALA A 1 45  ? 1.438   22.171 64.845  1.00 12.05 ? 45  ALA A N   1 
ATOM   255  C  CA  . ALA A 1 45  ? 0.579   21.525 63.948  1.00 14.79 ? 45  ALA A CA  1 
ATOM   256  C  C   . ALA A 1 45  ? -0.590  20.890 64.664  1.00 10.68 ? 45  ALA A C   1 
ATOM   257  O  O   . ALA A 1 45  ? -0.522  20.682 65.839  1.00 12.29 ? 45  ALA A O   1 
ATOM   258  C  CB  . ALA A 1 45  ? 1.316   20.357 63.216  1.00 10.94 ? 45  ALA A CB  1 
ATOM   259  N  N   . SER A 1 46  ? -1.668  20.572 63.937  1.00 10.54 ? 46  SER A N   1 
ATOM   260  C  CA  . SER A 1 46  ? -2.797  19.917 64.551  1.00 10.55 ? 46  SER A CA  1 
ATOM   261  C  C   . SER A 1 46  ? -3.548  19.121 63.491  1.00 9.59  ? 46  SER A C   1 
ATOM   262  O  O   . SER A 1 46  ? -3.425  19.363 62.309  1.00 11.20 ? 46  SER A O   1 
ATOM   263  C  CB  . SER A 1 46  ? -3.722  20.837 65.324  1.00 11.47 ? 46  SER A CB  1 
ATOM   264  O  OG  . SER A 1 46  ? -4.366  21.783 64.530  1.00 11.47 ? 46  SER A OG  1 
ATOM   265  N  N   . GLY A 1 47  ? -4.376  18.152 63.913  1.00 9.82  ? 47  GLY A N   1 
ATOM   266  C  CA  . GLY A 1 47  ? -5.174  17.387 63.023  1.00 10.34 ? 47  GLY A CA  1 
ATOM   267  C  C   . GLY A 1 47  ? -6.094  16.451 63.812  1.00 10.66 ? 47  GLY A C   1 
ATOM   268  O  O   . GLY A 1 47  ? -6.223  16.588 64.995  1.00 10.85 ? 47  GLY A O   1 
ATOM   269  N  N   . LYS A 1 48  ? -6.724  15.531 63.116  1.00 11.10 ? 48  LYS A N   1 
ATOM   270  C  CA  . LYS A 1 48  ? -7.681  14.626 63.721  1.00 13.79 ? 48  LYS A CA  1 
ATOM   271  C  C   . LYS A 1 48  ? -7.418  13.241 63.213  1.00 11.35 ? 48  LYS A C   1 
ATOM   272  O  O   . LYS A 1 48  ? -7.126  13.031 62.052  1.00 12.90 ? 48  LYS A O   1 
ATOM   273  C  CB  . LYS A 1 48  ? -9.190  14.991 63.367  1.00 21.52 ? 48  LYS A CB  1 
ATOM   274  N  N   . THR A 1 49  ? -7.612  12.233 64.051  1.00 11.21 ? 49  THR A N   1 
ATOM   275  C  CA  . THR A 1 49  ? -7.448  10.809 63.618  1.00 11.12 ? 49  THR A CA  1 
ATOM   276  C  C   . THR A 1 49  ? -8.528  10.427 62.677  1.00 11.33 ? 49  THR A C   1 
ATOM   277  O  O   . THR A 1 49  ? -9.675  10.870 62.754  1.00 12.85 ? 49  THR A O   1 
ATOM   278  C  CB  . THR A 1 49  ? -7.390  9.831  64.793  1.00 10.77 ? 49  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 49  ? -8.612  9.881  65.531  1.00 12.21 ? 49  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 49  ? -6.207  10.076 65.735  1.00 11.91 ? 49  THR A CG2 1 
ATOM   281  N  N   . SER A 1 50  ? -8.154  9.592  61.753  1.00 12.19 ? 50  SER A N   1 
ATOM   282  C  CA  . SER A 1 50  ? -9.016  9.005  60.726  1.00 14.01 ? 50  SER A CA  1 
ATOM   283  C  C   . SER A 1 50  ? -9.822  7.832  61.267  1.00 14.33 ? 50  SER A C   1 
ATOM   284  O  O   . SER A 1 50  ? -9.720  7.476  62.426  1.00 15.18 ? 50  SER A O   1 
ATOM   285  C  CB  . SER A 1 50  ? -8.144  8.536  59.596  1.00 16.38 ? 50  SER A CB  1 
ATOM   286  O  OG  . SER A 1 50  ? -7.462  7.368  59.983  1.00 17.62 ? 50  SER A OG  1 
ATOM   287  N  N   . GLU A 1 51  ? -10.511 7.153  60.362  1.00 17.20 ? 51  GLU A N   1 
ATOM   288  C  CA  . GLU A 1 51  ? -11.324 5.971  60.704  1.00 19.46 ? 51  GLU A CA  1 
ATOM   289  C  C   . GLU A 1 51  ? -10.446 4.794  61.154  1.00 18.70 ? 51  GLU A C   1 
ATOM   290  O  O   . GLU A 1 51  ? -10.890 3.868  61.839  1.00 20.71 ? 51  GLU A O   1 
ATOM   291  C  CB  . GLU A 1 51  ? -12.216 5.560  59.472  1.00 24.84 ? 51  GLU A CB  1 
ATOM   292  N  N   . SER A 1 52  ? -9.161  4.841  60.816  1.00 17.09 ? 52  SER A N   1 
ATOM   293  C  CA  . SER A 1 52  ? -8.195  3.838  61.293  1.00 16.53 ? 52  SER A CA  1 
ATOM   294  C  C   . SER A 1 52  ? -7.516  4.258  62.591  1.00 13.85 ? 52  SER A C   1 
ATOM   295  O  O   . SER A 1 52  ? -6.650  3.542  63.075  1.00 16.03 ? 52  SER A O   1 
ATOM   296  C  CB  . SER A 1 52  ? -7.113  3.639  60.242  1.00 22.79 ? 52  SER A CB  1 
ATOM   297  O  OG  . SER A 1 52  ? -6.249  4.789  60.096  1.00 24.82 ? 52  SER A OG  1 
ATOM   298  N  N   . GLY A 1 53  ? -7.867  5.401  63.161  1.00 12.86 ? 53  GLY A N   1 
ATOM   299  C  CA  . GLY A 1 53  ? -7.217  5.873  64.348  1.00 12.44 ? 53  GLY A CA  1 
ATOM   300  C  C   . GLY A 1 53  ? -5.903  6.537  64.111  1.00 11.42 ? 53  GLY A C   1 
ATOM   301  O  O   . GLY A 1 53  ? -5.186  6.855  65.067  1.00 12.38 ? 53  GLY A O   1 
ATOM   302  N  N   . GLU A 1 54  ? -5.516  6.732  62.871  1.00 13.45 ? 54  GLU A N   1 
ATOM   303  C  CA  . GLU A 1 54  ? -4.224  7.317  62.490  1.00 13.38 ? 54  GLU A CA  1 
ATOM   304  C  C   . GLU A 1 54  ? -4.347  8.735  62.082  1.00 11.05 ? 54  GLU A C   1 
ATOM   305  O  O   . GLU A 1 54  ? -5.302  9.136  61.434  1.00 13.79 ? 54  GLU A O   1 
ATOM   306  C  CB  . GLU A 1 54  ? -3.550  6.510  61.410  1.00 16.71 ? 54  GLU A CB  1 
ATOM   307  C  CG  . GLU A 1 54  ? -3.352  5.049  61.860  1.00 18.09 ? 54  GLU A CG  1 
ATOM   308  C  CD  . GLU A 1 54  ? -2.461  4.226  60.968  1.00 32.00 ? 54  GLU A CD  1 
ATOM   309  O  OE1 . GLU A 1 54  ? -2.537  4.371  59.752  1.00 39.09 ? 54  GLU A OE1 1 
ATOM   310  N  N   . LEU A 1 55  ? -3.283  9.496  62.331  1.00 11.39 ? 55  LEU A N   1 
ATOM   311  C  CA  . LEU A 1 55  ? -3.168  10.860 61.894  1.00 11.18 ? 55  LEU A CA  1 
ATOM   312  C  C   . LEU A 1 55  ? -1.844  11.027 61.220  1.00 11.84 ? 55  LEU A C   1 
ATOM   313  O  O   . LEU A 1 55  ? -0.798  10.947 61.859  1.00 12.20 ? 55  LEU A O   1 
ATOM   314  C  CB  . LEU A 1 55  ? -3.304  11.783 63.094  1.00 11.27 ? 55  LEU A CB  1 
ATOM   315  C  CG  . LEU A 1 55  ? -2.913  13.262 62.889  1.00 12.66 ? 55  LEU A CG  1 
ATOM   316  C  CD1 . LEU A 1 55  ? -3.648  13.841 61.713  1.00 13.23 ? 55  LEU A CD1 1 
ATOM   317  C  CD2 . LEU A 1 55  ? -3.253  14.004 64.170  1.00 13.35 ? 55  LEU A CD2 1 
ATOM   318  N  N   . HIS A 1 56  ? -1.884  11.185 59.905  1.00 14.48 ? 56  HIS A N   1 
ATOM   319  C  CA  . HIS A 1 56  ? -0.764  11.425 59.034  1.00 16.31 ? 56  HIS A CA  1 
ATOM   320  C  C   . HIS A 1 56  ? -0.805  12.893 58.588  1.00 16.75 ? 56  HIS A C   1 
ATOM   321  O  O   . HIS A 1 56  ? -1.823  13.541 58.685  1.00 18.01 ? 56  HIS A O   1 
ATOM   322  C  CB  . HIS A 1 56  ? -0.894  10.529 57.772  1.00 17.11 ? 56  HIS A CB  1 
ATOM   323  C  CG  . HIS A 1 56  ? -0.750  9.079  58.065  1.00 19.41 ? 56  HIS A CG  1 
ATOM   324  N  ND1 . HIS A 1 56  ? -1.794  8.257  58.365  1.00 25.31 ? 56  HIS A ND1 1 
ATOM   325  C  CD2 . HIS A 1 56  ? 0.358   8.349  58.242  1.00 23.43 ? 56  HIS A CD2 1 
ATOM   326  C  CE1 . HIS A 1 56  ? -1.346  7.058  58.665  1.00 26.56 ? 56  HIS A CE1 1 
ATOM   327  N  NE2 . HIS A 1 56  ? -0.038  7.087  58.579  1.00 30.37 ? 56  HIS A NE2 1 
ATOM   328  N  N   . GLY A 1 57  ? 0.266   13.365 58.077  1.00 18.28 ? 57  GLY A N   1 
ATOM   329  C  CA  . GLY A 1 57  ? 0.285   14.655 57.458  1.00 18.23 ? 57  GLY A CA  1 
ATOM   330  C  C   . GLY A 1 57  ? 0.359   15.830 58.403  1.00 15.56 ? 57  GLY A C   1 
ATOM   331  O  O   . GLY A 1 57  ? 0.181   16.968 57.993  1.00 17.20 ? 57  GLY A O   1 
ATOM   332  N  N   . LEU A 1 58  ? 0.725   15.610 59.630  1.00 13.31 ? 58  LEU A N   1 
ATOM   333  C  CA  . LEU A 1 58  ? 0.889   16.707 60.562  1.00 12.98 ? 58  LEU A CA  1 
ATOM   334  C  C   . LEU A 1 58  ? 1.943   17.688 60.092  1.00 12.70 ? 58  LEU A C   1 
ATOM   335  O  O   . LEU A 1 58  ? 1.778   18.895 60.245  1.00 14.66 ? 58  LEU A O   1 
ATOM   336  C  CB  . LEU A 1 58  ? 1.214   16.255 61.977  1.00 12.61 ? 58  LEU A CB  1 
ATOM   337  C  CG  . LEU A 1 58  ? 0.021   15.820 62.849  1.00 13.82 ? 58  LEU A CG  1 
ATOM   338  C  CD1 . LEU A 1 58  ? 0.468   15.009 64.047  1.00 14.24 ? 58  LEU A CD1 1 
ATOM   339  C  CD2 . LEU A 1 58  ? -0.790  17.056 63.286  1.00 14.70 ? 58  LEU A CD2 1 
ATOM   340  N  N   . THR A 1 59  ? 3.070   17.157 59.618  1.00 12.61 ? 59  THR A N   1 
ATOM   341  C  CA  . THR A 1 59  ? 4.221   18.009 59.310  1.00 11.88 ? 59  THR A CA  1 
ATOM   342  C  C   . THR A 1 59  ? 5.030   17.452 58.179  1.00 13.25 ? 59  THR A C   1 
ATOM   343  O  O   . THR A 1 59  ? 4.638   16.496 57.546  1.00 15.58 ? 59  THR A O   1 
ATOM   344  C  CB  . THR A 1 59  ? 5.019   18.274 60.565  1.00 13.19 ? 59  THR A CB  1 
ATOM   345  O  OG1 . THR A 1 59  ? 5.960   19.344 60.377  1.00 14.13 ? 59  THR A OG1 1 
ATOM   346  C  CG2 . THR A 1 59  ? 5.788   17.091 61.023  1.00 13.78 ? 59  THR A CG2 1 
ATOM   347  N  N   . THR A 1 60  ? 6.135   18.090 57.848  1.00 15.11 ? 60  THR A N   1 
ATOM   348  C  CA  . THR A 1 60  ? 6.999   17.765 56.740  1.00 14.26 ? 60  THR A CA  1 
ATOM   349  C  C   . THR A 1 60  ? 8.418   17.686 57.248  1.00 13.59 ? 60  THR A C   1 
ATOM   350  O  O   . THR A 1 60  ? 8.763   18.184 58.330  1.00 13.32 ? 60  THR A O   1 
ATOM   351  C  CB  . THR A 1 60  ? 6.956   18.853 55.648  1.00 15.41 ? 60  THR A CB  1 
ATOM   352  O  OG1 . THR A 1 60  ? 7.492   20.063 56.197  1.00 15.66 ? 60  THR A OG1 1 
ATOM   353  C  CG2 . THR A 1 60  ? 5.531   19.106 55.161  1.00 18.05 ? 60  THR A CG2 1 
ATOM   354  N  N   . GLU A 1 61  ? 9.289   17.086 56.478  1.00 14.69 ? 61  GLU A N   1 
ATOM   355  C  CA  . GLU A 1 61  ? 10.700  17.010 56.823  1.00 15.38 ? 61  GLU A CA  1 
ATOM   356  C  C   . GLU A 1 61  ? 11.313  18.418 56.947  1.00 14.34 ? 61  GLU A C   1 
ATOM   357  O  O   . GLU A 1 61  ? 12.214  18.606 57.733  1.00 15.90 ? 61  GLU A O   1 
ATOM   358  C  CB  . GLU A 1 61  ? 11.470  16.283 55.727  1.00 19.37 ? 61  GLU A CB  1 
ATOM   359  N  N   . GLU A 1 62  ? 10.827  19.360 56.170  1.00 13.87 ? 62  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 62  ? 11.365  20.733 56.260  1.00 14.48 ? 62  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 62  ? 10.926  21.446 57.525  1.00 13.63 ? 62  GLU A C   1 
ATOM   362  O  O   . GLU A 1 62  ? 11.707  22.148 58.164  1.00 15.46 ? 62  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 62  ? 10.924  21.549 55.062  1.00 18.31 ? 62  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 62  ? 11.438  21.167 53.710  1.00 21.79 ? 62  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 62  ? 10.906  19.860 53.142  1.00 22.60 ? 62  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 62  ? 9.747   19.412 53.447  1.00 22.37 ? 62  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 62  ? 11.738  19.254 52.387  1.00 36.10 ? 62  GLU A OE2 1 
ATOM   368  N  N   . GLU A 1 63  ? 9.687   21.283 57.906  1.00 12.85 ? 63  GLU A N   1 
ATOM   369  C  CA  . GLU A 1 63  ? 9.102   21.992 59.038  1.00 12.63 ? 63  GLU A CA  1 
ATOM   370  C  C   . GLU A 1 63  ? 9.539   21.404 60.383  1.00 11.42 ? 63  GLU A C   1 
ATOM   371  O  O   . GLU A 1 63  ? 9.646   22.094 61.350  1.00 11.51 ? 63  GLU A O   1 
ATOM   372  C  CB  . GLU A 1 63  ? 7.606   22.035 58.906  1.00 12.70 ? 63  GLU A CB  1 
ATOM   373  C  CG  . GLU A 1 63  ? 6.842   22.743 59.959  1.00 15.57 ? 63  GLU A CG  1 
ATOM   374  C  CD  . GLU A 1 63  ? 5.340   22.704 59.671  1.00 20.90 ? 63  GLU A CD  1 
ATOM   375  O  OE1 . GLU A 1 63  ? 4.653   21.678 59.952  1.00 18.52 ? 63  GLU A OE1 1 
ATOM   376  O  OE2 . GLU A 1 63  ? 4.874   23.734 59.150  1.00 23.63 ? 63  GLU A OE2 1 
ATOM   377  N  N   . PHE A 1 64  ? 9.741   20.097 60.424  1.00 11.71 ? 64  PHE A N   1 
ATOM   378  C  CA  . PHE A 1 64  ? 9.991   19.363 61.671  1.00 10.92 ? 64  PHE A CA  1 
ATOM   379  C  C   . PHE A 1 64  ? 11.430  19.409 62.034  1.00 10.22 ? 64  PHE A C   1 
ATOM   380  O  O   . PHE A 1 64  ? 12.155  18.404 61.927  1.00 12.33 ? 64  PHE A O   1 
ATOM   381  C  CB  . PHE A 1 64  ? 9.434   17.945 61.500  1.00 11.62 ? 64  PHE A CB  1 
ATOM   382  C  CG  . PHE A 1 64  ? 9.368   17.131 62.786  1.00 11.17 ? 64  PHE A CG  1 
ATOM   383  C  CD1 . PHE A 1 64  ? 8.807   17.600 63.913  1.00 13.07 ? 64  PHE A CD1 1 
ATOM   384  C  CD2 . PHE A 1 64  ? 9.933   15.834 62.830  1.00 14.27 ? 64  PHE A CD2 1 
ATOM   385  C  CE1 . PHE A 1 64  ? 8.740   16.795 65.069  1.00 13.98 ? 64  PHE A CE1 1 
ATOM   386  C  CE2 . PHE A 1 64  ? 9.849   15.051 63.938  1.00 16.67 ? 64  PHE A CE2 1 
ATOM   387  C  CZ  . PHE A 1 64  ? 9.217   15.518 65.048  1.00 15.76 ? 64  PHE A CZ  1 
ATOM   388  N  N   . VAL A 1 65  ? 11.863  20.530 62.522  1.00 10.23 ? 65  VAL A N   1 
ATOM   389  C  CA  . VAL A 1 65  ? 13.271  20.757 62.934  1.00 9.83  ? 65  VAL A CA  1 
ATOM   390  C  C   . VAL A 1 65  ? 13.506  20.203 64.331  1.00 11.54 ? 65  VAL A C   1 
ATOM   391  O  O   . VAL A 1 65  ? 12.608  19.691 65.001  1.00 11.21 ? 65  VAL A O   1 
ATOM   392  C  CB  . VAL A 1 65  ? 13.519  22.297 62.868  1.00 10.96 ? 65  VAL A CB  1 
ATOM   393  C  CG1 . VAL A 1 65  ? 13.481  22.808 61.435  1.00 12.65 ? 65  VAL A CG1 1 
ATOM   394  C  CG2 . VAL A 1 65  ? 12.560  23.078 63.743  1.00 12.85 ? 65  VAL A CG2 1 
ATOM   395  N  N   . GLU A 1 66  ? 14.739  20.309 64.786  1.00 11.39 ? 66  GLU A N   1 
ATOM   396  C  CA  . GLU A 1 66  ? 15.025  19.965 66.196  1.00 12.70 ? 66  GLU A CA  1 
ATOM   397  C  C   . GLU A 1 66  ? 14.167  20.827 67.100  1.00 12.41 ? 66  GLU A C   1 
ATOM   398  O  O   . GLU A 1 66  ? 13.841  21.939 66.730  1.00 13.93 ? 66  GLU A O   1 
ATOM   399  C  CB  . GLU A 1 66  ? 16.456  20.340 66.591  1.00 14.54 ? 66  GLU A CB  1 
ATOM   400  C  CG  . GLU A 1 66  ? 17.527  19.539 65.891  1.00 15.34 ? 66  GLU A CG  1 
ATOM   401  C  CD  . GLU A 1 66  ? 18.890  19.806 66.500  1.00 13.79 ? 66  GLU A CD  1 
ATOM   402  O  OE1 . GLU A 1 66  ? 19.647  20.597 65.929  1.00 14.45 ? 66  GLU A OE1 1 
ATOM   403  O  OE2 . GLU A 1 66  ? 19.169  19.247 67.559  1.00 15.75 ? 66  GLU A OE2 1 
ATOM   404  N  N   . GLY A 1 67  ? 13.817  20.301 68.250  1.00 10.99 ? 67  GLY A N   1 
ATOM   405  C  CA  . GLY A 1 67  ? 13.133  21.058 69.251  1.00 12.75 ? 67  GLY A CA  1 
ATOM   406  C  C   . GLY A 1 67  ? 12.549  20.167 70.290  1.00 11.12 ? 67  GLY A C   1 
ATOM   407  O  O   . GLY A 1 67  ? 12.654  18.937 70.236  1.00 11.25 ? 67  GLY A O   1 
ATOM   408  N  N   . ILE A 1 68  ? 11.917  20.758 71.270  1.00 11.27 ? 68  ILE A N   1 
ATOM   409  C  CA  . ILE A 1 68  ? 11.112  20.047 72.276  1.00 10.43 ? 68  ILE A CA  1 
ATOM   410  C  C   . ILE A 1 68  ? 9.691   20.181 71.873  1.00 10.18 ? 68  ILE A C   1 
ATOM   411  O  O   . ILE A 1 68  ? 9.186   21.306 71.688  1.00 10.97 ? 68  ILE A O   1 
ATOM   412  C  CB  . ILE A 1 68  ? 11.362  20.588 73.699  1.00 11.54 ? 68  ILE A CB  1 
ATOM   413  C  CG1 . ILE A 1 68  ? 12.845  20.473 74.100  1.00 15.51 ? 68  ILE A CG1 1 
ATOM   414  C  CG2 . ILE A 1 68  ? 10.499  19.864 74.667  1.00 14.07 ? 68  ILE A CG2 1 
ATOM   415  C  CD1 . ILE A 1 68  ? 13.179  21.120 75.445  1.00 19.50 ? 68  ILE A CD1 1 
ATOM   416  N  N   . TYR A 1 69  ? 9.030   19.075 71.634  1.00 10.19 ? 69  TYR A N   1 
ATOM   417  C  CA  . TYR A 1 69  ? 7.655   19.017 71.143  1.00 9.49  ? 69  TYR A CA  1 
ATOM   418  C  C   . TYR A 1 69  ? 6.721   18.453 72.180  1.00 10.21 ? 69  TYR A C   1 
ATOM   419  O  O   . TYR A 1 69  ? 7.103   17.602 72.999  1.00 11.20 ? 69  TYR A O   1 
ATOM   420  C  CB  . TYR A 1 69  ? 7.604   18.156 69.886  1.00 10.55 ? 69  TYR A CB  1 
ATOM   421  C  CG  . TYR A 1 69  ? 8.277   18.813 68.706  1.00 10.47 ? 69  TYR A CG  1 
ATOM   422  C  CD1 . TYR A 1 69  ? 9.628   18.706 68.479  1.00 10.70 ? 69  TYR A CD1 1 
ATOM   423  C  CD2 . TYR A 1 69  ? 7.555   19.548 67.759  1.00 10.24 ? 69  TYR A CD2 1 
ATOM   424  C  CE1 . TYR A 1 69  ? 10.259  19.299 67.412  1.00 10.28 ? 69  TYR A CE1 1 
ATOM   425  C  CE2 . TYR A 1 69  ? 8.174   20.128 66.690  1.00 11.45 ? 69  TYR A CE2 1 
ATOM   426  C  CZ  . TYR A 1 69  ? 9.549   20.022 66.523  1.00 10.59 ? 69  TYR A CZ  1 
ATOM   427  O  OH  . TYR A 1 69  ? 10.112  20.650 65.446  1.00 12.94 ? 69  TYR A OH  1 
ATOM   428  N  N   . LYS A 1 70  ? 5.485   18.925 72.170  1.00 10.46 ? 70  LYS A N   1 
ATOM   429  C  CA  . LYS A 1 70  ? 4.429   18.420 72.983  1.00 11.40 ? 70  LYS A CA  1 
ATOM   430  C  C   . LYS A 1 70  ? 3.297   17.973 72.050  1.00 11.03 ? 70  LYS A C   1 
ATOM   431  O  O   . LYS A 1 70  ? 2.826   18.783 71.280  1.00 12.29 ? 70  LYS A O   1 
ATOM   432  C  CB  . LYS A 1 70  ? 3.874   19.479 73.945  1.00 13.92 ? 70  LYS A CB  1 
ATOM   433  C  CG  . LYS A 1 70  ? 2.639   18.998 74.633  1.00 19.42 ? 70  LYS A CG  1 
ATOM   434  C  CD  . LYS A 1 70  ? 2.363   19.702 75.896  1.00 28.25 ? 70  LYS A CD  1 
ATOM   435  C  CE  . LYS A 1 70  ? 2.214   21.184 75.684  1.00 31.34 ? 70  LYS A CE  1 
ATOM   436  N  NZ  . LYS A 1 70  ? 1.652   21.796 76.905  1.00 45.39 ? 70  LYS A NZ  1 
ATOM   437  N  N   . VAL A 1 71  ? 2.869   16.740 72.170  1.00 12.24 ? 71  VAL A N   1 
ATOM   438  C  CA  . VAL A 1 71  ? 1.702   16.223 71.451  1.00 11.70 ? 71  VAL A CA  1 
ATOM   439  C  C   . VAL A 1 71  ? 0.576   16.053 72.441  1.00 12.02 ? 71  VAL A C   1 
ATOM   440  O  O   . VAL A 1 71  ? 0.719   15.269 73.386  1.00 13.78 ? 71  VAL A O   1 
ATOM   441  C  CB  . VAL A 1 71  ? 2.029   14.904 70.779  1.00 12.56 ? 71  VAL A CB  1 
ATOM   442  C  CG1 . VAL A 1 71  ? 0.823   14.289 70.090  1.00 14.59 ? 71  VAL A CG1 1 
ATOM   443  C  CG2 . VAL A 1 71  ? 3.216   15.023 69.881  1.00 13.61 ? 71  VAL A CG2 1 
ATOM   444  N  N   . GLU A 1 72  ? -0.505  16.820 72.306  1.00 12.00 ? 72  GLU A N   1 
ATOM   445  C  CA  . GLU A 1 72  ? -1.644  16.793 73.212  1.00 12.26 ? 72  GLU A CA  1 
ATOM   446  C  C   . GLU A 1 72  ? -2.800  16.140 72.466  1.00 10.71 ? 72  GLU A C   1 
ATOM   447  O  O   . GLU A 1 72  ? -3.290  16.661 71.495  1.00 12.91 ? 72  GLU A O   1 
ATOM   448  C  CB  . GLU A 1 72  ? -2.026  18.217 73.662  1.00 15.71 ? 72  GLU A CB  1 
ATOM   449  C  CG  . GLU A 1 72  ? -1.187  18.865 74.820  1.00 25.00 ? 72  GLU A CG  1 
ATOM   450  C  CD  . GLU A 1 72  ? -1.875  20.077 75.530  1.00 29.34 ? 72  GLU A CD  1 
ATOM   451  O  OE1 . GLU A 1 72  ? -2.808  20.621 74.908  1.00 30.18 ? 72  GLU A OE1 1 
ATOM   452  N  N   . ILE A 1 73  ? -3.217  15.013 72.934  1.00 11.51 ? 73  ILE A N   1 
ATOM   453  C  CA  . ILE A 1 73  ? -4.293  14.237 72.354  1.00 12.46 ? 73  ILE A CA  1 
ATOM   454  C  C   . ILE A 1 73  ? -5.537  14.555 73.138  1.00 11.87 ? 73  ILE A C   1 
ATOM   455  O  O   . ILE A 1 73  ? -5.583  14.307 74.311  1.00 11.95 ? 73  ILE A O   1 
ATOM   456  C  CB  . ILE A 1 73  ? -3.947  12.739 72.373  1.00 11.73 ? 73  ILE A CB  1 
ATOM   457  C  CG1 . ILE A 1 73  ? -2.651  12.477 71.586  1.00 13.84 ? 73  ILE A CG1 1 
ATOM   458  C  CG2 . ILE A 1 73  ? -5.130  11.941 71.825  1.00 13.10 ? 73  ILE A CG2 1 
ATOM   459  C  CD1 . ILE A 1 73  ? -2.083  11.072 71.825  1.00 15.75 ? 73  ILE A CD1 1 
ATOM   460  N  N   . ASP A 1 74  ? -6.598  15.026 72.483  1.00 11.36 ? 74  ASP A N   1 
ATOM   461  C  CA  . ASP A 1 74  ? -7.818  15.482 73.151  1.00 12.73 ? 74  ASP A CA  1 
ATOM   462  C  C   . ASP A 1 74  ? -8.721  14.309 73.508  1.00 12.61 ? 74  ASP A C   1 
ATOM   463  O  O   . ASP A 1 74  ? -9.738  14.069 72.947  1.00 13.56 ? 74  ASP A O   1 
ATOM   464  C  CB  . ASP A 1 74  ? -8.534  16.554 72.327  1.00 12.94 ? 74  ASP A CB  1 
ATOM   465  C  CG  . ASP A 1 74  ? -9.755  17.057 73.011  1.00 16.58 ? 74  ASP A CG  1 
ATOM   466  O  OD1 . ASP A 1 74  ? -9.962  16.826 74.224  1.00 17.49 ? 74  ASP A OD1 1 
ATOM   467  O  OD2 . ASP A 1 74  ? -10.553 17.716 72.318  1.00 19.62 ? 74  ASP A OD2 1 
ATOM   468  N  N   . THR A 1 75  ? -8.300  13.606 74.540  1.00 12.25 ? 75  THR A N   1 
ATOM   469  C  CA  . THR A 1 75  ? -9.034  12.478 75.025  1.00 12.89 ? 75  THR A CA  1 
ATOM   470  C  C   . THR A 1 75  ? -10.325 12.855 75.750  1.00 13.27 ? 75  THR A C   1 
ATOM   471  O  O   . THR A 1 75  ? -11.302 12.094 75.692  1.00 14.28 ? 75  THR A O   1 
ATOM   472  C  CB  . THR A 1 75  ? -8.145  11.592 75.878  1.00 13.77 ? 75  THR A CB  1 
ATOM   473  O  OG1 . THR A 1 75  ? -7.749  12.344 77.039  1.00 13.87 ? 75  THR A OG1 1 
ATOM   474  C  CG2 . THR A 1 75  ? -6.925  11.118 75.137  1.00 15.07 ? 75  THR A CG2 1 
ATOM   475  N  N   . LYS A 1 76  ? -10.364 14.048 76.323  1.00 13.14 ? 76  LYS A N   1 
ATOM   476  C  CA  . LYS A 1 76  ? -11.565 14.426 77.036  1.00 13.42 ? 76  LYS A CA  1 
ATOM   477  C  C   . LYS A 1 76  ? -12.711 14.569 76.053  1.00 12.37 ? 76  LYS A C   1 
ATOM   478  O  O   . LYS A 1 76  ? -13.817 14.068 76.319  1.00 13.94 ? 76  LYS A O   1 
ATOM   479  C  CB  . LYS A 1 76  ? -11.308 15.740 77.795  1.00 17.02 ? 76  LYS A CB  1 
ATOM   480  C  CG  . LYS A 1 76  ? -12.510 16.210 78.598  1.00 20.41 ? 76  LYS A CG  1 
ATOM   481  C  CD  . LYS A 1 76  ? -12.203 17.400 79.480  1.00 28.29 ? 76  LYS A CD  1 
ATOM   482  N  N   . SER A 1 77  ? -12.517 15.237 74.919  1.00 12.99 ? 77  SER A N   1 
ATOM   483  C  CA  . SER A 1 77  ? -13.587 15.372 73.951  1.00 13.00 ? 77  SER A CA  1 
ATOM   484  C  C   . SER A 1 77  ? -13.999 14.053 73.332  1.00 12.63 ? 77  SER A C   1 
ATOM   485  O  O   . SER A 1 77  ? -15.141 13.863 73.057  1.00 13.71 ? 77  SER A O   1 
ATOM   486  C  CB  . SER A 1 77  ? -13.200 16.319 72.813  1.00 15.43 ? 77  SER A CB  1 
ATOM   487  O  OG  . SER A 1 77  ? -12.999 17.623 73.285  1.00 18.08 ? 77  SER A OG  1 
ATOM   488  N  N   . TYR A 1 78  ? -13.041 13.146 73.152  1.00 13.69 ? 78  TYR A N   1 
ATOM   489  C  CA  . TYR A 1 78  ? -13.311 11.798 72.627  1.00 12.69 ? 78  TYR A CA  1 
ATOM   490  C  C   . TYR A 1 78  ? -14.299 11.082 73.551  1.00 12.94 ? 78  TYR A C   1 
ATOM   491  O  O   . TYR A 1 78  ? -15.340 10.578 73.093  1.00 13.55 ? 78  TYR A O   1 
ATOM   492  C  CB  . TYR A 1 78  ? -12.030 11.031 72.492  1.00 12.73 ? 78  TYR A CB  1 
ATOM   493  C  CG  . TYR A 1 78  ? -12.244 9.623  72.062  1.00 12.64 ? 78  TYR A CG  1 
ATOM   494  C  CD1 . TYR A 1 78  ? -12.609 9.341  70.735  1.00 12.86 ? 78  TYR A CD1 1 
ATOM   495  C  CD2 . TYR A 1 78  ? -12.111 8.540  72.952  1.00 13.27 ? 78  TYR A CD2 1 
ATOM   496  C  CE1 . TYR A 1 78  ? -12.823 8.065  70.322  1.00 14.39 ? 78  TYR A CE1 1 
ATOM   497  C  CE2 . TYR A 1 78  ? -12.401 7.248  72.495  1.00 12.74 ? 78  TYR A CE2 1 
ATOM   498  C  CZ  . TYR A 1 78  ? -12.681 7.024  71.209  1.00 12.99 ? 78  TYR A CZ  1 
ATOM   499  O  OH  . TYR A 1 78  ? -12.932 5.744  70.775  1.00 13.88 ? 78  TYR A OH  1 
ATOM   500  N  N   . TRP A 1 79  ? -13.999 11.013 74.840  1.00 13.37 ? 79  TRP A N   1 
ATOM   501  C  CA  . TRP A 1 79  ? -14.840 10.318 75.774  1.00 12.69 ? 79  TRP A CA  1 
ATOM   502  C  C   . TRP A 1 79  ? -16.214 10.980 75.881  1.00 13.92 ? 79  TRP A C   1 
ATOM   503  O  O   . TRP A 1 79  ? -17.247 10.318 75.877  1.00 15.67 ? 79  TRP A O   1 
ATOM   504  C  CB  . TRP A 1 79  ? -14.172 10.149 77.129  1.00 13.15 ? 79  TRP A CB  1 
ATOM   505  C  CG  . TRP A 1 79  ? -13.027 9.160  77.042  1.00 13.78 ? 79  TRP A CG  1 
ATOM   506  C  CD1 . TRP A 1 79  ? -11.678 9.410  77.292  1.00 12.60 ? 79  TRP A CD1 1 
ATOM   507  C  CD2 . TRP A 1 79  ? -13.091 7.779  76.709  1.00 12.37 ? 79  TRP A CD2 1 
ATOM   508  N  NE1 . TRP A 1 79  ? -10.951 8.334  77.097  1.00 11.99 ? 79  TRP A NE1 1 
ATOM   509  C  CE2 . TRP A 1 79  ? -11.745 7.277  76.765  1.00 13.10 ? 79  TRP A CE2 1 
ATOM   510  C  CE3 . TRP A 1 79  ? -14.105 6.902  76.369  1.00 14.03 ? 79  TRP A CE3 1 
ATOM   511  C  CZ2 . TRP A 1 79  ? -11.438 5.970  76.446  1.00 13.42 ? 79  TRP A CZ2 1 
ATOM   512  C  CZ3 . TRP A 1 79  ? -13.799 5.595  76.066  1.00 16.03 ? 79  TRP A CZ3 1 
ATOM   513  C  CH2 . TRP A 1 79  ? -12.463 5.135  76.107  1.00 15.40 ? 79  TRP A CH2 1 
ATOM   514  N  N   . LYS A 1 80  ? -16.223 12.286 75.953  1.00 14.08 ? 80  LYS A N   1 
ATOM   515  C  CA  . LYS A 1 80  ? -17.478 13.047 76.096  1.00 14.05 ? 80  LYS A CA  1 
ATOM   516  C  C   . LYS A 1 80  ? -18.385 12.866 74.905  1.00 15.61 ? 80  LYS A C   1 
ATOM   517  O  O   . LYS A 1 80  ? -19.603 12.695 75.052  1.00 16.93 ? 80  LYS A O   1 
ATOM   518  C  CB  . LYS A 1 80  ? -17.198 14.570 76.351  1.00 18.69 ? 80  LYS A CB  1 
ATOM   519  N  N   . ALA A 1 81  ? -17.803 12.693 73.748  1.00 15.00 ? 81  ALA A N   1 
ATOM   520  C  CA  . ALA A 1 81  ? -18.623 12.465 72.554  1.00 16.22 ? 81  ALA A CA  1 
ATOM   521  C  C   . ALA A 1 81  ? -19.249 11.072 72.591  1.00 16.93 ? 81  ALA A C   1 
ATOM   522  O  O   . ALA A 1 81  ? -20.290 10.852 71.991  1.00 20.28 ? 81  ALA A O   1 
ATOM   523  C  CB  . ALA A 1 81  ? -17.794 12.601 71.270  1.00 17.90 ? 81  ALA A CB  1 
ATOM   524  N  N   . LEU A 1 82  ? -18.637 10.131 73.304  1.00 16.34 ? 82  LEU A N   1 
ATOM   525  C  CA  . LEU A 1 82  ? -19.159 8.740  73.460  1.00 15.33 ? 82  LEU A CA  1 
ATOM   526  C  C   . LEU A 1 82  ? -20.076 8.699  74.670  1.00 15.97 ? 82  LEU A C   1 
ATOM   527  O  O   . LEU A 1 82  ? -20.545 7.626  75.027  1.00 18.15 ? 82  LEU A O   1 
ATOM   528  C  CB  . LEU A 1 82  ? -18.022 7.796  73.639  1.00 15.68 ? 82  LEU A CB  1 
ATOM   529  C  CG  . LEU A 1 82  ? -17.179 7.559  72.416  1.00 20.20 ? 82  LEU A CG  1 
ATOM   530  C  CD1 . LEU A 1 82  ? -15.979 6.704  72.765  1.00 24.53 ? 82  LEU A CD1 1 
ATOM   531  C  CD2 . LEU A 1 82  ? -17.955 7.115  71.196  1.00 25.00 ? 82  LEU A CD2 1 
ATOM   532  N  N   . GLY A 1 83  ? -20.330 9.827  75.287  1.00 16.86 ? 83  GLY A N   1 
ATOM   533  C  CA  . GLY A 1 83  ? -21.206 9.972  76.401  1.00 17.45 ? 83  GLY A CA  1 
ATOM   534  C  C   . GLY A 1 83  ? -20.650 9.514  77.712  1.00 15.86 ? 83  GLY A C   1 
ATOM   535  O  O   . GLY A 1 83  ? -21.400 9.215  78.642  1.00 18.97 ? 83  GLY A O   1 
ATOM   536  N  N   . ILE A 1 84  ? -19.324 9.535  77.820  1.00 15.74 ? 84  ILE A N   1 
ATOM   537  C  CA  . ILE A 1 84  ? -18.587 9.075  79.006  1.00 17.25 ? 84  ILE A CA  1 
ATOM   538  C  C   . ILE A 1 84  ? -17.873 10.244 79.665  1.00 18.98 ? 84  ILE A C   1 
ATOM   539  O  O   . ILE A 1 84  ? -17.355 11.122 78.936  1.00 20.74 ? 84  ILE A O   1 
ATOM   540  C  CB  . ILE A 1 84  ? -17.557 7.993  78.551  1.00 18.24 ? 84  ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 84  ? -18.301 6.710  78.138  1.00 26.85 ? 84  ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 84  ? -16.580 7.657  79.673  1.00 17.44 ? 84  ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 84  ? -17.722 6.015  76.928  1.00 35.09 ? 84  ILE A CD1 1 
ATOM   544  N  N   . SER A 1 85  ? -17.890 10.284 80.993  1.00 17.16 ? 85  SER A N   1 
ATOM   545  C  CA  . SER A 1 85  ? -17.191 11.340 81.766  1.00 17.48 ? 85  SER A CA  1 
ATOM   546  C  C   . SER A 1 85  ? -15.773 10.856 82.054  1.00 15.44 ? 85  SER A C   1 
ATOM   547  O  O   . SER A 1 85  ? -15.596 10.000 82.898  1.00 21.99 ? 85  SER A O   1 
ATOM   548  C  CB  . SER A 1 85  ? -17.875 11.645 83.063  1.00 23.20 ? 85  SER A CB  1 
ATOM   549  O  OG  . SER A 1 85  ? -19.190 12.114 82.862  1.00 28.31 ? 85  SER A OG  1 
ATOM   550  N  N   . PRO A 1 86  ? -14.741 11.348 81.366  1.00 14.13 ? 86  PRO A N   1 
ATOM   551  C  CA  . PRO A 1 86  ? -13.380 10.800 81.613  1.00 16.37 ? 86  PRO A CA  1 
ATOM   552  C  C   . PRO A 1 86  ? -12.658 11.555 82.687  1.00 15.32 ? 86  PRO A C   1 
ATOM   553  O  O   . PRO A 1 86  ? -13.019 12.669 83.056  1.00 16.42 ? 86  PRO A O   1 
ATOM   554  C  CB  . PRO A 1 86  ? -12.689 10.971 80.243  1.00 19.94 ? 86  PRO A CB  1 
ATOM   555  C  CG  . PRO A 1 86  ? -13.183 12.321 79.905  1.00 19.88 ? 86  PRO A CG  1 
ATOM   556  C  CD  . PRO A 1 86  ? -14.703 12.322 80.290  1.00 21.99 ? 86  PRO A CD  1 
ATOM   557  N  N   . PHE A 1 87  ? -11.547 11.002 83.076  1.00 13.51 ? 87  PHE A N   1 
ATOM   558  C  CA  . PHE A 1 87  ? -10.721 11.574 84.111  1.00 13.61 ? 87  PHE A CA  1 
ATOM   559  C  C   . PHE A 1 87  ? -9.730  12.645 83.603  1.00 12.52 ? 87  PHE A C   1 
ATOM   560  O  O   . PHE A 1 87  ? -9.648  13.737 84.176  1.00 14.18 ? 87  PHE A O   1 
ATOM   561  C  CB  . PHE A 1 87  ? -9.969  10.472 84.847  1.00 14.49 ? 87  PHE A CB  1 
ATOM   562  C  CG  . PHE A 1 87  ? -9.193  10.961 86.014  1.00 13.84 ? 87  PHE A CG  1 
ATOM   563  C  CD1 . PHE A 1 87  ? -9.872  11.321 87.156  1.00 16.16 ? 87  PHE A CD1 1 
ATOM   564  C  CD2 . PHE A 1 87  ? -7.878  11.091 85.909  1.00 15.09 ? 87  PHE A CD2 1 
ATOM   565  C  CE1 . PHE A 1 87  ? -9.124  11.735 88.228  1.00 18.77 ? 87  PHE A CE1 1 
ATOM   566  C  CE2 . PHE A 1 87  ? -7.126  11.542 86.961  1.00 19.30 ? 87  PHE A CE2 1 
ATOM   567  C  CZ  . PHE A 1 87  ? -7.744  11.840 88.125  1.00 16.83 ? 87  PHE A CZ  1 
ATOM   568  N  N   . HIS A 1 88  ? -8.983  12.314 82.561  1.00 12.65 ? 88  HIS A N   1 
ATOM   569  C  CA  . HIS A 1 88  ? -7.886  13.190 82.114  1.00 12.18 ? 88  HIS A CA  1 
ATOM   570  C  C   . HIS A 1 88  ? -8.398  14.236 81.133  1.00 12.36 ? 88  HIS A C   1 
ATOM   571  O  O   . HIS A 1 88  ? -9.370  14.011 80.443  1.00 13.96 ? 88  HIS A O   1 
ATOM   572  C  CB  . HIS A 1 88  ? -6.763  12.387 81.473  1.00 13.24 ? 88  HIS A CB  1 
ATOM   573  C  CG  . HIS A 1 88  ? -6.231  11.299 82.317  1.00 13.73 ? 88  HIS A CG  1 
ATOM   574  N  ND1 . HIS A 1 88  ? -5.257  11.444 83.254  1.00 17.33 ? 88  HIS A ND1 1 
ATOM   575  C  CD2 . HIS A 1 88  ? -6.621  10.027 82.384  1.00 11.40 ? 88  HIS A CD2 1 
ATOM   576  C  CE1 . HIS A 1 88  ? -5.064  10.286 83.875  1.00 12.54 ? 88  HIS A CE1 1 
ATOM   577  N  NE2 . HIS A 1 88  ? -5.887  9.414  83.343  1.00 17.14 ? 88  HIS A NE2 1 
ATOM   578  N  N   . GLU A 1 89  ? -7.718  15.340 81.071  1.00 13.77 ? 89  GLU A N   1 
ATOM   579  C  CA  . GLU A 1 89  ? -7.967  16.381 80.094  1.00 15.14 ? 89  GLU A CA  1 
ATOM   580  C  C   . GLU A 1 89  ? -7.404  15.992 78.749  1.00 16.40 ? 89  GLU A C   1 
ATOM   581  O  O   . GLU A 1 89  ? -8.039  16.243 77.672  1.00 18.27 ? 89  GLU A O   1 
ATOM   582  C  CB  . GLU A 1 89  ? -7.346  17.722 80.487  1.00 18.59 ? 89  GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 89  ? -7.993  18.291 81.713  1.00 22.98 ? 89  GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 89  ? -9.436  18.752 81.479  1.00 25.34 ? 89  GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 89  ? -9.623  19.583 80.548  1.00 32.18 ? 89  GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 89  ? -10.279 18.208 82.215  1.00 32.95 ? 89  GLU A OE2 1 
ATOM   587  N  N   . HIS A 1 90  ? -6.294  15.292 78.731  1.00 16.90 ? 90  HIS A N   1 
ATOM   588  C  CA  . HIS A 1 90  ? -5.585  14.885 77.506  1.00 14.90 ? 90  HIS A CA  1 
ATOM   589  C  C   . HIS A 1 90  ? -4.621  13.720 77.784  1.00 17.36 ? 90  HIS A C   1 
ATOM   590  O  O   . HIS A 1 90  ? -4.421  13.368 78.939  1.00 21.17 ? 90  HIS A O   1 
ATOM   591  C  CB  . HIS A 1 90  ? -4.882  15.988 76.741  1.00 25.54 ? 90  HIS A CB  1 
ATOM   592  C  CG  . HIS A 1 90  ? -4.479  17.195 77.501  1.00 29.42 ? 90  HIS A CG  1 
ATOM   593  N  ND1 . HIS A 1 90  ? -3.280  17.271 78.159  1.00 41.64 ? 90  HIS A ND1 1 
ATOM   594  C  CD2 . HIS A 1 90  ? -5.063  18.413 77.622  1.00 40.15 ? 90  HIS A CD2 1 
ATOM   595  C  CE1 . HIS A 1 90  ? -3.173  18.455 78.723  1.00 42.50 ? 90  HIS A CE1 1 
ATOM   596  N  NE2 . HIS A 1 90  ? -4.234  19.177 78.397  1.00 48.86 ? 90  HIS A NE2 1 
ATOM   597  N  N   . ALA A 1 91  ? -4.163  13.074 76.709  1.00 19.21 ? 91  ALA A N   1 
ATOM   598  C  CA  . ALA A 1 91  ? -2.985  12.215 76.718  1.00 18.48 ? 91  ALA A CA  1 
ATOM   599  C  C   . ALA A 1 91  ? -1.885  12.896 76.031  1.00 22.73 ? 91  ALA A C   1 
ATOM   600  O  O   . ALA A 1 91  ? -2.118  13.620 75.123  1.00 20.13 ? 91  ALA A O   1 
ATOM   601  C  CB  . ALA A 1 91  ? -3.268  10.883 76.076  1.00 20.46 ? 91  ALA A CB  1 
ATOM   602  N  N   . GLU A 1 92  ? -0.655  12.635 76.420  1.00 22.21 ? 92  GLU A N   1 
ATOM   603  C  CA  . GLU A 1 92  ? 0.435   13.432 75.869  1.00 20.21 ? 92  GLU A CA  1 
ATOM   604  C  C   . GLU A 1 92  ? 1.788   12.769 75.841  1.00 21.68 ? 92  GLU A C   1 
ATOM   605  O  O   . GLU A 1 92  ? 2.024   11.784 76.538  1.00 18.78 ? 92  GLU A O   1 
ATOM   606  C  CB  . GLU A 1 92  ? 0.529   14.702 76.693  0.50 14.02 ? 92  GLU A CB  1 
ATOM   607  C  CG  . GLU A 1 92  ? 0.983   14.386 78.180  0.50 18.37 ? 92  GLU A CG  1 
ATOM   608  C  CD  . GLU A 1 92  ? 2.447   14.237 78.359  0.50 17.31 ? 92  GLU A CD  1 
ATOM   609  O  OE1 . GLU A 1 92  ? 2.952   13.413 79.230  0.50 15.04 ? 92  GLU A OE1 1 
ATOM   610  O  OE2 . GLU A 1 92  ? 3.145   15.012 77.707  0.50 20.17 ? 92  GLU A OE2 1 
ATOM   611  N  N   . VAL A 1 93  ? 2.685   13.381 75.095  1.00 17.86 ? 93  VAL A N   1 
ATOM   612  C  CA  . VAL A 1 93  ? 4.040   13.169 75.163  1.00 15.86 ? 93  VAL A CA  1 
ATOM   613  C  C   . VAL A 1 93  ? 4.692   14.500 74.969  1.00 12.78 ? 93  VAL A C   1 
ATOM   614  O  O   . VAL A 1 93  ? 4.367   15.283 74.074  1.00 13.04 ? 93  VAL A O   1 
ATOM   615  C  CB  . VAL A 1 93  ? 4.617   12.119 74.092  1.00 18.74 ? 93  VAL A CB  1 
ATOM   616  C  CG1 . VAL A 1 93  ? 4.100   10.781 74.231  1.00 23.78 ? 93  VAL A CG1 1 
ATOM   617  C  CG2 . VAL A 1 93  ? 4.392   12.606 72.700  1.00 23.41 ? 93  VAL A CG2 1 
ATOM   618  N  N   . VAL A 1 94  ? 5.732   14.652 75.740  1.00 12.23 ? 94  VAL A N   1 
ATOM   619  C  CA  . VAL A 1 94  ? 6.685   15.766 75.529  1.00 9.60  ? 94  VAL A CA  1 
ATOM   620  C  C   . VAL A 1 94  ? 8.069   15.136 75.329  1.00 9.71  ? 94  VAL A C   1 
ATOM   621  O  O   . VAL A 1 94  ? 8.462   14.302 76.164  1.00 11.25 ? 94  VAL A O   1 
ATOM   622  C  CB  . VAL A 1 94  ? 6.687   16.683 76.766  1.00 12.05 ? 94  VAL A CB  1 
ATOM   623  C  CG1 . VAL A 1 94  ? 7.678   17.816 76.500  1.00 14.31 ? 94  VAL A CG1 1 
ATOM   624  C  CG2 . VAL A 1 94  ? 5.313   17.282 77.007  1.00 15.61 ? 94  VAL A CG2 1 
ATOM   625  N  N   . PHE A 1 95  ? 8.748   15.500 74.261  1.00 10.21 ? 95  PHE A N   1 
ATOM   626  C  CA  . PHE A 1 95  ? 9.997   14.869 73.893  1.00 10.77 ? 95  PHE A CA  1 
ATOM   627  C  C   . PHE A 1 95  ? 10.866  15.810 73.080  1.00 10.17 ? 95  PHE A C   1 
ATOM   628  O  O   . PHE A 1 95  ? 10.389  16.650 72.354  1.00 11.83 ? 95  PHE A O   1 
ATOM   629  C  CB  . PHE A 1 95  ? 9.774   13.543 73.117  1.00 11.69 ? 95  PHE A CB  1 
ATOM   630  C  CG  . PHE A 1 95  ? 9.094   13.756 71.786  1.00 12.09 ? 95  PHE A CG  1 
ATOM   631  C  CD1 . PHE A 1 95  ? 7.747   13.942 71.689  1.00 13.91 ? 95  PHE A CD1 1 
ATOM   632  C  CD2 . PHE A 1 95  ? 9.828   13.707 70.631  1.00 12.61 ? 95  PHE A CD2 1 
ATOM   633  C  CE1 . PHE A 1 95  ? 7.121   14.076 70.389  1.00 17.21 ? 95  PHE A CE1 1 
ATOM   634  C  CE2 . PHE A 1 95  ? 9.267   13.799 69.410  1.00 14.89 ? 95  PHE A CE2 1 
ATOM   635  C  CZ  . PHE A 1 95  ? 7.919   13.995 69.319  1.00 16.07 ? 95  PHE A CZ  1 
ATOM   636  N  N   . THR A 1 96  ? 12.162  15.608 73.173  1.00 11.20 ? 96  THR A N   1 
ATOM   637  C  CA  . THR A 1 96  ? 13.115  16.268 72.278  1.00 11.93 ? 96  THR A CA  1 
ATOM   638  C  C   . THR A 1 96  ? 13.231  15.479 70.998  1.00 12.28 ? 96  THR A C   1 
ATOM   639  O  O   . THR A 1 96  ? 13.469  14.285 71.022  1.00 13.62 ? 96  THR A O   1 
ATOM   640  C  CB  . THR A 1 96  ? 14.493  16.395 72.942  1.00 13.58 ? 96  THR A CB  1 
ATOM   641  O  OG1 . THR A 1 96  ? 14.372  17.161 74.162  1.00 15.30 ? 96  THR A OG1 1 
ATOM   642  C  CG2 . THR A 1 96  ? 15.482  17.021 72.029  1.00 16.08 ? 96  THR A CG2 1 
ATOM   643  N  N   . ALA A 1 97  ? 13.056  16.130 69.886  1.00 11.29 ? 97  ALA A N   1 
ATOM   644  C  CA  . ALA A 1 97  ? 13.058  15.494 68.582  1.00 11.10 ? 97  ALA A CA  1 
ATOM   645  C  C   . ALA A 1 97  ? 14.292  15.867 67.755  1.00 11.46 ? 97  ALA A C   1 
ATOM   646  O  O   . ALA A 1 97  ? 14.747  17.006 67.803  1.00 11.35 ? 97  ALA A O   1 
ATOM   647  C  CB  . ALA A 1 97  ? 11.850  15.901 67.760  1.00 13.24 ? 97  ALA A CB  1 
ATOM   648  N  N   . ASN A 1 98  ? 14.798  14.930 67.021  1.00 10.73 ? 98  ASN A N   1 
ATOM   649  C  CA  . ASN A 1 98  ? 15.828  15.170 65.962  1.00 11.28 ? 98  ASN A CA  1 
ATOM   650  C  C   . ASN A 1 98  ? 17.178  15.625 66.469  1.00 12.56 ? 98  ASN A C   1 
ATOM   651  O  O   . ASN A 1 98  ? 17.955  16.166 65.723  1.00 12.47 ? 98  ASN A O   1 
ATOM   652  C  CB  . ASN A 1 98  ? 15.300  16.126 64.856  1.00 12.15 ? 98  ASN A CB  1 
ATOM   653  C  CG  . ASN A 1 98  ? 13.950  15.742 64.346  1.00 12.06 ? 98  ASN A CG  1 
ATOM   654  O  OD1 . ASN A 1 98  ? 12.981  16.569 64.374  1.00 14.75 ? 98  ASN A OD1 1 
ATOM   655  N  ND2 . ASN A 1 98  ? 13.788  14.555 63.939  1.00 10.60 ? 98  ASN A ND2 1 
ATOM   656  N  N   . ASP A 1 99  ? 17.490  15.371 67.736  1.00 13.11 ? 99  ASP A N   1 
ATOM   657  C  CA  . ASP A 1 99  ? 18.749  15.912 68.339  1.00 13.73 ? 99  ASP A CA  1 
ATOM   658  C  C   . ASP A 1 99  ? 19.995  15.290 67.694  1.00 14.05 ? 99  ASP A C   1 
ATOM   659  O  O   . ASP A 1 99  ? 21.008  15.968 67.631  1.00 15.92 ? 99  ASP A O   1 
ATOM   660  C  CB  . ASP A 1 99  ? 18.723  15.787 69.868  1.00 16.84 ? 99  ASP A CB  1 
ATOM   661  C  CG  . ASP A 1 99  ? 19.500  16.916 70.543  1.00 22.25 ? 99  ASP A CG  1 
ATOM   662  O  OD1 . ASP A 1 99  ? 20.244  17.636 69.841  1.00 20.93 ? 99  ASP A OD1 1 
ATOM   663  O  OD2 . ASP A 1 99  ? 19.350  17.088 71.759  1.00 26.83 ? 99  ASP A OD2 1 
ATOM   664  N  N   . SER A 1 100 ? 19.897  14.056 67.248  1.00 15.88 ? 100 SER A N   1 
ATOM   665  C  CA  . SER A 1 100 ? 20.999  13.345 66.575  1.00 19.06 ? 100 SER A CA  1 
ATOM   666  C  C   . SER A 1 100 ? 20.680  13.193 65.101  1.00 20.16 ? 100 SER A C   1 
ATOM   667  O  O   . SER A 1 100 ? 21.104  12.259 64.420  1.00 23.74 ? 100 SER A O   1 
ATOM   668  C  CB  . SER A 1 100 ? 21.266  11.974 67.214  1.00 22.46 ? 100 SER A CB  1 
ATOM   669  O  OG  . SER A 1 100 ? 21.795  12.213 68.466  1.00 28.48 ? 100 SER A OG  1 
ATOM   670  N  N   . GLY A 1 101 ? 19.972  14.173 64.527  1.00 18.18 ? 101 GLY A N   1 
ATOM   671  C  CA  . GLY A 1 101 ? 19.563  14.132 63.163  1.00 17.83 ? 101 GLY A CA  1 
ATOM   672  C  C   . GLY A 1 101 ? 18.106  13.715 63.048  1.00 15.69 ? 101 GLY A C   1 
ATOM   673  O  O   . GLY A 1 101 ? 17.472  13.254 64.005  1.00 15.15 ? 101 GLY A O   1 
ATOM   674  N  N   . PRO A 1 102 ? 17.575  13.847 61.820  1.00 15.62 ? 102 PRO A N   1 
ATOM   675  C  CA  . PRO A 1 102 ? 16.162  13.579 61.618  1.00 13.88 ? 102 PRO A CA  1 
ATOM   676  C  C   . PRO A 1 102 ? 15.827  12.131 61.928  1.00 15.32 ? 102 PRO A C   1 
ATOM   677  O  O   . PRO A 1 102 ? 16.560  11.215 61.601  1.00 14.80 ? 102 PRO A O   1 
ATOM   678  C  CB  . PRO A 1 102 ? 15.968  13.793 60.141  1.00 17.51 ? 102 PRO A CB  1 
ATOM   679  C  CG  . PRO A 1 102 ? 17.008  14.807 59.727  1.00 18.95 ? 102 PRO A CG  1 
ATOM   680  C  CD  . PRO A 1 102 ? 18.190  14.456 60.599  1.00 18.28 ? 102 PRO A CD  1 
ATOM   681  N  N   . ARG A 1 103 ? 14.696  11.915 62.555  1.00 13.92 ? 103 ARG A N   1 
ATOM   682  C  CA  . ARG A 1 103 ? 14.093  10.629 62.795  1.00 13.69 ? 103 ARG A CA  1 
ATOM   683  C  C   . ARG A 1 103 ? 12.628  10.684 62.450  1.00 14.54 ? 103 ARG A C   1 
ATOM   684  O  O   . ARG A 1 103 ? 12.046  11.754 62.415  1.00 14.92 ? 103 ARG A O   1 
ATOM   685  C  CB  . ARG A 1 103 ? 14.246  10.190 64.256  1.00 15.00 ? 103 ARG A CB  1 
ATOM   686  C  CG  . ARG A 1 103 ? 15.667  10.067 64.762  1.00 15.35 ? 103 ARG A CG  1 
ATOM   687  C  CD  . ARG A 1 103 ? 16.395  8.918  64.090  1.00 16.90 ? 103 ARG A CD  1 
ATOM   688  N  NE  . ARG A 1 103 ? 17.716  8.718  64.697  1.00 20.84 ? 103 ARG A NE  1 
ATOM   689  C  CZ  . ARG A 1 103 ? 18.813  9.370  64.351  1.00 21.89 ? 103 ARG A CZ  1 
ATOM   690  N  NH1 . ARG A 1 103 ? 18.799  10.211 63.331  1.00 20.64 ? 103 ARG A NH1 1 
ATOM   691  N  NH2 . ARG A 1 103 ? 19.946  9.135  65.003  1.00 23.40 ? 103 ARG A NH2 1 
ATOM   692  N  N   . ARG A 1 104 ? 12.014  9.527  62.262  1.00 13.11 ? 104 ARG A N   1 
ATOM   693  C  CA  . ARG A 1 104 ? 10.585  9.383  62.136  1.00 15.33 ? 104 ARG A CA  1 
ATOM   694  C  C   . ARG A 1 104 ? 10.020  8.909  63.469  1.00 11.74 ? 104 ARG A C   1 
ATOM   695  O  O   . ARG A 1 104 ? 10.510  7.953  64.004  1.00 14.79 ? 104 ARG A O   1 
ATOM   696  C  CB  . ARG A 1 104 ? 10.250  8.412  61.034  1.00 17.51 ? 104 ARG A CB  1 
ATOM   697  N  N   . TYR A 1 105 ? 8.983   9.548  63.915  1.00 11.99 ? 105 TYR A N   1 
ATOM   698  C  CA  . TYR A 1 105 ? 8.354   9.310  65.200  1.00 10.98 ? 105 TYR A CA  1 
ATOM   699  C  C   . TYR A 1 105 ? 6.922   8.889  65.010  1.00 11.57 ? 105 TYR A C   1 
ATOM   700  O  O   . TYR A 1 105 ? 6.136   9.567  64.386  1.00 13.79 ? 105 TYR A O   1 
ATOM   701  C  CB  . TYR A 1 105 ? 8.361   10.606 66.076  1.00 11.76 ? 105 TYR A CB  1 
ATOM   702  C  CG  . TYR A 1 105 ? 9.751   11.103 66.406  1.00 11.62 ? 105 TYR A CG  1 
ATOM   703  C  CD1 . TYR A 1 105 ? 10.420  11.915 65.546  1.00 12.14 ? 105 TYR A CD1 1 
ATOM   704  C  CD2 . TYR A 1 105 ? 10.397  10.684 67.547  1.00 12.22 ? 105 TYR A CD2 1 
ATOM   705  C  CE1 . TYR A 1 105 ? 11.699  12.315 65.793  1.00 12.34 ? 105 TYR A CE1 1 
ATOM   706  C  CE2 . TYR A 1 105 ? 11.661  11.139 67.829  1.00 12.79 ? 105 TYR A CE2 1 
ATOM   707  C  CZ  . TYR A 1 105 ? 12.307  11.946 66.961  1.00 11.72 ? 105 TYR A CZ  1 
ATOM   708  O  OH  . TYR A 1 105 ? 13.608  12.332 67.187  1.00 14.02 ? 105 TYR A OH  1 
ATOM   709  N  N   . THR A 1 106 ? 6.551   7.757  65.598  1.00 10.69 ? 106 THR A N   1 
ATOM   710  C  CA  . THR A 1 106 ? 5.156   7.382  65.751  1.00 10.92 ? 106 THR A CA  1 
ATOM   711  C  C   . THR A 1 106 ? 4.804   7.393  67.206  1.00 10.79 ? 106 THR A C   1 
ATOM   712  O  O   . THR A 1 106 ? 5.489   6.751  68.027  1.00 12.39 ? 106 THR A O   1 
ATOM   713  C  CB  . THR A 1 106 ? 4.875   5.998  65.178  1.00 12.98 ? 106 THR A CB  1 
ATOM   714  O  OG1 . THR A 1 106 ? 5.115   5.974  63.786  1.00 17.46 ? 106 THR A OG1 1 
ATOM   715  C  CG2 . THR A 1 106 ? 3.432   5.581  65.379  1.00 17.50 ? 106 THR A CG2 1 
ATOM   716  N  N   . ILE A 1 107 ? 3.801   8.168  67.590  1.00 11.20 ? 107 ILE A N   1 
ATOM   717  C  CA  . ILE A 1 107 ? 3.305   8.252  68.924  1.00 11.03 ? 107 ILE A CA  1 
ATOM   718  C  C   . ILE A 1 107 ? 2.020   7.442  68.982  1.00 11.80 ? 107 ILE A C   1 
ATOM   719  O  O   . ILE A 1 107 ? 1.071   7.786  68.281  1.00 13.31 ? 107 ILE A O   1 
ATOM   720  C  CB  . ILE A 1 107 ? 3.021   9.682  69.373  1.00 13.95 ? 107 ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 107 ? 4.259   10.595 69.190  1.00 15.82 ? 107 ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 107 ? 2.500   9.711  70.796  1.00 16.78 ? 107 ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 107 ? 5.490   10.106 69.928  1.00 15.98 ? 107 ILE A CD1 1 
ATOM   724  N  N   . ALA A 1 108 ? 2.029   6.324  69.693  1.00 12.07 ? 108 ALA A N   1 
ATOM   725  C  CA  . ALA A 1 108 ? 0.860   5.431  69.827  1.00 13.79 ? 108 ALA A CA  1 
ATOM   726  C  C   . ALA A 1 108 ? 0.277   5.606  71.198  1.00 14.77 ? 108 ALA A C   1 
ATOM   727  O  O   . ALA A 1 108 ? 0.961   5.428  72.179  1.00 19.68 ? 108 ALA A O   1 
ATOM   728  C  CB  . ALA A 1 108 ? 1.289   3.972  69.616  1.00 16.72 ? 108 ALA A CB  1 
ATOM   729  N  N   . ALA A 1 109 ? -1.027  5.890  71.254  1.00 13.09 ? 109 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 109 ? -1.730  6.074  72.537  1.00 11.59 ? 109 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 109 ? -2.881  5.080  72.680  1.00 11.31 ? 109 ALA A C   1 
ATOM   732  O  O   . ALA A 1 109 ? -3.570  4.795  71.711  1.00 14.20 ? 109 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 109 ? -2.273  7.485  72.602  1.00 13.31 ? 109 ALA A CB  1 
ATOM   734  N  N   . LEU A 1 110 ? -3.069  4.556  73.852  1.00 9.43  ? 110 LEU A N   1 
ATOM   735  C  CA  . LEU A 1 110 ? -4.129  3.601  74.197  1.00 10.20 ? 110 LEU A CA  1 
ATOM   736  C  C   . LEU A 1 110 ? -4.986  4.223  75.285  1.00 9.39  ? 110 LEU A C   1 
ATOM   737  O  O   . LEU A 1 110 ? -4.447  4.595  76.332  1.00 10.51 ? 110 LEU A O   1 
ATOM   738  C  CB  . LEU A 1 110 ? -3.501  2.308  74.678  1.00 11.48 ? 110 LEU A CB  1 
ATOM   739  C  CG  . LEU A 1 110 ? -4.464  1.193  75.057  1.00 13.19 ? 110 LEU A CG  1 
ATOM   740  C  CD1 . LEU A 1 110 ? -5.307  0.766  73.869  1.00 13.54 ? 110 LEU A CD1 1 
ATOM   741  C  CD2 . LEU A 1 110 ? -3.732  -0.009 75.588  1.00 16.73 ? 110 LEU A CD2 1 
ATOM   742  N  N   . LEU A 1 111 ? -6.280  4.368  75.045  1.00 9.85  ? 111 LEU A N   1 
ATOM   743  C  CA  . LEU A 1 111 ? -7.155  5.145  75.914  1.00 10.58 ? 111 LEU A CA  1 
ATOM   744  C  C   . LEU A 1 111 ? -8.190  4.321  76.681  1.00 10.29 ? 111 LEU A C   1 
ATOM   745  O  O   . LEU A 1 111 ? -8.863  3.505  76.088  1.00 10.13 ? 111 LEU A O   1 
ATOM   746  C  CB  . LEU A 1 111 ? -7.927  6.188  75.104  1.00 11.03 ? 111 LEU A CB  1 
ATOM   747  C  CG  . LEU A 1 111 ? -7.116  7.049  74.139  1.00 11.54 ? 111 LEU A CG  1 
ATOM   748  C  CD1 . LEU A 1 111 ? -8.085  7.974  73.493  1.00 14.10 ? 111 LEU A CD1 1 
ATOM   749  C  CD2 . LEU A 1 111 ? -5.942  7.744  74.881  1.00 12.59 ? 111 LEU A CD2 1 
ATOM   750  N  N   . SER A 1 112 ? -8.333  4.642  77.964  1.00 10.35 ? 112 SER A N   1 
ATOM   751  C  CA  . SER A 1 112 ? -9.441  4.213  78.794  1.00 11.08 ? 112 SER A CA  1 
ATOM   752  C  C   . SER A 1 112 ? -9.942  5.463  79.546  1.00 10.21 ? 112 SER A C   1 
ATOM   753  O  O   . SER A 1 112 ? -9.295  6.449  79.654  1.00 11.15 ? 112 SER A O   1 
ATOM   754  C  CB  . SER A 1 112 ? -9.006  3.141  79.772  1.00 11.51 ? 112 SER A CB  1 
ATOM   755  O  OG  . SER A 1 112 ? -8.451  2.046  79.126  1.00 15.32 ? 112 SER A OG  1 
ATOM   756  N  N   . PRO A 1 113 ? -11.164 5.342  80.085  1.00 10.11 ? 113 PRO A N   1 
ATOM   757  C  CA  . PRO A 1 113 ? -11.707 6.571  80.716  1.00 11.15 ? 113 PRO A CA  1 
ATOM   758  C  C   . PRO A 1 113 ? -10.884 7.116  81.853  1.00 11.74 ? 113 PRO A C   1 
ATOM   759  O  O   . PRO A 1 113 ? -10.887 8.308  82.076  1.00 11.84 ? 113 PRO A O   1 
ATOM   760  C  CB  . PRO A 1 113 ? -13.108 6.133  81.150  1.00 12.62 ? 113 PRO A CB  1 
ATOM   761  C  CG  . PRO A 1 113 ? -13.505 5.143  80.112  1.00 14.19 ? 113 PRO A CG  1 
ATOM   762  C  CD  . PRO A 1 113 ? -12.231 4.376  79.804  1.00 12.28 ? 113 PRO A CD  1 
ATOM   763  N  N   . TYR A 1 114 ? -10.199 6.250  82.606  1.00 9.99  ? 114 TYR A N   1 
ATOM   764  C  CA  . TYR A 1 114 ? -9.387  6.685  83.764  1.00 10.06 ? 114 TYR A CA  1 
ATOM   765  C  C   . TYR A 1 114 ? -7.905  6.398  83.596  1.00 10.37 ? 114 TYR A C   1 
ATOM   766  O  O   . TYR A 1 114 ? -7.151  6.449  84.551  1.00 12.15 ? 114 TYR A O   1 
ATOM   767  C  CB  . TYR A 1 114 ? -9.897  6.104  85.118  1.00 11.01 ? 114 TYR A CB  1 
ATOM   768  C  CG  . TYR A 1 114 ? -11.079 6.794  85.646  1.00 11.01 ? 114 TYR A CG  1 
ATOM   769  C  CD1 . TYR A 1 114 ? -12.322 6.659  85.110  1.00 15.62 ? 114 TYR A CD1 1 
ATOM   770  C  CD2 . TYR A 1 114 ? -10.969 7.593  86.730  1.00 12.44 ? 114 TYR A CD2 1 
ATOM   771  C  CE1 . TYR A 1 114 ? -13.443 7.260  85.596  1.00 22.75 ? 114 TYR A CE1 1 
ATOM   772  C  CE2 . TYR A 1 114 ? -12.065 8.207  87.292  1.00 16.49 ? 114 TYR A CE2 1 
ATOM   773  C  CZ  . TYR A 1 114 ? -13.310 8.036  86.721  1.00 18.82 ? 114 TYR A CZ  1 
ATOM   774  O  OH  . TYR A 1 114 ? -14.400 8.661  87.287  1.00 27.49 ? 114 TYR A OH  1 
ATOM   775  N  N   . SER A 1 115 ? -7.463  6.114  82.341  1.00 10.40 ? 115 SER A N   1 
ATOM   776  C  CA  . SER A 1 115 ? -6.087  5.713  82.118  1.00 10.38 ? 115 SER A CA  1 
ATOM   777  C  C   . SER A 1 115 ? -5.681  5.946  80.712  1.00 9.94  ? 115 SER A C   1 
ATOM   778  O  O   . SER A 1 115 ? -6.469  5.876  79.800  1.00 12.23 ? 115 SER A O   1 
ATOM   779  C  CB  . SER A 1 115 ? -5.923  4.269  82.507  1.00 11.65 ? 115 SER A CB  1 
ATOM   780  O  OG  . SER A 1 115 ? -4.641  3.742  82.374  1.00 15.15 ? 115 SER A OG  1 
ATOM   781  N  N   . TYR A 1 116 ? -4.386  6.156  80.525  1.00 9.75  ? 116 TYR A N   1 
ATOM   782  C  CA  . TYR A 1 116 ? -3.857  6.149  79.144  1.00 9.42  ? 116 TYR A CA  1 
ATOM   783  C  C   . TYR A 1 116 ? -2.420  5.658  79.220  1.00 9.30  ? 116 TYR A C   1 
ATOM   784  O  O   . TYR A 1 116 ? -1.736  5.758  80.218  1.00 9.79  ? 116 TYR A O   1 
ATOM   785  C  CB  . TYR A 1 116 ? -3.949  7.487  78.400  1.00 9.91  ? 116 TYR A CB  1 
ATOM   786  C  CG  . TYR A 1 116 ? -3.127  8.594  79.000  1.00 12.09 ? 116 TYR A CG  1 
ATOM   787  C  CD1 . TYR A 1 116 ? -1.810  8.799  78.635  1.00 13.73 ? 116 TYR A CD1 1 
ATOM   788  C  CD2 . TYR A 1 116 ? -3.680  9.431  79.949  1.00 15.05 ? 116 TYR A CD2 1 
ATOM   789  C  CE1 . TYR A 1 116 ? -1.064  9.822  79.195  1.00 13.94 ? 116 TYR A CE1 1 
ATOM   790  C  CE2 . TYR A 1 116 ? -2.950  10.457 80.519  1.00 17.19 ? 116 TYR A CE2 1 
ATOM   791  C  CZ  . TYR A 1 116 ? -1.637  10.652 80.140  1.00 13.95 ? 116 TYR A CZ  1 
ATOM   792  O  OH  . TYR A 1 116 ? -0.913  11.655 80.715  1.00 17.72 ? 116 TYR A OH  1 
ATOM   793  N  N   . SER A 1 117 ? -2.019  5.122  78.097  1.00 9.96  ? 117 SER A N   1 
ATOM   794  C  CA  A SER A 1 117 ? -0.607  4.856  77.881  0.50 11.88 ? 117 SER A CA  1 
ATOM   795  C  CA  B SER A 1 117 ? -0.646  4.701  77.831  0.50 11.91 ? 117 SER A CA  1 
ATOM   796  C  C   . SER A 1 117 ? -0.135  5.336  76.537  1.00 12.76 ? 117 SER A C   1 
ATOM   797  O  O   . SER A 1 117 ? -0.923  5.495  75.579  1.00 15.45 ? 117 SER A O   1 
ATOM   798  C  CB  A SER A 1 117 ? -0.345  3.378  77.991  0.50 17.08 ? 117 SER A CB  1 
ATOM   799  C  CB  B SER A 1 117 ? -0.667  3.147  77.733  0.50 17.73 ? 117 SER A CB  1 
ATOM   800  O  OG  A SER A 1 117 ? -0.577  2.842  76.724  0.50 16.78 ? 117 SER A OG  1 
ATOM   801  O  OG  B SER A 1 117 ? 0.632   2.553  77.705  0.50 18.71 ? 117 SER A OG  1 
ATOM   802  N  N   . THR A 1 118 ? 1.124   5.680  76.505  1.00 14.31 ? 118 THR A N   1 
ATOM   803  C  CA  . THR A 1 118 ? 1.694   6.113  75.221  1.00 16.50 ? 118 THR A CA  1 
ATOM   804  C  C   . THR A 1 118 ? 3.043   5.437  75.060  1.00 18.30 ? 118 THR A C   1 
ATOM   805  O  O   . THR A 1 118 ? 3.740   5.194  76.030  1.00 17.56 ? 118 THR A O   1 
ATOM   806  C  CB  . THR A 1 118 ? 1.781   7.636  75.121  1.00 19.78 ? 118 THR A CB  1 
ATOM   807  O  OG1 . THR A 1 118 ? 2.232   7.970  73.813  1.00 27.49 ? 118 THR A OG1 1 
ATOM   808  C  CG2 . THR A 1 118 ? 2.689   8.262  76.158  1.00 21.48 ? 118 THR A CG2 1 
ATOM   809  N  N   . THR A 1 119 ? 3.327   5.147  73.811  1.00 14.79 ? 119 THR A N   1 
ATOM   810  C  CA  A THR A 1 119 ? 4.639   4.728  73.364  0.50 11.59 ? 119 THR A CA  1 
ATOM   811  C  CA  B THR A 1 119 ? 4.660   4.659  73.374  0.50 11.85 ? 119 THR A CA  1 
ATOM   812  C  C   . THR A 1 119 ? 5.151   5.442  72.135  1.00 10.77 ? 119 THR A C   1 
ATOM   813  O  O   . THR A 1 119 ? 4.339   5.945  71.391  1.00 13.82 ? 119 THR A O   1 
ATOM   814  C  CB  A THR A 1 119 ? 4.574   3.226  73.187  0.50 16.00 ? 119 THR A CB  1 
ATOM   815  C  CB  B THR A 1 119 ? 4.841   3.060  73.190  0.50 16.83 ? 119 THR A CB  1 
ATOM   816  O  OG1 A THR A 1 119 ? 3.650   2.871  74.217  0.50 16.39 ? 119 THR A OG1 1 
ATOM   817  O  OG1 B THR A 1 119 ? 6.252   2.720  73.328  0.50 17.97 ? 119 THR A OG1 1 
ATOM   818  C  CG2 A THR A 1 119 ? 6.059   2.611  73.384  0.50 14.52 ? 119 THR A CG2 1 
ATOM   819  C  CG2 B THR A 1 119 ? 4.335   2.573  71.906  0.50 13.71 ? 119 THR A CG2 1 
ATOM   820  N  N   . ALA A 1 120 ? 6.463   5.555  72.025  1.00 12.02 ? 120 ALA A N   1 
ATOM   821  C  CA  . ALA A 1 120 ? 7.085   6.125  70.852  1.00 11.20 ? 120 ALA A CA  1 
ATOM   822  C  C   . ALA A 1 120 ? 7.816   5.041  70.123  1.00 11.24 ? 120 ALA A C   1 
ATOM   823  O  O   . ALA A 1 120 ? 8.547   4.231  70.707  1.00 13.63 ? 120 ALA A O   1 
ATOM   824  C  CB  . ALA A 1 120 ? 8.040   7.227  71.254  1.00 14.27 ? 120 ALA A CB  1 
ATOM   825  N  N   . VAL A 1 121 ? 7.661   5.035  68.805  1.00 11.00 ? 121 VAL A N   1 
ATOM   826  C  CA  . VAL A 1 121 ? 8.458   4.233  67.898  1.00 12.17 ? 121 VAL A CA  1 
ATOM   827  C  C   . VAL A 1 121 ? 9.270   5.161  67.063  1.00 12.31 ? 121 VAL A C   1 
ATOM   828  O  O   . VAL A 1 121 ? 8.726   5.999  66.368  1.00 13.39 ? 121 VAL A O   1 
ATOM   829  C  CB  . VAL A 1 121 ? 7.544   3.374  66.987  1.00 15.01 ? 121 VAL A CB  1 
ATOM   830  C  CG1 . VAL A 1 121 ? 8.422   2.501  66.116  1.00 19.03 ? 121 VAL A CG1 1 
ATOM   831  C  CG2 . VAL A 1 121 ? 6.533   2.644  67.799  1.00 21.06 ? 121 VAL A CG2 1 
ATOM   832  N  N   . VAL A 1 122 ? 10.586  5.088  67.170  1.00 12.20 ? 122 VAL A N   1 
ATOM   833  C  CA  . VAL A 1 122 ? 11.507  6.063  66.550  1.00 13.57 ? 122 VAL A CA  1 
ATOM   834  C  C   . VAL A 1 122 ? 12.370  5.288  65.574  1.00 13.78 ? 122 VAL A C   1 
ATOM   835  O  O   . VAL A 1 122 ? 13.046  4.353  65.948  1.00 15.30 ? 122 VAL A O   1 
ATOM   836  C  CB  . VAL A 1 122 ? 12.365  6.756  67.635  1.00 14.23 ? 122 VAL A CB  1 
ATOM   837  C  CG1 . VAL A 1 122 ? 13.253  7.841  67.011  1.00 15.68 ? 122 VAL A CG1 1 
ATOM   838  C  CG2 . VAL A 1 122 ? 11.498  7.415  68.707  1.00 14.58 ? 122 VAL A CG2 1 
ATOM   839  N  N   . THR A 1 123 ? 12.343  5.659  64.307  1.00 13.65 ? 123 THR A N   1 
ATOM   840  C  CA  . THR A 1 123 ? 13.138  5.071  63.293  1.00 15.89 ? 123 THR A CA  1 
ATOM   841  C  C   . THR A 1 123 ? 14.009  6.038  62.564  1.00 15.60 ? 123 THR A C   1 
ATOM   842  O  O   . THR A 1 123 ? 13.734  7.213  62.471  1.00 16.94 ? 123 THR A O   1 
ATOM   843  C  CB  . THR A 1 123 ? 12.284  4.316  62.327  1.00 21.78 ? 123 THR A CB  1 
ATOM   844  O  OG1 . THR A 1 123 ? 11.420  5.222  61.624  1.00 28.35 ? 123 THR A OG1 1 
ATOM   845  C  CG2 . THR A 1 123 ? 11.389  3.339  63.055  1.00 25.42 ? 123 THR A CG2 1 
ATOM   846  N  N   . ASN A 1 124 ? 15.067  5.572  61.947  1.00 20.90 ? 124 ASN A N   1 
ATOM   847  C  CA  . ASN A 1 124 ? 16.043  6.459  61.297  1.00 21.41 ? 124 ASN A CA  1 
ATOM   848  C  C   . ASN A 1 124 ? 15.833  6.287  59.822  1.00 31.80 ? 124 ASN A C   1 
ATOM   849  O  O   . ASN A 1 124 ? 16.066  5.224  59.308  1.00 40.43 ? 124 ASN A O   1 
ATOM   850  C  CB  . ASN A 1 124 ? 17.481  6.077  61.698  1.00 26.15 ? 124 ASN A CB  1 
ATOM   851  C  CG  . ASN A 1 124 ? 18.507  7.100  61.250  1.00 26.65 ? 124 ASN A CG  1 
ATOM   852  O  OD1 . ASN A 1 124 ? 18.316  7.911  60.282  1.00 33.22 ? 124 ASN A OD1 1 
ATOM   853  N  ND2 . ASN A 1 124 ? 19.671  6.986  61.860  1.00 37.38 ? 124 ASN A ND2 1 
ATOM   854  N  N   . PRO A 1 125 ? 15.411  7.378  59.129  1.00 34.27 ? 125 PRO A N   1 
ATOM   855  C  CA  . PRO A 1 125 ? 15.034  7.311  57.718  1.00 41.00 ? 125 PRO A CA  1 
ATOM   856  C  CB  . PRO A 1 125 ? 14.428  8.691  57.488  1.00 29.85 ? 125 PRO A CB  1 
ATOM   857  C  CG  . PRO A 1 125 ? 15.206  9.547  58.398  1.00 29.29 ? 125 PRO A CG  1 
ATOM   858  C  CD  . PRO A 1 125 ? 15.507  8.768  59.596  1.00 27.70 ? 125 PRO A CD  1 
ATOM   859  N  N   . PRO B 1 11  ? -5.531  13.453 100.366 1.00 23.18 ? 11  PRO B N   1 
ATOM   860  C  CA  . PRO B 1 11  ? -6.419  13.545 99.212  1.00 21.43 ? 11  PRO B CA  1 
ATOM   861  C  C   . PRO B 1 11  ? -5.737  13.209 97.918  1.00 19.07 ? 11  PRO B C   1 
ATOM   862  O  O   . PRO B 1 11  ? -6.423  12.854 97.034  1.00 21.97 ? 11  PRO B O   1 
ATOM   863  C  CB  . PRO B 1 11  ? -6.891  15.006 99.179  1.00 32.97 ? 11  PRO B CB  1 
ATOM   864  C  CG  . PRO B 1 11  ? -5.868  15.735 99.970  1.00 42.47 ? 11  PRO B CG  1 
ATOM   865  C  CD  . PRO B 1 11  ? -5.397  14.750 101.020 1.00 34.01 ? 11  PRO B CD  1 
ATOM   866  N  N   . LEU B 1 12  ? -4.420  13.412 97.811  1.00 18.03 ? 12  LEU B N   1 
ATOM   867  C  CA  . LEU B 1 12  ? -3.690  13.180 96.570  1.00 17.15 ? 12  LEU B CA  1 
ATOM   868  C  C   . LEU B 1 12  ? -2.406  12.461 96.850  1.00 18.04 ? 12  LEU B C   1 
ATOM   869  O  O   . LEU B 1 12  ? -1.565  12.963 97.558  1.00 21.85 ? 12  LEU B O   1 
ATOM   870  C  CB  . LEU B 1 12  ? -3.395  14.515 95.851  1.00 17.35 ? 12  LEU B CB  1 
ATOM   871  C  CG  . LEU B 1 12  ? -2.623  14.439 94.539  1.00 17.89 ? 12  LEU B CG  1 
ATOM   872  C  CD1 . LEU B 1 12  ? -3.398  13.702 93.512  1.00 21.86 ? 12  LEU B CD1 1 
ATOM   873  C  CD2 . LEU B 1 12  ? -2.294  15.821 93.968  1.00 21.76 ? 12  LEU B CD2 1 
ATOM   874  N  N   . MET B 1 13  ? -2.213  11.316 96.221  1.00 15.44 ? 13  MET B N   1 
ATOM   875  C  CA  . MET B 1 13  ? -1.023  10.516 96.370  1.00 15.17 ? 13  MET B CA  1 
ATOM   876  C  C   . MET B 1 13  ? -0.521  10.160 94.955  1.00 12.97 ? 13  MET B C   1 
ATOM   877  O  O   . MET B 1 13  ? -1.311  10.041 94.039  1.00 14.06 ? 13  MET B O   1 
ATOM   878  C  CB  . MET B 1 13  ? -1.250  9.204  97.135  1.00 20.64 ? 13  MET B CB  1 
ATOM   879  C  CG  . MET B 1 13  ? 0.069   8.448  97.482  0.50 18.36 ? 13  MET B CG  1 
ATOM   880  S  SD  . MET B 1 13  ? 0.535   7.087  96.424  0.50 20.03 ? 13  MET B SD  1 
ATOM   881  N  N   . VAL B 1 14  ? 0.780   10.031 94.763  1.00 13.07 ? 14  VAL B N   1 
ATOM   882  C  CA  . VAL B 1 14  ? 1.355   9.629  93.498  1.00 12.17 ? 14  VAL B CA  1 
ATOM   883  C  C   . VAL B 1 14  ? 2.183   8.372  93.754  1.00 15.51 ? 14  VAL B C   1 
ATOM   884  O  O   . VAL B 1 14  ? 2.951   8.345  94.696  1.00 16.43 ? 14  VAL B O   1 
ATOM   885  C  CB  . VAL B 1 14  ? 2.187   10.748 92.910  1.00 14.81 ? 14  VAL B CB  1 
ATOM   886  C  CG1 . VAL B 1 14  ? 2.840   10.353 91.604  1.00 16.06 ? 14  VAL B CG1 1 
ATOM   887  C  CG2 . VAL B 1 14  ? 1.296   11.952 92.704  1.00 15.48 ? 14  VAL B CG2 1 
ATOM   888  N  N   . LYS B 1 15  ? 2.060   7.372  92.897  1.00 12.73 ? 15  LYS B N   1 
ATOM   889  C  CA  . LYS B 1 15  ? 2.829   6.148  93.010  1.00 14.65 ? 15  LYS B CA  1 
ATOM   890  C  C   . LYS B 1 15  ? 3.457   5.832  91.668  1.00 13.27 ? 15  LYS B C   1 
ATOM   891  O  O   . LYS B 1 15  ? 2.761   5.896  90.653  1.00 15.93 ? 15  LYS B O   1 
ATOM   892  C  CB  . LYS B 1 15  ? 1.920   4.956  93.457  0.50 11.80 ? 15  LYS B CB  1 
ATOM   893  C  CG  . LYS B 1 15  ? 2.758   3.677  93.631  0.50 17.77 ? 15  LYS B CG  1 
ATOM   894  C  CD  . LYS B 1 15  ? 1.866   2.562  94.096  0.50 23.00 ? 15  LYS B CD  1 
ATOM   895  C  CE  . LYS B 1 15  ? 2.593   1.250  94.030  0.50 25.75 ? 15  LYS B CE  1 
ATOM   896  N  NZ  . LYS B 1 15  ? 3.674   1.393  94.995  0.50 27.35 ? 15  LYS B NZ  1 
ATOM   897  N  N   . VAL B 1 16  ? 4.743   5.520  91.651  1.00 12.35 ? 16  VAL B N   1 
ATOM   898  C  CA  . VAL B 1 16  ? 5.490   5.329  90.400  1.00 11.93 ? 16  VAL B CA  1 
ATOM   899  C  C   . VAL B 1 16  ? 6.234   4.009  90.436  1.00 11.14 ? 16  VAL B C   1 
ATOM   900  O  O   . VAL B 1 16  ? 6.944   3.721  91.388  1.00 12.36 ? 16  VAL B O   1 
ATOM   901  C  CB  . VAL B 1 16  ? 6.437   6.528  90.148  1.00 12.27 ? 16  VAL B CB  1 
ATOM   902  C  CG1 . VAL B 1 16  ? 7.000   6.482  88.751  1.00 11.92 ? 16  VAL B CG1 1 
ATOM   903  C  CG2 . VAL B 1 16  ? 5.757   7.890  90.338  1.00 14.07 ? 16  VAL B CG2 1 
ATOM   904  N  N   . LEU B 1 17  ? 6.095   3.236  89.343  1.00 11.56 ? 17  LEU B N   1 
ATOM   905  C  CA  . LEU B 1 17  ? 6.740   1.948  89.166  1.00 11.01 ? 17  LEU B CA  1 
ATOM   906  C  C   . LEU B 1 17  ? 7.662   1.976  87.968  1.00 11.48 ? 17  LEU B C   1 
ATOM   907  O  O   . LEU B 1 17  ? 7.406   2.696  87.013  1.00 11.53 ? 17  LEU B O   1 
ATOM   908  C  CB  . LEU B 1 17  ? 5.716   0.834  89.037  1.00 12.96 ? 17  LEU B CB  1 
ATOM   909  C  CG  . LEU B 1 17  ? 4.822   0.589  90.252  1.00 14.16 ? 17  LEU B CG  1 
ATOM   910  C  CD1 . LEU B 1 17  ? 3.852   -0.549 89.917  1.00 17.71 ? 17  LEU B CD1 1 
ATOM   911  C  CD2 . LEU B 1 17  ? 5.668   0.269  91.464  1.00 15.81 ? 17  LEU B CD2 1 
ATOM   912  N  N   . ASP B 1 18  ? 8.696   1.139  87.988  1.00 11.35 ? 18  ASP B N   1 
ATOM   913  C  CA  . ASP B 1 18  ? 9.693   1.023  86.905  1.00 10.85 ? 18  ASP B CA  1 
ATOM   914  C  C   . ASP B 1 18  ? 9.555   -0.341 86.219  1.00 9.71  ? 18  ASP B C   1 
ATOM   915  O  O   . ASP B 1 18  ? 9.734   -1.371 86.859  1.00 11.15 ? 18  ASP B O   1 
ATOM   916  C  CB  . ASP B 1 18  ? 11.051  1.214  87.563  1.00 10.37 ? 18  ASP B CB  1 
ATOM   917  C  CG  . ASP B 1 18  ? 12.255  1.016  86.671  1.00 11.51 ? 18  ASP B CG  1 
ATOM   918  O  OD1 . ASP B 1 18  ? 12.167  0.296  85.661  1.00 11.83 ? 18  ASP B OD1 1 
ATOM   919  O  OD2 . ASP B 1 18  ? 13.312  1.576  86.983  1.00 14.22 ? 18  ASP B OD2 1 
ATOM   920  N  N   . ALA B 1 19  ? 9.174   -0.328 84.962  1.00 9.99  ? 19  ALA B N   1 
ATOM   921  C  CA  . ALA B 1 19  ? 8.892   -1.546 84.189  1.00 12.03 ? 19  ALA B CA  1 
ATOM   922  C  C   . ALA B 1 19  ? 10.155  -2.253 83.680  1.00 11.50 ? 19  ALA B C   1 
ATOM   923  O  O   . ALA B 1 19  ? 10.065  -3.338 83.136  1.00 13.08 ? 19  ALA B O   1 
ATOM   924  C  CB  . ALA B 1 19  ? 7.983   -1.173 83.045  1.00 13.36 ? 19  ALA B CB  1 
ATOM   925  N  N   . VAL B 1 20  ? 11.302  -1.565 83.713  1.00 12.07 ? 20  VAL B N   1 
ATOM   926  C  CA  . VAL B 1 20  ? 12.582  -2.079 83.269  1.00 12.93 ? 20  VAL B CA  1 
ATOM   927  C  C   . VAL B 1 20  ? 13.237  -2.877 84.333  1.00 13.75 ? 20  VAL B C   1 
ATOM   928  O  O   . VAL B 1 20  ? 13.743  -3.972 84.112  1.00 17.68 ? 20  VAL B O   1 
ATOM   929  C  CB  . VAL B 1 20  ? 13.514  -0.958 82.770  1.00 16.97 ? 20  VAL B CB  1 
ATOM   930  C  CG1 . VAL B 1 20  ? 14.914  -1.457 82.472  1.00 19.13 ? 20  VAL B CG1 1 
ATOM   931  C  CG2 . VAL B 1 20  ? 12.944  -0.315 81.523  1.00 16.76 ? 20  VAL B CG2 1 
ATOM   932  N  N   . ARG B 1 21  ? 13.285  -2.332 85.526  1.00 13.03 ? 21  ARG B N   1 
ATOM   933  C  CA  . ARG B 1 21  ? 13.944  -2.964 86.640  1.00 15.02 ? 21  ARG B CA  1 
ATOM   934  C  C   . ARG B 1 21  ? 13.014  -3.748 87.522  1.00 13.40 ? 21  ARG B C   1 
ATOM   935  O  O   . ARG B 1 21  ? 13.461  -4.469 88.405  1.00 15.96 ? 21  ARG B O   1 
ATOM   936  C  CB  . ARG B 1 21  ? 14.576  -1.885 87.499  1.00 18.80 ? 21  ARG B CB  1 
ATOM   937  N  N   . GLY B 1 22  ? 11.722  -3.612 87.349  1.00 12.48 ? 22  GLY B N   1 
ATOM   938  C  CA  . GLY B 1 22  ? 10.753  -4.321 88.118  1.00 13.43 ? 22  GLY B CA  1 
ATOM   939  C  C   . GLY B 1 22  ? 10.767  -3.918 89.558  1.00 12.06 ? 22  GLY B C   1 
ATOM   940  O  O   . GLY B 1 22  ? 10.867  -4.705 90.476  1.00 13.51 ? 22  GLY B O   1 
ATOM   941  N  N   . SER B 1 23  ? 10.645  -2.609 89.787  1.00 13.05 ? 23  SER B N   1 
ATOM   942  C  CA  . SER B 1 23  ? 10.810  -2.031 91.107  1.00 14.08 ? 23  SER B CA  1 
ATOM   943  C  C   . SER B 1 23  ? 9.958   -0.775 91.240  1.00 11.99 ? 23  SER B C   1 
ATOM   944  O  O   . SER B 1 23  ? 9.547   -0.183 90.287  1.00 13.60 ? 23  SER B O   1 
ATOM   945  C  CB  . SER B 1 23  ? 12.256  -1.587 91.337  1.00 17.30 ? 23  SER B CB  1 
ATOM   946  O  OG  . SER B 1 23  ? 12.616  -0.515 90.462  1.00 19.77 ? 23  SER B OG  1 
ATOM   947  N  N   . PRO B 1 24  ? 9.762   -0.344 92.510  1.00 12.53 ? 24  PRO B N   1 
ATOM   948  C  CA  . PRO B 1 24  ? 9.328   1.051  92.693  1.00 12.53 ? 24  PRO B CA  1 
ATOM   949  C  C   . PRO B 1 24  ? 10.298  1.995  92.029  1.00 12.88 ? 24  PRO B C   1 
ATOM   950  O  O   . PRO B 1 24  ? 11.462  1.709  91.956  1.00 13.26 ? 24  PRO B O   1 
ATOM   951  C  CB  . PRO B 1 24  ? 9.276   1.267  94.190  1.00 14.74 ? 24  PRO B CB  1 
ATOM   952  C  CG  . PRO B 1 24  ? 9.663   0.010  94.779  1.00 24.94 ? 24  PRO B CG  1 
ATOM   953  C  CD  . PRO B 1 24  ? 10.184  -0.927 93.785  1.00 13.87 ? 24  PRO B CD  1 
ATOM   954  N  N   . ALA B 1 25  ? 9.801   3.140  91.534  1.00 12.09 ? 25  ALA B N   1 
ATOM   955  C  CA  . ALA B 1 25  ? 10.671  4.176  91.036  1.00 12.50 ? 25  ALA B CA  1 
ATOM   956  C  C   . ALA B 1 25  ? 10.946  5.145  92.176  1.00 14.00 ? 25  ALA B C   1 
ATOM   957  O  O   . ALA B 1 25  ? 10.081  5.883  92.553  1.00 12.87 ? 25  ALA B O   1 
ATOM   958  C  CB  . ALA B 1 25  ? 10.021  4.914  89.850  1.00 12.53 ? 25  ALA B CB  1 
ATOM   959  N  N   . ILE B 1 26  ? 12.151  5.066  92.694  1.00 13.35 ? 26  ILE B N   1 
ATOM   960  C  CA  . ILE B 1 26  ? 12.559  5.735  93.857  1.00 13.68 ? 26  ILE B CA  1 
ATOM   961  C  C   . ILE B 1 26  ? 13.211  7.044  93.547  1.00 15.28 ? 26  ILE B C   1 
ATOM   962  O  O   . ILE B 1 26  ? 13.961  7.146  92.590  1.00 15.59 ? 26  ILE B O   1 
ATOM   963  C  CB  . ILE B 1 26  ? 13.514  4.807  94.699  1.00 16.33 ? 26  ILE B CB  1 
ATOM   964  C  CG1 . ILE B 1 26  ? 12.832  3.468  95.004  1.00 18.73 ? 26  ILE B CG1 1 
ATOM   965  C  CG2 . ILE B 1 26  ? 14.069  5.462  95.973  1.00 21.99 ? 26  ILE B CG2 1 
ATOM   966  C  CD1 . ILE B 1 26  ? 13.819  2.429  95.449  1.00 23.46 ? 26  ILE B CD1 1 
ATOM   967  N  N   . ASN B 1 27  ? 12.970  8.053  94.337  1.00 14.11 ? 27  ASN B N   1 
ATOM   968  C  CA  . ASN B 1 27  ? 13.611  9.371  94.240  1.00 17.31 ? 27  ASN B CA  1 
ATOM   969  C  C   . ASN B 1 27  ? 13.267  10.089 92.955  1.00 15.19 ? 27  ASN B C   1 
ATOM   970  O  O   . ASN B 1 27  ? 14.064  10.813 92.408  1.00 18.60 ? 27  ASN B O   1 
ATOM   971  C  CB  . ASN B 1 27  ? 15.125  9.273  94.445  1.00 19.00 ? 27  ASN B CB  1 
ATOM   972  C  CG  . ASN B 1 27  ? 15.729  10.572 94.906  1.00 29.77 ? 27  ASN B CG  1 
ATOM   973  O  OD1 . ASN B 1 27  ? 15.127  11.218 95.758  1.00 31.79 ? 27  ASN B OD1 1 
ATOM   974  N  ND2 . ASN B 1 27  ? 16.879  10.976 94.328  1.00 36.51 ? 27  ASN B ND2 1 
ATOM   975  N  N   . VAL B 1 28  ? 12.050  9.887  92.465  1.00 13.49 ? 28  VAL B N   1 
ATOM   976  C  CA  . VAL B 1 28  ? 11.544  10.610 91.319  1.00 14.06 ? 28  VAL B CA  1 
ATOM   977  C  C   . VAL B 1 28  ? 10.893  11.901 91.745  1.00 11.98 ? 28  VAL B C   1 
ATOM   978  O  O   . VAL B 1 28  ? 10.081  11.916 92.656  1.00 13.07 ? 28  VAL B O   1 
ATOM   979  C  CB  . VAL B 1 28  ? 10.474  9.730  90.598  1.00 15.98 ? 28  VAL B CB  1 
ATOM   980  C  CG1 . VAL B 1 28  ? 9.924   10.487 89.370  1.00 19.97 ? 28  VAL B CG1 1 
ATOM   981  C  CG2 . VAL B 1 28  ? 11.012  8.420  90.183  1.00 18.92 ? 28  VAL B CG2 1 
ATOM   982  N  N   . ALA B 1 29  ? 11.317  13.009 91.143  1.00 12.95 ? 29  ALA B N   1 
ATOM   983  C  CA  . ALA B 1 29  ? 10.712  14.319 91.399  1.00 12.60 ? 29  ALA B CA  1 
ATOM   984  C  C   . ALA B 1 29  ? 9.352   14.429 90.747  1.00 13.20 ? 29  ALA B C   1 
ATOM   985  O  O   . ALA B 1 29  ? 9.170   14.039 89.594  1.00 14.19 ? 29  ALA B O   1 
ATOM   986  C  CB  . ALA B 1 29  ? 11.609  15.436 90.909  1.00 13.91 ? 29  ALA B CB  1 
ATOM   987  N  N   . VAL B 1 30  ? 8.407   14.952 91.525  1.00 12.81 ? 30  VAL B N   1 
ATOM   988  C  CA  . VAL B 1 30  ? 7.047   15.132 91.113  1.00 13.92 ? 30  VAL B CA  1 
ATOM   989  C  C   . VAL B 1 30  ? 6.630   16.544 91.456  1.00 14.32 ? 30  VAL B C   1 
ATOM   990  O  O   . VAL B 1 30  ? 6.748   16.950 92.584  1.00 15.13 ? 30  VAL B O   1 
ATOM   991  C  CB  . VAL B 1 30  ? 6.107   14.120 91.806  1.00 13.84 ? 30  VAL B CB  1 
ATOM   992  C  CG1 . VAL B 1 30  ? 4.656   14.359 91.382  1.00 17.18 ? 30  VAL B CG1 1 
ATOM   993  C  CG2 . VAL B 1 30  ? 6.495   12.700 91.538  1.00 14.70 ? 30  VAL B CG2 1 
ATOM   994  N  N   . HIS B 1 31  ? 6.070   17.273 90.480  1.00 15.14 ? 31  HIS B N   1 
ATOM   995  C  CA  . HIS B 1 31  ? 5.527   18.597 90.751  1.00 15.20 ? 31  HIS B CA  1 
ATOM   996  C  C   . HIS B 1 31  ? 4.072   18.628 90.320  1.00 16.49 ? 31  HIS B C   1 
ATOM   997  O  O   . HIS B 1 31  ? 3.735   18.159 89.242  1.00 18.99 ? 31  HIS B O   1 
ATOM   998  C  CB  . HIS B 1 31  ? 6.252   19.658 89.901  1.00 18.72 ? 31  HIS B CB  1 
ATOM   999  C  CG  . HIS B 1 31  ? 7.644   19.943 90.386  1.00 25.32 ? 31  HIS B CG  1 
ATOM   1000 N  ND1 . HIS B 1 31  ? 8.736   19.149 90.083  1.00 26.07 ? 31  HIS B ND1 1 
ATOM   1001 C  CD2 . HIS B 1 31  ? 8.084   20.863 91.268  1.00 27.58 ? 31  HIS B CD2 1 
ATOM   1002 C  CE1 . HIS B 1 31  ? 9.818   19.650 90.674  1.00 25.55 ? 31  HIS B CE1 1 
ATOM   1003 N  NE2 . HIS B 1 31  ? 9.430   20.678 91.425  1.00 28.57 ? 31  HIS B NE2 1 
ATOM   1004 N  N   . VAL B 1 32  ? 3.235   19.179 91.166  1.00 14.75 ? 32  VAL B N   1 
ATOM   1005 C  CA  . VAL B 1 32  ? 1.818   19.339 90.879  1.00 14.68 ? 32  VAL B CA  1 
ATOM   1006 C  C   . VAL B 1 32  ? 1.545   20.821 90.720  1.00 14.50 ? 32  VAL B C   1 
ATOM   1007 O  O   . VAL B 1 32  ? 1.989   21.650 91.483  1.00 16.58 ? 32  VAL B O   1 
ATOM   1008 C  CB  . VAL B 1 32  ? 0.982   18.782 91.986  1.00 14.96 ? 32  VAL B CB  1 
ATOM   1009 C  CG1 . VAL B 1 32  ? -0.501  18.743 91.640  1.00 15.58 ? 32  VAL B CG1 1 
ATOM   1010 C  CG2 . VAL B 1 32  ? 1.431   17.361 92.366  1.00 14.53 ? 32  VAL B CG2 1 
ATOM   1011 N  N   . PHE B 1 33  ? 0.727   21.095 89.740  1.00 15.74 ? 33  PHE B N   1 
ATOM   1012 C  CA  . PHE B 1 33  ? 0.329   22.473 89.370  1.00 17.49 ? 33  PHE B CA  1 
ATOM   1013 C  C   . PHE B 1 33  ? -1.222  22.499 89.295  1.00 18.06 ? 33  PHE B C   1 
ATOM   1014 O  O   . PHE B 1 33  ? -1.873  21.507 89.030  1.00 15.27 ? 33  PHE B O   1 
ATOM   1015 C  CB  . PHE B 1 33  ? 0.894   22.890 88.021  1.00 20.46 ? 33  PHE B CB  1 
ATOM   1016 C  CG  . PHE B 1 33  ? 2.385   22.794 87.938  1.00 20.08 ? 33  PHE B CG  1 
ATOM   1017 C  CD1 . PHE B 1 33  ? 2.989   21.597 87.633  1.00 22.33 ? 33  PHE B CD1 1 
ATOM   1018 C  CD2 . PHE B 1 33  ? 3.163   23.909 88.106  1.00 22.94 ? 33  PHE B CD2 1 
ATOM   1019 C  CE1 . PHE B 1 33  ? 4.352   21.531 87.481  1.00 22.64 ? 33  PHE B CE1 1 
ATOM   1020 C  CE2 . PHE B 1 33  ? 4.562   23.821 88.042  1.00 25.44 ? 33  PHE B CE2 1 
ATOM   1021 C  CZ  . PHE B 1 33  ? 5.141   22.635 87.694  1.00 23.29 ? 33  PHE B CZ  1 
ATOM   1022 N  N   . ARG B 1 34  ? -1.767  23.646 89.568  1.00 18.34 ? 34  ARG B N   1 
ATOM   1023 C  CA  . ARG B 1 34  ? -3.235  23.900 89.410  1.00 18.24 ? 34  ARG B CA  1 
ATOM   1024 C  C   . ARG B 1 34  ? -3.418  24.971 88.369  1.00 18.25 ? 34  ARG B C   1 
ATOM   1025 O  O   . ARG B 1 34  ? -2.693  25.949 88.391  1.00 20.69 ? 34  ARG B O   1 
ATOM   1026 C  CB  . ARG B 1 34  ? -3.852  24.325 90.757  1.00 20.46 ? 34  ARG B CB  1 
ATOM   1027 C  CG  . ARG B 1 34  ? -5.373  24.448 90.777  1.00 21.30 ? 34  ARG B CG  1 
ATOM   1028 C  CD  . ARG B 1 34  ? -5.957  24.806 92.162  1.00 24.84 ? 34  ARG B CD  1 
ATOM   1029 N  N   . LYS B 1 35  ? -4.423  24.817 87.515  1.00 18.83 ? 35  LYS B N   1 
ATOM   1030 C  CA  . LYS B 1 35  ? -4.591  25.748 86.406  1.00 19.08 ? 35  LYS B CA  1 
ATOM   1031 C  C   . LYS B 1 35  ? -5.236  27.001 86.958  1.00 22.47 ? 35  LYS B C   1 
ATOM   1032 O  O   . LYS B 1 35  ? -6.265  26.929 87.642  1.00 22.03 ? 35  LYS B O   1 
ATOM   1033 C  CB  . LYS B 1 35  ? -5.439  25.177 85.268  1.00 25.28 ? 35  LYS B CB  1 
ATOM   1034 N  N   . ALA B 1 36  ? -4.611  28.146 86.660  1.00 22.77 ? 36  ALA B N   1 
ATOM   1035 C  CA  . ALA B 1 36  ? -5.073  29.452 87.089  1.00 25.10 ? 36  ALA B CA  1 
ATOM   1036 C  C   . ALA B 1 36  ? -6.097  29.993 86.093  1.00 26.02 ? 36  ALA B C   1 
ATOM   1037 O  O   . ALA B 1 36  ? -6.251  29.481 84.952  1.00 27.78 ? 36  ALA B O   1 
ATOM   1038 C  CB  . ALA B 1 36  ? -3.892  30.376 87.215  1.00 26.04 ? 36  ALA B CB  1 
ATOM   1039 N  N   . ALA B 1 37  ? -6.753  31.078 86.484  1.00 28.56 ? 37  ALA B N   1 
ATOM   1040 C  CA  . ALA B 1 37  ? -7.798  31.724 85.621  1.00 30.70 ? 37  ALA B CA  1 
ATOM   1041 C  C   . ALA B 1 37  ? -7.270  32.197 84.256  1.00 34.00 ? 37  ALA B C   1 
ATOM   1042 O  O   . ALA B 1 37  ? -8.004  32.194 83.279  1.00 38.96 ? 37  ALA B O   1 
ATOM   1043 C  CB  . ALA B 1 37  ? -8.463  32.893 86.352  1.00 35.19 ? 37  ALA B CB  1 
ATOM   1044 N  N   . ASP B 1 38  ? -5.995  32.581 84.178  1.00 32.84 ? 38  ASP B N   1 
ATOM   1045 C  CA  . ASP B 1 38  ? -5.393  32.968 82.913  1.00 29.93 ? 38  ASP B CA  1 
ATOM   1046 C  C   . ASP B 1 38  ? -4.847  31.812 82.097  1.00 31.12 ? 38  ASP B C   1 
ATOM   1047 O  O   . ASP B 1 38  ? -4.035  32.045 81.194  1.00 40.56 ? 38  ASP B O   1 
ATOM   1048 C  CB  . ASP B 1 38  ? -4.283  34.018 83.136  1.00 32.56 ? 38  ASP B CB  1 
ATOM   1049 C  CG  . ASP B 1 38  ? -3.160  33.545 84.037  1.00 39.23 ? 38  ASP B CG  1 
ATOM   1050 O  OD1 . ASP B 1 38  ? -3.179  32.399 84.475  1.00 40.80 ? 38  ASP B OD1 1 
ATOM   1051 O  OD2 . ASP B 1 38  ? -2.228  34.346 84.320  1.00 36.30 ? 38  ASP B OD2 1 
ATOM   1052 N  N   . ASP B 1 39  ? -5.278  30.588 82.405  1.00 34.76 ? 39  ASP B N   1 
ATOM   1053 C  CA  . ASP B 1 39  ? -4.830  29.337 81.728  1.00 31.06 ? 39  ASP B CA  1 
ATOM   1054 C  C   . ASP B 1 39  ? -3.333  28.982 82.007  1.00 26.40 ? 39  ASP B C   1 
ATOM   1055 O  O   . ASP B 1 39  ? -2.791  28.034 81.427  1.00 38.46 ? 39  ASP B O   1 
ATOM   1056 C  CB  . ASP B 1 39  ? -5.244  29.307 80.228  1.00 35.78 ? 39  ASP B CB  1 
ATOM   1057 N  N   . THR B 1 40  ? -2.687  29.684 82.951  1.00 30.35 ? 40  THR B N   1 
ATOM   1058 C  CA  . THR B 1 40  ? -1.319  29.283 83.366  1.00 29.50 ? 40  THR B CA  1 
ATOM   1059 C  C   . THR B 1 40  ? -1.316  28.265 84.530  1.00 30.43 ? 40  THR B C   1 
ATOM   1060 O  O   . THR B 1 40  ? -2.302  28.102 85.207  1.00 25.86 ? 40  THR B O   1 
ATOM   1061 C  CB  . THR B 1 40  ? -0.412  30.451 83.764  1.00 30.58 ? 40  THR B CB  1 
ATOM   1062 O  OG1 . THR B 1 40  ? -0.852  31.016 85.005  1.00 30.54 ? 40  THR B OG1 1 
ATOM   1063 C  CG2 . THR B 1 40  ? -0.398  31.502 82.657  1.00 35.67 ? 40  THR B CG2 1 
ATOM   1064 N  N   . TRP B 1 41  ? -0.159  27.680 84.772  1.00 27.35 ? 41  TRP B N   1 
ATOM   1065 C  CA  . TRP B 1 41  ? -0.003  26.591 85.737  1.00 24.75 ? 41  TRP B CA  1 
ATOM   1066 C  C   . TRP B 1 41  ? 0.674   27.122 86.980  1.00 24.56 ? 41  TRP B C   1 
ATOM   1067 O  O   . TRP B 1 41  ? 1.824   27.518 86.942  1.00 34.59 ? 41  TRP B O   1 
ATOM   1068 C  CB  . TRP B 1 41  ? 0.836   25.471 85.124  1.00 27.63 ? 41  TRP B CB  1 
ATOM   1069 C  CG  . TRP B 1 41  ? 0.209   24.711 84.093  1.00 24.00 ? 41  TRP B CG  1 
ATOM   1070 C  CD1 . TRP B 1 41  ? 0.553   24.674 82.753  1.00 32.95 ? 41  TRP B CD1 1 
ATOM   1071 C  CD2 . TRP B 1 41  ? -0.952  23.868 84.228  1.00 21.19 ? 41  TRP B CD2 1 
ATOM   1072 N  NE1 . TRP B 1 41  ? -0.277  23.785 82.073  1.00 32.79 ? 41  TRP B NE1 1 
ATOM   1073 C  CE2 . TRP B 1 41  ? -1.223  23.310 82.950  1.00 26.94 ? 41  TRP B CE2 1 
ATOM   1074 C  CE3 . TRP B 1 41  ? -1.743  23.477 85.320  1.00 20.46 ? 41  TRP B CE3 1 
ATOM   1075 C  CZ2 . TRP B 1 41  ? -2.278  22.432 82.749  1.00 26.30 ? 41  TRP B CZ2 1 
ATOM   1076 C  CZ3 . TRP B 1 41  ? -2.832  22.604 85.100  1.00 20.47 ? 41  TRP B CZ3 1 
ATOM   1077 C  CH2 . TRP B 1 41  ? -3.058  22.096 83.852  1.00 25.05 ? 41  TRP B CH2 1 
ATOM   1078 N  N   . GLU B 1 42  ? -0.039  27.126 88.080  1.00 23.17 ? 42  GLU B N   1 
ATOM   1079 C  CA  . GLU B 1 42  ? 0.431   27.694 89.318  1.00 23.80 ? 42  GLU B CA  1 
ATOM   1080 C  C   . GLU B 1 42  ? 0.997   26.492 90.126  1.00 26.28 ? 42  GLU B C   1 
ATOM   1081 O  O   . GLU B 1 42  ? 0.289   25.520 90.400  1.00 23.16 ? 42  GLU B O   1 
ATOM   1082 C  CB  . GLU B 1 42  ? -0.797  28.275 90.044  1.00 27.31 ? 42  GLU B CB  1 
ATOM   1083 N  N   . PRO B 1 43  ? 2.267   26.563 90.575  1.00 24.92 ? 43  PRO B N   1 
ATOM   1084 C  CA  . PRO B 1 43  ? 2.751   25.528 91.472  1.00 22.33 ? 43  PRO B CA  1 
ATOM   1085 C  C   . PRO B 1 43  ? 1.814   25.302 92.670  1.00 21.67 ? 43  PRO B C   1 
ATOM   1086 O  O   . PRO B 1 43  ? 1.298   26.236 93.242  1.00 27.74 ? 43  PRO B O   1 
ATOM   1087 C  CB  . PRO B 1 43  ? 4.098   26.073 91.966  1.00 25.53 ? 43  PRO B CB  1 
ATOM   1088 C  CG  . PRO B 1 43  ? 4.584   26.874 90.798  1.00 30.36 ? 43  PRO B CG  1 
ATOM   1089 C  CD  . PRO B 1 43  ? 3.361   27.454 90.126  1.00 28.33 ? 43  PRO B CD  1 
ATOM   1090 N  N   . PHE B 1 44  ? 1.602   24.027 93.006  1.00 19.28 ? 44  PHE B N   1 
ATOM   1091 C  CA  . PHE B 1 44  ? 0.655   23.617 94.018  1.00 18.32 ? 44  PHE B CA  1 
ATOM   1092 C  C   . PHE B 1 44  ? 1.266   22.728 95.098  1.00 17.41 ? 44  PHE B C   1 
ATOM   1093 O  O   . PHE B 1 44  ? 0.979   22.897 96.262  1.00 19.83 ? 44  PHE B O   1 
ATOM   1094 C  CB  . PHE B 1 44  ? -0.551  22.908 93.301  1.00 19.10 ? 44  PHE B CB  1 
ATOM   1095 C  CG  . PHE B 1 44  ? -1.562  22.392 94.227  1.00 21.72 ? 44  PHE B CG  1 
ATOM   1096 C  CD1 . PHE B 1 44  ? -2.540  23.256 94.702  1.00 19.90 ? 44  PHE B CD1 1 
ATOM   1097 C  CD2 . PHE B 1 44  ? -1.616  21.069 94.563  1.00 20.19 ? 44  PHE B CD2 1 
ATOM   1098 C  CE1 . PHE B 1 44  ? -3.485  22.783 95.617  1.00 22.50 ? 44  PHE B CE1 1 
ATOM   1099 C  CE2 . PHE B 1 44  ? -2.558  20.496 95.468  1.00 18.83 ? 44  PHE B CE2 1 
ATOM   1100 C  CZ  . PHE B 1 44  ? -3.473  21.458 96.067  1.00 23.33 ? 44  PHE B CZ  1 
ATOM   1101 N  N   . ALA B 1 45  ? 2.115   21.736 94.687  1.00 15.53 ? 45  ALA B N   1 
ATOM   1102 C  CA  . ALA B 1 45  ? 2.719   20.731 95.646  1.00 20.19 ? 45  ALA B CA  1 
ATOM   1103 C  C   . ALA B 1 45  ? 3.849   20.103 94.886  1.00 14.94 ? 45  ALA B C   1 
ATOM   1104 O  O   . ALA B 1 45  ? 3.819   20.060 93.649  1.00 17.44 ? 45  ALA B O   1 
ATOM   1105 C  CB  . ALA B 1 45  ? 1.728   19.736 96.175  1.00 20.32 ? 45  ALA B CB  1 
ATOM   1106 N  N   . SER B 1 46  ? 4.835   19.579 95.590  1.00 15.10 ? 46  SER B N   1 
ATOM   1107 C  CA  . SER B 1 46  ? 5.862   18.775 94.978  1.00 14.62 ? 46  SER B CA  1 
ATOM   1108 C  C   . SER B 1 46  ? 6.584   17.920 96.019  1.00 13.75 ? 46  SER B C   1 
ATOM   1109 O  O   . SER B 1 46  ? 6.411   18.101 97.220  1.00 16.70 ? 46  SER B O   1 
ATOM   1110 C  CB  . SER B 1 46  ? 6.892   19.597 94.180  1.00 16.24 ? 46  SER B CB  1 
ATOM   1111 O  OG  . SER B 1 46  ? 7.473   20.567 94.991  1.00 17.21 ? 46  SER B OG  1 
ATOM   1112 N  N   . GLY B 1 47  ? 7.366   16.966 95.523  1.00 13.64 ? 47  GLY B N   1 
ATOM   1113 C  CA  . GLY B 1 47  ? 8.129   16.092 96.408  1.00 13.92 ? 47  GLY B CA  1 
ATOM   1114 C  C   . GLY B 1 47  ? 8.867   15.051 95.571  1.00 13.06 ? 47  GLY B C   1 
ATOM   1115 O  O   . GLY B 1 47  ? 8.902   15.142 94.367  1.00 14.68 ? 47  GLY B O   1 
ATOM   1116 N  N   . LYS B 1 48  ? 9.497   14.119 96.266  1.00 14.36 ? 48  LYS B N   1 
ATOM   1117 C  CA  . LYS B 1 48  ? 10.191  13.001 95.649  1.00 14.69 ? 48  LYS B CA  1 
ATOM   1118 C  C   . LYS B 1 48  ? 9.629   11.683 96.170  1.00 14.73 ? 48  LYS B C   1 
ATOM   1119 O  O   . LYS B 1 48  ? 9.337   11.554 97.342  1.00 15.79 ? 48  LYS B O   1 
ATOM   1120 C  CB  . LYS B 1 48  ? 11.698  13.055 95.882  1.00 19.13 ? 48  LYS B CB  1 
ATOM   1121 C  CG  . LYS B 1 48  ? 12.394  14.249 95.208  1.00 25.56 ? 48  LYS B CG  1 
ATOM   1122 C  CD  . LYS B 1 48  ? 13.648  13.874 94.433  1.00 33.61 ? 48  LYS B CD  1 
ATOM   1123 C  CE  . LYS B 1 48  ? 14.709  14.976 94.452  1.00 42.12 ? 48  LYS B CE  1 
ATOM   1124 N  N   . THR B 1 49  ? 9.466   10.701 95.293  1.00 13.82 ? 49  THR B N   1 
ATOM   1125 C  CA  . THR B 1 49  ? 8.964   9.418  95.687  1.00 13.13 ? 49  THR B CA  1 
ATOM   1126 C  C   . THR B 1 49  ? 9.930   8.760  96.681  1.00 13.38 ? 49  THR B C   1 
ATOM   1127 O  O   . THR B 1 49  ? 11.151  8.897  96.619  1.00 14.23 ? 49  THR B O   1 
ATOM   1128 C  CB  . THR B 1 49  ? 8.729   8.463  94.494  1.00 12.81 ? 49  THR B CB  1 
ATOM   1129 O  OG1 . THR B 1 49  ? 9.975   8.285  93.801  1.00 13.50 ? 49  THR B OG1 1 
ATOM   1130 C  CG2 . THR B 1 49  ? 7.636   9.015  93.581  1.00 14.11 ? 49  THR B CG2 1 
ATOM   1131 N  N   . SER B 1 50  ? 9.349   8.011  97.570  1.00 13.45 ? 50  SER B N   1 
ATOM   1132 C  CA  . SER B 1 50  ? 10.056  7.324  98.636  1.00 14.95 ? 50  SER B CA  1 
ATOM   1133 C  C   . SER B 1 50  ? 10.601  5.966  98.101  1.00 15.67 ? 50  SER B C   1 
ATOM   1134 O  O   . SER B 1 50  ? 10.467  5.657  96.932  1.00 14.93 ? 50  SER B O   1 
ATOM   1135 C  CB  . SER B 1 50  ? 9.071   6.961  99.761  1.00 15.26 ? 50  SER B CB  1 
ATOM   1136 O  OG  . SER B 1 50  ? 8.164   5.931  99.286  1.00 19.84 ? 50  SER B OG  1 
ATOM   1137 N  N   . GLU B 1 51  ? 11.186  5.170  98.986  1.00 19.18 ? 51  GLU B N   1 
ATOM   1138 C  CA  . GLU B 1 51  ? 11.683  3.795  98.652  1.00 18.26 ? 51  GLU B CA  1 
ATOM   1139 C  C   . GLU B 1 51  ? 10.628  2.871  98.147  1.00 18.96 ? 51  GLU B C   1 
ATOM   1140 O  O   . GLU B 1 51  ? 10.955  1.917  97.491  1.00 19.84 ? 51  GLU B O   1 
ATOM   1141 C  CB  . GLU B 1 51  ? 12.312  3.153  99.881  1.00 22.32 ? 51  GLU B CB  1 
ATOM   1142 N  N   . SER B 1 52  ? 9.369   3.175  98.447  1.00 16.63 ? 52  SER B N   1 
ATOM   1143 C  CA  . SER B 1 52  ? 8.238   2.396  97.986  1.00 18.11 ? 52  SER B CA  1 
ATOM   1144 C  C   . SER B 1 52  ? 7.673   2.910  96.650  1.00 14.83 ? 52  SER B C   1 
ATOM   1145 O  O   . SER B 1 52  ? 6.708   2.378  96.147  1.00 17.75 ? 52  SER B O   1 
ATOM   1146 C  CB  . SER B 1 52  ? 7.112   2.380  99.048  1.00 23.80 ? 52  SER B CB  1 
ATOM   1147 O  OG  . SER B 1 52  ? 6.463   3.655  99.122  1.00 26.41 ? 52  SER B OG  1 
ATOM   1148 N  N   . GLY B 1 53  ? 8.248   3.976  96.126  1.00 13.49 ? 53  GLY B N   1 
ATOM   1149 C  CA  . GLY B 1 53  ? 7.753   4.602  94.925  1.00 14.20 ? 53  GLY B CA  1 
ATOM   1150 C  C   . GLY B 1 53  ? 6.605   5.524  95.155  1.00 13.67 ? 53  GLY B C   1 
ATOM   1151 O  O   . GLY B 1 53  ? 5.955   5.944  94.183  1.00 13.04 ? 53  GLY B O   1 
ATOM   1152 N  N   . GLU B 1 54  ? 6.287   5.824  96.411  1.00 15.15 ? 54  GLU B N   1 
ATOM   1153 C  CA  . GLU B 1 54  ? 5.084   6.591  96.732  1.00 13.81 ? 54  GLU B CA  1 
ATOM   1154 C  C   . GLU B 1 54  ? 5.462   7.963  97.202  1.00 13.15 ? 54  GLU B C   1 
ATOM   1155 O  O   . GLU B 1 54  ? 6.504   8.200  97.814  1.00 15.40 ? 54  GLU B O   1 
ATOM   1156 C  CB  . GLU B 1 54  ? 4.221   5.852  97.757  1.00 16.46 ? 54  GLU B CB  1 
ATOM   1157 C  CG  . GLU B 1 54  ? 3.812   4.490  97.269  1.00 22.85 ? 54  GLU B CG  1 
ATOM   1158 C  CD  . GLU B 1 54  ? 2.832   3.698  98.090  1.00 30.17 ? 54  GLU B CD  1 
ATOM   1159 O  OE1 . GLU B 1 54  ? 2.426   4.142  99.132  1.00 32.41 ? 54  GLU B OE1 1 
ATOM   1160 O  OE2 . GLU B 1 54  ? 2.457   2.579  97.674  1.00 37.19 ? 54  GLU B OE2 1 
ATOM   1161 N  N   . LEU B 1 55  ? 4.568   8.888  96.967  1.00 13.84 ? 55  LEU B N   1 
ATOM   1162 C  CA  . LEU B 1 55  ? 4.709   10.253 97.390  1.00 13.25 ? 55  LEU B CA  1 
ATOM   1163 C  C   . LEU B 1 55  ? 3.407   10.650 98.061  1.00 14.46 ? 55  LEU B C   1 
ATOM   1164 O  O   . LEU B 1 55  ? 2.372   10.809 97.413  1.00 15.86 ? 55  LEU B O   1 
ATOM   1165 C  CB  . LEU B 1 55  ? 5.044   11.180 96.267  1.00 13.45 ? 55  LEU B CB  1 
ATOM   1166 C  CG  . LEU B 1 55  ? 5.127   12.648 96.546  1.00 15.67 ? 55  LEU B CG  1 
ATOM   1167 C  CD1 . LEU B 1 55  ? 5.998   12.994 97.769  1.00 18.07 ? 55  LEU B CD1 1 
ATOM   1168 C  CD2 . LEU B 1 55  ? 5.623   13.382 95.366  1.00 15.64 ? 55  LEU B CD2 1 
ATOM   1169 N  N   . HIS B 1 56  ? 3.440   10.700 99.378  1.00 18.00 ? 56  HIS B N   1 
ATOM   1170 C  CA  . HIS B 1 56  ? 2.350   11.042 100.248 1.00 19.80 ? 56  HIS B CA  1 
ATOM   1171 C  C   . HIS B 1 56  ? 2.567   12.478 100.783 1.00 21.75 ? 56  HIS B C   1 
ATOM   1172 O  O   . HIS B 1 56  ? 3.643   13.065 100.655 1.00 21.68 ? 56  HIS B O   1 
ATOM   1173 C  CB  . HIS B 1 56  ? 2.281   10.067 101.464 1.00 22.41 ? 56  HIS B CB  1 
ATOM   1174 C  CG  . HIS B 1 56  ? 1.973   8.661  101.119 1.00 25.35 ? 56  HIS B CG  1 
ATOM   1175 N  ND1 . HIS B 1 56  ? 2.942   7.740  100.830 1.00 38.31 ? 56  HIS B ND1 1 
ATOM   1176 C  CD2 . HIS B 1 56  ? 0.791   8.013  101.070 1.00 31.47 ? 56  HIS B CD2 1 
ATOM   1177 C  CE1 . HIS B 1 56  ? 2.374   6.577  100.604 1.00 27.34 ? 56  HIS B CE1 1 
ATOM   1178 N  NE2 . HIS B 1 56  ? 1.065   6.715  100.733 1.00 37.30 ? 56  HIS B NE2 1 
ATOM   1179 N  N   . GLY B 1 57  ? 1.544   13.060 101.357 1.00 21.85 ? 57  GLY B N   1 
ATOM   1180 C  CA  . GLY B 1 57  ? 1.715   14.337 101.998 1.00 23.02 ? 57  GLY B CA  1 
ATOM   1181 C  C   . GLY B 1 57  ? 1.791   15.543 101.101 1.00 21.82 ? 57  GLY B C   1 
ATOM   1182 O  O   . GLY B 1 57  ? 2.227   16.603 101.526 1.00 26.26 ? 57  GLY B O   1 
ATOM   1183 N  N   . LEU B 1 58  ? 1.374   15.426 99.873  1.00 18.26 ? 58  LEU B N   1 
ATOM   1184 C  CA  . LEU B 1 58  ? 1.430   16.509 98.900  1.00 19.70 ? 58  LEU B CA  1 
ATOM   1185 C  C   . LEU B 1 58  ? 0.522   17.636 99.316  1.00 19.19 ? 58  LEU B C   1 
ATOM   1186 O  O   . LEU B 1 58  ? 0.883   18.802 99.186  1.00 25.84 ? 58  LEU B O   1 
ATOM   1187 C  CB  . LEU B 1 58  ? 1.053   16.072 97.460  1.00 17.52 ? 58  LEU B CB  1 
ATOM   1188 C  CG  . LEU B 1 58  ? 2.178   15.340 96.706  1.00 18.53 ? 58  LEU B CG  1 
ATOM   1189 C  CD1 . LEU B 1 58  ? 1.603   14.604 95.551  1.00 21.08 ? 58  LEU B CD1 1 
ATOM   1190 C  CD2 . LEU B 1 58  ? 3.330   16.275 96.339  1.00 23.41 ? 58  LEU B CD2 1 
ATOM   1191 N  N   . THR B 1 59  ? -0.695  17.311 99.803  1.00 20.53 ? 59  THR B N   1 
ATOM   1192 C  CA  . THR B 1 59  ? -1.622  18.409 100.063 1.00 19.80 ? 59  THR B CA  1 
ATOM   1193 C  C   . THR B 1 59  ? -2.528  18.046 101.211 1.00 22.15 ? 59  THR B C   1 
ATOM   1194 O  O   . THR B 1 59  ? -2.381  17.024 101.803 1.00 26.50 ? 59  THR B O   1 
ATOM   1195 C  CB  . THR B 1 59  ? -2.356  18.782 98.739  1.00 22.20 ? 59  THR B CB  1 
ATOM   1196 O  OG1 . THR B 1 59  ? -2.986  20.063 98.802  1.00 24.52 ? 59  THR B OG1 1 
ATOM   1197 C  CG2 . THR B 1 59  ? -3.369  17.714 98.437  1.00 21.29 ? 59  THR B CG2 1 
ATOM   1198 N  N   . THR B 1 60  ? -3.436  18.967 101.558 1.00 23.37 ? 60  THR B N   1 
ATOM   1199 C  CA  . THR B 1 60  ? -4.474  18.753 102.561 1.00 22.83 ? 60  THR B CA  1 
ATOM   1200 C  C   . THR B 1 60  ? -5.843  18.880 101.940 1.00 21.36 ? 60  THR B C   1 
ATOM   1201 O  O   . THR B 1 60  ? -5.957  19.386 100.845 1.00 20.85 ? 60  THR B O   1 
ATOM   1202 C  CB  . THR B 1 60  ? -4.393  19.758 103.685 1.00 22.83 ? 60  THR B CB  1 
ATOM   1203 O  OG1 . THR B 1 60  ? -4.572  21.102 103.128 1.00 28.81 ? 60  THR B OG1 1 
ATOM   1204 C  CG2 . THR B 1 60  ? -3.045  19.640 104.424 1.00 33.28 ? 60  THR B CG2 1 
ATOM   1205 N  N   . GLU B 1 61  ? -6.878  18.405 102.616 1.00 22.41 ? 61  GLU B N   1 
ATOM   1206 C  CA  . GLU B 1 61  ? -8.209  18.520 102.124 1.00 24.47 ? 61  GLU B CA  1 
ATOM   1207 C  C   . GLU B 1 61  ? -8.584  19.976 101.860 1.00 22.46 ? 61  GLU B C   1 
ATOM   1208 O  O   . GLU B 1 61  ? -9.276  20.264 100.880 1.00 22.71 ? 61  GLU B O   1 
ATOM   1209 C  CB  . GLU B 1 61  ? -9.230  17.942 103.115 1.00 26.45 ? 61  GLU B CB  1 
ATOM   1210 N  N   . GLU B 1 62  ? -8.184  20.900 102.759 1.00 23.46 ? 62  GLU B N   1 
ATOM   1211 C  CA  . GLU B 1 62  ? -8.602  22.274 102.673 1.00 24.37 ? 62  GLU B CA  1 
ATOM   1212 C  C   . GLU B 1 62  ? -7.942  22.909 101.448 1.00 20.78 ? 62  GLU B C   1 
ATOM   1213 O  O   . GLU B 1 62  ? -8.522  23.782 100.839 1.00 27.21 ? 62  GLU B O   1 
ATOM   1214 C  CB  . GLU B 1 62  ? -8.214  23.056 103.936 1.00 28.43 ? 62  GLU B CB  1 
ATOM   1215 N  N   . GLU B 1 63  ? -6.705  22.487 101.053 1.00 20.58 ? 63  GLU B N   1 
ATOM   1216 C  CA  . GLU B 1 63  ? -6.019  23.085 99.929  1.00 18.19 ? 63  GLU B CA  1 
ATOM   1217 C  C   . GLU B 1 63  ? -6.492  22.545 98.601  1.00 18.75 ? 63  GLU B C   1 
ATOM   1218 O  O   . GLU B 1 63  ? -6.382  23.239 97.586  1.00 22.14 ? 63  GLU B O   1 
ATOM   1219 C  CB  . GLU B 1 63  ? -4.469  22.848 100.094 0.50 15.99 ? 63  GLU B CB  1 
ATOM   1220 C  CG  . GLU B 1 63  ? -3.964  23.499 101.382 0.50 19.56 ? 63  GLU B CG  1 
ATOM   1221 C  CD  . GLU B 1 63  ? -2.523  23.131 101.661 0.50 20.50 ? 63  GLU B CD  1 
ATOM   1222 O  OE1 . GLU B 1 63  ? -2.253  21.983 102.070 0.50 26.61 ? 63  GLU B OE1 1 
ATOM   1223 O  OE2 . GLU B 1 63  ? -1.670  23.967 101.380 0.50 27.67 ? 63  GLU B OE2 1 
ATOM   1224 N  N   . PHE B 1 64  ? -6.919  21.323 98.568  1.00 19.41 ? 64  PHE B N   1 
ATOM   1225 C  CA  . PHE B 1 64  ? -7.206  20.613 97.312  1.00 18.44 ? 64  PHE B CA  1 
ATOM   1226 C  C   . PHE B 1 64  ? -8.634  20.813 96.853  1.00 20.39 ? 64  PHE B C   1 
ATOM   1227 O  O   . PHE B 1 64  ? -9.508  20.009 97.147  1.00 25.92 ? 64  PHE B O   1 
ATOM   1228 C  CB  . PHE B 1 64  ? -6.843  19.141 97.535  1.00 19.62 ? 64  PHE B CB  1 
ATOM   1229 C  CG  . PHE B 1 64  ? -6.879  18.324 96.277  1.00 19.89 ? 64  PHE B CG  1 
ATOM   1230 C  CD1 . PHE B 1 64  ? -6.158  18.689 95.152  1.00 18.95 ? 64  PHE B CD1 1 
ATOM   1231 C  CD2 . PHE B 1 64  ? -7.566  17.128 96.253  1.00 27.55 ? 64  PHE B CD2 1 
ATOM   1232 C  CE1 . PHE B 1 64  ? -6.154  17.888 93.990  1.00 18.48 ? 64  PHE B CE1 1 
ATOM   1233 C  CE2 . PHE B 1 64  ? -7.556  16.335 95.098  1.00 30.07 ? 64  PHE B CE2 1 
ATOM   1234 C  CZ  . PHE B 1 64  ? -6.837  16.711 93.978  1.00 22.79 ? 64  PHE B CZ  1 
ATOM   1235 N  N   . VAL B 1 65  ? -8.845  21.900 96.159  1.00 15.40 ? 65  VAL B N   1 
ATOM   1236 C  CA  . VAL B 1 65  ? -10.189 22.287 95.683  1.00 14.70 ? 65  VAL B CA  1 
ATOM   1237 C  C   . VAL B 1 65  ? -10.442 21.761 94.261  1.00 17.23 ? 65  VAL B C   1 
ATOM   1238 O  O   . VAL B 1 65  ? -9.518  21.332 93.522  1.00 16.33 ? 65  VAL B O   1 
ATOM   1239 C  CB  . VAL B 1 65  ? -10.317 23.806 95.682  1.00 16.67 ? 65  VAL B CB  1 
ATOM   1240 C  CG1 . VAL B 1 65  ? -10.244 24.380 97.078  1.00 18.75 ? 65  VAL B CG1 1 
ATOM   1241 C  CG2 . VAL B 1 65  ? -9.325  24.503 94.727  1.00 17.50 ? 65  VAL B CG2 1 
ATOM   1242 N  N   . GLU B 1 66  ? -11.692 21.713 93.811  1.00 17.85 ? 66  GLU B N   1 
ATOM   1243 C  CA  . GLU B 1 66  ? -11.961 21.354 92.463  1.00 16.79 ? 66  GLU B CA  1 
ATOM   1244 C  C   . GLU B 1 66  ? -11.157 22.190 91.500  1.00 16.76 ? 66  GLU B C   1 
ATOM   1245 O  O   . GLU B 1 66  ? -10.876 23.383 91.768  1.00 19.86 ? 66  GLU B O   1 
ATOM   1246 C  CB  . GLU B 1 66  ? -13.459 21.536 92.111  1.00 19.46 ? 66  GLU B CB  1 
ATOM   1247 C  CG  . GLU B 1 66  ? -14.339 20.602 92.878  1.00 22.16 ? 66  GLU B CG  1 
ATOM   1248 C  CD  . GLU B 1 66  ? -15.822 20.767 92.436  1.00 20.36 ? 66  GLU B CD  1 
ATOM   1249 O  OE1 . GLU B 1 66  ? -16.430 21.852 92.590  1.00 22.71 ? 66  GLU B OE1 1 
ATOM   1250 O  OE2 . GLU B 1 66  ? -16.413 19.859 91.888  1.00 25.12 ? 66  GLU B OE2 1 
ATOM   1251 N  N   . GLY B 1 67  ? -10.851 21.667 90.315  1.00 18.15 ? 67  GLY B N   1 
ATOM   1252 C  CA  . GLY B 1 67  ? -10.118 22.445 89.320  1.00 20.64 ? 67  GLY B CA  1 
ATOM   1253 C  C   . GLY B 1 67  ? -9.323  21.462 88.475  1.00 15.51 ? 67  GLY B C   1 
ATOM   1254 O  O   . GLY B 1 67  ? -9.522  20.266 88.569  1.00 17.44 ? 67  GLY B O   1 
ATOM   1255 N  N   . ILE B 1 68  ? -8.497  21.999 87.604  1.00 17.61 ? 68  ILE B N   1 
ATOM   1256 C  CA  . ILE B 1 68  ? -7.663  21.242 86.708  1.00 16.09 ? 68  ILE B CA  1 
ATOM   1257 C  C   . ILE B 1 68  ? -6.273  21.202 87.263  1.00 14.56 ? 68  ILE B C   1 
ATOM   1258 O  O   . ILE B 1 68  ? -5.719  22.241 87.567  1.00 16.00 ? 68  ILE B O   1 
ATOM   1259 C  CB  . ILE B 1 68  ? -7.674  21.822 85.289  1.00 17.44 ? 68  ILE B CB  1 
ATOM   1260 C  CG1 . ILE B 1 68  ? -9.085  21.732 84.642  1.00 23.72 ? 68  ILE B CG1 1 
ATOM   1261 C  CG2 . ILE B 1 68  ? -6.748  21.068 84.374  1.00 19.38 ? 68  ILE B CG2 1 
ATOM   1262 C  CD1 . ILE B 1 68  ? -9.244  22.449 83.363  1.00 26.40 ? 68  ILE B CD1 1 
ATOM   1263 N  N   . TYR B 1 69  ? -5.708  20.012 87.345  1.00 14.46 ? 69  TYR B N   1 
ATOM   1264 C  CA  . TYR B 1 69  ? -4.380  19.815 87.952  1.00 14.15 ? 69  TYR B CA  1 
ATOM   1265 C  C   . TYR B 1 69  ? -3.499  19.145 86.984  1.00 14.87 ? 69  TYR B C   1 
ATOM   1266 O  O   . TYR B 1 69  ? -3.957  18.342 86.172  1.00 14.11 ? 69  TYR B O   1 
ATOM   1267 C  CB  . TYR B 1 69  ? -4.518  18.952 89.206  1.00 14.51 ? 69  TYR B CB  1 
ATOM   1268 C  CG  . TYR B 1 69  ? -5.170  19.665 90.354  1.00 14.84 ? 69  TYR B CG  1 
ATOM   1269 C  CD1 . TYR B 1 69  ? -6.552  19.712 90.471  1.00 14.87 ? 69  TYR B CD1 1 
ATOM   1270 C  CD2 . TYR B 1 69  ? -4.392  20.293 91.301  1.00 14.92 ? 69  TYR B CD2 1 
ATOM   1271 C  CE1 . TYR B 1 69  ? -7.120  20.411 91.506  1.00 16.08 ? 69  TYR B CE1 1 
ATOM   1272 C  CE2 . TYR B 1 69  ? -4.971  20.987 92.334  1.00 16.32 ? 69  TYR B CE2 1 
ATOM   1273 C  CZ  . TYR B 1 69  ? -6.332  21.057 92.463  1.00 14.89 ? 69  TYR B CZ  1 
ATOM   1274 O  OH  . TYR B 1 69  ? -6.874  21.738 93.532  1.00 17.01 ? 69  TYR B OH  1 
ATOM   1275 N  N   . LYS B 1 70  ? -2.188  19.429 87.055  1.00 14.54 ? 70  LYS B N   1 
ATOM   1276 C  CA  . LYS B 1 70  ? -1.176  18.765 86.329  1.00 15.30 ? 70  LYS B CA  1 
ATOM   1277 C  C   . LYS B 1 70  ? -0.166  18.150 87.275  1.00 12.62 ? 70  LYS B C   1 
ATOM   1278 O  O   . LYS B 1 70  ? 0.393   18.821 88.133  1.00 15.79 ? 70  LYS B O   1 
ATOM   1279 C  CB  . LYS B 1 70  ? -0.456  19.803 85.400  1.00 17.00 ? 70  LYS B CB  1 
ATOM   1280 C  CG  . LYS B 1 70  ? 0.735   19.188 84.704  1.00 20.06 ? 70  LYS B CG  1 
ATOM   1281 C  CD  . LYS B 1 70  ? 1.422   19.978 83.630  1.00 21.27 ? 70  LYS B CD  1 
ATOM   1282 C  CE  . LYS B 1 70  ? 1.939   21.305 84.161  1.00 26.57 ? 70  LYS B CE  1 
ATOM   1283 N  NZ  . LYS B 1 70  ? 2.908   22.003 83.185  1.00 33.99 ? 70  LYS B NZ  1 
ATOM   1284 N  N   . VAL B 1 71  ? 0.078   16.854 87.117  1.00 14.50 ? 71  VAL B N   1 
ATOM   1285 C  CA  . VAL B 1 71  ? 1.137   16.170 87.835  1.00 15.18 ? 71  VAL B CA  1 
ATOM   1286 C  C   . VAL B 1 71  ? 2.270   15.905 86.848  1.00 15.50 ? 71  VAL B C   1 
ATOM   1287 O  O   . VAL B 1 71  ? 2.085   15.200 85.922  1.00 16.36 ? 71  VAL B O   1 
ATOM   1288 C  CB  . VAL B 1 71  ? 0.632   14.859 88.400  1.00 16.13 ? 71  VAL B CB  1 
ATOM   1289 C  CG1 . VAL B 1 71  ? 1.743   14.041 89.057  1.00 16.51 ? 71  VAL B CG1 1 
ATOM   1290 C  CG2 . VAL B 1 71  ? -0.496  15.104 89.384  1.00 16.75 ? 71  VAL B CG2 1 
ATOM   1291 N  N   . GLU B 1 72  ? 3.404   16.559 87.053  1.00 15.71 ? 72  GLU B N   1 
ATOM   1292 C  CA  . GLU B 1 72  ? 4.579   16.446 86.162  1.00 15.44 ? 72  GLU B CA  1 
ATOM   1293 C  C   . GLU B 1 72  ? 5.565   15.532 86.891  1.00 14.15 ? 72  GLU B C   1 
ATOM   1294 O  O   . GLU B 1 72  ? 6.085   15.879 87.947  1.00 14.91 ? 72  GLU B O   1 
ATOM   1295 C  CB  . GLU B 1 72  ? 5.236   17.870 85.985  1.00 20.33 ? 72  GLU B CB  1 
ATOM   1296 C  CG  . GLU B 1 72  ? 6.226   18.003 84.856  1.00 24.01 ? 72  GLU B CG  1 
ATOM   1297 C  CD  . GLU B 1 72  ? 6.473   19.485 84.377  1.00 33.70 ? 72  GLU B CD  1 
ATOM   1298 N  N   . ILE B 1 73  ? 5.861   14.386 86.305  1.00 14.93 ? 73  ILE B N   1 
ATOM   1299 C  CA  . ILE B 1 73  ? 6.804   13.412 86.862  1.00 12.66 ? 73  ILE B CA  1 
ATOM   1300 C  C   . ILE B 1 73  ? 8.101   13.515 86.072  1.00 13.93 ? 73  ILE B C   1 
ATOM   1301 O  O   . ILE B 1 73  ? 8.096   13.360 84.841  1.00 14.29 ? 73  ILE B O   1 
ATOM   1302 C  CB  . ILE B 1 73  ? 6.210   12.014 86.759  1.00 15.68 ? 73  ILE B CB  1 
ATOM   1303 C  CG1 . ILE B 1 73  ? 4.862   11.926 87.458  1.00 16.84 ? 73  ILE B CG1 1 
ATOM   1304 C  CG2 . ILE B 1 73  ? 7.166   11.027 87.326  1.00 17.08 ? 73  ILE B CG2 1 
ATOM   1305 C  CD1 . ILE B 1 73  ? 4.100   10.660 87.202  1.00 19.06 ? 73  ILE B CD1 1 
ATOM   1306 N  N   . ASP B 1 74  ? 9.216   13.791 86.740  1.00 13.05 ? 74  ASP B N   1 
ATOM   1307 C  CA  . ASP B 1 74  ? 10.468  13.978 86.040  1.00 13.82 ? 74  ASP B CA  1 
ATOM   1308 C  C   . ASP B 1 74  ? 11.145  12.640 85.697  1.00 11.79 ? 74  ASP B C   1 
ATOM   1309 O  O   . ASP B 1 74  ? 12.117  12.227 86.302  1.00 14.33 ? 74  ASP B O   1 
ATOM   1310 C  CB  . ASP B 1 74  ? 11.438  14.866 86.817  1.00 13.74 ? 74  ASP B CB  1 
ATOM   1311 C  CG  . ASP B 1 74  ? 12.692  15.198 85.988  1.00 15.22 ? 74  ASP B CG  1 
ATOM   1312 O  OD1 . ASP B 1 74  ? 12.833  14.760 84.808  1.00 17.54 ? 74  ASP B OD1 1 
ATOM   1313 O  OD2 . ASP B 1 74  ? 13.519  15.897 86.572  1.00 21.72 ? 74  ASP B OD2 1 
ATOM   1314 N  N   . THR B 1 75  ? 10.604  12.010 84.685  1.00 12.69 ? 75  THR B N   1 
ATOM   1315 C  CA  . THR B 1 75  ? 11.055  10.718 84.225  1.00 12.16 ? 75  THR B CA  1 
ATOM   1316 C  C   . THR B 1 75  ? 12.463  10.784 83.614  1.00 12.52 ? 75  THR B C   1 
ATOM   1317 O  O   . THR B 1 75  ? 13.261  9.861  83.739  1.00 11.64 ? 75  THR B O   1 
ATOM   1318 C  CB  . THR B 1 75  ? 10.050  10.105 83.283  1.00 13.67 ? 75  THR B CB  1 
ATOM   1319 O  OG1 . THR B 1 75  ? 9.897   10.959 82.151  1.00 13.21 ? 75  THR B OG1 1 
ATOM   1320 C  CG2 . THR B 1 75  ? 8.710   9.897  83.947  1.00 14.78 ? 75  THR B CG2 1 
ATOM   1321 N  N   . LYS B 1 76  ? 12.773  11.864 82.927  1.00 13.02 ? 76  LYS B N   1 
ATOM   1322 C  CA  . LYS B 1 76  ? 14.067  11.993 82.275  1.00 13.55 ? 76  LYS B CA  1 
ATOM   1323 C  C   . LYS B 1 76  ? 15.207  11.935 83.277  1.00 14.31 ? 76  LYS B C   1 
ATOM   1324 O  O   . LYS B 1 76  ? 16.169  11.223 83.088  1.00 13.24 ? 76  LYS B O   1 
ATOM   1325 C  CB  . LYS B 1 76  ? 14.138  13.285 81.442  1.00 14.63 ? 76  LYS B CB  1 
ATOM   1326 C  CG  . LYS B 1 76  ? 15.392  13.368 80.622  1.00 16.75 ? 76  LYS B CG  1 
ATOM   1327 C  CD  . LYS B 1 76  ? 15.351  14.649 79.792  1.00 19.50 ? 76  LYS B CD  1 
ATOM   1328 C  CE  . LYS B 1 76  ? 16.374  14.669 78.688  1.00 24.72 ? 76  LYS B CE  1 
ATOM   1329 N  NZ  . LYS B 1 76  ? 16.331  15.950 77.909  1.00 27.04 ? 76  LYS B NZ  1 
ATOM   1330 N  N   . SER B 1 77  ? 15.084  12.671 84.366  1.00 13.50 ? 77  SER B N   1 
ATOM   1331 C  CA  . SER B 1 77  ? 16.111  12.654 85.410  1.00 13.15 ? 77  SER B CA  1 
ATOM   1332 C  C   . SER B 1 77  ? 16.233  11.270 86.076  1.00 12.46 ? 77  SER B C   1 
ATOM   1333 O  O   . SER B 1 77  ? 17.312  10.818 86.411  1.00 15.15 ? 77  SER B O   1 
ATOM   1334 C  CB  . SER B 1 77  ? 15.865  13.752 86.480  1.00 15.37 ? 77  SER B CB  1 
ATOM   1335 O  OG  . SER B 1 77  ? 15.953  15.063 85.963  1.00 20.01 ? 77  SER B OG  1 
ATOM   1336 N  N   . TYR B 1 78  ? 15.092  10.605 86.244  1.00 12.75 ? 78  TYR B N   1 
ATOM   1337 C  CA  . TYR B 1 78  ? 15.038  9.248  86.799  1.00 13.11 ? 78  TYR B CA  1 
ATOM   1338 C  C   . TYR B 1 78  ? 15.861  8.295  85.973  1.00 12.82 ? 78  TYR B C   1 
ATOM   1339 O  O   . TYR B 1 78  ? 16.765  7.608  86.471  1.00 13.97 ? 78  TYR B O   1 
ATOM   1340 C  CB  . TYR B 1 78  ? 13.589  8.808  86.932  1.00 12.30 ? 78  TYR B CB  1 
ATOM   1341 C  CG  . TYR B 1 78  ? 13.507  7.392  87.428  1.00 11.47 ? 78  TYR B CG  1 
ATOM   1342 C  CD1 . TYR B 1 78  ? 13.729  7.089  88.782  1.00 13.04 ? 78  TYR B CD1 1 
ATOM   1343 C  CD2 . TYR B 1 78  ? 13.196  6.353  86.559  1.00 12.05 ? 78  TYR B CD2 1 
ATOM   1344 C  CE1 . TYR B 1 78  ? 13.668  5.769  89.227  1.00 14.12 ? 78  TYR B CE1 1 
ATOM   1345 C  CE2 . TYR B 1 78  ? 13.121  5.065  86.971  1.00 12.41 ? 78  TYR B CE2 1 
ATOM   1346 C  CZ  . TYR B 1 78  ? 13.375  4.755  88.302  1.00 12.82 ? 78  TYR B CZ  1 
ATOM   1347 O  OH  . TYR B 1 78  ? 13.312  3.451  88.803  1.00 14.17 ? 78  TYR B OH  1 
ATOM   1348 N  N   . TRP B 1 79  ? 15.591  8.256  84.673  1.00 13.24 ? 79  TRP B N   1 
ATOM   1349 C  CA  . TRP B 1 79  ? 16.265  7.322  83.796  1.00 13.13 ? 79  TRP B CA  1 
ATOM   1350 C  C   . TRP B 1 79  ? 17.704  7.631  83.730  1.00 13.59 ? 79  TRP B C   1 
ATOM   1351 O  O   . TRP B 1 79  ? 18.557  6.761  83.767  1.00 15.59 ? 79  TRP B O   1 
ATOM   1352 C  CB  . TRP B 1 79  ? 15.610  7.272  82.393  1.00 11.68 ? 79  TRP B CB  1 
ATOM   1353 C  CG  . TRP B 1 79  ? 14.259  6.654  82.404  1.00 11.64 ? 79  TRP B CG  1 
ATOM   1354 C  CD1 . TRP B 1 79  ? 13.093  7.252  82.048  1.00 11.37 ? 79  TRP B CD1 1 
ATOM   1355 C  CD2 . TRP B 1 79  ? 13.892  5.311  82.793  1.00 12.00 ? 79  TRP B CD2 1 
ATOM   1356 N  NE1 . TRP B 1 79  ? 12.040  6.391  82.156  1.00 10.88 ? 79  TRP B NE1 1 
ATOM   1357 C  CE2 . TRP B 1 79  ? 12.497  5.179  82.600  1.00 10.07 ? 79  TRP B CE2 1 
ATOM   1358 C  CE3 . TRP B 1 79  ? 14.598  4.199  83.261  1.00 14.50 ? 79  TRP B CE3 1 
ATOM   1359 C  CZ2 . TRP B 1 79  ? 11.823  4.006  82.919  1.00 11.35 ? 79  TRP B CZ2 1 
ATOM   1360 C  CZ3 . TRP B 1 79  ? 13.897  3.047  83.565  1.00 13.10 ? 79  TRP B CZ3 1 
ATOM   1361 C  CH2 . TRP B 1 79  ? 12.552  2.965  83.412  1.00 12.96 ? 79  TRP B CH2 1 
ATOM   1362 N  N   . LYS B 1 80  ? 18.073  8.911  83.656  1.00 13.67 ? 80  LYS B N   1 
ATOM   1363 C  CA  . LYS B 1 80  ? 19.488  9.249  83.548  1.00 15.83 ? 80  LYS B CA  1 
ATOM   1364 C  C   . LYS B 1 80  ? 20.240  8.895  84.803  1.00 15.10 ? 80  LYS B C   1 
ATOM   1365 O  O   . LYS B 1 80  ? 21.383  8.500  84.740  1.00 16.98 ? 80  LYS B O   1 
ATOM   1366 C  CB  . LYS B 1 80  ? 19.635  10.692 83.195  1.00 17.66 ? 80  LYS B CB  1 
ATOM   1367 C  CG  . LYS B 1 80  ? 19.204  10.962 81.729  1.00 22.27 ? 80  LYS B CG  1 
ATOM   1368 C  CD  . LYS B 1 80  ? 19.555  12.294 81.045  1.00 24.76 ? 80  LYS B CD  1 
ATOM   1369 C  CE  . LYS B 1 80  ? 19.663  13.499 81.949  1.00 37.21 ? 80  LYS B CE  1 
ATOM   1370 N  N   . ALA B 1 81  ? 19.611  8.985  85.955  1.00 14.33 ? 81  ALA B N   1 
ATOM   1371 C  CA  . ALA B 1 81  ? 20.288  8.628  87.187  1.00 16.16 ? 81  ALA B CA  1 
ATOM   1372 C  C   . ALA B 1 81  ? 20.540  7.090  87.255  1.00 16.10 ? 81  ALA B C   1 
ATOM   1373 O  O   . ALA B 1 81  ? 21.481  6.632  87.933  1.00 20.50 ? 81  ALA B O   1 
ATOM   1374 C  CB  . ALA B 1 81  ? 19.508  9.083  88.402  1.00 19.53 ? 81  ALA B CB  1 
ATOM   1375 N  N   . LEU B 1 82  ? 19.808  6.306  86.473  1.00 16.73 ? 82  LEU B N   1 
ATOM   1376 C  CA  . LEU B 1 82  ? 19.984  4.860  86.359  1.00 17.82 ? 82  LEU B CA  1 
ATOM   1377 C  C   . LEU B 1 82  ? 20.850  4.452  85.171  1.00 20.22 ? 82  LEU B C   1 
ATOM   1378 O  O   . LEU B 1 82  ? 21.087  3.244  84.980  1.00 20.37 ? 82  LEU B O   1 
ATOM   1379 C  CB  . LEU B 1 82  ? 18.599  4.212  86.227  1.00 18.61 ? 82  LEU B CB  1 
ATOM   1380 C  CG  . LEU B 1 82  ? 17.701  4.225  87.430  1.00 24.43 ? 82  LEU B CG  1 
ATOM   1381 C  CD1 . LEU B 1 82  ? 16.399  3.535  87.220  1.00 26.65 ? 82  LEU B CD1 1 
ATOM   1382 C  CD2 . LEU B 1 82  ? 18.488  3.568  88.541  1.00 32.24 ? 82  LEU B CD2 1 
ATOM   1383 N  N   . GLY B 1 83  ? 21.314  5.412  84.389  1.00 17.31 ? 83  GLY B N   1 
ATOM   1384 C  CA  . GLY B 1 83  ? 22.161  5.114  83.254  1.00 16.90 ? 83  GLY B CA  1 
ATOM   1385 C  C   . GLY B 1 83  ? 21.384  4.640  82.054  1.00 16.11 ? 83  GLY B C   1 
ATOM   1386 O  O   . GLY B 1 83  ? 21.949  3.970  81.179  1.00 20.33 ? 83  GLY B O   1 
ATOM   1387 N  N   . ILE B 1 84  ? 20.099  4.940  81.989  1.00 16.96 ? 84  ILE B N   1 
ATOM   1388 C  CA  . ILE B 1 84  ? 19.238  4.404  80.910  1.00 15.97 ? 84  ILE B CA  1 
ATOM   1389 C  C   . ILE B 1 84  ? 18.746  5.530  80.039  1.00 16.14 ? 84  ILE B C   1 
ATOM   1390 O  O   . ILE B 1 84  ? 18.359  6.570  80.536  1.00 15.26 ? 84  ILE B O   1 
ATOM   1391 C  CB  . ILE B 1 84  ? 18.059  3.674  81.552  1.00 14.78 ? 84  ILE B CB  1 
ATOM   1392 C  CG1 . ILE B 1 84  ? 18.525  2.383  82.237  1.00 18.81 ? 84  ILE B CG1 1 
ATOM   1393 C  CG2 . ILE B 1 84  ? 16.981  3.332  80.521  1.00 20.00 ? 84  ILE B CG2 1 
ATOM   1394 C  CD1 . ILE B 1 84  ? 17.542  1.718  83.201  1.00 19.31 ? 84  ILE B CD1 1 
ATOM   1395 N  N   . SER B 1 85  ? 18.790  5.352  78.734  1.00 16.51 ? 85  SER B N   1 
ATOM   1396 C  CA  . SER B 1 85  ? 18.465  6.385  77.779  1.00 14.80 ? 85  SER B CA  1 
ATOM   1397 C  C   . SER B 1 85  ? 16.921  6.599  77.617  1.00 14.21 ? 85  SER B C   1 
ATOM   1398 O  O   . SER B 1 85  ? 16.222  5.695  77.233  1.00 14.49 ? 85  SER B O   1 
ATOM   1399 C  CB  . SER B 1 85  ? 18.989  6.047  76.432  1.00 19.65 ? 85  SER B CB  1 
ATOM   1400 O  OG  . SER B 1 85  ? 18.764  7.102  75.540  1.00 22.88 ? 85  SER B OG  1 
ATOM   1401 N  N   . PRO B 1 86  ? 16.400  7.799  77.958  1.00 14.30 ? 86  PRO B N   1 
ATOM   1402 C  CA  . PRO B 1 86  ? 14.976  8.029  77.948  1.00 13.84 ? 86  PRO B CA  1 
ATOM   1403 C  C   . PRO B 1 86  ? 14.462  8.782  76.709  1.00 13.06 ? 86  PRO B C   1 
ATOM   1404 O  O   . PRO B 1 86  ? 15.178  9.605  76.156  1.00 17.74 ? 86  PRO B O   1 
ATOM   1405 C  CB  . PRO B 1 86  ? 14.739  8.945  79.175  1.00 15.82 ? 86  PRO B CB  1 
ATOM   1406 C  CG  . PRO B 1 86  ? 15.991  9.761  79.224  1.00 15.63 ? 86  PRO B CG  1 
ATOM   1407 C  CD  . PRO B 1 86  ? 17.097  8.895  78.683  1.00 16.29 ? 86  PRO B CD  1 
ATOM   1408 N  N   . PHE B 1 87  ? 13.177  8.641  76.354  1.00 11.78 ? 87  PHE B N   1 
ATOM   1409 C  CA  . PHE B 1 87  ? 12.538  9.392  75.269  1.00 12.58 ? 87  PHE B CA  1 
ATOM   1410 C  C   . PHE B 1 87  ? 11.848  10.645 75.727  1.00 12.06 ? 87  PHE B C   1 
ATOM   1411 O  O   . PHE B 1 87  ? 12.060  11.712 75.123  1.00 12.93 ? 87  PHE B O   1 
ATOM   1412 C  CB  . PHE B 1 87  ? 11.472  8.497  74.630  1.00 13.34 ? 87  PHE B CB  1 
ATOM   1413 C  CG  . PHE B 1 87  ? 10.652  9.185  73.562  1.00 13.28 ? 87  PHE B CG  1 
ATOM   1414 C  CD1 . PHE B 1 87  ? 11.168  9.499  72.358  1.00 15.22 ? 87  PHE B CD1 1 
ATOM   1415 C  CD2 . PHE B 1 87  ? 9.336   9.528  73.821  1.00 13.95 ? 87  PHE B CD2 1 
ATOM   1416 C  CE1 . PHE B 1 87  ? 10.420  10.151 71.400  1.00 16.82 ? 87  PHE B CE1 1 
ATOM   1417 C  CE2 . PHE B 1 87  ? 8.577   10.193 72.879  1.00 17.32 ? 87  PHE B CE2 1 
ATOM   1418 C  CZ  . PHE B 1 87  ? 9.140   10.463 71.670  1.00 16.55 ? 87  PHE B CZ  1 
ATOM   1419 N  N   . HIS B 1 88  ? 11.019  10.605 76.770  1.00 13.02 ? 88  HIS B N   1 
ATOM   1420 C  CA  . HIS B 1 88  ? 10.220  11.746 77.148  1.00 13.30 ? 88  HIS B CA  1 
ATOM   1421 C  C   . HIS B 1 88  ? 10.997  12.718 78.001  1.00 13.70 ? 88  HIS B C   1 
ATOM   1422 O  O   . HIS B 1 88  ? 11.939  12.368 78.768  1.00 16.17 ? 88  HIS B O   1 
ATOM   1423 C  CB  . HIS B 1 88  ? 9.032   11.275 77.968  1.00 14.12 ? 88  HIS B CB  1 
ATOM   1424 C  CG  . HIS B 1 88  ? 8.163   10.252 77.282  1.00 15.08 ? 88  HIS B CG  1 
ATOM   1425 N  ND1 . HIS B 1 88  ? 8.295   8.900  77.449  1.00 17.98 ? 88  HIS B ND1 1 
ATOM   1426 C  CD2 . HIS B 1 88  ? 7.163   10.421 76.378  1.00 20.19 ? 88  HIS B CD2 1 
ATOM   1427 C  CE1 . HIS B 1 88  ? 7.390   8.293  76.711  1.00 22.98 ? 88  HIS B CE1 1 
ATOM   1428 N  NE2 . HIS B 1 88  ? 6.672   9.178  76.063  1.00 27.26 ? 88  HIS B NE2 1 
ATOM   1429 N  N   . GLU B 1 89  ? 10.601  13.980 77.957  1.00 13.94 ? 89  GLU B N   1 
ATOM   1430 C  CA  . GLU B 1 89  ? 11.114  14.980 78.836  1.00 14.95 ? 89  GLU B CA  1 
ATOM   1431 C  C   . GLU B 1 89  ? 10.627  14.701 80.262  1.00 15.37 ? 89  GLU B C   1 
ATOM   1432 O  O   . GLU B 1 89  ? 11.337  14.965 81.246  1.00 19.25 ? 89  GLU B O   1 
ATOM   1433 C  CB  . GLU B 1 89  ? 10.805  16.446 78.400  1.00 16.67 ? 89  GLU B CB  1 
ATOM   1434 C  CG  . GLU B 1 89  ? 11.564  16.930 77.216  1.00 18.63 ? 89  GLU B CG  1 
ATOM   1435 C  CD  . GLU B 1 89  ? 13.029  17.022 77.480  1.00 21.83 ? 89  GLU B CD  1 
ATOM   1436 O  OE1 . GLU B 1 89  ? 13.476  17.899 78.257  1.00 27.77 ? 89  GLU B OE1 1 
ATOM   1437 O  OE2 . GLU B 1 89  ? 13.798  16.277 76.836  1.00 19.19 ? 89  GLU B OE2 1 
ATOM   1438 N  N   . HIS B 1 90  ? 9.382   14.322 80.394  1.00 14.83 ? 90  HIS B N   1 
ATOM   1439 C  CA  . HIS B 1 90  ? 8.712   14.118 81.627  1.00 15.84 ? 90  HIS B CA  1 
ATOM   1440 C  C   . HIS B 1 90  ? 7.467   13.533 81.291  1.00 15.67 ? 90  HIS B C   1 
ATOM   1441 O  O   . HIS B 1 90  ? 7.159   13.439 80.124  1.00 19.83 ? 90  HIS B O   1 
ATOM   1442 C  CB  . HIS B 1 90  ? 8.541   15.419 82.447  1.00 18.70 ? 90  HIS B CB  1 
ATOM   1443 C  CG  . HIS B 1 90  ? 8.059   16.624 81.715  1.00 20.79 ? 90  HIS B CG  1 
ATOM   1444 N  ND1 . HIS B 1 90  ? 6.777   16.789 81.302  1.00 27.90 ? 90  HIS B ND1 1 
ATOM   1445 C  CD2 . HIS B 1 90  ? 8.730   17.712 81.277  1.00 23.19 ? 90  HIS B CD2 1 
ATOM   1446 C  CE1 . HIS B 1 90  ? 6.649   17.915 80.643  1.00 24.91 ? 90  HIS B CE1 1 
ATOM   1447 N  NE2 . HIS B 1 90  ? 7.823   18.512 80.633  1.00 30.68 ? 90  HIS B NE2 1 
ATOM   1448 N  N   . ALA B 1 91  ? 6.697   13.151 82.282  1.00 16.47 ? 91  ALA B N   1 
ATOM   1449 C  CA  . ALA B 1 91  ? 5.289   12.785 82.049  1.00 18.20 ? 91  ALA B CA  1 
ATOM   1450 C  C   . ALA B 1 91  ? 4.420   13.801 82.684  1.00 19.20 ? 91  ALA B C   1 
ATOM   1451 O  O   . ALA B 1 91  ? 4.677   14.140 83.809  1.00 25.16 ? 91  ALA B O   1 
ATOM   1452 C  CB  . ALA B 1 91  ? 5.043   11.402 82.666  1.00 19.85 ? 91  ALA B CB  1 
ATOM   1453 N  N   . GLU B 1 92  ? 3.408   14.297 81.984  1.00 19.71 ? 92  GLU B N   1 
ATOM   1454 C  CA  . GLU B 1 92  ? 2.481   15.335 82.447  1.00 22.12 ? 92  GLU B CA  1 
ATOM   1455 C  C   . GLU B 1 92  ? 1.103   14.705 82.493  1.00 19.45 ? 92  GLU B C   1 
ATOM   1456 O  O   . GLU B 1 92  ? 0.523   14.391 81.422  1.00 27.16 ? 92  GLU B O   1 
ATOM   1457 C  CB  . GLU B 1 92  ? 2.383   16.495 81.406  1.00 29.69 ? 92  GLU B CB  1 
ATOM   1458 C  CG  . GLU B 1 92  ? 3.499   17.505 81.361  0.50 26.95 ? 92  GLU B CG  1 
ATOM   1459 C  CD  . GLU B 1 92  ? 3.293   18.719 80.425  0.50 20.87 ? 92  GLU B CD  1 
ATOM   1460 O  OE1 . GLU B 1 92  ? 2.207   19.193 79.991  0.50 26.13 ? 92  GLU B OE1 1 
ATOM   1461 O  OE2 . GLU B 1 92  ? 4.340   19.263 80.076  0.50 23.32 ? 92  GLU B OE2 1 
ATOM   1462 N  N   . VAL B 1 93  ? 0.537   14.504 83.674  1.00 15.73 ? 93  VAL B N   1 
ATOM   1463 C  CA  . VAL B 1 93  ? -0.741  13.882 83.822  1.00 16.66 ? 93  VAL B CA  1 
ATOM   1464 C  C   . VAL B 1 93  ? -1.760  14.978 84.227  1.00 14.70 ? 93  VAL B C   1 
ATOM   1465 O  O   . VAL B 1 93  ? -1.650  15.523 85.288  1.00 14.37 ? 93  VAL B O   1 
ATOM   1466 C  CB  . VAL B 1 93  ? -0.691  12.785 84.824  1.00 17.60 ? 93  VAL B CB  1 
ATOM   1467 C  CG1 . VAL B 1 93  ? -2.069  12.102 85.051  1.00 16.05 ? 93  VAL B CG1 1 
ATOM   1468 C  CG2 . VAL B 1 93  ? 0.414   11.808 84.531  1.00 20.61 ? 93  VAL B CG2 1 
ATOM   1469 N  N   . VAL B 1 94  ? -2.710  15.303 83.340  1.00 15.88 ? 94  VAL B N   1 
ATOM   1470 C  CA  . VAL B 1 94  ? -3.563  16.458 83.601  1.00 14.99 ? 94  VAL B CA  1 
ATOM   1471 C  C   . VAL B 1 94  ? -4.998  15.973 83.741  1.00 13.98 ? 94  VAL B C   1 
ATOM   1472 O  O   . VAL B 1 94  ? -5.514  15.237 82.906  1.00 14.23 ? 94  VAL B O   1 
ATOM   1473 C  CB  . VAL B 1 94  ? -3.437  17.452 82.372  1.00 15.80 ? 94  VAL B CB  1 
ATOM   1474 C  CG1 . VAL B 1 94  ? -4.324  18.661 82.632  1.00 19.22 ? 94  VAL B CG1 1 
ATOM   1475 C  CG2 . VAL B 1 94  ? -1.992  17.947 82.158  1.00 19.54 ? 94  VAL B CG2 1 
ATOM   1476 N  N   . PHE B 1 95  ? -5.692  16.448 84.769  1.00 14.23 ? 95  PHE B N   1 
ATOM   1477 C  CA  . PHE B 1 95  ? -7.014  15.914 85.116  1.00 15.79 ? 95  PHE B CA  1 
ATOM   1478 C  C   . PHE B 1 95  ? -7.860  16.918 85.847  1.00 15.67 ? 95  PHE B C   1 
ATOM   1479 O  O   . PHE B 1 95  ? -7.354  17.871 86.414  1.00 14.70 ? 95  PHE B O   1 
ATOM   1480 C  CB  . PHE B 1 95  ? -6.918  14.649 85.968  1.00 16.26 ? 95  PHE B CB  1 
ATOM   1481 C  CG  . PHE B 1 95  ? -6.320  14.886 87.338  1.00 15.04 ? 95  PHE B CG  1 
ATOM   1482 C  CD1 . PHE B 1 95  ? -4.924  14.822 87.530  1.00 20.03 ? 95  PHE B CD1 1 
ATOM   1483 C  CD2 . PHE B 1 95  ? -7.134  15.030 88.434  1.00 17.15 ? 95  PHE B CD2 1 
ATOM   1484 C  CE1 . PHE B 1 95  ? -4.385  15.045 88.803  1.00 19.43 ? 95  PHE B CE1 1 
ATOM   1485 C  CE2 . PHE B 1 95  ? -6.610  15.186 89.689  1.00 21.03 ? 95  PHE B CE2 1 
ATOM   1486 C  CZ  . PHE B 1 95  ? -5.245  15.216 89.890  1.00 21.52 ? 95  PHE B CZ  1 
ATOM   1487 N  N   . THR B 1 96  ? -9.150  16.650 85.859  1.00 18.08 ? 96  THR B N   1 
ATOM   1488 C  CA  . THR B 1 96  ? -10.074 17.542 86.583  1.00 18.75 ? 96  THR B CA  1 
ATOM   1489 C  C   . THR B 1 96  ? -10.472 16.881 87.894  1.00 18.71 ? 96  THR B C   1 
ATOM   1490 O  O   . THR B 1 96  ? -10.873 15.726 87.872  1.00 22.98 ? 96  THR B O   1 
ATOM   1491 C  CB  . THR B 1 96  ? -11.314 17.870 85.735  1.00 19.89 ? 96  THR B CB  1 
ATOM   1492 O  OG1 . THR B 1 96  ? -10.940 18.662 84.613  1.00 23.30 ? 96  THR B OG1 1 
ATOM   1493 C  CG2 . THR B 1 96  ? -12.358 18.625 86.526  1.00 26.61 ? 96  THR B CG2 1 
ATOM   1494 N  N   . ALA B 1 97  ? -10.298 17.600 88.996  1.00 17.25 ? 97  ALA B N   1 
ATOM   1495 C  CA  . ALA B 1 97  ? -10.791 17.112 90.295  1.00 17.05 ? 97  ALA B CA  1 
ATOM   1496 C  C   . ALA B 1 97  ? -12.241 17.576 90.482  1.00 22.60 ? 97  ALA B C   1 
ATOM   1497 O  O   . ALA B 1 97  ? -12.495 18.763 90.378  1.00 19.33 ? 97  ALA B O   1 
ATOM   1498 C  CB  . ALA B 1 97  ? -9.940  17.656 91.394  1.00 21.37 ? 97  ALA B CB  1 
ATOM   1499 N  N   . ASN B 1 98  ? -13.137 16.631 90.734  1.00 24.12 ? 98  ASN B N   1 
ATOM   1500 C  CA  . ASN B 1 98  ? -14.580 16.931 90.928  1.00 23.24 ? 98  ASN B CA  1 
ATOM   1501 C  C   . ASN B 1 98  ? -15.004 16.446 92.325  1.00 26.03 ? 98  ASN B C   1 
ATOM   1502 O  O   . ASN B 1 98  ? -14.681 15.314 92.665  1.00 30.93 ? 98  ASN B O   1 
ATOM   1503 C  CB  . ASN B 1 98  ? -15.401 16.271 89.820  1.00 30.43 ? 98  ASN B CB  1 
ATOM   1504 N  N   . GLY B 1 101 ? -18.849 13.482 96.114  1.00 38.66 ? 101 GLY B N   1 
ATOM   1505 C  CA  . GLY B 1 101 ? -18.822 13.116 97.535  1.00 36.56 ? 101 GLY B CA  1 
ATOM   1506 C  C   . GLY B 1 101 ? -17.402 12.851 98.018  1.00 34.20 ? 101 GLY B C   1 
ATOM   1507 O  O   . GLY B 1 101 ? -16.470 13.386 97.396  1.00 37.80 ? 101 GLY B O   1 
ATOM   1508 N  N   . PRO B 1 102 ? -17.193 12.088 99.112  1.00 33.16 ? 102 PRO B N   1 
ATOM   1509 C  CA  . PRO B 1 102 ? -15.862 11.871 99.664  1.00 31.75 ? 102 PRO B CA  1 
ATOM   1510 C  C   . PRO B 1 102 ? -14.927 11.167 98.663  1.00 35.23 ? 102 PRO B C   1 
ATOM   1511 O  O   . PRO B 1 102 ? -15.295 10.124 98.166  1.00 42.19 ? 102 PRO B O   1 
ATOM   1512 C  CB  . PRO B 1 102 ? -16.136 10.976 100.872 1.00 35.76 ? 102 PRO B CB  1 
ATOM   1513 C  CG  . PRO B 1 102 ? -17.571 11.246 101.228 1.00 34.79 ? 102 PRO B CG  1 
ATOM   1514 C  CD  . PRO B 1 102 ? -18.239 11.422 99.885  1.00 32.04 ? 102 PRO B CD  1 
ATOM   1515 N  N   . ARG B 1 103 ? -13.737 11.728 98.437  1.00 32.04 ? 103 ARG B N   1 
ATOM   1516 C  CA  . ARG B 1 103 ? -12.838 11.163 97.395  1.00 27.98 ? 103 ARG B CA  1 
ATOM   1517 C  C   . ARG B 1 103 ? -11.344 11.329 97.705  1.00 33.34 ? 103 ARG B C   1 
ATOM   1518 O  O   . ARG B 1 103 ? -10.921 12.404 98.154  1.00 35.26 ? 103 ARG B O   1 
ATOM   1519 C  CB  . ARG B 1 103 ? -13.121 11.817 96.039  1.00 34.52 ? 103 ARG B CB  1 
ATOM   1520 N  N   . ARG B 1 104 ? -10.574 10.281 97.439  1.00 22.96 ? 104 ARG B N   1 
ATOM   1521 C  CA  . ARG B 1 104 ? -9.108  10.350 97.544  1.00 24.29 ? 104 ARG B CA  1 
ATOM   1522 C  C   . ARG B 1 104 ? -8.595  9.969  96.157  1.00 22.50 ? 104 ARG B C   1 
ATOM   1523 O  O   . ARG B 1 104 ? -9.168  9.068  95.548  1.00 21.14 ? 104 ARG B O   1 
ATOM   1524 C  CB  . ARG B 1 104 ? -8.583  9.379  98.591  1.00 33.47 ? 104 ARG B CB  1 
ATOM   1525 N  N   . TYR B 1 105 ? -7.546  10.641 95.717  1.00 18.80 ? 105 TYR B N   1 
ATOM   1526 C  CA  . TYR B 1 105 ? -7.012  10.398 94.363  1.00 17.74 ? 105 TYR B CA  1 
ATOM   1527 C  C   . TYR B 1 105 ? -5.611  9.834  94.441  1.00 17.08 ? 105 TYR B C   1 
ATOM   1528 O  O   . TYR B 1 105 ? -4.779  10.357 95.163  1.00 18.75 ? 105 TYR B O   1 
ATOM   1529 C  CB  . TYR B 1 105 ? -6.898  11.703 93.579  1.00 19.34 ? 105 TYR B CB  1 
ATOM   1530 C  CG  . TYR B 1 105 ? -8.193  12.384 93.230  1.00 18.41 ? 105 TYR B CG  1 
ATOM   1531 C  CD1 . TYR B 1 105 ? -8.931  13.052 94.191  1.00 22.20 ? 105 TYR B CD1 1 
ATOM   1532 C  CD2 . TYR B 1 105 ? -8.672  12.373 91.933  1.00 23.67 ? 105 TYR B CD2 1 
ATOM   1533 C  CE1 . TYR B 1 105 ? -10.119 13.683 93.873  1.00 25.53 ? 105 TYR B CE1 1 
ATOM   1534 C  CE2 . TYR B 1 105 ? -9.858  13.000 91.597  1.00 27.95 ? 105 TYR B CE2 1 
ATOM   1535 C  CZ  . TYR B 1 105 ? -10.584 13.655 92.571  1.00 24.24 ? 105 TYR B CZ  1 
ATOM   1536 O  OH  . TYR B 1 105 ? -11.750 14.278 92.244  1.00 30.47 ? 105 TYR B OH  1 
ATOM   1537 N  N   . THR B 1 106 ? -5.398  8.735  93.744  1.00 14.67 ? 106 THR B N   1 
ATOM   1538 C  CA  . THR B 1 106 ? -4.045  8.209  93.556  1.00 12.71 ? 106 THR B CA  1 
ATOM   1539 C  C   . THR B 1 106 ? -3.761  8.264  92.072  1.00 13.24 ? 106 THR B C   1 
ATOM   1540 O  O   . THR B 1 106 ? -4.500  7.735  91.250  1.00 15.84 ? 106 THR B O   1 
ATOM   1541 C  CB  . THR B 1 106 ? -3.860  6.776  94.024  1.00 15.53 ? 106 THR B CB  1 
ATOM   1542 O  OG1 . THR B 1 106 ? -4.077  6.737  95.438  1.00 20.44 ? 106 THR B OG1 1 
ATOM   1543 C  CG2 . THR B 1 106 ? -2.558  6.299  93.725  1.00 17.49 ? 106 THR B CG2 1 
ATOM   1544 N  N   . ILE B 1 107 ? -2.653  8.905  91.752  1.00 12.29 ? 107 ILE B N   1 
ATOM   1545 C  CA  . ILE B 1 107 ? -2.178  8.942  90.377  1.00 12.49 ? 107 ILE B CA  1 
ATOM   1546 C  C   . ILE B 1 107 ? -1.047  7.955  90.312  1.00 13.73 ? 107 ILE B C   1 
ATOM   1547 O  O   . ILE B 1 107 ? -0.011  8.147  90.917  1.00 14.80 ? 107 ILE B O   1 
ATOM   1548 C  CB  . ILE B 1 107 ? -1.654  10.346 89.968  1.00 15.38 ? 107 ILE B CB  1 
ATOM   1549 C  CG1 . ILE B 1 107 ? -2.750  11.397 90.111  1.00 17.66 ? 107 ILE B CG1 1 
ATOM   1550 C  CG2 . ILE B 1 107 ? -1.026  10.318 88.591  1.00 16.49 ? 107 ILE B CG2 1 
ATOM   1551 C  CD1 . ILE B 1 107 ? -4.067  11.123 89.387  1.00 16.52 ? 107 ILE B CD1 1 
ATOM   1552 N  N   . ALA B 1 108 ? -1.228  6.899  89.562  1.00 11.89 ? 108 ALA B N   1 
ATOM   1553 C  CA  . ALA B 1 108 ? -0.240  5.848  89.457  1.00 14.91 ? 108 ALA B CA  1 
ATOM   1554 C  C   . ALA B 1 108 ? 0.377   5.866  88.066  1.00 13.27 ? 108 ALA B C   1 
ATOM   1555 O  O   . ALA B 1 108 ? -0.307  6.045  87.060  1.00 16.59 ? 108 ALA B O   1 
ATOM   1556 C  CB  . ALA B 1 108 ? -0.945  4.527  89.675  1.00 17.10 ? 108 ALA B CB  1 
ATOM   1557 N  N   . ALA B 1 109 ? 1.675   5.692  87.984  1.00 11.85 ? 109 ALA B N   1 
ATOM   1558 C  CA  . ALA B 1 109 ? 2.358   5.677  86.691  1.00 11.91 ? 109 ALA B CA  1 
ATOM   1559 C  C   . ALA B 1 109 ? 3.335   4.534  86.628  1.00 11.11 ? 109 ALA B C   1 
ATOM   1560 O  O   . ALA B 1 109 ? 4.010   4.229  87.620  1.00 13.20 ? 109 ALA B O   1 
ATOM   1561 C  CB  . ALA B 1 109 ? 3.110   7.011  86.483  1.00 14.56 ? 109 ALA B CB  1 
ATOM   1562 N  N   . LEU B 1 110 ? 3.407   3.934  85.442  1.00 10.32 ? 110 LEU B N   1 
ATOM   1563 C  CA  . LEU B 1 110 ? 4.327   2.849  85.151  1.00 9.42  ? 110 LEU B CA  1 
ATOM   1564 C  C   . LEU B 1 110 ? 5.252   3.294  84.053  1.00 9.63  ? 110 LEU B C   1 
ATOM   1565 O  O   . LEU B 1 110 ? 4.809   3.667  82.980  1.00 10.72 ? 110 LEU B O   1 
ATOM   1566 C  CB  . LEU B 1 110 ? 3.501   1.609  84.703  1.00 12.34 ? 110 LEU B CB  1 
ATOM   1567 C  CG  . LEU B 1 110 ? 4.351   0.404  84.240  1.00 12.18 ? 110 LEU B CG  1 
ATOM   1568 C  CD1 . LEU B 1 110 ? 5.200   -0.161 85.429  1.00 11.84 ? 110 LEU B CD1 1 
ATOM   1569 C  CD2 . LEU B 1 110 ? 3.469   -0.743 83.738  1.00 15.57 ? 110 LEU B CD2 1 
ATOM   1570 N  N   . LEU B 1 111 ? 6.549   3.312  84.310  1.00 9.70  ? 111 LEU B N   1 
ATOM   1571 C  CA  . LEU B 1 111 ? 7.524   3.897  83.437  1.00 9.59  ? 111 LEU B CA  1 
ATOM   1572 C  C   . LEU B 1 111 ? 8.393   2.914  82.681  1.00 9.50  ? 111 LEU B C   1 
ATOM   1573 O  O   . LEU B 1 111 ? 8.949   2.000  83.295  1.00 9.98  ? 111 LEU B O   1 
ATOM   1574 C  CB  . LEU B 1 111 ? 8.462   4.838  84.225  1.00 10.78 ? 111 LEU B CB  1 
ATOM   1575 C  CG  . LEU B 1 111 ? 7.880   5.865  85.185  1.00 11.76 ? 111 LEU B CG  1 
ATOM   1576 C  CD1 . LEU B 1 111 ? 9.018   6.661  85.820  1.00 13.19 ? 111 LEU B CD1 1 
ATOM   1577 C  CD2 . LEU B 1 111 ? 6.887   6.711  84.478  1.00 12.04 ? 111 LEU B CD2 1 
ATOM   1578 N  N   . SER B 1 112 ? 8.554   3.162  81.417  1.00 9.81  ? 112 SER B N   1 
ATOM   1579 C  CA  . SER B 1 112 ? 9.577   2.557  80.562  1.00 10.22 ? 112 SER B CA  1 
ATOM   1580 C  C   . SER B 1 112 ? 10.265  3.704  79.786  1.00 10.47 ? 112 SER B C   1 
ATOM   1581 O  O   . SER B 1 112 ? 9.821   4.800  79.746  1.00 11.61 ? 112 SER B O   1 
ATOM   1582 C  CB  . SER B 1 112 ? 8.976   1.545  79.553  1.00 10.88 ? 112 SER B CB  1 
ATOM   1583 O  OG  . SER B 1 112 ? 8.339   0.501  80.206  1.00 13.60 ? 112 SER B OG  1 
ATOM   1584 N  N   . PRO B 1 113 ? 11.428  3.403  79.231  1.00 10.06 ? 113 PRO B N   1 
ATOM   1585 C  CA  . PRO B 1 113 ? 12.187  4.465  78.600  1.00 10.19 ? 113 PRO B CA  1 
ATOM   1586 C  C   . PRO B 1 113 ? 11.502  5.143  77.446  1.00 11.22 ? 113 PRO B C   1 
ATOM   1587 O  O   . PRO B 1 113 ? 11.691  6.337  77.330  1.00 11.77 ? 113 PRO B O   1 
ATOM   1588 C  CB  . PRO B 1 113 ? 13.521  3.758  78.212  1.00 12.89 ? 113 PRO B CB  1 
ATOM   1589 C  CG  . PRO B 1 113 ? 13.674  2.712  79.280  1.00 13.32 ? 113 PRO B CG  1 
ATOM   1590 C  CD  . PRO B 1 113 ? 12.265  2.187  79.415  1.00 11.38 ? 113 PRO B CD  1 
ATOM   1591 N  N   . TYR B 1 114 ? 10.732  4.430  76.660  1.00 10.97 ? 114 TYR B N   1 
ATOM   1592 C  CA  . TYR B 1 114 ? 10.046  4.986  75.487  1.00 10.37 ? 114 TYR B CA  1 
ATOM   1593 C  C   . TYR B 1 114 ? 8.543   4.875  75.615  1.00 11.01 ? 114 TYR B C   1 
ATOM   1594 O  O   . TYR B 1 114 ? 7.828   5.093  74.640  1.00 13.06 ? 114 TYR B O   1 
ATOM   1595 C  CB  . TYR B 1 114 ? 10.515  4.334  74.203  1.00 11.41 ? 114 TYR B CB  1 
ATOM   1596 C  CG  . TYR B 1 114 ? 11.794  4.926  73.659  1.00 10.55 ? 114 TYR B CG  1 
ATOM   1597 C  CD1 . TYR B 1 114 ? 12.980  4.791  74.368  1.00 14.71 ? 114 TYR B CD1 1 
ATOM   1598 C  CD2 . TYR B 1 114 ? 11.806  5.684  72.532  1.00 10.88 ? 114 TYR B CD2 1 
ATOM   1599 C  CE1 . TYR B 1 114 ? 14.168  5.324  73.861  1.00 21.26 ? 114 TYR B CE1 1 
ATOM   1600 C  CE2 . TYR B 1 114 ? 12.989  6.234  72.062  1.00 11.92 ? 114 TYR B CE2 1 
ATOM   1601 C  CZ  . TYR B 1 114 ? 14.159  6.043  72.720  1.00 18.50 ? 114 TYR B CZ  1 
ATOM   1602 O  OH  . TYR B 1 114 ? 15.304  6.574  72.241  1.00 36.38 ? 114 TYR B OH  1 
ATOM   1603 N  N   . SER B 1 115 ? 8.025   4.686  76.842  1.00 10.72 ? 115 SER B N   1 
ATOM   1604 C  CA  . SER B 1 115 ? 6.604   4.551  77.066  1.00 9.60  ? 115 SER B CA  1 
ATOM   1605 C  C   . SER B 1 115 ? 6.303   4.804  78.503  1.00 10.52 ? 115 SER B C   1 
ATOM   1606 O  O   . SER B 1 115 ? 7.052   4.489  79.372  1.00 12.68 ? 115 SER B O   1 
ATOM   1607 C  CB  . SER B 1 115 ? 6.168   3.146  76.715  1.00 11.32 ? 115 SER B CB  1 
ATOM   1608 O  OG  . SER B 1 115 ? 4.808   2.921  76.847  1.00 14.72 ? 115 SER B OG  1 
ATOM   1609 N  N   . TYR B 1 116 ? 5.138   5.381  78.757  1.00 10.26 ? 116 TYR B N   1 
ATOM   1610 C  CA  A TYR B 1 116 ? 4.577   5.341  80.123  0.50 9.21  ? 116 TYR B CA  1 
ATOM   1611 C  CA  B TYR B 1 116 ? 4.586   5.362  80.107  0.50 9.19  ? 116 TYR B CA  1 
ATOM   1612 C  C   . TYR B 1 116 ? 3.058   5.154  80.116  1.00 9.77  ? 116 TYR B C   1 
ATOM   1613 O  O   . TYR B 1 116 ? 2.403   5.451  79.109  1.00 9.77  ? 116 TYR B O   1 
ATOM   1614 C  CB  A TYR B 1 116 ? 4.900   6.558  80.988  0.50 10.88 ? 116 TYR B CB  1 
ATOM   1615 C  CB  B TYR B 1 116 ? 4.970   6.618  80.881  0.50 10.91 ? 116 TYR B CB  1 
ATOM   1616 C  CG  A TYR B 1 116 ? 4.301   7.868  80.504  0.50 12.44 ? 116 TYR B CG  1 
ATOM   1617 C  CG  B TYR B 1 116 ? 4.170   7.916  80.598  0.50 11.88 ? 116 TYR B CG  1 
ATOM   1618 C  CD1 A TYR B 1 116 ? 5.000   8.602  79.581  0.50 15.80 ? 116 TYR B CD1 1 
ATOM   1619 C  CD1 B TYR B 1 116 ? 3.025   8.156  81.311  0.50 14.59 ? 116 TYR B CD1 1 
ATOM   1620 C  CD2 A TYR B 1 116 ? 3.087   8.322  80.913  0.50 15.49 ? 116 TYR B CD2 1 
ATOM   1621 C  CD2 B TYR B 1 116 ? 4.580   8.885  79.678  0.50 13.24 ? 116 TYR B CD2 1 
ATOM   1622 C  CE1 A TYR B 1 116 ? 4.543   9.753  79.062  0.50 20.36 ? 116 TYR B CE1 1 
ATOM   1623 C  CE1 B TYR B 1 116 ? 2.261   9.341  81.161  0.50 16.79 ? 116 TYR B CE1 1 
ATOM   1624 C  CE2 A TYR B 1 116 ? 2.609   9.551  80.425  0.50 21.42 ? 116 TYR B CE2 1 
ATOM   1625 C  CE2 B TYR B 1 116 ? 3.797   10.053 79.480  0.50 14.49 ? 116 TYR B CE2 1 
ATOM   1626 C  CZ  A TYR B 1 116 ? 3.376   10.225 79.477  0.50 19.01 ? 116 TYR B CZ  1 
ATOM   1627 C  CZ  B TYR B 1 116 ? 2.625   10.244 80.253  0.50 16.69 ? 116 TYR B CZ  1 
ATOM   1628 O  OH  A TYR B 1 116 ? 3.007   11.411 78.929  0.50 27.62 ? 116 TYR B OH  1 
ATOM   1629 O  OH  B TYR B 1 116 ? 1.806   11.349 80.154  0.50 18.49 ? 116 TYR B OH  1 
ATOM   1630 N  N   . SER B 1 117 ? 2.580   4.640  81.215  1.00 9.71  ? 117 SER B N   1 
ATOM   1631 C  CA  . SER B 1 117 ? 1.135   4.491  81.428  1.00 9.92  ? 117 SER B CA  1 
ATOM   1632 C  C   . SER B 1 117 ? 0.781   5.158  82.744  1.00 10.80 ? 117 SER B C   1 
ATOM   1633 O  O   . SER B 1 117 ? 1.588   5.180  83.647  1.00 12.49 ? 117 SER B O   1 
ATOM   1634 C  CB  . SER B 1 117 ? 0.750   3.032  81.412  1.00 18.38 ? 117 SER B CB  1 
ATOM   1635 O  OG  . SER B 1 117 ? 0.868   2.452  82.689  1.00 30.11 ? 117 SER B OG  1 
ATOM   1636 N  N   . THR B 1 118 ? -0.405  5.731  82.766  1.00 10.66 ? 118 THR B N   1 
ATOM   1637 C  CA  . THR B 1 118 ? -0.870  6.298  84.008  1.00 11.43 ? 118 THR B CA  1 
ATOM   1638 C  C   . THR B 1 118 ? -2.332  5.932  84.168  1.00 12.85 ? 118 THR B C   1 
ATOM   1639 O  O   . THR B 1 118 ? -3.109  5.836  83.201  1.00 15.35 ? 118 THR B O   1 
ATOM   1640 C  CB  . THR B 1 118 ? -0.595  7.800  84.014  1.00 11.97 ? 118 THR B CB  1 
ATOM   1641 O  OG1 . THR B 1 118 ? -0.922  8.276  85.308  1.00 14.54 ? 118 THR B OG1 1 
ATOM   1642 C  CG2 . THR B 1 118 ? -1.362  8.599  82.975  1.00 14.01 ? 118 THR B CG2 1 
ATOM   1643 N  N   . THR B 1 119 ? -2.711  5.763  85.402  1.00 12.11 ? 119 THR B N   1 
ATOM   1644 C  CA  A THR B 1 119 ? -4.131  5.549  85.798  0.50 12.39 ? 119 THR B CA  1 
ATOM   1645 C  CA  B THR B 1 119 ? -4.121  5.498  85.775  0.50 12.31 ? 119 THR B CA  1 
ATOM   1646 C  C   . THR B 1 119 ? -4.515  6.274  87.053  1.00 10.95 ? 119 THR B C   1 
ATOM   1647 O  O   . THR B 1 119 ? -3.622  6.694  87.783  1.00 12.81 ? 119 THR B O   1 
ATOM   1648 C  CB  A THR B 1 119 ? -4.374  4.083  86.040  0.50 13.44 ? 119 THR B CB  1 
ATOM   1649 C  CB  B THR B 1 119 ? -4.436  3.977  85.909  0.50 14.51 ? 119 THR B CB  1 
ATOM   1650 O  OG1 A THR B 1 119 ? -3.586  3.446  85.061  0.50 18.48 ? 119 THR B OG1 1 
ATOM   1651 O  OG1 B THR B 1 119 ? -5.846  3.814  85.948  0.50 16.23 ? 119 THR B OG1 1 
ATOM   1652 C  CG2 A THR B 1 119 ? -5.847  3.751  85.941  0.50 9.75  ? 119 THR B CG2 1 
ATOM   1653 C  CG2 B THR B 1 119 ? -3.839  3.380  87.174  0.50 12.24 ? 119 THR B CG2 1 
ATOM   1654 N  N   . ALA B 1 120 ? -5.777  6.590  87.176  1.00 12.52 ? 120 ALA B N   1 
ATOM   1655 C  CA  . ALA B 1 120 ? -6.259  7.247  88.402  1.00 12.84 ? 120 ALA B CA  1 
ATOM   1656 C  C   . ALA B 1 120 ? -7.052  6.251  89.230  1.00 14.21 ? 120 ALA B C   1 
ATOM   1657 O  O   . ALA B 1 120 ? -7.862  5.530  88.661  1.00 16.19 ? 120 ALA B O   1 
ATOM   1658 C  CB  . ALA B 1 120 ? -7.097  8.424  88.001  1.00 17.48 ? 120 ALA B CB  1 
ATOM   1659 N  N   . VAL B 1 121 ? -6.791  6.206  90.520  1.00 14.85 ? 121 VAL B N   1 
ATOM   1660 C  CA  . VAL B 1 121 ? -7.558  5.351  91.459  1.00 16.96 ? 121 VAL B CA  1 
ATOM   1661 C  C   . VAL B 1 121 ? -8.290  6.348  92.353  1.00 16.90 ? 121 VAL B C   1 
ATOM   1662 O  O   . VAL B 1 121 ? -7.633  7.045  93.118  1.00 18.57 ? 121 VAL B O   1 
ATOM   1663 C  CB  . VAL B 1 121 ? -6.650  4.387  92.233  1.00 19.88 ? 121 VAL B CB  1 
ATOM   1664 C  CG1 . VAL B 1 121 ? -7.461  3.388  93.039  1.00 25.85 ? 121 VAL B CG1 1 
ATOM   1665 C  CG2 . VAL B 1 121 ? -5.667  3.681  91.313  1.00 23.91 ? 121 VAL B CG2 1 
ATOM   1666 N  N   . VAL B 1 122 ? -9.594  6.461  92.157  1.00 19.03 ? 122 VAL B N   1 
ATOM   1667 C  CA  . VAL B 1 122 ? -10.408 7.458  92.905  1.00 20.63 ? 122 VAL B CA  1 
ATOM   1668 C  C   . VAL B 1 122 ? -11.316 6.667  93.842  1.00 26.24 ? 122 VAL B C   1 
ATOM   1669 O  O   . VAL B 1 122 ? -12.145 5.919  93.331  1.00 23.91 ? 122 VAL B O   1 
ATOM   1670 C  CB  . VAL B 1 122 ? -11.176 8.390  91.950  1.00 24.57 ? 122 VAL B CB  1 
ATOM   1671 C  CG1 . VAL B 1 122 ? -11.933 9.468  92.704  1.00 29.58 ? 122 VAL B CG1 1 
ATOM   1672 C  CG2 . VAL B 1 122 ? -10.236 9.011  90.928  1.00 23.02 ? 122 VAL B CG2 1 
ATOM   1673 N  N   . THR B 1 123 ? -11.126 6.822  95.151  1.00 22.12 ? 123 THR B N   1 
ATOM   1674 C  CA  . THR B 1 123 ? -11.872 6.016  96.148  1.00 24.02 ? 123 THR B CA  1 
ATOM   1675 C  C   . THR B 1 123 ? -12.636 6.938  97.103  1.00 31.57 ? 123 THR B C   1 
ATOM   1676 O  O   . THR B 1 123 ? -12.186 8.053  97.270  1.00 28.58 ? 123 THR B O   1 
ATOM   1677 C  CB  . THR B 1 123 ? -10.881 5.127  96.897  1.00 29.98 ? 123 THR B CB  1 
ATOM   1678 O  OG1 . THR B 1 123 ? -9.826  5.917  97.445  1.00 29.44 ? 123 THR B OG1 1 
ATOM   1679 C  CG2 . THR B 1 123 ? -10.303 4.042  96.011  1.00 25.56 ? 123 THR B CG2 1 
HETATM 1680 CA CA  . CA  C 2 .   ? 21.388  18.443 67.889  0.80 17.88 ? 201 CA  A CA  1 
HETATM 1681 C  C12 . MSR D 3 .   ? 0.003   0.017  70.650  0.50 25.17 ? 202 MSR A C12 1 
HETATM 1682 C  C13 . MSR D 3 .   ? -0.243  0.204  69.287  0.50 23.14 ? 202 MSR A C13 1 
HETATM 1683 C  C14 . MSR D 3 .   ? -1.047  1.264  68.874  0.50 22.53 ? 202 MSR A C14 1 
HETATM 1684 O  O17 . MSR D 3 .   ? -1.347  1.474  67.589  0.50 27.95 ? 202 MSR A O17 1 
HETATM 1685 C  C15 . MSR D 3 .   ? -1.554  2.189  69.768  0.50 18.66 ? 202 MSR A C15 1 
HETATM 1686 C  C16 . MSR D 3 .   ? -1.287  2.014  71.112  0.50 20.32 ? 202 MSR A C16 1 
HETATM 1687 C  C11 . MSR D 3 .   ? -0.461  0.992  71.587  0.50 22.11 ? 202 MSR A C11 1 
HETATM 1688 N  N3  . MSR D 3 .   ? -0.215  0.870  72.905  0.50 21.89 ? 202 MSR A N3  1 
HETATM 1689 C  C4  . MSR D 3 .   ? 0.070   1.890  73.674  0.50 18.72 ? 202 MSR A C4  1 
HETATM 1690 C  C5  . MSR D 3 .   ? 0.251   1.371  74.943  0.50 18.65 ? 202 MSR A C5  1 
HETATM 1691 N  NFE . MSR D 3 .   ? 0.007   0.005  74.832  0.50 24.95 ? 202 MSR A NFE 1 
HETATM 1692 C  C2  . MSR D 3 .   ? -0.239  -0.286 73.553  0.50 23.94 ? 202 MSR A C2  1 
HETATM 1693 CA CA  . CA  E 2 .   ? -18.372 19.611 90.260  0.80 32.08 ? 201 CA  B CA  1 
HETATM 1694 C  C12 . MSR F 3 .   ? 0.258   -0.301 87.057  0.50 24.14 ? 202 MSR B C12 1 
HETATM 1695 C  C13 . MSR F 3 .   ? -0.074  -0.553 85.773  0.50 19.73 ? 202 MSR B C13 1 
HETATM 1696 C  C14 . MSR F 3 .   ? -0.167  0.450  84.801  0.50 22.99 ? 202 MSR B C14 1 
HETATM 1697 O  O17 . MSR F 3 .   ? -0.487  0.136  83.523  0.50 32.46 ? 202 MSR B O17 1 
HETATM 1698 C  C15 . MSR F 3 .   ? 0.040   1.737  85.195  0.50 22.68 ? 202 MSR B C15 1 
HETATM 1699 C  C16 . MSR F 3 .   ? 0.285   1.987  86.535  0.50 25.45 ? 202 MSR B C16 1 
HETATM 1700 C  C11 . MSR F 3 .   ? 0.457   0.978  87.481  0.50 29.59 ? 202 MSR B C11 1 
HETATM 1701 N  N3  . MSR F 3 .   ? 0.743   1.142  88.736  0.50 28.65 ? 202 MSR B N3  1 
HETATM 1702 C  C4  . MSR F 3 .   ? 0.168   0.422  89.717  0.50 24.58 ? 202 MSR B C4  1 
HETATM 1703 C  C5  . MSR F 3 .   ? 0.686   0.917  90.866  0.50 27.28 ? 202 MSR B C5  1 
HETATM 1704 N  NFE . MSR F 3 .   ? 1.511   1.927  90.500  0.50 25.32 ? 202 MSR B NFE 1 
HETATM 1705 C  C2  . MSR F 3 .   ? 1.573   2.100  89.133  0.50 21.39 ? 202 MSR B C2  1 
HETATM 1706 O  O   . HOH G 4 .   ? 15.248  11.070 68.768  1.00 22.82 ? 301 HOH A O   1 
HETATM 1707 O  O   . HOH G 4 .   ? -2.733  13.837 80.899  1.00 23.84 ? 302 HOH A O   1 
HETATM 1708 O  O   . HOH G 4 .   ? 20.614  19.607 71.567  1.00 13.48 ? 303 HOH A O   1 
HETATM 1709 O  O   . HOH G 4 .   ? 0.900   13.186 61.239  1.00 15.89 ? 304 HOH A O   1 
HETATM 1710 O  O   . HOH G 4 .   ? 5.351   13.111 78.121  1.00 16.52 ? 305 HOH A O   1 
HETATM 1711 O  O   . HOH G 4 .   ? -21.595 12.614 70.483  1.00 26.55 ? 306 HOH A O   1 
HETATM 1712 O  O   . HOH G 4 .   ? -0.537  20.073 59.564  1.00 19.12 ? 307 HOH A O   1 
HETATM 1713 O  O   . HOH G 4 .   ? -9.616  11.787 78.903  1.00 14.84 ? 308 HOH A O   1 
HETATM 1714 O  O   . HOH G 4 .   ? -16.644 7.594  83.523  1.00 22.74 ? 309 HOH A O   1 
HETATM 1715 O  O   . HOH G 4 .   ? -2.825  18.508 59.801  1.00 19.21 ? 310 HOH A O   1 
HETATM 1716 O  O   . HOH G 4 .   ? -6.810  12.159 59.493  1.00 25.75 ? 311 HOH A O   1 
HETATM 1717 O  O   . HOH G 4 .   ? 16.250  18.982 74.933  1.00 25.12 ? 312 HOH A O   1 
HETATM 1718 O  O   . HOH G 4 .   ? 13.969  16.708 58.605  1.00 22.79 ? 313 HOH A O   1 
HETATM 1719 O  O   . HOH G 4 .   ? 17.827  12.323 66.568  1.00 18.62 ? 314 HOH A O   1 
HETATM 1720 O  O   . HOH G 4 .   ? 12.124  23.615 70.866  1.00 17.36 ? 315 HOH A O   1 
HETATM 1721 O  O   . HOH G 4 .   ? 12.996  1.638  65.422  1.00 27.41 ? 316 HOH A O   1 
HETATM 1722 O  O   . HOH G 4 .   ? 1.848   18.764 56.697  1.00 27.08 ? 317 HOH A O   1 
HETATM 1723 O  O   . HOH G 4 .   ? 14.350  16.818 61.295  1.00 18.86 ? 318 HOH A O   1 
HETATM 1724 O  O   . HOH G 4 .   ? 2.374   24.741 58.455  1.00 26.74 ? 319 HOH A O   1 
HETATM 1725 O  O   . HOH G 4 .   ? 7.681   1.393  71.335  1.00 20.61 ? 320 HOH A O   1 
HETATM 1726 O  O   . HOH G 4 .   ? -6.198  10.385 78.307  1.00 19.60 ? 321 HOH A O   1 
HETATM 1727 O  O   . HOH G 4 .   ? -8.071  8.316  77.948  1.00 12.85 ? 322 HOH A O   1 
HETATM 1728 O  O   . HOH G 4 .   ? -10.841 14.655 70.430  1.00 13.82 ? 323 HOH A O   1 
HETATM 1729 O  O   . HOH G 4 .   ? 13.629  12.075 72.756  1.00 18.74 ? 324 HOH A O   1 
HETATM 1730 O  O   . HOH G 4 .   ? 3.984   14.262 59.656  1.00 17.17 ? 325 HOH A O   1 
HETATM 1731 O  O   . HOH G 4 .   ? -12.315 16.004 67.407  1.00 19.55 ? 326 HOH A O   1 
HETATM 1732 O  O   . HOH G 4 .   ? 3.133   21.119 57.633  1.00 25.37 ? 327 HOH A O   1 
HETATM 1733 O  O   . HOH G 4 .   ? 0.852   3.288  74.215  0.50 26.77 ? 328 HOH A O   1 
HETATM 1734 O  O   . HOH G 4 .   ? 8.432   5.558  63.586  1.00 27.67 ? 329 HOH A O   1 
HETATM 1735 O  O   . HOH G 4 .   ? -8.880  9.850  80.800  1.00 13.61 ? 330 HOH A O   1 
HETATM 1736 O  O   . HOH G 4 .   ? 12.433  14.215 61.054  1.00 22.06 ? 331 HOH A O   1 
HETATM 1737 O  O   . HOH G 4 .   ? -0.706  23.594 67.278  1.00 16.79 ? 332 HOH A O   1 
HETATM 1738 O  O   . HOH G 4 .   ? 1.959   22.695 60.597  1.00 25.36 ? 333 HOH A O   1 
HETATM 1739 O  O   . HOH G 4 .   ? 11.642  30.775 69.031  1.00 25.56 ? 334 HOH A O   1 
HETATM 1740 O  O   . HOH G 4 .   ? -13.668 5.543  68.006  1.00 21.85 ? 335 HOH A O   1 
HETATM 1741 O  O   . HOH G 4 .   ? 9.173   24.855 61.990  1.00 20.24 ? 336 HOH A O   1 
HETATM 1742 O  O   . HOH G 4 .   ? -5.728  2.679  78.423  1.00 21.42 ? 337 HOH A O   1 
HETATM 1743 O  O   . HOH G 4 .   ? -14.247 20.114 72.487  1.00 26.44 ? 338 HOH A O   1 
HETATM 1744 O  O   . HOH G 4 .   ? -12.042 17.533 69.836  1.00 22.19 ? 339 HOH A O   1 
HETATM 1745 O  O   . HOH G 4 .   ? 14.416  3.671  68.440  1.00 18.09 ? 340 HOH A O   1 
HETATM 1746 O  O   . HOH G 4 .   ? 16.043  13.714 69.750  1.00 16.23 ? 341 HOH A O   1 
HETATM 1747 O  O   . HOH G 4 .   ? 16.878  18.430 69.244  1.00 18.54 ? 342 HOH A O   1 
HETATM 1748 O  O   . HOH G 4 .   ? -13.219 13.349 69.662  1.00 23.33 ? 343 HOH A O   1 
HETATM 1749 O  O   . HOH G 4 .   ? 7.962   15.396 54.427  1.00 27.58 ? 344 HOH A O   1 
HETATM 1750 O  O   . HOH G 4 .   ? -3.509  15.977 58.947  1.00 20.00 ? 345 HOH A O   1 
HETATM 1751 O  O   . HOH G 4 .   ? 8.457   26.734 68.406  1.00 18.21 ? 346 HOH A O   1 
HETATM 1752 O  O   . HOH G 4 .   ? -4.551  11.163 58.498  1.00 22.23 ? 347 HOH A O   1 
HETATM 1753 O  O   . HOH G 4 .   ? -6.053  15.672 60.166  1.00 14.60 ? 348 HOH A O   1 
HETATM 1754 O  O   . HOH G 4 .   ? 6.525   25.965 66.153  1.00 21.93 ? 349 HOH A O   1 
HETATM 1755 O  O   . HOH G 4 .   ? 21.653  20.424 69.366  1.00 25.86 ? 350 HOH A O   1 
HETATM 1756 O  O   . HOH G 4 .   ? 21.110  11.360 61.156  1.00 32.09 ? 351 HOH A O   1 
HETATM 1757 O  O   . HOH G 4 .   ? 16.037  23.187 69.003  1.00 24.65 ? 352 HOH A O   1 
HETATM 1758 O  O   . HOH G 4 .   ? -0.894  24.642 64.732  1.00 34.10 ? 353 HOH A O   1 
HETATM 1759 O  O   . HOH G 4 .   ? 16.231  20.781 70.609  1.00 23.00 ? 354 HOH A O   1 
HETATM 1760 O  O   . HOH G 4 .   ? 17.485  9.991  68.020  1.00 24.42 ? 355 HOH A O   1 
HETATM 1761 O  O   . HOH G 4 .   ? -3.249  24.080 68.162  1.00 16.37 ? 356 HOH A O   1 
HETATM 1762 O  O   . HOH G 4 .   ? 14.733  24.604 70.803  1.00 26.99 ? 357 HOH A O   1 
HETATM 1763 O  O   . HOH G 4 .   ? 16.681  18.193 61.685  1.00 17.53 ? 358 HOH A O   1 
HETATM 1764 O  O   . HOH G 4 .   ? -4.153  25.545 70.340  1.00 29.04 ? 359 HOH A O   1 
HETATM 1765 O  O   . HOH G 4 .   ? 16.429  21.088 73.277  1.00 27.14 ? 360 HOH A O   1 
HETATM 1766 O  O   . HOH G 4 .   ? 1.771   23.947 55.841  1.00 27.90 ? 361 HOH A O   1 
HETATM 1767 O  O   . HOH H 4 .   ? -0.000  -0.000 81.513  0.50 25.22 ? 301 HOH B O   1 
HETATM 1768 O  O   . HOH H 4 .   ? -18.468 21.804 91.163  1.00 32.01 ? 302 HOH B O   1 
HETATM 1769 O  O   . HOH H 4 .   ? 13.354  14.173 75.355  1.00 17.07 ? 303 HOH B O   1 
HETATM 1770 O  O   . HOH H 4 .   ? 11.712  10.155 80.406  1.00 15.64 ? 304 HOH B O   1 
HETATM 1771 O  O   . HOH H 4 .   ? -18.708 18.584 92.288  1.00 31.62 ? 305 HOH B O   1 
HETATM 1772 O  O   . HOH H 4 .   ? 16.051  -4.973 83.147  1.00 19.56 ? 306 HOH B O   1 
HETATM 1773 O  O   . HOH H 4 .   ? 10.597  8.300  78.832  1.00 21.20 ? 307 HOH B O   1 
HETATM 1774 O  O   . HOH H 4 .   ? 8.415   10.857 99.788  1.00 24.77 ? 308 HOH B O   1 
HETATM 1775 O  O   . HOH H 4 .   ? 22.903  8.278  82.487  1.00 20.73 ? 309 HOH B O   1 
HETATM 1776 O  O   . HOH H 4 .   ? -7.305  6.364  95.743  1.00 27.38 ? 310 HOH B O   1 
HETATM 1777 O  O   . HOH H 4 .   ? -1.972  14.676 99.661  1.00 24.40 ? 311 HOH B O   1 
HETATM 1778 O  O   . HOH H 4 .   ? 9.235   6.905  81.404  1.00 12.25 ? 312 HOH B O   1 
HETATM 1779 O  O   . HOH H 4 .   ? -3.455  9.183  85.965  1.00 15.17 ? 313 HOH B O   1 
HETATM 1780 O  O   . HOH H 4 .   ? 19.522  12.478 86.599  1.00 23.86 ? 314 HOH B O   1 
HETATM 1781 O  O   . HOH H 4 .   ? 3.695   1.997  79.210  1.00 24.88 ? 315 HOH B O   1 
HETATM 1782 O  O   . HOH H 4 .   ? 14.193  3.206  91.426  1.00 17.64 ? 316 HOH B O   1 
HETATM 1783 O  O   . HOH H 4 .   ? 16.421  3.146  76.129  1.00 18.04 ? 317 HOH B O   1 
HETATM 1784 O  O   . HOH H 4 .   ? -8.142  24.926 88.206  1.00 26.64 ? 318 HOH B O   1 
HETATM 1785 O  O   . HOH H 4 .   ? 16.007  5.610  91.443  1.00 31.12 ? 319 HOH B O   1 
HETATM 1786 O  O   . HOH H 4 .   ? -0.584  3.137  84.988  0.50 30.07 ? 320 HOH B O   1 
HETATM 1787 O  O   . HOH H 4 .   ? 13.141  12.573 88.905  1.00 17.10 ? 321 HOH B O   1 
HETATM 1788 O  O   . HOH H 4 .   ? 7.931   9.285  80.865  1.00 22.05 ? 322 HOH B O   1 
HETATM 1789 O  O   . HOH H 4 .   ? -13.633 5.905  90.854  1.00 28.54 ? 323 HOH B O   1 
HETATM 1790 O  O   . HOH H 4 .   ? 5.945   10.015 100.661 1.00 24.57 ? 324 HOH B O   1 
HETATM 1791 O  O   . HOH H 4 .   ? 5.683   1.426  80.919  1.00 23.95 ? 325 HOH B O   1 
HETATM 1792 O  O   . HOH H 4 .   ? 9.503   14.606 99.179  1.00 23.07 ? 326 HOH B O   1 
HETATM 1793 O  O   . HOH H 4 .   ? 7.299   -2.636 87.965  1.00 17.85 ? 327 HOH B O   1 
HETATM 1794 O  O   . HOH H 4 .   ? -6.883  25.984 101.994 1.00 29.06 ? 328 HOH B O   1 
HETATM 1795 O  O   . HOH H 4 .   ? 8.763   17.198 87.744  1.00 24.45 ? 329 HOH B O   1 
HETATM 1796 O  O   . HOH H 4 .   ? 16.856  7.336  89.477  1.00 26.39 ? 330 HOH B O   1 
HETATM 1797 O  O   . HOH H 4 .   ? 11.932  6.477  101.624 1.00 27.98 ? 331 HOH B O   1 
HETATM 1798 O  O   . HOH H 4 .   ? 9.544   20.945 78.455  1.00 33.39 ? 332 HOH B O   1 
HETATM 1799 O  O   . HOH H 4 .   ? 9.161   23.822 93.601  1.00 27.04 ? 333 HOH B O   1 
HETATM 1800 O  O   . HOH H 4 .   ? 17.921  1.099  77.563  1.00 28.59 ? 334 HOH B O   1 
HETATM 1801 O  O   . HOH H 4 .   ? 17.311  -3.834 81.085  1.00 24.43 ? 335 HOH B O   1 
HETATM 1802 O  O   . HOH H 4 .   ? 17.114  -0.399 79.835  1.00 28.99 ? 336 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  ? 0.5744 0.7277 0.5397 -0.1383 -0.1992 -0.1474 10  CYS A N   
2    C  CA  . CYS A 10  ? 0.7427 0.6867 0.4201 0.1975  -0.0591 -0.0589 10  CYS A CA  
3    C  C   . CYS A 10  ? 0.4565 0.3450 0.3362 -0.0821 0.0785  -0.0647 10  CYS A C   
4    O  O   . CYS A 10  ? 0.4315 0.3060 0.6497 -0.0592 0.2379  -0.0835 10  CYS A O   
5    N  N   . PRO A 11  ? 0.2440 0.2807 0.1720 -0.0395 0.0428  0.0270  11  PRO A N   
6    C  CA  . PRO A 11  ? 0.1997 0.1988 0.1935 0.0093  0.0142  0.0592  11  PRO A CA  
7    C  C   . PRO A 11  ? 0.1673 0.1731 0.1655 0.0187  0.0153  0.0521  11  PRO A C   
8    O  O   . PRO A 11  ? 0.1824 0.1869 0.1971 -0.0056 -0.0027 0.0813  11  PRO A O   
9    C  CB  . PRO A 11  ? 0.2908 0.2775 0.2233 -0.0970 0.0178  0.0637  11  PRO A CB  
10   C  CG  . PRO A 11  ? 0.2855 0.1468 0.4935 -0.0229 0.1323  0.0713  11  PRO A CG  
11   C  CD  . PRO A 11  ? 0.3149 0.4102 0.1946 -0.0204 -0.0121 0.1243  11  PRO A CD  
12   N  N   . LEU A 12  ? 0.1686 0.1721 0.1605 -0.0097 0.0131  0.0607  12  LEU A N   
13   C  CA  . LEU A 12  ? 0.1677 0.1619 0.1626 -0.0056 0.0164  0.0562  12  LEU A CA  
14   C  C   . LEU A 12  ? 0.1513 0.1796 0.2046 0.0058  0.0020  0.0919  12  LEU A C   
15   O  O   . LEU A 12  ? 0.1563 0.3081 0.3249 -0.0184 -0.0351 0.1735  12  LEU A O   
16   C  CB  . LEU A 12  ? 0.1789 0.2165 0.1899 0.0229  -0.0063 0.0683  12  LEU A CB  
17   C  CG  . LEU A 12  ? 0.2069 0.2030 0.2394 0.0105  0.0213  0.0386  12  LEU A CG  
18   C  CD1 . LEU A 12  ? 0.2063 0.2378 0.2069 0.0632  0.0048  0.0160  12  LEU A CD1 
19   C  CD2 . LEU A 12  ? 0.2374 0.1907 0.3243 0.0121  0.0051  0.0670  12  LEU A CD2 
20   N  N   . MET A 13  ? 0.1473 0.1467 0.1567 0.0047  0.0080  0.0492  13  MET A N   
21   C  CA  . MET A 13  ? 0.1430 0.1803 0.1467 -0.0214 -0.0040 0.0440  13  MET A CA  
22   C  C   . MET A 13  ? 0.1278 0.1348 0.1528 -0.0051 -0.0140 0.0295  13  MET A C   
23   O  O   . MET A 13  ? 0.1344 0.1921 0.1501 -0.0016 0.0008  0.0465  13  MET A O   
24   C  CB  . MET A 13  ? 0.2082 0.2240 0.1887 -0.0614 0.0264  0.0308  13  MET A CB  
25   C  CG  . MET A 13  ? 0.3126 0.2871 0.2549 -0.0359 0.0267  -0.0095 13  MET A CG  
26   S  SD  . MET A 13  ? 0.2360 0.1781 0.2325 -0.0277 0.0127  -0.0291 13  MET A SD  
27   N  N   . VAL A 14  ? 0.1314 0.1446 0.1111 -0.0228 -0.0059 0.0114  14  VAL A N   
28   C  CA  . VAL A 14  ? 0.1386 0.1480 0.1192 0.0041  -0.0132 0.0319  14  VAL A CA  
29   C  C   . VAL A 14  ? 0.1105 0.1705 0.1667 -0.0144 -0.0109 0.0283  14  VAL A C   
30   O  O   . VAL A 14  ? 0.1449 0.1985 0.1986 -0.0443 -0.0343 0.0610  14  VAL A O   
31   C  CB  . VAL A 14  ? 0.1558 0.1612 0.1529 0.0006  0.0090  0.0097  14  VAL A CB  
32   C  CG1 . VAL A 14  ? 0.1504 0.1780 0.1807 0.0326  -0.0032 -0.0108 14  VAL A CG1 
33   C  CG2 . VAL A 14  ? 0.1615 0.1262 0.1592 0.0205  0.0154  -0.0025 14  VAL A CG2 
34   N  N   . LYS A 15  ? 0.1317 0.1628 0.1278 -0.0176 0.0067  0.0076  15  LYS A N   
35   C  CA  . LYS A 15  ? 0.1642 0.1700 0.1118 -0.0417 -0.0084 0.0195  15  LYS A CA  
36   C  C   . LYS A 15  ? 0.1553 0.1479 0.1131 -0.0244 -0.0103 0.0279  15  LYS A C   
37   O  O   . LYS A 15  ? 0.1699 0.2153 0.1174 -0.0327 -0.0009 0.0397  15  LYS A O   
38   C  CB  . LYS A 15  ? 0.1583 0.1345 0.1029 -0.0195 0.0482  -0.0254 15  LYS A CB  
39   C  CG  . LYS A 15  ? 0.2255 0.1937 0.2432 -0.0434 0.0565  0.0003  15  LYS A CG  
40   C  CD  . LYS A 15  ? 0.2857 0.2004 0.2580 -0.0203 0.0218  0.0087  15  LYS A CD  
41   C  CE  . LYS A 15  ? 0.3135 0.1706 0.2993 -0.0258 -0.0102 -0.0110 15  LYS A CE  
42   N  NZ  . LYS A 15  ? 0.3739 0.3717 0.3545 -0.0029 -0.0137 -0.0378 15  LYS A NZ  
43   N  N   . VAL A 16  ? 0.1498 0.1599 0.1035 -0.0388 -0.0027 0.0028  16  VAL A N   
44   C  CA  . VAL A 16  ? 0.1384 0.1401 0.1205 -0.0250 -0.0142 -0.0019 16  VAL A CA  
45   C  C   . VAL A 16  ? 0.1356 0.1465 0.1417 -0.0359 -0.0123 0.0023  16  VAL A C   
46   O  O   . VAL A 16  ? 0.1679 0.1534 0.1303 -0.0379 -0.0134 0.0003  16  VAL A O   
47   C  CB  . VAL A 16  ? 0.1545 0.1357 0.1463 -0.0207 0.0050  0.0276  16  VAL A CB  
48   C  CG1 . VAL A 16  ? 0.1729 0.1754 0.1294 -0.0394 0.0075  0.0214  16  VAL A CG1 
49   C  CG2 . VAL A 16  ? 0.1674 0.1373 0.1204 -0.0208 -0.0130 0.0092  16  VAL A CG2 
50   N  N   . LEU A 17  ? 0.1609 0.1300 0.1470 -0.0489 -0.0134 0.0123  17  LEU A N   
51   C  CA  . LEU A 17  ? 0.1641 0.1182 0.1365 -0.0279 -0.0010 -0.0073 17  LEU A CA  
52   C  C   . LEU A 17  ? 0.1447 0.1299 0.1192 -0.0174 -0.0004 0.0035  17  LEU A C   
53   O  O   . LEU A 17  ? 0.1486 0.1586 0.1158 -0.0431 -0.0061 0.0014  17  LEU A O   
54   C  CB  . LEU A 17  ? 0.1786 0.1427 0.1240 -0.0371 0.0000  0.0005  17  LEU A CB  
55   C  CG  . LEU A 17  ? 0.2072 0.1861 0.1433 -0.0051 0.0075  0.0116  17  LEU A CG  
56   C  CD1 . LEU A 17  ? 0.2479 0.1662 0.2102 0.0073  0.0228  -0.0433 17  LEU A CD1 
57   C  CD2 . LEU A 17  ? 0.2576 0.2240 0.1882 -0.0015 -0.0297 -0.0514 17  LEU A CD2 
58   N  N   . ASP A 18  ? 0.1458 0.1385 0.1390 -0.0429 0.0071  -0.0077 18  ASP A N   
59   C  CA  . ASP A 18  ? 0.1566 0.0953 0.1287 -0.0286 0.0013  -0.0031 18  ASP A CA  
60   C  C   . ASP A 18  ? 0.1473 0.1108 0.1182 -0.0367 -0.0339 0.0030  18  ASP A C   
61   O  O   . ASP A 18  ? 0.1596 0.1165 0.1438 -0.0307 -0.0132 -0.0084 18  ASP A O   
62   C  CB  . ASP A 18  ? 0.1696 0.0951 0.1764 -0.0218 -0.0146 0.0139  18  ASP A CB  
63   C  CG  . ASP A 18  ? 0.1639 0.1690 0.1586 -0.0062 -0.0448 0.0335  18  ASP A CG  
64   O  OD1 . ASP A 18  ? 0.1685 0.1503 0.1512 -0.0250 -0.0118 0.0193  18  ASP A OD1 
65   O  OD2 . ASP A 18  ? 0.1861 0.1589 0.2186 -0.0272 -0.0041 0.0280  18  ASP A OD2 
66   N  N   . ALA A 19  ? 0.1358 0.1009 0.1126 -0.0127 -0.0085 -0.0023 19  ALA A N   
67   C  CA  . ALA A 19  ? 0.1539 0.0999 0.1390 -0.0029 0.0016  0.0079  19  ALA A CA  
68   C  C   . ALA A 19  ? 0.1685 0.0938 0.1389 -0.0203 0.0006  0.0083  19  ALA A C   
69   O  O   . ALA A 19  ? 0.2215 0.0949 0.1651 -0.0196 0.0021  0.0119  19  ALA A O   
70   C  CB  . ALA A 19  ? 0.1520 0.1257 0.1794 -0.0030 0.0006  0.0372  19  ALA A CB  
71   N  N   . VAL A 20  ? 0.1689 0.1037 0.1619 -0.0281 0.0164  0.0294  20  VAL A N   
72   C  CA  . VAL A 20  ? 0.1743 0.1464 0.1680 -0.0239 0.0497  -0.0048 20  VAL A CA  
73   C  C   . VAL A 20  ? 0.1537 0.1344 0.1806 -0.0311 0.0133  0.0227  20  VAL A C   
74   O  O   . VAL A 20  ? 0.2109 0.1678 0.2117 -0.0698 0.0277  -0.0095 20  VAL A O   
75   C  CB  . VAL A 20  ? 0.1895 0.1750 0.1309 -0.0226 0.0447  0.0114  20  VAL A CB  
76   C  CG1 . VAL A 20  ? 0.2200 0.1514 0.2462 -0.0396 0.0654  -0.0422 20  VAL A CG1 
77   C  CG2 . VAL A 20  ? 0.2503 0.2127 0.1256 -0.0256 0.0137  0.0010  20  VAL A CG2 
78   N  N   . ARG A 21  ? 0.1530 0.1310 0.1645 -0.0382 -0.0053 0.0107  21  ARG A N   
79   C  CA  . ARG A 21  ? 0.1717 0.1868 0.1727 -0.0293 0.0170  -0.0123 21  ARG A CA  
80   C  C   . ARG A 21  ? 0.1803 0.1197 0.1376 -0.0312 -0.0224 -0.0292 21  ARG A C   
81   O  O   . ARG A 21  ? 0.2138 0.1969 0.1915 -0.0718 -0.0068 -0.0414 21  ARG A O   
82   C  CB  . ARG A 21  ? 0.2294 0.2452 0.2235 0.0051  -0.0668 -0.0268 21  ARG A CB  
83   C  CG  . ARG A 21  ? 0.3071 0.3385 0.4555 0.0120  -0.0173 -0.0494 21  ARG A CG  
84   C  CD  . ARG A 21  ? 0.4405 0.3710 0.5303 0.1100  -0.0136 -0.0251 21  ARG A CD  
85   N  NE  . ARG A 21  ? 0.5046 0.5872 0.6603 0.1524  0.0161  -0.0040 21  ARG A NE  
86   N  N   . GLY A 22  ? 0.1650 0.1218 0.1252 -0.0277 -0.0039 -0.0179 22  GLY A N   
87   C  CA  . GLY A 22  ? 0.2117 0.1088 0.1363 -0.0286 -0.0009 0.0213  22  GLY A CA  
88   C  C   . GLY A 22  ? 0.1338 0.1023 0.1406 0.0104  0.0050  -0.0240 22  GLY A C   
89   O  O   . GLY A 22  ? 0.1791 0.1146 0.1488 0.0005  -0.0146 -0.0074 22  GLY A O   
90   N  N   . SER A 23  ? 0.1863 0.1002 0.1505 -0.0183 0.0130  0.0073  23  SER A N   
91   C  CA  . SER A 23  ? 0.1831 0.1280 0.1552 -0.0102 0.0138  -0.0010 23  SER A CA  
92   C  C   . SER A 23  ? 0.1972 0.1148 0.1380 -0.0257 -0.0187 0.0336  23  SER A C   
93   O  O   . SER A 23  ? 0.2020 0.1536 0.1230 -0.0523 -0.0289 0.0006  23  SER A O   
94   C  CB  . SER A 23  ? 0.1925 0.1650 0.1839 -0.0566 -0.0141 0.0479  23  SER A CB  
95   O  OG  . SER A 23  ? 0.2353 0.2505 0.2978 -0.0224 -0.0083 0.0035  23  SER A OG  
96   N  N   . PRO A 24  ? 0.1976 0.1156 0.1488 -0.0422 -0.0317 -0.0122 24  PRO A N   
97   C  CA  . PRO A 24  ? 0.1723 0.1398 0.1340 -0.0459 -0.0135 0.0102  24  PRO A CA  
98   C  C   . PRO A 24  ? 0.1571 0.1409 0.1601 -0.0425 0.0003  0.0278  24  PRO A C   
99   O  O   . PRO A 24  ? 0.1755 0.1398 0.1966 -0.0320 -0.0126 0.0161  24  PRO A O   
100  C  CB  . PRO A 24  ? 0.2418 0.1482 0.1657 -0.0416 0.0170  0.0343  24  PRO A CB  
101  C  CG  . PRO A 24  ? 0.4057 0.2791 0.1353 -0.1296 0.0201  0.0255  24  PRO A CG  
102  C  CD  . PRO A 24  ? 0.1889 0.1630 0.1493 -0.0249 -0.0281 0.0118  24  PRO A CD  
103  N  N   . ALA A 25  ? 0.1594 0.1083 0.1793 -0.0200 -0.0003 0.0040  25  ALA A N   
104  C  CA  . ALA A 25  ? 0.1401 0.1210 0.1680 -0.0245 -0.0030 0.0107  25  ALA A CA  
105  C  C   . ALA A 25  ? 0.1618 0.1058 0.2046 -0.0187 -0.0166 0.0266  25  ALA A C   
106  O  O   . ALA A 25  ? 0.1581 0.1201 0.2104 -0.0281 -0.0154 0.0356  25  ALA A O   
107  C  CB  . ALA A 25  ? 0.1672 0.1260 0.1473 -0.0316 -0.0072 0.0176  25  ALA A CB  
108  N  N   . ILE A 26  ? 0.1484 0.1581 0.1811 -0.0294 -0.0004 0.0299  26  ILE A N   
109  C  CA  . ILE A 26  ? 0.1869 0.1380 0.1720 -0.0282 -0.0164 0.0165  26  ILE A CA  
110  C  C   . ILE A 26  ? 0.1875 0.1599 0.1733 -0.0131 -0.0260 -0.0083 26  ILE A C   
111  O  O   . ILE A 26  ? 0.1908 0.1535 0.2097 -0.0359 -0.0238 -0.0055 26  ILE A O   
112  C  CB  . ILE A 26  ? 0.2794 0.1464 0.1863 -0.0649 -0.0569 0.0084  26  ILE A CB  
113  C  CG1 . ILE A 26  ? 0.2547 0.1646 0.2704 -0.0304 -0.0501 0.0353  26  ILE A CG1 
114  C  CG2 . ILE A 26  ? 0.3257 0.2832 0.3275 -0.0666 -0.0377 0.0268  26  ILE A CG2 
115  C  CD1 . ILE A 26  ? 0.3659 0.3452 0.4452 -0.0650 -0.1424 0.0088  26  ILE A CD1 
116  N  N   . ASN A 27  ? 0.1614 0.1730 0.1563 -0.0143 -0.0334 -0.0205 27  ASN A N   
117  C  CA  . ASN A 27  ? 0.1656 0.1495 0.1914 0.0025  -0.0180 0.0015  27  ASN A CA  
118  C  C   . ASN A 27  ? 0.1442 0.1494 0.2203 -0.0013 -0.0125 -0.0185 27  ASN A C   
119  O  O   . ASN A 27  ? 0.1484 0.1679 0.2626 0.0088  -0.0319 -0.0176 27  ASN A O   
120  C  CB  . ASN A 27  ? 0.1755 0.1633 0.3117 0.0147  -0.0703 -0.0152 27  ASN A CB  
121  C  CG  . ASN A 27  ? 0.2620 0.3028 0.3158 0.0068  -0.0465 -0.0121 27  ASN A CG  
122  O  OD1 . ASN A 27  ? 0.2212 0.4224 0.2997 0.0149  -0.0874 -0.0073 27  ASN A OD1 
123  N  ND2 . ASN A 27  ? 0.2769 0.4348 0.4337 -0.0469 -0.1185 0.0693  27  ASN A ND2 
124  N  N   . VAL A 28  ? 0.1458 0.1209 0.1885 -0.0044 -0.0123 0.0194  28  VAL A N   
125  C  CA  . VAL A 28  ? 0.1396 0.1397 0.1506 -0.0198 0.0031  0.0128  28  VAL A CA  
126  C  C   . VAL A 28  ? 0.1174 0.1286 0.1388 0.0056  0.0104  0.0142  28  VAL A C   
127  O  O   . VAL A 28  ? 0.1400 0.1214 0.1639 -0.0144 0.0204  0.0100  28  VAL A O   
128  C  CB  . VAL A 28  ? 0.1562 0.1204 0.1635 -0.0170 0.0055  0.0172  28  VAL A CB  
129  C  CG1 . VAL A 28  ? 0.2132 0.1540 0.1721 -0.0319 -0.0271 0.0237  28  VAL A CG1 
130  C  CG2 . VAL A 28  ? 0.1892 0.1606 0.2065 -0.0430 -0.0067 0.0402  28  VAL A CG2 
131  N  N   . ALA A 29  ? 0.1377 0.1169 0.1320 -0.0121 0.0148  0.0031  29  ALA A N   
132  C  CA  . ALA A 29  ? 0.1326 0.1289 0.1298 -0.0108 0.0105  0.0200  29  ALA A CA  
133  C  C   . ALA A 29  ? 0.1446 0.1058 0.1251 -0.0051 -0.0072 0.0220  29  ALA A C   
134  O  O   . ALA A 29  ? 0.1382 0.1357 0.1208 -0.0267 -0.0028 0.0122  29  ALA A O   
135  C  CB  . ALA A 29  ? 0.1579 0.1241 0.1665 0.0066  -0.0182 0.0054  29  ALA A CB  
136  N  N   . VAL A 30  ? 0.1372 0.1460 0.1262 -0.0044 -0.0103 0.0394  30  VAL A N   
137  C  CA  . VAL A 30  ? 0.1362 0.1281 0.1482 -0.0108 0.0013  0.0341  30  VAL A CA  
138  C  C   . VAL A 30  ? 0.1339 0.1269 0.1228 -0.0075 -0.0160 0.0194  30  VAL A C   
139  O  O   . VAL A 30  ? 0.1496 0.1293 0.1454 -0.0006 -0.0219 0.0334  30  VAL A O   
140  C  CB  . VAL A 30  ? 0.1475 0.1390 0.1138 0.0000  -0.0072 0.0331  30  VAL A CB  
141  C  CG1 . VAL A 30  ? 0.1565 0.1212 0.2172 0.0140  -0.0194 -0.0037 30  VAL A CG1 
142  C  CG2 . VAL A 30  ? 0.1413 0.1309 0.1609 0.0001  -0.0099 0.0500  30  VAL A CG2 
143  N  N   . HIS A 31  ? 0.1414 0.1220 0.1409 -0.0015 -0.0161 0.0362  31  HIS A N   
144  C  CA  . HIS A 31  ? 0.1260 0.1009 0.1941 -0.0061 -0.0122 0.0166  31  HIS A CA  
145  C  C   . HIS A 31  ? 0.1298 0.1189 0.1511 -0.0073 -0.0110 0.0275  31  HIS A C   
146  O  O   . HIS A 31  ? 0.1254 0.1825 0.1837 -0.0258 -0.0230 0.0502  31  HIS A O   
147  C  CB  . HIS A 31  ? 0.1399 0.1598 0.1813 -0.0163 -0.0085 0.0051  31  HIS A CB  
148  C  CG  . HIS A 31  ? 0.1404 0.1537 0.2284 -0.0067 -0.0047 -0.0010 31  HIS A CG  
149  N  ND1 . HIS A 31  ? 0.1714 0.1972 0.2855 0.0046  -0.0481 0.0157  31  HIS A ND1 
150  C  CD2 . HIS A 31  ? 0.1456 0.1526 0.1704 -0.0053 -0.0155 0.0119  31  HIS A CD2 
151  C  CE1 . HIS A 31  ? 0.1153 0.1546 0.2282 -0.0031 -0.0103 -0.0086 31  HIS A CE1 
152  N  NE2 . HIS A 31  ? 0.1682 0.2688 0.2761 0.0249  -0.0412 0.0081  31  HIS A NE2 
153  N  N   . VAL A 32  ? 0.1228 0.1164 0.1435 0.0020  -0.0203 0.0398  32  VAL A N   
154  C  CA  . VAL A 32  ? 0.1317 0.1111 0.1661 -0.0013 -0.0189 0.0434  32  VAL A CA  
155  C  C   . VAL A 32  ? 0.1282 0.1305 0.1605 0.0247  -0.0250 -0.0014 32  VAL A C   
156  O  O   . VAL A 32  ? 0.1149 0.1220 0.1914 0.0067  -0.0195 0.0232  32  VAL A O   
157  C  CB  . VAL A 32  ? 0.1415 0.1082 0.1810 -0.0062 -0.0105 0.0361  32  VAL A CB  
158  C  CG1 . VAL A 32  ? 0.1453 0.1367 0.1734 0.0143  -0.0246 -0.0094 32  VAL A CG1 
159  C  CG2 . VAL A 32  ? 0.1553 0.1404 0.1671 0.0057  -0.0149 0.0022  32  VAL A CG2 
160  N  N   . PHE A 33  ? 0.1474 0.1071 0.1719 0.0047  -0.0301 0.0335  33  PHE A N   
161  C  CA  . PHE A 33  ? 0.1719 0.0819 0.2012 0.0037  -0.0219 0.0274  33  PHE A CA  
162  C  C   . PHE A 33  ? 0.1539 0.1057 0.1684 0.0115  -0.0192 0.0438  33  PHE A C   
163  O  O   . PHE A 33  ? 0.1320 0.1158 0.1716 -0.0023 -0.0147 0.0345  33  PHE A O   
164  C  CB  . PHE A 33  ? 0.1349 0.1400 0.2300 0.0085  -0.0347 -0.0146 33  PHE A CB  
165  C  CG  . PHE A 33  ? 0.1596 0.1326 0.2706 0.0092  -0.0216 -0.0233 33  PHE A CG  
166  C  CD1 . PHE A 33  ? 0.1751 0.1641 0.2860 0.0185  -0.0309 -0.0233 33  PHE A CD1 
167  C  CD2 . PHE A 33  ? 0.1818 0.1523 0.2694 0.0055  0.0203  -0.0144 33  PHE A CD2 
168  C  CE1 . PHE A 33  ? 0.1807 0.2027 0.2263 -0.0402 -0.0011 -0.0239 33  PHE A CE1 
169  C  CE2 . PHE A 33  ? 0.1570 0.1695 0.3463 0.0537  -0.0218 0.0246  33  PHE A CE2 
170  C  CZ  . PHE A 33  ? 0.1642 0.2083 0.2676 -0.0020 0.0121  -0.0057 33  PHE A CZ  
171  N  N   . ARG A 34  ? 0.1403 0.1210 0.2217 0.0177  -0.0329 0.0462  34  ARG A N   
172  C  CA  . ARG A 34  ? 0.1642 0.1127 0.2039 0.0133  -0.0228 -0.0090 34  ARG A CA  
173  C  C   . ARG A 34  ? 0.1455 0.1073 0.2061 0.0036  0.0009  0.0256  34  ARG A C   
174  O  O   . ARG A 34  ? 0.1716 0.1129 0.2306 -0.0041 -0.0365 0.0313  34  ARG A O   
175  C  CB  . ARG A 34  ? 0.1697 0.1027 0.1895 -0.0195 -0.0583 -0.0255 34  ARG A CB  
176  C  CG  . ARG A 34  ? 0.1609 0.1270 0.2092 -0.0126 -0.0210 0.0433  34  ARG A CG  
177  C  CD  . ARG A 34  ? 0.2010 0.1450 0.1650 -0.0263 -0.0224 0.0361  34  ARG A CD  
178  N  NE  . ARG A 34  ? 0.2015 0.1646 0.1942 -0.0207 -0.0108 0.0420  34  ARG A NE  
179  C  CZ  . ARG A 34  ? 0.2045 0.1314 0.1757 -0.0021 0.0221  0.0210  34  ARG A CZ  
180  N  NH1 . ARG A 34  ? 0.1646 0.1417 0.2593 -0.0083 0.0071  0.0484  34  ARG A NH1 
181  N  NH2 . ARG A 34  ? 0.1898 0.1397 0.2509 -0.0181 0.0375  -0.0002 34  ARG A NH2 
182  N  N   . LYS A 35  ? 0.1416 0.1207 0.1794 0.0000  -0.0099 0.0341  35  LYS A N   
183  C  CA  . LYS A 35  ? 0.1480 0.1496 0.2104 -0.0179 0.0040  0.0154  35  LYS A CA  
184  C  C   . LYS A 35  ? 0.1403 0.1467 0.1907 -0.0260 -0.0011 -0.0169 35  LYS A C   
185  O  O   . LYS A 35  ? 0.1670 0.1404 0.2451 -0.0283 0.0169  -0.0162 35  LYS A O   
186  C  CB  . LYS A 35  ? 0.1788 0.2243 0.1933 0.0191  -0.0235 0.0193  35  LYS A CB  
187  N  N   . ALA A 36  ? 0.2107 0.1112 0.2484 -0.0143 -0.0146 -0.0030 36  ALA A N   
188  C  CA  . ALA A 36  ? 0.2603 0.1381 0.2462 -0.0500 0.0011  -0.0169 36  ALA A CA  
189  C  C   . ALA A 36  ? 0.2265 0.1684 0.2104 -0.0177 0.0586  -0.0282 36  ALA A C   
190  O  O   . ALA A 36  ? 0.2638 0.2541 0.2336 -0.0784 -0.0457 0.0247  36  ALA A O   
191  C  CB  . ALA A 36  ? 0.3349 0.1543 0.2354 -0.0241 0.0155  0.0291  36  ALA A CB  
192  N  N   . ALA A 37  ? 0.3253 0.2719 0.2837 -0.1333 0.0700  -0.0299 37  ALA A N   
193  C  CA  . ALA A 37  ? 0.3380 0.2967 0.3177 -0.1095 0.0735  -0.1248 37  ALA A CA  
194  C  C   . ALA A 37  ? 0.3639 0.3101 0.2388 -0.0982 0.0466  -0.0294 37  ALA A C   
195  O  O   . ALA A 37  ? 0.4662 0.5433 0.3811 -0.2531 -0.0501 -0.1148 37  ALA A O   
196  C  CB  . ALA A 37  ? 0.4032 0.4213 0.2979 -0.2177 0.1194  -0.1489 37  ALA A CB  
197  N  N   . ASP A 38  ? 0.3895 0.2172 0.3722 -0.1216 0.0680  -0.0833 38  ASP A N   
198  C  CA  . ASP A 38  ? 0.4380 0.3109 0.4192 -0.1035 0.0810  -0.0701 38  ASP A CA  
199  C  C   . ASP A 38  ? 0.4411 0.3260 0.2370 -0.1443 0.0818  -0.0997 38  ASP A C   
200  O  O   . ASP A 38  ? 0.6478 0.3816 0.2586 -0.2046 0.1543  -0.1387 38  ASP A O   
201  C  CB  . ASP A 38  ? 0.5193 0.2714 0.3030 -0.0688 0.0683  -0.0874 38  ASP A CB  
202  C  CG  . ASP A 38  ? 0.5365 0.2248 0.5923 0.0201  -0.0145 -0.0359 38  ASP A CG  
203  O  OD1 . ASP A 38  ? 0.4232 0.2195 0.5038 -0.0432 0.0348  -0.0469 38  ASP A OD1 
204  O  OD2 . ASP A 38  ? 0.6288 0.3014 0.6484 0.0508  0.1443  0.0062  38  ASP A OD2 
205  N  N   . ASP A 39  ? 0.3938 0.3744 0.2609 -0.1440 0.0638  -0.0446 39  ASP A N   
206  C  CA  . ASP A 39  ? 0.3922 0.4220 0.2065 -0.1272 0.0088  -0.0129 39  ASP A CA  
207  C  C   . ASP A 39  ? 0.4247 0.3524 0.3748 0.0185  0.0971  -0.0565 39  ASP A C   
208  O  O   . ASP A 39  ? 0.5950 0.3838 0.4193 0.0055  0.1745  -0.0065 39  ASP A O   
209  C  CB  . ASP A 39  ? 0.6009 0.6360 0.2523 -0.2202 -0.0582 -0.1024 39  ASP A CB  
210  N  N   . THR A 40  ? 0.3571 0.2963 0.3310 -0.0547 0.1436  -0.0893 40  THR A N   
211  C  CA  . THR A 40  ? 0.3849 0.2387 0.4134 -0.0347 0.1127  -0.0985 40  THR A CA  
212  C  C   . THR A 40  ? 0.3078 0.2131 0.2578 0.0071  0.0626  0.0136  40  THR A C   
213  O  O   . THR A 40  ? 0.2258 0.2418 0.3054 -0.0293 0.0253  -0.0006 40  THR A O   
214  C  CB  . THR A 40  ? 0.3903 0.3299 0.3718 -0.0027 0.0375  -0.0454 40  THR A CB  
215  O  OG1 . THR A 40  ? 0.4620 0.1985 0.4615 0.0966  0.0048  -0.0430 40  THR A OG1 
216  C  CG2 . THR A 40  ? 0.4481 0.3338 0.3814 0.0146  0.0857  -0.0746 40  THR A CG2 
217  N  N   . TRP A 41  ? 0.3458 0.3699 0.3561 -0.0022 0.2668  -0.1953 41  TRP A N   
218  C  CA  . TRP A 41  ? 0.2138 0.2795 0.3227 0.0719  0.0885  -0.0481 41  TRP A CA  
219  C  C   . TRP A 41  ? 0.2692 0.2955 0.4288 0.0815  0.0233  0.0027  41  TRP A C   
220  O  O   . TRP A 41  ? 0.3335 0.4856 0.5600 0.3290  0.2130  0.2132  41  TRP A O   
221  C  CB  . TRP A 41  ? 0.1913 0.2314 0.3572 0.0989  0.1406  -0.0711 41  TRP A CB  
222  C  CG  . TRP A 41  ? 0.2284 0.2263 0.3155 0.0294  0.0439  -0.0976 41  TRP A CG  
223  C  CD1 . TRP A 41  ? 0.3080 0.3364 0.3272 0.1752  0.1189  -0.1522 41  TRP A CD1 
224  C  CD2 . TRP A 41  ? 0.1795 0.1700 0.2587 0.0231  0.0361  0.0361  41  TRP A CD2 
225  N  NE1 . TRP A 41  ? 0.3808 0.3627 0.3003 0.1242  0.1036  -0.0440 41  TRP A NE1 
226  C  CE2 . TRP A 41  ? 0.3164 0.1786 0.2730 0.0667  0.0975  -0.0018 41  TRP A CE2 
227  C  CE3 . TRP A 41  ? 0.1643 0.1541 0.2011 -0.0092 0.0050  -0.0055 41  TRP A CE3 
228  C  CZ2 . TRP A 41  ? 0.2871 0.2431 0.2483 0.0781  0.0292  0.0568  41  TRP A CZ2 
229  C  CZ3 . TRP A 41  ? 0.1565 0.1559 0.2266 0.0071  0.0407  -0.0081 41  TRP A CZ3 
230  C  CH2 . TRP A 41  ? 0.2345 0.2098 0.2679 0.0852  0.0077  0.0084  41  TRP A CH2 
231  N  N   . GLU A 42  ? 0.1773 0.1205 0.2945 0.0148  -0.0753 0.0125  42  GLU A N   
232  C  CA  . GLU A 42  ? 0.2203 0.1383 0.2891 0.0494  -0.0546 0.0170  42  GLU A CA  
233  C  C   . GLU A 42  ? 0.1577 0.1433 0.3732 0.0094  -0.0829 0.0068  42  GLU A C   
234  O  O   . GLU A 42  ? 0.1819 0.1158 0.3948 0.0099  -0.0607 0.0219  42  GLU A O   
235  C  CB  . GLU A 42  ? 0.3616 0.2542 0.2438 -0.0797 -0.0956 0.1049  42  GLU A CB  
236  N  N   . PRO A 43  ? 0.1747 0.1142 0.2863 0.0060  -0.0405 0.0068  43  PRO A N   
237  C  CA  . PRO A 43  ? 0.1715 0.1339 0.2570 0.0090  -0.0469 0.0118  43  PRO A CA  
238  C  C   . PRO A 43  ? 0.2456 0.1550 0.2630 -0.0026 0.0196  0.0821  43  PRO A C   
239  O  O   . PRO A 43  ? 0.3860 0.1561 0.3174 -0.0595 0.0951  0.0288  43  PRO A O   
240  C  CB  . PRO A 43  ? 0.2656 0.1647 0.2809 0.0325  -0.1346 0.0035  43  PRO A CB  
241  C  CG  . PRO A 43  ? 0.2829 0.2232 0.4108 0.0872  -0.1593 -0.0580 43  PRO A CG  
242  C  CD  . PRO A 43  ? 0.2442 0.1431 0.3051 0.0273  -0.0787 -0.0139 43  PRO A CD  
243  N  N   . PHE A 44  ? 0.1345 0.1405 0.2075 -0.0212 -0.0023 0.0467  44  PHE A N   
244  C  CA  . PHE A 44  ? 0.1446 0.1388 0.2210 -0.0130 0.0052  0.0252  44  PHE A CA  
245  C  C   . PHE A 44  ? 0.1615 0.1436 0.1422 -0.0170 -0.0093 0.0577  44  PHE A C   
246  O  O   . PHE A 44  ? 0.1566 0.1754 0.1699 -0.0185 -0.0309 0.0663  44  PHE A O   
247  C  CB  . PHE A 44  ? 0.1668 0.1292 0.1911 -0.0373 -0.0050 0.0247  44  PHE A CB  
248  C  CG  . PHE A 44  ? 0.1583 0.1641 0.1741 -0.0144 0.0099  0.0565  44  PHE A CG  
249  C  CD1 . PHE A 44  ? 0.1634 0.1909 0.2508 -0.0061 0.0048  0.0605  44  PHE A CD1 
250  C  CD2 . PHE A 44  ? 0.1277 0.1676 0.1731 0.0092  -0.0181 0.0522  44  PHE A CD2 
251  C  CE1 . PHE A 44  ? 0.1766 0.1269 0.2283 -0.0150 0.0096  0.0311  44  PHE A CE1 
252  C  CE2 . PHE A 44  ? 0.1410 0.1771 0.2482 -0.0092 -0.0028 0.0177  44  PHE A CE2 
253  C  CZ  . PHE A 44  ? 0.1562 0.2264 0.1396 -0.0135 0.0069  -0.0355 44  PHE A CZ  
254  N  N   . ALA A 45  ? 0.1446 0.1097 0.2034 -0.0118 -0.0048 0.0392  45  ALA A N   
255  C  CA  . ALA A 45  ? 0.1220 0.2153 0.2244 -0.0197 0.0153  -0.0195 45  ALA A CA  
256  C  C   . ALA A 45  ? 0.1239 0.1471 0.1348 -0.0021 -0.0261 0.0629  45  ALA A C   
257  O  O   . ALA A 45  ? 0.1599 0.1599 0.1471 -0.0380 -0.0251 0.0499  45  ALA A O   
258  C  CB  . ALA A 45  ? 0.1425 0.1161 0.1570 -0.0222 0.0058  -0.0058 45  ALA A CB  
259  N  N   . SER A 46  ? 0.1377 0.1145 0.1481 -0.0104 -0.0230 0.0937  46  SER A N   
260  C  CA  . SER A 46  ? 0.1387 0.1180 0.1440 -0.0109 -0.0060 0.0442  46  SER A CA  
261  C  C   . SER A 46  ? 0.1154 0.1380 0.1108 0.0157  0.0022  0.0325  46  SER A C   
262  O  O   . SER A 46  ? 0.1586 0.1392 0.1276 -0.0141 -0.0131 0.0263  46  SER A O   
263  C  CB  . SER A 46  ? 0.1536 0.1239 0.1582 -0.0053 -0.0156 0.0396  46  SER A CB  
264  O  OG  . SER A 46  ? 0.1608 0.1400 0.1349 0.0016  -0.0268 0.0281  46  SER A OG  
265  N  N   . GLY A 47  ? 0.1097 0.1176 0.1458 0.0016  -0.0024 0.0402  47  GLY A N   
266  C  CA  . GLY A 47  ? 0.1250 0.1428 0.1250 0.0069  0.0068  0.0474  47  GLY A CA  
267  C  C   . GLY A 47  ? 0.1367 0.1223 0.1457 0.0017  0.0005  0.0425  47  GLY A C   
268  O  O   . GLY A 47  ? 0.1444 0.1166 0.1510 -0.0097 -0.0064 0.0362  47  GLY A O   
269  N  N   . LYS A 48  ? 0.1527 0.1477 0.1211 -0.0028 0.0006  0.0262  48  LYS A N   
270  C  CA  . LYS A 48  ? 0.1820 0.1356 0.2062 -0.0374 0.0313  0.0061  48  LYS A CA  
271  C  C   . LYS A 48  ? 0.1578 0.1388 0.1346 -0.0294 -0.0170 0.0332  48  LYS A C   
272  O  O   . LYS A 48  ? 0.1909 0.1395 0.1596 -0.0125 -0.0177 0.0274  48  LYS A O   
273  C  CB  . LYS A 48  ? 0.1898 0.1238 0.5041 -0.0171 0.1437  0.0452  48  LYS A CB  
274  N  N   . THR A 49  ? 0.1320 0.1240 0.1699 -0.0132 0.0050  0.0254  49  THR A N   
275  C  CA  . THR A 49  ? 0.1701 0.1151 0.1372 -0.0163 -0.0117 0.0098  49  THR A CA  
276  C  C   . THR A 49  ? 0.1375 0.1209 0.1720 -0.0151 -0.0105 0.0353  49  THR A C   
277  O  O   . THR A 49  ? 0.1726 0.1506 0.1648 -0.0175 -0.0135 0.0307  49  THR A O   
278  C  CB  . THR A 49  ? 0.1483 0.0955 0.1655 -0.0011 -0.0195 0.0259  49  THR A CB  
279  O  OG1 . THR A 49  ? 0.1392 0.1362 0.1883 -0.0136 -0.0068 0.0146  49  THR A OG1 
280  C  CG2 . THR A 49  ? 0.1543 0.1328 0.1651 -0.0149 -0.0034 0.0088  49  THR A CG2 
281  N  N   . SER A 50  ? 0.1697 0.1426 0.1506 -0.0142 -0.0172 0.0151  50  SER A N   
282  C  CA  . SER A 50  ? 0.2132 0.1493 0.1695 -0.0246 -0.0455 0.0224  50  SER A CA  
283  C  C   . SER A 50  ? 0.1925 0.1782 0.1735 -0.0345 -0.0561 0.0404  50  SER A C   
284  O  O   . SER A 50  ? 0.2335 0.1708 0.1725 -0.0186 -0.0542 0.0056  50  SER A O   
285  C  CB  . SER A 50  ? 0.2481 0.1821 0.1920 -0.0236 -0.0542 0.0399  50  SER A CB  
286  O  OG  . SER A 50  ? 0.2429 0.2140 0.2125 -0.0366 -0.0330 -0.0124 50  SER A OG  
287  N  N   . GLU A 51  ? 0.2567 0.2057 0.1911 -0.0566 -0.0625 0.0350  51  GLU A N   
288  C  CA  . GLU A 51  ? 0.2442 0.2418 0.2534 -0.0738 -0.0402 0.0025  51  GLU A CA  
289  C  C   . GLU A 51  ? 0.3129 0.1927 0.2048 -0.0699 -0.0387 0.0213  51  GLU A C   
290  O  O   . GLU A 51  ? 0.3270 0.1896 0.2701 -0.0773 0.0098  0.0138  51  GLU A O   
291  C  CB  . GLU A 51  ? 0.3342 0.2466 0.3629 -0.1255 -0.1064 -0.0049 51  GLU A CB  
292  N  N   . SER A 52  ? 0.2834 0.1621 0.2039 -0.0526 -0.0417 0.0037  52  SER A N   
293  C  CA  . SER A 52  ? 0.2942 0.1643 0.1694 -0.0563 -0.0239 0.0015  52  SER A CA  
294  C  C   . SER A 52  ? 0.1989 0.1650 0.1622 -0.0276 0.0226  -0.0046 52  SER A C   
295  O  O   . SER A 52  ? 0.2178 0.1487 0.2426 -0.0272 0.0128  -0.0023 52  SER A O   
296  C  CB  . SER A 52  ? 0.3378 0.2705 0.2573 -0.0381 -0.0134 -0.1115 52  SER A CB  
297  O  OG  . SER A 52  ? 0.3692 0.3394 0.2345 0.0257  0.0375  0.0427  52  SER A OG  
298  N  N   . GLY A 53  ? 0.2014 0.1361 0.1511 -0.0449 -0.0150 -0.0004 53  GLY A N   
299  C  CA  . GLY A 53  ? 0.2095 0.1434 0.1195 -0.0351 -0.0156 0.0292  53  GLY A CA  
300  C  C   . GLY A 53  ? 0.1702 0.1309 0.1325 -0.0137 -0.0015 0.0022  53  GLY A C   
301  O  O   . GLY A 53  ? 0.1723 0.1658 0.1322 -0.0201 -0.0204 0.0386  53  GLY A O   
302  N  N   . GLU A 54  ? 0.1918 0.1825 0.1365 -0.0531 -0.0138 -0.0022 54  GLU A N   
303  C  CA  . GLU A 54  ? 0.1583 0.1962 0.1537 -0.0131 -0.0024 0.0232  54  GLU A CA  
304  C  C   . GLU A 54  ? 0.1636 0.1668 0.0893 -0.0228 -0.0032 -0.0001 54  GLU A C   
305  O  O   . GLU A 54  ? 0.1743 0.1999 0.1495 -0.0352 -0.0254 0.0472  54  GLU A O   
306  C  CB  . GLU A 54  ? 0.2204 0.1675 0.2467 -0.0404 0.0855  0.0346  54  GLU A CB  
307  C  CG  . GLU A 54  ? 0.3016 0.1850 0.2005 -0.0352 0.0189  0.0137  54  GLU A CG  
308  C  CD  . GLU A 54  ? 0.5432 0.3507 0.3217 -0.0106 0.0981  -0.0857 54  GLU A CD  
309  O  OE1 . GLU A 54  ? 0.7339 0.3272 0.4241 0.0392  0.1733  -0.0667 54  GLU A OE1 
310  N  N   . LEU A 55  ? 0.1471 0.1448 0.1408 0.0069  -0.0221 0.0233  55  LEU A N   
311  C  CA  . LEU A 55  ? 0.1501 0.1300 0.1444 0.0048  -0.0062 0.0210  55  LEU A CA  
312  C  C   . LEU A 55  ? 0.1833 0.1094 0.1572 -0.0095 -0.0153 -0.0252 55  LEU A C   
313  O  O   . LEU A 55  ? 0.1578 0.1473 0.1583 -0.0329 0.0144  0.0078  55  LEU A O   
314  C  CB  . LEU A 55  ? 0.1395 0.1384 0.1501 -0.0050 -0.0181 0.0197  55  LEU A CB  
315  C  CG  . LEU A 55  ? 0.1315 0.1544 0.1950 -0.0081 0.0114  0.0171  55  LEU A CG  
316  C  CD1 . LEU A 55  ? 0.1505 0.1504 0.2015 -0.0228 0.0086  0.0331  55  LEU A CD1 
317  C  CD2 . LEU A 55  ? 0.1627 0.1078 0.2367 -0.0262 0.0267  -0.0031 55  LEU A CD2 
318  N  N   . HIS A 56  ? 0.2443 0.1597 0.1460 -0.0317 0.0233  -0.0180 56  HIS A N   
319  C  CA  . HIS A 56  ? 0.2736 0.1775 0.1685 -0.0436 0.0352  0.0080  56  HIS A CA  
320  C  C   . HIS A 56  ? 0.2300 0.2361 0.1699 0.0128  -0.0012 0.0583  56  HIS A C   
321  O  O   . HIS A 56  ? 0.2513 0.2254 0.2075 -0.0337 -0.0176 0.0409  56  HIS A O   
322  C  CB  . HIS A 56  ? 0.2350 0.1926 0.2224 -0.0325 0.0195  -0.0138 56  HIS A CB  
323  C  CG  . HIS A 56  ? 0.3266 0.2164 0.1941 -0.0405 0.0872  -0.0277 56  HIS A CG  
324  N  ND1 . HIS A 56  ? 0.4138 0.1921 0.3558 -0.0253 0.1565  0.0298  56  HIS A ND1 
325  C  CD2 . HIS A 56  ? 0.3253 0.2187 0.3463 -0.0262 0.0456  -0.0082 56  HIS A CD2 
326  C  CE1 . HIS A 56  ? 0.4445 0.1207 0.4437 -0.1424 0.0989  0.0271  56  HIS A CE1 
327  N  NE2 . HIS A 56  ? 0.4954 0.1876 0.4706 -0.0177 0.0334  -0.0052 56  HIS A NE2 
328  N  N   . GLY A 57  ? 0.2499 0.2020 0.2425 -0.0724 0.0222  -0.0269 57  GLY A N   
329  C  CA  . GLY A 57  ? 0.2335 0.2198 0.2391 -0.0835 0.0127  0.0153  57  GLY A CA  
330  C  C   . GLY A 57  ? 0.1642 0.1958 0.2309 0.0187  -0.0354 0.0346  57  GLY A C   
331  O  O   . GLY A 57  ? 0.2106 0.2142 0.2286 -0.0262 -0.0571 0.0727  57  GLY A O   
332  N  N   . LEU A 58  ? 0.1437 0.1352 0.2267 -0.0279 -0.0335 0.0428  58  LEU A N   
333  C  CA  . LEU A 58  ? 0.1589 0.1583 0.1760 -0.0111 0.0013  0.0320  58  LEU A CA  
334  C  C   . LEU A 58  ? 0.1198 0.1746 0.1880 0.0035  -0.0021 0.0286  58  LEU A C   
335  O  O   . LEU A 58  ? 0.1816 0.1711 0.2040 -0.0013 0.0034  0.0413  58  LEU A O   
336  C  CB  . LEU A 58  ? 0.1477 0.1413 0.1899 -0.0157 -0.0229 0.0189  58  LEU A CB  
337  C  CG  . LEU A 58  ? 0.1219 0.1554 0.2478 -0.0021 -0.0156 0.0525  58  LEU A CG  
338  C  CD1 . LEU A 58  ? 0.1765 0.1786 0.1858 -0.0127 -0.0107 0.0307  58  LEU A CD1 
339  C  CD2 . LEU A 58  ? 0.1901 0.1675 0.2009 -0.0101 0.0033  0.0450  58  LEU A CD2 
340  N  N   . THR A 59  ? 0.1487 0.1521 0.1782 -0.0296 -0.0132 0.0449  59  THR A N   
341  C  CA  . THR A 59  ? 0.1446 0.1457 0.1609 -0.0189 -0.0168 0.0358  59  THR A CA  
342  C  C   . THR A 59  ? 0.1935 0.1282 0.1816 -0.0332 0.0100  0.0318  59  THR A C   
343  O  O   . THR A 59  ? 0.2061 0.1691 0.2165 -0.0371 0.0192  0.0111  59  THR A O   
344  C  CB  . THR A 59  ? 0.1735 0.1503 0.1772 -0.0311 -0.0187 0.0246  59  THR A CB  
345  O  OG1 . THR A 59  ? 0.1708 0.1634 0.2025 -0.0290 -0.0067 0.0370  59  THR A OG1 
346  C  CG2 . THR A 59  ? 0.1498 0.1604 0.2133 -0.0203 -0.0211 0.0190  59  THR A CG2 
347  N  N   . THR A 60  ? 0.1955 0.1619 0.2167 -0.0559 0.0268  0.0238  60  THR A N   
348  C  CA  . THR A 60  ? 0.1652 0.2171 0.1593 -0.0496 0.0063  0.0258  60  THR A CA  
349  C  C   . THR A 60  ? 0.2040 0.1456 0.1666 -0.0292 -0.0186 0.0159  60  THR A C   
350  O  O   . THR A 60  ? 0.1915 0.1457 0.1688 -0.0252 -0.0040 0.0173  60  THR A O   
351  C  CB  . THR A 60  ? 0.1885 0.2136 0.1831 -0.0095 -0.0262 0.0115  60  THR A CB  
352  O  OG1 . THR A 60  ? 0.2307 0.1776 0.1868 -0.0376 -0.0039 0.0264  60  THR A OG1 
353  C  CG2 . THR A 60  ? 0.2214 0.2696 0.1945 -0.0324 -0.0267 0.0520  60  THR A CG2 
354  N  N   . GLU A 61  ? 0.2043 0.1878 0.1659 -0.0114 -0.0098 0.0175  61  GLU A N   
355  C  CA  . GLU A 61  ? 0.2041 0.1612 0.2187 0.0045  -0.0057 -0.0358 61  GLU A CA  
356  C  C   . GLU A 61  ? 0.1801 0.1906 0.1738 -0.0011 -0.0014 0.0260  61  GLU A C   
357  O  O   . GLU A 61  ? 0.1888 0.1962 0.2191 0.0000  -0.0233 0.0014  61  GLU A O   
358  C  CB  . GLU A 61  ? 0.2624 0.1430 0.3305 -0.0092 0.0615  -0.0431 61  GLU A CB  
359  N  N   . GLU A 62  ? 0.1768 0.1634 0.1866 -0.0127 0.0040  0.0314  62  GLU A N   
360  C  CA  . GLU A 62  ? 0.2075 0.1598 0.1827 -0.0124 0.0227  0.0512  62  GLU A CA  
361  C  C   . GLU A 62  ? 0.1658 0.1470 0.2051 -0.0269 0.0023  0.0125  62  GLU A C   
362  O  O   . GLU A 62  ? 0.1643 0.1762 0.2468 -0.0205 0.0046  -0.0073 62  GLU A O   
363  C  CB  . GLU A 62  ? 0.2514 0.2164 0.2277 -0.0504 0.0329  0.0749  62  GLU A CB  
364  C  CG  . GLU A 62  ? 0.3244 0.2662 0.2374 -0.0449 0.0792  0.0722  62  GLU A CG  
365  C  CD  . GLU A 62  ? 0.2988 0.3345 0.2252 -0.0259 0.0310  0.0385  62  GLU A CD  
366  O  OE1 . GLU A 62  ? 0.2920 0.3379 0.2200 -0.0413 -0.0034 0.0668  62  GLU A OE1 
367  O  OE2 . GLU A 62  ? 0.4305 0.5438 0.3972 0.0591  0.1192  -0.0254 62  GLU A OE2 
368  N  N   . GLU A 63  ? 0.1475 0.1499 0.1907 -0.0093 -0.0117 0.0470  63  GLU A N   
369  C  CA  . GLU A 63  ? 0.1397 0.1543 0.1858 -0.0201 -0.0205 0.0561  63  GLU A CA  
370  C  C   . GLU A 63  ? 0.1288 0.1394 0.1654 -0.0132 -0.0170 0.0105  63  GLU A C   
371  O  O   . GLU A 63  ? 0.1420 0.1175 0.1775 -0.0069 -0.0215 0.0362  63  GLU A O   
372  C  CB  . GLU A 63  ? 0.1695 0.1867 0.1261 0.0032  -0.0161 0.0537  63  GLU A CB  
373  C  CG  . GLU A 63  ? 0.2213 0.1956 0.1747 -0.0197 -0.0049 0.0327  63  GLU A CG  
374  C  CD  . GLU A 63  ? 0.2149 0.2463 0.3329 0.0634  -0.0064 0.0466  63  GLU A CD  
375  O  OE1 . GLU A 63  ? 0.2177 0.2298 0.2559 0.0008  -0.0245 0.0273  63  GLU A OE1 
376  O  OE2 . GLU A 63  ? 0.1861 0.2183 0.4933 -0.0032 0.0142  0.1061  63  GLU A OE2 
377  N  N   . PHE A 64  ? 0.1461 0.1382 0.1604 -0.0132 -0.0046 0.0143  64  PHE A N   
378  C  CA  . PHE A 64  ? 0.1328 0.1254 0.1567 -0.0047 0.0000  0.0356  64  PHE A CA  
379  C  C   . PHE A 64  ? 0.1286 0.1071 0.1527 -0.0058 -0.0002 0.0145  64  PHE A C   
380  O  O   . PHE A 64  ? 0.1490 0.1490 0.1702 0.0027  -0.0103 0.0237  64  PHE A O   
381  C  CB  . PHE A 64  ? 0.1403 0.1381 0.1631 0.0047  -0.0441 0.0235  64  PHE A CB  
382  C  CG  . PHE A 64  ? 0.1299 0.1339 0.1603 -0.0052 -0.0384 0.0079  64  PHE A CG  
383  C  CD1 . PHE A 64  ? 0.2015 0.1218 0.1732 -0.0161 -0.0143 0.0107  64  PHE A CD1 
384  C  CD2 . PHE A 64  ? 0.1614 0.1546 0.2261 0.0195  0.0005  0.0440  64  PHE A CD2 
385  C  CE1 . PHE A 64  ? 0.1787 0.1600 0.1924 -0.0292 0.0139  0.0086  64  PHE A CE1 
386  C  CE2 . PHE A 64  ? 0.2569 0.1197 0.2565 -0.0160 -0.0380 0.0641  64  PHE A CE2 
387  C  CZ  . PHE A 64  ? 0.2182 0.1799 0.2005 -0.0431 -0.0266 0.0269  64  PHE A CZ  
388  N  N   . VAL A 65  ? 0.1179 0.1153 0.1553 -0.0034 -0.0086 0.0041  65  VAL A N   
389  C  CA  . VAL A 65  ? 0.1491 0.1138 0.1103 -0.0109 -0.0026 -0.0161 65  VAL A CA  
390  C  C   . VAL A 65  ? 0.1433 0.1419 0.1529 -0.0224 0.0054  0.0259  65  VAL A C   
391  O  O   . VAL A 65  ? 0.1326 0.1375 0.1557 -0.0170 0.0051  0.0471  65  VAL A O   
392  C  CB  . VAL A 65  ? 0.1447 0.1193 0.1524 -0.0217 -0.0037 0.0120  65  VAL A CB  
393  C  CG1 . VAL A 65  ? 0.1570 0.1625 0.1611 -0.0066 -0.0031 0.0251  65  VAL A CG1 
394  C  CG2 . VAL A 65  ? 0.1586 0.1287 0.2007 -0.0138 0.0337  0.0088  65  VAL A CG2 
395  N  N   . GLU A 66  ? 0.1175 0.1291 0.1860 -0.0168 -0.0104 0.0318  66  GLU A N   
396  C  CA  . GLU A 66  ? 0.1316 0.1726 0.1780 0.0112  -0.0282 0.0438  66  GLU A CA  
397  C  C   . GLU A 66  ? 0.1378 0.1426 0.1910 -0.0070 -0.0190 0.0389  66  GLU A C   
398  O  O   . GLU A 66  ? 0.1995 0.1583 0.1713 0.0129  0.0227  0.0452  66  GLU A O   
399  C  CB  . GLU A 66  ? 0.1638 0.1926 0.1959 -0.0187 -0.0204 0.0042  66  GLU A CB  
400  C  CG  . GLU A 66  ? 0.1999 0.2191 0.1636 0.0118  -0.0074 0.0443  66  GLU A CG  
401  C  CD  . GLU A 66  ? 0.1570 0.1777 0.1893 -0.0003 0.0030  0.0866  66  GLU A CD  
402  O  OE1 . GLU A 66  ? 0.1457 0.2061 0.1971 0.0024  0.0050  0.0735  66  GLU A OE1 
403  O  OE2 . GLU A 66  ? 0.1843 0.2172 0.1967 -0.0256 -0.0167 0.0814  66  GLU A OE2 
404  N  N   . GLY A 67  ? 0.1551 0.1125 0.1496 -0.0025 -0.0071 0.0110  67  GLY A N   
405  C  CA  . GLY A 67  ? 0.1671 0.1586 0.1587 -0.0181 0.0082  0.0205  67  GLY A CA  
406  C  C   . GLY A 67  ? 0.1428 0.1380 0.1416 -0.0209 0.0084  0.0183  67  GLY A C   
407  O  O   . GLY A 67  ? 0.1474 0.1374 0.1425 0.0061  0.0034  0.0186  67  GLY A O   
408  N  N   . ILE A 68  ? 0.1542 0.1325 0.1413 -0.0169 -0.0147 0.0126  68  ILE A N   
409  C  CA  . ILE A 68  ? 0.1428 0.1191 0.1343 -0.0065 -0.0064 0.0206  68  ILE A CA  
410  C  C   . ILE A 68  ? 0.1594 0.0993 0.1279 0.0150  -0.0242 0.0371  68  ILE A C   
411  O  O   . ILE A 68  ? 0.1525 0.1165 0.1478 -0.0082 -0.0271 0.0288  68  ILE A O   
412  C  CB  . ILE A 68  ? 0.1426 0.1513 0.1443 0.0003  0.0071  0.0052  68  ILE A CB  
413  C  CG1 . ILE A 68  ? 0.1695 0.2463 0.1734 0.0254  -0.0200 0.0088  68  ILE A CG1 
414  C  CG2 . ILE A 68  ? 0.1893 0.2036 0.1414 0.0110  -0.0028 0.0161  68  ILE A CG2 
415  C  CD1 . ILE A 68  ? 0.2280 0.3008 0.2121 -0.0222 -0.0843 0.0057  68  ILE A CD1 
416  N  N   . TYR A 69  ? 0.1285 0.1229 0.1355 0.0047  -0.0123 0.0258  69  TYR A N   
417  C  CA  . TYR A 69  ? 0.1158 0.1084 0.1362 0.0020  -0.0030 0.0325  69  TYR A CA  
418  C  C   . TYR A 69  ? 0.1327 0.1240 0.1311 -0.0171 -0.0080 0.0399  69  TYR A C   
419  O  O   . TYR A 69  ? 0.1367 0.1273 0.1615 0.0031  0.0049  0.0515  69  TYR A O   
420  C  CB  . TYR A 69  ? 0.1115 0.1231 0.1660 -0.0132 -0.0057 0.0209  69  TYR A CB  
421  C  CG  . TYR A 69  ? 0.1301 0.1098 0.1579 -0.0173 -0.0046 0.0247  69  TYR A CG  
422  C  CD1 . TYR A 69  ? 0.1255 0.1339 0.1471 -0.0011 0.0044  0.0432  69  TYR A CD1 
423  C  CD2 . TYR A 69  ? 0.1181 0.1057 0.1652 0.0072  0.0180  0.0182  69  TYR A CD2 
424  C  CE1 . TYR A 69  ? 0.1163 0.1261 0.1481 -0.0048 -0.0164 0.0317  69  TYR A CE1 
425  C  CE2 . TYR A 69  ? 0.1296 0.1514 0.1541 0.0193  0.0056  0.0130  69  TYR A CE2 
426  C  CZ  . TYR A 69  ? 0.1336 0.1418 0.1269 0.0038  -0.0025 0.0409  69  TYR A CZ  
427  O  OH  . TYR A 69  ? 0.1568 0.1666 0.1681 0.0023  -0.0035 0.0613  69  TYR A OH  
428  N  N   . LYS A 70  ? 0.1171 0.1255 0.1547 -0.0030 0.0102  0.0283  70  LYS A N   
429  C  CA  . LYS A 70  ? 0.1288 0.1538 0.1505 -0.0310 -0.0087 0.0189  70  LYS A CA  
430  C  C   . LYS A 70  ? 0.1297 0.1334 0.1557 -0.0059 -0.0142 0.0293  70  LYS A C   
431  O  O   . LYS A 70  ? 0.1295 0.1544 0.1831 -0.0060 -0.0191 0.0439  70  LYS A O   
432  C  CB  . LYS A 70  ? 0.1611 0.1796 0.1882 -0.0075 -0.0116 0.0084  70  LYS A CB  
433  C  CG  . LYS A 70  ? 0.1404 0.3010 0.2964 0.0108  0.0311  -0.0536 70  LYS A CG  
434  C  CD  . LYS A 70  ? 0.2807 0.4405 0.3520 0.0841  0.0302  -0.1241 70  LYS A CD  
435  C  CE  . LYS A 70  ? 0.3507 0.4378 0.4022 0.0331  0.1302  -0.0674 70  LYS A CE  
436  N  NZ  . LYS A 70  ? 0.5271 0.6964 0.5011 -0.0605 0.2255  -0.2271 70  LYS A NZ  
437  N  N   . VAL A 71  ? 0.1497 0.1322 0.1828 -0.0122 -0.0365 0.0247  71  VAL A N   
438  C  CA  . VAL A 71  ? 0.1208 0.1451 0.1784 -0.0122 -0.0211 0.0701  71  VAL A CA  
439  C  C   . VAL A 71  ? 0.1500 0.1245 0.1820 -0.0290 -0.0091 0.0489  71  VAL A C   
440  O  O   . VAL A 71  ? 0.1629 0.1654 0.1950 -0.0247 -0.0052 0.0625  71  VAL A O   
441  C  CB  . VAL A 71  ? 0.1425 0.1336 0.2011 -0.0127 -0.0132 0.0359  71  VAL A CB  
442  C  CG1 . VAL A 71  ? 0.1625 0.1990 0.1927 -0.0220 -0.0106 -0.0035 71  VAL A CG1 
443  C  CG2 . VAL A 71  ? 0.1931 0.1386 0.1852 -0.0015 0.0035  -0.0103 71  VAL A CG2 
444  N  N   . GLU A 72  ? 0.1289 0.1580 0.1687 -0.0175 -0.0150 0.0301  72  GLU A N   
445  C  CA  . GLU A 72  ? 0.1730 0.1522 0.1403 -0.0198 -0.0203 0.0196  72  GLU A CA  
446  C  C   . GLU A 72  ? 0.1310 0.1437 0.1322 -0.0221 -0.0129 0.0478  72  GLU A C   
447  O  O   . GLU A 72  ? 0.1538 0.1641 0.1727 -0.0352 -0.0329 0.0531  72  GLU A O   
448  C  CB  . GLU A 72  ? 0.2310 0.1722 0.1935 -0.0104 -0.0145 -0.0035 72  GLU A CB  
449  C  CG  . GLU A 72  ? 0.2655 0.3135 0.3706 -0.1086 0.0025  -0.0906 72  GLU A CG  
450  C  CD  . GLU A 72  ? 0.4466 0.3194 0.3486 0.0652  0.1929  0.0190  72  GLU A CD  
451  O  OE1 . GLU A 72  ? 0.4687 0.3032 0.3746 0.0864  0.0844  -0.0182 72  GLU A OE1 
452  N  N   . ILE A 73  ? 0.1507 0.1478 0.1388 -0.0280 -0.0031 0.0141  73  ILE A N   
453  C  CA  . ILE A 73  ? 0.1193 0.1715 0.1823 -0.0299 -0.0141 0.0183  73  ILE A CA  
454  C  C   . ILE A 73  ? 0.1590 0.1724 0.1195 -0.0283 0.0011  0.0376  73  ILE A C   
455  O  O   . ILE A 73  ? 0.1604 0.1658 0.1278 -0.0264 0.0073  0.0273  73  ILE A O   
456  C  CB  . ILE A 73  ? 0.1676 0.1479 0.1300 -0.0240 0.0041  0.0248  73  ILE A CB  
457  C  CG1 . ILE A 73  ? 0.1810 0.1526 0.1921 -0.0071 0.0091  0.0486  73  ILE A CG1 
458  C  CG2 . ILE A 73  ? 0.1449 0.1633 0.1892 -0.0192 0.0334  -0.0141 73  ILE A CG2 
459  C  CD1 . ILE A 73  ? 0.2103 0.1911 0.1970 0.0015  0.0101  0.0383  73  ILE A CD1 
460  N  N   . ASP A 74  ? 0.1552 0.1392 0.1371 -0.0218 0.0118  0.0085  74  ASP A N   
461  C  CA  . ASP A 74  ? 0.1679 0.1225 0.1929 -0.0154 0.0149  0.0245  74  ASP A CA  
462  C  C   . ASP A 74  ? 0.1530 0.1728 0.1530 -0.0354 -0.0017 0.0067  74  ASP A C   
463  O  O   . ASP A 74  ? 0.1535 0.1466 0.2150 -0.0163 -0.0121 0.0029  74  ASP A O   
464  C  CB  . ASP A 74  ? 0.1616 0.1381 0.1918 -0.0355 -0.0028 0.0173  74  ASP A CB  
465  C  CG  . ASP A 74  ? 0.1899 0.2041 0.2360 -0.0132 -0.0055 0.0062  74  ASP A CG  
466  O  OD1 . ASP A 74  ? 0.1793 0.2344 0.2507 -0.0270 0.0425  -0.0363 74  ASP A OD1 
467  O  OD2 . ASP A 74  ? 0.2118 0.2067 0.3270 0.0372  0.0601  0.1074  74  ASP A OD2 
468  N  N   . THR A 75  ? 0.1406 0.1614 0.1633 -0.0299 0.0070  0.0403  75  THR A N   
469  C  CA  . THR A 75  ? 0.1981 0.1288 0.1629 -0.0296 0.0327  0.0330  75  THR A CA  
470  C  C   . THR A 75  ? 0.1427 0.1945 0.1668 -0.0507 0.0251  0.0220  75  THR A C   
471  O  O   . THR A 75  ? 0.1330 0.1890 0.2203 -0.0363 -0.0120 0.0605  75  THR A O   
472  C  CB  . THR A 75  ? 0.2045 0.1533 0.1652 -0.0148 0.0479  0.0566  75  THR A CB  
473  O  OG1 . THR A 75  ? 0.1519 0.1954 0.1796 -0.0030 0.0067  0.0338  75  THR A OG1 
474  C  CG2 . THR A 75  ? 0.2261 0.1477 0.1987 -0.0059 0.0370  0.0072  75  THR A CG2 
475  N  N   . LYS A 76  ? 0.1244 0.1899 0.1847 -0.0556 0.0092  0.0031  76  LYS A N   
476  C  CA  . LYS A 76  ? 0.1387 0.2121 0.1588 -0.0440 0.0058  0.0293  76  LYS A CA  
477  C  C   . LYS A 76  ? 0.1150 0.1532 0.2015 0.0005  -0.0040 0.0248  76  LYS A C   
478  O  O   . LYS A 76  ? 0.1324 0.1891 0.2080 -0.0208 0.0182  0.0087  76  LYS A O   
479  C  CB  . LYS A 76  ? 0.1655 0.2496 0.2315 -0.0100 -0.0339 -0.0443 76  LYS A CB  
480  C  CG  . LYS A 76  ? 0.2248 0.3057 0.2448 0.0210  0.0130  0.0106  76  LYS A CG  
481  C  CD  . LYS A 76  ? 0.3128 0.4870 0.2748 0.1127  -0.1317 -0.0909 76  LYS A CD  
482  N  N   . SER A 77  ? 0.1528 0.1627 0.1780 -0.0085 -0.0143 0.0139  77  SER A N   
483  C  CA  . SER A 77  ? 0.1627 0.1447 0.1865 -0.0149 -0.0142 0.0130  77  SER A CA  
484  C  C   . SER A 77  ? 0.1526 0.1420 0.1852 -0.0224 -0.0115 0.0031  77  SER A C   
485  O  O   . SER A 77  ? 0.1395 0.1732 0.2082 -0.0157 -0.0222 -0.0057 77  SER A O   
486  C  CB  . SER A 77  ? 0.2168 0.1459 0.2234 -0.0153 0.0079  0.0213  77  SER A CB  
487  O  OG  . SER A 77  ? 0.2391 0.1452 0.3025 0.0134  0.0206  0.0405  77  SER A OG  
488  N  N   . TYR A 78  ? 0.1729 0.1216 0.2255 -0.0136 0.0056  0.0198  78  TYR A N   
489  C  CA  . TYR A 78  ? 0.1686 0.1399 0.1736 0.0019  -0.0231 0.0510  78  TYR A CA  
490  C  C   . TYR A 78  ? 0.1505 0.1446 0.1962 -0.0227 -0.0049 0.0061  78  TYR A C   
491  O  O   . TYR A 78  ? 0.1331 0.1790 0.2027 -0.0177 -0.0299 0.0270  78  TYR A O   
492  C  CB  . TYR A 78  ? 0.1711 0.1474 0.1652 -0.0115 0.0045  0.0210  78  TYR A CB  
493  C  CG  . TYR A 78  ? 0.1567 0.1530 0.1704 0.0129  0.0072  0.0206  78  TYR A CG  
494  C  CD1 . TYR A 78  ? 0.1408 0.1871 0.1605 0.0065  0.0152  0.0272  78  TYR A CD1 
495  C  CD2 . TYR A 78  ? 0.1393 0.1746 0.1900 -0.0076 -0.0350 0.0378  78  TYR A CD2 
496  C  CE1 . TYR A 78  ? 0.2075 0.1733 0.1657 0.0292  0.0288  0.0227  78  TYR A CE1 
497  C  CE2 . TYR A 78  ? 0.1675 0.1519 0.1645 0.0111  -0.0074 0.0266  78  TYR A CE2 
498  C  CZ  . TYR A 78  ? 0.1594 0.1752 0.1588 -0.0151 -0.0001 0.0119  78  TYR A CZ  
499  O  OH  . TYR A 78  ? 0.1687 0.1605 0.1980 0.0068  -0.0018 0.0232  78  TYR A OH  
500  N  N   . TRP A 79  ? 0.1646 0.1882 0.1549 -0.0226 0.0051  0.0237  79  TRP A N   
501  C  CA  . TRP A 79  ? 0.1525 0.1853 0.1442 -0.0223 -0.0119 0.0486  79  TRP A CA  
502  C  C   . TRP A 79  ? 0.1653 0.1674 0.1962 -0.0232 -0.0068 0.0423  79  TRP A C   
503  O  O   . TRP A 79  ? 0.1439 0.2325 0.2188 -0.0431 -0.0032 0.0542  79  TRP A O   
504  C  CB  . TRP A 79  ? 0.1712 0.1414 0.1869 -0.0215 -0.0031 0.0490  79  TRP A CB  
505  C  CG  . TRP A 79  ? 0.1466 0.1679 0.2088 -0.0178 -0.0123 0.0321  79  TRP A CG  
506  C  CD1 . TRP A 79  ? 0.1357 0.1431 0.1996 -0.0348 0.0233  -0.0005 79  TRP A CD1 
507  C  CD2 . TRP A 79  ? 0.1444 0.1707 0.1547 -0.0180 -0.0082 0.0528  79  TRP A CD2 
508  N  NE1 . TRP A 79  ? 0.1617 0.1448 0.1488 -0.0053 0.0032  0.0278  79  TRP A NE1 
509  C  CE2 . TRP A 79  ? 0.1376 0.1778 0.1820 -0.0182 0.0050  0.0327  79  TRP A CE2 
510  C  CE3 . TRP A 79  ? 0.1470 0.2248 0.1610 -0.0220 -0.0175 0.0011  79  TRP A CE3 
511  C  CZ2 . TRP A 79  ? 0.1604 0.1823 0.1672 -0.0179 -0.0020 0.0396  79  TRP A CZ2 
512  C  CZ3 . TRP A 79  ? 0.1362 0.2425 0.2301 -0.0310 0.0063  0.0304  79  TRP A CZ3 
513  C  CH2 . TRP A 79  ? 0.1820 0.1767 0.2261 -0.0095 -0.0230 0.0506  79  TRP A CH2 
514  N  N   . LYS A 80  ? 0.1422 0.1786 0.2139 -0.0098 -0.0124 0.0477  80  LYS A N   
515  C  CA  . LYS A 80  ? 0.1317 0.1971 0.2048 0.0073  -0.0049 0.0447  80  LYS A CA  
516  C  C   . LYS A 80  ? 0.1645 0.1756 0.2527 -0.0242 -0.0188 0.0260  80  LYS A C   
517  O  O   . LYS A 80  ? 0.1442 0.1884 0.3103 -0.0167 -0.0200 0.0071  80  LYS A O   
518  C  CB  . LYS A 80  ? 0.1718 0.1975 0.3408 0.0250  0.0433  0.0238  80  LYS A CB  
519  N  N   . ALA A 81  ? 0.1402 0.1778 0.2519 -0.0212 -0.0470 0.0074  81  ALA A N   
520  C  CA  . ALA A 81  ? 0.2042 0.1698 0.2423 0.0018  -0.0502 0.0358  81  ALA A CA  
521  C  C   . ALA A 81  ? 0.1554 0.2163 0.2714 -0.0420 -0.0259 0.0029  81  ALA A C   
522  O  O   . ALA A 81  ? 0.2115 0.2348 0.3241 -0.0727 -0.0726 0.0181  81  ALA A O   
523  C  CB  . ALA A 81  ? 0.2770 0.1911 0.2119 -0.0246 -0.0711 0.0259  81  ALA A CB  
524  N  N   . LEU A 82  ? 0.1993 0.1819 0.2395 -0.0102 -0.0100 0.0108  82  LEU A N   
525  C  CA  . LEU A 82  ? 0.1445 0.2038 0.2341 -0.0258 -0.0652 0.0243  82  LEU A CA  
526  C  C   . LEU A 82  ? 0.1734 0.1816 0.2517 -0.0278 0.0131  -0.0114 82  LEU A C   
527  O  O   . LEU A 82  ? 0.1920 0.2304 0.2670 -0.0391 0.0380  0.0011  82  LEU A O   
528  C  CB  . LEU A 82  ? 0.1356 0.1993 0.2606 -0.0622 -0.0206 -0.0153 82  LEU A CB  
529  C  CG  . LEU A 82  ? 0.1841 0.2849 0.2984 -0.0728 -0.0002 -0.0155 82  LEU A CG  
530  C  CD1 . LEU A 82  ? 0.2724 0.3704 0.2889 -0.0039 -0.0455 -0.0503 82  LEU A CD1 
531  C  CD2 . LEU A 82  ? 0.1974 0.4081 0.3441 -0.0420 0.0561  -0.1422 82  LEU A CD2 
532  N  N   . GLY A 83  ? 0.1406 0.2189 0.2807 -0.0196 0.0037  0.0268  83  GLY A N   
533  C  CA  . GLY A 83  ? 0.1586 0.2105 0.2938 -0.0152 -0.0211 -0.0405 83  GLY A CA  
534  C  C   . GLY A 83  ? 0.1614 0.2252 0.2158 -0.0142 0.0017  -0.0008 83  GLY A C   
535  O  O   . GLY A 83  ? 0.1701 0.2610 0.2896 -0.0258 0.0256  0.0108  83  GLY A O   
536  N  N   . ILE A 84  ? 0.1480 0.2101 0.2398 -0.0381 -0.0129 -0.0042 84  ILE A N   
537  C  CA  . ILE A 84  ? 0.1272 0.2829 0.2452 -0.0184 0.0208  0.0021  84  ILE A CA  
538  C  C   . ILE A 84  ? 0.1842 0.2347 0.3022 -0.0663 -0.0459 0.0556  84  ILE A C   
539  O  O   . ILE A 84  ? 0.2633 0.2194 0.3049 -0.0847 -0.0619 0.0385  84  ILE A O   
540  C  CB  . ILE A 84  ? 0.2174 0.3086 0.1669 0.0418  0.0078  -0.0360 84  ILE A CB  
541  C  CG1 . ILE A 84  ? 0.3568 0.2876 0.3754 0.1786  -0.1945 -0.1444 84  ILE A CG1 
542  C  CG2 . ILE A 84  ? 0.2262 0.2382 0.1981 -0.0154 0.0190  0.0234  84  ILE A CG2 
543  C  CD1 . ILE A 84  ? 0.4701 0.4377 0.4255 -0.0964 0.0390  -0.0190 84  ILE A CD1 
544  N  N   . SER A 85  ? 0.1526 0.1953 0.3040 -0.0187 -0.0271 -0.0025 85  SER A N   
545  C  CA  . SER A 85  ? 0.1519 0.2341 0.2781 -0.0314 -0.0247 -0.0327 85  SER A CA  
546  C  C   . SER A 85  ? 0.1414 0.2059 0.2392 -0.0380 0.0146  -0.0493 85  SER A C   
547  O  O   . SER A 85  ? 0.2387 0.3191 0.2776 -0.0390 -0.0005 0.0574  85  SER A O   
548  C  CB  . SER A 85  ? 0.1796 0.3523 0.3496 0.0458  0.0562  -0.0656 85  SER A CB  
549  O  OG  . SER A 85  ? 0.2354 0.3313 0.5086 -0.0027 -0.0308 -0.1163 85  SER A OG  
550  N  N   . PRO A 86  ? 0.1633 0.1753 0.1983 -0.0108 0.0085  -0.0110 86  PRO A N   
551  C  CA  . PRO A 86  ? 0.1400 0.2654 0.2164 -0.0305 0.0021  -0.0492 86  PRO A CA  
552  C  C   . PRO A 86  ? 0.1545 0.2235 0.2040 -0.0095 0.0105  -0.0676 86  PRO A C   
553  O  O   . PRO A 86  ? 0.2032 0.2254 0.1950 -0.0063 -0.0311 -0.0183 86  PRO A O   
554  C  CB  . PRO A 86  ? 0.2016 0.3220 0.2340 -0.0876 0.0276  -0.0660 86  PRO A CB  
555  C  CG  . PRO A 86  ? 0.2342 0.3194 0.2014 -0.1347 0.0161  0.0131  86  PRO A CG  
556  C  CD  . PRO A 86  ? 0.2350 0.2884 0.3118 -0.0700 -0.0023 0.0653  86  PRO A CD  
557  N  N   . PHE A 87  ? 0.1718 0.1714 0.1701 -0.0156 -0.0101 -0.0374 87  PHE A N   
558  C  CA  . PHE A 87  ? 0.1657 0.1713 0.1798 -0.0099 -0.0178 -0.0370 87  PHE A CA  
559  C  C   . PHE A 87  ? 0.1734 0.1326 0.1697 0.0121  0.0056  -0.0511 87  PHE A C   
560  O  O   . PHE A 87  ? 0.1776 0.1668 0.1941 -0.0131 0.0179  -0.0682 87  PHE A O   
561  C  CB  . PHE A 87  ? 0.1738 0.1634 0.2131 -0.0223 0.0253  -0.0146 87  PHE A CB  
562  C  CG  . PHE A 87  ? 0.2017 0.1214 0.2025 -0.0176 0.0203  0.0210  87  PHE A CG  
563  C  CD1 . PHE A 87  ? 0.1724 0.2756 0.1657 -0.0321 0.0070  0.0362  87  PHE A CD1 
564  C  CD2 . PHE A 87  ? 0.2110 0.1633 0.1988 0.0051  0.0024  -0.0150 87  PHE A CD2 
565  C  CE1 . PHE A 87  ? 0.3081 0.1952 0.2096 -0.0190 -0.0413 0.0072  87  PHE A CE1 
566  C  CE2 . PHE A 87  ? 0.2816 0.2208 0.2306 0.0169  -0.0373 -0.0054 87  PHE A CE2 
567  C  CZ  . PHE A 87  ? 0.2680 0.1743 0.1969 -0.0339 -0.1029 -0.0498 87  PHE A CZ  
568  N  N   . HIS A 88  ? 0.1688 0.1368 0.1749 0.0046  0.0051  -0.0192 88  HIS A N   
569  C  CA  . HIS A 88  ? 0.1701 0.1224 0.1701 -0.0122 -0.0065 -0.0056 88  HIS A CA  
570  C  C   . HIS A 88  ? 0.1510 0.1641 0.1545 0.0060  0.0086  -0.0174 88  HIS A C   
571  O  O   . HIS A 88  ? 0.1673 0.1589 0.2042 -0.0154 -0.0254 0.0032  88  HIS A O   
572  C  CB  . HIS A 88  ? 0.1845 0.1533 0.1652 -0.0426 -0.0084 -0.0050 88  HIS A CB  
573  C  CG  . HIS A 88  ? 0.1457 0.1555 0.2203 -0.0020 0.0141  -0.0374 88  HIS A CG  
574  N  ND1 . HIS A 88  ? 0.2160 0.1658 0.2765 0.0068  -0.0060 0.0089  88  HIS A ND1 
575  C  CD2 . HIS A 88  ? 0.1790 0.1225 0.1316 -0.0359 -0.0010 -0.0293 88  HIS A CD2 
576  C  CE1 . HIS A 88  ? 0.1394 0.1444 0.1927 0.0067  -0.0388 -0.0409 88  HIS A CE1 
577  N  NE2 . HIS A 88  ? 0.2359 0.1965 0.2188 -0.0180 -0.0287 -0.0056 88  HIS A NE2 
578  N  N   . GLU A 89  ? 0.1891 0.1384 0.1955 -0.0130 0.0072  0.0080  89  GLU A N   
579  C  CA  . GLU A 89  ? 0.1760 0.1533 0.2457 -0.0056 -0.0387 0.0410  89  GLU A CA  
580  C  C   . GLU A 89  ? 0.2150 0.2213 0.1866 -0.0696 -0.0220 0.0455  89  GLU A C   
581  O  O   . GLU A 89  ? 0.2474 0.2327 0.2139 -0.0615 -0.0390 0.0409  89  GLU A O   
582  C  CB  . GLU A 89  ? 0.1998 0.1489 0.3574 -0.0059 -0.0201 0.0131  89  GLU A CB  
583  C  CG  . GLU A 89  ? 0.3114 0.2140 0.3474 0.0207  -0.0163 0.0156  89  GLU A CG  
584  C  CD  . GLU A 89  ? 0.3381 0.2098 0.4148 0.0950  0.0383  -0.0219 89  GLU A CD  
585  O  OE1 . GLU A 89  ? 0.4227 0.3483 0.4516 0.0846  -0.0496 -0.0387 89  GLU A OE1 
586  O  OE2 . GLU A 89  ? 0.4346 0.4202 0.3970 -0.1371 0.0533  -0.1236 89  GLU A OE2 
587  N  N   . HIS A 90  ? 0.2062 0.2564 0.1795 -0.0694 -0.0202 0.0135  90  HIS A N   
588  C  CA  . HIS A 90  ? 0.2295 0.1771 0.1594 -0.0613 -0.0194 0.0372  90  HIS A CA  
589  C  C   . HIS A 90  ? 0.1662 0.3838 0.1094 -0.0119 -0.0385 -0.0048 90  HIS A C   
590  O  O   . HIS A 90  ? 0.1767 0.4688 0.1585 -0.0229 -0.0091 0.0860  90  HIS A O   
591  C  CB  . HIS A 90  ? 0.4078 0.2728 0.2896 -0.1665 0.0131  0.0807  90  HIS A CB  
592  C  CG  . HIS A 90  ? 0.4552 0.4154 0.2472 -0.1180 0.1993  0.0158  90  HIS A CG  
593  N  ND1 . HIS A 90  ? 0.5952 0.6167 0.3700 -0.1857 0.0365  0.0618  90  HIS A ND1 
594  C  CD2 . HIS A 90  ? 0.5606 0.4761 0.4886 -0.0610 0.1468  -0.0212 90  HIS A CD2 
595  C  CE1 . HIS A 90  ? 0.5224 0.4564 0.6357 -0.2364 0.1086  0.0757  90  HIS A CE1 
596  N  NE2 . HIS A 90  ? 0.8217 0.2329 0.8016 0.0177  0.1538  -0.1912 90  HIS A NE2 
597  N  N   . ALA A 91  ? 0.1860 0.4341 0.1095 0.0111  -0.0231 0.0683  91  ALA A N   
598  C  CA  . ALA A 91  ? 0.2018 0.3502 0.1500 -0.0034 -0.0145 0.1369  91  ALA A CA  
599  C  C   . ALA A 91  ? 0.1789 0.4987 0.1859 0.0137  0.0278  0.1978  91  ALA A C   
600  O  O   . ALA A 91  ? 0.1996 0.3515 0.2137 -0.0177 0.0098  0.1256  91  ALA A O   
601  C  CB  . ALA A 91  ? 0.1667 0.3547 0.2558 0.0849  0.0555  0.1229  91  ALA A CB  
602  N  N   . GLU A 92  ? 0.1968 0.3430 0.3038 -0.0068 0.0005  0.1516  92  GLU A N   
603  C  CA  . GLU A 92  ? 0.2363 0.2537 0.2777 -0.0164 0.0697  0.0517  92  GLU A CA  
604  C  C   . GLU A 92  ? 0.2202 0.2908 0.3127 -0.0211 0.0422  0.1384  92  GLU A C   
605  O  O   . GLU A 92  ? 0.2076 0.2510 0.2547 -0.0374 0.0171  0.0475  92  GLU A O   
606  C  CB  . GLU A 92  ? 0.1259 0.2283 0.1783 0.0133  -0.0141 0.0192  92  GLU A CB  
607  C  CG  . GLU A 92  ? 0.2609 0.2334 0.2037 -0.0003 -0.1080 -0.0466 92  GLU A CG  
608  C  CD  . GLU A 92  ? 0.2488 0.2055 0.2031 0.0121  0.0421  -0.0733 92  GLU A CD  
609  O  OE1 . GLU A 92  ? 0.1907 0.2019 0.1785 0.0080  -0.0139 -0.0445 92  GLU A OE1 
610  O  OE2 . GLU A 92  ? 0.2735 0.2589 0.2337 0.0141  -0.0214 0.0536  92  GLU A OE2 
611  N  N   . VAL A 93  ? 0.2054 0.2396 0.2336 -0.0296 -0.0173 0.1449  93  VAL A N   
612  C  CA  . VAL A 93  ? 0.2352 0.1749 0.1923 -0.0559 -0.0403 0.0292  93  VAL A CA  
613  C  C   . VAL A 93  ? 0.1863 0.1272 0.1719 -0.0001 0.0222  0.0658  93  VAL A C   
614  O  O   . VAL A 93  ? 0.1590 0.1513 0.1850 -0.0308 -0.0178 0.0479  93  VAL A O   
615  C  CB  . VAL A 93  ? 0.2459 0.1962 0.2697 0.0081  -0.0715 -0.0173 93  VAL A CB  
616  C  CG1 . VAL A 93  ? 0.3113 0.2160 0.3760 -0.0301 0.0170  -0.0353 93  VAL A CG1 
617  C  CG2 . VAL A 93  ? 0.3049 0.2975 0.2870 0.0229  0.0090  -0.0921 93  VAL A CG2 
618  N  N   . VAL A 94  ? 0.1560 0.1561 0.1526 -0.0085 -0.0045 0.0210  94  VAL A N   
619  C  CA  . VAL A 94  ? 0.1378 0.1227 0.1041 -0.0034 -0.0069 0.0282  94  VAL A CA  
620  C  C   . VAL A 94  ? 0.1547 0.0985 0.1157 -0.0218 -0.0081 0.0238  94  VAL A C   
621  O  O   . VAL A 94  ? 0.1910 0.1129 0.1233 0.0232  -0.0100 0.0291  94  VAL A O   
622  C  CB  . VAL A 94  ? 0.1711 0.1709 0.1158 0.0158  0.0090  0.0225  94  VAL A CB  
623  C  CG1 . VAL A 94  ? 0.1894 0.1515 0.2026 0.0115  0.0330  0.0084  94  VAL A CG1 
624  C  CG2 . VAL A 94  ? 0.1846 0.2456 0.1627 -0.0013 0.0148  -0.0695 94  VAL A CG2 
625  N  N   . PHE A 95  ? 0.1414 0.1304 0.1159 0.0039  -0.0042 0.0279  95  PHE A N   
626  C  CA  . PHE A 95  ? 0.1556 0.1216 0.1319 0.0193  -0.0116 0.0312  95  PHE A CA  
627  C  C   . PHE A 95  ? 0.1392 0.1075 0.1396 0.0081  -0.0284 0.0245  95  PHE A C   
628  O  O   . PHE A 95  ? 0.1362 0.1342 0.1790 0.0316  -0.0003 0.0390  95  PHE A O   
629  C  CB  . PHE A 95  ? 0.1634 0.1117 0.1689 0.0192  -0.0125 -0.0002 95  PHE A CB  
630  C  CG  . PHE A 95  ? 0.1666 0.0998 0.1927 0.0102  0.0042  0.0034  95  PHE A CG  
631  C  CD1 . PHE A 95  ? 0.1556 0.1661 0.2067 0.0049  0.0107  -0.0403 95  PHE A CD1 
632  C  CD2 . PHE A 95  ? 0.2036 0.1248 0.1508 0.0093  -0.0085 0.0170  95  PHE A CD2 
633  C  CE1 . PHE A 95  ? 0.1906 0.2301 0.2330 0.0403  -0.0232 -0.0241 95  PHE A CE1 
634  C  CE2 . PHE A 95  ? 0.2741 0.1462 0.1452 -0.0196 0.0095  0.0005  95  PHE A CE2 
635  C  CZ  . PHE A 95  ? 0.2580 0.1787 0.1738 -0.0028 -0.0496 0.0150  95  PHE A CZ  
636  N  N   . THR A 96  ? 0.1300 0.1325 0.1628 0.0111  -0.0305 0.0357  96  THR A N   
637  C  CA  . THR A 96  ? 0.1397 0.1304 0.1829 0.0099  0.0005  0.0444  96  THR A CA  
638  C  C   . THR A 96  ? 0.1662 0.1220 0.1780 0.0083  -0.0096 0.0428  96  THR A C   
639  O  O   . THR A 96  ? 0.2085 0.1431 0.1658 0.0446  0.0134  0.0368  96  THR A O   
640  C  CB  . THR A 96  ? 0.1399 0.1561 0.2199 0.0216  0.0051  0.0218  96  THR A CB  
641  O  OG1 . THR A 96  ? 0.1710 0.1999 0.2103 -0.0133 -0.0267 0.0242  96  THR A OG1 
642  C  CG2 . THR A 96  ? 0.1549 0.2323 0.2238 -0.0072 -0.0146 0.0399  96  THR A CG2 
643  N  N   . ALA A 97  ? 0.1427 0.1393 0.1468 -0.0077 0.0048  0.0205  97  ALA A N   
644  C  CA  . ALA A 97  ? 0.1453 0.1453 0.1309 -0.0040 0.0054  0.0330  97  ALA A CA  
645  C  C   . ALA A 97  ? 0.1561 0.1145 0.1648 0.0045  0.0082  0.0151  97  ALA A C   
646  O  O   . ALA A 97  ? 0.1544 0.1240 0.1525 0.0011  0.0068  0.0270  97  ALA A O   
647  C  CB  . ALA A 97  ? 0.1650 0.1951 0.1430 0.0308  -0.0118 0.0131  97  ALA A CB  
648  N  N   . ASN A 98  ? 0.1475 0.1263 0.1338 -0.0150 0.0106  0.0375  98  ASN A N   
649  C  CA  . ASN A 98  ? 0.1585 0.1285 0.1415 0.0103  0.0278  0.0152  98  ASN A CA  
650  C  C   . ASN A 98  ? 0.1370 0.1572 0.1828 -0.0292 0.0467  0.0171  98  ASN A C   
651  O  O   . ASN A 98  ? 0.1520 0.1485 0.1731 -0.0241 0.0258  0.0288  98  ASN A O   
652  C  CB  . ASN A 98  ? 0.1578 0.1546 0.1490 0.0076  0.0158  0.0132  98  ASN A CB  
653  C  CG  . ASN A 98  ? 0.1568 0.1504 0.1508 0.0086  0.0226  0.0394  98  ASN A CG  
654  O  OD1 . ASN A 98  ? 0.1729 0.1893 0.1980 -0.0035 -0.0034 0.0382  98  ASN A OD1 
655  N  ND2 . ASN A 98  ? 0.1051 0.1422 0.1554 0.0104  0.0102  0.0273  98  ASN A ND2 
656  N  N   . ASP A 99  ? 0.1453 0.1639 0.1890 -0.0287 0.0292  0.0432  99  ASP A N   
657  C  CA  . ASP A 99  ? 0.1766 0.1318 0.2131 -0.0148 -0.0116 0.0460  99  ASP A CA  
658  C  C   . ASP A 99  ? 0.1636 0.1664 0.2038 -0.0180 -0.0101 0.0520  99  ASP A C   
659  O  O   . ASP A 99  ? 0.1606 0.1883 0.2558 -0.0147 -0.0213 0.0055  99  ASP A O   
660  C  CB  . ASP A 99  ? 0.1661 0.2922 0.1812 -0.0314 -0.0121 0.0622  99  ASP A CB  
661  C  CG  . ASP A 99  ? 0.2988 0.3460 0.2003 -0.0652 -0.0055 0.0497  99  ASP A CG  
662  O  OD1 . ASP A 99  ? 0.2023 0.2716 0.3211 -0.0062 -0.0167 -0.0062 99  ASP A OD1 
663  O  OD2 . ASP A 99  ? 0.2711 0.5010 0.2473 -0.0457 0.0117  -0.0223 99  ASP A OD2 
664  N  N   . SER A 100 ? 0.1508 0.1840 0.2683 -0.0042 0.0272  0.0287  100 SER A N   
665  C  CA  . SER A 100 ? 0.1530 0.2057 0.3653 0.0103  0.0318  -0.0072 100 SER A CA  
666  C  C   . SER A 100 ? 0.2108 0.2098 0.3453 -0.0456 0.0608  -0.0243 100 SER A C   
667  O  O   . SER A 100 ? 0.3341 0.2823 0.2854 0.0751  -0.0109 -0.0289 100 SER A O   
668  C  CB  . SER A 100 ? 0.2957 0.2521 0.3054 0.0995  -0.0244 -0.0534 100 SER A CB  
669  O  OG  . SER A 100 ? 0.3815 0.2557 0.4448 0.0890  -0.1385 -0.0173 100 SER A OG  
670  N  N   . GLY A 101 ? 0.2255 0.2119 0.2530 -0.0286 0.0360  -0.0239 101 GLY A N   
671  C  CA  . GLY A 101 ? 0.2101 0.1980 0.2691 -0.0364 0.0441  -0.0022 101 GLY A CA  
672  C  C   . GLY A 101 ? 0.1924 0.1699 0.2336 0.0173  0.0299  0.0465  101 GLY A C   
673  O  O   . GLY A 101 ? 0.1975 0.1671 0.2109 -0.0069 0.0351  0.0354  101 GLY A O   
674  N  N   . PRO A 102 ? 0.1864 0.1627 0.2442 -0.0093 0.0854  0.0324  102 PRO A N   
675  C  CA  . PRO A 102 ? 0.1663 0.1759 0.1849 -0.0081 0.0344  -0.0167 102 PRO A CA  
676  C  C   . PRO A 102 ? 0.1830 0.1565 0.2426 -0.0087 0.0572  0.0098  102 PRO A C   
677  O  O   . PRO A 102 ? 0.2023 0.1575 0.2024 -0.0132 0.0597  0.0175  102 PRO A O   
678  C  CB  . PRO A 102 ? 0.2283 0.2340 0.2027 -0.0289 0.0539  -0.0154 102 PRO A CB  
679  C  CG  . PRO A 102 ? 0.2733 0.2263 0.2202 -0.0243 0.0457  -0.0098 102 PRO A CG  
680  C  CD  . PRO A 102 ? 0.1977 0.2424 0.2543 -0.0428 0.0567  0.0522  102 PRO A CD  
681  N  N   . ARG A 103 ? 0.1715 0.1400 0.2173 0.0046  0.0546  0.0291  103 ARG A N   
682  C  CA  . ARG A 103 ? 0.1734 0.1489 0.1977 -0.0007 0.0587  0.0216  103 ARG A CA  
683  C  C   . ARG A 103 ? 0.1945 0.1333 0.2244 0.0164  0.0364  0.0250  103 ARG A C   
684  O  O   . ARG A 103 ? 0.1585 0.1965 0.2118 -0.0129 0.0280  0.0493  103 ARG A O   
685  C  CB  . ARG A 103 ? 0.1686 0.1888 0.2123 0.0128  0.0247  0.0714  103 ARG A CB  
686  C  CG  . ARG A 103 ? 0.1619 0.1553 0.2660 -0.0267 0.0103  0.0535  103 ARG A CG  
687  C  CD  . ARG A 103 ? 0.1760 0.1469 0.3191 -0.0105 0.0041  0.0581  103 ARG A CD  
688  N  NE  . ARG A 103 ? 0.1646 0.2127 0.4142 0.0215  0.0122  0.0456  103 ARG A NE  
689  C  CZ  . ARG A 103 ? 0.1835 0.2565 0.3915 0.0267  0.0250  0.0392  103 ARG A CZ  
690  N  NH1 . ARG A 103 ? 0.1697 0.2139 0.4004 -0.0176 0.0331  0.0202  103 ARG A NH1 
691  N  NH2 . ARG A 103 ? 0.1661 0.2655 0.4574 -0.0087 -0.0175 0.0336  103 ARG A NH2 
692  N  N   . ARG A 104 ? 0.1478 0.1961 0.1542 -0.0024 0.0404  0.0159  104 ARG A N   
693  C  CA  . ARG A 104 ? 0.1536 0.2487 0.1799 -0.0035 0.0146  0.0515  104 ARG A CA  
694  C  C   . ARG A 104 ? 0.1513 0.1365 0.1582 0.0072  0.0194  -0.0112 104 ARG A C   
695  O  O   . ARG A 104 ? 0.1742 0.1797 0.2078 0.0430  0.0435  0.0423  104 ARG A O   
696  C  CB  . ARG A 104 ? 0.2308 0.2730 0.1611 -0.0533 0.0287  0.0503  104 ARG A CB  
697  N  N   . TYR A 105 ? 0.1432 0.1420 0.1702 -0.0002 0.0203  0.0372  105 TYR A N   
698  C  CA  . TYR A 105 ? 0.1244 0.1360 0.1566 0.0089  -0.0001 0.0211  105 TYR A CA  
699  C  C   . TYR A 105 ? 0.1227 0.1120 0.2048 0.0185  0.0007  0.0334  105 TYR A C   
700  O  O   . TYR A 105 ? 0.1351 0.1821 0.2066 -0.0141 0.0104  0.0514  105 TYR A O   
701  C  CB  . TYR A 105 ? 0.1423 0.1225 0.1820 0.0105  0.0159  0.0278  105 TYR A CB  
702  C  CG  . TYR A 105 ? 0.1532 0.0946 0.1934 0.0016  0.0261  0.0312  105 TYR A CG  
703  C  CD1 . TYR A 105 ? 0.1979 0.0896 0.1738 0.0016  0.0019  0.0489  105 TYR A CD1 
704  C  CD2 . TYR A 105 ? 0.1489 0.1448 0.1704 -0.0125 0.0192  0.0617  105 TYR A CD2 
705  C  CE1 . TYR A 105 ? 0.1674 0.1299 0.1712 -0.0296 0.0331  0.0312  105 TYR A CE1 
706  C  CE2 . TYR A 105 ? 0.1552 0.1464 0.1841 -0.0134 0.0129  0.0330  105 TYR A CE2 
707  C  CZ  . TYR A 105 ? 0.1557 0.1400 0.1493 -0.0324 0.0250  -0.0058 105 TYR A CZ  
708  O  OH  . TYR A 105 ? 0.1513 0.1350 0.2460 -0.0170 0.0022  0.0262  105 TYR A OH  
709  N  N   . THR A 106 ? 0.1363 0.1221 0.1474 0.0053  0.0160  0.0239  106 THR A N   
710  C  CA  . THR A 106 ? 0.1563 0.1393 0.1192 -0.0121 0.0072  0.0116  106 THR A CA  
711  C  C   . THR A 106 ? 0.1589 0.1424 0.1085 0.0077  0.0022  0.0138  106 THR A C   
712  O  O   . THR A 106 ? 0.1388 0.1765 0.1554 0.0112  0.0311  0.0322  106 THR A O   
713  C  CB  . THR A 106 ? 0.1954 0.1462 0.1514 -0.0109 -0.0068 -0.0080 106 THR A CB  
714  O  OG1 . THR A 106 ? 0.3145 0.2011 0.1477 -0.0237 0.0025  -0.0256 106 THR A OG1 
715  C  CG2 . THR A 106 ? 0.2376 0.1797 0.2477 -0.0722 0.0185  0.0009  106 THR A CG2 
716  N  N   . ILE A 107 ? 0.1509 0.1552 0.1192 -0.0054 0.0103  0.0273  107 ILE A N   
717  C  CA  . ILE A 107 ? 0.1351 0.1738 0.1100 0.0015  0.0014  0.0162  107 ILE A CA  
718  C  C   . ILE A 107 ? 0.1276 0.1755 0.1450 0.0221  -0.0057 0.0415  107 ILE A C   
719  O  O   . ILE A 107 ? 0.1443 0.2302 0.1309 0.0096  -0.0008 0.0277  107 ILE A O   
720  C  CB  . ILE A 107 ? 0.1473 0.1916 0.1908 0.0307  -0.0230 -0.0152 107 ILE A CB  
721  C  CG1 . ILE A 107 ? 0.2214 0.1702 0.2093 0.0354  -0.0275 -0.0086 107 ILE A CG1 
722  C  CG2 . ILE A 107 ? 0.1928 0.2481 0.1966 0.0529  -0.0062 -0.0528 107 ILE A CG2 
723  C  CD1 . ILE A 107 ? 0.1882 0.2115 0.2071 0.0158  -0.0095 -0.0034 107 ILE A CD1 
724  N  N   . ALA A 108 ? 0.1277 0.1957 0.1350 0.0034  0.0003  0.0328  108 ALA A N   
725  C  CA  . ALA A 108 ? 0.1906 0.2218 0.1114 -0.0207 -0.0349 0.0281  108 ALA A CA  
726  C  C   . ALA A 108 ? 0.1456 0.2706 0.1450 -0.0179 -0.0215 0.0701  108 ALA A C   
727  O  O   . ALA A 108 ? 0.1406 0.4700 0.1371 0.0295  0.0014  0.0633  108 ALA A O   
728  C  CB  . ALA A 108 ? 0.2270 0.2402 0.1679 -0.0525 0.0115  0.0242  108 ALA A CB  
729  N  N   . ALA A 109 ? 0.1450 0.2153 0.1367 -0.0286 -0.0054 0.0698  109 ALA A N   
730  C  CA  . ALA A 109 ? 0.1491 0.1462 0.1449 -0.0371 -0.0105 0.0550  109 ALA A CA  
731  C  C   . ALA A 109 ? 0.1878 0.1181 0.1238 -0.0420 -0.0224 0.0092  109 ALA A C   
732  O  O   . ALA A 109 ? 0.1716 0.2348 0.1330 -0.0684 -0.0066 0.0365  109 ALA A O   
733  C  CB  . ALA A 109 ? 0.1695 0.1456 0.1904 -0.0534 -0.0092 0.0462  109 ALA A CB  
734  N  N   . LEU A 110 ? 0.1322 0.1143 0.1115 -0.0127 0.0028  0.0027  110 LEU A N   
735  C  CA  . LEU A 110 ? 0.1227 0.1141 0.1504 -0.0117 0.0085  -0.0085 110 LEU A CA  
736  C  C   . LEU A 110 ? 0.1406 0.0940 0.1221 -0.0341 -0.0155 -0.0085 110 LEU A C   
737  O  O   . LEU A 110 ? 0.1439 0.1410 0.1143 -0.0154 -0.0062 -0.0140 110 LEU A O   
738  C  CB  . LEU A 110 ? 0.1659 0.1359 0.1344 -0.0178 0.0314  0.0066  110 LEU A CB  
739  C  CG  . LEU A 110 ? 0.1802 0.1361 0.1847 -0.0330 0.0112  0.0396  110 LEU A CG  
740  C  CD1 . LEU A 110 ? 0.1839 0.1107 0.2197 0.0108  0.0255  -0.0278 110 LEU A CD1 
741  C  CD2 . LEU A 110 ? 0.2690 0.1784 0.1880 -0.0126 0.0149  0.0584  110 LEU A CD2 
742  N  N   . LEU A 111 ? 0.1188 0.1220 0.1334 -0.0317 0.0048  -0.0069 111 LEU A N   
743  C  CA  . LEU A 111 ? 0.1429 0.1332 0.1256 -0.0196 0.0115  -0.0010 111 LEU A CA  
744  C  C   . LEU A 111 ? 0.1571 0.1066 0.1269 -0.0454 -0.0012 -0.0054 111 LEU A C   
745  O  O   . LEU A 111 ? 0.1479 0.1146 0.1221 -0.0282 0.0137  -0.0079 111 LEU A O   
746  C  CB  . LEU A 111 ? 0.1465 0.1418 0.1307 -0.0096 0.0158  0.0077  111 LEU A CB  
747  C  CG  . LEU A 111 ? 0.1757 0.1262 0.1364 -0.0321 0.0011  0.0185  111 LEU A CG  
748  C  CD1 . LEU A 111 ? 0.1628 0.1585 0.2144 -0.0165 0.0148  0.0421  111 LEU A CD1 
749  C  CD2 . LEU A 111 ? 0.1759 0.1504 0.1518 -0.0193 0.0198  -0.0073 111 LEU A CD2 
750  N  N   . SER A 112 ? 0.1398 0.1367 0.1167 -0.0274 0.0076  -0.0264 112 SER A N   
751  C  CA  . SER A 112 ? 0.1401 0.1430 0.1377 -0.0169 0.0051  0.0075  112 SER A CA  
752  C  C   . SER A 112 ? 0.1223 0.1662 0.0992 -0.0022 0.0198  0.0236  112 SER A C   
753  O  O   . SER A 112 ? 0.1405 0.1198 0.1630 -0.0370 0.0094  0.0052  112 SER A O   
754  C  CB  . SER A 112 ? 0.1801 0.1491 0.1080 0.0117  0.0125  -0.0082 112 SER A CB  
755  O  OG  . SER A 112 ? 0.2558 0.1545 0.1715 0.0169  0.0303  0.0107  112 SER A OG  
756  N  N   . PRO A 113 ? 0.1405 0.1039 0.1398 -0.0308 -0.0053 -0.0044 113 PRO A N   
757  C  CA  . PRO A 113 ? 0.1529 0.1194 0.1510 -0.0126 0.0286  0.0195  113 PRO A CA  
758  C  C   . PRO A 113 ? 0.1517 0.1336 0.1606 0.0156  0.0080  -0.0153 113 PRO A C   
759  O  O   . PRO A 113 ? 0.1605 0.1276 0.1617 0.0072  0.0102  -0.0056 113 PRO A O   
760  C  CB  . PRO A 113 ? 0.1571 0.1325 0.1897 -0.0029 0.0551  -0.0152 113 PRO A CB  
761  C  CG  . PRO A 113 ? 0.1664 0.1795 0.1932 -0.0351 0.0390  -0.0176 113 PRO A CG  
762  C  CD  . PRO A 113 ? 0.1470 0.1432 0.1761 -0.0204 0.0228  -0.0204 113 PRO A CD  
763  N  N   . TYR A 114 ? 0.1295 0.1228 0.1271 -0.0084 0.0167  0.0123  114 TYR A N   
764  C  CA  . TYR A 114 ? 0.1494 0.1158 0.1170 0.0061  0.0068  0.0033  114 TYR A CA  
765  C  C   . TYR A 114 ? 0.1458 0.1150 0.1331 0.0112  -0.0022 0.0017  114 TYR A C   
766  O  O   . TYR A 114 ? 0.1426 0.1861 0.1329 0.0087  0.0092  -0.0064 114 TYR A O   
767  C  CB  . TYR A 114 ? 0.1565 0.1497 0.1119 -0.0046 0.0076  -0.0056 114 TYR A CB  
768  C  CG  . TYR A 114 ? 0.1408 0.1396 0.1377 -0.0211 0.0159  0.0135  114 TYR A CG  
769  C  CD1 . TYR A 114 ? 0.1542 0.2697 0.1693 0.0097  0.0251  -0.1003 114 TYR A CD1 
770  C  CD2 . TYR A 114 ? 0.1554 0.1441 0.1732 0.0006  -0.0002 -0.0058 114 TYR A CD2 
771  C  CE1 . TYR A 114 ? 0.1382 0.4940 0.2319 0.0060  0.0519  -0.1036 114 TYR A CE1 
772  C  CE2 . TYR A 114 ? 0.2255 0.2269 0.1739 -0.0022 0.0270  -0.0797 114 TYR A CE2 
773  C  CZ  . TYR A 114 ? 0.1907 0.3143 0.2100 0.0645  0.0635  -0.0604 114 TYR A CZ  
774  O  OH  . TYR A 114 ? 0.2556 0.5122 0.2764 0.1542  0.0874  -0.0826 114 TYR A OH  
775  N  N   . SER A 115 ? 0.1324 0.1287 0.1339 -0.0125 0.0114  0.0016  115 SER A N   
776  C  CA  . SER A 115 ? 0.1294 0.1271 0.1378 -0.0218 0.0216  -0.0058 115 SER A CA  
777  C  C   . SER A 115 ? 0.1354 0.1272 0.1149 -0.0228 -0.0144 -0.0029 115 SER A C   
778  O  O   . SER A 115 ? 0.1414 0.1807 0.1424 -0.0075 -0.0200 -0.0120 115 SER A O   
779  C  CB  . SER A 115 ? 0.1571 0.1523 0.1328 -0.0302 -0.0103 -0.0157 115 SER A CB  
780  O  OG  . SER A 115 ? 0.2110 0.1798 0.1847 0.0125  0.0107  0.0037  115 SER A OG  
781  N  N   . TYR A 116 ? 0.1369 0.1220 0.1115 -0.0090 -0.0135 -0.0133 116 TYR A N   
782  C  CA  . TYR A 116 ? 0.1289 0.1365 0.0925 0.0075  -0.0205 0.0022  116 TYR A CA  
783  C  C   . TYR A 116 ? 0.1339 0.1163 0.1030 -0.0077 -0.0040 -0.0148 116 TYR A C   
784  O  O   . TYR A 116 ? 0.1278 0.1250 0.1190 0.0071  -0.0139 -0.0110 116 TYR A O   
785  C  CB  . TYR A 116 ? 0.1199 0.1463 0.1104 0.0061  0.0056  0.0085  116 TYR A CB  
786  C  CG  . TYR A 116 ? 0.1584 0.1292 0.1717 0.0304  -0.0360 0.0040  116 TYR A CG  
787  C  CD1 . TYR A 116 ? 0.1920 0.1354 0.1940 0.0389  -0.0310 0.0045  116 TYR A CD1 
788  C  CD2 . TYR A 116 ? 0.2275 0.1506 0.1936 0.0200  -0.0098 -0.0014 116 TYR A CD2 
789  C  CE1 . TYR A 116 ? 0.1909 0.1491 0.1894 0.0096  -0.0484 -0.0215 116 TYR A CE1 
790  C  CE2 . TYR A 116 ? 0.2500 0.1733 0.2298 -0.0058 -0.0044 0.0271  116 TYR A CE2 
791  C  CZ  . TYR A 116 ? 0.2116 0.1138 0.2044 -0.0233 0.0020  0.0119  116 TYR A CZ  
792  O  OH  . TYR A 116 ? 0.2482 0.1564 0.2687 0.0220  -0.0706 -0.0492 116 TYR A OH  
793  N  N   . SER A 117 ? 0.1330 0.1311 0.1141 0.0133  -0.0160 0.0048  117 SER A N   
794  C  CA  A SER A 117 ? 0.1551 0.2134 0.0829 0.0402  -0.0068 0.0029  117 SER A CA  
795  C  CA  B SER A 117 ? 0.1588 0.2093 0.0843 0.0247  -0.0006 -0.0046 117 SER A CA  
796  C  C   . SER A 117 ? 0.1710 0.2081 0.1055 0.0450  -0.0050 -0.0080 117 SER A C   
797  O  O   . SER A 117 ? 0.1429 0.3106 0.1334 0.0421  0.0017  0.0057  117 SER A O   
798  C  CB  A SER A 117 ? 0.2337 0.2403 0.1747 0.1350  -0.0234 -0.0434 117 SER A CB  
799  C  CB  B SER A 117 ? 0.2776 0.2117 0.1844 0.0959  -0.0085 -0.1062 117 SER A CB  
800  O  OG  A SER A 117 ? 0.2582 0.1541 0.2251 0.0060  -0.0211 -0.0832 117 SER A OG  
801  O  OG  B SER A 117 ? 0.2021 0.2476 0.2611 0.0624  -0.0306 -0.0194 117 SER A OG  
802  N  N   . THR A 118 ? 0.1314 0.2955 0.1167 -0.0005 0.0170  -0.0071 118 THR A N   
803  C  CA  . THR A 118 ? 0.1744 0.3146 0.1377 0.0390  0.0133  0.0479  118 THR A CA  
804  C  C   . THR A 118 ? 0.1803 0.3884 0.1265 0.0317  0.0173  0.0234  118 THR A C   
805  O  O   . THR A 118 ? 0.1708 0.3527 0.1435 0.0599  0.0071  -0.0037 118 THR A O   
806  C  CB  . THR A 118 ? 0.1553 0.2985 0.2976 0.0621  -0.0267 0.0297  118 THR A CB  
807  O  OG1 . THR A 118 ? 0.3248 0.3368 0.3827 0.0479  0.0229  0.0931  118 THR A OG1 
808  C  CG2 . THR A 118 ? 0.2077 0.3568 0.2514 -0.0636 -0.0171 0.0585  118 THR A CG2 
809  N  N   . THR A 119 ? 0.1311 0.2814 0.1493 -0.0014 -0.0106 0.0243  119 THR A N   
810  C  CA  A THR A 119 ? 0.1559 0.1978 0.0865 0.0376  0.0017  0.0125  119 THR A CA  
811  C  CA  B THR A 119 ? 0.1608 0.1918 0.0977 0.0227  0.0146  0.0068  119 THR A CA  
812  C  C   . THR A 119 ? 0.1488 0.1528 0.1074 0.0104  0.0164  0.0004  119 THR A C   
813  O  O   . THR A 119 ? 0.1318 0.2138 0.1792 0.0173  0.0045  0.0359  119 THR A O   
814  C  CB  A THR A 119 ? 0.2305 0.2198 0.1575 -0.0854 0.0105  0.0124  119 THR A CB  
815  C  CB  B THR A 119 ? 0.2354 0.1747 0.2292 -0.0443 -0.0313 0.0205  119 THR A CB  
816  O  OG1 A THR A 119 ? 0.2422 0.2193 0.1612 -0.0090 0.0418  0.0798  119 THR A OG1 
817  O  OG1 B THR A 119 ? 0.2425 0.1731 0.2670 -0.0354 0.0432  0.0866  119 THR A OG1 
818  C  CG2 A THR A 119 ? 0.2634 0.1058 0.1822 0.0130  0.0605  -0.0446 119 THR A CG2 
819  C  CG2 B THR A 119 ? 0.2296 0.1031 0.1880 -0.0493 0.0427  0.0349  119 THR A CG2 
820  N  N   . ALA A 120 ? 0.1329 0.1952 0.1285 0.0256  0.0119  0.0403  120 ALA A N   
821  C  CA  . ALA A 120 ? 0.1506 0.1461 0.1289 0.0200  0.0211  0.0382  120 ALA A CA  
822  C  C   . ALA A 120 ? 0.1404 0.1244 0.1622 0.0266  0.0105  0.0380  120 ALA A C   
823  O  O   . ALA A 120 ? 0.1502 0.2037 0.1639 0.0482  0.0173  0.0270  120 ALA A O   
824  C  CB  . ALA A 120 ? 0.1586 0.1708 0.2125 -0.0013 0.0202  0.0031  120 ALA A CB  
825  N  N   . VAL A 121 ? 0.1435 0.1341 0.1403 0.0185  0.0187  0.0199  121 VAL A N   
826  C  CA  . VAL A 121 ? 0.1635 0.1530 0.1457 0.0127  0.0190  0.0286  121 VAL A CA  
827  C  C   . VAL A 121 ? 0.1685 0.1317 0.1674 0.0343  0.0287  0.0367  121 VAL A C   
828  O  O   . VAL A 121 ? 0.1558 0.1561 0.1967 0.0243  0.0396  0.0388  121 VAL A O   
829  C  CB  . VAL A 121 ? 0.2018 0.1880 0.1804 0.0021  -0.0144 0.0160  121 VAL A CB  
830  C  CG1 . VAL A 121 ? 0.3055 0.1857 0.2319 0.0139  -0.0005 -0.0071 121 VAL A CG1 
831  C  CG2 . VAL A 121 ? 0.2580 0.2585 0.2835 -0.0515 -0.0351 0.0495  121 VAL A CG2 
832  N  N   . VAL A 122 ? 0.1621 0.1360 0.1652 0.0155  0.0220  0.0208  122 VAL A N   
833  C  CA  . VAL A 122 ? 0.1587 0.1596 0.1971 -0.0122 0.0624  0.0064  122 VAL A CA  
834  C  C   . VAL A 122 ? 0.1730 0.1704 0.1799 0.0004  0.0156  0.0484  122 VAL A C   
835  O  O   . VAL A 122 ? 0.2077 0.1701 0.2032 0.0392  0.0330  0.0433  122 VAL A O   
836  C  CB  . VAL A 122 ? 0.1841 0.1545 0.2019 -0.0092 0.0176  0.0452  122 VAL A CB  
837  C  CG1 . VAL A 122 ? 0.2143 0.2008 0.1805 -0.0250 0.0199  0.0432  122 VAL A CG1 
838  C  CG2 . VAL A 122 ? 0.1920 0.2091 0.1527 -0.0270 -0.0138 0.0267  122 VAL A CG2 
839  N  N   . THR A 123 ? 0.1703 0.1544 0.1938 0.0182  0.0331  0.0037  123 THR A N   
840  C  CA  . THR A 123 ? 0.2055 0.1722 0.2260 0.0206  0.0736  -0.0115 123 THR A CA  
841  C  C   . THR A 123 ? 0.2225 0.2111 0.1589 0.0107  0.0629  -0.0009 123 THR A C   
842  O  O   . THR A 123 ? 0.2017 0.1975 0.2442 0.0294  0.0438  0.0241  123 THR A O   
843  C  CB  . THR A 123 ? 0.2045 0.2656 0.3573 0.0175  0.0668  -0.0487 123 THR A CB  
844  O  OG1 . THR A 123 ? 0.3920 0.3387 0.3464 0.0615  -0.0997 -0.1065 123 THR A OG1 
845  C  CG2 . THR A 123 ? 0.2434 0.3380 0.3842 -0.0854 0.0475  -0.0655 123 THR A CG2 
846  N  N   . ASN A 124 ? 0.2423 0.2540 0.2978 0.0392  0.1268  0.0125  124 ASN A N   
847  C  CA  . ASN A 124 ? 0.2722 0.2410 0.3000 0.0345  0.1539  0.0413  124 ASN A CA  
848  C  C   . ASN A 124 ? 0.5573 0.2984 0.3523 -0.0894 0.1710  -0.0523 124 ASN A C   
849  O  O   . ASN A 124 ? 0.6400 0.4231 0.4731 -0.1113 0.2184  -0.1681 124 ASN A O   
850  C  CB  . ASN A 124 ? 0.2858 0.2806 0.4270 0.0127  0.1360  0.0122  124 ASN A CB  
851  C  CG  . ASN A 124 ? 0.2423 0.3828 0.3874 0.0142  0.0866  0.0191  124 ASN A CG  
852  O  OD1 . ASN A 124 ? 0.3971 0.4440 0.4209 -0.0272 0.2001  0.0128  124 ASN A OD1 
853  N  ND2 . ASN A 124 ? 0.2159 0.5161 0.6882 -0.0653 0.0642  -0.0213 124 ASN A ND2 
854  N  N   . PRO A 125 ? 0.5757 0.4344 0.2920 -0.0373 0.0755  -0.0135 125 PRO A N   
855  C  CA  . PRO A 125 ? 0.6162 0.4439 0.4977 0.0305  -0.0982 0.0281  125 PRO A CA  
856  C  CB  . PRO A 125 ? 0.4261 0.4211 0.2866 0.0318  -0.0261 0.0297  125 PRO A CB  
857  C  CG  . PRO A 125 ? 0.3489 0.3587 0.4051 0.0128  0.0191  0.0314  125 PRO A CG  
858  C  CD  . PRO A 125 ? 0.3088 0.4054 0.3382 -0.0378 0.0257  0.0175  125 PRO A CD  
859  N  N   . PRO B 11  ? 0.2704 0.3128 0.2973 0.0124  0.0696  -0.0908 11  PRO B N   
860  C  CA  . PRO B 11  ? 0.1859 0.2801 0.3479 -0.0411 0.0781  -0.0693 11  PRO B CA  
861  C  C   . PRO B 11  ? 0.2027 0.2534 0.2682 0.0407  0.0021  -0.1129 11  PRO B C   
862  O  O   . PRO B 11  ? 0.2197 0.2994 0.3154 0.0168  -0.0213 -0.1064 11  PRO B O   
863  C  CB  . PRO B 11  ? 0.4564 0.4849 0.3114 0.2227  -0.0288 -0.0235 11  PRO B CB  
864  C  CG  . PRO B 11  ? 0.5444 0.2944 0.7750 0.1349  0.1694  -0.2581 11  PRO B CG  
865  C  CD  . PRO B 11  ? 0.3824 0.4439 0.4658 -0.0389 0.0229  -0.1909 11  PRO B CD  
866  N  N   . LEU B 12  ? 0.2011 0.2270 0.2567 0.0360  0.0123  -0.1110 12  LEU B N   
867  C  CA  . LEU B 12  ? 0.2142 0.2075 0.2297 0.0149  0.0253  -0.0620 12  LEU B CA  
868  C  C   . LEU B 12  ? 0.2207 0.2293 0.2351 0.0347  -0.0096 -0.0978 12  LEU B C   
869  O  O   . LEU B 12  ? 0.2286 0.2803 0.3212 0.0117  -0.0312 -0.1704 12  LEU B O   
870  C  CB  . LEU B 12  ? 0.2002 0.2138 0.2450 -0.0024 -0.0098 -0.0748 12  LEU B CB  
871  C  CG  . LEU B 12  ? 0.2254 0.2104 0.2437 0.0107  0.0214  -0.0294 12  LEU B CG  
872  C  CD1 . LEU B 12  ? 0.2779 0.2414 0.3110 -0.0701 -0.0345 -0.0578 12  LEU B CD1 
873  C  CD2 . LEU B 12  ? 0.2610 0.2824 0.2832 0.0005  0.0039  0.0139  12  LEU B CD2 
874  N  N   . MET B 13  ? 0.1944 0.1976 0.1945 0.0166  0.0043  -0.0655 13  MET B N   
875  C  CA  . MET B 13  ? 0.1760 0.2561 0.1439 0.0175  -0.0206 -0.0555 13  MET B CA  
876  C  C   . MET B 13  ? 0.1674 0.1928 0.1325 0.0000  -0.0223 -0.0510 13  MET B C   
877  O  O   . MET B 13  ? 0.1698 0.2134 0.1507 0.0084  -0.0062 -0.0936 13  MET B O   
878  C  CB  . MET B 13  ? 0.3041 0.3094 0.1706 0.0994  0.0877  -0.0132 13  MET B CB  
879  C  CG  . MET B 13  ? 0.2544 0.2412 0.2017 0.0188  0.1384  -0.0092 13  MET B CG  
880  S  SD  . MET B 13  ? 0.2572 0.2423 0.2612 -0.0021 -0.0031 -0.0495 13  MET B SD  
881  N  N   . VAL B 14  ? 0.1999 0.1968 0.0997 0.0235  -0.0146 -0.0403 14  VAL B N   
882  C  CA  . VAL B 14  ? 0.1846 0.1876 0.0900 0.0047  -0.0125 -0.0288 14  VAL B CA  
883  C  C   . VAL B 14  ? 0.2056 0.2255 0.1580 0.0569  -0.0442 -0.0617 14  VAL B C   
884  O  O   . VAL B 14  ? 0.2402 0.2235 0.1603 0.0693  -0.0416 -0.0627 14  VAL B O   
885  C  CB  . VAL B 14  ? 0.1893 0.2141 0.1591 0.0103  -0.0029 -0.0176 14  VAL B CB  
886  C  CG1 . VAL B 14  ? 0.1599 0.2431 0.2071 -0.0224 0.0032  -0.0539 14  VAL B CG1 
887  C  CG2 . VAL B 14  ? 0.1875 0.1990 0.2016 -0.0400 -0.0094 -0.0129 14  VAL B CG2 
888  N  N   . LYS B 15  ? 0.1630 0.1880 0.1326 0.0357  -0.0063 -0.0339 15  LYS B N   
889  C  CA  . LYS B 15  ? 0.1806 0.2164 0.1596 0.0419  -0.0135 -0.0483 15  LYS B CA  
890  C  C   . LYS B 15  ? 0.1551 0.2153 0.1335 0.0279  -0.0502 -0.0472 15  LYS B C   
891  O  O   . LYS B 15  ? 0.1904 0.2751 0.1395 0.0564  -0.0324 -0.0535 15  LYS B O   
892  C  CB  . LYS B 15  ? 0.1582 0.1517 0.1383 0.0296  0.0180  -0.0346 15  LYS B CB  
893  C  CG  . LYS B 15  ? 0.2402 0.1867 0.2482 0.0347  0.0418  -0.0062 15  LYS B CG  
894  C  CD  . LYS B 15  ? 0.3010 0.2328 0.3400 -0.0088 0.0317  0.0160  15  LYS B CD  
895  C  CE  . LYS B 15  ? 0.3362 0.2908 0.3513 0.0383  0.0338  0.0127  15  LYS B CE  
896  N  NZ  . LYS B 15  ? 0.3756 0.3641 0.2993 -0.0296 0.0281  0.0327  15  LYS B NZ  
897  N  N   . VAL B 16  ? 0.1747 0.1691 0.1254 0.0298  -0.0298 -0.0214 16  VAL B N   
898  C  CA  . VAL B 16  ? 0.1693 0.1582 0.1258 0.0387  -0.0297 -0.0026 16  VAL B CA  
899  C  C   . VAL B 16  ? 0.1608 0.1463 0.1160 0.0197  -0.0144 0.0126  16  VAL B C   
900  O  O   . VAL B 16  ? 0.1888 0.1638 0.1171 0.0295  -0.0179 -0.0189 16  VAL B O   
901  C  CB  . VAL B 16  ? 0.1715 0.1635 0.1310 0.0438  -0.0154 -0.0142 16  VAL B CB  
902  C  CG1 . VAL B 16  ? 0.1701 0.1592 0.1236 0.0292  -0.0294 0.0009  16  VAL B CG1 
903  C  CG2 . VAL B 16  ? 0.1845 0.1801 0.1697 0.0337  -0.0358 -0.0542 16  VAL B CG2 
904  N  N   . LEU B 17  ? 0.1420 0.1705 0.1267 0.0357  -0.0215 -0.0253 17  LEU B N   
905  C  CA  . LEU B 17  ? 0.1383 0.1684 0.1114 0.0253  -0.0293 -0.0006 17  LEU B CA  
906  C  C   . LEU B 17  ? 0.1556 0.1630 0.1173 0.0149  -0.0112 -0.0062 17  LEU B C   
907  O  O   . LEU B 17  ? 0.1628 0.1487 0.1265 0.0248  -0.0038 -0.0154 17  LEU B O   
908  C  CB  . LEU B 17  ? 0.1910 0.1597 0.1417 0.0181  0.0000  -0.0268 17  LEU B CB  
909  C  CG  . LEU B 17  ? 0.1977 0.1862 0.1540 -0.0021 0.0094  -0.0120 17  LEU B CG  
910  C  CD1 . LEU B 17  ? 0.2080 0.2338 0.2309 -0.0166 0.0011  -0.0121 17  LEU B CD1 
911  C  CD2 . LEU B 17  ? 0.2133 0.2274 0.1600 -0.0164 0.0175  0.0139  17  LEU B CD2 
912  N  N   . ASP B 18  ? 0.1699 0.1249 0.1362 0.0265  0.0103  0.0105  18  ASP B N   
913  C  CA  . ASP B 18  ? 0.1678 0.1090 0.1354 -0.0057 -0.0085 -0.0094 18  ASP B CA  
914  C  C   . ASP B 18  ? 0.1619 0.1063 0.1005 -0.0082 0.0067  0.0007  18  ASP B C   
915  O  O   . ASP B 18  ? 0.1666 0.1182 0.1386 0.0114  0.0135  0.0039  18  ASP B O   
916  C  CB  . ASP B 18  ? 0.1597 0.0978 0.1362 -0.0149 -0.0059 -0.0077 18  ASP B CB  
917  C  CG  . ASP B 18  ? 0.1491 0.1399 0.1483 -0.0176 -0.0078 0.0232  18  ASP B CG  
918  O  OD1 . ASP B 18  ? 0.1520 0.1331 0.1641 0.0076  0.0000  -0.0271 18  ASP B OD1 
919  O  OD2 . ASP B 18  ? 0.1473 0.1632 0.2294 -0.0147 0.0018  0.0024  18  ASP B OD2 
920  N  N   . ALA B 19  ? 0.1578 0.1187 0.1031 0.0094  0.0122  -0.0018 19  ALA B N   
921  C  CA  . ALA B 19  ? 0.1824 0.1223 0.1523 -0.0053 0.0071  -0.0168 19  ALA B CA  
922  C  C   . ALA B 19  ? 0.1866 0.0979 0.1523 0.0160  -0.0152 0.0042  19  ALA B C   
923  O  O   . ALA B 19  ? 0.2323 0.1119 0.1527 0.0090  0.0061  -0.0195 19  ALA B O   
924  C  CB  . ALA B 19  ? 0.1594 0.2056 0.1427 -0.0117 0.0194  -0.0281 19  ALA B CB  
925  N  N   . VAL B 20  ? 0.1996 0.1051 0.1537 0.0202  0.0287  0.0203  20  VAL B N   
926  C  CA  . VAL B 20  ? 0.1759 0.1214 0.1939 0.0282  0.0364  0.0088  20  VAL B CA  
927  C  C   . VAL B 20  ? 0.1936 0.1358 0.1927 0.0565  0.0415  0.0087  20  VAL B C   
928  O  O   . VAL B 20  ? 0.2671 0.1336 0.2710 0.0785  0.1037  0.0381  20  VAL B O   
929  C  CB  . VAL B 20  ? 0.2404 0.1764 0.2277 0.0313  0.1090  0.0469  20  VAL B CB  
930  C  CG1 . VAL B 20  ? 0.2725 0.1761 0.2779 0.0539  0.1296  0.0604  20  VAL B CG1 
931  C  CG2 . VAL B 20  ? 0.2508 0.2015 0.1842 -0.0031 0.0721  0.0029  20  VAL B CG2 
932  N  N   . ARG B 21  ? 0.1835 0.1527 0.1590 0.0129  0.0214  0.0187  21  ARG B N   
933  C  CA  . ARG B 21  ? 0.1676 0.2078 0.1951 0.0309  -0.0187 0.0238  21  ARG B CA  
934  C  C   . ARG B 21  ? 0.1917 0.1357 0.1817 0.0422  0.0085  0.0080  21  ARG B C   
935  O  O   . ARG B 21  ? 0.1968 0.1747 0.2346 0.0361  -0.0006 0.0411  21  ARG B O   
936  C  CB  . ARG B 21  ? 0.1855 0.2517 0.2770 -0.0394 -0.0549 0.0944  21  ARG B CB  
937  N  N   . GLY B 22  ? 0.1875 0.1366 0.1498 0.0188  0.0150  -0.0184 22  GLY B N   
938  C  CA  . GLY B 22  ? 0.2008 0.1394 0.1698 0.0233  0.0365  0.0021  22  GLY B CA  
939  C  C   . GLY B 22  ? 0.1806 0.1470 0.1307 -0.0147 0.0208  0.0348  22  GLY B C   
940  O  O   . GLY B 22  ? 0.2135 0.1529 0.1469 0.0000  -0.0084 0.0106  22  GLY B O   
941  N  N   . SER B 23  ? 0.2095 0.1349 0.1513 -0.0004 -0.0123 -0.0071 23  SER B N   
942  C  CA  . SER B 23  ? 0.2413 0.1508 0.1426 0.0404  -0.0371 -0.0133 23  SER B CA  
943  C  C   . SER B 23  ? 0.1901 0.1401 0.1253 0.0224  -0.0161 -0.0276 23  SER B C   
944  O  O   . SER B 23  ? 0.2035 0.1791 0.1338 0.0475  -0.0260 -0.0084 23  SER B O   
945  C  CB  . SER B 23  ? 0.2884 0.1983 0.1704 0.0453  -0.0554 -0.0415 23  SER B CB  
946  O  OG  . SER B 23  ? 0.2192 0.2789 0.2530 0.0133  -0.0315 -0.0319 23  SER B OG  
947  N  N   . PRO B 24  ? 0.2095 0.1313 0.1350 0.0101  -0.0064 0.0070  24  PRO B N   
948  C  CA  . PRO B 24  ? 0.2087 0.1407 0.1263 0.0322  -0.0261 0.0011  24  PRO B CA  
949  C  C   . PRO B 24  ? 0.1551 0.1658 0.1682 0.0178  -0.0113 0.0031  24  PRO B C   
950  O  O   . PRO B 24  ? 0.1755 0.1404 0.1879 0.0001  -0.0339 -0.0080 24  PRO B O   
951  C  CB  . PRO B 24  ? 0.2302 0.1797 0.1501 0.0291  -0.0215 -0.0212 24  PRO B CB  
952  C  CG  . PRO B 24  ? 0.5410 0.2481 0.1585 0.1164  -0.0156 -0.0034 24  PRO B CG  
953  C  CD  . PRO B 24  ? 0.2269 0.1600 0.1399 0.0009  -0.0133 -0.0041 24  PRO B CD  
954  N  N   . ALA B 25  ? 0.1550 0.1255 0.1786 0.0102  0.0017  -0.0012 25  ALA B N   
955  C  CA  . ALA B 25  ? 0.1180 0.1543 0.2024 0.0334  0.0089  0.0097  25  ALA B CA  
956  C  C   . ALA B 25  ? 0.1862 0.1341 0.2114 0.0213  -0.0120 0.0080  25  ALA B C   
957  O  O   . ALA B 25  ? 0.1891 0.1403 0.1595 0.0125  -0.0155 -0.0291 25  ALA B O   
958  C  CB  . ALA B 25  ? 0.1304 0.1700 0.1756 0.0223  0.0031  -0.0388 25  ALA B CB  
959  N  N   . ILE B 26  ? 0.1720 0.1502 0.1849 0.0177  -0.0099 -0.0125 26  ILE B N   
960  C  CA  . ILE B 26  ? 0.1968 0.1925 0.1303 0.0086  -0.0272 -0.0037 26  ILE B CA  
961  C  C   . ILE B 26  ? 0.1962 0.1973 0.1871 0.0209  -0.0141 -0.0179 26  ILE B C   
962  O  O   . ILE B 26  ? 0.1951 0.1767 0.2205 0.0097  -0.0297 0.0037  26  ILE B O   
963  C  CB  . ILE B 26  ? 0.2655 0.1898 0.1649 0.0047  -0.0120 0.0335  26  ILE B CB  
964  C  CG1 . ILE B 26  ? 0.2257 0.2450 0.2409 0.0008  -0.0394 0.0564  26  ILE B CG1 
965  C  CG2 . ILE B 26  ? 0.2729 0.3304 0.2319 0.0575  -0.0045 -0.0170 26  ILE B CG2 
966  C  CD1 . ILE B 26  ? 0.3138 0.2323 0.3452 0.0252  -0.0461 0.0130  26  ILE B CD1 
967  N  N   . ASN B 27  ? 0.1648 0.2117 0.1593 0.0125  -0.0281 -0.0001 27  ASN B N   
968  C  CA  . ASN B 27  ? 0.1805 0.2340 0.2430 -0.0138 -0.0284 -0.0217 27  ASN B CA  
969  C  C   . ASN B 27  ? 0.2046 0.1965 0.1760 -0.0028 -0.0087 -0.0603 27  ASN B C   
970  O  O   . ASN B 27  ? 0.2007 0.2480 0.2577 -0.0044 -0.0271 -0.0189 27  ASN B O   
971  C  CB  . ASN B 27  ? 0.1925 0.2345 0.2947 0.0381  -0.0370 -0.0117 27  ASN B CB  
972  C  CG  . ASN B 27  ? 0.3478 0.4061 0.3770 -0.0629 -0.0082 -0.0980 27  ASN B CG  
973  O  OD1 . ASN B 27  ? 0.3172 0.4095 0.4810 0.0118  -0.0566 -0.1722 27  ASN B OD1 
974  N  ND2 . ASN B 27  ? 0.3635 0.4144 0.6091 0.0258  -0.0218 -0.0806 27  ASN B ND2 
975  N  N   . VAL B 28  ? 0.1827 0.1476 0.1820 0.0200  -0.0002 0.0008  28  VAL B N   
976  C  CA  . VAL B 28  ? 0.2283 0.1326 0.1733 0.0157  -0.0096 -0.0121 28  VAL B CA  
977  C  C   . VAL B 28  ? 0.1539 0.1503 0.1509 -0.0078 -0.0040 -0.0053 28  VAL B C   
978  O  O   . VAL B 28  ? 0.1873 0.1455 0.1636 0.0052  0.0098  -0.0106 28  VAL B O   
979  C  CB  . VAL B 28  ? 0.2563 0.1331 0.2177 0.0334  -0.0352 -0.0185 28  VAL B CB  
980  C  CG1 . VAL B 28  ? 0.3331 0.1612 0.2643 0.0444  -0.0703 -0.0157 28  VAL B CG1 
981  C  CG2 . VAL B 28  ? 0.2835 0.1798 0.2553 0.0657  -0.0015 -0.0125 28  VAL B CG2 
982  N  N   . ALA B 29  ? 0.1647 0.1555 0.1717 0.0216  0.0001  -0.0080 29  ALA B N   
983  C  CA  . ALA B 29  ? 0.1540 0.1393 0.1852 0.0191  0.0110  -0.0127 29  ALA B CA  
984  C  C   . ALA B 29  ? 0.1707 0.1910 0.1395 0.0193  -0.0036 -0.0003 29  ALA B C   
985  O  O   . ALA B 29  ? 0.1930 0.2029 0.1432 0.0218  -0.0043 0.0036  29  ALA B O   
986  C  CB  . ALA B 29  ? 0.1909 0.1378 0.1995 -0.0019 -0.0095 -0.0329 29  ALA B CB  
987  N  N   . VAL B 30  ? 0.1514 0.1866 0.1485 0.0271  -0.0148 -0.0221 30  VAL B N   
988  C  CA  . VAL B 30  ? 0.1810 0.1897 0.1580 0.0022  -0.0480 -0.0389 30  VAL B CA  
989  C  C   . VAL B 30  ? 0.1840 0.1898 0.1700 0.0432  0.0114  -0.0058 30  VAL B C   
990  O  O   . VAL B 30  ? 0.1879 0.1944 0.1924 0.0357  -0.0044 -0.0221 30  VAL B O   
991  C  CB  . VAL B 30  ? 0.1704 0.2027 0.1525 -0.0157 -0.0330 -0.0570 30  VAL B CB  
992  C  CG1 . VAL B 30  ? 0.1862 0.2174 0.2491 0.0020  -0.0457 -0.0415 30  VAL B CG1 
993  C  CG2 . VAL B 30  ? 0.1942 0.1940 0.1703 -0.0127 -0.0322 -0.0274 30  VAL B CG2 
994  N  N   . HIS B 31  ? 0.1715 0.2181 0.1856 0.0399  -0.0002 -0.0145 31  HIS B N   
995  C  CA  . HIS B 31  ? 0.1523 0.2071 0.2180 0.0460  -0.0073 -0.0004 31  HIS B CA  
996  C  C   . HIS B 31  ? 0.2133 0.1956 0.2176 0.0503  -0.0075 -0.0164 31  HIS B C   
997  O  O   . HIS B 31  ? 0.1655 0.3065 0.2494 0.0586  -0.0203 -0.0493 31  HIS B O   
998  C  CB  . HIS B 31  ? 0.2124 0.2433 0.2555 0.0415  -0.0197 0.0064  31  HIS B CB  
999  C  CG  . HIS B 31  ? 0.2386 0.3145 0.4090 -0.0169 0.0348  0.0592  31  HIS B CG  
1000 N  ND1 . HIS B 31  ? 0.2276 0.3151 0.4478 -0.0025 0.0063  0.0407  31  HIS B ND1 
1001 C  CD2 . HIS B 31  ? 0.3383 0.2903 0.4192 -0.0840 -0.0064 0.0755  31  HIS B CD2 
1002 C  CE1 . HIS B 31  ? 0.2242 0.3108 0.4357 -0.0301 0.0525  0.0196  31  HIS B CE1 
1003 N  NE2 . HIS B 31  ? 0.3478 0.3310 0.4067 -0.0532 0.0456  -0.0223 31  HIS B NE2 
1004 N  N   . VAL B 32  ? 0.1579 0.1990 0.2032 0.0211  -0.0164 -0.0512 32  VAL B N   
1005 C  CA  . VAL B 32  ? 0.1339 0.2054 0.2182 -0.0049 0.0026  -0.0298 32  VAL B CA  
1006 C  C   . VAL B 32  ? 0.1707 0.1795 0.2007 0.0000  -0.0185 -0.0516 32  VAL B C   
1007 O  O   . VAL B 32  ? 0.1777 0.2039 0.2482 0.0009  -0.0326 -0.0278 32  VAL B O   
1008 C  CB  . VAL B 32  ? 0.1757 0.2040 0.1885 0.0009  -0.0029 -0.0583 32  VAL B CB  
1009 C  CG1 . VAL B 32  ? 0.1701 0.2162 0.2055 0.0054  0.0000  -0.0321 32  VAL B CG1 
1010 C  CG2 . VAL B 32  ? 0.1747 0.1913 0.1861 -0.0023 -0.0157 -0.0450 32  VAL B CG2 
1011 N  N   . PHE B 33  ? 0.1996 0.1620 0.2365 -0.0138 -0.0245 0.0046  33  PHE B N   
1012 C  CA  . PHE B 33  ? 0.1836 0.1872 0.2935 -0.0185 -0.0273 -0.0313 33  PHE B CA  
1013 C  C   . PHE B 33  ? 0.1848 0.1600 0.3412 -0.0103 -0.0342 -0.0527 33  PHE B C   
1014 O  O   . PHE B 33  ? 0.1545 0.1889 0.2367 0.0048  -0.0157 -0.0207 33  PHE B O   
1015 C  CB  . PHE B 33  ? 0.1917 0.2194 0.3664 -0.0020 -0.0153 0.0755  33  PHE B CB  
1016 C  CG  . PHE B 33  ? 0.1861 0.2245 0.3522 0.0221  -0.0385 0.0105  33  PHE B CG  
1017 C  CD1 . PHE B 33  ? 0.2179 0.2757 0.3546 0.0598  -0.0102 0.0075  33  PHE B CD1 
1018 C  CD2 . PHE B 33  ? 0.2376 0.2757 0.3582 -0.0222 0.0146  0.0280  33  PHE B CD2 
1019 C  CE1 . PHE B 33  ? 0.2277 0.3006 0.3318 0.0765  -0.0252 -0.0048 33  PHE B CE1 
1020 C  CE2 . PHE B 33  ? 0.1996 0.3184 0.4485 0.0056  0.0157  0.0640  33  PHE B CE2 
1021 C  CZ  . PHE B 33  ? 0.2419 0.3330 0.3100 0.0298  0.0120  0.0199  33  PHE B CZ  
1022 N  N   . ARG B 34  ? 0.1932 0.1741 0.3294 0.0117  -0.0835 -0.0669 34  ARG B N   
1023 C  CA  . ARG B 34  ? 0.1935 0.1947 0.3047 0.0369  -0.0630 -0.0321 34  ARG B CA  
1024 C  C   . ARG B 34  ? 0.2310 0.1506 0.3118 -0.0140 -0.0444 -0.0383 34  ARG B C   
1025 O  O   . ARG B 34  ? 0.2478 0.2018 0.3363 -0.0166 -0.0934 -0.0026 34  ARG B O   
1026 C  CB  . ARG B 34  ? 0.2242 0.2346 0.3186 0.0652  0.0030  -0.0316 34  ARG B CB  
1027 C  CG  . ARG B 34  ? 0.2519 0.2286 0.3286 0.0385  0.0104  -0.0123 34  ARG B CG  
1028 C  CD  . ARG B 34  ? 0.2634 0.4222 0.2578 0.0236  0.0349  0.1182  34  ARG B CD  
1029 N  N   . LYS B 35  ? 0.2432 0.1933 0.2788 0.0147  -0.0522 -0.0058 35  LYS B N   
1030 C  CA  . LYS B 35  ? 0.2308 0.2381 0.2560 -0.0114 0.0045  -0.0031 35  LYS B CA  
1031 C  C   . LYS B 35  ? 0.3101 0.2978 0.2458 0.0895  -0.0040 0.0271  35  LYS B C   
1032 O  O   . LYS B 35  ? 0.2539 0.2043 0.3786 0.0443  0.0059  -0.0109 35  LYS B O   
1033 C  CB  . LYS B 35  ? 0.2615 0.2622 0.4367 0.0391  -0.1203 -0.0800 35  LYS B CB  
1034 N  N   . ALA B 36  ? 0.2517 0.2829 0.3302 0.0670  -0.0197 -0.0115 36  ALA B N   
1035 C  CA  . ALA B 36  ? 0.2840 0.3536 0.3158 0.0561  0.0090  -0.0569 36  ALA B CA  
1036 C  C   . ALA B 36  ? 0.3558 0.2491 0.3835 0.1054  -0.0341 -0.0528 36  ALA B C   
1037 O  O   . ALA B 36  ? 0.3230 0.3159 0.4167 0.0451  -0.0039 0.0198  36  ALA B O   
1038 C  CB  . ALA B 36  ? 0.3181 0.3003 0.3709 0.0542  -0.0351 0.0297  36  ALA B CB  
1039 N  N   . ALA B 37  ? 0.5064 0.2524 0.3260 0.1270  0.0329  0.0209  37  ALA B N   
1040 C  CA  . ALA B 37  ? 0.4082 0.3096 0.4484 0.1264  -0.0042 0.0368  37  ALA B CA  
1041 C  C   . ALA B 37  ? 0.4247 0.4344 0.4328 0.1308  -0.0497 0.0926  37  ALA B C   
1042 O  O   . ALA B 37  ? 0.4637 0.5905 0.4261 0.2446  -0.0236 -0.0284 37  ALA B O   
1043 C  CB  . ALA B 37  ? 0.5072 0.3404 0.4894 0.1343  0.0643  0.0341  37  ALA B CB  
1044 N  N   . ASP B 38  ? 0.4099 0.4534 0.3843 0.1811  0.0147  0.0981  38  ASP B N   
1045 C  CA  . ASP B 38  ? 0.4156 0.3819 0.3396 0.0704  0.0169  0.0512  38  ASP B CA  
1046 C  C   . ASP B 38  ? 0.5172 0.3079 0.3574 0.1218  0.0719  0.1210  38  ASP B C   
1047 O  O   . ASP B 38  ? 0.4716 0.5145 0.5548 0.1146  0.1537  0.2390  38  ASP B O   
1048 C  CB  . ASP B 38  ? 0.3945 0.3592 0.4832 0.0482  0.0745  0.0357  38  ASP B CB  
1049 C  CG  . ASP B 38  ? 0.5387 0.3711 0.5805 -0.0599 -0.0749 0.0482  38  ASP B CG  
1050 O  OD1 . ASP B 38  ? 0.5385 0.3920 0.6196 0.0579  0.0499  0.1426  38  ASP B OD1 
1051 O  OD2 . ASP B 38  ? 0.4986 0.3207 0.5599 -0.0720 0.0335  0.0679  38  ASP B OD2 
1052 N  N   . ASP B 39  ? 0.5669 0.3199 0.4338 0.1221  0.1041  0.1157  39  ASP B N   
1053 C  CA  . ASP B 39  ? 0.4213 0.4374 0.3211 0.0870  -0.0108 0.0583  39  ASP B CA  
1054 C  C   . ASP B 39  ? 0.3503 0.2900 0.3627 0.0250  0.0939  0.0246  39  ASP B C   
1055 O  O   . ASP B 39  ? 0.5493 0.4699 0.4421 0.0597  0.1145  -0.0528 39  ASP B O   
1056 C  CB  . ASP B 39  ? 0.6187 0.4526 0.2880 -0.0056 -0.0307 0.1137  39  ASP B CB  
1057 N  N   . THR B 40  ? 0.3613 0.3260 0.4659 0.0014  -0.0228 0.0127  40  THR B N   
1058 C  CA  . THR B 40  ? 0.3078 0.3437 0.4693 -0.0205 0.0416  0.0661  40  THR B CA  
1059 C  C   . THR B 40  ? 0.3879 0.2946 0.4737 0.0513  0.0587  0.0831  40  THR B C   
1060 O  O   . THR B 40  ? 0.3328 0.2838 0.3660 0.0103  0.0338  -0.0467 40  THR B O   
1061 C  CB  . THR B 40  ? 0.3549 0.3608 0.4460 0.0128  0.0198  0.0118  40  THR B CB  
1062 O  OG1 . THR B 40  ? 0.4088 0.3152 0.4362 -0.0007 -0.0066 0.0129  40  THR B OG1 
1063 C  CG2 . THR B 40  ? 0.5185 0.3907 0.4461 0.0109  0.0561  0.0176  40  THR B CG2 
1064 N  N   . TRP B 41  ? 0.3072 0.3118 0.4203 -0.0862 0.0368  -0.0025 41  TRP B N   
1065 C  CA  . TRP B 41  ? 0.3883 0.2473 0.3046 -0.0597 0.0471  -0.0596 41  TRP B CA  
1066 C  C   . TRP B 41  ? 0.2902 0.2520 0.3910 -0.0089 -0.0055 -0.0068 41  TRP B C   
1067 O  O   . TRP B 41  ? 0.3286 0.4208 0.5647 -0.1233 0.0410  -0.0724 41  TRP B O   
1068 C  CB  . TRP B 41  ? 0.3280 0.3254 0.3964 -0.0338 0.0546  -0.0371 41  TRP B CB  
1069 C  CG  . TRP B 41  ? 0.2915 0.3339 0.2862 -0.0047 -0.0152 0.0382  41  TRP B CG  
1070 C  CD1 . TRP B 41  ? 0.4024 0.4704 0.3791 -0.1173 0.0751  0.0509  41  TRP B CD1 
1071 C  CD2 . TRP B 41  ? 0.2763 0.2477 0.2811 0.0319  0.0104  -0.0145 41  TRP B CD2 
1072 N  NE1 . TRP B 41  ? 0.3706 0.5243 0.3509 -0.1251 0.0606  -0.0134 41  TRP B NE1 
1073 C  CE2 . TRP B 41  ? 0.3976 0.3423 0.2836 -0.0607 0.0188  0.0278  41  TRP B CE2 
1074 C  CE3 . TRP B 41  ? 0.2189 0.2620 0.2965 0.0244  -0.0079 0.0385  41  TRP B CE3 
1075 C  CZ2 . TRP B 41  ? 0.3510 0.3370 0.3110 -0.0286 -0.0742 -0.0280 41  TRP B CZ2 
1076 C  CZ3 . TRP B 41  ? 0.2589 0.2351 0.2835 0.0500  0.0022  0.0073  41  TRP B CZ3 
1077 C  CH2 . TRP B 41  ? 0.3104 0.2942 0.3472 0.0846  -0.0148 -0.0756 41  TRP B CH2 
1078 N  N   . GLU B 42  ? 0.3097 0.2203 0.3501 -0.0428 -0.1127 0.0244  42  GLU B N   
1079 C  CA  . GLU B 42  ? 0.2986 0.2545 0.3510 -0.0315 -0.0729 -0.0418 42  GLU B CA  
1080 C  C   . GLU B 42  ? 0.3014 0.3096 0.3875 -0.0815 -0.0810 0.0682  42  GLU B C   
1081 O  O   . GLU B 42  ? 0.2505 0.1760 0.4535 -0.0162 -0.0925 -0.0331 42  GLU B O   
1082 C  CB  . GLU B 42  ? 0.3848 0.2985 0.3542 0.0415  0.0147  0.0340  42  GLU B CB  
1083 N  N   . PRO B 43  ? 0.2955 0.2144 0.4369 -0.0688 -0.0839 0.0171  43  PRO B N   
1084 C  CA  . PRO B 43  ? 0.2826 0.2005 0.3652 -0.0547 -0.1060 -0.0205 43  PRO B CA  
1085 C  C   . PRO B 43  ? 0.3139 0.1790 0.3305 -0.0654 -0.0599 -0.1120 43  PRO B C   
1086 O  O   . PRO B 43  ? 0.3555 0.1695 0.5288 -0.0099 -0.0967 -0.0635 43  PRO B O   
1087 C  CB  . PRO B 43  ? 0.2268 0.2840 0.4589 -0.0494 -0.0825 0.0108  43  PRO B CB  
1088 C  CG  . PRO B 43  ? 0.3930 0.3026 0.4579 -0.0923 -0.0669 0.0026  43  PRO B CG  
1089 C  CD  . PRO B 43  ? 0.3579 0.3141 0.4044 -0.1119 -0.0543 0.0654  43  PRO B CD  
1090 N  N   . PHE B 44  ? 0.2002 0.2418 0.2905 0.0230  0.0072  -0.0110 44  PHE B N   
1091 C  CA  . PHE B 44  ? 0.1877 0.2142 0.2938 0.0159  -0.0200 -0.0599 44  PHE B CA  
1092 C  C   . PHE B 44  ? 0.1716 0.2715 0.2182 0.0296  0.0004  -0.1155 44  PHE B C   
1093 O  O   . PHE B 44  ? 0.2537 0.2429 0.2567 0.0539  -0.0033 -0.0903 44  PHE B O   
1094 C  CB  . PHE B 44  ? 0.2047 0.2464 0.2744 0.0471  -0.0532 -0.0835 44  PHE B CB  
1095 C  CG  . PHE B 44  ? 0.2093 0.2401 0.3759 0.0404  -0.0286 -0.1356 44  PHE B CG  
1096 C  CD1 . PHE B 44  ? 0.2430 0.2720 0.2410 0.0279  -0.0461 -0.0952 44  PHE B CD1 
1097 C  CD2 . PHE B 44  ? 0.2222 0.3013 0.2434 -0.0306 0.0213  -0.0761 44  PHE B CD2 
1098 C  CE1 . PHE B 44  ? 0.2373 0.3529 0.2647 0.0704  0.0029  -0.0814 44  PHE B CE1 
1099 C  CE2 . PHE B 44  ? 0.3678 0.0928 0.2546 -0.0191 -0.0310 -0.0148 44  PHE B CE2 
1100 C  CZ  . PHE B 44  ? 0.1972 0.3883 0.3009 0.0137  -0.0534 -0.1557 44  PHE B CZ  
1101 N  N   . ALA B 45  ? 0.2283 0.1819 0.1797 0.0163  0.0077  -0.0095 45  ALA B N   
1102 C  CA  . ALA B 45  ? 0.2599 0.1348 0.3722 0.0340  0.0282  0.0080  45  ALA B CA  
1103 C  C   . ALA B 45  ? 0.1871 0.1647 0.2158 -0.0098 -0.0197 -0.0242 45  ALA B C   
1104 O  O   . ALA B 45  ? 0.1823 0.2526 0.2278 0.0341  -0.0466 -0.0482 45  ALA B O   
1105 C  CB  . ALA B 45  ? 0.1992 0.2429 0.3298 0.0107  0.0097  -0.0694 45  ALA B CB  
1106 N  N   . SER B 46  ? 0.1692 0.2125 0.1920 0.0031  -0.0254 -0.0748 46  SER B N   
1107 C  CA  . SER B 46  ? 0.1747 0.1736 0.2070 -0.0182 -0.0073 -0.0463 46  SER B CA  
1108 C  C   . SER B 46  ? 0.1792 0.1769 0.1661 -0.0111 0.0240  -0.0405 46  SER B C   
1109 O  O   . SER B 46  ? 0.2414 0.2041 0.1887 0.0205  0.0002  -0.0717 46  SER B O   
1110 C  CB  . SER B 46  ? 0.2169 0.1502 0.2499 0.0140  -0.0021 -0.0590 46  SER B CB  
1111 O  OG  . SER B 46  ? 0.2001 0.1759 0.2776 -0.0291 -0.0228 -0.0937 46  SER B OG  
1112 N  N   . GLY B 47  ? 0.1869 0.1617 0.1697 0.0110  0.0066  -0.0394 47  GLY B N   
1113 C  CA  . GLY B 47  ? 0.1845 0.1592 0.1852 0.0162  -0.0268 -0.0548 47  GLY B CA  
1114 C  C   . GLY B 47  ? 0.1830 0.1515 0.1616 -0.0104 -0.0437 -0.0365 47  GLY B C   
1115 O  O   . GLY B 47  ? 0.2051 0.1829 0.1697 0.0070  -0.0454 -0.0303 47  GLY B O   
1116 N  N   . LYS B 48  ? 0.2346 0.1638 0.1471 0.0303  -0.0295 -0.0278 48  LYS B N   
1117 C  CA  . LYS B 48  ? 0.2186 0.1895 0.1498 -0.0012 -0.0127 -0.0607 48  LYS B CA  
1118 C  C   . LYS B 48  ? 0.2144 0.1510 0.1940 0.0216  -0.0230 -0.0518 48  LYS B C   
1119 O  O   . LYS B 48  ? 0.2461 0.1857 0.1680 0.0235  -0.0127 -0.0352 48  LYS B O   
1120 C  CB  . LYS B 48  ? 0.2093 0.1931 0.3243 0.0170  0.0062  -0.0440 48  LYS B CB  
1121 C  CG  . LYS B 48  ? 0.3290 0.1541 0.4879 0.0431  0.0048  -0.0455 48  LYS B CG  
1122 C  CD  . LYS B 48  ? 0.4346 0.3339 0.5084 -0.0319 0.0544  -0.0392 48  LYS B CD  
1123 C  CE  . LYS B 48  ? 0.6135 0.3176 0.6691 -0.1292 -0.0892 -0.0288 48  LYS B CE  
1124 N  N   . THR B 49  ? 0.2007 0.1529 0.1713 0.0168  -0.0271 -0.0333 49  THR B N   
1125 C  CA  . THR B 49  ? 0.1924 0.1326 0.1735 -0.0002 -0.0270 -0.0224 49  THR B CA  
1126 C  C   . THR B 49  ? 0.1558 0.1954 0.1570 0.0124  -0.0069 -0.0192 49  THR B C   
1127 O  O   . THR B 49  ? 0.1854 0.2070 0.1484 0.0113  -0.0212 -0.0204 49  THR B O   
1128 C  CB  . THR B 49  ? 0.1627 0.1422 0.1817 -0.0098 -0.0199 -0.0253 49  THR B CB  
1129 O  OG1 . THR B 49  ? 0.1618 0.1721 0.1788 0.0176  -0.0189 -0.0164 49  THR B OG1 
1130 C  CG2 . THR B 49  ? 0.1790 0.1969 0.1600 0.0125  -0.0231 -0.0186 49  THR B CG2 
1131 N  N   . SER B 50  ? 0.2056 0.1994 0.1058 0.0022  -0.0040 -0.0145 50  SER B N   
1132 C  CA  . SER B 50  ? 0.1987 0.2217 0.1474 0.0128  -0.0251 0.0088  50  SER B CA  
1133 C  C   . SER B 50  ? 0.2222 0.1985 0.1744 -0.0021 -0.0437 -0.0203 50  SER B C   
1134 O  O   . SER B 50  ? 0.2253 0.1814 0.1605 0.0262  -0.0409 -0.0100 50  SER B O   
1135 C  CB  . SER B 50  ? 0.2526 0.1733 0.1538 0.0392  -0.0072 0.0114  50  SER B CB  
1136 O  OG  . SER B 50  ? 0.3057 0.2147 0.2332 0.0089  -0.0278 0.0468  50  SER B OG  
1137 N  N   . GLU B 51  ? 0.2677 0.2702 0.1907 0.0800  -0.0746 -0.0161 51  GLU B N   
1138 C  CA  . GLU B 51  ? 0.2820 0.2346 0.1770 0.0681  -0.0489 -0.0129 51  GLU B CA  
1139 C  C   . GLU B 51  ? 0.3016 0.2640 0.1544 0.0552  -0.0347 0.0199  51  GLU B C   
1140 O  O   . GLU B 51  ? 0.2949 0.2394 0.2192 0.0464  -0.0083 -0.0033 51  GLU B O   
1141 C  CB  . GLU B 51  ? 0.3590 0.2636 0.2253 0.0799  -0.1029 0.0204  51  GLU B CB  
1142 N  N   . SER B 52  ? 0.2893 0.2093 0.1330 0.0400  0.0038  -0.0077 52  SER B N   
1143 C  CA  . SER B 52  ? 0.3013 0.1816 0.2051 0.0067  -0.0022 0.0380  52  SER B CA  
1144 C  C   . SER B 52  ? 0.2500 0.1438 0.1697 0.0032  0.0164  0.0006  52  SER B C   
1145 O  O   . SER B 52  ? 0.2828 0.1911 0.2004 -0.0162 0.0007  -0.0020 52  SER B O   
1146 C  CB  . SER B 52  ? 0.3311 0.3131 0.2600 -0.0225 0.0239  0.1147  52  SER B CB  
1147 O  OG  . SER B 52  ? 0.3123 0.3941 0.2968 -0.0370 -0.0003 -0.0459 52  SER B OG  
1148 N  N   . GLY B 53  ? 0.2239 0.1657 0.1230 0.0037  -0.0141 -0.0273 53  GLY B N   
1149 C  CA  . GLY B 53  ? 0.1762 0.2041 0.1590 0.0091  -0.0097 0.0128  53  GLY B CA  
1150 C  C   . GLY B 53  ? 0.2012 0.1699 0.1483 0.0064  -0.0275 0.0037  53  GLY B C   
1151 O  O   . GLY B 53  ? 0.1883 0.1702 0.1370 0.0111  -0.0227 -0.0240 53  GLY B O   
1152 N  N   . GLU B 54  ? 0.2037 0.2296 0.1421 0.0354  -0.0175 -0.0132 54  GLU B N   
1153 C  CA  . GLU B 54  ? 0.1894 0.1867 0.1484 0.0054  -0.0307 -0.0333 54  GLU B CA  
1154 C  C   . GLU B 54  ? 0.1775 0.1930 0.1291 0.0116  -0.0334 -0.0185 54  GLU B C   
1155 O  O   . GLU B 54  ? 0.1654 0.2487 0.1707 0.0234  -0.0224 -0.0306 54  GLU B O   
1156 C  CB  . GLU B 54  ? 0.2015 0.2242 0.1997 0.0315  0.0094  0.0063  54  GLU B CB  
1157 C  CG  . GLU B 54  ? 0.2733 0.2453 0.3493 0.0057  -0.0249 -0.0113 54  GLU B CG  
1158 C  CD  . GLU B 54  ? 0.4794 0.3023 0.3646 -0.0035 0.0933  -0.0571 54  GLU B CD  
1159 O  OE1 . GLU B 54  ? 0.5294 0.3541 0.3477 -0.0174 0.1659  -0.0038 54  GLU B OE1 
1160 O  OE2 . GLU B 54  ? 0.5089 0.3177 0.5862 -0.1015 0.0888  -0.0457 54  GLU B OE2 
1161 N  N   . LEU B 55  ? 0.1980 0.1737 0.1539 0.0158  -0.0531 -0.0115 55  LEU B N   
1162 C  CA  . LEU B 55  ? 0.1679 0.1790 0.1565 0.0123  -0.0100 -0.0125 55  LEU B CA  
1163 C  C   . LEU B 55  ? 0.1924 0.1587 0.1983 0.0135  -0.0059 -0.0381 55  LEU B C   
1164 O  O   . LEU B 55  ? 0.1894 0.2424 0.1708 0.0380  -0.0073 -0.0420 55  LEU B O   
1165 C  CB  . LEU B 55  ? 0.1758 0.1619 0.1731 0.0067  -0.0138 -0.0362 55  LEU B CB  
1166 C  CG  . LEU B 55  ? 0.2183 0.1703 0.2067 0.0234  0.0020  0.0066  55  LEU B CG  
1167 C  CD1 . LEU B 55  ? 0.2494 0.1866 0.2504 -0.0057 -0.0442 -0.0207 55  LEU B CD1 
1168 C  CD2 . LEU B 55  ? 0.2238 0.1657 0.2045 -0.0113 -0.0246 -0.0012 55  LEU B CD2 
1169 N  N   . HIS B 56  ? 0.2290 0.2715 0.1831 0.0119  0.0370  -0.0594 56  HIS B N   
1170 C  CA  . HIS B 56  ? 0.2687 0.2865 0.1968 -0.0165 0.0766  -0.0707 56  HIS B CA  
1171 C  C   . HIS B 56  ? 0.2589 0.3047 0.2627 0.0264  0.0302  -0.0674 56  HIS B C   
1172 O  O   . HIS B 56  ? 0.2653 0.3064 0.2517 -0.0046 0.0116  -0.0776 56  HIS B O   
1173 C  CB  . HIS B 56  ? 0.3486 0.2254 0.2775 0.0540  0.1497  -0.0557 56  HIS B CB  
1174 C  CG  . HIS B 56  ? 0.4424 0.2562 0.2644 0.0855  0.0481  -0.0386 56  HIS B CG  
1175 N  ND1 . HIS B 56  ? 0.4569 0.2067 0.7919 -0.0086 0.1020  -0.0289 56  HIS B ND1 
1176 C  CD2 . HIS B 56  ? 0.4635 0.3606 0.3714 0.0348  0.0420  -0.0044 56  HIS B CD2 
1177 C  CE1 . HIS B 56  ? 0.4205 0.3321 0.2859 -0.0872 0.1013  -0.0890 56  HIS B CE1 
1178 N  NE2 . HIS B 56  ? 0.5677 0.4208 0.4287 0.0401  0.0467  -0.0732 56  HIS B NE2 
1179 N  N   . GLY B 57  ? 0.2940 0.2661 0.2698 0.0373  0.0606  -0.0562 57  GLY B N   
1180 C  CA  . GLY B 57  ? 0.2982 0.3204 0.2560 0.0528  0.0138  -0.1178 57  GLY B CA  
1181 C  C   . GLY B 57  ? 0.2503 0.3202 0.2584 0.0639  -0.0521 -0.1091 57  GLY B C   
1182 O  O   . GLY B 57  ? 0.3966 0.3168 0.2843 0.0567  -0.0887 -0.1260 57  GLY B O   
1183 N  N   . LEU B 58  ? 0.2380 0.2118 0.2439 0.0171  -0.0316 -0.0872 58  LEU B N   
1184 C  CA  . LEU B 58  ? 0.2576 0.2734 0.2174 0.0173  -0.0051 -0.0826 58  LEU B CA  
1185 C  C   . LEU B 58  ? 0.2413 0.2367 0.2509 0.0386  -0.0439 -0.0600 58  LEU B C   
1186 O  O   . LEU B 58  ? 0.4598 0.2358 0.2863 0.0240  -0.0817 -0.0758 58  LEU B O   
1187 C  CB  . LEU B 58  ? 0.2197 0.2512 0.1947 0.0308  -0.0158 -0.0036 58  LEU B CB  
1188 C  CG  . LEU B 58  ? 0.3084 0.1651 0.2303 0.0214  -0.0055 -0.0212 58  LEU B CG  
1189 C  CD1 . LEU B 58  ? 0.3254 0.2079 0.2673 0.0253  -0.0533 -0.0782 58  LEU B CD1 
1190 C  CD2 . LEU B 58  ? 0.2968 0.2153 0.3772 0.0501  0.1113  -0.1115 58  LEU B CD2 
1191 N  N   . THR B 59  ? 0.2332 0.2351 0.3118 0.0305  -0.0252 -0.1426 59  THR B N   
1192 C  CA  . THR B 59  ? 0.2632 0.2161 0.2729 0.0306  -0.0377 -0.1449 59  THR B CA  
1193 C  C   . THR B 59  ? 0.3318 0.2751 0.2344 0.0543  -0.0426 -0.0942 59  THR B C   
1194 O  O   . THR B 59  ? 0.3593 0.2919 0.3555 0.0781  0.0168  -0.1126 59  THR B O   
1195 C  CB  . THR B 59  ? 0.3235 0.2361 0.2837 0.0555  -0.0659 -0.1372 59  THR B CB  
1196 O  OG1 . THR B 59  ? 0.3546 0.2590 0.3180 0.0749  -0.0705 -0.1284 59  THR B OG1 
1197 C  CG2 . THR B 59  ? 0.2562 0.2778 0.2747 0.0296  -0.0751 -0.0088 59  THR B CG2 
1198 N  N   . THR B 60  ? 0.3213 0.2390 0.3275 0.0689  -0.0007 -0.0713 60  THR B N   
1199 C  CA  . THR B 60  ? 0.3207 0.2753 0.2713 0.0758  -0.0484 -0.0994 60  THR B CA  
1200 C  C   . THR B 60  ? 0.3131 0.2326 0.2658 0.0854  0.0087  -0.1125 60  THR B C   
1201 O  O   . THR B 60  ? 0.3207 0.2200 0.2514 0.0453  -0.0308 -0.0774 60  THR B O   
1202 C  CB  . THR B 60  ? 0.2732 0.3421 0.2519 0.0404  -0.0545 -0.0968 60  THR B CB  
1203 O  OG1 . THR B 60  ? 0.3495 0.3277 0.4174 0.0982  -0.0733 -0.1497 60  THR B OG1 
1204 C  CG2 . THR B 60  ? 0.3436 0.5268 0.3939 -0.0001 -0.1560 -0.0702 60  THR B CG2 
1205 N  N   . GLU B 61  ? 0.3246 0.2594 0.2671 0.0362  0.0037  -0.0828 61  GLU B N   
1206 C  CA  . GLU B 61  ? 0.3134 0.2535 0.3628 0.0463  -0.0302 -0.0697 61  GLU B CA  
1207 C  C   . GLU B 61  ? 0.3312 0.2387 0.2832 0.0274  -0.0461 -0.0477 61  GLU B C   
1208 O  O   . GLU B 61  ? 0.2917 0.2308 0.3402 0.0524  -0.0463 -0.0484 61  GLU B O   
1209 C  CB  . GLU B 61  ? 0.3961 0.2593 0.3493 0.1113  -0.0169 -0.0180 61  GLU B CB  
1210 N  N   . GLU B 62  ? 0.3158 0.3200 0.2553 0.1135  -0.0242 -0.0721 62  GLU B N   
1211 C  CA  . GLU B 62  ? 0.2669 0.2515 0.4074 0.0122  0.0229  -0.0929 62  GLU B CA  
1212 C  C   . GLU B 62  ? 0.2593 0.2187 0.3113 0.0195  -0.0585 -0.0974 62  GLU B C   
1213 O  O   . GLU B 62  ? 0.2610 0.2687 0.5041 0.0307  0.0280  0.0578  62  GLU B O   
1214 C  CB  . GLU B 62  ? 0.4905 0.2419 0.3475 -0.0027 0.1384  -0.0914 62  GLU B CB  
1215 N  N   . GLU B 63  ? 0.2602 0.2542 0.2673 0.0047  0.0361  -0.0662 63  GLU B N   
1216 C  CA  . GLU B 63  ? 0.2028 0.2140 0.2743 0.0067  -0.0326 -0.0749 63  GLU B CA  
1217 C  C   . GLU B 63  ? 0.2008 0.2267 0.2849 -0.0111 -0.0138 -0.1143 63  GLU B C   
1218 O  O   . GLU B 63  ? 0.2501 0.2516 0.3394 0.0504  0.0340  -0.0477 63  GLU B O   
1219 C  CB  . GLU B 63  ? 0.1458 0.2044 0.2571 0.0319  0.0315  -0.0673 63  GLU B CB  
1220 C  CG  . GLU B 63  ? 0.2139 0.2539 0.2752 0.0174  -0.0382 -0.0121 63  GLU B CG  
1221 C  CD  . GLU B 63  ? 0.2339 0.2460 0.2990 -0.0161 -0.0580 -0.0305 63  GLU B CD  
1222 O  OE1 . GLU B 63  ? 0.2710 0.3212 0.4187 0.0560  -0.0176 0.0221  63  GLU B OE1 
1223 O  OE2 . GLU B 63  ? 0.3235 0.3106 0.4173 -0.0144 0.0195  -0.0319 63  GLU B OE2 
1224 N  N   . PHE B 64  ? 0.1964 0.2531 0.2877 -0.0065 -0.0308 -0.0782 64  PHE B N   
1225 C  CA  . PHE B 64  ? 0.1822 0.2354 0.2828 0.0227  -0.0401 -0.0684 64  PHE B CA  
1226 C  C   . PHE B 64  ? 0.1872 0.2517 0.3354 0.0453  -0.0062 0.0074  64  PHE B C   
1227 O  O   . PHE B 64  ? 0.2509 0.3083 0.4255 0.0553  0.0539  0.0560  64  PHE B O   
1228 C  CB  . PHE B 64  ? 0.1992 0.2438 0.3025 0.0538  -0.0263 -0.0689 64  PHE B CB  
1229 C  CG  . PHE B 64  ? 0.1803 0.2915 0.2837 0.0433  -0.0388 -0.0533 64  PHE B CG  
1230 C  CD1 . PHE B 64  ? 0.2710 0.2262 0.2226 0.0464  -0.0421 -0.0981 64  PHE B CD1 
1231 C  CD2 . PHE B 64  ? 0.4423 0.3899 0.2144 -0.0367 0.0215  -0.0708 64  PHE B CD2 
1232 C  CE1 . PHE B 64  ? 0.2608 0.2461 0.1950 0.0574  -0.0385 -0.0477 64  PHE B CE1 
1233 C  CE2 . PHE B 64  ? 0.4426 0.4171 0.2825 0.0024  -0.0102 -0.1387 64  PHE B CE2 
1234 C  CZ  . PHE B 64  ? 0.3234 0.2267 0.3156 0.0320  -0.0391 -0.0600 64  PHE B CZ  
1235 N  N   . VAL B 65  ? 0.1767 0.1686 0.2396 0.0007  -0.0280 -0.0908 65  VAL B N   
1236 C  CA  . VAL B 65  ? 0.1559 0.1530 0.2496 0.0022  0.0006  -0.0444 65  VAL B CA  
1237 C  C   . VAL B 65  ? 0.1796 0.2558 0.2192 0.0428  0.0048  -0.0585 65  VAL B C   
1238 O  O   . VAL B 65  ? 0.1845 0.2235 0.2123 0.0088  0.0065  -0.0935 65  VAL B O   
1239 C  CB  . VAL B 65  ? 0.2165 0.1735 0.2434 -0.0058 -0.0195 -0.0679 65  VAL B CB  
1240 C  CG1 . VAL B 65  ? 0.2294 0.1898 0.2932 0.0734  -0.0344 -0.0403 65  VAL B CG1 
1241 C  CG2 . VAL B 65  ? 0.2122 0.2187 0.2338 0.0140  -0.0004 -0.0548 65  VAL B CG2 
1242 N  N   . GLU B 66  ? 0.1680 0.2461 0.2641 0.0267  -0.0028 -0.0956 66  GLU B N   
1243 C  CA  . GLU B 66  ? 0.2113 0.1816 0.2448 0.0295  -0.0094 -0.0558 66  GLU B CA  
1244 C  C   . GLU B 66  ? 0.1973 0.2281 0.2114 0.0173  -0.0240 -0.0305 66  GLU B C   
1245 O  O   . GLU B 66  ? 0.2375 0.2187 0.2981 0.0081  0.0105  -0.0731 66  GLU B O   
1246 C  CB  . GLU B 66  ? 0.1987 0.2632 0.2774 0.0463  0.0066  -0.0573 66  GLU B CB  
1247 C  CG  . GLU B 66  ? 0.1867 0.2901 0.3649 -0.0179 0.0312  -0.1009 66  GLU B CG  
1248 C  CD  . GLU B 66  ? 0.2409 0.2887 0.2439 -0.0141 0.0034  -0.1028 66  GLU B CD  
1249 O  OE1 . GLU B 66  ? 0.2589 0.3060 0.2977 0.0032  0.0120  -0.1364 66  GLU B OE1 
1250 O  OE2 . GLU B 66  ? 0.2436 0.3059 0.4047 -0.0274 -0.0328 -0.0861 66  GLU B OE2 
1251 N  N   . GLY B 67  ? 0.2173 0.2443 0.2280 0.0504  -0.0147 -0.0362 67  GLY B N   
1252 C  CA  . GLY B 67  ? 0.2788 0.1941 0.3113 0.0879  0.0108  -0.0183 67  GLY B CA  
1253 C  C   . GLY B 67  ? 0.2373 0.1632 0.1885 0.0422  0.0025  -0.0006 67  GLY B C   
1254 O  O   . GLY B 67  ? 0.2078 0.2168 0.2378 0.0222  -0.0027 -0.0431 67  GLY B O   
1255 N  N   . ILE B 68  ? 0.1925 0.2376 0.2388 0.0802  0.0026  0.0155  68  ILE B N   
1256 C  CA  . ILE B 68  ? 0.1518 0.2016 0.2579 0.0210  -0.0131 -0.0286 68  ILE B CA  
1257 C  C   . ILE B 68  ? 0.1825 0.1511 0.2194 0.0209  -0.0127 -0.0426 68  ILE B C   
1258 O  O   . ILE B 68  ? 0.2294 0.1452 0.2332 0.0152  -0.0309 -0.0104 68  ILE B O   
1259 C  CB  . ILE B 68  ? 0.1944 0.2606 0.2076 0.0263  -0.0213 -0.0195 68  ILE B CB  
1260 C  CG1 . ILE B 68  ? 0.2722 0.3947 0.2342 0.0038  -0.0434 0.0236  68  ILE B CG1 
1261 C  CG2 . ILE B 68  ? 0.2585 0.2573 0.2204 0.0370  -0.0096 -0.0402 68  ILE B CG2 
1262 C  CD1 . ILE B 68  ? 0.3279 0.3519 0.3232 0.0164  -0.1188 0.0683  68  ILE B CD1 
1263 N  N   . TYR B 69  ? 0.1710 0.1605 0.2178 0.0272  -0.0132 -0.0574 69  TYR B N   
1264 C  CA  . TYR B 69  ? 0.1403 0.1725 0.2247 0.0257  -0.0067 -0.0407 69  TYR B CA  
1265 C  C   . TYR B 69  ? 0.1888 0.1980 0.1781 0.0162  -0.0090 -0.0338 69  TYR B C   
1266 O  O   . TYR B 69  ? 0.1581 0.1695 0.2085 0.0239  0.0157  -0.0309 69  TYR B O   
1267 C  CB  . TYR B 69  ? 0.1642 0.1846 0.2026 0.0325  -0.0099 -0.0356 69  TYR B CB  
1268 C  CG  . TYR B 69  ? 0.1642 0.1794 0.2201 0.0291  -0.0006 -0.0511 69  TYR B CG  
1269 C  CD1 . TYR B 69  ? 0.1352 0.1763 0.2532 0.0117  -0.0174 -0.0745 69  TYR B CD1 
1270 C  CD2 . TYR B 69  ? 0.1501 0.1980 0.2186 0.0010  0.0132  -0.0517 69  TYR B CD2 
1271 C  CE1 . TYR B 69  ? 0.1671 0.2206 0.2232 0.0202  -0.0294 -0.0849 69  TYR B CE1 
1272 C  CE2 . TYR B 69  ? 0.1315 0.2745 0.2142 -0.0187 -0.0189 -0.0981 69  TYR B CE2 
1273 C  CZ  . TYR B 69  ? 0.1712 0.2044 0.1901 0.0157  0.0011  -0.0877 69  TYR B CZ  
1274 O  OH  . TYR B 69  ? 0.1958 0.2284 0.2219 -0.0008 0.0009  -0.1166 69  TYR B OH  
1275 N  N   . LYS B 70  ? 0.1672 0.1655 0.2196 0.0191  0.0154  -0.0233 70  LYS B N   
1276 C  CA  . LYS B 70  ? 0.1657 0.1825 0.2331 0.0417  -0.0122 -0.0125 70  LYS B CA  
1277 C  C   . LYS B 70  ? 0.1341 0.1440 0.2012 0.0048  -0.0222 -0.0232 70  LYS B C   
1278 O  O   . LYS B 70  ? 0.1810 0.1893 0.2295 0.0207  -0.0344 -0.0449 70  LYS B O   
1279 C  CB  . LYS B 70  ? 0.2251 0.1992 0.2214 -0.0057 -0.0013 -0.0502 70  LYS B CB  
1280 C  CG  . LYS B 70  ? 0.2140 0.3055 0.2426 0.0167  0.0132  -0.0006 70  LYS B CG  
1281 C  CD  . LYS B 70  ? 0.2491 0.2911 0.2679 0.0062  0.0055  0.0004  70  LYS B CD  
1282 C  CE  . LYS B 70  ? 0.3683 0.2560 0.3852 -0.0449 0.0316  0.0301  70  LYS B CE  
1283 N  NZ  . LYS B 70  ? 0.4641 0.3687 0.4584 -0.0508 0.1084  0.0725  70  LYS B NZ  
1284 N  N   . VAL B 71  ? 0.1853 0.1766 0.1890 0.0264  -0.0022 0.0017  71  VAL B N   
1285 C  CA  . VAL B 71  ? 0.1548 0.1851 0.2370 0.0565  -0.0011 -0.0221 71  VAL B CA  
1286 C  C   . VAL B 71  ? 0.1883 0.2176 0.1827 0.0056  -0.0348 -0.0599 71  VAL B C   
1287 O  O   . VAL B 71  ? 0.1930 0.2257 0.2029 0.0456  -0.0127 -0.0420 71  VAL B O   
1288 C  CB  . VAL B 71  ? 0.1672 0.2223 0.2231 0.0010  -0.0468 -0.0535 71  VAL B CB  
1289 C  CG1 . VAL B 71  ? 0.1951 0.2337 0.1982 0.0346  -0.0388 -0.0299 71  VAL B CG1 
1290 C  CG2 . VAL B 71  ? 0.1649 0.2668 0.2047 0.0110  -0.0207 -0.0166 71  VAL B CG2 
1291 N  N   . GLU B 72  ? 0.1800 0.2110 0.2056 0.0492  -0.0081 -0.0322 72  GLU B N   
1292 C  CA  . GLU B 72  ? 0.1754 0.2412 0.1699 0.0385  -0.0054 0.0029  72  GLU B CA  
1293 C  C   . GLU B 72  ? 0.1493 0.2357 0.1523 0.0575  -0.0273 -0.0159 72  GLU B C   
1294 O  O   . GLU B 72  ? 0.1879 0.2035 0.1749 0.0466  -0.0134 0.0015  72  GLU B O   
1295 C  CB  . GLU B 72  ? 0.2604 0.2601 0.2518 0.0266  -0.0027 0.0625  72  GLU B CB  
1296 C  CG  . GLU B 72  ? 0.3233 0.3254 0.2634 0.0330  0.0320  -0.0294 72  GLU B CG  
1297 C  CD  . GLU B 72  ? 0.5575 0.3872 0.3354 -0.0731 0.1153  0.1267  72  GLU B CD  
1298 N  N   . ILE B 73  ? 0.1574 0.2558 0.1538 0.0465  -0.0142 -0.0025 73  ILE B N   
1299 C  CA  . ILE B 73  ? 0.1697 0.2001 0.1110 0.0307  0.0039  -0.0093 73  ILE B CA  
1300 C  C   . ILE B 73  ? 0.1607 0.2253 0.1431 0.0326  -0.0104 -0.0147 73  ILE B C   
1301 O  O   . ILE B 73  ? 0.1613 0.2385 0.1430 0.0425  0.0018  0.0192  73  ILE B O   
1302 C  CB  . ILE B 73  ? 0.1989 0.2526 0.1441 -0.0041 0.0049  -0.0323 73  ILE B CB  
1303 C  CG1 . ILE B 73  ? 0.1952 0.2691 0.1755 -0.0339 -0.0305 -0.0324 73  ILE B CG1 
1304 C  CG2 . ILE B 73  ? 0.2176 0.2263 0.2047 -0.0014 0.0185  -0.0144 73  ILE B CG2 
1305 C  CD1 . ILE B 73  ? 0.2581 0.2746 0.1911 -0.0514 0.0130  -0.0438 73  ILE B CD1 
1306 N  N   . ASP B 74  ? 0.1433 0.1832 0.1690 0.0028  0.0044  -0.0054 74  ASP B N   
1307 C  CA  . ASP B 74  ? 0.1596 0.1630 0.2023 -0.0013 0.0154  -0.0370 74  ASP B CA  
1308 C  C   . ASP B 74  ? 0.1419 0.1402 0.1659 0.0091  0.0068  -0.0161 74  ASP B C   
1309 O  O   . ASP B 74  ? 0.1867 0.1678 0.1897 0.0165  -0.0116 -0.0129 74  ASP B O   
1310 C  CB  . ASP B 74  ? 0.1788 0.1087 0.2343 0.0227  0.0037  -0.0385 74  ASP B CB  
1311 C  CG  . ASP B 74  ? 0.1933 0.1538 0.2312 0.0040  0.0234  -0.0088 74  ASP B CG  
1312 O  OD1 . ASP B 74  ? 0.2133 0.1895 0.2635 0.0249  0.0712  -0.0068 74  ASP B OD1 
1313 O  OD2 . ASP B 74  ? 0.2118 0.1989 0.4144 -0.0393 0.0443  -0.0805 74  ASP B OD2 
1314 N  N   . THR B 75  ? 0.1658 0.1313 0.1850 0.0197  -0.0360 -0.0045 75  THR B N   
1315 C  CA  . THR B 75  ? 0.1580 0.1333 0.1707 0.0154  0.0024  0.0037  75  THR B CA  
1316 C  C   . THR B 75  ? 0.1564 0.1545 0.1647 0.0102  0.0235  0.0160  75  THR B C   
1317 O  O   . THR B 75  ? 0.1540 0.1449 0.1433 0.0214  0.0010  -0.0096 75  THR B O   
1318 C  CB  . THR B 75  ? 0.1521 0.1541 0.2130 0.0129  -0.0035 -0.0033 75  THR B CB  
1319 O  OG1 . THR B 75  ? 0.1730 0.1664 0.1623 0.0472  -0.0153 -0.0059 75  THR B OG1 
1320 C  CG2 . THR B 75  ? 0.1700 0.1498 0.2417 -0.0060 0.0321  -0.0235 75  THR B CG2 
1321 N  N   . LYS B 76  ? 0.1677 0.1285 0.1983 0.0087  0.0069  -0.0037 76  LYS B N   
1322 C  CA  . LYS B 76  ? 0.1886 0.1470 0.1790 0.0190  0.0259  0.0009  76  LYS B CA  
1323 C  C   . LYS B 76  ? 0.1850 0.1250 0.2336 0.0230  0.0054  -0.0070 76  LYS B C   
1324 O  O   . LYS B 76  ? 0.1701 0.1380 0.1949 0.0072  0.0138  0.0192  76  LYS B O   
1325 C  CB  . LYS B 76  ? 0.1681 0.1609 0.2267 -0.0095 0.0106  0.0128  76  LYS B CB  
1326 C  CG  . LYS B 76  ? 0.2445 0.2166 0.1751 0.0120  0.0459  0.0620  76  LYS B CG  
1327 C  CD  . LYS B 76  ? 0.2667 0.2523 0.2218 0.0234  0.0291  0.0704  76  LYS B CD  
1328 C  CE  . LYS B 76  ? 0.3419 0.3143 0.2831 -0.0531 0.0875  0.0987  76  LYS B CE  
1329 N  NZ  . LYS B 76  ? 0.2583 0.3307 0.4383 -0.0088 0.0283  0.1361  76  LYS B NZ  
1330 N  N   . SER B 77  ? 0.1583 0.1160 0.2384 0.0092  0.0097  0.0107  77  SER B N   
1331 C  CA  . SER B 77  ? 0.1735 0.1643 0.1615 0.0119  0.0149  -0.0012 77  SER B CA  
1332 C  C   . SER B 77  ? 0.1346 0.1456 0.1932 0.0097  0.0051  -0.0047 77  SER B C   
1333 O  O   . SER B 77  ? 0.1685 0.1541 0.2529 0.0075  -0.0136 -0.0079 77  SER B O   
1334 C  CB  . SER B 77  ? 0.2141 0.1535 0.2162 0.0097  0.0084  -0.0183 77  SER B CB  
1335 O  OG  . SER B 77  ? 0.2578 0.1732 0.3292 0.0000  0.0184  0.0052  77  SER B OG  
1336 N  N   . TYR B 78  ? 0.1355 0.1716 0.1771 0.0146  0.0021  0.0186  78  TYR B N   
1337 C  CA  . TYR B 78  ? 0.1333 0.1818 0.1827 0.0274  -0.0139 0.0308  78  TYR B CA  
1338 C  C   . TYR B 78  ? 0.1229 0.1387 0.2252 0.0106  -0.0222 0.0138  78  TYR B C   
1339 O  O   . TYR B 78  ? 0.1739 0.1463 0.2104 0.0215  -0.0431 0.0151  78  TYR B O   
1340 C  CB  . TYR B 78  ? 0.1615 0.1400 0.1658 0.0105  -0.0017 0.0050  78  TYR B CB  
1341 C  CG  . TYR B 78  ? 0.1447 0.1397 0.1512 -0.0041 0.0179  0.0047  78  TYR B CG  
1342 C  CD1 . TYR B 78  ? 0.1927 0.1412 0.1616 0.0087  -0.0069 -0.0030 78  TYR B CD1 
1343 C  CD2 . TYR B 78  ? 0.1681 0.1499 0.1395 -0.0141 -0.0158 0.0006  78  TYR B CD2 
1344 C  CE1 . TYR B 78  ? 0.2447 0.1473 0.1444 -0.0054 -0.0165 -0.0045 78  TYR B CE1 
1345 C  CE2 . TYR B 78  ? 0.1871 0.1525 0.1318 -0.0219 0.0110  -0.0132 78  TYR B CE2 
1346 C  CZ  . TYR B 78  ? 0.2048 0.1461 0.1360 -0.0305 0.0091  0.0238  78  TYR B CZ  
1347 O  OH  . TYR B 78  ? 0.1958 0.1610 0.1817 -0.0195 -0.0139 0.0258  78  TYR B OH  
1348 N  N   . TRP B 79  ? 0.1637 0.1267 0.2125 0.0297  -0.0355 0.0092  79  TRP B N   
1349 C  CA  . TRP B 79  ? 0.1360 0.1426 0.2202 0.0218  -0.0302 -0.0089 79  TRP B CA  
1350 C  C   . TRP B 79  ? 0.1222 0.1725 0.2216 0.0210  -0.0177 -0.0080 79  TRP B C   
1351 O  O   . TRP B 79  ? 0.1337 0.1887 0.2697 0.0208  -0.0188 -0.0471 79  TRP B O   
1352 C  CB  . TRP B 79  ? 0.1450 0.1067 0.1918 0.0005  -0.0134 -0.0074 79  TRP B CB  
1353 C  CG  . TRP B 79  ? 0.1263 0.1396 0.1763 0.0296  0.0061  0.0004  79  TRP B CG  
1354 C  CD1 . TRP B 79  ? 0.1428 0.1379 0.1510 0.0375  -0.0129 0.0017  79  TRP B CD1 
1355 C  CD2 . TRP B 79  ? 0.1335 0.1479 0.1745 0.0190  -0.0134 -0.0019 79  TRP B CD2 
1356 N  NE1 . TRP B 79  ? 0.1165 0.1519 0.1448 0.0118  -0.0162 -0.0046 79  TRP B NE1 
1357 C  CE2 . TRP B 79  ? 0.1416 0.1388 0.1021 0.0092  -0.0204 -0.0030 79  TRP B CE2 
1358 C  CE3 . TRP B 79  ? 0.1658 0.1471 0.2380 0.0191  -0.0469 0.0213  79  TRP B CE3 
1359 C  CZ2 . TRP B 79  ? 0.1295 0.1285 0.1731 0.0144  0.0061  0.0000  79  TRP B CZ2 
1360 C  CZ3 . TRP B 79  ? 0.1633 0.1507 0.1836 0.0439  -0.0369 0.0080  79  TRP B CZ3 
1361 C  CH2 . TRP B 79  ? 0.1637 0.1486 0.1799 0.0254  -0.0053 -0.0084 79  TRP B CH2 
1362 N  N   . LYS B 80  ? 0.1504 0.1621 0.2067 0.0236  0.0086  0.0241  80  LYS B N   
1363 C  CA  . LYS B 80  ? 0.1429 0.1981 0.2602 -0.0174 -0.0186 0.0217  80  LYS B CA  
1364 C  C   . LYS B 80  ? 0.1447 0.1897 0.2390 0.0007  -0.0058 0.0465  80  LYS B C   
1365 O  O   . LYS B 80  ? 0.1395 0.2052 0.3004 0.0045  -0.0150 0.0176  80  LYS B O   
1366 C  CB  . LYS B 80  ? 0.1500 0.2152 0.3056 -0.0499 -0.0310 0.0501  80  LYS B CB  
1367 C  CG  . LYS B 80  ? 0.2246 0.3220 0.2996 0.0336  0.0431  0.0743  80  LYS B CG  
1368 C  CD  . LYS B 80  ? 0.2700 0.2446 0.4258 0.0331  -0.0552 0.0526  80  LYS B CD  
1369 C  CE  . LYS B 80  ? 0.6677 0.4018 0.3440 0.0795  0.1035  -0.0919 80  LYS B CE  
1370 N  N   . ALA B 81  ? 0.1380 0.1582 0.2482 -0.0053 -0.0201 -0.0032 81  ALA B N   
1371 C  CA  . ALA B 81  ? 0.1904 0.2170 0.2065 0.0151  -0.0334 -0.0286 81  ALA B CA  
1372 C  C   . ALA B 81  ? 0.1597 0.2294 0.2226 0.0249  -0.0156 -0.0217 81  ALA B C   
1373 O  O   . ALA B 81  ? 0.2343 0.2592 0.2854 0.0057  -0.0738 0.0380  81  ALA B O   
1374 C  CB  . ALA B 81  ? 0.2497 0.2859 0.2063 0.0645  -0.0433 -0.0299 81  ALA B CB  
1375 N  N   . LEU B 82  ? 0.1932 0.1699 0.2723 -0.0113 -0.0349 0.0241  82  LEU B N   
1376 C  CA  . LEU B 82  ? 0.2106 0.1627 0.3037 0.0320  -0.0337 0.0395  82  LEU B CA  
1377 C  C   . LEU B 82  ? 0.2059 0.1783 0.3838 0.0685  -0.0438 0.0237  82  LEU B C   
1378 O  O   . LEU B 82  ? 0.2222 0.1910 0.3604 0.0744  0.0014  0.0373  82  LEU B O   
1379 C  CB  . LEU B 82  ? 0.1928 0.1925 0.3215 -0.0047 -0.0015 0.0826  82  LEU B CB  
1380 C  CG  . LEU B 82  ? 0.2754 0.2240 0.4288 0.0082  0.0024  0.0446  82  LEU B CG  
1381 C  CD1 . LEU B 82  ? 0.2325 0.3375 0.4426 -0.0082 -0.0060 0.0511  82  LEU B CD1 
1382 C  CD2 . LEU B 82  ? 0.3518 0.4110 0.4621 0.0613  -0.0205 0.0941  82  LEU B CD2 
1383 N  N   . GLY B 83  ? 0.1659 0.1622 0.3296 0.0294  -0.0334 -0.0491 83  GLY B N   
1384 C  CA  . GLY B 83  ? 0.1318 0.2200 0.2903 0.0434  -0.0326 -0.0325 83  GLY B CA  
1385 C  C   . GLY B 83  ? 0.1601 0.1909 0.2611 0.0364  -0.0089 0.0107  83  GLY B C   
1386 O  O   . GLY B 83  ? 0.1456 0.2698 0.3568 0.0436  -0.0211 -0.0272 83  GLY B O   
1387 N  N   . ILE B 84  ? 0.1413 0.1956 0.3074 -0.0092 0.0059  -0.0381 84  ILE B N   
1388 C  CA  . ILE B 84  ? 0.1429 0.1868 0.2768 0.0046  0.0284  -0.0319 84  ILE B CA  
1389 C  C   . ILE B 84  ? 0.1481 0.1725 0.2924 -0.0009 0.0171  -0.0355 84  ILE B C   
1390 O  O   . ILE B 84  ? 0.1563 0.1874 0.2358 -0.0078 0.0227  0.0039  84  ILE B O   
1391 C  CB  . ILE B 84  ? 0.1542 0.1395 0.2679 0.0243  0.0017  -0.0152 84  ILE B CB  
1392 C  CG1 . ILE B 84  ? 0.2454 0.1630 0.3061 0.0529  -0.0178 -0.0202 84  ILE B CG1 
1393 C  CG2 . ILE B 84  ? 0.2311 0.2027 0.3257 -0.0224 -0.0544 -0.0068 84  ILE B CG2 
1394 C  CD1 . ILE B 84  ? 0.2204 0.2217 0.2915 0.0615  -0.0406 0.0460  84  ILE B CD1 
1395 N  N   . SER B 85  ? 0.1481 0.1471 0.3320 0.0067  0.0135  -0.0281 85  SER B N   
1396 C  CA  . SER B 85  ? 0.1273 0.1921 0.2430 -0.0388 0.0015  -0.0106 85  SER B CA  
1397 C  C   . SER B 85  ? 0.1388 0.1625 0.2384 -0.0235 0.0155  -0.0257 85  SER B C   
1398 O  O   . SER B 85  ? 0.1426 0.1415 0.2662 -0.0150 0.0011  -0.0276 85  SER B O   
1399 C  CB  . SER B 85  ? 0.1830 0.2901 0.2733 -0.0300 0.0373  -0.0595 85  SER B CB  
1400 O  OG  . SER B 85  ? 0.2183 0.2825 0.3686 -0.0794 0.0394  -0.0615 85  SER B OG  
1401 N  N   . PRO B 86  ? 0.1399 0.1669 0.2366 -0.0165 0.0142  0.0002  86  PRO B N   
1402 C  CA  . PRO B 86  ? 0.1401 0.1852 0.2003 0.0039  0.0138  0.0536  86  PRO B CA  
1403 C  C   . PRO B 86  ? 0.1704 0.1808 0.1449 -0.0175 0.0258  0.0251  86  PRO B C   
1404 O  O   . PRO B 86  ? 0.2369 0.2449 0.1922 -0.0662 0.0098  0.0312  86  PRO B O   
1405 C  CB  . PRO B 86  ? 0.1858 0.2374 0.1777 0.0517  0.0364  0.0148  86  PRO B CB  
1406 C  CG  . PRO B 86  ? 0.2504 0.1831 0.1602 0.0133  -0.0028 -0.0023 86  PRO B CG  
1407 C  CD  . PRO B 86  ? 0.1735 0.1949 0.2502 -0.0284 0.0563  -0.0403 86  PRO B CD  
1408 N  N   . PHE B 87  ? 0.1595 0.1253 0.1627 -0.0070 0.0099  -0.0071 87  PHE B N   
1409 C  CA  . PHE B 87  ? 0.1992 0.1439 0.1347 0.0103  0.0491  -0.0080 87  PHE B CA  
1410 C  C   . PHE B 87  ? 0.1762 0.1370 0.1450 -0.0028 0.0227  -0.0100 87  PHE B C   
1411 O  O   . PHE B 87  ? 0.1928 0.1339 0.1644 -0.0287 0.0125  -0.0063 87  PHE B O   
1412 C  CB  . PHE B 87  ? 0.1941 0.1711 0.1415 -0.0218 0.0212  0.0160  87  PHE B CB  
1413 C  CG  . PHE B 87  ? 0.2237 0.1193 0.1614 -0.0210 -0.0144 -0.0190 87  PHE B CG  
1414 C  CD1 . PHE B 87  ? 0.2469 0.1248 0.2066 0.0128  0.0295  0.0212  87  PHE B CD1 
1415 C  CD2 . PHE B 87  ? 0.2458 0.1292 0.1550 -0.0273 0.0044  0.0165  87  PHE B CD2 
1416 C  CE1 . PHE B 87  ? 0.2512 0.1499 0.2380 -0.0508 -0.0148 0.0523  87  PHE B CE1 
1417 C  CE2 . PHE B 87  ? 0.2515 0.1708 0.2357 -0.0319 -0.0190 0.0355  87  PHE B CE2 
1418 C  CZ  . PHE B 87  ? 0.2922 0.1215 0.2152 -0.0459 -0.0827 0.0275  87  PHE B CZ  
1419 N  N   . HIS B 88  ? 0.2142 0.1479 0.1326 0.0426  0.0199  0.0200  88  HIS B N   
1420 C  CA  . HIS B 88  ? 0.2065 0.1648 0.1340 0.0527  0.0318  0.0037  88  HIS B CA  
1421 C  C   . HIS B 88  ? 0.2104 0.1593 0.1508 0.0479  -0.0348 0.0151  88  HIS B C   
1422 O  O   . HIS B 88  ? 0.2713 0.1850 0.1579 0.0877  -0.0459 -0.0029 88  HIS B O   
1423 C  CB  . HIS B 88  ? 0.2088 0.1639 0.1638 0.0864  0.0408  0.0469  88  HIS B CB  
1424 C  CG  . HIS B 88  ? 0.1932 0.1421 0.2377 0.0407  0.0529  0.0692  88  HIS B CG  
1425 N  ND1 . HIS B 88  ? 0.2731 0.1445 0.2653 0.0938  0.0630  0.0705  88  HIS B ND1 
1426 C  CD2 . HIS B 88  ? 0.2747 0.1483 0.3439 0.0637  -0.0250 -0.0460 88  HIS B CD2 
1427 C  CE1 . HIS B 88  ? 0.3264 0.1891 0.3575 0.1044  0.0976  0.0127  88  HIS B CE1 
1428 N  NE2 . HIS B 88  ? 0.3598 0.1127 0.5633 0.0019  0.0201  -0.0668 88  HIS B NE2 
1429 N  N   . GLU B 89  ? 0.2108 0.1579 0.1607 0.0743  -0.0168 0.0131  89  GLU B N   
1430 C  CA  . GLU B 89  ? 0.2183 0.1581 0.1913 0.0599  -0.0196 -0.0263 89  GLU B CA  
1431 C  C   . GLU B 89  ? 0.2165 0.1919 0.1757 0.0874  -0.0380 -0.0326 89  GLU B C   
1432 O  O   . GLU B 89  ? 0.2440 0.3355 0.1516 0.0846  -0.0490 -0.0398 89  GLU B O   
1433 C  CB  . GLU B 89  ? 0.2723 0.1453 0.2158 0.0479  -0.0284 -0.0471 89  GLU B CB  
1434 C  CG  . GLU B 89  ? 0.3200 0.1716 0.2160 0.0194  -0.0584 -0.0311 89  GLU B CG  
1435 C  CD  . GLU B 89  ? 0.3115 0.2483 0.2695 0.0043  -0.0612 -0.0031 89  GLU B CD  
1436 O  OE1 . GLU B 89  ? 0.3491 0.3844 0.3215 -0.0496 -0.0152 -0.0638 89  GLU B OE1 
1437 O  OE2 . GLU B 89  ? 0.3001 0.1905 0.2384 -0.0044 -0.0549 0.0249  89  GLU B OE2 
1438 N  N   . HIS B 90  ? 0.2059 0.2103 0.1471 0.0803  -0.0199 -0.0144 90  HIS B N   
1439 C  CA  . HIS B 90  ? 0.2341 0.2042 0.1633 0.0728  -0.0148 -0.0041 90  HIS B CA  
1440 C  C   . HIS B 90  ? 0.2460 0.2193 0.1301 0.0285  0.0047  -0.0485 90  HIS B C   
1441 O  O   . HIS B 90  ? 0.2676 0.3690 0.1166 0.0183  0.0227  -0.0252 90  HIS B O   
1442 C  CB  . HIS B 90  ? 0.2781 0.2104 0.2218 0.0408  0.0267  -0.0297 90  HIS B CB  
1443 C  CG  . HIS B 90  ? 0.2669 0.2128 0.3099 0.0233  0.0593  -0.0425 90  HIS B CG  
1444 N  ND1 . HIS B 90  ? 0.3730 0.2022 0.4845 0.0331  -0.0338 0.0123  90  HIS B ND1 
1445 C  CD2 . HIS B 90  ? 0.3148 0.2356 0.3306 0.0633  0.0594  0.0552  90  HIS B CD2 
1446 C  CE1 . HIS B 90  ? 0.3478 0.3208 0.2777 0.0487  -0.0085 0.0819  90  HIS B CE1 
1447 N  NE2 . HIS B 90  ? 0.4696 0.2526 0.4433 0.1140  -0.0364 -0.0487 90  HIS B NE2 
1448 N  N   . ALA B 91  ? 0.2198 0.2554 0.1504 0.0214  0.0071  -0.0425 91  ALA B N   
1449 C  CA  . ALA B 91  ? 0.2429 0.2665 0.1821 -0.0208 0.0345  -0.0689 91  ALA B CA  
1450 C  C   . ALA B 91  ? 0.2228 0.3273 0.1792 -0.0114 0.0261  -0.0769 91  ALA B C   
1451 O  O   . ALA B 91  ? 0.1949 0.5173 0.2438 0.0704  -0.0104 -0.1508 91  ALA B O   
1452 C  CB  . ALA B 91  ? 0.3475 0.2791 0.1276 -0.0815 -0.0334 -0.0129 91  ALA B CB  
1453 N  N   . GLU B 92  ? 0.2425 0.3154 0.1909 0.0152  0.0241  -0.0731 92  GLU B N   
1454 C  CA  . GLU B 92  ? 0.1764 0.3920 0.2718 0.0437  0.0331  -0.0620 92  GLU B CA  
1455 C  C   . GLU B 92  ? 0.2523 0.3032 0.1833 -0.0457 0.0009  -0.0017 92  GLU B C   
1456 O  O   . GLU B 92  ? 0.2925 0.5379 0.2016 -0.1107 0.0022  -0.0809 92  GLU B O   
1457 C  CB  . GLU B 92  ? 0.3046 0.4006 0.4229 -0.0008 -0.0634 -0.0160 92  GLU B CB  
1458 C  CG  . GLU B 92  ? 0.3322 0.3358 0.3557 -0.0148 0.0828  -0.0127 92  GLU B CG  
1459 C  CD  . GLU B 92  ? 0.2584 0.3195 0.2148 0.0349  0.0424  -0.0804 92  GLU B CD  
1460 O  OE1 . GLU B 92  ? 0.3147 0.3439 0.3342 -0.0077 0.0480  -0.0675 92  GLU B OE1 
1461 O  OE2 . GLU B 92  ? 0.2998 0.2533 0.3327 0.0892  0.0286  -0.0133 92  GLU B OE2 
1462 N  N   . VAL B 93  ? 0.1948 0.1862 0.2166 0.0180  -0.0051 -0.0112 93  VAL B N   
1463 C  CA  . VAL B 93  ? 0.1976 0.2115 0.2239 -0.0015 0.0158  -0.0643 93  VAL B CA  
1464 C  C   . VAL B 93  ? 0.2089 0.1945 0.1548 0.0397  -0.0395 -0.0632 93  VAL B C   
1465 O  O   . VAL B 93  ? 0.1542 0.1977 0.1940 0.0295  -0.0047 -0.0199 93  VAL B O   
1466 C  CB  . VAL B 93  ? 0.2202 0.1940 0.2542 0.0261  -0.0719 -0.0584 93  VAL B CB  
1467 C  CG1 . VAL B 93  ? 0.1752 0.1781 0.2566 0.0354  -0.0230 -0.0250 93  VAL B CG1 
1468 C  CG2 . VAL B 93  ? 0.2372 0.2070 0.3385 0.0272  -0.0810 -0.0306 93  VAL B CG2 
1469 N  N   . VAL B 94  ? 0.1953 0.2098 0.1980 0.0356  -0.0097 -0.0199 94  VAL B N   
1470 C  CA  . VAL B 94  ? 0.1894 0.1826 0.1974 0.0126  0.0116  -0.0150 94  VAL B CA  
1471 C  C   . VAL B 94  ? 0.2187 0.1636 0.1488 -0.0195 -0.0153 -0.0106 94  VAL B C   
1472 O  O   . VAL B 94  ? 0.1971 0.1670 0.1762 0.0126  -0.0201 -0.0175 94  VAL B O   
1473 C  CB  . VAL B 94  ? 0.1937 0.2072 0.1992 -0.0026 0.0076  0.0049  94  VAL B CB  
1474 C  CG1 . VAL B 94  ? 0.2376 0.2012 0.2915 -0.0055 -0.0335 0.0506  94  VAL B CG1 
1475 C  CG2 . VAL B 94  ? 0.2489 0.2537 0.2395 -0.0245 -0.0041 0.0519  94  VAL B CG2 
1476 N  N   . PHE B 95  ? 0.1700 0.1814 0.1889 0.0040  -0.0066 -0.0345 95  PHE B N   
1477 C  CA  . PHE B 95  ? 0.1709 0.2202 0.2088 -0.0100 -0.0320 -0.0408 95  PHE B CA  
1478 C  C   . PHE B 95  ? 0.1873 0.1939 0.2141 0.0121  -0.0193 -0.0134 95  PHE B C   
1479 O  O   . PHE B 95  ? 0.1733 0.1654 0.2197 0.0073  0.0039  -0.0218 95  PHE B O   
1480 C  CB  . PHE B 95  ? 0.2215 0.1981 0.1980 0.0155  0.0159  -0.0600 95  PHE B CB  
1481 C  CG  . PHE B 95  ? 0.2091 0.1565 0.2055 -0.0197 0.0033  -0.0474 95  PHE B CG  
1482 C  CD1 . PHE B 95  ? 0.2805 0.2042 0.2763 0.0163  -0.0728 -0.0551 95  PHE B CD1 
1483 C  CD2 . PHE B 95  ? 0.2173 0.2267 0.2075 0.0277  -0.0248 -0.0044 95  PHE B CD2 
1484 C  CE1 . PHE B 95  ? 0.2539 0.2020 0.2822 0.0060  -0.0730 -0.0274 95  PHE B CE1 
1485 C  CE2 . PHE B 95  ? 0.3773 0.2266 0.1951 0.0159  -0.0375 -0.0403 95  PHE B CE2 
1486 C  CZ  . PHE B 95  ? 0.3544 0.1858 0.2772 -0.0168 -0.0821 -0.0281 95  PHE B CZ  
1487 N  N   . THR B 96  ? 0.1707 0.2876 0.2286 -0.0136 0.0054  -0.0687 96  THR B N   
1488 C  CA  . THR B 96  ? 0.1847 0.2524 0.2752 0.0417  -0.0181 -0.0456 96  THR B CA  
1489 C  C   . THR B 96  ? 0.2204 0.2514 0.2390 -0.0102 -0.0289 -0.0755 96  THR B C   
1490 O  O   . THR B 96  ? 0.3133 0.3125 0.2470 0.0020  0.0307  -0.0552 96  THR B O   
1491 C  CB  . THR B 96  ? 0.1854 0.3170 0.2533 0.0147  0.0028  -0.0061 96  THR B CB  
1492 O  OG1 . THR B 96  ? 0.2675 0.3872 0.2305 0.0222  -0.0062 0.0083  96  THR B OG1 
1493 C  CG2 . THR B 96  ? 0.1817 0.4577 0.3717 0.0690  0.0333  -0.0299 96  THR B CG2 
1494 N  N   . ALA B 97  ? 0.2003 0.2390 0.2159 0.0149  -0.0072 -0.0444 97  ALA B N   
1495 C  CA  . ALA B 97  ? 0.2672 0.1843 0.1960 0.0361  0.0109  0.0116  97  ALA B CA  
1496 C  C   . ALA B 97  ? 0.2722 0.2612 0.3252 0.0621  0.0094  0.0098  97  ALA B C   
1497 O  O   . ALA B 97  ? 0.1709 0.2686 0.2948 0.0066  -0.0052 -0.0832 97  ALA B O   
1498 C  CB  . ALA B 97  ? 0.2185 0.2857 0.3077 0.0424  -0.0110 -0.0181 97  ALA B CB  
1499 N  N   . ASN B 98  ? 0.2694 0.2723 0.3744 0.0388  0.1021  -0.0532 98  ASN B N   
1500 C  CA  . ASN B 98  ? 0.2475 0.3107 0.3246 -0.0130 0.0058  -0.0299 98  ASN B CA  
1501 C  C   . ASN B 98  ? 0.3464 0.3969 0.2455 0.0242  0.0075  -0.0259 98  ASN B C   
1502 O  O   . ASN B 98  ? 0.2786 0.4777 0.4186 -0.0377 0.0482  -0.0231 98  ASN B O   
1503 C  CB  . ASN B 98  ? 0.3762 0.3959 0.3840 -0.1133 -0.0195 -0.0943 98  ASN B CB  
1504 N  N   . GLY B 101 ? 0.4322 0.3465 0.6899 -0.1072 -0.1037 -0.0064 101 GLY B N   
1505 C  CA  . GLY B 101 ? 0.4758 0.4153 0.4977 -0.0248 -0.0655 -0.0927 101 GLY B CA  
1506 C  C   . GLY B 101 ? 0.3822 0.3838 0.5333 -0.0526 0.0892  -0.0297 101 GLY B C   
1507 O  O   . GLY B 101 ? 0.4408 0.3774 0.6179 -0.0092 0.2103  -0.1061 101 GLY B O   
1508 N  N   . PRO B 102 ? 0.4206 0.3447 0.4945 -0.0967 0.0495  -0.0154 102 PRO B N   
1509 C  CA  . PRO B 102 ? 0.4757 0.3873 0.3430 0.0650  0.0763  0.0253  102 PRO B CA  
1510 C  C   . PRO B 102 ? 0.3688 0.4181 0.5514 0.0320  0.1441  -0.0143 102 PRO B C   
1511 O  O   . PRO B 102 ? 0.5274 0.5248 0.5508 -0.0531 0.1734  -0.1865 102 PRO B O   
1512 C  CB  . PRO B 102 ? 0.4748 0.4445 0.4393 -0.0137 0.0980  0.0764  102 PRO B CB  
1513 C  CG  . PRO B 102 ? 0.5151 0.3309 0.4757 0.1166  0.1372  -0.0044 102 PRO B CG  
1514 C  CD  . PRO B 102 ? 0.3558 0.3576 0.5039 0.0073  0.0685  -0.0026 102 PRO B CD  
1515 N  N   . ARG B 103 ? 0.3950 0.2962 0.5261 -0.0266 0.1550  -0.0494 103 ARG B N   
1516 C  CA  . ARG B 103 ? 0.3455 0.3435 0.3739 0.0524  0.0882  -0.0082 103 ARG B CA  
1517 C  C   . ARG B 103 ? 0.3989 0.3413 0.5263 0.0889  -0.0511 -0.1787 103 ARG B C   
1518 O  O   . ARG B 103 ? 0.4095 0.3775 0.5526 0.0646  0.0026  -0.2354 103 ARG B O   
1519 C  CB  . ARG B 103 ? 0.3741 0.4394 0.4978 0.1209  0.0953  0.1521  103 ARG B CB  
1520 N  N   . ARG B 104 ? 0.3108 0.2343 0.3270 0.0048  0.0619  -0.0636 104 ARG B N   
1521 C  CA  . ARG B 104 ? 0.2415 0.3784 0.3028 -0.0386 0.0411  -0.1186 104 ARG B CA  
1522 C  C   . ARG B 104 ? 0.2295 0.2959 0.3293 -0.0333 0.0536  -0.0912 104 ARG B C   
1523 O  O   . ARG B 104 ? 0.2419 0.2906 0.2707 -0.0503 0.0505  -0.0432 104 ARG B O   
1524 C  CB  . ARG B 104 ? 0.3624 0.6540 0.2553 0.0505  0.0738  -0.0919 104 ARG B CB  
1525 N  N   . TYR B 105 ? 0.2386 0.2448 0.2306 0.0086  0.0164  -0.1384 105 TYR B N   
1526 C  CA  . TYR B 105 ? 0.2186 0.2452 0.2103 -0.0389 -0.0234 -0.1601 105 TYR B CA  
1527 C  C   . TYR B 105 ? 0.1910 0.2399 0.2178 -0.0211 -0.0083 -0.0969 105 TYR B C   
1528 O  O   . TYR B 105 ? 0.1961 0.2729 0.2433 0.0151  -0.0040 -0.1406 105 TYR B O   
1529 C  CB  . TYR B 105 ? 0.1954 0.2218 0.3175 -0.0168 0.0359  -0.0976 105 TYR B CB  
1530 C  CG  . TYR B 105 ? 0.2336 0.1860 0.2795 0.0041  -0.0015 -0.0825 105 TYR B CG  
1531 C  CD1 . TYR B 105 ? 0.2372 0.3016 0.3045 0.0159  -0.0284 -0.1151 105 TYR B CD1 
1532 C  CD2 . TYR B 105 ? 0.2540 0.3993 0.2459 0.0351  0.0458  -0.0583 105 TYR B CD2 
1533 C  CE1 . TYR B 105 ? 0.2281 0.3299 0.4118 0.0049  -0.0247 -0.0339 105 TYR B CE1 
1534 C  CE2 . TYR B 105 ? 0.3580 0.3904 0.3135 0.0093  -0.0898 0.0188  105 TYR B CE2 
1535 C  CZ  . TYR B 105 ? 0.2253 0.2604 0.4353 -0.0372 -0.0629 0.0411  105 TYR B CZ  
1536 O  OH  . TYR B 105 ? 0.2088 0.4685 0.4801 0.0187  -0.0565 0.0762  105 TYR B OH  
1537 N  N   . THR B 106 ? 0.1734 0.2208 0.1632 -0.0309 0.0223  -0.0719 106 THR B N   
1538 C  CA  . THR B 106 ? 0.1669 0.1792 0.1367 -0.0276 -0.0061 -0.0661 106 THR B CA  
1539 C  C   . THR B 106 ? 0.1723 0.1911 0.1396 -0.0070 -0.0132 -0.0886 106 THR B C   
1540 O  O   . THR B 106 ? 0.1923 0.2498 0.1594 -0.0539 0.0117  -0.0931 106 THR B O   
1541 C  CB  . THR B 106 ? 0.2145 0.2104 0.1650 -0.0262 0.0068  -0.0450 106 THR B CB  
1542 O  OG1 . THR B 106 ? 0.3627 0.2447 0.1690 -0.0922 0.0209  0.0051  106 THR B OG1 
1543 C  CG2 . THR B 106 ? 0.2602 0.2041 0.1999 0.0393  -0.0147 0.0533  106 THR B CG2 
1544 N  N   . ILE B 107 ? 0.1688 0.1840 0.1142 -0.0363 -0.0187 -0.0430 107 ILE B N   
1545 C  CA  . ILE B 107 ? 0.1797 0.1777 0.1169 0.0010  -0.0332 -0.0204 107 ILE B CA  
1546 C  C   . ILE B 107 ? 0.1603 0.2181 0.1432 0.0013  -0.0420 -0.0501 107 ILE B C   
1547 O  O   . ILE B 107 ? 0.1625 0.2475 0.1520 0.0023  -0.0251 -0.0396 107 ILE B O   
1548 C  CB  . ILE B 107 ? 0.1938 0.2196 0.1709 -0.0155 -0.0363 -0.0024 107 ILE B CB  
1549 C  CG1 . ILE B 107 ? 0.2353 0.2174 0.2182 -0.0050 0.0040  -0.0138 107 ILE B CG1 
1550 C  CG2 . ILE B 107 ? 0.2181 0.2469 0.1614 -0.0518 -0.0198 -0.0315 107 ILE B CG2 
1551 C  CD1 . ILE B 107 ? 0.2436 0.1776 0.2062 0.0148  -0.0229 -0.0185 107 ILE B CD1 
1552 N  N   . ALA B 108 ? 0.1368 0.2166 0.0983 0.0152  -0.0094 -0.0472 108 ALA B N   
1553 C  CA  . ALA B 108 ? 0.1754 0.2855 0.1055 0.0577  -0.0032 -0.0602 108 ALA B CA  
1554 C  C   . ALA B 108 ? 0.1524 0.2413 0.1104 0.0158  -0.0109 -0.0489 108 ALA B C   
1555 O  O   . ALA B 108 ? 0.1556 0.3456 0.1290 0.0414  -0.0001 -0.0420 108 ALA B O   
1556 C  CB  . ALA B 108 ? 0.2373 0.2532 0.1592 0.0758  0.0019  -0.0465 108 ALA B CB  
1557 N  N   . ALA B 109 ? 0.1335 0.1970 0.1196 0.0275  -0.0163 -0.0700 109 ALA B N   
1558 C  CA  . ALA B 109 ? 0.1503 0.1504 0.1518 0.0335  -0.0042 -0.0563 109 ALA B CA  
1559 C  C   . ALA B 109 ? 0.1475 0.1796 0.0949 0.0285  -0.0158 0.0003  109 ALA B C   
1560 O  O   . ALA B 109 ? 0.1906 0.1976 0.1131 0.0574  -0.0350 -0.0370 109 ALA B O   
1561 C  CB  . ALA B 109 ? 0.1864 0.1626 0.2042 0.0268  -0.0091 -0.0636 109 ALA B CB  
1562 N  N   . LEU B 110 ? 0.1459 0.1481 0.0980 0.0304  -0.0138 -0.0029 110 LEU B N   
1563 C  CA  . LEU B 110 ? 0.1080 0.1348 0.1149 0.0089  -0.0049 -0.0098 110 LEU B CA  
1564 C  C   . LEU B 110 ? 0.1420 0.1180 0.1057 0.0283  -0.0079 -0.0137 110 LEU B C   
1565 O  O   . LEU B 110 ? 0.1572 0.1438 0.1063 0.0171  -0.0075 -0.0024 110 LEU B O   
1566 C  CB  . LEU B 110 ? 0.1675 0.1288 0.1725 0.0173  -0.0137 -0.0312 110 LEU B CB  
1567 C  CG  . LEU B 110 ? 0.1780 0.1218 0.1627 0.0063  0.0020  -0.0157 110 LEU B CG  
1568 C  CD1 . LEU B 110 ? 0.1886 0.1165 0.1448 0.0174  0.0288  -0.0191 110 LEU B CD1 
1569 C  CD2 . LEU B 110 ? 0.2294 0.1558 0.2061 0.0101  -0.0168 -0.0630 110 LEU B CD2 
1570 N  N   . LEU B 111 ? 0.1355 0.1184 0.1145 0.0155  0.0020  0.0062  111 LEU B N   
1571 C  CA  . LEU B 111 ? 0.1353 0.1039 0.1251 0.0126  -0.0099 0.0075  111 LEU B CA  
1572 C  C   . LEU B 111 ? 0.1448 0.1167 0.0995 0.0148  -0.0161 -0.0083 111 LEU B C   
1573 O  O   . LEU B 111 ? 0.1313 0.1197 0.1282 0.0129  -0.0025 0.0061  111 LEU B O   
1574 C  CB  . LEU B 111 ? 0.1522 0.1298 0.1275 0.0244  -0.0138 0.0016  111 LEU B CB  
1575 C  CG  . LEU B 111 ? 0.1596 0.1504 0.1367 0.0260  0.0029  -0.0327 111 LEU B CG  
1576 C  CD1 . LEU B 111 ? 0.1964 0.1370 0.1676 0.0098  -0.0231 -0.0472 111 LEU B CD1 
1577 C  CD2 . LEU B 111 ? 0.1481 0.1328 0.1765 0.0055  0.0231  -0.0214 111 LEU B CD2 
1578 N  N   . SER B 112 ? 0.1275 0.1405 0.1046 0.0398  -0.0183 -0.0029 112 SER B N   
1579 C  CA  . SER B 112 ? 0.1363 0.1297 0.1223 0.0177  0.0066  -0.0082 112 SER B CA  
1580 C  C   . SER B 112 ? 0.1086 0.1599 0.1292 0.0117  0.0255  -0.0204 112 SER B C   
1581 O  O   . SER B 112 ? 0.1611 0.1296 0.1503 0.0421  -0.0151 -0.0277 112 SER B O   
1582 C  CB  . SER B 112 ? 0.1416 0.1562 0.1155 0.0018  -0.0052 0.0025  112 SER B CB  
1583 O  OG  . SER B 112 ? 0.1935 0.1706 0.1524 -0.0308 0.0029  -0.0054 112 SER B OG  
1584 N  N   . PRO B 113 ? 0.1583 0.0925 0.1312 0.0136  -0.0109 -0.0097 113 PRO B N   
1585 C  CA  . PRO B 113 ? 0.1394 0.1322 0.1155 -0.0116 0.0224  -0.0257 113 PRO B CA  
1586 C  C   . PRO B 113 ? 0.1214 0.1227 0.1819 -0.0128 0.0181  -0.0100 113 PRO B C   
1587 O  O   . PRO B 113 ? 0.1659 0.1136 0.1676 -0.0098 0.0130  -0.0113 113 PRO B O   
1588 C  CB  . PRO B 113 ? 0.1663 0.1332 0.1902 -0.0238 0.0297  -0.0231 113 PRO B CB  
1589 C  CG  . PRO B 113 ? 0.1485 0.1755 0.1818 0.0102  0.0275  -0.0288 113 PRO B CG  
1590 C  CD  . PRO B 113 ? 0.1520 0.1532 0.1271 0.0100  -0.0006 0.0165  113 PRO B CD  
1591 N  N   . TYR B 114 ? 0.1357 0.1051 0.1758 0.0000  0.0128  -0.0052 114 TYR B N   
1592 C  CA  . TYR B 114 ? 0.1520 0.0879 0.1541 0.0049  0.0212  -0.0086 114 TYR B CA  
1593 C  C   . TYR B 114 ? 0.1448 0.1331 0.1402 0.0107  0.0013  0.0024  114 TYR B C   
1594 O  O   . TYR B 114 ? 0.1391 0.2121 0.1450 0.0214  0.0078  0.0240  114 TYR B O   
1595 C  CB  . TYR B 114 ? 0.1666 0.1058 0.1609 0.0050  0.0159  -0.0242 114 TYR B CB  
1596 C  CG  . TYR B 114 ? 0.1459 0.1172 0.1376 0.0189  0.0132  0.0209  114 TYR B CG  
1597 C  CD1 . TYR B 114 ? 0.1631 0.2530 0.1426 0.0413  0.0317  0.0668  114 TYR B CD1 
1598 C  CD2 . TYR B 114 ? 0.1604 0.1334 0.1193 0.0032  0.0203  -0.0199 114 TYR B CD2 
1599 C  CE1 . TYR B 114 ? 0.1694 0.4468 0.1916 0.0082  0.0370  0.0376  114 TYR B CE1 
1600 C  CE2 . TYR B 114 ? 0.2022 0.1505 0.0999 -0.0074 0.0337  -0.0170 114 TYR B CE2 
1601 C  CZ  . TYR B 114 ? 0.1706 0.2970 0.2352 -0.0800 0.0187  0.0055  114 TYR B CZ  
1602 O  OH  . TYR B 114 ? 0.2229 0.8123 0.3467 -0.2778 0.1717  0.0200  114 TYR B OH  
1603 N  N   . SER B 115 ? 0.1265 0.1333 0.1474 0.0143  -0.0035 -0.0041 115 SER B N   
1604 C  CA  . SER B 115 ? 0.1237 0.1126 0.1285 0.0085  -0.0023 -0.0001 115 SER B CA  
1605 C  C   . SER B 115 ? 0.1210 0.1550 0.1235 0.0396  0.0075  -0.0003 115 SER B C   
1606 O  O   . SER B 115 ? 0.1556 0.1793 0.1468 0.0388  0.0001  0.0162  115 SER B O   
1607 C  CB  . SER B 115 ? 0.1452 0.1475 0.1374 0.0251  0.0065  0.0012  115 SER B CB  
1608 O  OG  . SER B 115 ? 0.1979 0.1601 0.2013 -0.0052 0.0137  -0.0099 115 SER B OG  
1609 N  N   . TYR B 116 ? 0.1646 0.1339 0.0912 0.0076  -0.0033 0.0158  116 TYR B N   
1610 C  CA  A TYR B 116 ? 0.1281 0.1132 0.1086 0.0096  -0.0043 0.0127  116 TYR B CA  
1611 C  CA  B TYR B 116 ? 0.1271 0.1124 0.1095 0.0117  -0.0058 0.0138  116 TYR B CA  
1612 C  C   . TYR B 116 ? 0.1392 0.1083 0.1237 0.0111  -0.0198 -0.0023 116 TYR B C   
1613 O  O   . TYR B 116 ? 0.1437 0.1280 0.0993 0.0130  0.0056  -0.0002 116 TYR B O   
1614 C  CB  A TYR B 116 ? 0.1285 0.1513 0.1333 0.0000  0.0052  -0.0176 116 TYR B CB  
1615 C  CB  B TYR B 116 ? 0.1254 0.1555 0.1334 -0.0032 -0.0043 -0.0160 116 TYR B CB  
1616 C  CG  A TYR B 116 ? 0.1554 0.1555 0.1616 -0.0355 -0.0166 0.0097  116 TYR B CG  
1617 C  CG  B TYR B 116 ? 0.1501 0.1442 0.1568 -0.0337 -0.0314 0.0095  116 TYR B CG  
1618 C  CD1 A TYR B 116 ? 0.2436 0.1323 0.2242 -0.0598 -0.0308 0.0539  116 TYR B CD1 
1619 C  CD1 B TYR B 116 ? 0.1831 0.0830 0.2880 -0.0393 -0.0050 0.0136  116 TYR B CD1 
1620 C  CD2 A TYR B 116 ? 0.2056 0.1206 0.2623 -0.0061 -0.0029 0.0013  116 TYR B CD2 
1621 C  CD2 B TYR B 116 ? 0.1791 0.1253 0.1983 -0.0445 -0.0793 0.0317  116 TYR B CD2 
1622 C  CE1 A TYR B 116 ? 0.3302 0.1276 0.3155 -0.0803 -0.0954 0.0836  116 TYR B CE1 
1623 C  CE1 B TYR B 116 ? 0.2570 0.1077 0.2731 -0.0060 -0.0669 0.0090  116 TYR B CE1 
1624 C  CE2 A TYR B 116 ? 0.2869 0.1296 0.3971 -0.0234 -0.0863 0.0605  116 TYR B CE2 
1625 C  CE2 B TYR B 116 ? 0.2087 0.1238 0.2178 -0.0342 0.0142  0.0272  116 TYR B CE2 
1626 C  CZ  A TYR B 116 ? 0.4008 0.0612 0.2602 0.0612  -0.0476 -0.0260 116 TYR B CZ  
1627 C  CZ  B TYR B 116 ? 0.1999 0.1287 0.3055 -0.0219 -0.0644 0.0359  116 TYR B CZ  
1628 O  OH  A TYR B 116 ? 0.2933 0.1080 0.6480 0.0441  -0.0483 0.1213  116 TYR B OH  
1629 O  OH  B TYR B 116 ? 0.1098 0.1344 0.4584 -0.0231 -0.0233 -0.0601 116 TYR B OH  
1630 N  N   . SER B 117 ? 0.1447 0.1124 0.1119 0.0054  -0.0122 0.0112  117 SER B N   
1631 C  CA  . SER B 117 ? 0.1326 0.1306 0.1136 -0.0021 0.0056  -0.0086 117 SER B CA  
1632 C  C   . SER B 117 ? 0.1315 0.1704 0.1084 -0.0010 0.0059  0.0116  117 SER B C   
1633 O  O   . SER B 117 ? 0.1453 0.2033 0.1257 0.0306  -0.0216 -0.0202 117 SER B O   
1634 C  CB  . SER B 117 ? 0.2761 0.2162 0.2057 -0.0839 0.0623  -0.0534 117 SER B CB  
1635 O  OG  . SER B 117 ? 0.6115 0.2003 0.3323 -0.0034 0.0688  -0.0430 117 SER B OG  
1636 N  N   . THR B 118 ? 0.1290 0.1777 0.0982 0.0090  0.0039  0.0131  118 THR B N   
1637 C  CA  . THR B 118 ? 0.1337 0.1875 0.1129 0.0293  -0.0039 0.0175  118 THR B CA  
1638 C  C   . THR B 118 ? 0.1370 0.2328 0.1183 0.0408  0.0010  0.0188  118 THR B C   
1639 O  O   . THR B 118 ? 0.1598 0.2738 0.1494 0.0068  0.0086  0.0165  118 THR B O   
1640 C  CB  . THR B 118 ? 0.1727 0.1826 0.0995 0.0133  -0.0070 -0.0004 118 THR B CB  
1641 O  OG1 . THR B 118 ? 0.1965 0.1949 0.1608 0.0333  -0.0128 -0.0327 118 THR B OG1 
1642 C  CG2 . THR B 118 ? 0.1905 0.1722 0.1695 0.0377  -0.0115 0.0268  118 THR B CG2 
1643 N  N   . THR B 119 ? 0.1279 0.1931 0.1390 0.0149  -0.0135 -0.0005 119 THR B N   
1644 C  CA  A THR B 119 ? 0.1314 0.1861 0.1533 -0.0041 0.0106  -0.0066 119 THR B CA  
1645 C  CA  B THR B 119 ? 0.1355 0.1736 0.1585 0.0030  0.0160  -0.0088 119 THR B CA  
1646 C  C   . THR B 119 ? 0.1567 0.1486 0.1106 -0.0141 -0.0072 0.0070  119 THR B C   
1647 O  O   . THR B 119 ? 0.1403 0.1756 0.1705 0.0014  0.0087  -0.0306 119 THR B O   
1648 C  CB  A THR B 119 ? 0.1440 0.1876 0.1787 -0.0088 -0.0242 -0.0094 119 THR B CB  
1649 C  CB  B THR B 119 ? 0.2029 0.1598 0.1885 0.0142  -0.0123 -0.0262 119 THR B CB  
1650 O  OG1 A THR B 119 ? 0.2847 0.2237 0.1935 0.0184  -0.0152 -0.0247 119 THR B OG1 
1651 O  OG1 B THR B 119 ? 0.2204 0.1578 0.2385 -0.0323 0.0188  -0.0115 119 THR B OG1 
1652 C  CG2 A THR B 119 ? 0.1252 0.0843 0.1607 -0.0112 0.0120  -0.0020 119 THR B CG2 
1653 C  CG2 B THR B 119 ? 0.1656 0.1176 0.1817 0.0433  0.0009  -0.0496 119 THR B CG2 
1654 N  N   . ALA B 120 ? 0.1313 0.2014 0.1428 0.0074  -0.0085 -0.0378 120 ALA B N   
1655 C  CA  . ALA B 120 ? 0.1606 0.1951 0.1322 -0.0058 0.0170  -0.0547 120 ALA B CA  
1656 C  C   . ALA B 120 ? 0.1321 0.1969 0.2106 -0.0336 0.0190  -0.0577 120 ALA B C   
1657 O  O   . ALA B 120 ? 0.1879 0.2648 0.1621 -0.0586 0.0329  -0.0782 120 ALA B O   
1658 C  CB  . ALA B 120 ? 0.2181 0.1753 0.2708 0.0044  0.0247  -0.0250 120 ALA B CB  
1659 N  N   . VAL B 121 ? 0.1770 0.1832 0.2040 -0.0575 -0.0033 -0.0470 121 VAL B N   
1660 C  CA  . VAL B 121 ? 0.2210 0.1922 0.2309 -0.0802 -0.0258 -0.0527 121 VAL B CA  
1661 C  C   . VAL B 121 ? 0.2479 0.2111 0.1830 -0.0545 0.0035  -0.0125 121 VAL B C   
1662 O  O   . VAL B 121 ? 0.2087 0.2798 0.2168 -0.0641 0.0456  -0.0963 121 VAL B O   
1663 C  CB  . VAL B 121 ? 0.2494 0.2712 0.2348 -0.0636 0.0164  -0.0032 121 VAL B CB  
1664 C  CG1 . VAL B 121 ? 0.4147 0.2420 0.3254 -0.1458 0.0032  -0.0073 121 VAL B CG1 
1665 C  CG2 . VAL B 121 ? 0.3472 0.2387 0.3226 -0.0357 -0.0485 0.0363  121 VAL B CG2 
1666 N  N   . VAL B 122 ? 0.2180 0.2696 0.2355 -0.0402 0.0270  -0.0490 122 VAL B N   
1667 C  CA  . VAL B 122 ? 0.1828 0.3204 0.2803 -0.0124 -0.0019 -0.0661 122 VAL B CA  
1668 C  C   . VAL B 122 ? 0.3105 0.3838 0.3027 -0.1131 0.0566  -0.0898 122 VAL B C   
1669 O  O   . VAL B 122 ? 0.2962 0.3351 0.2769 -0.0620 0.0486  -0.0587 122 VAL B O   
1670 C  CB  . VAL B 122 ? 0.2148 0.2995 0.4189 -0.0262 0.0602  -0.0173 122 VAL B CB  
1671 C  CG1 . VAL B 122 ? 0.3228 0.4346 0.3664 0.0608  0.0043  -0.0949 122 VAL B CG1 
1672 C  CG2 . VAL B 122 ? 0.3128 0.2687 0.2930 -0.0247 0.0349  -0.0375 122 VAL B CG2 
1673 N  N   . THR B 123 ? 0.3154 0.2277 0.2974 -0.0277 0.0691  -0.0181 123 THR B N   
1674 C  CA  . THR B 123 ? 0.4108 0.2682 0.2335 -0.0456 0.0763  -0.0396 123 THR B CA  
1675 C  C   . THR B 123 ? 0.5850 0.1702 0.4442 -0.0179 0.1080  -0.1315 123 THR B C   
1676 O  O   . THR B 123 ? 0.4762 0.2605 0.3490 -0.0750 0.1719  -0.0880 123 THR B O   
1677 C  CB  . THR B 123 ? 0.4055 0.3471 0.3864 0.0112  0.0103  -0.0557 123 THR B CB  
1678 O  OG1 . THR B 123 ? 0.4315 0.3105 0.3764 0.0379  0.0293  -0.0487 123 THR B OG1 
1679 C  CG2 . THR B 123 ? 0.3812 0.3020 0.2880 0.0532  0.0578  -0.0939 123 THR B CG2 
1680 CA CA  . CA  C .   ? 0.1701 0.2025 0.3068 -0.0146 0.0053  0.0327  201 CA  A CA  
1681 C  C12 . MSR D .   ? 0.3176 0.3839 0.2548 0.0554  -0.0031 0.0076  202 MSR A C12 
1682 C  C13 . MSR D .   ? 0.3317 0.3118 0.2356 0.0191  0.0166  -0.0034 202 MSR A C13 
1683 C  C14 . MSR D .   ? 0.3300 0.2900 0.2361 -0.0239 0.0229  0.0012  202 MSR A C14 
1684 O  O17 . MSR D .   ? 0.3385 0.4055 0.3179 0.0717  -0.0541 0.0194  202 MSR A O17 
1685 C  C15 . MSR D .   ? 0.1958 0.2281 0.2851 -0.0174 0.0005  0.0323  202 MSR A C15 
1686 C  C16 . MSR D .   ? 0.1736 0.3316 0.2667 -0.0361 0.0192  0.0341  202 MSR A C16 
1687 C  C11 . MSR D .   ? 0.2667 0.2539 0.3195 -0.0399 0.0181  0.0288  202 MSR A C11 
1688 N  N3  . MSR D .   ? 0.2874 0.2568 0.2873 -0.0212 -0.0210 -0.0184 202 MSR A N3  
1689 C  C4  . MSR D .   ? 0.2476 0.2001 0.2633 -0.0064 0.0099  -0.0008 202 MSR A C4  
1690 C  C5  . MSR D .   ? 0.2005 0.2466 0.2614 0.0486  -0.0477 -0.0092 202 MSR A C5  
1691 N  NFE . MSR D .   ? 0.3117 0.2545 0.3815 0.0701  -0.0106 -0.0173 202 MSR A NFE 
1692 C  C2  . MSR D .   ? 0.3585 0.2602 0.2908 -0.0290 0.0435  0.0188  202 MSR A C2  
1693 CA CA  . CA  E .   ? 0.3116 0.4692 0.4381 0.0004  0.0288  -0.0925 201 CA  B CA  
1694 C  C12 . MSR F .   ? 0.3020 0.2416 0.3733 0.0007  0.0433  0.0479  202 MSR B C12 
1695 C  C13 . MSR F .   ? 0.1885 0.2522 0.3087 0.0397  0.0197  -0.0150 202 MSR B C13 
1696 C  C14 . MSR F .   ? 0.2656 0.3196 0.2883 -0.0162 0.0186  -0.0240 202 MSR B C14 
1697 O  O17 . MSR F .   ? 0.3987 0.4711 0.3635 0.0434  0.0113  -0.0479 202 MSR B O17 
1698 C  C15 . MSR F .   ? 0.2459 0.2675 0.3481 -0.0084 0.0205  0.1020  202 MSR B C15 
1699 C  C16 . MSR F .   ? 0.3337 0.2837 0.3496 -0.0804 0.0638  -0.0566 202 MSR B C16 
1700 C  C11 . MSR F .   ? 0.4054 0.3530 0.3655 0.0028  -0.0177 -0.0685 202 MSR B C11 
1701 N  N3  . MSR F .   ? 0.3231 0.4292 0.3360 -0.0048 -0.0205 0.0097  202 MSR B N3  
1702 C  C4  . MSR F .   ? 0.2602 0.2260 0.4474 0.0454  -0.0170 0.0175  202 MSR B C4  
1703 C  C5  . MSR F .   ? 0.3054 0.3719 0.3590 0.0367  0.0914  0.0443  202 MSR B C5  
1704 N  NFE . MSR F .   ? 0.3437 0.2379 0.3805 -0.0135 -0.0093 -0.0149 202 MSR B NFE 
1705 C  C2  . MSR F .   ? 0.2242 0.2260 0.3625 0.0234  0.0250  0.0760  202 MSR B C2  
1706 O  O   . HOH G .   ? 0.2503 0.2978 0.3187 0.0458  -0.0731 0.0377  301 HOH A O   
1707 O  O   . HOH G .   ? 0.3705 0.2608 0.2745 0.1570  -0.0933 -0.0737 302 HOH A O   
1708 O  O   . HOH G .   ? 0.1547 0.1703 0.1869 -0.0058 -0.0071 0.0322  303 HOH A O   
1709 O  O   . HOH G .   ? 0.1935 0.1776 0.2326 0.0040  0.0008  0.0121  304 HOH A O   
1710 O  O   . HOH G .   ? 0.2830 0.2032 0.1413 -0.0818 -0.0208 0.0436  305 HOH A O   
1711 O  O   . HOH G .   ? 0.2305 0.3706 0.4074 0.0178  -0.0992 0.0627  306 HOH A O   
1712 O  O   . HOH G .   ? 0.2719 0.2249 0.2296 0.0682  -0.0206 0.0511  307 HOH A O   
1713 O  O   . HOH G .   ? 0.1755 0.1970 0.1913 -0.0278 0.0027  0.0007  308 HOH A O   
1714 O  O   . HOH G .   ? 0.2289 0.2202 0.4148 0.0475  -0.0335 0.0362  309 HOH A O   
1715 O  O   . HOH G .   ? 0.2658 0.2555 0.2084 0.0301  -0.0279 0.0271  310 HOH A O   
1716 O  O   . HOH G .   ? 0.4002 0.4068 0.1711 0.0021  -0.0256 -0.0291 311 HOH A O   
1717 O  O   . HOH G .   ? 0.2303 0.3066 0.4175 -0.0370 -0.0427 -0.0623 312 HOH A O   
1718 O  O   . HOH G .   ? 0.3202 0.2612 0.2843 0.0277  -0.0688 0.0333  313 HOH A O   
1719 O  O   . HOH G .   ? 0.2407 0.1829 0.2838 -0.0343 -0.0269 0.0197  314 HOH A O   
1720 O  O   . HOH G .   ? 0.2277 0.1417 0.2900 -0.0192 0.0694  0.0458  315 HOH A O   
1721 O  O   . HOH G .   ? 0.4422 0.2380 0.3611 -0.0494 0.0557  0.0159  316 HOH A O   
1722 O  O   . HOH G .   ? 0.2619 0.4207 0.3460 -0.0909 -0.0455 0.1520  317 HOH A O   
1723 O  O   . HOH G .   ? 0.2282 0.2267 0.2616 0.0363  0.0523  0.0966  318 HOH A O   
1724 O  O   . HOH G .   ? 0.3439 0.2555 0.4163 -0.0884 -0.0367 0.1142  319 HOH A O   
1725 O  O   . HOH G .   ? 0.2870 0.2362 0.2600 0.0066  0.0299  0.0316  320 HOH A O   
1726 O  O   . HOH G .   ? 0.2316 0.2142 0.2987 0.0030  -0.0175 0.0528  321 HOH A O   
1727 O  O   . HOH G .   ? 0.1826 0.1565 0.1489 -0.0115 0.0066  0.0185  322 HOH A O   
1728 O  O   . HOH G .   ? 0.1630 0.1940 0.1678 -0.0029 0.0103  0.0166  323 HOH A O   
1729 O  O   . HOH G .   ? 0.2327 0.2019 0.2773 0.0155  0.0371  0.0819  324 HOH A O   
1730 O  O   . HOH G .   ? 0.2159 0.1668 0.2695 -0.0198 -0.0215 0.0716  325 HOH A O   
1731 O  O   . HOH G .   ? 0.2476 0.1973 0.2977 -0.0059 0.0192  0.0246  326 HOH A O   
1732 O  O   . HOH G .   ? 0.3387 0.2744 0.3505 0.0378  -0.0281 0.0256  327 HOH A O   
1733 O  O   . HOH G .   ? 0.3622 0.3666 0.2883 -0.0013 -0.0023 -0.0187 328 HOH A O   
1734 O  O   . HOH G .   ? 0.5140 0.3099 0.2274 -0.1302 0.0295  -0.0051 329 HOH A O   
1735 O  O   . HOH G .   ? 0.1809 0.1424 0.1938 -0.0079 0.0149  -0.0136 330 HOH A O   
1736 O  O   . HOH G .   ? 0.2286 0.2239 0.3857 0.0340  -0.0008 -0.0095 331 HOH A O   
1737 O  O   . HOH G .   ? 0.2191 0.1838 0.2348 0.0312  -0.0234 -0.0040 332 HOH A O   
1738 O  O   . HOH G .   ? 0.2806 0.3786 0.3040 0.0210  -0.0054 0.0818  333 HOH A O   
1739 O  O   . HOH G .   ? 0.4470 0.2304 0.2937 -0.0230 0.0870  0.0454  334 HOH A O   
1740 O  O   . HOH G .   ? 0.2261 0.2981 0.3061 -0.0725 -0.0164 0.0372  335 HOH A O   
1741 O  O   . HOH G .   ? 0.2867 0.1908 0.2914 0.0115  0.0194  -0.0003 336 HOH A O   
1742 O  O   . HOH G .   ? 0.2469 0.2623 0.3045 -0.0178 0.0208  0.0452  337 HOH A O   
1743 O  O   . HOH G .   ? 0.3666 0.2777 0.3603 0.0397  0.0794  0.1005  338 HOH A O   
1744 O  O   . HOH G .   ? 0.2533 0.3001 0.2896 0.0146  0.0210  0.0863  339 HOH A O   
1745 O  O   . HOH G .   ? 0.2031 0.2312 0.2529 -0.0202 0.0184  0.0762  340 HOH A O   
1746 O  O   . HOH G .   ? 0.1904 0.2119 0.2141 0.0363  0.0159  0.0652  341 HOH A O   
1747 O  O   . HOH G .   ? 0.2565 0.1858 0.2621 -0.0049 -0.0097 0.0516  342 HOH A O   
1748 O  O   . HOH G .   ? 0.2637 0.3195 0.3030 -0.0386 -0.0310 0.0738  343 HOH A O   
1749 O  O   . HOH G .   ? 0.3399 0.4042 0.3036 0.0222  -0.0547 -0.1009 344 HOH A O   
1750 O  O   . HOH G .   ? 0.2716 0.2243 0.2639 0.0205  0.0219  0.0300  345 HOH A O   
1751 O  O   . HOH G .   ? 0.2551 0.1910 0.2456 0.0123  0.0096  0.0220  346 HOH A O   
1752 O  O   . HOH G .   ? 0.2777 0.3446 0.2223 -0.0335 -0.0585 -0.0240 347 HOH A O   
1753 O  O   . HOH G .   ? 0.2125 0.1744 0.1676 0.0186  0.0058  0.0231  348 HOH A O   
1754 O  O   . HOH G .   ? 0.3195 0.2252 0.2883 0.0452  0.0261  0.0645  349 HOH A O   
1755 O  O   . HOH G .   ? 0.3475 0.3309 0.3041 0.0801  0.1235  0.1040  350 HOH A O   
1756 O  O   . HOH G .   ? 0.3837 0.3865 0.4489 -0.0400 0.0787  -0.0456 351 HOH A O   
1757 O  O   . HOH G .   ? 0.3391 0.2864 0.3110 -0.0289 0.0297  0.0559  352 HOH A O   
1758 O  O   . HOH G .   ? 0.7533 0.3463 0.1959 0.2241  -0.1042 0.0539  353 HOH A O   
1759 O  O   . HOH G .   ? 0.3156 0.2300 0.3281 0.0725  -0.0186 0.0136  354 HOH A O   
1760 O  O   . HOH G .   ? 0.2870 0.2948 0.3457 0.0112  0.0266  0.0757  355 HOH A O   
1761 O  O   . HOH G .   ? 0.1822 0.1991 0.2407 0.0422  -0.0069 0.0574  356 HOH A O   
1762 O  O   . HOH G .   ? 0.2655 0.3738 0.3862 -0.0307 0.0403  -0.0629 357 HOH A O   
1763 O  O   . HOH G .   ? 0.2734 0.1523 0.2401 0.0221  0.0379  0.0169  358 HOH A O   
1764 O  O   . HOH G .   ? 0.4367 0.3721 0.2944 0.1480  0.0448  0.0309  359 HOH A O   
1765 O  O   . HOH G .   ? 0.3028 0.4108 0.3175 -0.0203 0.0114  0.0142  360 HOH A O   
1766 O  O   . HOH G .   ? 0.3601 0.2772 0.4227 0.0167  0.0812  0.0560  361 HOH A O   
1767 O  O   . HOH H .   ? 0.3780 0.1650 0.4150 -0.0051 0.0001  -0.0001 301 HOH B O   
1768 O  O   . HOH H .   ? 0.3960 0.5139 0.3063 0.1898  -0.0743 -0.1566 302 HOH B O   
1769 O  O   . HOH H .   ? 0.2123 0.2322 0.2041 -0.0063 -0.0213 0.0750  303 HOH B O   
1770 O  O   . HOH H .   ? 0.2114 0.2266 0.1561 0.1000  0.0124  0.0326  304 HOH B O   
1771 O  O   . HOH H .   ? 0.4930 0.2758 0.4324 -0.0616 0.1250  -0.1731 305 HOH B O   
1772 O  O   . HOH H .   ? 0.1738 0.1915 0.3779 0.0403  0.0217  -0.0652 306 HOH B O   
1773 O  O   . HOH H .   ? 0.3869 0.1643 0.2543 0.1095  0.1082  0.0480  307 HOH B O   
1774 O  O   . HOH H .   ? 0.3781 0.3649 0.1979 0.0197  0.0207  0.0005  308 HOH B O   
1775 O  O   . HOH H .   ? 0.2851 0.2356 0.2666 -0.0360 0.0332  0.0219  309 HOH B O   
1776 O  O   . HOH H .   ? 0.4190 0.3746 0.2466 0.0779  0.0039  -0.0351 310 HOH B O   
1777 O  O   . HOH H .   ? 0.3092 0.3029 0.3147 0.0382  -0.0363 -0.1275 311 HOH B O   
1778 O  O   . HOH H .   ? 0.1476 0.1463 0.1716 0.0215  0.0002  -0.0199 312 HOH B O   
1779 O  O   . HOH H .   ? 0.1993 0.1636 0.2134 0.0123  0.0169  -0.0118 313 HOH B O   
1780 O  O   . HOH H .   ? 0.2492 0.2589 0.3982 -0.0289 0.0059  -0.0279 314 HOH B O   
1781 O  O   . HOH H .   ? 0.3083 0.1975 0.4394 0.0602  0.0906  0.0251  315 HOH B O   
1782 O  O   . HOH H .   ? 0.2462 0.2142 0.2098 0.0679  -0.0320 -0.0198 316 HOH B O   
1783 O  O   . HOH H .   ? 0.1645 0.1945 0.3262 -0.0036 0.0066  -0.0794 317 HOH B O   
1784 O  O   . HOH H .   ? 0.3589 0.2406 0.4124 0.0180  -0.0313 -0.0595 318 HOH B O   
1785 O  O   . HOH H .   ? 0.3437 0.4334 0.4052 0.0327  0.0399  -0.0510 319 HOH B O   
1786 O  O   . HOH H .   ? 0.4461 0.3101 0.3861 -0.0203 0.0121  0.0637  320 HOH B O   
1787 O  O   . HOH H .   ? 0.2115 0.2220 0.2163 0.0199  0.0092  -0.0148 321 HOH B O   
1788 O  O   . HOH H .   ? 0.2864 0.2939 0.2572 0.0381  0.0276  -0.0195 322 HOH B O   
1789 O  O   . HOH H .   ? 0.2679 0.4441 0.3722 0.0309  0.0389  -0.1375 323 HOH B O   
1790 O  O   . HOH H .   ? 0.3223 0.4296 0.1813 -0.0213 -0.0415 0.0170  324 HOH B O   
1791 O  O   . HOH H .   ? 0.2495 0.4220 0.2383 -0.0065 0.0228  -0.0069 325 HOH B O   
1792 O  O   . HOH H .   ? 0.4541 0.2451 0.1771 -0.0217 -0.0401 -0.0160 326 HOH B O   
1793 O  O   . HOH H .   ? 0.2033 0.2508 0.2239 -0.0425 -0.0046 0.0232  327 HOH B O   
1794 O  O   . HOH H .   ? 0.4256 0.3124 0.3659 0.1117  -0.0493 -0.0410 328 HOH B O   
1795 O  O   . HOH H .   ? 0.2152 0.3280 0.3856 0.0230  -0.0268 -0.0913 329 HOH B O   
1796 O  O   . HOH H .   ? 0.3107 0.3825 0.3094 -0.0392 -0.0412 -0.0306 330 HOH B O   
1797 O  O   . HOH H .   ? 0.4143 0.3589 0.2899 -0.0007 -0.1274 -0.0653 331 HOH B O   
1798 O  O   . HOH H .   ? 0.4632 0.4279 0.3776 -0.0067 -0.0488 -0.0383 332 HOH B O   
1799 O  O   . HOH H .   ? 0.2979 0.3409 0.3885 0.0472  0.0153  -0.0569 333 HOH B O   
1800 O  O   . HOH H .   ? 0.3352 0.3146 0.4365 -0.0749 -0.0352 -0.0578 334 HOH B O   
1801 O  O   . HOH H .   ? 0.1976 0.3738 0.3567 0.0673  0.0669  -0.0280 335 HOH B O   
1802 O  O   . HOH H .   ? 0.4252 0.3286 0.3476 -0.1104 -0.0192 -0.0207 336 HOH B O   
# 
