data_9H7L
# 
_entry.id   9H7L 
# 
_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   9H7L         pdb_00009h7l 10.2210/pdb9h7l/pdb 
WWPDB D_1292142801 ?            ?                   
# 
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                        9H7L 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.wood@ucl.ac.uk 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Wood 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4106-775X 
# 
_audit_author.name               'Chen, W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8180-366X 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Plos One' ? ? 1932-6203 ? ? 20 ? e0323816 e0323816 
'Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.' 2025 ? 
10.1371/journal.pone.0323816 40367241 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv    ? ? 2692-8205 ? ? ?  ? ?        ?        
'Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method'  2025 ? 
10.1101/2025.02.22.639275    ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, W.' 1 0000-0002-8180-366X 
1       'Chen, W.' 2 0000-0002-8180-366X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Transthyretin                                13777.360 2  ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                                40.078    2  ? ? ? ? 
3 non-polymer syn '4-phenyl-2H-pyrazolo[3,4-b]pyridin-3-amine' 210.235   2  ? ? ? ? 
4 water       nat water                                        18.015    98 ? ? ? ? 
# 
_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-phenyl-2H-pyrazolo[3,4-b]pyridin-3-amine' A1IS0 
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 
A1IS0 non-polymer         . '4-phenyl-2H-pyrazolo[3,4-b]pyridin-3-amine' ? 'C12 H10 N4'     210.235 
ALA   'L-peptide linking' y ALANINE                                      ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                     ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                   ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                              ? 'C4 H7 N O4'     133.103 
CA    non-polymer         . 'CALCIUM ION'                                ? 'Ca 2'           40.078  
CYS   'L-peptide linking' y CYSTEINE                                     ? 'C3 H7 N O2 S'   121.158 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                              ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                      ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                    ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                        ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                   ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                      ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                       ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                   ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                      ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                       ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                    ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                   ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                     ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                       ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 ?   ?   ?   A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  CYS 10  10  ?   ?   ?   B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ASP 39  39  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 ?   ?   ?   B . n 
B 1 102 PRO 102 102 ?   ?   ?   B . n 
B 1 103 ARG 103 103 ?   ?   ?   B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 THR 123 123 123 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        A1IS0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IS0 
_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 A1IS0 1  202 2  A1IS0 361 A . 
E 2 CA    1  201 1  CA    CA  B . 
F 3 A1IS0 1  202 1  A1IS0 361 B . 
G 4 HOH   1  301 53 HOH   HOH A . 
G 4 HOH   2  302 79 HOH   HOH A . 
G 4 HOH   3  303 59 HOH   HOH A . 
G 4 HOH   4  304 90 HOH   HOH A . 
G 4 HOH   5  305 7  HOH   HOH A . 
G 4 HOH   6  306 24 HOH   HOH A . 
G 4 HOH   7  307 31 HOH   HOH A . 
G 4 HOH   8  308 33 HOH   HOH A . 
G 4 HOH   9  309 29 HOH   HOH A . 
G 4 HOH   10 310 47 HOH   HOH A . 
G 4 HOH   11 311 76 HOH   HOH A . 
G 4 HOH   12 312 75 HOH   HOH A . 
G 4 HOH   13 313 18 HOH   HOH A . 
G 4 HOH   14 314 16 HOH   HOH A . 
G 4 HOH   15 315 3  HOH   HOH A . 
G 4 HOH   16 316 43 HOH   HOH A . 
G 4 HOH   17 317 69 HOH   HOH A . 
G 4 HOH   18 318 54 HOH   HOH A . 
G 4 HOH   19 319 13 HOH   HOH A . 
G 4 HOH   20 320 27 HOH   HOH A . 
G 4 HOH   21 321 5  HOH   HOH A . 
G 4 HOH   22 322 6  HOH   HOH A . 
G 4 HOH   23 323 45 HOH   HOH A . 
G 4 HOH   24 324 40 HOH   HOH A . 
G 4 HOH   25 325 20 HOH   HOH A . 
G 4 HOH   26 326 32 HOH   HOH A . 
G 4 HOH   27 327 48 HOH   HOH A . 
G 4 HOH   28 328 22 HOH   HOH A . 
G 4 HOH   29 329 30 HOH   HOH A . 
G 4 HOH   30 330 8  HOH   HOH A . 
G 4 HOH   31 331 10 HOH   HOH A . 
G 4 HOH   32 332 17 HOH   HOH A . 
G 4 HOH   33 333 28 HOH   HOH A . 
G 4 HOH   34 334 15 HOH   HOH A . 
G 4 HOH   35 335 96 HOH   HOH A . 
G 4 HOH   36 336 56 HOH   HOH A . 
G 4 HOH   37 337 41 HOH   HOH A . 
G 4 HOH   38 338 11 HOH   HOH A . 
G 4 HOH   39 339 39 HOH   HOH A . 
G 4 HOH   40 340 83 HOH   HOH A . 
G 4 HOH   41 341 21 HOH   HOH A . 
G 4 HOH   42 342 66 HOH   HOH A . 
G 4 HOH   43 343 42 HOH   HOH A . 
G 4 HOH   44 344 26 HOH   HOH A . 
G 4 HOH   45 345 97 HOH   HOH A . 
G 4 HOH   46 346 87 HOH   HOH A . 
G 4 HOH   47 347 85 HOH   HOH A . 
G 4 HOH   48 348 86 HOH   HOH A . 
G 4 HOH   49 349 46 HOH   HOH A . 
G 4 HOH   50 350 58 HOH   HOH A . 
G 4 HOH   51 351 88 HOH   HOH A . 
G 4 HOH   52 352 93 HOH   HOH A . 
G 4 HOH   53 353 63 HOH   HOH A . 
G 4 HOH   54 354 19 HOH   HOH A . 
G 4 HOH   55 355 72 HOH   HOH A . 
G 4 HOH   56 356 49 HOH   HOH A . 
G 4 HOH   57 357 74 HOH   HOH A . 
G 4 HOH   58 358 64 HOH   HOH A . 
G 4 HOH   59 359 71 HOH   HOH A . 
G 4 HOH   60 360 92 HOH   HOH A . 
H 4 HOH   1  301 62 HOH   HOH B . 
H 4 HOH   2  302 80 HOH   HOH B . 
H 4 HOH   3  303 84 HOH   HOH B . 
H 4 HOH   4  304 89 HOH   HOH B . 
H 4 HOH   5  305 68 HOH   HOH B . 
H 4 HOH   6  306 67 HOH   HOH B . 
H 4 HOH   7  307 34 HOH   HOH B . 
H 4 HOH   8  308 4  HOH   HOH B . 
H 4 HOH   9  309 51 HOH   HOH B . 
H 4 HOH   10 310 60 HOH   HOH B . 
H 4 HOH   11 311 38 HOH   HOH B . 
H 4 HOH   12 312 94 HOH   HOH B . 
H 4 HOH   13 313 9  HOH   HOH B . 
H 4 HOH   14 314 2  HOH   HOH B . 
H 4 HOH   15 315 73 HOH   HOH B . 
H 4 HOH   16 316 55 HOH   HOH B . 
H 4 HOH   17 317 81 HOH   HOH B . 
H 4 HOH   18 318 1  HOH   HOH B . 
H 4 HOH   19 319 35 HOH   HOH B . 
H 4 HOH   20 320 37 HOH   HOH B . 
H 4 HOH   21 321 12 HOH   HOH B . 
H 4 HOH   22 322 23 HOH   HOH B . 
H 4 HOH   23 323 61 HOH   HOH B . 
H 4 HOH   24 324 50 HOH   HOH B . 
H 4 HOH   25 325 52 HOH   HOH B . 
H 4 HOH   26 326 36 HOH   HOH B . 
H 4 HOH   27 327 65 HOH   HOH B . 
H 4 HOH   28 328 98 HOH   HOH B . 
H 4 HOH   29 329 95 HOH   HOH B . 
H 4 HOH   30 330 25 HOH   HOH B . 
H 4 HOH   31 331 91 HOH   HOH B . 
H 4 HOH   32 332 57 HOH   HOH B . 
H 4 HOH   33 333 14 HOH   HOH B . 
H 4 HOH   34 334 82 HOH   HOH B . 
H 4 HOH   35 335 77 HOH   HOH B . 
H 4 HOH   36 336 70 HOH   HOH B . 
H 4 HOH   37 337 44 HOH   HOH B . 
H 4 HOH   38 338 78 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A CYS 10  ? N   ? A CYS 10  N   
2  1 Y 1 A CYS 10  ? CA  ? A CYS 10  CA  
3  1 Y 1 A CYS 10  ? CB  ? A CYS 10  CB  
4  1 Y 1 A CYS 10  ? SG  ? A CYS 10  SG  
5  1 Y 1 A LYS 15  ? NZ  ? A LYS 15  NZ  
6  1 Y 1 A ARG 21  ? CZ  ? A ARG 21  CZ  
7  1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
8  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
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 THR 40  ? CG2 ? A THR 40  CG2 
15 1 Y 1 A GLU 42  ? CG  ? A GLU 42  CG  
16 1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
17 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
18 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
19 1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
20 1 Y 1 A GLU 51  ? CG  ? A GLU 51  CG  
21 1 Y 1 A GLU 51  ? CD  ? A GLU 51  CD  
22 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
23 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
24 1 Y 1 A GLU 61  ? CG  ? A GLU 61  CG  
25 1 Y 1 A GLU 61  ? CD  ? A GLU 61  CD  
26 1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
27 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
28 1 Y 1 A GLU 62  ? OE2 ? A GLU 62  OE2 
29 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
30 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
31 1 Y 1 A SER 100 ? OG  ? A SER 100 OG  
32 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
33 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
34 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
35 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
36 1 Y 1 B ARG 21  ? CG  ? B ARG 21  CG  
37 1 Y 1 B ARG 21  ? CD  ? B ARG 21  CD  
38 1 Y 1 B ARG 21  ? NE  ? B ARG 21  NE  
39 1 Y 1 B ARG 21  ? CZ  ? B ARG 21  CZ  
40 1 Y 1 B ARG 21  ? NH1 ? B ARG 21  NH1 
41 1 Y 1 B ARG 21  ? NH2 ? B ARG 21  NH2 
42 1 Y 1 B ARG 34  ? CZ  ? B ARG 34  CZ  
43 1 Y 1 B ARG 34  ? NH1 ? B ARG 34  NH1 
44 1 Y 1 B ARG 34  ? NH2 ? B ARG 34  NH2 
45 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
46 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
47 1 Y 1 B ASP 39  ? CG  ? B ASP 39  CG  
48 1 Y 1 B ASP 39  ? OD1 ? B ASP 39  OD1 
49 1 Y 1 B ASP 39  ? OD2 ? B ASP 39  OD2 
50 1 Y 1 B THR 40  ? CG2 ? B THR 40  CG2 
51 1 Y 1 B GLU 42  ? CG  ? B GLU 42  CG  
52 1 Y 1 B GLU 42  ? CD  ? B GLU 42  CD  
53 1 Y 1 B GLU 42  ? OE1 ? B GLU 42  OE1 
54 1 Y 1 B GLU 42  ? OE2 ? B GLU 42  OE2 
55 1 Y 1 B LYS 48  ? CG  ? B LYS 48  CG  
56 1 Y 1 B LYS 48  ? CD  ? B LYS 48  CD  
57 1 Y 1 B LYS 48  ? CE  ? B LYS 48  CE  
58 1 Y 1 B LYS 48  ? NZ  ? B LYS 48  NZ  
59 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
60 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
61 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
62 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
63 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
64 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
65 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
66 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
67 1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
68 1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
69 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
70 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
71 1 Y 1 B GLU 63  ? CG  ? B GLU 63  CG  
72 1 Y 1 B GLU 63  ? CD  ? B GLU 63  CD  
73 1 Y 1 B GLU 63  ? OE1 ? B GLU 63  OE1 
74 1 Y 1 B GLU 63  ? OE2 ? B GLU 63  OE2 
75 1 Y 1 B LYS 80  ? NZ  ? B LYS 80  NZ  
76 1 Y 1 B ASN 98  ? CG  ? B ASN 98  CG  
77 1 Y 1 B ASN 98  ? OD1 ? B ASN 98  OD1 
78 1 Y 1 B ASN 98  ? ND2 ? B ASN 98  ND2 
79 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
80 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
81 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
82 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
83 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
84 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                     9H7L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.503 
_cell.length_a_esd                 ? 
_cell.length_b                     84.336 
_cell.length_b_esd                 ? 
_cell.length_c                     65.742 
_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                         9H7L 
_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                   9H7L 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.47 
_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                                       9H7L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.18 
_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                                     77826 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.92 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.8 
_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                                0.025 
_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                              0.051 
_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                                    1.18 
_reflns_shell.d_res_low                                     1.21 
_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                             5235 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.375 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.652 
_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]                            0.05 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.02 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.06 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.203 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.965 
_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                                 9H7L 
_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                            1.18 
_refine.ls_d_res_low                             35.69 
_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                     73851 
_refine.ls_number_reflns_R_free                  3923 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.14 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17261 
_refine.ls_R_factor_R_free                       0.19234 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17154 
_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                       0.036 
_refine.pdbx_overall_ESU_R_Free                  0.036 
_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                             1.152 
_refine.overall_SU_ML                            0.024 
_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                       1.18 
_refine_hist.d_res_low                        35.69 
_refine_hist.number_atoms_solvent             98 
_refine_hist.number_atoms_total               1776 
_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        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.023  0.019  1746 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  1567 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.314  1.954  2397 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.948  3.000  3593 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.015  5.000  227  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.116 23.793 58   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.092 15.000 235  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.418 15.000 2    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.121  0.200  280  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  1968 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  402  ? 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' ? 2.455  1.510  897  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.455  1.510  898  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.767  2.272  1115 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.766  2.272  1116 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.083  1.742  849  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.082  1.742  850  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.575  2.524  1279 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.527  13.412 1933 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.526  13.414 1934 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 7.330  3.000  3312 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 15.468 5.000  25   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 10.024 5.000  3335 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.180 
_refine_ls_shell.d_res_low                        1.211 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             275 
_refine_ls_shell.number_reflns_R_work             5235 
_refine_ls_shell.percent_reflns_obs               96.13 
_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                  0.274 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.309 
# 
_struct.entry_id                     9H7L 
_struct.title                        'Human Transthyretin in Complex with 4-phenyl-1H-pyrazolo[3,4-b]pyridin-3-amine' 
_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        9H7L 
_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 9H7L A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7L B 1 ? 127 ? P02766 21 ? 147 ? 1 127 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H 
1 2 A,B,C,D,E,F,G,H 
# 
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 ? ? ? ? ? ? ? 2.574 ? ? 
metalc2 metalc ? ? A ASP 99 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.530 ? ? 
metalc3 metalc ? ? A ASP 99 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc4 metalc ? ? C CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? A CA  201 A HOH 346 1_555 ? ? ? ? ? ? ? 2.830 ? ? 
metalc5 metalc ? ? C CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? A CA  201 A HOH 347 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc6 metalc ? ? B GLU 66 OE2 ? ? ? 1_555 E CA  . CA ? ? B GLU 66  B CA  201 1_555 ? ? ? ? ? ? ? 2.610 ? ? 
# 
_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_555 100.4 ? 
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 76.1  ? 
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 71.2  ? 
4  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 346 ? 1_555 80.3  ? 
5  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 346 ? 1_555 67.8  ? 
6  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 346 ? 1_555 127.5 ? 
7  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 347 ? 1_555 88.2  ? 
8  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 347 ? 1_555 145.1 ? 
9  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 347 ? 1_555 78.4  ? 
10 O   ? G HOH .  ? A HOH 346 ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? G HOH .  ? A HOH 347 ? 1_555 146.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? VAL B 122 ? SER B 115 VAL B 122 
AA1 6 TYR B 105 ? SER B 112 ? TYR B 105 SER B 112 
AA1 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA1 8 SER B 23  ? PRO B 24  ? SER B 23  PRO B 24  
AA2 1 GLU A 54  ? LEU A 55  ? GLU A 54  LEU A 55  
AA2 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA2 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA2 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA2 5 SER B 115 ? VAL B 122 ? SER B 115 VAL B 122 
AA2 6 TYR B 105 ? SER B 112 ? TYR B 105 SER B 112 
AA2 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA2 8 GLU B 54  ? LEU B 55  ? GLU B 54  LEU B 55  
AA3 1 TRP A 41  ? LYS A 48  ? TRP A 41  LYS A 48  
AA3 2 ALA A 29  ? LYS A 35  ? ALA A 29  LYS A 35  
AA3 3 GLY A 67  ? ILE A 73  ? GLY A 67  ILE A 73  
AA3 4 ALA A 91  ? ALA A 97  ? ALA A 91  ALA A 97  
AA4 1 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
AA4 2 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA4 3 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA4 4 ALA B 91  ? ALA B 97  ? ALA B 91  ALA B 97  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA1 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA1 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA1 5 6 O VAL B 121 ? O VAL B 121 N THR B 106 ? N THR B 106 
AA1 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA2 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA2 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA2 5 6 O VAL B 121 ? O VAL B 121 N THR B 106 ? N THR B 106 
AA2 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N ILE A 73  ? N ILE A 73  O ALA A 91  ? O ALA A 91  
AA4 1 2 O ALA B 45  ? O ALA B 45  N VAL B 32  ? N VAL B 32  
AA4 2 3 N HIS B 31  ? N HIS B 31  O GLU B 72  ? O GLU B 72  
AA4 3 4 N GLY B 67  ? N GLY B 67  O ALA B 97  ? O ALA B 97  
# 
_pdbx_entry_details.entry_id                   9H7L 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CA A CA  201 ? ? O A HOH 301 ? ? 1.69 
2 1 O  A ASP 99  ? ? O A HOH 301 ? ? 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD  A GLU 63  ? A OE2 A GLU 63  ? A 1.173 1.252 -0.079 0.011 N 
2 1 CD  B GLU 54  ? ? OE1 B GLU 54  ? ? 1.183 1.252 -0.069 0.011 N 
3 1 CE1 B TYR 116 ? ? CZ  B TYR 116 ? ? 1.289 1.381 -0.092 0.013 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB  B ALA 45 ? ? CA B ALA 45 ? ? C   B ALA 45 ? ? 120.24 110.10 10.14 1.50 N 
2 1 OE1 B GLU 66 ? ? CD B GLU 66 ? ? OE2 B GLU 66 ? ? 115.57 123.30 -7.73 1.20 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 A1IS0 202 ? D A1IS0 . 
2 1 B A1IS0 202 ? F A1IS0 . 
3 1 B A1IS0 202 ? F A1IS0 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A THR 3   ? A THR 3   
4  1 Y 1 A GLY 4   ? A GLY 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A LYS 9   ? A LYS 9   
10 1 Y 1 A PRO 125 ? A PRO 125 
11 1 Y 1 A LYS 126 ? A LYS 126 
12 1 Y 1 A GLU 127 ? A GLU 127 
13 1 Y 1 B GLY 1   ? B GLY 1   
14 1 Y 1 B PRO 2   ? B PRO 2   
15 1 Y 1 B THR 3   ? B THR 3   
16 1 Y 1 B GLY 4   ? B GLY 4   
17 1 Y 1 B THR 5   ? B THR 5   
18 1 Y 1 B GLY 6   ? B GLY 6   
19 1 Y 1 B GLU 7   ? B GLU 7   
20 1 Y 1 B SER 8   ? B SER 8   
21 1 Y 1 B LYS 9   ? B LYS 9   
22 1 Y 1 B CYS 10  ? B CYS 10  
23 1 Y 1 B ASP 99  ? B ASP 99  
24 1 Y 1 B SER 100 ? B SER 100 
25 1 Y 1 B GLY 101 ? B GLY 101 
26 1 Y 1 B PRO 102 ? B PRO 102 
27 1 Y 1 B ARG 103 ? B ARG 103 
28 1 Y 1 B ASN 124 ? B ASN 124 
29 1 Y 1 B PRO 125 ? B PRO 125 
30 1 Y 1 B LYS 126 ? B LYS 126 
31 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 
A1IS0 C5   C  Y N 1   
A1IS0 C6   C  Y N 2   
A1IS0 C4   C  Y N 3   
A1IS0 C3   C  Y N 4   
A1IS0 C2   C  Y N 5   
A1IS0 C1   C  Y N 6   
A1IS0 C9   C  Y N 7   
A1IS0 C11  C  Y N 8   
A1IS0 C10  C  Y N 9   
A1IS0 N3   N  N N 10  
A1IS0 N1   N  Y N 11  
A1IS0 N2   N  Y N 12  
A1IS0 N    N  Y N 13  
A1IS0 C    C  Y N 14  
A1IS0 C8   C  Y N 15  
A1IS0 C7   C  Y N 16  
A1IS0 H1   H  N N 17  
A1IS0 H2   H  N N 18  
A1IS0 H3   H  N N 19  
A1IS0 H4   H  N N 20  
A1IS0 H5   H  N N 21  
A1IS0 H6   H  N N 22  
A1IS0 H7   H  N N 23  
A1IS0 H8   H  N N 24  
A1IS0 H9   H  N N 25  
A1IS0 H10  H  N N 26  
ALA   N    N  N N 27  
ALA   CA   C  N S 28  
ALA   C    C  N N 29  
ALA   O    O  N N 30  
ALA   CB   C  N N 31  
ALA   OXT  O  N N 32  
ALA   H    H  N N 33  
ALA   H2   H  N N 34  
ALA   HA   H  N N 35  
ALA   HB1  H  N N 36  
ALA   HB2  H  N N 37  
ALA   HB3  H  N N 38  
ALA   HXT  H  N N 39  
ARG   N    N  N N 40  
ARG   CA   C  N S 41  
ARG   C    C  N N 42  
ARG   O    O  N N 43  
ARG   CB   C  N N 44  
ARG   CG   C  N N 45  
ARG   CD   C  N N 46  
ARG   NE   N  N N 47  
ARG   CZ   C  N N 48  
ARG   NH1  N  N N 49  
ARG   NH2  N  N N 50  
ARG   OXT  O  N N 51  
ARG   H    H  N N 52  
ARG   H2   H  N N 53  
ARG   HA   H  N N 54  
ARG   HB2  H  N N 55  
ARG   HB3  H  N N 56  
ARG   HG2  H  N N 57  
ARG   HG3  H  N N 58  
ARG   HD2  H  N N 59  
ARG   HD3  H  N N 60  
ARG   HE   H  N N 61  
ARG   HH11 H  N N 62  
ARG   HH12 H  N N 63  
ARG   HH21 H  N N 64  
ARG   HH22 H  N N 65  
ARG   HXT  H  N N 66  
ASN   N    N  N N 67  
ASN   CA   C  N S 68  
ASN   C    C  N N 69  
ASN   O    O  N N 70  
ASN   CB   C  N N 71  
ASN   CG   C  N N 72  
ASN   OD1  O  N N 73  
ASN   ND2  N  N N 74  
ASN   OXT  O  N N 75  
ASN   H    H  N N 76  
ASN   H2   H  N N 77  
ASN   HA   H  N N 78  
ASN   HB2  H  N N 79  
ASN   HB3  H  N N 80  
ASN   HD21 H  N N 81  
ASN   HD22 H  N N 82  
ASN   HXT  H  N N 83  
ASP   N    N  N N 84  
ASP   CA   C  N S 85  
ASP   C    C  N N 86  
ASP   O    O  N N 87  
ASP   CB   C  N N 88  
ASP   CG   C  N N 89  
ASP   OD1  O  N N 90  
ASP   OD2  O  N N 91  
ASP   OXT  O  N N 92  
ASP   H    H  N N 93  
ASP   H2   H  N N 94  
ASP   HA   H  N N 95  
ASP   HB2  H  N N 96  
ASP   HB3  H  N N 97  
ASP   HD2  H  N N 98  
ASP   HXT  H  N N 99  
CA    CA   CA N N 100 
CYS   N    N  N N 101 
CYS   CA   C  N R 102 
CYS   C    C  N N 103 
CYS   O    O  N N 104 
CYS   CB   C  N N 105 
CYS   SG   S  N N 106 
CYS   OXT  O  N N 107 
CYS   H    H  N N 108 
CYS   H2   H  N N 109 
CYS   HA   H  N N 110 
CYS   HB2  H  N N 111 
CYS   HB3  H  N N 112 
CYS   HG   H  N N 113 
CYS   HXT  H  N N 114 
GLU   N    N  N N 115 
GLU   CA   C  N S 116 
GLU   C    C  N N 117 
GLU   O    O  N N 118 
GLU   CB   C  N N 119 
GLU   CG   C  N N 120 
GLU   CD   C  N N 121 
GLU   OE1  O  N N 122 
GLU   OE2  O  N N 123 
GLU   OXT  O  N N 124 
GLU   H    H  N N 125 
GLU   H2   H  N N 126 
GLU   HA   H  N N 127 
GLU   HB2  H  N N 128 
GLU   HB3  H  N N 129 
GLU   HG2  H  N N 130 
GLU   HG3  H  N N 131 
GLU   HE2  H  N N 132 
GLU   HXT  H  N N 133 
GLY   N    N  N N 134 
GLY   CA   C  N N 135 
GLY   C    C  N N 136 
GLY   O    O  N N 137 
GLY   OXT  O  N N 138 
GLY   H    H  N N 139 
GLY   H2   H  N N 140 
GLY   HA2  H  N N 141 
GLY   HA3  H  N N 142 
GLY   HXT  H  N N 143 
HIS   N    N  N N 144 
HIS   CA   C  N S 145 
HIS   C    C  N N 146 
HIS   O    O  N N 147 
HIS   CB   C  N N 148 
HIS   CG   C  Y N 149 
HIS   ND1  N  Y N 150 
HIS   CD2  C  Y N 151 
HIS   CE1  C  Y N 152 
HIS   NE2  N  Y N 153 
HIS   OXT  O  N N 154 
HIS   H    H  N N 155 
HIS   H2   H  N N 156 
HIS   HA   H  N N 157 
HIS   HB2  H  N N 158 
HIS   HB3  H  N N 159 
HIS   HD1  H  N N 160 
HIS   HD2  H  N N 161 
HIS   HE1  H  N N 162 
HIS   HE2  H  N N 163 
HIS   HXT  H  N N 164 
HOH   O    O  N N 165 
HOH   H1   H  N N 166 
HOH   H2   H  N N 167 
ILE   N    N  N N 168 
ILE   CA   C  N S 169 
ILE   C    C  N N 170 
ILE   O    O  N N 171 
ILE   CB   C  N S 172 
ILE   CG1  C  N N 173 
ILE   CG2  C  N N 174 
ILE   CD1  C  N N 175 
ILE   OXT  O  N N 176 
ILE   H    H  N N 177 
ILE   H2   H  N N 178 
ILE   HA   H  N N 179 
ILE   HB   H  N N 180 
ILE   HG12 H  N N 181 
ILE   HG13 H  N N 182 
ILE   HG21 H  N N 183 
ILE   HG22 H  N N 184 
ILE   HG23 H  N N 185 
ILE   HD11 H  N N 186 
ILE   HD12 H  N N 187 
ILE   HD13 H  N N 188 
ILE   HXT  H  N N 189 
LEU   N    N  N N 190 
LEU   CA   C  N S 191 
LEU   C    C  N N 192 
LEU   O    O  N N 193 
LEU   CB   C  N N 194 
LEU   CG   C  N N 195 
LEU   CD1  C  N N 196 
LEU   CD2  C  N N 197 
LEU   OXT  O  N N 198 
LEU   H    H  N N 199 
LEU   H2   H  N N 200 
LEU   HA   H  N N 201 
LEU   HB2  H  N N 202 
LEU   HB3  H  N N 203 
LEU   HG   H  N N 204 
LEU   HD11 H  N N 205 
LEU   HD12 H  N N 206 
LEU   HD13 H  N N 207 
LEU   HD21 H  N N 208 
LEU   HD22 H  N N 209 
LEU   HD23 H  N N 210 
LEU   HXT  H  N N 211 
LYS   N    N  N N 212 
LYS   CA   C  N S 213 
LYS   C    C  N N 214 
LYS   O    O  N N 215 
LYS   CB   C  N N 216 
LYS   CG   C  N N 217 
LYS   CD   C  N N 218 
LYS   CE   C  N N 219 
LYS   NZ   N  N N 220 
LYS   OXT  O  N N 221 
LYS   H    H  N N 222 
LYS   H2   H  N N 223 
LYS   HA   H  N N 224 
LYS   HB2  H  N N 225 
LYS   HB3  H  N N 226 
LYS   HG2  H  N N 227 
LYS   HG3  H  N N 228 
LYS   HD2  H  N N 229 
LYS   HD3  H  N N 230 
LYS   HE2  H  N N 231 
LYS   HE3  H  N N 232 
LYS   HZ1  H  N N 233 
LYS   HZ2  H  N N 234 
LYS   HZ3  H  N N 235 
LYS   HXT  H  N N 236 
MET   N    N  N N 237 
MET   CA   C  N S 238 
MET   C    C  N N 239 
MET   O    O  N N 240 
MET   CB   C  N N 241 
MET   CG   C  N N 242 
MET   SD   S  N N 243 
MET   CE   C  N N 244 
MET   OXT  O  N N 245 
MET   H    H  N N 246 
MET   H2   H  N N 247 
MET   HA   H  N N 248 
MET   HB2  H  N N 249 
MET   HB3  H  N N 250 
MET   HG2  H  N N 251 
MET   HG3  H  N N 252 
MET   HE1  H  N N 253 
MET   HE2  H  N N 254 
MET   HE3  H  N N 255 
MET   HXT  H  N N 256 
PHE   N    N  N N 257 
PHE   CA   C  N S 258 
PHE   C    C  N N 259 
PHE   O    O  N N 260 
PHE   CB   C  N N 261 
PHE   CG   C  Y N 262 
PHE   CD1  C  Y N 263 
PHE   CD2  C  Y N 264 
PHE   CE1  C  Y N 265 
PHE   CE2  C  Y N 266 
PHE   CZ   C  Y N 267 
PHE   OXT  O  N N 268 
PHE   H    H  N N 269 
PHE   H2   H  N N 270 
PHE   HA   H  N N 271 
PHE   HB2  H  N N 272 
PHE   HB3  H  N N 273 
PHE   HD1  H  N N 274 
PHE   HD2  H  N N 275 
PHE   HE1  H  N N 276 
PHE   HE2  H  N N 277 
PHE   HZ   H  N N 278 
PHE   HXT  H  N N 279 
PRO   N    N  N N 280 
PRO   CA   C  N S 281 
PRO   C    C  N N 282 
PRO   O    O  N N 283 
PRO   CB   C  N N 284 
PRO   CG   C  N N 285 
PRO   CD   C  N N 286 
PRO   OXT  O  N N 287 
PRO   H    H  N N 288 
PRO   HA   H  N N 289 
PRO   HB2  H  N N 290 
PRO   HB3  H  N N 291 
PRO   HG2  H  N N 292 
PRO   HG3  H  N N 293 
PRO   HD2  H  N N 294 
PRO   HD3  H  N N 295 
PRO   HXT  H  N N 296 
SER   N    N  N N 297 
SER   CA   C  N S 298 
SER   C    C  N N 299 
SER   O    O  N N 300 
SER   CB   C  N N 301 
SER   OG   O  N N 302 
SER   OXT  O  N N 303 
SER   H    H  N N 304 
SER   H2   H  N N 305 
SER   HA   H  N N 306 
SER   HB2  H  N N 307 
SER   HB3  H  N N 308 
SER   HG   H  N N 309 
SER   HXT  H  N N 310 
THR   N    N  N N 311 
THR   CA   C  N S 312 
THR   C    C  N N 313 
THR   O    O  N N 314 
THR   CB   C  N R 315 
THR   OG1  O  N N 316 
THR   CG2  C  N N 317 
THR   OXT  O  N N 318 
THR   H    H  N N 319 
THR   H2   H  N N 320 
THR   HA   H  N N 321 
THR   HB   H  N N 322 
THR   HG1  H  N N 323 
THR   HG21 H  N N 324 
THR   HG22 H  N N 325 
THR   HG23 H  N N 326 
THR   HXT  H  N N 327 
TRP   N    N  N N 328 
TRP   CA   C  N S 329 
TRP   C    C  N N 330 
TRP   O    O  N N 331 
TRP   CB   C  N N 332 
TRP   CG   C  Y N 333 
TRP   CD1  C  Y N 334 
TRP   CD2  C  Y N 335 
TRP   NE1  N  Y N 336 
TRP   CE2  C  Y N 337 
TRP   CE3  C  Y N 338 
TRP   CZ2  C  Y N 339 
TRP   CZ3  C  Y N 340 
TRP   CH2  C  Y N 341 
TRP   OXT  O  N N 342 
TRP   H    H  N N 343 
TRP   H2   H  N N 344 
TRP   HA   H  N N 345 
TRP   HB2  H  N N 346 
TRP   HB3  H  N N 347 
TRP   HD1  H  N N 348 
TRP   HE1  H  N N 349 
TRP   HE3  H  N N 350 
TRP   HZ2  H  N N 351 
TRP   HZ3  H  N N 352 
TRP   HH2  H  N N 353 
TRP   HXT  H  N N 354 
TYR   N    N  N N 355 
TYR   CA   C  N S 356 
TYR   C    C  N N 357 
TYR   O    O  N N 358 
TYR   CB   C  N N 359 
TYR   CG   C  Y N 360 
TYR   CD1  C  Y N 361 
TYR   CD2  C  Y N 362 
TYR   CE1  C  Y N 363 
TYR   CE2  C  Y N 364 
TYR   CZ   C  Y N 365 
TYR   OH   O  N N 366 
TYR   OXT  O  N N 367 
TYR   H    H  N N 368 
TYR   H2   H  N N 369 
TYR   HA   H  N N 370 
TYR   HB2  H  N N 371 
TYR   HB3  H  N N 372 
TYR   HD1  H  N N 373 
TYR   HD2  H  N N 374 
TYR   HE1  H  N N 375 
TYR   HE2  H  N N 376 
TYR   HH   H  N N 377 
TYR   HXT  H  N N 378 
VAL   N    N  N N 379 
VAL   CA   C  N S 380 
VAL   C    C  N N 381 
VAL   O    O  N N 382 
VAL   CB   C  N N 383 
VAL   CG1  C  N N 384 
VAL   CG2  C  N N 385 
VAL   OXT  O  N N 386 
VAL   H    H  N N 387 
VAL   H2   H  N N 388 
VAL   HA   H  N N 389 
VAL   HB   H  N N 390 
VAL   HG11 H  N N 391 
VAL   HG12 H  N N 392 
VAL   HG13 H  N N 393 
VAL   HG21 H  N N 394 
VAL   HG22 H  N N 395 
VAL   HG23 H  N N 396 
VAL   HXT  H  N N 397 
# 
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 
A1IS0 N2  N1   sing Y N 1   
A1IS0 N2  C1   doub Y N 2   
A1IS0 N1  C11  sing Y N 3   
A1IS0 N   C1   sing Y N 4   
A1IS0 N   C    doub Y N 5   
A1IS0 C1  C2   sing Y N 6   
A1IS0 C11 C2   doub Y N 7   
A1IS0 C11 N3   sing N N 8   
A1IS0 C   C4   sing Y N 9   
A1IS0 C2  C3   sing Y N 10  
A1IS0 C4  C3   doub Y N 11  
A1IS0 C3  C5   sing N N 12  
A1IS0 C5  C6   doub Y N 13  
A1IS0 C5  C10  sing Y N 14  
A1IS0 C6  C7   sing Y N 15  
A1IS0 C10 C9   doub Y N 16  
A1IS0 C7  C8   doub Y N 17  
A1IS0 C9  C8   sing Y N 18  
A1IS0 C6  H1   sing N N 19  
A1IS0 C4  H2   sing N N 20  
A1IS0 C9  H3   sing N N 21  
A1IS0 C10 H4   sing N N 22  
A1IS0 N3  H5   sing N N 23  
A1IS0 N3  H6   sing N N 24  
A1IS0 N1  H7   sing N N 25  
A1IS0 C   H8   sing N N 26  
A1IS0 C8  H9   sing N N 27  
A1IS0 C7  H10  sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
GLU   N   CA   sing N N 111 
GLU   N   H    sing N N 112 
GLU   N   H2   sing N N 113 
GLU   CA  C    sing N N 114 
GLU   CA  CB   sing N N 115 
GLU   CA  HA   sing N N 116 
GLU   C   O    doub N N 117 
GLU   C   OXT  sing N N 118 
GLU   CB  CG   sing N N 119 
GLU   CB  HB2  sing N N 120 
GLU   CB  HB3  sing N N 121 
GLU   CG  CD   sing N N 122 
GLU   CG  HG2  sing N N 123 
GLU   CG  HG3  sing N N 124 
GLU   CD  OE1  doub N N 125 
GLU   CD  OE2  sing N N 126 
GLU   OE2 HE2  sing N N 127 
GLU   OXT HXT  sing N N 128 
GLY   N   CA   sing N N 129 
GLY   N   H    sing N N 130 
GLY   N   H2   sing N N 131 
GLY   CA  C    sing N N 132 
GLY   CA  HA2  sing N N 133 
GLY   CA  HA3  sing N N 134 
GLY   C   O    doub N N 135 
GLY   C   OXT  sing N N 136 
GLY   OXT HXT  sing N N 137 
HIS   N   CA   sing N N 138 
HIS   N   H    sing N N 139 
HIS   N   H2   sing N N 140 
HIS   CA  C    sing N N 141 
HIS   CA  CB   sing N N 142 
HIS   CA  HA   sing N N 143 
HIS   C   O    doub N N 144 
HIS   C   OXT  sing N N 145 
HIS   CB  CG   sing N N 146 
HIS   CB  HB2  sing N N 147 
HIS   CB  HB3  sing N N 148 
HIS   CG  ND1  sing Y N 149 
HIS   CG  CD2  doub Y N 150 
HIS   ND1 CE1  doub Y N 151 
HIS   ND1 HD1  sing N N 152 
HIS   CD2 NE2  sing Y N 153 
HIS   CD2 HD2  sing N N 154 
HIS   CE1 NE2  sing Y N 155 
HIS   CE1 HE1  sing N N 156 
HIS   NE2 HE2  sing N N 157 
HIS   OXT HXT  sing N N 158 
HOH   O   H1   sing N N 159 
HOH   O   H2   sing N N 160 
ILE   N   CA   sing N N 161 
ILE   N   H    sing N N 162 
ILE   N   H2   sing N N 163 
ILE   CA  C    sing N N 164 
ILE   CA  CB   sing N N 165 
ILE   CA  HA   sing N N 166 
ILE   C   O    doub N N 167 
ILE   C   OXT  sing N N 168 
ILE   CB  CG1  sing N N 169 
ILE   CB  CG2  sing N N 170 
ILE   CB  HB   sing N N 171 
ILE   CG1 CD1  sing N N 172 
ILE   CG1 HG12 sing N N 173 
ILE   CG1 HG13 sing N N 174 
ILE   CG2 HG21 sing N N 175 
ILE   CG2 HG22 sing N N 176 
ILE   CG2 HG23 sing N N 177 
ILE   CD1 HD11 sing N N 178 
ILE   CD1 HD12 sing N N 179 
ILE   CD1 HD13 sing N N 180 
ILE   OXT HXT  sing N N 181 
LEU   N   CA   sing N N 182 
LEU   N   H    sing N N 183 
LEU   N   H2   sing N N 184 
LEU   CA  C    sing N N 185 
LEU   CA  CB   sing N N 186 
LEU   CA  HA   sing N N 187 
LEU   C   O    doub N N 188 
LEU   C   OXT  sing N N 189 
LEU   CB  CG   sing N N 190 
LEU   CB  HB2  sing N N 191 
LEU   CB  HB3  sing N N 192 
LEU   CG  CD1  sing N N 193 
LEU   CG  CD2  sing N N 194 
LEU   CG  HG   sing N N 195 
LEU   CD1 HD11 sing N N 196 
LEU   CD1 HD12 sing N N 197 
LEU   CD1 HD13 sing N N 198 
LEU   CD2 HD21 sing N N 199 
LEU   CD2 HD22 sing N N 200 
LEU   CD2 HD23 sing N N 201 
LEU   OXT HXT  sing N N 202 
LYS   N   CA   sing N N 203 
LYS   N   H    sing N N 204 
LYS   N   H2   sing N N 205 
LYS   CA  C    sing N N 206 
LYS   CA  CB   sing N N 207 
LYS   CA  HA   sing N N 208 
LYS   C   O    doub N N 209 
LYS   C   OXT  sing N N 210 
LYS   CB  CG   sing N N 211 
LYS   CB  HB2  sing N N 212 
LYS   CB  HB3  sing N N 213 
LYS   CG  CD   sing N N 214 
LYS   CG  HG2  sing N N 215 
LYS   CG  HG3  sing N N 216 
LYS   CD  CE   sing N N 217 
LYS   CD  HD2  sing N N 218 
LYS   CD  HD3  sing N N 219 
LYS   CE  NZ   sing N N 220 
LYS   CE  HE2  sing N N 221 
LYS   CE  HE3  sing N N 222 
LYS   NZ  HZ1  sing N N 223 
LYS   NZ  HZ2  sing N N 224 
LYS   NZ  HZ3  sing N N 225 
LYS   OXT HXT  sing N N 226 
MET   N   CA   sing N N 227 
MET   N   H    sing N N 228 
MET   N   H2   sing N N 229 
MET   CA  C    sing N N 230 
MET   CA  CB   sing N N 231 
MET   CA  HA   sing N N 232 
MET   C   O    doub N N 233 
MET   C   OXT  sing N N 234 
MET   CB  CG   sing N N 235 
MET   CB  HB2  sing N N 236 
MET   CB  HB3  sing N N 237 
MET   CG  SD   sing N N 238 
MET   CG  HG2  sing N N 239 
MET   CG  HG3  sing N N 240 
MET   SD  CE   sing N N 241 
MET   CE  HE1  sing N N 242 
MET   CE  HE2  sing N N 243 
MET   CE  HE3  sing N N 244 
MET   OXT HXT  sing N N 245 
PHE   N   CA   sing N N 246 
PHE   N   H    sing N N 247 
PHE   N   H2   sing N N 248 
PHE   CA  C    sing N N 249 
PHE   CA  CB   sing N N 250 
PHE   CA  HA   sing N N 251 
PHE   C   O    doub N N 252 
PHE   C   OXT  sing N N 253 
PHE   CB  CG   sing N N 254 
PHE   CB  HB2  sing N N 255 
PHE   CB  HB3  sing N N 256 
PHE   CG  CD1  doub Y N 257 
PHE   CG  CD2  sing Y N 258 
PHE   CD1 CE1  sing Y N 259 
PHE   CD1 HD1  sing N N 260 
PHE   CD2 CE2  doub Y N 261 
PHE   CD2 HD2  sing N N 262 
PHE   CE1 CZ   doub Y N 263 
PHE   CE1 HE1  sing N N 264 
PHE   CE2 CZ   sing Y N 265 
PHE   CE2 HE2  sing N N 266 
PHE   CZ  HZ   sing N N 267 
PHE   OXT HXT  sing N N 268 
PRO   N   CA   sing N N 269 
PRO   N   CD   sing N N 270 
PRO   N   H    sing N N 271 
PRO   CA  C    sing N N 272 
PRO   CA  CB   sing N N 273 
PRO   CA  HA   sing N N 274 
PRO   C   O    doub N N 275 
PRO   C   OXT  sing N N 276 
PRO   CB  CG   sing N N 277 
PRO   CB  HB2  sing N N 278 
PRO   CB  HB3  sing N N 279 
PRO   CG  CD   sing N N 280 
PRO   CG  HG2  sing N N 281 
PRO   CG  HG3  sing N N 282 
PRO   CD  HD2  sing N N 283 
PRO   CD  HD3  sing N N 284 
PRO   OXT HXT  sing N N 285 
SER   N   CA   sing N N 286 
SER   N   H    sing N N 287 
SER   N   H2   sing N N 288 
SER   CA  C    sing N N 289 
SER   CA  CB   sing N N 290 
SER   CA  HA   sing N N 291 
SER   C   O    doub N N 292 
SER   C   OXT  sing N N 293 
SER   CB  OG   sing N N 294 
SER   CB  HB2  sing N N 295 
SER   CB  HB3  sing N N 296 
SER   OG  HG   sing N N 297 
SER   OXT HXT  sing N N 298 
THR   N   CA   sing N N 299 
THR   N   H    sing N N 300 
THR   N   H2   sing N N 301 
THR   CA  C    sing N N 302 
THR   CA  CB   sing N N 303 
THR   CA  HA   sing N N 304 
THR   C   O    doub N N 305 
THR   C   OXT  sing N N 306 
THR   CB  OG1  sing N N 307 
THR   CB  CG2  sing N N 308 
THR   CB  HB   sing N N 309 
THR   OG1 HG1  sing N N 310 
THR   CG2 HG21 sing N N 311 
THR   CG2 HG22 sing N N 312 
THR   CG2 HG23 sing N N 313 
THR   OXT HXT  sing N N 314 
TRP   N   CA   sing N N 315 
TRP   N   H    sing N N 316 
TRP   N   H2   sing N N 317 
TRP   CA  C    sing N N 318 
TRP   CA  CB   sing N N 319 
TRP   CA  HA   sing N N 320 
TRP   C   O    doub N N 321 
TRP   C   OXT  sing N N 322 
TRP   CB  CG   sing N N 323 
TRP   CB  HB2  sing N N 324 
TRP   CB  HB3  sing N N 325 
TRP   CG  CD1  doub Y N 326 
TRP   CG  CD2  sing Y N 327 
TRP   CD1 NE1  sing Y N 328 
TRP   CD1 HD1  sing N N 329 
TRP   CD2 CE2  doub Y N 330 
TRP   CD2 CE3  sing Y N 331 
TRP   NE1 CE2  sing Y N 332 
TRP   NE1 HE1  sing N N 333 
TRP   CE2 CZ2  sing Y N 334 
TRP   CE3 CZ3  doub Y N 335 
TRP   CE3 HE3  sing N N 336 
TRP   CZ2 CH2  doub Y N 337 
TRP   CZ2 HZ2  sing N N 338 
TRP   CZ3 CH2  sing Y N 339 
TRP   CZ3 HZ3  sing N N 340 
TRP   CH2 HH2  sing N N 341 
TRP   OXT HXT  sing N N 342 
TYR   N   CA   sing N N 343 
TYR   N   H    sing N N 344 
TYR   N   H2   sing N N 345 
TYR   CA  C    sing N N 346 
TYR   CA  CB   sing N N 347 
TYR   CA  HA   sing N N 348 
TYR   C   O    doub N N 349 
TYR   C   OXT  sing N N 350 
TYR   CB  CG   sing N N 351 
TYR   CB  HB2  sing N N 352 
TYR   CB  HB3  sing N N 353 
TYR   CG  CD1  doub Y N 354 
TYR   CG  CD2  sing Y N 355 
TYR   CD1 CE1  sing Y N 356 
TYR   CD1 HD1  sing N N 357 
TYR   CD2 CE2  doub Y N 358 
TYR   CD2 HD2  sing N N 359 
TYR   CE1 CZ   doub Y N 360 
TYR   CE1 HE1  sing N N 361 
TYR   CE2 CZ   sing Y N 362 
TYR   CE2 HE2  sing N N 363 
TYR   CZ  OH   sing N N 364 
TYR   OH  HH   sing N N 365 
TYR   OXT HXT  sing N N 366 
VAL   N   CA   sing N N 367 
VAL   N   H    sing N N 368 
VAL   N   H2   sing N N 369 
VAL   CA  C    sing N N 370 
VAL   CA  CB   sing N N 371 
VAL   CA  HA   sing N N 372 
VAL   C   O    doub N N 373 
VAL   C   OXT  sing N N 374 
VAL   CB  CG1  sing N N 375 
VAL   CB  CG2  sing N N 376 
VAL   CB  HB   sing N N 377 
VAL   CG1 HG11 sing N N 378 
VAL   CG1 HG12 sing N N 379 
VAL   CG1 HG13 sing N N 380 
VAL   CG2 HG21 sing N N 381 
VAL   CG2 HG22 sing N N 382 
VAL   CG2 HG23 sing N N 383 
VAL   OXT HXT  sing N N 384 
# 
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                    9H7L 
_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]   0.023528 
_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]   0.011857 
_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]   0.015211 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    C  C   . CYS   A 1 10  ? 6.852   11.228 -4.879  1.00 28.95 ? 10  CYS   A C   1 
ATOM   2    O  O   . CYS   A 1 10  ? 7.001   10.185 -4.357  1.00 34.33 ? 10  CYS   A O   1 
ATOM   3    N  N   . PRO   A 1 11  ? 7.485   12.332 -4.426  1.00 18.64 ? 11  PRO   A N   1 
ATOM   4    C  CA  . PRO   A 1 11  ? 8.328   12.179 -3.283  1.00 15.66 ? 11  PRO   A CA  1 
ATOM   5    C  C   . PRO   A 1 11  ? 7.680   12.156 -1.919  1.00 13.11 ? 11  PRO   A C   1 
ATOM   6    O  O   . PRO   A 1 11  ? 8.368   11.816 -0.967  1.00 14.00 ? 11  PRO   A O   1 
ATOM   7    C  CB  . PRO   A 1 11  ? 9.325   13.275 -3.409  1.00 20.75 ? 11  PRO   A CB  1 
ATOM   8    C  CG  . PRO   A 1 11  ? 8.518   14.263 -3.967  1.00 23.23 ? 11  PRO   A CG  1 
ATOM   9    C  CD  . PRO   A 1 11  ? 7.685   13.654 -5.021  1.00 20.68 ? 11  PRO   A CD  1 
ATOM   10   N  N   . LEU   A 1 12  ? 6.417   12.458 -1.816  1.00 12.89 ? 12  LEU   A N   1 
ATOM   11   C  CA  . LEU   A 1 12  ? 5.725   12.425 -0.557  1.00 12.52 ? 12  LEU   A CA  1 
ATOM   12   C  C   . LEU   A 1 12  ? 4.314   11.855 -0.775  1.00 13.09 ? 12  LEU   A C   1 
ATOM   13   O  O   . LEU   A 1 12  ? 3.560   12.427 -1.551  1.00 18.24 ? 12  LEU   A O   1 
ATOM   14   C  CB  . LEU   A 1 12  ? 5.615   13.849 0.040   1.00 14.79 ? 12  LEU   A CB  1 
ATOM   15   C  CG  . LEU   A 1 12  ? 4.917   13.957 1.390   1.00 14.35 ? 12  LEU   A CG  1 
ATOM   16   C  CD1 . LEU   A 1 12  ? 5.579   13.146 2.468   1.00 14.87 ? 12  LEU   A CD1 1 
ATOM   17   C  CD2 . LEU   A 1 12  ? 4.798   15.446 1.756   1.00 17.31 ? 12  LEU   A CD2 1 
ATOM   18   N  N   . MET   A 1 13  ? 3.987   10.732 -0.124  1.00 11.40 ? 13  MET   A N   1 
ATOM   19   C  CA  . MET   A 1 13  ? 2.702   10.069 -0.291  1.00 12.55 ? 13  MET   A CA  1 
ATOM   20   C  C   . MET   A 1 13  ? 2.172   9.773  1.110   1.00 10.02 ? 13  MET   A C   1 
ATOM   21   O  O   . MET   A 1 13  ? 2.957   9.518  1.999   1.00 11.61 ? 13  MET   A O   1 
ATOM   22   C  CB  . MET   A 1 13  ? 2.830   8.744  -1.063  1.00 16.83 ? 13  MET   A CB  1 
ATOM   23   C  CG  . MET   A 1 13  ? 1.482   8.116  -1.522  0.50 16.03 ? 13  MET   A CG  1 
ATOM   24   S  SD  . MET   A 1 13  ? 0.757   6.905  -0.364  0.50 17.61 ? 13  MET   A SD  1 
ATOM   25   C  CE  . MET   A 1 13  ? 1.676   5.448  -0.820  0.50 24.04 ? 13  MET   A CE  1 
ATOM   26   N  N   . VAL   A 1 14  ? 0.874   9.806  1.235   1.00 10.27 ? 14  VAL   A N   1 
ATOM   27   C  CA  . VAL   A 1 14  ? 0.219   9.479  2.505   1.00 10.05 ? 14  VAL   A CA  1 
ATOM   28   C  C   . VAL   A 1 14  ? -0.847  8.394  2.267   1.00 11.50 ? 14  VAL   A C   1 
ATOM   29   O  O   . VAL   A 1 14  ? -1.560  8.472  1.312   1.00 13.39 ? 14  VAL   A O   1 
ATOM   30   C  CB  . VAL   A 1 14  ? -0.408  10.741 3.166   1.00 11.61 ? 14  VAL   A CB  1 
ATOM   31   C  CG1 . VAL   A 1 14  ? -1.070  10.381 4.466   1.00 13.60 ? 14  VAL   A CG1 1 
ATOM   32   C  CG2 . VAL   A 1 14  ? 0.664   11.822 3.345   1.00 11.77 ? 14  VAL   A CG2 1 
ATOM   33   N  N   . LYS   A 1 15  ? -0.889  7.400  3.131   1.00 10.68 ? 15  LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 15  ? -1.836  6.301  3.013   1.00 12.10 ? 15  LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 15  ? -2.488  6.122  4.348   1.00 11.16 ? 15  LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 15  ? -1.780  6.071  5.366   1.00 13.23 ? 15  LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 15  ? -1.152  5.056  2.601   1.00 14.67 ? 15  LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 15  ? -2.242  4.021  2.387   1.00 22.16 ? 15  LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 15  ? -1.745  2.751  1.765   1.00 28.70 ? 15  LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 15  ? -2.962  1.877  1.438   1.00 24.09 ? 15  LYS   A CE  1 
ATOM   41   N  N   . VAL   A 1 16  ? -3.800  6.017  4.382   1.00 10.69 ? 16  VAL   A N   1 
ATOM   42   C  CA  . VAL   A 1 16  ? -4.522  5.953  5.661   1.00 10.50 ? 16  VAL   A CA  1 
ATOM   43   C  C   . VAL   A 1 16  ? -5.533  4.797  5.597   1.00 9.94  ? 16  VAL   A C   1 
ATOM   44   O  O   . VAL   A 1 16  ? -6.307  4.682  4.665   1.00 10.75 ? 16  VAL   A O   1 
ATOM   45   C  CB  . VAL   A 1 16  ? -5.244  7.270  5.974   1.00 11.25 ? 16  VAL   A CB  1 
ATOM   46   C  CG1 . VAL   A 1 16  ? -5.744  7.266  7.417   1.00 10.79 ? 16  VAL   A CG1 1 
ATOM   47   C  CG2 . VAL   A 1 16  ? -4.324  8.487  5.794   1.00 11.37 ? 16  VAL   A CG2 1 
ATOM   48   N  N   . LEU   A 1 17  ? -5.527  3.969  6.644   1.00 9.78  ? 17  LEU   A N   1 
ATOM   49   C  CA  . LEU   A 1 17  ? -6.418  2.830  6.860   1.00 9.74  ? 17  LEU   A CA  1 
ATOM   50   C  C   . LEU   A 1 17  ? -7.278  3.049  8.102   1.00 8.90  ? 17  LEU   A C   1 
ATOM   51   O  O   . LEU   A 1 17  ? -6.873  3.696  9.040   1.00 9.86  ? 17  LEU   A O   1 
ATOM   52   C  CB  . LEU   A 1 17  ? -5.653  1.534  6.954   1.00 9.74  ? 17  LEU   A CB  1 
ATOM   53   C  CG  . LEU   A 1 17  ? -4.827  1.166  5.709   1.00 11.43 ? 17  LEU   A CG  1 
ATOM   54   C  CD1 . LEU   A 1 17  ? -4.079  -0.148 5.933   1.00 12.38 ? 17  LEU   A CD1 1 
ATOM   55   C  CD2 . LEU   A 1 17  ? -5.688  1.073  4.456   1.00 14.58 ? 17  LEU   A CD2 1 
ATOM   56   N  N   . ASP   A 1 18  ? -8.469  2.448  8.085   1.00 9.30  ? 18  ASP   A N   1 
ATOM   57   C  CA  . ASP   A 1 18  ? -9.463  2.524  9.170   1.00 8.84  ? 18  ASP   A CA  1 
ATOM   58   C  C   . ASP   A 1 18  ? -9.583  1.169  9.823   1.00 8.45  ? 18  ASP   A C   1 
ATOM   59   O  O   . ASP   A 1 18  ? -9.964  0.179  9.177   1.00 9.26  ? 18  ASP   A O   1 
ATOM   60   C  CB  . ASP   A 1 18  ? -10.810 2.985  8.564   1.00 9.51  ? 18  ASP   A CB  1 
ATOM   61   C  CG  . ASP   A 1 18  ? -11.938 3.105  9.531   1.00 10.76 ? 18  ASP   A CG  1 
ATOM   62   O  OD1 . ASP   A 1 18  ? -11.993 2.311  10.465  1.00 11.32 ? 18  ASP   A OD1 1 
ATOM   63   O  OD2 . ASP   A 1 18  ? -12.806 3.962  9.326   1.00 14.18 ? 18  ASP   A OD2 1 
ATOM   64   N  N   . ALA   A 1 19  ? -9.166  1.094  11.062  1.00 9.24  ? 19  ALA   A N   1 
ATOM   65   C  CA  . ALA   A 1 19  ? -9.120  -0.138 11.856  1.00 10.05 ? 19  ALA   A CA  1 
ATOM   66   C  C   . ALA   A 1 19  ? -10.464 -0.588 12.389  1.00 10.37 ? 19  ALA   A C   1 
ATOM   67   O  O   . ALA   A 1 19  ? -10.592 -1.708 12.899  1.00 11.90 ? 19  ALA   A O   1 
ATOM   68   C  CB  . ALA   A 1 19  ? -8.150  0.047  13.013  1.00 10.73 ? 19  ALA   A CB  1 
ATOM   69   N  N   . VAL   A 1 20  ? -11.490 0.238  12.304  1.00 10.50 ? 20  VAL   A N   1 
ATOM   70   C  CA  . VAL   A 1 20  ? -12.840 -0.095 12.759  1.00 11.91 ? 20  VAL   A CA  1 
ATOM   71   C  C   . VAL   A 1 20  ? -13.668 -0.675 11.650  1.00 12.89 ? 20  VAL   A C   1 
ATOM   72   O  O   . VAL   A 1 20  ? -14.401 -1.599 11.890  1.00 16.38 ? 20  VAL   A O   1 
ATOM   73   C  CB  . VAL   A 1 20  ? -13.560 1.153  13.314  1.00 14.32 ? 20  VAL   A CB  1 
ATOM   74   C  CG1 . VAL   A 1 20  ? -15.004 0.818  13.623  1.00 19.93 ? 20  VAL   A CG1 1 
ATOM   75   C  CG2 . VAL   A 1 20  ? -12.848 1.675  14.534  1.00 17.36 ? 20  VAL   A CG2 1 
ATOM   76   N  N   . ARG   A 1 21  ? -13.574 -0.098 10.469  1.00 12.85 ? 21  ARG   A N   1 
ATOM   77   C  CA  . ARG   A 1 21  ? -14.369 -0.512 9.342   1.00 16.12 ? 21  ARG   A CA  1 
ATOM   78   C  C   . ARG   A 1 21  ? -13.635 -1.563 8.494   1.00 13.23 ? 21  ARG   A C   1 
ATOM   79   O  O   . ARG   A 1 21  ? -14.260 -2.159 7.667   1.00 16.35 ? 21  ARG   A O   1 
ATOM   80   C  CB  . ARG   A 1 21  ? -14.736 0.763  8.468   1.00 18.99 ? 21  ARG   A CB  1 
ATOM   81   C  CG  . ARG   A 1 21  ? -15.570 1.815  9.231   1.00 24.10 ? 21  ARG   A CG  1 
ATOM   82   C  CD  . ARG   A 1 21  ? -15.759 3.239  8.582   1.00 22.45 ? 21  ARG   A CD  1 
ATOM   83   N  NE  . ARG   A 1 21  ? -16.488 3.227  7.358   1.00 36.27 ? 21  ARG   A NE  1 
ATOM   84   N  N   . GLY   A 1 22  ? -12.312 -1.693 8.673   1.00 10.21 ? 22  GLY   A N   1 
ATOM   85   C  CA  . GLY   A 1 22  ? -11.584 -2.642 7.838   1.00 9.94  ? 22  GLY   A CA  1 
ATOM   86   C  C   . GLY   A 1 22  ? -11.508 -2.194 6.419   1.00 9.38  ? 22  GLY   A C   1 
ATOM   87   O  O   . GLY   A 1 22  ? -11.766 -2.947 5.497   1.00 10.30 ? 22  GLY   A O   1 
ATOM   88   N  N   . SER   A 1 23  ? -11.141 -0.909 6.205   1.00 9.69  ? 23  SER   A N   1 
ATOM   89   C  CA  . SER   A 1 23  ? -11.219 -0.283 4.913   1.00 10.72 ? 23  SER   A CA  1 
ATOM   90   C  C   . SER   A 1 23  ? -10.149 0.763  4.829   1.00 9.86  ? 23  SER   A C   1 
ATOM   91   O  O   . SER   A 1 23  ? -9.629  1.239  5.827   1.00 10.47 ? 23  SER   A O   1 
ATOM   92   C  CB  . SER   A 1 23  ? -12.562 0.440  4.761   1.00 12.72 ? 23  SER   A CB  1 
ATOM   93   O  OG  . SER   A 1 23  ? -12.677 1.508  5.630   1.00 14.29 ? 23  SER   A OG  1 
ATOM   94   N  N   . PRO   A 1 24  ? -9.904  1.239  3.609   1.00 9.87  ? 24  PRO   A N   1 
ATOM   95   C  CA  . PRO   A 1 24  ? -9.174  2.511  3.470   1.00 10.69 ? 24  PRO   A CA  1 
ATOM   96   C  C   . PRO   A 1 24  ? -9.948  3.608  4.191   1.00 10.07 ? 24  PRO   A C   1 
ATOM   97   O  O   . PRO   A 1 24  ? -11.143 3.540  4.312   1.00 10.92 ? 24  PRO   A O   1 
ATOM   98   C  CB  . PRO   A 1 24  ? -9.134  2.775  1.958   1.00 13.44 ? 24  PRO   A CB  1 
ATOM   99   C  CG  . PRO   A 1 24  ? -9.738  1.648  1.347   1.00 23.29 ? 24  PRO   A CG  1 
ATOM   100  C  CD  . PRO   A 1 24  ? -10.370 0.758  2.311   1.00 11.93 ? 24  PRO   A CD  1 
ATOM   101  N  N   . ALA   A 1 25  ? -9.225  4.627  4.662   1.00 10.14 ? 25  ALA   A N   1 
ATOM   102  C  CA  . ALA   A 1 25  ? -9.859  5.818  5.218   1.00 10.09 ? 25  ALA   A CA  1 
ATOM   103  C  C   . ALA   A 1 25  ? -9.944  6.835  4.091   1.00 9.47  ? 25  ALA   A C   1 
ATOM   104  O  O   . ALA   A 1 25  ? -8.951  7.403  3.671   1.00 10.68 ? 25  ALA   A O   1 
ATOM   105  C  CB  . ALA   A 1 25  ? -9.037  6.327  6.375   1.00 11.54 ? 25  ALA   A CB  1 
ATOM   106  N  N   . ILE   A 1 26  ? -11.164 6.999  3.593   1.00 9.99  ? 26  ILE   A N   1 
ATOM   107  C  CA  . ILE   A 1 26  ? -11.404 7.765  2.381   1.00 11.29 ? 26  ILE   A CA  1 
ATOM   108  C  C   . ILE   A 1 26  ? -11.772 9.197  2.728   1.00 11.14 ? 26  ILE   A C   1 
ATOM   109  O  O   . ILE   A 1 26  ? -12.376 9.446  3.715   1.00 11.36 ? 26  ILE   A O   1 
ATOM   110  C  CB  . ILE   A 1 26  ? -12.573 7.101  1.583   1.00 14.60 ? 26  ILE   A CB  1 
ATOM   111  C  CG1 . ILE   A 1 26  ? -12.187 5.644  1.233   1.00 14.58 ? 26  ILE   A CG1 1 
ATOM   112  C  CG2 . ILE   A 1 26  ? -12.973 7.832  0.377   1.00 19.90 ? 26  ILE   A CG2 1 
ATOM   113  C  CD1 . ILE   A 1 26  ? -13.383 4.730  0.882   1.00 26.89 ? 26  ILE   A CD1 1 
ATOM   114  N  N   . ASN   A 1 27  ? -11.358 10.126 1.870   1.00 11.88 ? 27  ASN   A N   1 
ATOM   115  C  CA  . ASN   A 1 27  ? -11.708 11.552 2.029   1.00 13.63 ? 27  ASN   A CA  1 
ATOM   116  C  C   . ASN   A 1 27  ? -11.136 12.150 3.309   1.00 12.42 ? 27  ASN   A C   1 
ATOM   117  O  O   . ASN   A 1 27  ? -11.733 13.016 3.892   1.00 14.08 ? 27  ASN   A O   1 
ATOM   118  C  CB  . ASN   A 1 27  ? -13.243 11.774 1.973   1.00 16.00 ? 27  ASN   A CB  1 
ATOM   119  C  CG  . ASN   A 1 27  ? -13.889 11.362 0.628   0.50 14.58 ? 27  ASN   A CG  1 
ATOM   120  O  OD1 . ASN   A 1 27  ? -13.291 11.531 -0.440  0.50 18.54 ? 27  ASN   A OD1 1 
ATOM   121  N  ND2 . ASN   A 1 27  ? -15.122 10.755 0.676   0.50 15.48 ? 27  ASN   A ND2 1 
ATOM   122  N  N   . VAL   A 1 28  ? -9.961  11.729 3.731   1.00 11.65 ? 28  VAL   A N   1 
ATOM   123  C  CA  . VAL   A 1 28  ? -9.262  12.301 4.851   1.00 11.88 ? 28  VAL   A CA  1 
ATOM   124  C  C   . VAL   A 1 28  ? -8.477  13.486 4.365   1.00 11.11 ? 28  VAL   A C   1 
ATOM   125  O  O   . VAL   A 1 28  ? -7.631  13.340 3.501   1.00 11.23 ? 28  VAL   A O   1 
ATOM   126  C  CB  . VAL   A 1 28  ? -8.325  11.289 5.541   1.00 12.48 ? 28  VAL   A CB  1 
ATOM   127  C  CG1 . VAL   A 1 28  ? -7.553  11.929 6.674   1.00 13.40 ? 28  VAL   A CG1 1 
ATOM   128  C  CG2 . VAL   A 1 28  ? -9.046  10.035 6.034   1.00 15.15 ? 28  VAL   A CG2 1 
ATOM   129  N  N   . ALA   A 1 29  ? -8.686  14.659 4.970   1.00 10.62 ? 29  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 29  ? -7.872  15.846 4.667   1.00 9.77  ? 29  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 29  ? -6.510  15.733 5.278   1.00 10.00 ? 29  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 29  ? -6.382  15.340 6.450   1.00 10.90 ? 29  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 29  ? -8.586  17.075 5.178   1.00 11.12 ? 29  ALA   A CB  1 
ATOM   134  N  N   . VAL   A 1 30  ? -5.507  16.143 4.522   1.00 9.65  ? 30  VAL   A N   1 
ATOM   135  C  CA  . VAL   A 1 30  ? -4.119  16.121 4.955   1.00 9.66  ? 30  VAL   A CA  1 
ATOM   136  C  C   . VAL   A 1 30  ? -3.487  17.459 4.599   1.00 9.61  ? 30  VAL   A C   1 
ATOM   137  O  O   . VAL   A 1 30  ? -3.549  17.897 3.452   1.00 10.25 ? 30  VAL   A O   1 
ATOM   138  C  CB  . VAL   A 1 30  ? -3.329  14.984 4.278   1.00 10.42 ? 30  VAL   A CB  1 
ATOM   139  C  CG1 . VAL   A 1 30  ? -1.891  14.986 4.705   1.00 12.23 ? 30  VAL   A CG1 1 
ATOM   140  C  CG2 . VAL   A 1 30  ? -3.992  13.638 4.549   1.00 11.54 ? 30  VAL   A CG2 1 
ATOM   141  N  N   . HIS   A 1 31  ? -2.908  18.120 5.577   1.00 9.87  ? 31  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 31  ? -2.210  19.408 5.395   1.00 10.18 ? 31  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 31  ? -0.758  19.222 5.747   1.00 9.39  ? 31  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 31  ? -0.415  18.698 6.775   1.00 11.37 ? 31  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 31  ? -2.817  20.451 6.305   1.00 11.51 ? 31  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 31  ? -4.214  20.842 5.928   1.00 11.48 ? 31  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 31  ? -5.349  20.127 6.211   1.00 15.43 ? 31  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 31  ? -4.599  21.931 5.232   1.00 11.67 ? 31  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 31  ? -6.407  20.789 5.740   1.00 12.87 ? 31  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 31  ? -5.940  21.861 5.132   1.00 17.87 ? 31  HIS   A NE2 1 
ATOM   151  N  N   . VAL   A 1 32  ? 0.095   19.670 4.842   1.00 9.72  ? 32  VAL   A N   1 
ATOM   152  C  CA  . VAL   A 1 32  ? 1.557   19.598 5.001   1.00 10.07 ? 32  VAL   A CA  1 
ATOM   153  C  C   . VAL   A 1 32  ? 2.113   20.977 5.173   1.00 10.12 ? 32  VAL   A C   1 
ATOM   154  O  O   . VAL   A 1 32  ? 1.742   21.898 4.421   1.00 10.63 ? 32  VAL   A O   1 
ATOM   155  C  CB  . VAL   A 1 32  ? 2.251   18.874 3.829   1.00 10.02 ? 32  VAL   A CB  1 
ATOM   156  C  CG1 . VAL   A 1 32  ? 3.742   18.690 4.099   1.00 11.20 ? 32  VAL   A CG1 1 
ATOM   157  C  CG2 . VAL   A 1 32  ? 1.556   17.579 3.503   1.00 11.43 ? 32  VAL   A CG2 1 
ATOM   158  N  N   . PHE   A 1 33  ? 2.965   21.159 6.153   1.00 10.65 ? 33  PHE   A N   1 
ATOM   159  C  CA  . PHE   A 1 33  ? 3.617   22.420 6.469   1.00 11.21 ? 33  PHE   A CA  1 
ATOM   160  C  C   . PHE   A 1 33  ? 5.141   22.214 6.436   1.00 11.34 ? 33  PHE   A C   1 
ATOM   161  O  O   . PHE   A 1 33  ? 5.626   21.086 6.614   1.00 11.10 ? 33  PHE   A O   1 
ATOM   162  C  CB  . PHE   A 1 33  ? 3.201   22.962 7.838   1.00 12.02 ? 33  PHE   A CB  1 
ATOM   163  C  CG  . PHE   A 1 33  ? 1.731   23.086 7.949   1.00 13.66 ? 33  PHE   A CG  1 
ATOM   164  C  CD1 . PHE   A 1 33  ? 0.948   21.991 8.336   1.00 14.33 ? 33  PHE   A CD1 1 
ATOM   165  C  CD2 . PHE   A 1 33  ? 1.088   24.263 7.644   1.00 14.27 ? 33  PHE   A CD2 1 
ATOM   166  C  CE1 . PHE   A 1 33  ? -0.441  22.094 8.481   1.00 14.53 ? 33  PHE   A CE1 1 
ATOM   167  C  CE2 . PHE   A 1 33  ? -0.281  24.355 7.756   1.00 15.46 ? 33  PHE   A CE2 1 
ATOM   168  C  CZ  . PHE   A 1 33  ? -1.058  23.276 8.174   1.00 15.96 ? 33  PHE   A CZ  1 
ATOM   169  N  N   . ARG   A 1 34  ? 5.891   23.305 6.251   1.00 11.54 ? 34  ARG   A N   1 
ATOM   170  C  CA  . ARG   A 1 34  ? 7.343   23.284 6.241   1.00 10.97 ? 34  ARG   A CA  1 
ATOM   171  C  C   . ARG   A 1 34  ? 7.808   24.392 7.112   1.00 11.47 ? 34  ARG   A C   1 
ATOM   172  O  O   . ARG   A 1 34  ? 7.340   25.527 6.991   1.00 14.02 ? 34  ARG   A O   1 
ATOM   173  C  CB  . ARG   A 1 34  ? 7.919   23.378 4.804   1.00 12.72 ? 34  ARG   A CB  1 
ATOM   174  C  CG  . ARG   A 1 34  ? 9.431   23.336 4.760   1.00 12.55 ? 34  ARG   A CG  1 
ATOM   175  C  CD  . ARG   A 1 34  ? 9.912   23.546 3.353   1.00 13.78 ? 34  ARG   A CD  1 
ATOM   176  N  NE  . ARG   A 1 34  ? 11.373  23.583 3.286   1.00 13.77 ? 34  ARG   A NE  1 
ATOM   177  C  CZ  . ARG   A 1 34  ? 12.133  24.613 3.619   1.00 12.77 ? 34  ARG   A CZ  1 
ATOM   178  N  NH1 . ARG   A 1 34  ? 11.543  25.776 3.958   1.00 14.05 ? 34  ARG   A NH1 1 
ATOM   179  N  NH2 . ARG   A 1 34  ? 13.420  24.523 3.544   1.00 14.37 ? 34  ARG   A NH2 1 
ATOM   180  N  N   . LYS   A 1 35  ? 8.767   24.153 7.963   1.00 11.45 ? 35  LYS   A N   1 
ATOM   181  C  CA  . LYS   A 1 35  ? 9.278   25.167 8.881   1.00 12.85 ? 35  LYS   A CA  1 
ATOM   182  C  C   . LYS   A 1 35  ? 10.051  26.172 8.093   1.00 12.95 ? 35  LYS   A C   1 
ATOM   183  O  O   . LYS   A 1 35  ? 10.952  25.880 7.340   1.00 15.26 ? 35  LYS   A O   1 
ATOM   184  C  CB  . LYS   A 1 35  ? 10.144  24.527 9.980   1.00 15.62 ? 35  LYS   A CB  1 
ATOM   185  C  CG  . LYS   A 1 35  ? 9.911   25.092 11.348  1.00 26.44 ? 35  LYS   A CG  1 
ATOM   186  C  CD  . LYS   A 1 35  ? 10.474  24.144 12.474  1.00 27.78 ? 35  LYS   A CD  1 
ATOM   187  N  N   . ALA   A 1 36  ? 9.715   27.454 8.253   1.00 14.22 ? 36  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 36  ? 10.378  28.551 7.582   1.00 14.95 ? 36  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 36  ? 11.581  28.954 8.378   1.00 16.46 ? 36  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 36  ? 11.804  28.537 9.518   1.00 17.23 ? 36  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 36  ? 9.428   29.748 7.504   1.00 19.58 ? 36  ALA   A CB  1 
ATOM   192  N  N   . ALA   A 1 37  ? 12.322  29.901 7.819   1.00 19.83 ? 37  ALA   A N   1 
ATOM   193  C  CA  . ALA   A 1 37  ? 13.540  30.418 8.368   1.00 27.15 ? 37  ALA   A CA  1 
ATOM   194  C  C   . ALA   A 1 37  ? 13.353  31.006 9.742   1.00 24.66 ? 37  ALA   A C   1 
ATOM   195  O  O   . ALA   A 1 37  ? 14.271  30.979 10.584  1.00 29.33 ? 37  ALA   A O   1 
ATOM   196  C  CB  . ALA   A 1 37  ? 14.122  31.479 7.428   1.00 27.75 ? 37  ALA   A CB  1 
ATOM   197  N  N   . ASP   A 1 38  ? 12.194  31.606 9.932   1.00 21.62 ? 38  ASP   A N   1 
ATOM   198  C  CA  . ASP   A 1 38  ? 11.856  32.200 11.213  1.00 21.22 ? 38  ASP   A CA  1 
ATOM   199  C  C   . ASP   A 1 38  ? 11.243  31.252 12.197  1.00 25.66 ? 38  ASP   A C   1 
ATOM   200  O  O   . ASP   A 1 38  ? 10.696  31.688 13.215  1.00 31.81 ? 38  ASP   A O   1 
ATOM   201  C  CB  . ASP   A 1 38  ? 10.944  33.388 10.974  1.00 30.31 ? 38  ASP   A CB  1 
ATOM   202  C  CG  . ASP   A 1 38  ? 9.721   33.045 10.290  1.00 35.40 ? 38  ASP   A CG  1 
ATOM   203  O  OD1 . ASP   A 1 38  ? 9.285   31.869 10.336  1.00 26.93 ? 38  ASP   A OD1 1 
ATOM   204  O  OD2 . ASP   A 1 38  ? 9.163   33.987 9.728   1.00 50.79 ? 38  ASP   A OD2 1 
ATOM   205  N  N   . ASP   A 1 39  ? 11.316  29.958 11.928  1.00 22.64 ? 39  ASP   A N   1 
ATOM   206  C  CA  . ASP   A 1 39  ? 10.817  28.928 12.832  1.00 25.70 ? 39  ASP   A CA  1 
ATOM   207  C  C   . ASP   A 1 39  ? 9.304   28.835 12.869  1.00 26.71 ? 39  ASP   A C   1 
ATOM   208  O  O   . ASP   A 1 39  ? 8.787   28.134 13.709  1.00 38.90 ? 39  ASP   A O   1 
ATOM   209  C  CB  . ASP   A 1 39  ? 11.354  29.103 14.284  1.00 33.47 ? 39  ASP   A CB  1 
ATOM   210  N  N   . THR   A 1 40  ? 8.574   29.523 11.988  1.00 24.99 ? 40  THR   A N   1 
ATOM   211  C  CA  . THR   A 1 40  ? 7.114   29.330 11.921  1.00 25.62 ? 40  THR   A CA  1 
ATOM   212  C  C   . THR   A 1 40  ? 6.799   28.222 10.957  1.00 23.20 ? 40  THR   A C   1 
ATOM   213  O  O   . THR   A 1 40  ? 7.592   27.936 10.064  1.00 18.11 ? 40  THR   A O   1 
ATOM   214  C  CB  . THR   A 1 40  ? 6.357   30.616 11.503  1.00 29.91 ? 40  THR   A CB  1 
ATOM   215  O  OG1 . THR   A 1 40  ? 6.704   30.944 10.141  1.00 30.00 ? 40  THR   A OG1 1 
ATOM   216  N  N   . TRP   A 1 41  ? 5.617   27.630 11.117  1.00 23.88 ? 41  TRP   A N   1 
ATOM   217  C  CA  . TRP   A 1 41  ? 5.141   26.688 10.116  1.00 18.02 ? 41  TRP   A CA  1 
ATOM   218  C  C   . TRP   A 1 41  ? 4.487   27.396 8.955   1.00 21.24 ? 41  TRP   A C   1 
ATOM   219  O  O   . TRP   A 1 41  ? 3.467   28.166 9.125   1.00 54.64 ? 41  TRP   A O   1 
ATOM   220  C  CB  . TRP   A 1 41  ? 4.144   25.728 10.750  1.00 19.28 ? 41  TRP   A CB  1 
ATOM   221  C  CG  . TRP   A 1 41  ? 4.741   24.752 11.690  1.00 17.77 ? 41  TRP   A CG  1 
ATOM   222  C  CD1 . TRP   A 1 41  ? 4.587   24.715 13.059  1.00 24.54 ? 41  TRP   A CD1 1 
ATOM   223  C  CD2 . TRP   A 1 41  ? 5.594   23.649 11.370  1.00 16.05 ? 41  TRP   A CD2 1 
ATOM   224  N  NE1 . TRP   A 1 41  ? 5.230   23.624 13.586  1.00 26.38 ? 41  TRP   A NE1 1 
ATOM   225  C  CE2 . TRP   A 1 41  ? 5.881   22.968 12.571  1.00 20.94 ? 41  TRP   A CE2 1 
ATOM   226  C  CE3 . TRP   A 1 41  ? 6.122   23.139 10.181  1.00 14.95 ? 41  TRP   A CE3 1 
ATOM   227  C  CZ2 . TRP   A 1 41  ? 6.732   21.858 12.598  1.00 22.39 ? 41  TRP   A CZ2 1 
ATOM   228  C  CZ3 . TRP   A 1 41  ? 6.936   22.083 10.203  1.00 14.95 ? 41  TRP   A CZ3 1 
ATOM   229  C  CH2 . TRP   A 1 41  ? 7.250   21.454 11.408  1.00 18.52 ? 41  TRP   A CH2 1 
ATOM   230  N  N   . GLU   A 1 42  ? 4.938   27.101 7.752   1.00 15.34 ? 42  GLU   A N   1 
ATOM   231  C  CA  . GLU   A 1 42  ? 4.371   27.665 6.567   1.00 17.28 ? 42  GLU   A CA  1 
ATOM   232  C  C   . GLU   A 1 42  ? 3.652   26.564 5.797   1.00 14.68 ? 42  GLU   A C   1 
ATOM   233  O  O   . GLU   A 1 42  ? 4.099   25.452 5.702   1.00 14.76 ? 42  GLU   A O   1 
ATOM   234  C  CB  . GLU   A 1 42  ? 5.481   28.221 5.627   1.00 21.42 ? 42  GLU   A CB  1 
ATOM   235  N  N   . PRO   A 1 43  ? 2.515   26.926 5.173   1.00 14.68 ? 43  PRO   A N   1 
ATOM   236  C  CA  . PRO   A 1 43  ? 1.769   25.927 4.362   1.00 15.58 ? 43  PRO   A CA  1 
ATOM   237  C  C   . PRO   A 1 43  ? 2.598   25.484 3.217   1.00 17.21 ? 43  PRO   A C   1 
ATOM   238  O  O   . PRO   A 1 43  ? 3.271   26.297 2.565   1.00 24.68 ? 43  PRO   A O   1 
ATOM   239  C  CB  . PRO   A 1 43  ? 0.549   26.719 3.880   1.00 18.85 ? 43  PRO   A CB  1 
ATOM   240  C  CG  . PRO   A 1 43  ? 0.500   27.955 4.687   1.00 24.31 ? 43  PRO   A CG  1 
ATOM   241  C  CD  . PRO   A 1 43  ? 1.830   28.264 5.154   1.00 18.67 ? 43  PRO   A CD  1 
ATOM   242  N  N   . PHE   A 1 44  ? 2.617   24.196 2.932   1.00 12.44 ? 44  PHE   A N   1 
ATOM   243  C  CA  . PHE   A 1 44  ? 3.426   23.611 1.895   1.00 12.04 ? 44  PHE   A CA  1 
ATOM   244  C  C   . PHE   A 1 44  ? 2.577   22.897 0.830   1.00 11.93 ? 44  PHE   A C   1 
ATOM   245  O  O   . PHE   A 1 44  ? 2.753   23.122 -0.352  1.00 14.03 ? 44  PHE   A O   1 
ATOM   246  C  CB  . PHE   A 1 44  ? 4.442   22.643 2.532   1.00 11.25 ? 44  PHE   A CB  1 
ATOM   247  C  CG  . PHE   A 1 44  ? 5.332   21.993 1.544   1.00 12.62 ? 44  PHE   A CG  1 
ATOM   248  C  CD1 . PHE   A 1 44  ? 6.398   22.674 0.984   1.00 13.72 ? 44  PHE   A CD1 1 
ATOM   249  C  CD2 . PHE   A 1 44  ? 5.077   20.719 1.096   1.00 12.56 ? 44  PHE   A CD2 1 
ATOM   250  C  CE1 . PHE   A 1 44  ? 7.175   22.038 0.002   1.00 13.35 ? 44  PHE   A CE1 1 
ATOM   251  C  CE2 . PHE   A 1 44  ? 5.828   20.154 0.113   1.00 12.90 ? 44  PHE   A CE2 1 
ATOM   252  C  CZ  . PHE   A 1 44  ? 6.883   20.785 -0.529  1.00 14.93 ? 44  PHE   A CZ  1 
ATOM   253  N  N   . ALA   A 1 45  ? 1.623   22.075 1.268   1.00 11.13 ? 45  ALA   A N   1 
ATOM   254  C  CA  . ALA   A 1 45  ? 0.732   21.460 0.451   1.00 11.72 ? 45  ALA   A CA  1 
ATOM   255  C  C   . ALA   A 1 45  ? -0.424  20.798 1.122   1.00 10.81 ? 45  ALA   A C   1 
ATOM   256  O  O   . ALA   A 1 45  ? -0.327  20.623 2.293   1.00 12.47 ? 45  ALA   A O   1 
ATOM   257  C  CB  . ALA   A 1 45  ? 1.431   20.239 -0.367  1.00 11.98 ? 45  ALA   A CB  1 
ATOM   258  N  N   . SER   A 1 46  ? -1.537  20.505 0.464   1.00 9.90  ? 46  SER   A N   1 
ATOM   259  C  CA  . SER   A 1 46  ? -2.636  19.791 1.075   1.00 9.67  ? 46  SER   A CA  1 
ATOM   260  C  C   . SER   A 1 46  ? -3.398  18.960 0.034   1.00 9.41  ? 46  SER   A C   1 
ATOM   261  O  O   . SER   A 1 46  ? -3.294  19.221 -1.140  1.00 10.79 ? 46  SER   A O   1 
ATOM   262  C  CB  . SER   A 1 46  ? -3.536  20.749 1.877   1.00 10.18 ? 46  SER   A CB  1 
ATOM   263  O  OG  . SER   A 1 46  ? -4.226  21.628 0.999   1.00 10.78 ? 46  SER   A OG  1 
ATOM   264  N  N   . GLY   A 1 47  ? -4.212  18.044 0.521   1.00 9.75  ? 47  GLY   A N   1 
ATOM   265  C  CA  . GLY   A 1 47  ? -5.016  17.218 -0.320  1.00 10.01 ? 47  GLY   A CA  1 
ATOM   266  C  C   . GLY   A 1 47  ? -5.897  16.307 0.493   1.00 9.47  ? 47  GLY   A C   1 
ATOM   267  O  O   . GLY   A 1 47  ? -6.011  16.475 1.688   1.00 10.50 ? 47  GLY   A O   1 
ATOM   268  N  N   . LYS   A 1 48  ? -6.551  15.371 -0.170  1.00 10.05 ? 48  LYS   A N   1 
ATOM   269  C  CA  . LYS   A 1 48  ? -7.371  14.411 0.567   1.00 11.19 ? 48  LYS   A CA  1 
ATOM   270  C  C   . LYS   A 1 48  ? -7.182  13.031 -0.008  1.00 10.32 ? 48  LYS   A C   1 
ATOM   271  O  O   . LYS   A 1 48  ? -6.872  12.817 -1.158  1.00 12.03 ? 48  LYS   A O   1 
ATOM   272  C  CB  . LYS   A 1 48  ? -8.796  14.802 0.641   1.00 15.41 ? 48  LYS   A CB  1 
ATOM   273  C  CG  . LYS   A 1 48  ? -9.382  14.884 -0.629  1.00 17.49 ? 48  LYS   A CG  1 
ATOM   274  C  CD  . LYS   A 1 48  ? -10.703 15.698 -0.580  1.00 27.77 ? 48  LYS   A CD  1 
ATOM   275  C  CE  . LYS   A 1 48  ? -11.707 14.943 0.265   1.00 28.17 ? 48  LYS   A CE  1 
ATOM   276  N  N   . THR   A 1 49  ? -7.364  12.039 0.862   1.00 10.90 ? 49  THR   A N   1 
ATOM   277  C  CA  . THR   A 1 49  ? -7.198  10.647 0.422   1.00 9.95  ? 49  THR   A CA  1 
ATOM   278  C  C   . THR   A 1 49  ? -8.319  10.225 -0.500  1.00 10.98 ? 49  THR   A C   1 
ATOM   279  O  O   . THR   A 1 49  ? -9.459  10.619 -0.366  1.00 11.64 ? 49  THR   A O   1 
ATOM   280  C  CB  . THR   A 1 49  ? -7.102  9.689  1.605   1.00 11.12 ? 49  THR   A CB  1 
ATOM   281  O  OG1 . THR   A 1 49  ? -8.326  9.725  2.358   1.00 11.00 ? 49  THR   A OG1 1 
ATOM   282  C  CG2 . THR   A 1 49  ? -5.891  9.963  2.541   1.00 11.54 ? 49  THR   A CG2 1 
ATOM   283  N  N   . SER   A 1 50  ? -7.951  9.385  -1.455  1.00 11.14 ? 50  SER   A N   1 
ATOM   284  C  CA  . SER   A 1 50  ? -8.825  8.847  -2.431  1.00 11.94 ? 50  SER   A CA  1 
ATOM   285  C  C   . SER   A 1 50  ? -9.643  7.676  -1.890  1.00 12.22 ? 50  SER   A C   1 
ATOM   286  O  O   . SER   A 1 50  ? -9.531  7.296  -0.728  1.00 12.77 ? 50  SER   A O   1 
ATOM   287  C  CB  . SER   A 1 50  ? -7.967  8.346  -3.605  1.00 14.20 ? 50  SER   A CB  1 
ATOM   288  O  OG  . SER   A 1 50  ? -7.313  7.156  -3.172  1.00 15.93 ? 50  SER   A OG  1 
ATOM   289  N  N   . GLU   A 1 51  ? -10.368 7.007  -2.759  1.00 13.50 ? 51  GLU   A N   1 
ATOM   290  C  CA  . GLU   A 1 51  ? -11.101 5.816  -2.450  1.00 15.27 ? 51  GLU   A CA  1 
ATOM   291  C  C   . GLU   A 1 51  ? -10.215 4.644  -1.983  1.00 14.43 ? 51  GLU   A C   1 
ATOM   292  O  O   . GLU   A 1 51  ? -10.661 3.754  -1.306  1.00 16.91 ? 51  GLU   A O   1 
ATOM   293  C  CB  . GLU   A 1 51  ? -12.051 5.461  -3.643  1.00 25.21 ? 51  GLU   A CB  1 
ATOM   294  N  N   . SER   A 1 52  ? -8.946  4.686  -2.316  1.00 13.51 ? 52  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 52  ? -7.978  3.669  -1.841  1.00 14.66 ? 52  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 52  ? -7.302  4.054  -0.575  1.00 12.02 ? 52  SER   A C   1 
ATOM   297  O  O   . SER   A 1 52  ? -6.441  3.371  -0.102  1.00 12.92 ? 52  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 52  ? -6.927  3.399  -2.936  1.00 17.84 ? 52  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 52  ? -6.157  4.576  -3.062  1.00 24.52 ? 52  SER   A OG  1 
ATOM   300  N  N   . GLY   A 1 53  ? -7.645  5.231  -0.006  1.00 11.46 ? 53  GLY   A N   1 
ATOM   301  C  CA  . GLY   A 1 53  ? -7.015  5.754  1.202   1.00 10.73 ? 53  GLY   A CA  1 
ATOM   302  C  C   . GLY   A 1 53  ? -5.671  6.395  0.921   1.00 10.38 ? 53  GLY   A C   1 
ATOM   303  O  O   . GLY   A 1 53  ? -4.949  6.702  1.844   1.00 11.71 ? 53  GLY   A O   1 
ATOM   304  N  N   . GLU   A 1 54  ? -5.331  6.636  -0.341  1.00 11.79 ? 54  GLU   A N   1 
ATOM   305  C  CA  . GLU   A 1 54  ? -4.023  7.150  -0.718  1.00 11.49 ? 54  GLU   A CA  1 
ATOM   306  C  C   . GLU   A 1 54  ? -4.127  8.591  -1.170  1.00 9.80  ? 54  GLU   A C   1 
ATOM   307  O  O   . GLU   A 1 54  ? -5.096  9.006  -1.745  1.00 11.71 ? 54  GLU   A O   1 
ATOM   308  C  CB  . GLU   A 1 54  ? -3.401  6.300  -1.796  1.00 16.17 ? 54  GLU   A CB  1 
ATOM   309  C  CG  . GLU   A 1 54  ? -3.148  4.846  -1.288  1.00 19.36 ? 54  GLU   A CG  1 
ATOM   310  C  CD  . GLU   A 1 54  ? -2.230  3.993  -2.137  1.00 26.89 ? 54  GLU   A CD  1 
ATOM   311  O  OE1 . GLU   A 1 54  ? -1.822  4.422  -3.230  0.50 53.48 ? 54  GLU   A OE1 1 
ATOM   312  O  OE2 . GLU   A 1 54  ? -1.999  2.830  -1.614  1.00 34.47 ? 54  GLU   A OE2 1 
ATOM   313  N  N   . LEU   A 1 55  ? -3.079  9.337  -0.923  1.00 10.27 ? 55  LEU   A N   1 
ATOM   314  C  CA  . LEU   A 1 55  ? -2.949  10.720 -1.339  1.00 9.75  ? 55  LEU   A CA  1 
ATOM   315  C  C   . LEU   A 1 55  ? -1.611  10.861 -2.039  1.00 11.20 ? 55  LEU   A C   1 
ATOM   316  O  O   . LEU   A 1 55  ? -0.583  10.809 -1.440  1.00 11.76 ? 55  LEU   A O   1 
ATOM   317  C  CB  . LEU   A 1 55  ? -3.071  11.648 -0.144  1.00 10.48 ? 55  LEU   A CB  1 
ATOM   318  C  CG  . LEU   A 1 55  ? -2.680  13.116 -0.385  1.00 10.69 ? 55  LEU   A CG  1 
ATOM   319  C  CD1 . LEU   A 1 55  ? -3.401  13.706 -1.585  1.00 12.44 ? 55  LEU   A CD1 1 
ATOM   320  C  CD2 . LEU   A 1 55  ? -3.007  13.882 0.869   1.00 11.80 ? 55  LEU   A CD2 1 
ATOM   321  N  N   . HIS   A 1 56  ? -1.691  11.026 -3.359  1.00 13.06 ? 56  HIS   A N   1 
ATOM   322  C  CA  . HIS   A 1 56  ? -0.613  11.274 -4.276  1.00 15.74 ? 56  HIS   A CA  1 
ATOM   323  C  C   . HIS   A 1 56  ? -0.651  12.750 -4.772  1.00 14.46 ? 56  HIS   A C   1 
ATOM   324  O  O   . HIS   A 1 56  ? -1.680  13.374 -4.682  1.00 16.46 ? 56  HIS   A O   1 
ATOM   325  C  CB  . HIS   A 1 56  ? -0.694  10.344 -5.499  1.00 18.48 ? 56  HIS   A CB  1 
ATOM   326  C  CG  . HIS   A 1 56  ? -0.612  8.899  -5.157  1.00 18.70 ? 56  HIS   A CG  1 
ATOM   327  N  ND1 . HIS   A 1 56  ? -1.690  8.111  -4.971  1.00 24.10 ? 56  HIS   A ND1 1 
ATOM   328  C  CD2 . HIS   A 1 56  ? 0.478   8.118  -4.945  1.00 23.43 ? 56  HIS   A CD2 1 
ATOM   329  C  CE1 . HIS   A 1 56  ? -1.286  6.890  -4.684  1.00 24.52 ? 56  HIS   A CE1 1 
ATOM   330  N  NE2 . HIS   A 1 56  ? 0.026   6.863  -4.652  1.00 33.41 ? 56  HIS   A NE2 1 
ATOM   331  N  N   . GLY   A 1 57  ? 0.415   13.212 -5.342  1.00 15.27 ? 57  GLY   A N   1 
ATOM   332  C  CA  . GLY   A 1 57  ? 0.395   14.502 -5.948  1.00 16.52 ? 57  GLY   A CA  1 
ATOM   333  C  C   . GLY   A 1 57  ? 0.609   15.674 -5.031  1.00 14.16 ? 57  GLY   A C   1 
ATOM   334  O  O   . GLY   A 1 57  ? 0.381   16.779 -5.483  1.00 16.54 ? 57  GLY   A O   1 
ATOM   335  N  N   . LEU   A 1 58  ? 0.988   15.478 -3.787  1.00 12.28 ? 58  LEU   A N   1 
ATOM   336  C  CA  . LEU   A 1 58  ? 1.181   16.593 -2.891  1.00 11.68 ? 58  LEU   A CA  1 
ATOM   337  C  C   . LEU   A 1 58  ? 2.244   17.541 -3.377  1.00 11.63 ? 58  LEU   A C   1 
ATOM   338  O  O   . LEU   A 1 58  ? 2.100   18.752 -3.250  1.00 13.09 ? 58  LEU   A O   1 
ATOM   339  C  CB  . LEU   A 1 58  ? 1.525   16.163 -1.462  1.00 11.04 ? 58  LEU   A CB  1 
ATOM   340  C  CG  . LEU   A 1 58  ? 0.302   15.719 -0.633  1.00 12.10 ? 58  LEU   A CG  1 
ATOM   341  C  CD1 . LEU   A 1 58  ? 0.766   14.948 0.589   1.00 13.87 ? 58  LEU   A CD1 1 
ATOM   342  C  CD2 . LEU   A 1 58  ? -0.600  16.905 -0.281  1.00 15.30 ? 58  LEU   A CD2 1 
ATOM   343  N  N   . THR   A 1 59  ? 3.349   17.015 -3.875  1.00 12.03 ? 59  THR   A N   1 
ATOM   344  C  CA  . THR   A 1 59  ? 4.475   17.829 -4.236  1.00 11.82 ? 59  THR   A CA  1 
ATOM   345  C  C   . THR   A 1 59  ? 5.290   17.235 -5.371  1.00 11.78 ? 59  THR   A C   1 
ATOM   346  O  O   . THR   A 1 59  ? 4.935   16.211 -5.949  1.00 15.36 ? 59  THR   A O   1 
ATOM   347  C  CB  . THR   A 1 59  ? 5.324   18.139 -2.990  1.00 12.07 ? 59  THR   A CB  1 
ATOM   348  O  OG1 . THR   A 1 59  ? 6.274   19.164 -3.247  1.00 12.38 ? 59  THR   A OG1 1 
ATOM   349  C  CG2 . THR   A 1 59  ? 6.038   16.911 -2.471  1.00 12.39 ? 59  THR   A CG2 1 
ATOM   350  N  N   . THR   A 1 60  ? 6.370   17.859 -5.722  1.00 13.48 ? 60  THR   A N   1 
ATOM   351  C  CA  . THR   A 1 60  ? 7.240   17.497 -6.820  1.00 13.15 ? 60  THR   A CA  1 
ATOM   352  C  C   . THR   A 1 60  ? 8.673   17.378 -6.257  1.00 12.65 ? 60  THR   A C   1 
ATOM   353  O  O   . THR   A 1 60  ? 9.021   17.919 -5.208  1.00 13.31 ? 60  THR   A O   1 
ATOM   354  C  CB  . THR   A 1 60  ? 7.241   18.595 -7.958  1.00 13.49 ? 60  THR   A CB  1 
ATOM   355  O  OG1 . THR   A 1 60  ? 7.800   19.775 -7.412  1.00 14.54 ? 60  THR   A OG1 1 
ATOM   356  C  CG2 . THR   A 1 60  ? 5.837   18.807 -8.453  1.00 18.79 ? 60  THR   A CG2 1 
ATOM   357  N  N   . GLU   A 1 61  ? 9.517   16.696 -7.040  1.00 13.30 ? 61  GLU   A N   1 
ATOM   358  C  CA  . GLU   A 1 61  ? 10.933  16.643 -6.701  1.00 15.53 ? 61  GLU   A CA  1 
ATOM   359  C  C   . GLU   A 1 61  ? 11.541  18.022 -6.617  1.00 13.94 ? 61  GLU   A C   1 
ATOM   360  O  O   . GLU   A 1 61  ? 12.416  18.234 -5.767  1.00 17.34 ? 61  GLU   A O   1 
ATOM   361  C  CB  . GLU   A 1 61  ? 11.674  15.827 -7.759  1.00 20.33 ? 61  GLU   A CB  1 
ATOM   362  N  N   . GLU   A 1 62  ? 11.107  18.931 -7.443  1.00 13.26 ? 62  GLU   A N   1 
ATOM   363  C  CA  . GLU   A 1 62  ? 11.683  20.278 -7.452  1.00 14.48 ? 62  GLU   A CA  1 
ATOM   364  C  C   . GLU   A 1 62  ? 11.300  21.041 -6.204  1.00 12.43 ? 62  GLU   A C   1 
ATOM   365  O  O   . GLU   A 1 62  ? 12.089  21.756 -5.613  1.00 13.67 ? 62  GLU   A O   1 
ATOM   366  C  CB  . GLU   A 1 62  ? 11.187  21.072 -8.668  1.00 17.93 ? 62  GLU   A CB  1 
ATOM   367  C  CG  . GLU   A 1 62  ? 11.717  20.598 -9.996  1.00 23.60 ? 62  GLU   A CG  1 
ATOM   368  C  CD  . GLU   A 1 62  ? 11.209  19.255 -10.473 1.00 26.68 ? 62  GLU   A CD  1 
ATOM   369  O  OE1 . GLU   A 1 62  ? 10.046  18.895 -10.147 1.00 22.75 ? 62  GLU   A OE1 1 
ATOM   370  N  N   . GLU   A 1 63  ? 10.045  20.933 -5.817  1.00 10.91 ? 63  GLU   A N   1 
ATOM   371  C  CA  A GLU   A 1 63  ? 9.611   21.756 -4.696  0.50 12.02 ? 63  GLU   A CA  1 
ATOM   372  C  CA  B GLU   A 1 63  ? 9.489   21.699 -4.669  0.50 12.59 ? 63  GLU   A CA  1 
ATOM   373  C  C   . GLU   A 1 63  ? 9.863   21.215 -3.243  1.00 10.47 ? 63  GLU   A C   1 
ATOM   374  O  O   . GLU   A 1 63  ? 9.925   21.936 -2.297  1.00 10.90 ? 63  GLU   A O   1 
ATOM   375  C  CB  A GLU   A 1 63  ? 8.153   22.196 -4.944  0.50 13.09 ? 63  GLU   A CB  1 
ATOM   376  C  CB  B GLU   A 1 63  ? 7.940   21.667 -4.759  0.50 11.89 ? 63  GLU   A CB  1 
ATOM   377  C  CG  A GLU   A 1 63  ? 8.076   23.324 -6.016  0.50 13.06 ? 63  GLU   A CG  1 
ATOM   378  C  CG  B GLU   A 1 63  ? 7.182   22.544 -3.751  0.50 12.94 ? 63  GLU   A CG  1 
ATOM   379  C  CD  A GLU   A 1 63  ? 6.657   23.784 -6.340  0.50 15.37 ? 63  GLU   A CD  1 
ATOM   380  C  CD  B GLU   A 1 63  ? 5.702   22.575 -3.994  0.50 12.53 ? 63  GLU   A CD  1 
ATOM   381  O  OE1 A GLU   A 1 63  ? 5.659   23.111 -6.035  0.50 17.86 ? 63  GLU   A OE1 1 
ATOM   382  O  OE1 B GLU   A 1 63  ? 5.204   23.618 -4.434  0.50 14.03 ? 63  GLU   A OE1 1 
ATOM   383  O  OE2 A GLU   A 1 63  ? 6.561   24.835 -6.853  0.50 13.50 ? 63  GLU   A OE2 1 
ATOM   384  O  OE2 B GLU   A 1 63  ? 5.011   21.567 -3.773  0.50 9.56  ? 63  GLU   A OE2 1 
ATOM   385  N  N   . PHE   A 1 64  ? 10.049  19.869 -3.173  1.00 10.86 ? 64  PHE   A N   1 
ATOM   386  C  CA  . PHE   A 1 64  ? 10.274  19.143 -1.956  1.00 9.80  ? 64  PHE   A CA  1 
ATOM   387  C  C   . PHE   A 1 64  ? 11.752  19.162 -1.578  1.00 10.03 ? 64  PHE   A C   1 
ATOM   388  O  O   . PHE   A 1 64  ? 12.464  18.172 -1.671  1.00 10.99 ? 64  PHE   A O   1 
ATOM   389  C  CB  . PHE   A 1 64  ? 9.741   17.726 -2.081  1.00 10.83 ? 64  PHE   A CB  1 
ATOM   390  C  CG  . PHE   A 1 64  ? 9.695   16.969 -0.807  1.00 10.87 ? 64  PHE   A CG  1 
ATOM   391  C  CD1 . PHE   A 1 64  ? 9.106   17.436 0.321   1.00 11.31 ? 64  PHE   A CD1 1 
ATOM   392  C  CD2 . PHE   A 1 64  ? 10.289  15.695 -0.746  1.00 14.10 ? 64  PHE   A CD2 1 
ATOM   393  C  CE1 . PHE   A 1 64  ? 9.060   16.659 1.511   1.00 12.16 ? 64  PHE   A CE1 1 
ATOM   394  C  CE2 . PHE   A 1 64  ? 10.222  14.948 0.377   1.00 15.16 ? 64  PHE   A CE2 1 
ATOM   395  C  CZ  . PHE   A 1 64  ? 9.594   15.410 1.506   1.00 14.65 ? 64  PHE   A CZ  1 
ATOM   396  N  N   . VAL   A 1 65  ? 12.196  20.356 -1.179  1.00 10.32 ? 65  VAL   A N   1 
ATOM   397  C  CA  . VAL   A 1 65  ? 13.563  20.609 -0.785  1.00 9.07  ? 65  VAL   A CA  1 
ATOM   398  C  C   . VAL   A 1 65  ? 13.809  20.133 0.628   1.00 9.60  ? 65  VAL   A C   1 
ATOM   399  O  O   . VAL   A 1 65  ? 12.911  19.625 1.300   1.00 11.05 ? 65  VAL   A O   1 
ATOM   400  C  CB  . VAL   A 1 65  ? 13.864  22.118 -0.922  1.00 11.04 ? 65  VAL   A CB  1 
ATOM   401  C  CG1 . VAL   A 1 65  ? 13.816  22.579 -2.382  1.00 12.80 ? 65  VAL   A CG1 1 
ATOM   402  C  CG2 . VAL   A 1 65  ? 12.952  23.023 -0.087  1.00 11.28 ? 65  VAL   A CG2 1 
ATOM   403  N  N   . GLU   A 1 66  ? 15.065  20.206 1.101   1.00 10.69 ? 66  GLU   A N   1 
ATOM   404  C  CA  . GLU   A 1 66  ? 15.397  19.912 2.486   1.00 10.15 ? 66  GLU   A CA  1 
ATOM   405  C  C   . GLU   A 1 66  ? 14.461  20.760 3.356   1.00 11.26 ? 66  GLU   A C   1 
ATOM   406  O  O   . GLU   A 1 66  ? 14.084  21.893 2.982   1.00 13.62 ? 66  GLU   A O   1 
ATOM   407  C  CB  . GLU   A 1 66  ? 16.829  20.299 2.795   1.00 12.00 ? 66  GLU   A CB  1 
ATOM   408  C  CG  . GLU   A 1 66  ? 17.876  19.485 2.135   1.00 12.36 ? 66  GLU   A CG  1 
ATOM   409  C  CD  . GLU   A 1 66  ? 19.237  19.735 2.784   1.00 12.72 ? 66  GLU   A CD  1 
ATOM   410  O  OE1 . GLU   A 1 66  ? 20.041  20.388 2.186   1.00 12.92 ? 66  GLU   A OE1 1 
ATOM   411  O  OE2 . GLU   A 1 66  ? 19.408  19.275 3.937   1.00 15.45 ? 66  GLU   A OE2 1 
ATOM   412  N  N   . GLY   A 1 67  ? 14.126  20.248 4.524   1.00 10.35 ? 67  GLY   A N   1 
ATOM   413  C  CA  . GLY   A 1 67  ? 13.417  21.006 5.500   1.00 11.67 ? 67  GLY   A CA  1 
ATOM   414  C  C   . GLY   A 1 67  ? 12.871  20.160 6.598   1.00 10.53 ? 67  GLY   A C   1 
ATOM   415  O  O   . GLY   A 1 67  ? 13.031  18.927 6.546   1.00 11.44 ? 67  GLY   A O   1 
ATOM   416  N  N   . ILE   A 1 68  ? 12.230  20.779 7.559   1.00 10.35 ? 68  ILE   A N   1 
ATOM   417  C  CA  . ILE   A 1 68  ? 11.463  20.096 8.559   1.00 10.43 ? 68  ILE   A CA  1 
ATOM   418  C  C   . ILE   A 1 68  ? 10.011  20.226 8.159   1.00 9.59  ? 68  ILE   A C   1 
ATOM   419  O  O   . ILE   A 1 68  ? 9.505   21.319 7.964   1.00 11.44 ? 68  ILE   A O   1 
ATOM   420  C  CB  . ILE   A 1 68  ? 11.694  20.662 9.983   1.00 10.91 ? 68  ILE   A CB  1 
ATOM   421  C  CG1 . ILE   A 1 68  ? 13.199  20.590 10.340  1.00 15.07 ? 68  ILE   A CG1 1 
ATOM   422  C  CG2 . ILE   A 1 68  ? 10.795  19.915 10.947  1.00 13.32 ? 68  ILE   A CG2 1 
ATOM   423  C  CD1 . ILE   A 1 68  ? 13.470  21.178 11.689  1.00 16.39 ? 68  ILE   A CD1 1 
ATOM   424  N  N   . TYR   A 1 69  ? 9.365   19.087 7.933   1.00 10.23 ? 69  TYR   A N   1 
ATOM   425  C  CA  . TYR   A 1 69  ? 8.006   18.998 7.464   1.00 10.12 ? 69  TYR   A CA  1 
ATOM   426  C  C   . TYR   A 1 69  ? 7.070   18.434 8.528   1.00 10.06 ? 69  TYR   A C   1 
ATOM   427  O  O   . TYR   A 1 69  ? 7.468   17.604 9.331   1.00 11.15 ? 69  TYR   A O   1 
ATOM   428  C  CB  . TYR   A 1 69  ? 7.929   18.122 6.191   1.00 10.34 ? 69  TYR   A CB  1 
ATOM   429  C  CG  . TYR   A 1 69  ? 8.604   18.764 5.010   1.00 10.35 ? 69  TYR   A CG  1 
ATOM   430  C  CD1 . TYR   A 1 69  ? 10.005  18.655 4.775   1.00 10.59 ? 69  TYR   A CD1 1 
ATOM   431  C  CD2 . TYR   A 1 69  ? 7.867   19.492 4.071   1.00 10.55 ? 69  TYR   A CD2 1 
ATOM   432  C  CE1 . TYR   A 1 69  ? 10.588  19.245 3.682   1.00 10.48 ? 69  TYR   A CE1 1 
ATOM   433  C  CE2 . TYR   A 1 69  ? 8.481   20.084 2.994   1.00 11.55 ? 69  TYR   A CE2 1 
ATOM   434  C  CZ  . TYR   A 1 69  ? 9.830   19.954 2.797   1.00 10.47 ? 69  TYR   A CZ  1 
ATOM   435  O  OH  . TYR   A 1 69  ? 10.417  20.558 1.690   1.00 12.25 ? 69  TYR   A OH  1 
ATOM   436  N  N   . LYS   A 1 70  ? 5.840   18.934 8.486   1.00 10.16 ? 70  LYS   A N   1 
ATOM   437  C  CA  . LYS   A 1 70  ? 4.760   18.464 9.324   1.00 10.69 ? 70  LYS   A CA  1 
ATOM   438  C  C   . LYS   A 1 70  ? 3.623   17.991 8.454   1.00 10.94 ? 70  LYS   A C   1 
ATOM   439  O  O   . LYS   A 1 70  ? 3.090   18.763 7.666   1.00 12.02 ? 70  LYS   A O   1 
ATOM   440  C  CB  . LYS   A 1 70  ? 4.239   19.569 10.258  1.00 13.38 ? 70  LYS   A CB  1 
ATOM   441  C  CG  . LYS   A 1 70  ? 3.016   19.160 11.001  1.00 15.35 ? 70  LYS   A CG  1 
ATOM   442  C  CD  . LYS   A 1 70  ? 2.769   19.776 12.292  1.00 22.26 ? 70  LYS   A CD  1 
ATOM   443  C  CE  . LYS   A 1 70  ? 2.739   21.204 12.105  1.00 21.56 ? 70  LYS   A CE  1 
ATOM   444  N  NZ  . LYS   A 1 70  ? 2.486   21.775 13.480  1.00 31.30 ? 70  LYS   A NZ  1 
ATOM   445  N  N   . VAL   A 1 71  ? 3.253   16.732 8.597   1.00 12.02 ? 71  VAL   A N   1 
ATOM   446  C  CA  . VAL   A 1 71  ? 2.066   16.195 7.919   1.00 12.43 ? 71  VAL   A CA  1 
ATOM   447  C  C   . VAL   A 1 71  ? 0.985   16.021 8.922   1.00 12.31 ? 71  VAL   A C   1 
ATOM   448  O  O   . VAL   A 1 71  ? 1.148   15.226 9.886   1.00 13.92 ? 71  VAL   A O   1 
ATOM   449  C  CB  . VAL   A 1 71  ? 2.444   14.832 7.256   1.00 13.90 ? 71  VAL   A CB  1 
ATOM   450  C  CG1 . VAL   A 1 71  ? 1.198   14.167 6.681   1.00 15.02 ? 71  VAL   A CG1 1 
ATOM   451  C  CG2 . VAL   A 1 71  ? 3.530   14.991 6.228   1.00 13.64 ? 71  VAL   A CG2 1 
ATOM   452  N  N   . GLU   A 1 72  ? -0.065  16.833 8.796   1.00 12.51 ? 72  GLU   A N   1 
ATOM   453  C  CA  . GLU   A 1 72  ? -1.190  16.846 9.713   1.00 12.63 ? 72  GLU   A CA  1 
ATOM   454  C  C   . GLU   A 1 72  ? -2.405  16.212 9.100   1.00 11.33 ? 72  GLU   A C   1 
ATOM   455  O  O   . GLU   A 1 72  ? -2.981  16.718 8.167   1.00 12.56 ? 72  GLU   A O   1 
ATOM   456  C  CB  . GLU   A 1 72  ? -1.490  18.245 10.083  1.00 15.68 ? 72  GLU   A CB  1 
ATOM   457  C  CG  . GLU   A 1 72  ? -2.211  18.323 11.317  1.00 22.05 ? 72  GLU   A CG  1 
ATOM   458  C  CD  . GLU   A 1 72  ? -2.406  19.822 11.551  1.00 32.20 ? 72  GLU   A CD  1 
ATOM   459  O  OE1 . GLU   A 1 72  ? -3.146  20.417 10.758  1.00 38.80 ? 72  GLU   A OE1 1 
ATOM   460  O  OE2 . GLU   A 1 72  ? -1.725  20.478 12.351  1.00 28.62 ? 72  GLU   A OE2 1 
ATOM   461  N  N   . ILE   A 1 73  ? -2.767  15.047 9.640   1.00 11.80 ? 73  ILE   A N   1 
ATOM   462  C  CA  . ILE   A 1 73  ? -3.872  14.236 9.096   1.00 11.43 ? 73  ILE   A CA  1 
ATOM   463  C  C   . ILE   A 1 73  ? -5.113  14.549 9.938   1.00 11.83 ? 73  ILE   A C   1 
ATOM   464  O  O   . ILE   A 1 73  ? -5.083  14.433 11.164  1.00 13.03 ? 73  ILE   A O   1 
ATOM   465  C  CB  . ILE   A 1 73  ? -3.525  12.738 9.207   1.00 11.85 ? 73  ILE   A CB  1 
ATOM   466  C  CG1 . ILE   A 1 73  ? -2.226  12.382 8.469   1.00 12.59 ? 73  ILE   A CG1 1 
ATOM   467  C  CG2 . ILE   A 1 73  ? -4.703  11.888 8.696   1.00 13.42 ? 73  ILE   A CG2 1 
ATOM   468  C  CD1 . ILE   A 1 73  ? -1.723  10.965 8.686   1.00 16.37 ? 73  ILE   A CD1 1 
ATOM   469  N  N   . ASP   A 1 74  ? -6.160  15.040 9.281   1.00 12.24 ? 74  ASP   A N   1 
ATOM   470  C  CA  . ASP   A 1 74  ? -7.359  15.498 9.976   1.00 13.53 ? 74  ASP   A CA  1 
ATOM   471  C  C   . ASP   A 1 74  ? -8.258  14.324 10.356  1.00 12.86 ? 74  ASP   A C   1 
ATOM   472  O  O   . ASP   A 1 74  ? -9.285  14.074 9.780   1.00 12.92 ? 74  ASP   A O   1 
ATOM   473  C  CB  . ASP   A 1 74  ? -8.121  16.527 9.172   1.00 15.50 ? 74  ASP   A CB  1 
ATOM   474  C  CG  . ASP   A 1 74  ? -9.362  17.057 9.922   1.00 22.60 ? 74  ASP   A CG  1 
ATOM   475  O  OD1 . ASP   A 1 74  ? -9.477  16.798 11.142  1.00 20.53 ? 74  ASP   A OD1 1 
ATOM   476  O  OD2 . ASP   A 1 74  ? -10.177 17.816 9.250   1.00 28.97 ? 74  ASP   A OD2 1 
ATOM   477  N  N   . THR   A 1 75  ? -7.817  13.597 11.361  1.00 11.80 ? 75  THR   A N   1 
ATOM   478  C  CA  . THR   A 1 75  ? -8.546  12.444 11.890  1.00 10.80 ? 75  THR   A CA  1 
ATOM   479  C  C   . THR   A 1 75  ? -9.864  12.855 12.490  1.00 11.75 ? 75  THR   A C   1 
ATOM   480  O  O   . THR   A 1 75  ? -10.831 12.125 12.443  1.00 11.45 ? 75  THR   A O   1 
ATOM   481  C  CB  . THR   A 1 75  ? -7.641  11.715 12.880  1.00 11.58 ? 75  THR   A CB  1 
ATOM   482  O  OG1 . THR   A 1 75  ? -7.306  12.543 13.980  1.00 11.59 ? 75  THR   A OG1 1 
ATOM   483  C  CG2 . THR   A 1 75  ? -6.364  11.177 12.255  1.00 12.15 ? 75  THR   A CG2 1 
ATOM   484  N  N   . LYS   A 1 76  ? -9.908  14.019 13.136  1.00 11.68 ? 76  LYS   A N   1 
ATOM   485  C  CA  . LYS   A 1 76  ? -11.135 14.448 13.789  1.00 13.18 ? 76  LYS   A CA  1 
ATOM   486  C  C   . LYS   A 1 76  ? -12.285 14.597 12.822  1.00 14.04 ? 76  LYS   A C   1 
ATOM   487  O  O   . LYS   A 1 76  ? -13.371 14.117 13.064  1.00 15.44 ? 76  LYS   A O   1 
ATOM   488  C  CB  . LYS   A 1 76  ? -10.896 15.710 14.563  1.00 14.57 ? 76  LYS   A CB  1 
ATOM   489  C  CG  . LYS   A 1 76  ? -12.093 16.135 15.397  1.00 16.24 ? 76  LYS   A CG  1 
ATOM   490  C  CD  . LYS   A 1 76  ? -11.781 17.409 16.192  1.00 18.26 ? 76  LYS   A CD  1 
ATOM   491  C  CE  . LYS   A 1 76  ? -12.916 17.810 17.142  1.00 22.01 ? 76  LYS   A CE  1 
ATOM   492  N  NZ  . LYS   A 1 76  ? -12.558 19.005 17.936  1.00 24.49 ? 76  LYS   A NZ  1 
ATOM   493  N  N   . SER   A 1 77  ? -12.046 15.279 11.721  1.00 15.54 ? 77  SER   A N   1 
ATOM   494  C  CA  . SER   A 1 77  ? -13.158 15.500 10.774  1.00 18.31 ? 77  SER   A CA  1 
ATOM   495  C  C   . SER   A 1 77  ? -13.559 14.166 10.133  1.00 17.86 ? 77  SER   A C   1 
ATOM   496  O  O   . SER   A 1 77  ? -14.715 13.990 9.808   1.00 19.69 ? 77  SER   A O   1 
ATOM   497  C  CB  . SER   A 1 77  ? -12.809 16.505 9.643   1.00 24.18 ? 77  SER   A CB  1 
ATOM   498  O  OG  . SER   A 1 77  ? -12.436 17.780 10.159  1.00 28.70 ? 77  SER   A OG  1 
ATOM   499  N  N   . TYR   A 1 78  ? -12.570 13.276 9.918   1.00 17.92 ? 78  TYR   A N   1 
ATOM   500  C  CA  . TYR   A 1 78  ? -12.858 11.962 9.399   1.00 17.66 ? 78  TYR   A CA  1 
ATOM   501  C  C   . TYR   A 1 78  ? -13.884 11.236 10.271  1.00 17.11 ? 78  TYR   A C   1 
ATOM   502  O  O   . TYR   A 1 78  ? -14.892 10.755 9.775   1.00 17.82 ? 78  TYR   A O   1 
ATOM   503  C  CB  . TYR   A 1 78  ? -11.547 11.151 9.262   1.00 15.01 ? 78  TYR   A CB  1 
ATOM   504  C  CG  . TYR   A 1 78  ? -11.786 9.699  8.832   1.00 15.68 ? 78  TYR   A CG  1 
ATOM   505  C  CD1 . TYR   A 1 78  ? -12.083 9.397  7.515   1.00 15.08 ? 78  TYR   A CD1 1 
ATOM   506  C  CD2 . TYR   A 1 78  ? -11.785 8.659  9.740   1.00 13.93 ? 78  TYR   A CD2 1 
ATOM   507  C  CE1 . TYR   A 1 78  ? -12.329 8.123  7.084   1.00 14.45 ? 78  TYR   A CE1 1 
ATOM   508  C  CE2 . TYR   A 1 78  ? -12.009 7.376  9.323   1.00 13.96 ? 78  TYR   A CE2 1 
ATOM   509  C  CZ  . TYR   A 1 78  ? -12.300 7.082  8.020   1.00 13.48 ? 78  TYR   A CZ  1 
ATOM   510  O  OH  . TYR   A 1 78  ? -12.536 5.823  7.584   1.00 14.68 ? 78  TYR   A OH  1 
ATOM   511  N  N   . TRP   A 1 79  ? -13.634 11.114 11.556  1.00 14.34 ? 79  TRP   A N   1 
ATOM   512  C  CA  . TRP   A 1 79  ? -14.531 10.426 12.420  1.00 13.77 ? 79  TRP   A CA  1 
ATOM   513  C  C   . TRP   A 1 79  ? -15.843 11.130 12.541  1.00 15.74 ? 79  TRP   A C   1 
ATOM   514  O  O   . TRP   A 1 79  ? -16.914 10.520 12.584  1.00 18.15 ? 79  TRP   A O   1 
ATOM   515  C  CB  . TRP   A 1 79  ? -13.911 10.175 13.756  1.00 12.88 ? 79  TRP   A CB  1 
ATOM   516  C  CG  . TRP   A 1 79  ? -12.731 9.213  13.742  1.00 11.78 ? 79  TRP   A CG  1 
ATOM   517  C  CD1 . TRP   A 1 79  ? -11.406 9.476  14.006  1.00 11.23 ? 79  TRP   A CD1 1 
ATOM   518  C  CD2 . TRP   A 1 79  ? -12.790 7.825  13.400  1.00 12.40 ? 79  TRP   A CD2 1 
ATOM   519  N  NE1 . TRP   A 1 79  ? -10.643 8.367  13.848  1.00 11.01 ? 79  TRP   A NE1 1 
ATOM   520  C  CE2 . TRP   A 1 79  ? -11.451 7.329  13.471  1.00 11.14 ? 79  TRP   A CE2 1 
ATOM   521  C  CE3 . TRP   A 1 79  ? -13.792 6.959  13.007  1.00 13.05 ? 79  TRP   A CE3 1 
ATOM   522  C  CZ2 . TRP   A 1 79  ? -11.119 6.018  13.130  1.00 11.81 ? 79  TRP   A CZ2 1 
ATOM   523  C  CZ3 . TRP   A 1 79  ? -13.480 5.645  12.711  1.00 14.82 ? 79  TRP   A CZ3 1 
ATOM   524  C  CH2 . TRP   A 1 79  ? -12.164 5.187  12.778  1.00 12.90 ? 79  TRP   A CH2 1 
ATOM   525  N  N   . LYS   A 1 80  ? -15.771 12.457 12.644  1.00 15.78 ? 80  LYS   A N   1 
ATOM   526  C  CA  . LYS   A 1 80  ? -17.035 13.198 12.809  1.00 20.34 ? 80  LYS   A CA  1 
ATOM   527  C  C   . LYS   A 1 80  ? -17.969 13.010 11.659  1.00 22.24 ? 80  LYS   A C   1 
ATOM   528  O  O   . LYS   A 1 80  ? -19.170 12.952 11.808  1.00 24.28 ? 80  LYS   A O   1 
ATOM   529  C  CB  . LYS   A 1 80  ? -16.764 14.654 13.102  1.00 18.24 ? 80  LYS   A CB  1 
ATOM   530  C  CG  . LYS   A 1 80  ? -16.207 14.821 14.511  1.00 21.35 ? 80  LYS   A CG  1 
ATOM   531  C  CD  . LYS   A 1 80  ? -15.908 16.267 14.898  1.00 25.20 ? 80  LYS   A CD  1 
ATOM   532  N  N   . ALA   A 1 81  ? -17.428 12.941 10.462  1.00 22.56 ? 81  ALA   A N   1 
ATOM   533  C  CA  . ALA   A 1 81  ? -18.214 12.658 9.249   1.00 23.99 ? 81  ALA   A CA  1 
ATOM   534  C  C   . ALA   A 1 81  ? -18.874 11.297 9.263   1.00 28.71 ? 81  ALA   A C   1 
ATOM   535  O  O   . ALA   A 1 81  ? -19.932 11.109 8.634   1.00 43.35 ? 81  ALA   A O   1 
ATOM   536  C  CB  . ALA   A 1 81  ? -17.403 12.890 7.962   1.00 30.88 ? 81  ALA   A CB  1 
ATOM   537  N  N   . LEU   A 1 82  ? -18.287 10.362 9.955   1.00 21.97 ? 82  LEU   A N   1 
ATOM   538  C  CA  . LEU   A 1 82  ? -18.886 9.039  10.135  1.00 23.56 ? 82  LEU   A CA  1 
ATOM   539  C  C   . LEU   A 1 82  ? -19.878 9.034  11.264  1.00 18.45 ? 82  LEU   A C   1 
ATOM   540  O  O   . LEU   A 1 82  ? -20.367 8.002  11.693  1.00 27.93 ? 82  LEU   A O   1 
ATOM   541  C  CB  . LEU   A 1 82  ? -17.789 7.996  10.377  1.00 22.04 ? 82  LEU   A CB  1 
ATOM   542  C  CG  . LEU   A 1 82  ? -16.958 7.845  9.095   1.00 22.30 ? 82  LEU   A CG  1 
ATOM   543  C  CD1 . LEU   A 1 82  ? -15.683 7.058  9.423   1.00 21.63 ? 82  LEU   A CD1 1 
ATOM   544  C  CD2 . LEU   A 1 82  ? -17.782 7.144  8.012   1.00 26.07 ? 82  LEU   A CD2 1 
ATOM   545  N  N   . GLY   A 1 83  ? -20.037 10.222 11.894  1.00 24.69 ? 83  GLY   A N   1 
ATOM   546  C  CA  . GLY   A 1 83  ? -20.966 10.375 13.022  1.00 23.34 ? 83  GLY   A CA  1 
ATOM   547  C  C   . GLY   A 1 83  ? -20.423 9.886  14.334  1.00 20.69 ? 83  GLY   A C   1 
ATOM   548  O  O   . GLY   A 1 83  ? -21.186 9.600  15.276  1.00 29.55 ? 83  GLY   A O   1 
ATOM   549  N  N   . ILE   A 1 84  ? -19.109 9.807  14.406  1.00 21.10 ? 84  ILE   A N   1 
ATOM   550  C  CA  . ILE   A 1 84  ? -18.375 9.332  15.561  1.00 18.62 ? 84  ILE   A CA  1 
ATOM   551  C  C   . ILE   A 1 84  ? -17.639 10.463 16.259  1.00 19.67 ? 84  ILE   A C   1 
ATOM   552  O  O   . ILE   A 1 84  ? -16.982 11.250 15.632  1.00 22.83 ? 84  ILE   A O   1 
ATOM   553  C  CB  . ILE   A 1 84  ? -17.371 8.172  15.158  1.00 18.39 ? 84  ILE   A CB  1 
ATOM   554  C  CG1 . ILE   A 1 84  ? -18.233 6.968  14.627  1.00 21.57 ? 84  ILE   A CG1 1 
ATOM   555  C  CG2 . ILE   A 1 84  ? -16.447 7.825  16.285  1.00 18.72 ? 84  ILE   A CG2 1 
ATOM   556  C  CD1 . ILE   A 1 84  ? -17.418 5.831  14.062  1.00 31.27 ? 84  ILE   A CD1 1 
ATOM   557  N  N   . SER   A 1 85  ? -17.669 10.499 17.584  1.00 16.39 ? 85  SER   A N   1 
ATOM   558  C  CA  A SER   A 1 85  ? -16.904 11.456 18.366  0.50 15.76 ? 85  SER   A CA  1 
ATOM   559  C  CA  B SER   A 1 85  ? -16.904 11.464 18.407  0.50 15.95 ? 85  SER   A CA  1 
ATOM   560  C  C   . SER   A 1 85  ? -15.510 10.910 18.761  1.00 14.85 ? 85  SER   A C   1 
ATOM   561  O  O   . SER   A 1 85  ? -15.341 10.023 19.540  1.00 18.98 ? 85  SER   A O   1 
ATOM   562  C  CB  A SER   A 1 85  ? -17.671 11.827 19.621  0.50 18.75 ? 85  SER   A CB  1 
ATOM   563  C  CB  B SER   A 1 85  ? -17.589 11.734 19.756  0.50 18.87 ? 85  SER   A CB  1 
ATOM   564  O  OG  A SER   A 1 85  ? -16.953 12.851 20.305  0.50 28.31 ? 85  SER   A OG  1 
ATOM   565  O  OG  B SER   A 1 85  ? -18.959 12.041 19.680  0.50 18.89 ? 85  SER   A OG  1 
ATOM   566  N  N   . PRO   A 1 86  ? -14.461 11.436 18.068  1.00 14.59 ? 86  PRO   A N   1 
ATOM   567  C  CA  . PRO   A 1 86  ? -13.159 10.910 18.326  1.00 13.79 ? 86  PRO   A CA  1 
ATOM   568  C  C   . PRO   A 1 86  ? -12.420 11.623 19.373  1.00 14.54 ? 86  PRO   A C   1 
ATOM   569  O  O   . PRO   A 1 86  ? -12.749 12.726 19.808  1.00 14.42 ? 86  PRO   A O   1 
ATOM   570  C  CB  . PRO   A 1 86  ? -12.446 11.164 16.993  1.00 18.25 ? 86  PRO   A CB  1 
ATOM   571  C  CG  . PRO   A 1 86  ? -12.993 12.486 16.580  1.00 19.42 ? 86  PRO   A CG  1 
ATOM   572  C  CD  . PRO   A 1 86  ? -14.433 12.415 17.012  1.00 17.05 ? 86  PRO   A CD  1 
ATOM   573  N  N   . PHE   A 1 87  ? -11.307 11.048 19.809  1.00 12.24 ? 87  PHE   A N   1 
ATOM   574  C  CA  . PHE   A 1 87  ? -10.492 11.621 20.878  1.00 12.71 ? 87  PHE   A CA  1 
ATOM   575  C  C   . PHE   A 1 87  ? -9.547  12.701 20.424  1.00 11.86 ? 87  PHE   A C   1 
ATOM   576  O  O   . PHE   A 1 87  ? -9.457  13.778 21.081  1.00 12.86 ? 87  PHE   A O   1 
ATOM   577  C  CB  . PHE   A 1 87  ? -9.688  10.522 21.541  1.00 12.49 ? 87  PHE   A CB  1 
ATOM   578  C  CG  . PHE   A 1 87  ? -8.915  10.957 22.736  1.00 12.74 ? 87  PHE   A CG  1 
ATOM   579  C  CD1 . PHE   A 1 87  ? -9.564  11.240 23.911  1.00 13.83 ? 87  PHE   A CD1 1 
ATOM   580  C  CD2 . PHE   A 1 87  ? -7.567  11.106 22.659  1.00 15.36 ? 87  PHE   A CD2 1 
ATOM   581  C  CE1 . PHE   A 1 87  ? -8.908  11.688 25.007  1.00 15.64 ? 87  PHE   A CE1 1 
ATOM   582  C  CE2 . PHE   A 1 87  ? -6.896  11.627 23.769  1.00 16.29 ? 87  PHE   A CE2 1 
ATOM   583  C  CZ  . PHE   A 1 87  ? -7.548  11.869 24.960  1.00 16.96 ? 87  PHE   A CZ  1 
ATOM   584  N  N   . HIS   A 1 88  ? -8.716  12.476 19.396  1.00 11.67 ? 88  HIS   A N   1 
ATOM   585  C  CA  . HIS   A 1 88  ? -7.641  13.371 19.027  1.00 10.93 ? 88  HIS   A CA  1 
ATOM   586  C  C   . HIS   A 1 88  ? -8.098  14.466 18.127  1.00 12.83 ? 88  HIS   A C   1 
ATOM   587  O  O   . HIS   A 1 88  ? -9.068  14.349 17.383  1.00 12.87 ? 88  HIS   A O   1 
ATOM   588  C  CB  . HIS   A 1 88  ? -6.502  12.577 18.323  1.00 11.25 ? 88  HIS   A CB  1 
ATOM   589  C  CG  . HIS   A 1 88  ? -5.959  11.494 19.170  1.00 11.65 ? 88  HIS   A CG  1 
ATOM   590  N  ND1 . HIS   A 1 88  ? -6.392  10.181 19.098  1.00 12.35 ? 88  HIS   A ND1 1 
ATOM   591  C  CD2 . HIS   A 1 88  ? -5.001  11.547 20.144  1.00 12.29 ? 88  HIS   A CD2 1 
ATOM   592  C  CE1 . HIS   A 1 88  ? -5.692  9.501  19.968  1.00 12.59 ? 88  HIS   A CE1 1 
ATOM   593  N  NE2 . HIS   A 1 88  ? -4.894  10.301 20.659  1.00 12.95 ? 88  HIS   A NE2 1 
ATOM   594  N  N   . GLU   A 1 89  ? -7.390  15.594 18.185  1.00 11.76 ? 89  GLU   A N   1 
ATOM   595  C  CA  . GLU   A 1 89  ? -7.667  16.687 17.279  1.00 14.09 ? 89  GLU   A CA  1 
ATOM   596  C  C   . GLU   A 1 89  ? -7.161  16.381 15.875  1.00 13.61 ? 89  GLU   A C   1 
ATOM   597  O  O   . GLU   A 1 89  ? -7.751  16.873 14.917  1.00 17.59 ? 89  GLU   A O   1 
ATOM   598  C  CB  . GLU   A 1 89  ? -7.011  17.942 17.809  1.00 15.05 ? 89  GLU   A CB  1 
ATOM   599  C  CG  . GLU   A 1 89  ? -7.678  18.581 18.997  1.00 17.03 ? 89  GLU   A CG  1 
ATOM   600  C  CD  . GLU   A 1 89  ? -9.105  19.057 18.697  1.00 19.83 ? 89  GLU   A CD  1 
ATOM   601  O  OE1 . GLU   A 1 89  ? -9.214  19.973 17.905  1.00 25.97 ? 89  GLU   A OE1 1 
ATOM   602  O  OE2 . GLU   A 1 89  ? -10.043 18.500 19.164  1.00 22.51 ? 89  GLU   A OE2 1 
ATOM   603  N  N   . HIS   A 1 90  ? -6.119  15.606 15.773  1.00 12.07 ? 90  HIS   A N   1 
ATOM   604  C  CA  . HIS   A 1 90  ? -5.427  15.300 14.519  1.00 11.63 ? 90  HIS   A CA  1 
ATOM   605  C  C   . HIS   A 1 90  ? -4.379  14.310 14.828  1.00 12.68 ? 90  HIS   A C   1 
ATOM   606  O  O   . HIS   A 1 90  ? -4.105  14.003 15.987  1.00 12.94 ? 90  HIS   A O   1 
ATOM   607  C  CB  . HIS   A 1 90  ? -4.859  16.565 13.808  1.00 13.51 ? 90  HIS   A CB  1 
ATOM   608  C  CG  . HIS   A 1 90  ? -3.835  17.281 14.628  1.00 14.67 ? 90  HIS   A CG  1 
ATOM   609  N  ND1 . HIS   A 1 90  ? -2.540  16.857 14.827  1.00 22.96 ? 90  HIS   A ND1 1 
ATOM   610  C  CD2 . HIS   A 1 90  ? -3.978  18.373 15.358  1.00 15.86 ? 90  HIS   A CD2 1 
ATOM   611  C  CE1 . HIS   A 1 90  ? -1.903  17.761 15.595  1.00 18.44 ? 90  HIS   A CE1 1 
ATOM   612  N  NE2 . HIS   A 1 90  ? -2.781  18.687 15.897  1.00 21.34 ? 90  HIS   A NE2 1 
ATOM   613  N  N   . ALA   A 1 91  ? -3.696  13.823 13.784  1.00 12.23 ? 91  ALA   A N   1 
ATOM   614  C  CA  . ALA   A 1 91  ? -2.469  13.078 13.959  1.00 13.21 ? 91  ALA   A CA  1 
ATOM   615  C  C   . ALA   A 1 91  ? -1.408  13.806 13.160  1.00 13.64 ? 91  ALA   A C   1 
ATOM   616  O  O   . ALA   A 1 91  ? -1.652  14.149 12.045  1.00 15.02 ? 91  ALA   A O   1 
ATOM   617  C  CB  . ALA   A 1 91  ? -2.649  11.667 13.420  1.00 13.74 ? 91  ALA   A CB  1 
ATOM   618  N  N   . GLU   A 1 92  ? -0.242  14.023 13.748  1.00 15.47 ? 92  GLU   A N   1 
ATOM   619  C  CA  . GLU   A 1 92  ? 0.825   14.725 13.038  1.00 15.22 ? 92  GLU   A CA  1 
ATOM   620  C  C   . GLU   A 1 92  ? 2.078   13.879 12.995  1.00 16.19 ? 92  GLU   A C   1 
ATOM   621  O  O   . GLU   A 1 92  ? 2.436   13.192 13.936  1.00 18.64 ? 92  GLU   A O   1 
ATOM   622  C  CB  . GLU   A 1 92  ? 1.090   16.088 13.580  1.00 18.63 ? 92  GLU   A CB  1 
ATOM   623  C  CG  . GLU   A 1 92  ? 1.562   16.090 15.000  1.00 18.79 ? 92  GLU   A CG  1 
ATOM   624  C  CD  . GLU   A 1 92  ? 1.975   17.453 15.471  0.50 14.99 ? 92  GLU   A CD  1 
ATOM   625  O  OE1 . GLU   A 1 92  ? 1.026   18.286 15.581  0.50 16.64 ? 92  GLU   A OE1 1 
ATOM   626  O  OE2 . GLU   A 1 92  ? 3.208   17.638 15.682  0.50 12.71 ? 92  GLU   A OE2 1 
ATOM   627  N  N   . VAL   A 1 93  ? 2.837   14.029 11.927  1.00 13.46 ? 93  VAL   A N   1 
ATOM   628  C  CA  . VAL   A 1 93  ? 4.117   13.419 11.758  1.00 13.63 ? 93  VAL   A CA  1 
ATOM   629  C  C   . VAL   A 1 93  ? 5.049   14.601 11.403  1.00 12.58 ? 93  VAL   A C   1 
ATOM   630  O  O   . VAL   A 1 93  ? 4.839   15.262 10.368  1.00 16.44 ? 93  VAL   A O   1 
ATOM   631  C  CB  . VAL   A 1 93  ? 3.976   12.374 10.624  1.00 15.56 ? 93  VAL   A CB  1 
ATOM   632  C  CG1 . VAL   A 1 93  ? 5.302   11.740 10.311  1.00 20.52 ? 93  VAL   A CG1 1 
ATOM   633  C  CG2 . VAL   A 1 93  ? 2.940   11.333 10.997  1.00 17.85 ? 93  VAL   A CG2 1 
ATOM   634  N  N   . VAL   A 1 94  ? 6.072   14.799 12.195  1.00 10.99 ? 94  VAL   A N   1 
ATOM   635  C  CA  . VAL   A 1 94  ? 7.059   15.860 11.962  1.00 10.69 ? 94  VAL   A CA  1 
ATOM   636  C  C   . VAL   A 1 94  ? 8.430   15.258 11.777  1.00 10.33 ? 94  VAL   A C   1 
ATOM   637  O  O   . VAL   A 1 94  ? 8.868   14.472 12.627  1.00 10.93 ? 94  VAL   A O   1 
ATOM   638  C  CB  . VAL   A 1 94  ? 7.050   16.855 13.117  1.00 11.75 ? 94  VAL   A CB  1 
ATOM   639  C  CG1 . VAL   A 1 94  ? 8.024   18.018 12.876  1.00 12.49 ? 94  VAL   A CG1 1 
ATOM   640  C  CG2 . VAL   A 1 94  ? 5.640   17.464 13.258  1.00 14.41 ? 94  VAL   A CG2 1 
ATOM   641  N  N   . PHE   A 1 95  ? 9.107   15.593 10.683  1.00 10.06 ? 95  PHE   A N   1 
ATOM   642  C  CA  . PHE   A 1 95  ? 10.363  14.956 10.358  1.00 10.13 ? 95  PHE   A CA  1 
ATOM   643  C  C   . PHE   A 1 95  ? 11.205  15.894 9.512   1.00 9.55  ? 95  PHE   A C   1 
ATOM   644  O  O   . PHE   A 1 95  ? 10.702  16.687 8.734   1.00 10.97 ? 95  PHE   A O   1 
ATOM   645  C  CB  . PHE   A 1 95  ? 10.135  13.620 9.595   1.00 10.83 ? 95  PHE   A CB  1 
ATOM   646  C  CG  . PHE   A 1 95  ? 9.424   13.763 8.261   1.00 10.99 ? 95  PHE   A CG  1 
ATOM   647  C  CD1 . PHE   A 1 95  ? 8.130   13.955 8.225   1.00 13.01 ? 95  PHE   A CD1 1 
ATOM   648  C  CD2 . PHE   A 1 95  ? 10.126  13.683 7.108   1.00 11.91 ? 95  PHE   A CD2 1 
ATOM   649  C  CE1 . PHE   A 1 95  ? 7.457   14.043 6.998   1.00 15.69 ? 95  PHE   A CE1 1 
ATOM   650  C  CE2 . PHE   A 1 95  ? 9.518   13.746 5.898   1.00 14.64 ? 95  PHE   A CE2 1 
ATOM   651  C  CZ  . PHE   A 1 95  ? 8.190   13.929 5.851   1.00 14.98 ? 95  PHE   A CZ  1 
ATOM   652  N  N   . THR   A 1 96  ? 12.506  15.694 9.617   1.00 10.20 ? 96  THR   A N   1 
ATOM   653  C  CA  . THR   A 1 96  ? 13.489  16.328 8.726   1.00 10.94 ? 96  THR   A CA  1 
ATOM   654  C  C   . THR   A 1 96  ? 13.582  15.496 7.452   1.00 10.77 ? 96  THR   A C   1 
ATOM   655  O  O   . THR   A 1 96  ? 13.788  14.275 7.534   1.00 13.68 ? 96  THR   A O   1 
ATOM   656  C  CB  . THR   A 1 96  ? 14.860  16.419 9.379   1.00 12.20 ? 96  THR   A CB  1 
ATOM   657  O  OG1 . THR   A 1 96  ? 14.747  17.182 10.573  1.00 14.06 ? 96  THR   A OG1 1 
ATOM   658  C  CG2 . THR   A 1 96  ? 15.840  17.048 8.440   1.00 13.74 ? 96  THR   A CG2 1 
ATOM   659  N  N   . ALA   A 1 97  ? 13.428  16.110 6.303   1.00 10.81 ? 97  ALA   A N   1 
ATOM   660  C  CA  . ALA   A 1 97  ? 13.451  15.451 5.028   1.00 10.70 ? 97  ALA   A CA  1 
ATOM   661  C  C   . ALA   A 1 97  ? 14.690  15.829 4.223   1.00 11.29 ? 97  ALA   A C   1 
ATOM   662  O  O   . ALA   A 1 97  ? 15.128  16.978 4.243   1.00 11.30 ? 97  ALA   A O   1 
ATOM   663  C  CB  . ALA   A 1 97  ? 12.211  15.830 4.259   1.00 11.84 ? 97  ALA   A CB  1 
ATOM   664  N  N   . ASN   A 1 98  ? 15.187  14.874 3.444   1.00 10.41 ? 98  ASN   A N   1 
ATOM   665  C  CA  . ASN   A 1 98  ? 16.194  15.089 2.435   1.00 11.66 ? 98  ASN   A CA  1 
ATOM   666  C  C   . ASN   A 1 98  ? 17.560  15.544 2.925   1.00 12.57 ? 98  ASN   A C   1 
ATOM   667  O  O   . ASN   A 1 98  ? 18.378  16.037 2.187   1.00 14.36 ? 98  ASN   A O   1 
ATOM   668  C  CB  . ASN   A 1 98  ? 15.646  16.020 1.333   1.00 12.85 ? 98  ASN   A CB  1 
ATOM   669  C  CG  . ASN   A 1 98  ? 14.295  15.614 0.821   1.00 11.76 ? 98  ASN   A CG  1 
ATOM   670  O  OD1 . ASN   A 1 98  ? 13.335  16.461 0.823   1.00 14.22 ? 98  ASN   A OD1 1 
ATOM   671  N  ND2 . ASN   A 1 98  ? 14.133  14.413 0.433   1.00 10.82 ? 98  ASN   A ND2 1 
ATOM   672  N  N   . ASP   A 1 99  ? 17.855  15.278 4.196   1.00 13.51 ? 99  ASP   A N   1 
ATOM   673  C  CA  . ASP   A 1 99  ? 19.108  15.803 4.772   1.00 14.01 ? 99  ASP   A CA  1 
ATOM   674  C  C   . ASP   A 1 99  ? 20.372  15.208 4.185   1.00 15.36 ? 99  ASP   A C   1 
ATOM   675  O  O   . ASP   A 1 99  ? 21.401  15.902 4.096   1.00 16.25 ? 99  ASP   A O   1 
ATOM   676  C  CB  . ASP   A 1 99  ? 19.135  15.796 6.300   1.00 16.88 ? 99  ASP   A CB  1 
ATOM   677  C  CG  . ASP   A 1 99  ? 20.018  17.008 6.929   1.00 28.22 ? 99  ASP   A CG  1 
ATOM   678  O  OD1 . ASP   A 1 99  ? 20.758  17.729 6.177   1.00 23.16 ? 99  ASP   A OD1 1 
ATOM   679  O  OD2 . ASP   A 1 99  ? 19.860  17.380 8.148   1.00 25.72 ? 99  ASP   A OD2 1 
ATOM   680  N  N   . SER   A 1 100 ? 20.308  13.975 3.750   1.00 18.00 ? 100 SER   A N   1 
ATOM   681  C  CA  . SER   A 1 100 ? 21.416  13.283 3.145   1.00 21.12 ? 100 SER   A CA  1 
ATOM   682  C  C   . SER   A 1 100 ? 21.060  13.021 1.655   1.00 19.52 ? 100 SER   A C   1 
ATOM   683  O  O   . SER   A 1 100 ? 21.378  11.997 1.071   1.00 28.34 ? 100 SER   A O   1 
ATOM   684  C  CB  . SER   A 1 100 ? 21.776  11.963 3.981   0.50 42.65 ? 100 SER   A CB  1 
ATOM   685  N  N   . GLY   A 1 101 ? 20.385  13.964 1.015   1.00 18.35 ? 101 GLY   A N   1 
ATOM   686  C  CA  . GLY   A 1 101 ? 19.967  13.885 -0.361  1.00 18.38 ? 101 GLY   A CA  1 
ATOM   687  C  C   . GLY   A 1 101 ? 18.487  13.516 -0.499  1.00 15.77 ? 101 GLY   A C   1 
ATOM   688  O  O   . GLY   A 1 101 ? 17.846  13.124 0.433   1.00 15.80 ? 101 GLY   A O   1 
ATOM   689  N  N   . PRO   A 1 102 ? 17.935  13.664 -1.721  1.00 16.65 ? 102 PRO   A N   1 
ATOM   690  C  CA  . PRO   A 1 102 ? 16.532  13.379 -1.924  1.00 14.13 ? 102 PRO   A CA  1 
ATOM   691  C  C   . PRO   A 1 102 ? 16.113  11.987 -1.568  1.00 14.68 ? 102 PRO   A C   1 
ATOM   692  O  O   . PRO   A 1 102 ? 16.806  11.028 -1.928  1.00 16.10 ? 102 PRO   A O   1 
ATOM   693  C  CB  . PRO   A 1 102 ? 16.303  13.634 -3.409  1.00 17.11 ? 102 PRO   A CB  1 
ATOM   694  C  CG  . PRO   A 1 102 ? 17.376  14.538 -3.797  1.00 21.86 ? 102 PRO   A CG  1 
ATOM   695  C  CD  . PRO   A 1 102 ? 18.536  14.215 -2.955  1.00 17.31 ? 102 PRO   A CD  1 
ATOM   696  N  N   . ARG   A 1 103 ? 14.990  11.854 -0.873  1.00 14.17 ? 103 ARG   A N   1 
ATOM   697  C  CA  . ARG   A 1 103 ? 14.336  10.558 -0.615  1.00 12.99 ? 103 ARG   A CA  1 
ATOM   698  C  C   . ARG   A 1 103 ? 12.904  10.626 -0.956  1.00 13.97 ? 103 ARG   A C   1 
ATOM   699  O  O   . ARG   A 1 103 ? 12.334  11.735 -1.040  1.00 14.49 ? 103 ARG   A O   1 
ATOM   700  C  CB  . ARG   A 1 103 ? 14.551  10.129 0.810   1.00 14.20 ? 103 ARG   A CB  1 
ATOM   701  C  CG  . ARG   A 1 103 ? 15.979  9.975  1.310   1.00 15.72 ? 103 ARG   A CG  1 
ATOM   702  C  CD  . ARG   A 1 103 ? 16.667  8.746  0.705   1.00 17.34 ? 103 ARG   A CD  1 
ATOM   703  N  NE  . ARG   A 1 103 ? 18.036  8.552  1.237   1.00 21.83 ? 103 ARG   A NE  1 
ATOM   704  C  CZ  . ARG   A 1 103 ? 19.095  9.231  0.832   1.00 23.71 ? 103 ARG   A CZ  1 
ATOM   705  N  NH1 . ARG   A 1 103 ? 19.024  10.041 -0.185  1.00 23.02 ? 103 ARG   A NH1 1 
ATOM   706  N  NH2 . ARG   A 1 103 ? 20.270  9.037  1.420   1.00 28.52 ? 103 ARG   A NH2 1 
ATOM   707  N  N   . ARG   A 1 104 ? 12.254  9.469  -1.079  1.00 14.09 ? 104 ARG   A N   1 
ATOM   708  C  CA  . ARG   A 1 104 ? 10.826  9.383  -1.210  1.00 12.71 ? 104 ARG   A CA  1 
ATOM   709  C  C   . ARG   A 1 104 ? 10.255  8.902  0.134   1.00 11.84 ? 104 ARG   A C   1 
ATOM   710  O  O   . ARG   A 1 104 ? 10.782  7.966  0.729   1.00 13.47 ? 104 ARG   A O   1 
ATOM   711  C  CB  . ARG   A 1 104 ? 10.458  8.450  -2.323  1.00 15.54 ? 104 ARG   A CB  1 
ATOM   712  C  CG  . ARG   A 1 104 ? 10.940  8.865  -3.673  1.00 21.34 ? 104 ARG   A CG  1 
ATOM   713  C  CD  . ARG   A 1 104 ? 10.271  8.032  -4.786  1.00 28.40 ? 104 ARG   A CD  1 
ATOM   714  N  N   . TYR   A 1 105 ? 9.200   9.535  0.575   1.00 10.90 ? 105 TYR   A N   1 
ATOM   715  C  CA  . TYR   A 1 105 ? 8.601   9.310  1.868   1.00 10.08 ? 105 TYR   A CA  1 
ATOM   716  C  C   . TYR   A 1 105 ? 7.168   8.919  1.710   1.00 9.95  ? 105 TYR   A C   1 
ATOM   717  O  O   . TYR   A 1 105 ? 6.379   9.619  1.092   1.00 12.16 ? 105 TYR   A O   1 
ATOM   718  C  CB  . TYR   A 1 105 ? 8.641   10.568 2.740   1.00 10.67 ? 105 TYR   A CB  1 
ATOM   719  C  CG  . TYR   A 1 105 ? 10.040  11.037 3.017   1.00 10.20 ? 105 TYR   A CG  1 
ATOM   720  C  CD1 . TYR   A 1 105 ? 10.712  11.875 2.114   1.00 11.16 ? 105 TYR   A CD1 1 
ATOM   721  C  CD2 . TYR   A 1 105 ? 10.719  10.634 4.170   1.00 10.99 ? 105 TYR   A CD2 1 
ATOM   722  C  CE1 . TYR   A 1 105 ? 12.024  12.293 2.354   1.00 11.59 ? 105 TYR   A CE1 1 
ATOM   723  C  CE2 . TYR   A 1 105 ? 11.991  11.080 4.414   1.00 11.55 ? 105 TYR   A CE2 1 
ATOM   724  C  CZ  . TYR   A 1 105 ? 12.663  11.909 3.492   1.00 10.92 ? 105 TYR   A CZ  1 
ATOM   725  O  OH  . TYR   A 1 105 ? 13.969  12.288 3.689   1.00 12.39 ? 105 TYR   A OH  1 
ATOM   726  N  N   . THR   A 1 106 ? 6.782   7.786  2.314   1.00 10.25 ? 106 THR   A N   1 
ATOM   727  C  CA  . THR   A 1 106 ? 5.386   7.412  2.468   1.00 10.70 ? 106 THR   A CA  1 
ATOM   728  C  C   . THR   A 1 106 ? 5.063   7.431  3.949   1.00 9.93  ? 106 THR   A C   1 
ATOM   729  O  O   . THR   A 1 106 ? 5.754   6.810  4.730   1.00 11.63 ? 106 THR   A O   1 
ATOM   730  C  CB  . THR   A 1 106 ? 5.097   6.001  1.912   1.00 12.44 ? 106 THR   A CB  1 
ATOM   731  O  OG1 . THR   A 1 106 ? 5.303   6.019  0.506   1.00 15.24 ? 106 THR   A OG1 1 
ATOM   732  C  CG2 . THR   A 1 106 ? 3.682   5.542  2.236   1.00 14.56 ? 106 THR   A CG2 1 
ATOM   733  N  N   . ILE   A 1 107 ? 4.051   8.184  4.327   1.00 10.12 ? 107 ILE   A N   1 
ATOM   734  C  CA  . ILE   A 1 107 ? 3.555   8.218  5.682   1.00 10.19 ? 107 ILE   A CA  1 
ATOM   735  C  C   . ILE   A 1 107 ? 2.272   7.387  5.693   1.00 10.76 ? 107 ILE   A C   1 
ATOM   736  O  O   . ILE   A 1 107 ? 1.310   7.737  5.038   1.00 11.34 ? 107 ILE   A O   1 
ATOM   737  C  CB  . ILE   A 1 107 ? 3.251   9.640  6.121   1.00 12.03 ? 107 ILE   A CB  1 
ATOM   738  C  CG1 . ILE   A 1 107 ? 4.470   10.554 5.973   1.00 13.24 ? 107 ILE   A CG1 1 
ATOM   739  C  CG2 . ILE   A 1 107 ? 2.697   9.625  7.550   1.00 14.56 ? 107 ILE   A CG2 1 
ATOM   740  C  CD1 . ILE   A 1 107 ? 5.749   10.084 6.654   1.00 15.10 ? 107 ILE   A CD1 1 
ATOM   741  N  N   . ALA   A 1 108 ? 2.304   6.257  6.403   1.00 10.94 ? 108 ALA   A N   1 
ATOM   742  C  CA  . ALA   A 1 108 ? 1.212   5.322  6.475   1.00 12.50 ? 108 ALA   A CA  1 
ATOM   743  C  C   . ALA   A 1 108 ? 0.579   5.444  7.864   1.00 12.56 ? 108 ALA   A C   1 
ATOM   744  O  O   . ALA   A 1 108 ? 1.297   5.428  8.848   1.00 16.67 ? 108 ALA   A O   1 
ATOM   745  C  CB  . ALA   A 1 108 ? 1.681   3.898  6.174   1.00 15.30 ? 108 ALA   A CB  1 
ATOM   746  N  N   . ALA   A 1 109 ? -0.715  5.520  7.929   1.00 11.97 ? 109 ALA   A N   1 
ATOM   747  C  CA  . ALA   A 1 109 ? -1.445  5.711  9.197   1.00 10.72 ? 109 ALA   A CA  1 
ATOM   748  C  C   . ALA   A 1 109 ? -2.581  4.731  9.312   1.00 9.99  ? 109 ALA   A C   1 
ATOM   749  O  O   . ALA   A 1 109 ? -3.206  4.351  8.342   1.00 12.33 ? 109 ALA   A O   1 
ATOM   750  C  CB  . ALA   A 1 109 ? -1.974  7.091  9.280   1.00 12.64 ? 109 ALA   A CB  1 
ATOM   751  N  N   . LEU   A 1 110 ? -2.834  4.317  10.541  1.00 9.26  ? 110 LEU   A N   1 
ATOM   752  C  CA  . LEU   A 1 110 ? -3.928  3.401  10.906  1.00 8.49  ? 110 LEU   A CA  1 
ATOM   753  C  C   . LEU   A 1 110 ? -4.737  4.071  11.998  1.00 8.13  ? 110 LEU   A C   1 
ATOM   754  O  O   . LEU   A 1 110 ? -4.182  4.412  13.018  1.00 9.77  ? 110 LEU   A O   1 
ATOM   755  C  CB  . LEU   A 1 110 ? -3.357  2.061  11.399  1.00 8.95  ? 110 LEU   A CB  1 
ATOM   756  C  CG  . LEU   A 1 110 ? -4.390  1.030  11.790  1.00 9.65  ? 110 LEU   A CG  1 
ATOM   757  C  CD1 . LEU   A 1 110 ? -5.277  0.669  10.611  1.00 9.66  ? 110 LEU   A CD1 1 
ATOM   758  C  CD2 . LEU   A 1 110 ? -3.716  -0.200 12.383  1.00 11.82 ? 110 LEU   A CD2 1 
ATOM   759  N  N   . LEU   A 1 111 ? -6.030  4.248  11.793  1.00 7.98  ? 111 LEU   A N   1 
ATOM   760  C  CA  . LEU   A 1 111 ? -6.859  5.036  12.683  1.00 8.65  ? 111 LEU   A CA  1 
ATOM   761  C  C   . LEU   A 1 111 ? -7.950  4.214  13.391  1.00 8.26  ? 111 LEU   A C   1 
ATOM   762  O  O   . LEU   A 1 111 ? -8.662  3.412  12.786  1.00 9.39  ? 111 LEU   A O   1 
ATOM   763  C  CB  . LEU   A 1 111 ? -7.606  6.102  11.873  1.00 9.37  ? 111 LEU   A CB  1 
ATOM   764  C  CG  . LEU   A 1 111 ? -6.802  7.020  10.971  1.00 9.33  ? 111 LEU   A CG  1 
ATOM   765  C  CD1 . LEU   A 1 111 ? -7.704  8.064  10.361  1.00 10.78 ? 111 LEU   A CD1 1 
ATOM   766  C  CD2 . LEU   A 1 111 ? -5.647  7.663  11.704  1.00 10.01 ? 111 LEU   A CD2 1 
ATOM   767  N  N   . SER   A 1 112 ? -8.146  4.544  14.654  1.00 9.35  ? 112 SER   A N   1 
ATOM   768  C  CA  . SER   A 1 112 ? -9.317  4.187  15.425  1.00 10.04 ? 112 SER   A CA  1 
ATOM   769  C  C   . SER   A 1 112 ? -9.759  5.437  16.177  1.00 10.33 ? 112 SER   A C   1 
ATOM   770  O  O   . SER   A 1 112 ? -9.053  6.408  16.301  1.00 10.58 ? 112 SER   A O   1 
ATOM   771  C  CB  . SER   A 1 112 ? -8.997  3.077  16.422  1.00 11.12 ? 112 SER   A CB  1 
ATOM   772  O  OG  . SER   A 1 112 ? -8.514  1.897  15.790  1.00 13.80 ? 112 SER   A OG  1 
ATOM   773  N  N   . PRO   A 1 113 ? -11.001 5.404  16.729  1.00 10.45 ? 113 PRO   A N   1 
ATOM   774  C  CA  . PRO   A 1 113 ? -11.504 6.662  17.335  1.00 11.25 ? 113 PRO   A CA  1 
ATOM   775  C  C   . PRO   A 1 113 ? -10.656 7.181  18.461  1.00 12.16 ? 113 PRO   A C   1 
ATOM   776  O  O   . PRO   A 1 113 ? -10.574 8.429  18.642  1.00 12.37 ? 113 PRO   A O   1 
ATOM   777  C  CB  . PRO   A 1 113 ? -12.910 6.245  17.782  1.00 13.21 ? 113 PRO   A CB  1 
ATOM   778  C  CG  . PRO   A 1 113 ? -13.344 5.292  16.723  1.00 14.88 ? 113 PRO   A CG  1 
ATOM   779  C  CD  . PRO   A 1 113 ? -12.119 4.461  16.482  1.00 12.33 ? 113 PRO   A CD  1 
ATOM   780  N  N   . TYR   A 1 114 ? -10.045 6.313  19.254  1.00 10.31 ? 114 TYR   A N   1 
ATOM   781  C  CA  . TYR   A 1 114 ? -9.211  6.709  20.409  1.00 11.67 ? 114 TYR   A CA  1 
ATOM   782  C  C   . TYR   A 1 114 ? -7.733  6.366  20.228  1.00 12.05 ? 114 TYR   A C   1 
ATOM   783  O  O   . TYR   A 1 114 ? -6.953  6.453  21.174  1.00 12.68 ? 114 TYR   A O   1 
ATOM   784  C  CB  . TYR   A 1 114 ? -9.733  6.136  21.745  1.00 11.94 ? 114 TYR   A CB  1 
ATOM   785  C  CG  . TYR   A 1 114 ? -10.916 6.838  22.279  1.00 11.52 ? 114 TYR   A CG  1 
ATOM   786  C  CD1 . TYR   A 1 114 ? -12.160 6.635  21.747  1.00 15.17 ? 114 TYR   A CD1 1 
ATOM   787  C  CD2 . TYR   A 1 114 ? -10.831 7.676  23.379  1.00 12.62 ? 114 TYR   A CD2 1 
ATOM   788  C  CE1 . TYR   A 1 114 ? -13.308 7.225  22.218  1.00 20.19 ? 114 TYR   A CE1 1 
ATOM   789  C  CE2 . TYR   A 1 114 ? -11.976 8.321  23.887  1.00 14.16 ? 114 TYR   A CE2 1 
ATOM   790  C  CZ  . TYR   A 1 114 ? -13.209 8.098  23.315  1.00 17.48 ? 114 TYR   A CZ  1 
ATOM   791  O  OH  . TYR   A 1 114 ? -14.329 8.717  23.811  1.00 22.59 ? 114 TYR   A OH  1 
ATOM   792  N  N   . SER   A 1 115 ? -7.277  6.103  18.988  1.00 11.69 ? 115 SER   A N   1 
ATOM   793  C  CA  . SER   A 1 115 ? -5.927  5.676  18.771  1.00 11.16 ? 115 SER   A CA  1 
ATOM   794  C  C   . SER   A 1 115 ? -5.492  5.937  17.359  1.00 11.89 ? 115 SER   A C   1 
ATOM   795  O  O   . SER   A 1 115 ? -6.300  5.842  16.436  1.00 14.33 ? 115 SER   A O   1 
ATOM   796  C  CB  . SER   A 1 115 ? -5.771  4.227  19.168  1.00 13.54 ? 115 SER   A CB  1 
ATOM   797  O  OG  . SER   A 1 115 ? -4.483  3.715  19.054  1.00 18.26 ? 115 SER   A OG  1 
ATOM   798  N  N   . TYR   A 1 116 ? -4.199  6.199  17.146  1.00 10.69 ? 116 TYR   A N   1 
ATOM   799  C  CA  . TYR   A 1 116 ? -3.664  6.174  15.777  1.00 10.78 ? 116 TYR   A CA  1 
ATOM   800  C  C   . TYR   A 1 116 ? -2.238  5.679  15.834  1.00 9.34  ? 116 TYR   A C   1 
ATOM   801  O  O   . TYR   A 1 116 ? -1.553  5.825  16.826  1.00 9.89  ? 116 TYR   A O   1 
ATOM   802  C  CB  . TYR   A 1 116 ? -3.795  7.527  15.063  1.00 12.55 ? 116 TYR   A CB  1 
ATOM   803  C  CG  . TYR   A 1 116 ? -3.009  8.625  15.692  1.00 11.27 ? 116 TYR   A CG  1 
ATOM   804  C  CD1 . TYR   A 1 116 ? -1.665  8.824  15.409  1.00 12.45 ? 116 TYR   A CD1 1 
ATOM   805  C  CD2 . TYR   A 1 116 ? -3.617  9.465  16.590  1.00 13.07 ? 116 TYR   A CD2 1 
ATOM   806  C  CE1 . TYR   A 1 116 ? -0.973  9.884  16.016  1.00 13.09 ? 116 TYR   A CE1 1 
ATOM   807  C  CE2 . TYR   A 1 116 ? -2.952  10.482 17.204  1.00 14.22 ? 116 TYR   A CE2 1 
ATOM   808  C  CZ  . TYR   A 1 116 ? -1.622  10.659 16.957  1.00 13.07 ? 116 TYR   A CZ  1 
ATOM   809  O  OH  . TYR   A 1 116 ? -0.963  11.692 17.630  1.00 16.06 ? 116 TYR   A OH  1 
ATOM   810  N  N   . SER   A 1 117 ? -1.800  5.136  14.710  1.00 10.02 ? 117 SER   A N   1 
ATOM   811  C  CA  . SER   A 1 117 ? -0.424  4.689  14.532  1.00 10.76 ? 117 SER   A CA  1 
ATOM   812  C  C   . SER   A 1 117 ? 0.028   5.217  13.198  1.00 10.26 ? 117 SER   A C   1 
ATOM   813  O  O   . SER   A 1 117 ? -0.693  5.172  12.227  1.00 10.81 ? 117 SER   A O   1 
ATOM   814  C  CB  . SER   A 1 117 ? -0.355  3.201  14.556  1.00 11.76 ? 117 SER   A CB  1 
ATOM   815  O  OG  . SER   A 1 117 ? 0.936   2.729  14.297  1.00 14.08 ? 117 SER   A OG  1 
ATOM   816  N  N   . THR   A 1 118 ? 1.277   5.641  13.174  1.00 10.53 ? 118 THR   A N   1 
ATOM   817  C  CA  A THR   A 1 118 ? 1.888   6.037  11.942  0.50 11.52 ? 118 THR   A CA  1 
ATOM   818  C  CA  B THR   A 1 118 ? 1.896   5.999  11.835  0.50 11.43 ? 118 THR   A CA  1 
ATOM   819  C  C   . THR   A 1 118 ? 3.292   5.394  11.757  1.00 10.37 ? 118 THR   A C   1 
ATOM   820  O  O   . THR   A 1 118 ? 3.987   5.183  12.745  1.00 11.21 ? 118 THR   A O   1 
ATOM   821  C  CB  A THR   A 1 118 ? 1.927   7.588  11.937  0.50 15.83 ? 118 THR   A CB  1 
ATOM   822  C  CB  B THR   A 1 118 ? 2.013   7.517  11.430  0.50 12.45 ? 118 THR   A CB  1 
ATOM   823  O  OG1 A THR   A 1 118 ? 2.347   7.980  10.699  0.50 16.26 ? 118 THR   A OG1 1 
ATOM   824  O  OG1 B THR   A 1 118 ? 3.114   8.094  12.104  0.50 13.30 ? 118 THR   A OG1 1 
ATOM   825  C  CG2 A THR   A 1 118 ? 2.917   8.239  12.860  0.50 20.73 ? 118 THR   A CG2 1 
ATOM   826  C  CG2 B THR   A 1 118 ? 0.708   8.279  11.722  0.50 9.81  ? 118 THR   A CG2 1 
ATOM   827  N  N   . THR   A 1 119 ? 3.640   5.106  10.517  1.00 10.07 ? 119 THR   A N   1 
ATOM   828  C  CA  . THR   A 1 119 ? 4.986   4.701  10.183  1.00 10.37 ? 119 THR   A CA  1 
ATOM   829  C  C   . THR   A 1 119 ? 5.456   5.420  8.940   1.00 9.35  ? 119 THR   A C   1 
ATOM   830  O  O   . THR   A 1 119 ? 4.644   5.876  8.155   1.00 11.71 ? 119 THR   A O   1 
ATOM   831  C  CB  . THR   A 1 119 ? 5.137   3.126  10.066  1.00 10.52 ? 119 THR   A CB  1 
ATOM   832  O  OG1 . THR   A 1 119 ? 6.520   2.779  10.172  1.00 11.12 ? 119 THR   A OG1 1 
ATOM   833  C  CG2 . THR   A 1 119 ? 4.548   2.611  8.825   1.00 12.35 ? 119 THR   A CG2 1 
ATOM   834  N  N   . ALA   A 1 120 ? 6.744   5.483  8.787   1.00 9.64  ? 120 ALA   A N   1 
ATOM   835  C  CA  . ALA   A 1 120 ? 7.348   6.072  7.573   1.00 9.84  ? 120 ALA   A CA  1 
ATOM   836  C  C   . ALA   A 1 120 ? 8.082   5.000  6.819   1.00 9.83  ? 120 ALA   A C   1 
ATOM   837  O  O   . ALA   A 1 120 ? 8.795   4.177  7.384   1.00 11.10 ? 120 ALA   A O   1 
ATOM   838  C  CB  . ALA   A 1 120 ? 8.295   7.182  7.946   1.00 11.64 ? 120 ALA   A CB  1 
ATOM   839  N  N   . VAL   A 1 121 ? 7.931   5.056  5.489   1.00 9.98  ? 121 VAL   A N   1 
ATOM   840  C  CA  . VAL   A 1 121 ? 8.674   4.245  4.539   1.00 10.37 ? 121 VAL   A CA  1 
ATOM   841  C  C   . VAL   A 1 121 ? 9.546   5.195  3.743   1.00 10.25 ? 121 VAL   A C   1 
ATOM   842  O  O   . VAL   A 1 121 ? 8.979   6.056  3.037   1.00 12.89 ? 121 VAL   A O   1 
ATOM   843  C  CB  . VAL   A 1 121 ? 7.773   3.409  3.646   1.00 11.69 ? 121 VAL   A CB  1 
ATOM   844  C  CG1 . VAL   A 1 121 ? 8.594   2.552  2.748   1.00 15.35 ? 121 VAL   A CG1 1 
ATOM   845  C  CG2 . VAL   A 1 121 ? 6.806   2.593  4.436   1.00 17.16 ? 121 VAL   A CG2 1 
ATOM   846  N  N   . VAL   A 1 122 ? 10.857  5.110  3.862   1.00 11.06 ? 122 VAL   A N   1 
ATOM   847  C  CA  . VAL   A 1 122 ? 11.774  6.040  3.239   1.00 11.61 ? 122 VAL   A CA  1 
ATOM   848  C  C   . VAL   A 1 122 ? 12.602  5.272  2.271   1.00 14.12 ? 122 VAL   A C   1 
ATOM   849  O  O   . VAL   A 1 122 ? 13.287  4.318  2.652   1.00 14.82 ? 122 VAL   A O   1 
ATOM   850  C  CB  . VAL   A 1 122 ? 12.650  6.696  4.295   1.00 14.47 ? 122 VAL   A CB  1 
ATOM   851  C  CG1 . VAL   A 1 122 ? 13.587  7.723  3.642   1.00 15.74 ? 122 VAL   A CG1 1 
ATOM   852  C  CG2 . VAL   A 1 122 ? 11.853  7.350  5.393   1.00 14.29 ? 122 VAL   A CG2 1 
ATOM   853  N  N   . THR   A 1 123 ? 12.576  5.678  1.006   1.00 13.19 ? 123 THR   A N   1 
ATOM   854  C  CA  . THR   A 1 123 ? 13.360  4.978  -0.019  1.00 15.47 ? 123 THR   A CA  1 
ATOM   855  C  C   . THR   A 1 123 ? 14.236  5.937  -0.778  1.00 16.07 ? 123 THR   A C   1 
ATOM   856  O  O   . THR   A 1 123 ? 13.970  7.153  -0.828  1.00 16.60 ? 123 THR   A O   1 
ATOM   857  C  CB  . THR   A 1 123 ? 12.425  4.226  -0.943  1.00 20.53 ? 123 THR   A CB  1 
ATOM   858  O  OG1 . THR   A 1 123 ? 11.608  5.099  -1.652  1.00 27.30 ? 123 THR   A OG1 1 
ATOM   859  C  CG2 . THR   A 1 123 ? 11.530  3.355  -0.200  1.00 24.12 ? 123 THR   A CG2 1 
ATOM   860  N  N   . ASN   A 1 124 ? 15.262  5.417  -1.374  1.00 21.54 ? 124 ASN   A N   1 
ATOM   861  C  CA  . ASN   A 1 124 ? 16.255  6.212  -2.087  1.00 21.14 ? 124 ASN   A CA  1 
ATOM   862  C  C   . ASN   A 1 124 ? 16.007  5.976  -3.571  1.00 38.49 ? 124 ASN   A C   1 
ATOM   863  O  O   . ASN   A 1 124 ? 15.554  6.933  -4.279  1.00 37.42 ? 124 ASN   A O   1 
ATOM   864  C  CB  . ASN   A 1 124 ? 17.678  5.810  -1.642  1.00 27.16 ? 124 ASN   A CB  1 
ATOM   865  C  CG  . ASN   A 1 124 ? 18.708  6.751  -2.202  1.00 28.62 ? 124 ASN   A CG  1 
ATOM   866  O  OD1 . ASN   A 1 124 ? 18.415  7.457  -3.168  1.00 28.86 ? 124 ASN   A OD1 1 
ATOM   867  N  ND2 . ASN   A 1 124 ? 19.885  6.798  -1.605  1.00 34.22 ? 124 ASN   A ND2 1 
ATOM   868  N  N   . PRO   B 1 11  ? -5.365  13.054 37.275  1.00 25.15 ? 11  PRO   B N   1 
ATOM   869  C  CA  . PRO   B 1 11  ? -6.232  13.250 36.126  1.00 23.35 ? 11  PRO   B CA  1 
ATOM   870  C  C   . PRO   B 1 11  ? -5.535  12.990 34.775  1.00 20.46 ? 11  PRO   B C   1 
ATOM   871  O  O   . PRO   B 1 11  ? -6.213  12.721 33.824  1.00 21.54 ? 11  PRO   B O   1 
ATOM   872  C  CB  . PRO   B 1 11  ? -6.619  14.718 36.163  1.00 35.80 ? 11  PRO   B CB  1 
ATOM   873  C  CG  . PRO   B 1 11  ? -5.753  15.302 37.218  1.00 34.21 ? 11  PRO   B CG  1 
ATOM   874  C  CD  . PRO   B 1 11  ? -5.201  14.264 38.071  1.00 30.24 ? 11  PRO   B CD  1 
ATOM   875  N  N   . LEU   B 1 12  ? -4.209  13.167 34.708  1.00 19.98 ? 12  LEU   B N   1 
ATOM   876  C  CA  . LEU   B 1 12  ? -3.453  12.982 33.445  1.00 18.49 ? 12  LEU   B CA  1 
ATOM   877  C  C   . LEU   B 1 12  ? -2.238  12.212 33.709  1.00 16.70 ? 12  LEU   B C   1 
ATOM   878  O  O   . LEU   B 1 12  ? -1.395  12.631 34.505  1.00 22.62 ? 12  LEU   B O   1 
ATOM   879  C  CB  . LEU   B 1 12  ? -3.098  14.355 32.847  1.00 19.41 ? 12  LEU   B CB  1 
ATOM   880  C  CG  . LEU   B 1 12  ? -2.362  14.329 31.505  1.00 18.54 ? 12  LEU   B CG  1 
ATOM   881  C  CD1 . LEU   B 1 12  ? -3.226  13.716 30.416  1.00 20.88 ? 12  LEU   B CD1 1 
ATOM   882  C  CD2 . LEU   B 1 12  ? -1.991  15.757 31.106  1.00 21.73 ? 12  LEU   B CD2 1 
ATOM   883  N  N   . MET   B 1 13  ? -2.066  11.108 33.008  1.00 17.03 ? 13  MET   B N   1 
ATOM   884  C  CA  . MET   B 1 13  ? -0.870  10.276 33.080  1.00 16.07 ? 13  MET   B CA  1 
ATOM   885  C  C   . MET   B 1 13  ? -0.356  9.999  31.663  1.00 13.86 ? 13  MET   B C   1 
ATOM   886  O  O   . MET   B 1 13  ? -1.166  9.859  30.758  1.00 13.97 ? 13  MET   B O   1 
ATOM   887  C  CB  . MET   B 1 13  ? -1.114  8.964  33.826  1.00 21.50 ? 13  MET   B CB  1 
ATOM   888  C  CG  . MET   B 1 13  ? 0.190   8.120  34.139  1.00 24.00 ? 13  MET   B CG  1 
ATOM   889  S  SD  . MET   B 1 13  ? 0.769   6.918  32.937  1.00 26.28 ? 13  MET   B SD  1 
ATOM   890  C  CE  . MET   B 1 13  ? -0.283  5.509  33.394  1.00 29.78 ? 13  MET   B CE  1 
ATOM   891  N  N   . VAL   B 1 14  ? 0.942   9.925  31.504  1.00 13.13 ? 14  VAL   B N   1 
ATOM   892  C  CA  . VAL   B 1 14  ? 1.585   9.601  30.202  1.00 13.97 ? 14  VAL   B CA  1 
ATOM   893  C  C   . VAL   B 1 14  ? 2.395   8.352  30.416  1.00 13.87 ? 14  VAL   B C   1 
ATOM   894  O  O   . VAL   B 1 14  ? 3.171   8.278  31.359  1.00 16.88 ? 14  VAL   B O   1 
ATOM   895  C  CB  . VAL   B 1 14  ? 2.427   10.759 29.667  1.00 14.12 ? 14  VAL   B CB  1 
ATOM   896  C  CG1 . VAL   B 1 14  ? 3.072   10.376 28.328  1.00 15.51 ? 14  VAL   B CG1 1 
ATOM   897  C  CG2 . VAL   B 1 14  ? 1.560   11.965 29.485  1.00 14.35 ? 14  VAL   B CG2 1 
ATOM   898  N  N   . LYS   B 1 15  ? 2.288   7.405  29.534  1.00 14.00 ? 15  LYS   B N   1 
ATOM   899  C  CA  . LYS   B 1 15  ? 3.048   6.195  29.594  1.00 14.50 ? 15  LYS   B CA  1 
ATOM   900  C  C   . LYS   B 1 15  ? 3.697   5.932  28.236  1.00 15.44 ? 15  LYS   B C   1 
ATOM   901  O  O   . LYS   B 1 15  ? 3.010   6.028  27.221  1.00 15.56 ? 15  LYS   B O   1 
ATOM   902  C  CB  . LYS   B 1 15  ? 2.170   5.031  29.934  1.00 17.55 ? 15  LYS   B CB  1 
ATOM   903  C  CG  . LYS   B 1 15  ? 2.974   3.797  30.071  1.00 22.11 ? 15  LYS   B CG  1 
ATOM   904  C  CD  . LYS   B 1 15  ? 2.222   2.701  30.763  1.00 28.98 ? 15  LYS   B CD  1 
ATOM   905  C  CE  . LYS   B 1 15  ? 3.040   1.421  30.913  1.00 28.62 ? 15  LYS   B CE  1 
ATOM   906  N  NZ  . LYS   B 1 15  ? 4.534   1.580  30.916  1.00 40.73 ? 15  LYS   B NZ  1 
ATOM   907  N  N   . VAL   B 1 16  ? 4.954   5.595  28.224  1.00 13.34 ? 16  VAL   B N   1 
ATOM   908  C  CA  . VAL   B 1 16  ? 5.747   5.442  26.999  1.00 13.97 ? 16  VAL   B CA  1 
ATOM   909  C  C   . VAL   B 1 16  ? 6.468   4.101  27.038  1.00 12.71 ? 16  VAL   B C   1 
ATOM   910  O  O   . VAL   B 1 16  ? 7.186   3.815  28.006  1.00 13.59 ? 16  VAL   B O   1 
ATOM   911  C  CB  . VAL   B 1 16  ? 6.735   6.611  26.797  1.00 13.73 ? 16  VAL   B CB  1 
ATOM   912  C  CG1 . VAL   B 1 16  ? 7.293   6.576  25.373  1.00 15.09 ? 16  VAL   B CG1 1 
ATOM   913  C  CG2 . VAL   B 1 16  ? 6.039   7.969  27.015  1.00 15.66 ? 16  VAL   B CG2 1 
ATOM   914  N  N   . LEU   B 1 17  ? 6.318   3.325  25.955  1.00 12.93 ? 17  LEU   B N   1 
ATOM   915  C  CA  . LEU   B 1 17  ? 6.943   2.021  25.785  1.00 11.92 ? 17  LEU   B CA  1 
ATOM   916  C  C   . LEU   B 1 17  ? 7.840   2.017  24.545  1.00 11.16 ? 17  LEU   B C   1 
ATOM   917  O  O   . LEU   B 1 17  ? 7.604   2.753  23.599  1.00 12.11 ? 17  LEU   B O   1 
ATOM   918  C  CB  . LEU   B 1 17  ? 5.909   0.901  25.676  1.00 12.67 ? 17  LEU   B CB  1 
ATOM   919  C  CG  . LEU   B 1 17  ? 4.976   0.698  26.876  1.00 15.36 ? 17  LEU   B CG  1 
ATOM   920  C  CD1 . LEU   B 1 17  ? 3.949   -0.435 26.613  1.00 22.31 ? 17  LEU   B CD1 1 
ATOM   921  C  CD2 . LEU   B 1 17  ? 5.794   0.365  28.158  1.00 18.14 ? 17  LEU   B CD2 1 
ATOM   922  N  N   . ASP   B 1 18  ? 8.843   1.155  24.571  1.00 10.72 ? 18  ASP   B N   1 
ATOM   923  C  CA  . ASP   B 1 18  ? 9.869   1.005  23.532  1.00 10.44 ? 18  ASP   B CA  1 
ATOM   924  C  C   . ASP   B 1 18  ? 9.675   -0.361 22.856  1.00 10.47 ? 18  ASP   B C   1 
ATOM   925  O  O   . ASP   B 1 18  ? 9.821   -1.407 23.504  1.00 11.52 ? 18  ASP   B O   1 
ATOM   926  C  CB  . ASP   B 1 18  ? 11.228  1.177  24.165  1.00 11.28 ? 18  ASP   B CB  1 
ATOM   927  C  CG  . ASP   B 1 18  ? 12.375  1.009  23.229  1.00 11.32 ? 18  ASP   B CG  1 
ATOM   928  O  OD1 . ASP   B 1 18  ? 12.289  0.241  22.271  1.00 12.10 ? 18  ASP   B OD1 1 
ATOM   929  O  OD2 . ASP   B 1 18  ? 13.434  1.616  23.513  1.00 14.06 ? 18  ASP   B OD2 1 
ATOM   930  N  N   . ALA   B 1 19  ? 9.292   -0.333 21.603  1.00 10.48 ? 19  ALA   B N   1 
ATOM   931  C  CA  . ALA   B 1 19  ? 8.995   -1.557 20.802  1.00 10.88 ? 19  ALA   B CA  1 
ATOM   932  C  C   . ALA   B 1 19  ? 10.262  -2.265 20.286  1.00 11.06 ? 19  ALA   B C   1 
ATOM   933  O  O   . ALA   B 1 19  ? 10.137  -3.350 19.758  1.00 12.71 ? 19  ALA   B O   1 
ATOM   934  C  CB  . ALA   B 1 19  ? 8.090   -1.196 19.661  1.00 11.33 ? 19  ALA   B CB  1 
ATOM   935  N  N   . VAL   B 1 20  ? 11.401  -1.583 20.321  1.00 11.49 ? 20  VAL   B N   1 
ATOM   936  C  CA  . VAL   B 1 20  ? 12.663  -2.165 19.895  1.00 11.40 ? 20  VAL   B CA  1 
ATOM   937  C  C   . VAL   B 1 20  ? 13.284  -3.021 20.991  1.00 12.49 ? 20  VAL   B C   1 
ATOM   938  O  O   . VAL   B 1 20  ? 13.759  -4.097 20.697  1.00 15.57 ? 20  VAL   B O   1 
ATOM   939  C  CB  . VAL   B 1 20  ? 13.639  -1.075 19.468  1.00 13.48 ? 20  VAL   B CB  1 
ATOM   940  C  CG1 . VAL   B 1 20  ? 15.042  -1.575 19.249  1.00 18.01 ? 20  VAL   B CG1 1 
ATOM   941  C  CG2 . VAL   B 1 20  ? 13.119  -0.377 18.222  1.00 15.59 ? 20  VAL   B CG2 1 
ATOM   942  N  N   . ARG   B 1 21  ? 13.314  -2.508 22.189  1.00 13.18 ? 21  ARG   B N   1 
ATOM   943  C  CA  . ARG   B 1 21  ? 13.947  -3.130 23.285  1.00 15.23 ? 21  ARG   B CA  1 
ATOM   944  C  C   . ARG   B 1 21  ? 12.974  -3.925 24.121  1.00 13.94 ? 21  ARG   B C   1 
ATOM   945  O  O   . ARG   B 1 21  ? 13.390  -4.729 24.976  1.00 16.62 ? 21  ARG   B O   1 
ATOM   946  C  CB  . ARG   B 1 21  ? 14.612  -2.090 24.172  1.00 19.45 ? 21  ARG   B CB  1 
ATOM   947  N  N   . GLY   B 1 22  ? 11.675  -3.757 23.948  1.00 12.57 ? 22  GLY   B N   1 
ATOM   948  C  CA  . GLY   B 1 22  ? 10.699  -4.465 24.753  1.00 13.48 ? 22  GLY   B CA  1 
ATOM   949  C  C   . GLY   B 1 22  ? 10.754  -4.009 26.184  1.00 13.75 ? 22  GLY   B C   1 
ATOM   950  O  O   . GLY   B 1 22  ? 10.788  -4.844 27.098  1.00 14.62 ? 22  GLY   B O   1 
ATOM   951  N  N   . SER   B 1 23  ? 10.661  -2.718 26.425  1.00 14.67 ? 23  SER   B N   1 
ATOM   952  C  CA  . SER   B 1 23  ? 10.851  -2.112 27.725  1.00 13.86 ? 23  SER   B CA  1 
ATOM   953  C  C   . SER   B 1 23  ? 10.024  -0.861 27.851  1.00 12.80 ? 23  SER   B C   1 
ATOM   954  O  O   . SER   B 1 23  ? 9.662   -0.259 26.861  1.00 14.07 ? 23  SER   B O   1 
ATOM   955  C  CB  . SER   B 1 23  ? 12.343  -1.747 27.901  1.00 16.06 ? 23  SER   B CB  1 
ATOM   956  O  OG  . SER   B 1 23  ? 12.709  -0.681 27.096  1.00 18.72 ? 23  SER   B OG  1 
ATOM   957  N  N   . PRO   B 1 24  ? 9.888   -0.375 29.074  1.00 13.02 ? 24  PRO   B N   1 
ATOM   958  C  CA  . PRO   B 1 24  ? 9.470   0.994  29.265  1.00 12.87 ? 24  PRO   B CA  1 
ATOM   959  C  C   . PRO   B 1 24  ? 10.481  1.942  28.594  1.00 13.42 ? 24  PRO   B C   1 
ATOM   960  O  O   . PRO   B 1 24  ? 11.657  1.630  28.518  1.00 14.23 ? 24  PRO   B O   1 
ATOM   961  C  CB  . PRO   B 1 24  ? 9.487   1.216  30.759  1.00 14.81 ? 24  PRO   B CB  1 
ATOM   962  C  CG  . PRO   B 1 24  ? 10.325  0.134  31.304  1.00 26.33 ? 24  PRO   B CG  1 
ATOM   963  C  CD  . PRO   B 1 24  ? 10.297  -0.989 30.332  1.00 15.09 ? 24  PRO   B CD  1 
ATOM   964  N  N   . ALA   B 1 25  ? 10.003  3.106  28.139  1.00 12.61 ? 25  ALA   B N   1 
ATOM   965  C  CA  . ALA   B 1 25  ? 10.888  4.143  27.599  1.00 13.01 ? 25  ALA   B CA  1 
ATOM   966  C  C   . ALA   B 1 25  ? 11.170  5.106  28.775  1.00 12.33 ? 25  ALA   B C   1 
ATOM   967  O  O   . ALA   B 1 25  ? 10.285  5.825  29.200  1.00 13.61 ? 25  ALA   B O   1 
ATOM   968  C  CB  . ALA   B 1 25  ? 10.263  4.849  26.464  1.00 13.99 ? 25  ALA   B CB  1 
ATOM   969  N  N   . ILE   B 1 26  ? 12.375  4.977  29.325  1.00 13.51 ? 26  ILE   B N   1 
ATOM   970  C  CA  . ILE   B 1 26  ? 12.747  5.635  30.546  1.00 15.19 ? 26  ILE   B CA  1 
ATOM   971  C  C   . ILE   B 1 26  ? 13.458  6.967  30.257  1.00 15.61 ? 26  ILE   B C   1 
ATOM   972  O  O   . ILE   B 1 26  ? 14.181  7.109  29.280  1.00 16.50 ? 26  ILE   B O   1 
ATOM   973  C  CB  . ILE   B 1 26  ? 13.708  4.704  31.333  1.00 19.26 ? 26  ILE   B CB  1 
ATOM   974  C  CG1 . ILE   B 1 26  ? 13.049  3.398  31.668  1.00 19.42 ? 26  ILE   B CG1 1 
ATOM   975  C  CG2 . ILE   B 1 26  ? 14.300  5.356  32.522  1.00 22.02 ? 26  ILE   B CG2 1 
ATOM   976  C  CD1 . ILE   B 1 26  ? 13.969  2.229  32.087  1.00 27.15 ? 26  ILE   B CD1 1 
ATOM   977  N  N   . ASN   B 1 27  ? 13.200  7.972  31.102  1.00 15.63 ? 27  ASN   B N   1 
ATOM   978  C  CA  A ASN   B 1 27  ? 13.891  9.271  31.009  0.50 15.96 ? 27  ASN   B CA  1 
ATOM   979  C  CA  B ASN   B 1 27  ? 13.849  9.296  30.966  0.50 16.88 ? 27  ASN   B CA  1 
ATOM   980  C  C   . ASN   B 1 27  ? 13.561  10.060 29.693  1.00 15.37 ? 27  ASN   B C   1 
ATOM   981  O  O   . ASN   B 1 27  ? 14.346  10.785 29.137  1.00 19.18 ? 27  ASN   B O   1 
ATOM   982  C  CB  A ASN   B 1 27  ? 15.406  9.133  31.244  0.50 17.64 ? 27  ASN   B CB  1 
ATOM   983  C  CB  B ASN   B 1 27  ? 15.327  9.205  31.092  0.50 19.19 ? 27  ASN   B CB  1 
ATOM   984  C  CG  A ASN   B 1 27  ? 16.039  10.444 31.661  0.50 20.00 ? 27  ASN   B CG  1 
ATOM   985  C  CG  B ASN   B 1 27  ? 15.733  9.102  32.480  0.50 22.68 ? 27  ASN   B CG  1 
ATOM   986  O  OD1 A ASN   B 1 27  ? 15.431  11.205 32.349  0.50 23.51 ? 27  ASN   B OD1 1 
ATOM   987  O  OD1 B ASN   B 1 27  ? 15.218  9.813  33.360  0.50 22.93 ? 27  ASN   B OD1 1 
ATOM   988  N  ND2 A ASN   B 1 27  ? 17.273  10.665 31.262  0.50 27.15 ? 27  ASN   B ND2 1 
ATOM   989  N  ND2 B ASN   B 1 27  ? 16.700  8.246  32.706  0.50 25.23 ? 27  ASN   B ND2 1 
ATOM   990  N  N   . VAL   B 1 28  ? 12.316  9.869  29.249  1.00 14.97 ? 28  VAL   B N   1 
ATOM   991  C  CA  . VAL   B 1 28  ? 11.775  10.566 28.114  1.00 14.00 ? 28  VAL   B CA  1 
ATOM   992  C  C   . VAL   B 1 28  ? 11.199  11.886 28.614  1.00 13.55 ? 28  VAL   B C   1 
ATOM   993  O  O   . VAL   B 1 28  ? 10.327  11.885 29.450  1.00 13.88 ? 28  VAL   B O   1 
ATOM   994  C  CB  . VAL   B 1 28  ? 10.692  9.735  27.374  1.00 15.15 ? 28  VAL   B CB  1 
ATOM   995  C  CG1 . VAL   B 1 28  ? 10.103  10.515 26.195  1.00 17.18 ? 28  VAL   B CG1 1 
ATOM   996  C  CG2 . VAL   B 1 28  ? 11.236  8.411  26.909  1.00 16.18 ? 28  VAL   B CG2 1 
ATOM   997  N  N   . ALA   B 1 29  ? 11.614  12.975 28.007  1.00 13.84 ? 29  ALA   B N   1 
ATOM   998  C  CA  . ALA   B 1 29  ? 11.062  14.299 28.378  1.00 14.95 ? 29  ALA   B CA  1 
ATOM   999  C  C   . ALA   B 1 29  ? 9.709   14.483 27.740  1.00 13.94 ? 29  ALA   B C   1 
ATOM   1000 O  O   . ALA   B 1 29  ? 9.498   14.148 26.558  1.00 14.78 ? 29  ALA   B O   1 
ATOM   1001 C  CB  . ALA   B 1 29  ? 11.985  15.394 27.924  1.00 16.64 ? 29  ALA   B CB  1 
ATOM   1002 N  N   . VAL   B 1 30  ? 8.747   15.035 28.504  1.00 14.02 ? 30  VAL   B N   1 
ATOM   1003 C  CA  . VAL   B 1 30  ? 7.406   15.209 28.074  1.00 13.61 ? 30  VAL   B CA  1 
ATOM   1004 C  C   . VAL   B 1 30  ? 6.957   16.590 28.552  1.00 14.15 ? 30  VAL   B C   1 
ATOM   1005 O  O   . VAL   B 1 30  ? 7.126   16.935 29.722  1.00 17.01 ? 30  VAL   B O   1 
ATOM   1006 C  CB  . VAL   B 1 30  ? 6.450   14.177 28.696  1.00 15.07 ? 30  VAL   B CB  1 
ATOM   1007 C  CG1 . VAL   B 1 30  ? 5.002   14.433 28.279  1.00 16.97 ? 30  VAL   B CG1 1 
ATOM   1008 C  CG2 . VAL   B 1 30  ? 6.889   12.792 28.358  1.00 15.18 ? 30  VAL   B CG2 1 
ATOM   1009 N  N   . HIS   B 1 31  ? 6.433   17.390 27.649  1.00 15.20 ? 31  HIS   B N   1 
ATOM   1010 C  CA  . HIS   B 1 31  ? 5.907   18.693 27.980  1.00 15.15 ? 31  HIS   B CA  1 
ATOM   1011 C  C   . HIS   B 1 31  ? 4.492   18.759 27.552  1.00 15.54 ? 31  HIS   B C   1 
ATOM   1012 O  O   . HIS   B 1 31  ? 4.155   18.367 26.463  1.00 16.93 ? 31  HIS   B O   1 
ATOM   1013 C  CB  . HIS   B 1 31  ? 6.662   19.822 27.329  1.00 18.99 ? 31  HIS   B CB  1 
ATOM   1014 C  CG  . HIS   B 1 31  ? 8.052   19.958 27.815  1.00 23.57 ? 31  HIS   B CG  1 
ATOM   1015 N  ND1 . HIS   B 1 31  ? 9.110   19.153 27.445  1.00 24.42 ? 31  HIS   B ND1 1 
ATOM   1016 C  CD2 . HIS   B 1 31  ? 8.520   20.804 28.737  1.00 26.16 ? 31  HIS   B CD2 1 
ATOM   1017 C  CE1 . HIS   B 1 31  ? 10.189  19.545 28.113  1.00 23.46 ? 31  HIS   B CE1 1 
ATOM   1018 N  NE2 . HIS   B 1 31  ? 9.856   20.564 28.893  1.00 27.38 ? 31  HIS   B NE2 1 
ATOM   1019 N  N   . VAL   B 1 32  ? 3.665   19.290 28.415  1.00 15.62 ? 32  VAL   B N   1 
ATOM   1020 C  CA  . VAL   B 1 32  ? 2.222   19.421 28.187  1.00 14.21 ? 32  VAL   B CA  1 
ATOM   1021 C  C   . VAL   B 1 32  ? 1.859   20.865 28.098  1.00 15.13 ? 32  VAL   B C   1 
ATOM   1022 O  O   . VAL   B 1 32  ? 2.348   21.675 28.909  1.00 17.63 ? 32  VAL   B O   1 
ATOM   1023 C  CB  . VAL   B 1 32  ? 1.395   18.722 29.256  1.00 14.94 ? 32  VAL   B CB  1 
ATOM   1024 C  CG1 . VAL   B 1 32  ? -0.089  18.778 28.897  1.00 15.32 ? 32  VAL   B CG1 1 
ATOM   1025 C  CG2 . VAL   B 1 32  ? 1.900   17.319 29.491  1.00 16.92 ? 32  VAL   B CG2 1 
ATOM   1026 N  N   . PHE   B 1 33  ? 1.041   21.217 27.128  1.00 15.65 ? 33  PHE   B N   1 
ATOM   1027 C  CA  . PHE   B 1 33  ? 0.588   22.585 26.909  1.00 18.17 ? 33  PHE   B CA  1 
ATOM   1028 C  C   . PHE   B 1 33  ? -0.949  22.585 26.811  1.00 16.60 ? 33  PHE   B C   1 
ATOM   1029 O  O   . PHE   B 1 33  ? -1.557  21.622 26.442  1.00 15.79 ? 33  PHE   B O   1 
ATOM   1030 C  CB  . PHE   B 1 33  ? 1.154   23.142 25.622  1.00 18.46 ? 33  PHE   B CB  1 
ATOM   1031 C  CG  . PHE   B 1 33  ? 2.643   23.128 25.596  1.00 19.76 ? 33  PHE   B CG  1 
ATOM   1032 C  CD1 . PHE   B 1 33  ? 3.311   21.965 25.227  1.00 23.68 ? 33  PHE   B CD1 1 
ATOM   1033 C  CD2 . PHE   B 1 33  ? 3.420   24.222 25.995  1.00 24.40 ? 33  PHE   B CD2 1 
ATOM   1034 C  CE1 . PHE   B 1 33  ? 4.659   21.911 25.220  1.00 23.25 ? 33  PHE   B CE1 1 
ATOM   1035 C  CE2 . PHE   B 1 33  ? 4.829   24.144 25.951  1.00 26.36 ? 33  PHE   B CE2 1 
ATOM   1036 C  CZ  . PHE   B 1 33  ? 5.443   22.986 25.568  1.00 25.61 ? 33  PHE   B CZ  1 
ATOM   1037 N  N   . ARG   B 1 34  ? -1.548  23.738 27.164  1.00 17.53 ? 34  ARG   B N   1 
ATOM   1038 C  CA  . ARG   B 1 34  ? -2.955  23.970 26.999  1.00 18.16 ? 34  ARG   B CA  1 
ATOM   1039 C  C   . ARG   B 1 34  ? -3.144  25.111 25.991  1.00 21.38 ? 34  ARG   B C   1 
ATOM   1040 O  O   . ARG   B 1 34  ? -2.520  26.119 26.114  1.00 23.65 ? 34  ARG   B O   1 
ATOM   1041 C  CB  . ARG   B 1 34  ? -3.640  24.235 28.394  1.00 19.67 ? 34  ARG   B CB  1 
ATOM   1042 C  CG  . ARG   B 1 34  ? -5.144  24.424 28.350  1.00 21.47 ? 34  ARG   B CG  1 
ATOM   1043 C  CD  . ARG   B 1 34  ? -5.913  24.700 29.702  1.00 27.54 ? 34  ARG   B CD  1 
ATOM   1044 N  NE  . ARG   B 1 34  ? -5.292  25.728 30.508  1.00 27.23 ? 34  ARG   B NE  1 
ATOM   1045 N  N   . LYS   B 1 35  ? -4.095  24.964 25.107  1.00 19.61 ? 35  LYS   B N   1 
ATOM   1046 C  CA  . LYS   B 1 35  ? -4.311  25.984 24.114  1.00 21.29 ? 35  LYS   B CA  1 
ATOM   1047 C  C   . LYS   B 1 35  ? -5.044  27.207 24.723  1.00 20.11 ? 35  LYS   B C   1 
ATOM   1048 O  O   . LYS   B 1 35  ? -6.047  27.076 25.377  1.00 22.83 ? 35  LYS   B O   1 
ATOM   1049 C  CB  . LYS   B 1 35  ? -5.197  25.460 22.997  1.00 21.64 ? 35  LYS   B CB  1 
ATOM   1050 C  CG  . LYS   B 1 35  ? -4.980  26.184 21.723  1.00 24.35 ? 35  LYS   B CG  1 
ATOM   1051 C  CD  . LYS   B 1 35  ? -5.611  25.405 20.574  1.00 30.33 ? 35  LYS   B CD  1 
ATOM   1052 N  N   . ALA   B 1 36  ? -4.518  28.376 24.440  1.00 26.42 ? 36  ALA   B N   1 
ATOM   1053 C  CA  . ALA   B 1 36  ? -5.020  29.660 24.990  1.00 26.37 ? 36  ALA   B CA  1 
ATOM   1054 C  C   . ALA   B 1 36  ? -6.019  30.187 24.031  1.00 27.12 ? 36  ALA   B C   1 
ATOM   1055 O  O   . ALA   B 1 36  ? -6.096  29.733 22.883  1.00 28.96 ? 36  ALA   B O   1 
ATOM   1056 C  CB  . ALA   B 1 36  ? -3.849  30.645 25.135  1.00 26.47 ? 36  ALA   B CB  1 
ATOM   1057 N  N   . ALA   B 1 37  ? -6.710  31.260 24.453  1.00 33.15 ? 37  ALA   B N   1 
ATOM   1058 C  CA  . ALA   B 1 37  ? -7.716  31.936 23.605  1.00 31.23 ? 37  ALA   B CA  1 
ATOM   1059 C  C   . ALA   B 1 37  ? -7.146  32.503 22.281  1.00 31.93 ? 37  ALA   B C   1 
ATOM   1060 O  O   . ALA   B 1 37  ? -7.881  32.552 21.282  1.00 39.60 ? 37  ALA   B O   1 
ATOM   1061 C  CB  . ALA   B 1 37  ? -8.439  33.036 24.390  1.00 31.79 ? 37  ALA   B CB  1 
ATOM   1062 N  N   . ASP   B 1 38  ? -5.874  32.925 22.277  1.00 31.36 ? 38  ASP   B N   1 
ATOM   1063 C  CA  . ASP   B 1 38  ? -5.228  33.458 21.055  1.00 36.20 ? 38  ASP   B CA  1 
ATOM   1064 C  C   . ASP   B 1 38  ? -4.672  32.373 20.127  1.00 31.18 ? 38  ASP   B C   1 
ATOM   1065 O  O   . ASP   B 1 38  ? -3.941  32.683 19.162  1.00 35.99 ? 38  ASP   B O   1 
ATOM   1066 C  CB  . ASP   B 1 38  ? -4.172  34.566 21.376  1.00 38.28 ? 38  ASP   B CB  1 
ATOM   1067 C  CG  . ASP   B 1 38  ? -3.021  34.081 22.233  1.00 39.43 ? 38  ASP   B CG  1 
ATOM   1068 O  OD1 . ASP   B 1 38  ? -2.998  32.887 22.626  1.00 39.37 ? 38  ASP   B OD1 1 
ATOM   1069 O  OD2 . ASP   B 1 38  ? -2.141  34.902 22.531  1.00 42.16 ? 38  ASP   B OD2 1 
ATOM   1070 N  N   . ASP   B 1 39  ? -5.042  31.115 20.413  1.00 30.15 ? 39  ASP   B N   1 
ATOM   1071 C  CA  . ASP   B 1 39  ? -4.560  29.935 19.693  1.00 32.06 ? 39  ASP   B CA  1 
ATOM   1072 C  C   . ASP   B 1 39  ? -3.064  29.627 19.925  1.00 34.57 ? 39  ASP   B C   1 
ATOM   1073 O  O   . ASP   B 1 39  ? -2.514  28.718 19.314  1.00 37.03 ? 39  ASP   B O   1 
ATOM   1074 C  CB  . ASP   B 1 39  ? -4.887  30.006 18.180  1.00 37.04 ? 39  ASP   B CB  1 
ATOM   1075 N  N   . THR   B 1 40  ? -2.401  30.360 20.820  1.00 31.29 ? 40  THR   B N   1 
ATOM   1076 C  CA  . THR   B 1 40  ? -1.059  29.969 21.250  1.00 34.40 ? 40  THR   B CA  1 
ATOM   1077 C  C   . THR   B 1 40  ? -1.127  28.875 22.364  1.00 27.48 ? 40  THR   B C   1 
ATOM   1078 O  O   . THR   B 1 40  ? -2.193  28.527 22.872  1.00 27.13 ? 40  THR   B O   1 
ATOM   1079 C  CB  . THR   B 1 40  ? -0.250  31.194 21.701  1.00 35.84 ? 40  THR   B CB  1 
ATOM   1080 O  OG1 . THR   B 1 40  ? -0.627  31.531 23.035  1.00 37.15 ? 40  THR   B OG1 1 
ATOM   1081 N  N   . TRP   B 1 41  ? 0.033   28.371 22.738  1.00 33.08 ? 41  TRP   B N   1 
ATOM   1082 C  CA  . TRP   B 1 41  ? 0.127   27.263 23.686  1.00 27.28 ? 41  TRP   B CA  1 
ATOM   1083 C  C   . TRP   B 1 41  ? 0.796   27.553 24.968  1.00 27.85 ? 41  TRP   B C   1 
ATOM   1084 O  O   . TRP   B 1 41  ? 2.016   27.818 25.041  1.00 44.83 ? 41  TRP   B O   1 
ATOM   1085 C  CB  . TRP   B 1 41  ? 0.891   26.140 23.050  1.00 27.94 ? 41  TRP   B CB  1 
ATOM   1086 C  CG  . TRP   B 1 41  ? 0.191   25.526 21.912  1.00 25.75 ? 41  TRP   B CG  1 
ATOM   1087 C  CD1 . TRP   B 1 41  ? 0.374   25.833 20.669  1.00 28.34 ? 41  TRP   B CD1 1 
ATOM   1088 C  CD2 . TRP   B 1 41  ? -0.874  24.533 21.950  1.00 24.38 ? 41  TRP   B CD2 1 
ATOM   1089 N  NE1 . TRP   B 1 41  ? -0.456  25.099 19.872  1.00 29.81 ? 41  TRP   B NE1 1 
ATOM   1090 C  CE2 . TRP   B 1 41  ? -1.250  24.288 20.651  1.00 25.17 ? 41  TRP   B CE2 1 
ATOM   1091 C  CE3 . TRP   B 1 41  ? -1.517  23.840 22.960  1.00 21.28 ? 41  TRP   B CE3 1 
ATOM   1092 C  CZ2 . TRP   B 1 41  ? -2.275  23.328 20.299  1.00 26.96 ? 41  TRP   B CZ2 1 
ATOM   1093 C  CZ3 . TRP   B 1 41  ? -2.537  22.922 22.644  1.00 21.03 ? 41  TRP   B CZ3 1 
ATOM   1094 C  CH2 . TRP   B 1 41  ? -2.889  22.667 21.339  1.00 23.89 ? 41  TRP   B CH2 1 
ATOM   1095 N  N   . GLU   B 1 42  ? -0.008  27.511 26.014  1.00 26.98 ? 42  GLU   B N   1 
ATOM   1096 C  CA  . GLU   B 1 42  ? 0.466   27.842 27.352  1.00 27.12 ? 42  GLU   B CA  1 
ATOM   1097 C  C   . GLU   B 1 42  ? 1.121   26.603 27.976  1.00 26.82 ? 42  GLU   B C   1 
ATOM   1098 O  O   . GLU   B 1 42  ? 0.528   25.550 28.023  1.00 24.04 ? 42  GLU   B O   1 
ATOM   1099 C  CB  . GLU   B 1 42  ? -0.753  28.260 28.199  1.00 26.40 ? 42  GLU   B CB  1 
ATOM   1100 N  N   . PRO   B 1 43  ? 2.276   26.759 28.633  1.00 27.56 ? 43  PRO   B N   1 
ATOM   1101 C  CA  . PRO   B 1 43  ? 2.860   25.639 29.330  1.00 25.76 ? 43  PRO   B CA  1 
ATOM   1102 C  C   . PRO   B 1 43  ? 1.894   25.242 30.412  1.00 25.00 ? 43  PRO   B C   1 
ATOM   1103 O  O   . PRO   B 1 43  ? 1.257   26.127 31.079  1.00 26.23 ? 43  PRO   B O   1 
ATOM   1104 C  CB  . PRO   B 1 43  ? 4.146   26.239 29.936  1.00 25.98 ? 43  PRO   B CB  1 
ATOM   1105 C  CG  . PRO   B 1 43  ? 4.502   27.178 28.919  1.00 30.85 ? 43  PRO   B CG  1 
ATOM   1106 C  CD  . PRO   B 1 43  ? 3.218   27.875 28.599  1.00 35.83 ? 43  PRO   B CD  1 
ATOM   1107 N  N   . PHE   B 1 44  ? 1.845   23.959 30.644  1.00 19.24 ? 44  PHE   B N   1 
ATOM   1108 C  CA  . PHE   B 1 44  ? 0.921   23.391 31.564  1.00 19.53 ? 44  PHE   B CA  1 
ATOM   1109 C  C   . PHE   B 1 44  ? 1.553   22.452 32.566  1.00 19.12 ? 44  PHE   B C   1 
ATOM   1110 O  O   . PHE   B 1 44  ? 1.304   22.604 33.793  1.00 21.47 ? 44  PHE   B O   1 
ATOM   1111 C  CB  . PHE   B 1 44  ? -0.261  22.747 30.822  1.00 19.30 ? 44  PHE   B CB  1 
ATOM   1112 C  CG  . PHE   B 1 44  ? -1.299  22.176 31.710  1.00 18.68 ? 44  PHE   B CG  1 
ATOM   1113 C  CD1 . PHE   B 1 44  ? -2.250  23.018 32.288  1.00 21.71 ? 44  PHE   B CD1 1 
ATOM   1114 C  CD2 . PHE   B 1 44  ? -1.309  20.851 32.011  1.00 18.65 ? 44  PHE   B CD2 1 
ATOM   1115 C  CE1 . PHE   B 1 44  ? -3.186  22.501 33.162  1.00 26.69 ? 44  PHE   B CE1 1 
ATOM   1116 C  CE2 . PHE   B 1 44  ? -2.281  20.218 32.834  1.00 22.27 ? 44  PHE   B CE2 1 
ATOM   1117 C  CZ  . PHE   B 1 44  ? -3.171  21.119 33.531  1.00 23.63 ? 44  PHE   B CZ  1 
ATOM   1118 N  N   . ALA   B 1 45  ? 2.438   21.556 32.050  1.00 16.85 ? 45  ALA   B N   1 
ATOM   1119 C  CA  . ALA   B 1 45  ? 3.043   20.435 32.946  1.00 20.26 ? 45  ALA   B CA  1 
ATOM   1120 C  C   . ALA   B 1 45  ? 4.224   19.970 32.201  1.00 17.41 ? 45  ALA   B C   1 
ATOM   1121 O  O   . ALA   B 1 45  ? 4.240   20.012 30.963  1.00 20.13 ? 45  ALA   B O   1 
ATOM   1122 C  CB  . ALA   B 1 45  ? 2.064   19.457 33.480  1.00 18.81 ? 45  ALA   B CB  1 
ATOM   1123 N  N   . SER   B 1 46  ? 5.192   19.387 32.889  1.00 17.66 ? 46  SER   B N   1 
ATOM   1124 C  CA  . SER   B 1 46  ? 6.270   18.650 32.197  1.00 15.81 ? 46  SER   B CA  1 
ATOM   1125 C  C   . SER   B 1 46  ? 6.953   17.713 33.166  1.00 14.88 ? 46  SER   B C   1 
ATOM   1126 O  O   . SER   B 1 46  ? 6.812   17.807 34.391  1.00 18.32 ? 46  SER   B O   1 
ATOM   1127 C  CB  . SER   B 1 46  ? 7.251   19.543 31.471  1.00 17.34 ? 46  SER   B CB  1 
ATOM   1128 O  OG  . SER   B 1 46  ? 7.862   20.320 32.438  1.00 17.49 ? 46  SER   B OG  1 
ATOM   1129 N  N   . GLY   B 1 47  ? 7.717   16.802 32.613  1.00 16.43 ? 47  GLY   B N   1 
ATOM   1130 C  CA  . GLY   B 1 47  ? 8.466   15.882 33.420  1.00 16.38 ? 47  GLY   B CA  1 
ATOM   1131 C  C   . GLY   B 1 47  ? 9.162   14.855 32.559  1.00 15.43 ? 47  GLY   B C   1 
ATOM   1132 O  O   . GLY   B 1 47  ? 9.204   14.987 31.378  1.00 16.54 ? 47  GLY   B O   1 
ATOM   1133 N  N   . LYS   B 1 48  ? 9.797   13.887 33.168  1.00 17.39 ? 48  LYS   B N   1 
ATOM   1134 C  CA  . LYS   B 1 48  ? 10.497  12.823 32.484  1.00 19.11 ? 48  LYS   B CA  1 
ATOM   1135 C  C   . LYS   B 1 48  ? 9.896   11.512 32.901  1.00 16.28 ? 48  LYS   B C   1 
ATOM   1136 O  O   . LYS   B 1 48  ? 9.617   11.322 34.076  1.00 17.65 ? 48  LYS   B O   1 
ATOM   1137 C  CB  . LYS   B 1 48  ? 11.969  12.773 32.800  1.00 25.56 ? 48  LYS   B CB  1 
ATOM   1138 N  N   . THR   B 1 49  ? 9.744   10.554 32.025  1.00 14.55 ? 49  THR   B N   1 
ATOM   1139 C  CA  . THR   B 1 49  ? 9.205   9.269  32.402  1.00 13.90 ? 49  THR   B CA  1 
ATOM   1140 C  C   . THR   B 1 49  ? 10.137  8.568  33.380  1.00 15.15 ? 49  THR   B C   1 
ATOM   1141 O  O   . THR   B 1 49  ? 11.367  8.670  33.290  1.00 15.61 ? 49  THR   B O   1 
ATOM   1142 C  CB  . THR   B 1 49  ? 8.979   8.355  31.193  1.00 13.81 ? 49  THR   B CB  1 
ATOM   1143 O  OG1 . THR   B 1 49  ? 10.214  8.181  30.480  1.00 13.85 ? 49  THR   B OG1 1 
ATOM   1144 C  CG2 . THR   B 1 49  ? 7.914   8.921  30.256  1.00 13.22 ? 49  THR   B CG2 1 
ATOM   1145 N  N   . SER   B 1 50  ? 9.523   7.808  34.265  1.00 14.76 ? 50  SER   B N   1 
ATOM   1146 C  CA  . SER   B 1 50  ? 10.196  7.052  35.296  1.00 16.36 ? 50  SER   B CA  1 
ATOM   1147 C  C   . SER   B 1 50  ? 10.760  5.751  34.755  1.00 15.84 ? 50  SER   B C   1 
ATOM   1148 O  O   . SER   B 1 50  ? 10.652  5.425  33.584  1.00 15.89 ? 50  SER   B O   1 
ATOM   1149 C  CB  . SER   B 1 50  ? 9.181   6.719  36.381  1.00 17.03 ? 50  SER   B CB  1 
ATOM   1150 O  OG  . SER   B 1 50  ? 8.302   5.730  35.933  1.00 19.21 ? 50  SER   B OG  1 
ATOM   1151 N  N   . GLU   B 1 51  ? 11.317  4.970  35.659  1.00 17.66 ? 51  GLU   B N   1 
ATOM   1152 C  CA  . GLU   B 1 51  ? 11.795  3.627  35.349  1.00 19.21 ? 51  GLU   B CA  1 
ATOM   1153 C  C   . GLU   B 1 51  ? 10.711  2.741  34.818  1.00 17.11 ? 51  GLU   B C   1 
ATOM   1154 O  O   . GLU   B 1 51  ? 11.011  1.801  34.084  1.00 20.85 ? 51  GLU   B O   1 
ATOM   1155 C  CB  . GLU   B 1 51  ? 12.415  2.982  36.610  1.00 28.82 ? 51  GLU   B CB  1 
ATOM   1156 N  N   . SER   B 1 52  ? 9.445   3.041  35.070  1.00 18.11 ? 52  SER   B N   1 
ATOM   1157 C  CA  . SER   B 1 52  ? 8.341   2.229  34.528  1.00 17.17 ? 52  SER   B CA  1 
ATOM   1158 C  C   . SER   B 1 52  ? 7.780   2.813  33.254  1.00 17.47 ? 52  SER   B C   1 
ATOM   1159 O  O   . SER   B 1 52  ? 6.844   2.298  32.744  1.00 18.24 ? 52  SER   B O   1 
ATOM   1160 C  CB  . SER   B 1 52  ? 7.183   2.134  35.536  1.00 20.77 ? 52  SER   B CB  1 
ATOM   1161 O  OG  . SER   B 1 52  ? 6.597   3.407  35.711  1.00 24.36 ? 52  SER   B OG  1 
ATOM   1162 N  N   . GLY   B 1 53  ? 8.395   3.858  32.713  1.00 15.62 ? 53  GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 1 53  ? 7.937   4.547  31.565  1.00 14.53 ? 53  GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 1 53  ? 6.765   5.439  31.759  1.00 14.23 ? 53  GLY   B C   1 
ATOM   1165 O  O   . GLY   B 1 53  ? 6.170   5.884  30.845  1.00 15.27 ? 53  GLY   B O   1 
ATOM   1166 N  N   . GLU   B 1 54  ? 6.428   5.731  33.013  1.00 17.66 ? 54  GLU   B N   1 
ATOM   1167 C  CA  . GLU   B 1 54  ? 5.257   6.493  33.348  1.00 17.04 ? 54  GLU   B CA  1 
ATOM   1168 C  C   . GLU   B 1 54  ? 5.617   7.828  33.869  1.00 15.55 ? 54  GLU   B C   1 
ATOM   1169 O  O   . GLU   B 1 54  ? 6.661   8.006  34.492  1.00 18.83 ? 54  GLU   B O   1 
ATOM   1170 C  CB  . GLU   B 1 54  ? 4.378   5.695  34.352  1.00 20.97 ? 54  GLU   B CB  1 
ATOM   1171 C  CG  . GLU   B 1 54  ? 3.883   4.369  33.737  1.00 22.92 ? 54  GLU   B CG  1 
ATOM   1172 C  CD  . GLU   B 1 54  ? 2.885   3.512  34.559  1.00 28.43 ? 54  GLU   B CD  1 
ATOM   1173 O  OE1 . GLU   B 1 54  ? 2.517   3.944  35.597  1.00 37.83 ? 54  GLU   B OE1 1 
ATOM   1174 O  OE2 . GLU   B 1 54  ? 2.442   2.406  34.129  1.00 33.30 ? 54  GLU   B OE2 1 
ATOM   1175 N  N   . LEU   B 1 55  ? 4.764   8.781  33.629  1.00 16.31 ? 55  LEU   B N   1 
ATOM   1176 C  CA  . LEU   B 1 55  ? 4.868   10.099 34.173  1.00 15.33 ? 55  LEU   B CA  1 
ATOM   1177 C  C   . LEU   B 1 55  ? 3.560   10.468 34.817  1.00 19.42 ? 55  LEU   B C   1 
ATOM   1178 O  O   . LEU   B 1 55  ? 2.563   10.687 34.121  1.00 20.36 ? 55  LEU   B O   1 
ATOM   1179 C  CB  . LEU   B 1 55  ? 5.272   11.033 33.032  1.00 16.81 ? 55  LEU   B CB  1 
ATOM   1180 C  CG  . LEU   B 1 55  ? 5.343   12.496 33.382  1.00 17.22 ? 55  LEU   B CG  1 
ATOM   1181 C  CD1 . LEU   B 1 55  ? 6.229   12.811 34.565  1.00 19.61 ? 55  LEU   B CD1 1 
ATOM   1182 C  CD2 . LEU   B 1 55  ? 5.817   13.265 32.168  1.00 18.22 ? 55  LEU   B CD2 1 
ATOM   1183 N  N   . HIS   B 1 56  ? 3.629   10.513 36.142  1.00 21.67 ? 56  HIS   B N   1 
ATOM   1184 C  CA  . HIS   B 1 56  ? 2.530   10.744 37.029  1.00 26.44 ? 56  HIS   B CA  1 
ATOM   1185 C  C   . HIS   B 1 56  ? 2.747   12.156 37.625  1.00 24.28 ? 56  HIS   B C   1 
ATOM   1186 O  O   . HIS   B 1 56  ? 3.832   12.767 37.520  1.00 25.25 ? 56  HIS   B O   1 
ATOM   1187 C  CB  . HIS   B 1 56  ? 2.517   9.755  38.193  1.00 34.44 ? 56  HIS   B CB  1 
ATOM   1188 C  CG  . HIS   B 1 56  ? 2.075   8.394  37.798  1.00 38.11 ? 56  HIS   B CG  1 
ATOM   1189 N  ND1 . HIS   B 1 56  ? 2.952   7.422  37.397  1.00 49.67 ? 56  HIS   B ND1 1 
ATOM   1190 C  CD2 . HIS   B 1 56  ? 0.845   7.834  37.748  1.00 39.02 ? 56  HIS   B CD2 1 
ATOM   1191 C  CE1 . HIS   B 1 56  ? 2.285   6.328  37.095  1.00 43.52 ? 56  HIS   B CE1 1 
ATOM   1192 N  NE2 . HIS   B 1 56  ? 1.003   6.549  37.299  1.00 45.36 ? 56  HIS   B NE2 1 
ATOM   1193 N  N   . GLY   B 1 57  ? 1.713   12.673 38.249  1.00 26.07 ? 57  GLY   B N   1 
ATOM   1194 C  CA  . GLY   B 1 57  ? 1.884   13.886 39.018  1.00 25.20 ? 57  GLY   B CA  1 
ATOM   1195 C  C   . GLY   B 1 57  ? 1.985   15.115 38.195  1.00 23.19 ? 57  GLY   B C   1 
ATOM   1196 O  O   . GLY   B 1 57  ? 2.384   16.102 38.706  1.00 26.90 ? 57  GLY   B O   1 
ATOM   1197 N  N   . LEU   B 1 58  ? 1.551   15.064 36.931  1.00 20.73 ? 58  LEU   B N   1 
ATOM   1198 C  CA  . LEU   B 1 58  ? 1.581   16.194 36.005  1.00 22.45 ? 58  LEU   B CA  1 
ATOM   1199 C  C   . LEU   B 1 58  ? 0.698   17.300 36.506  1.00 19.83 ? 58  LEU   B C   1 
ATOM   1200 O  O   . LEU   B 1 58  ? 1.060   18.465 36.344  1.00 23.43 ? 58  LEU   B O   1 
ATOM   1201 C  CB  . LEU   B 1 58  ? 1.185   15.830 34.559  1.00 19.38 ? 58  LEU   B CB  1 
ATOM   1202 C  CG  . LEU   B 1 58  ? 2.313   15.066 33.890  1.00 20.04 ? 58  LEU   B CG  1 
ATOM   1203 C  CD1 . LEU   B 1 58  ? 1.805   14.369 32.643  1.00 23.77 ? 58  LEU   B CD1 1 
ATOM   1204 C  CD2 . LEU   B 1 58  ? 3.441   15.997 33.626  1.00 24.87 ? 58  LEU   B CD2 1 
ATOM   1205 N  N   . THR   B 1 59  ? -0.511  16.965 36.949  1.00 21.82 ? 59  THR   B N   1 
ATOM   1206 C  CA  . THR   B 1 59  ? -1.445  18.047 37.322  1.00 22.11 ? 59  THR   B CA  1 
ATOM   1207 C  C   . THR   B 1 59  ? -2.397  17.574 38.386  1.00 19.44 ? 59  THR   B C   1 
ATOM   1208 O  O   . THR   B 1 59  ? -2.302  16.499 38.900  1.00 23.14 ? 59  THR   B O   1 
ATOM   1209 C  CB  . THR   B 1 59  ? -2.196  18.463 36.023  1.00 21.68 ? 59  THR   B CB  1 
ATOM   1210 O  OG1 . THR   B 1 59  ? -2.977  19.619 36.260  1.00 26.16 ? 59  THR   B OG1 1 
ATOM   1211 C  CG2 . THR   B 1 59  ? -3.184  17.397 35.590  1.00 22.95 ? 59  THR   B CG2 1 
ATOM   1212 N  N   . THR   B 1 60  ? -3.278  18.476 38.771  1.00 26.18 ? 60  THR   B N   1 
ATOM   1213 C  CA  . THR   B 1 60  ? -4.315  18.186 39.752  1.00 25.04 ? 60  THR   B CA  1 
ATOM   1214 C  C   . THR   B 1 60  ? -5.658  18.410 39.106  1.00 20.84 ? 60  THR   B C   1 
ATOM   1215 O  O   . THR   B 1 60  ? -5.752  19.102 38.056  1.00 20.47 ? 60  THR   B O   1 
ATOM   1216 C  CB  . THR   B 1 60  ? -4.199  19.116 40.967  1.00 27.78 ? 60  THR   B CB  1 
ATOM   1217 O  OG1 . THR   B 1 60  ? -4.345  20.484 40.512  1.00 30.00 ? 60  THR   B OG1 1 
ATOM   1218 C  CG2 . THR   B 1 60  ? -2.863  18.954 41.726  1.00 31.45 ? 60  THR   B CG2 1 
ATOM   1219 N  N   . GLU   B 1 61  ? -6.721  17.947 39.751  1.00 22.58 ? 61  GLU   B N   1 
ATOM   1220 C  CA  . GLU   B 1 61  ? -8.053  18.100 39.246  1.00 20.28 ? 61  GLU   B CA  1 
ATOM   1221 C  C   . GLU   B 1 61  ? -8.395  19.557 39.085  1.00 21.07 ? 61  GLU   B C   1 
ATOM   1222 O  O   . GLU   B 1 61  ? -8.970  19.922 38.086  1.00 21.28 ? 61  GLU   B O   1 
ATOM   1223 C  CB  . GLU   B 1 61  ? -9.079  17.425 40.189  1.00 25.24 ? 61  GLU   B CB  1 
ATOM   1224 N  N   . GLU   B 1 62  ? -8.034  20.420 40.049  1.00 22.36 ? 62  GLU   B N   1 
ATOM   1225 C  CA  . GLU   B 1 62  ? -8.498  21.815 39.950  1.00 22.53 ? 62  GLU   B CA  1 
ATOM   1226 C  C   . GLU   B 1 62  ? -7.782  22.541 38.768  1.00 18.06 ? 62  GLU   B C   1 
ATOM   1227 O  O   . GLU   B 1 62  ? -8.363  23.417 38.098  1.00 23.62 ? 62  GLU   B O   1 
ATOM   1228 C  CB  . GLU   B 1 62  ? -8.167  22.610 41.241  1.00 26.82 ? 62  GLU   B CB  1 
ATOM   1229 N  N   . GLU   B 1 63  ? -6.560  22.135 38.465  1.00 20.78 ? 63  GLU   B N   1 
ATOM   1230 C  CA  . GLU   B 1 63  ? -5.806  22.785 37.399  1.00 21.47 ? 63  GLU   B CA  1 
ATOM   1231 C  C   . GLU   B 1 63  ? -6.244  22.285 36.024  1.00 20.00 ? 63  GLU   B C   1 
ATOM   1232 O  O   . GLU   B 1 63  ? -6.107  23.011 35.044  1.00 23.42 ? 63  GLU   B O   1 
ATOM   1233 C  CB  . GLU   B 1 63  ? -4.256  22.532 37.500  1.00 26.32 ? 63  GLU   B CB  1 
ATOM   1234 N  N   . PHE   B 1 64  ? -6.720  21.069 35.937  1.00 20.47 ? 64  PHE   B N   1 
ATOM   1235 C  CA  . PHE   B 1 64  ? -6.955  20.405 34.673  1.00 18.78 ? 64  PHE   B CA  1 
ATOM   1236 C  C   . PHE   B 1 64  ? -8.392  20.691 34.182  1.00 17.51 ? 64  PHE   B C   1 
ATOM   1237 O  O   . PHE   B 1 64  ? -9.278  19.857 34.227  1.00 22.65 ? 64  PHE   B O   1 
ATOM   1238 C  CB  . PHE   B 1 64  ? -6.690  18.901 34.831  1.00 18.29 ? 64  PHE   B CB  1 
ATOM   1239 C  CG  . PHE   B 1 64  ? -6.663  18.144 33.545  1.00 19.38 ? 64  PHE   B CG  1 
ATOM   1240 C  CD1 . PHE   B 1 64  ? -5.948  18.596 32.457  1.00 19.04 ? 64  PHE   B CD1 1 
ATOM   1241 C  CD2 . PHE   B 1 64  ? -7.262  16.923 33.481  1.00 30.82 ? 64  PHE   B CD2 1 
ATOM   1242 C  CE1 . PHE   B 1 64  ? -5.875  17.840 31.289  1.00 21.75 ? 64  PHE   B CE1 1 
ATOM   1243 C  CE2 . PHE   B 1 64  ? -7.218  16.184 32.310  1.00 28.25 ? 64  PHE   B CE2 1 
ATOM   1244 C  CZ  . PHE   B 1 64  ? -6.519  16.674 31.214  1.00 22.87 ? 64  PHE   B CZ  1 
ATOM   1245 N  N   . VAL   B 1 65  ? -8.609  21.823 33.600  1.00 17.54 ? 65  VAL   B N   1 
ATOM   1246 C  CA  . VAL   B 1 65  ? -9.916  22.196 33.090  1.00 17.52 ? 65  VAL   B CA  1 
ATOM   1247 C  C   . VAL   B 1 65  ? -10.151 21.782 31.666  1.00 18.58 ? 65  VAL   B C   1 
ATOM   1248 O  O   . VAL   B 1 65  ? -9.209  21.404 30.924  1.00 18.78 ? 65  VAL   B O   1 
ATOM   1249 C  CB  . VAL   B 1 65  ? -10.068 23.709 33.217  1.00 20.65 ? 65  VAL   B CB  1 
ATOM   1250 C  CG1 . VAL   B 1 65  ? -9.976  24.237 34.667  1.00 21.63 ? 65  VAL   B CG1 1 
ATOM   1251 C  CG2 . VAL   B 1 65  ? -9.100  24.466 32.341  1.00 25.13 ? 65  VAL   B CG2 1 
ATOM   1252 N  N   . GLU   B 1 66  ? -11.371 21.814 31.231  1.00 21.85 ? 66  GLU   B N   1 
ATOM   1253 C  CA  . GLU   B 1 66  ? -11.713 21.521 29.863  1.00 21.01 ? 66  GLU   B CA  1 
ATOM   1254 C  C   . GLU   B 1 66  ? -10.879 22.377 28.929  1.00 22.41 ? 66  GLU   B C   1 
ATOM   1255 O  O   . GLU   B 1 66  ? -10.585 23.490 29.203  1.00 24.47 ? 66  GLU   B O   1 
ATOM   1256 C  CB  . GLU   B 1 66  ? -13.236 21.723 29.617  1.00 20.47 ? 66  GLU   B CB  1 
ATOM   1257 C  CG  . GLU   B 1 66  ? -14.166 20.675 30.216  1.00 21.27 ? 66  GLU   B CG  1 
ATOM   1258 C  CD  . GLU   B 1 66  ? -15.601 20.942 29.785  1.00 22.77 ? 66  GLU   B CD  1 
ATOM   1259 O  OE1 . GLU   B 1 66  ? -16.244 21.934 30.038  1.00 22.21 ? 66  GLU   B OE1 1 
ATOM   1260 O  OE2 . GLU   B 1 66  ? -16.223 20.031 29.213  1.00 27.91 ? 66  GLU   B OE2 1 
ATOM   1261 N  N   . GLY   B 1 67  ? -10.434 21.800 27.827  1.00 21.60 ? 67  GLY   B N   1 
ATOM   1262 C  CA  . GLY   B 1 67  ? -9.637  22.550 26.853  1.00 23.84 ? 67  GLY   B CA  1 
ATOM   1263 C  C   . GLY   B 1 67  ? -8.897  21.599 25.946  1.00 19.17 ? 67  GLY   B C   1 
ATOM   1264 O  O   . GLY   B 1 67  ? -9.113  20.410 25.981  1.00 18.83 ? 67  GLY   B O   1 
ATOM   1265 N  N   . ILE   B 1 68  ? -8.166  22.180 25.020  1.00 17.46 ? 68  ILE   B N   1 
ATOM   1266 C  CA  . ILE   B 1 68  ? -7.329  21.392 24.111  1.00 15.15 ? 68  ILE   B CA  1 
ATOM   1267 C  C   . ILE   B 1 68  ? -5.900  21.333 24.705  1.00 16.39 ? 68  ILE   B C   1 
ATOM   1268 O  O   . ILE   B 1 68  ? -5.325  22.342 25.030  1.00 19.32 ? 68  ILE   B O   1 
ATOM   1269 C  CB  . ILE   B 1 68  ? -7.280  22.007 22.713  1.00 17.74 ? 68  ILE   B CB  1 
ATOM   1270 C  CG1 . ILE   B 1 68  ? -8.664  22.021 22.123  1.00 21.15 ? 68  ILE   B CG1 1 
ATOM   1271 C  CG2 . ILE   B 1 68  ? -6.331  21.211 21.790  1.00 16.29 ? 68  ILE   B CG2 1 
ATOM   1272 C  CD1 . ILE   B 1 68  ? -8.802  22.779 20.829  1.00 27.62 ? 68  ILE   B CD1 1 
ATOM   1273 N  N   . TYR   B 1 69  ? -5.360  20.150 24.824  1.00 13.60 ? 69  TYR   B N   1 
ATOM   1274 C  CA  . TYR   B 1 69  ? -4.082  19.897 25.419  1.00 13.34 ? 69  TYR   B CA  1 
ATOM   1275 C  C   . TYR   B 1 69  ? -3.172  19.242 24.333  1.00 12.79 ? 69  TYR   B C   1 
ATOM   1276 O  O   . TYR   B 1 69  ? -3.640  18.460 23.465  1.00 13.90 ? 69  TYR   B O   1 
ATOM   1277 C  CB  . TYR   B 1 69  ? -4.191  18.982 26.611  1.00 14.13 ? 69  TYR   B CB  1 
ATOM   1278 C  CG  . TYR   B 1 69  ? -4.845  19.669 27.776  1.00 15.03 ? 69  TYR   B CG  1 
ATOM   1279 C  CD1 . TYR   B 1 69  ? -6.227  19.770 27.879  1.00 16.50 ? 69  TYR   B CD1 1 
ATOM   1280 C  CD2 . TYR   B 1 69  ? -4.069  20.257 28.748  1.00 16.03 ? 69  TYR   B CD2 1 
ATOM   1281 C  CE1 . TYR   B 1 69  ? -6.827  20.424 28.952  1.00 16.44 ? 69  TYR   B CE1 1 
ATOM   1282 C  CE2 . TYR   B 1 69  ? -4.681  20.923 29.855  1.00 16.75 ? 69  TYR   B CE2 1 
ATOM   1283 C  CZ  . TYR   B 1 69  ? -6.044  21.025 29.911  1.00 16.46 ? 69  TYR   B CZ  1 
ATOM   1284 O  OH  . TYR   B 1 69  ? -6.607  21.691 30.989  1.00 20.34 ? 69  TYR   B OH  1 
ATOM   1285 N  N   . LYS   B 1 70  ? -1.897  19.558 24.462  1.00 12.29 ? 70  LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 1 70  ? -0.869  18.997 23.623  1.00 13.58 ? 70  LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 1 70  ? 0.187   18.365 24.494  1.00 13.42 ? 70  LYS   B C   1 
ATOM   1288 O  O   . LYS   B 1 70  ? 0.738   19.046 25.363  1.00 15.20 ? 70  LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 1 70  ? -0.240  20.089 22.724  1.00 15.55 ? 70  LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 1 70  ? 0.981   19.659 21.980  1.00 15.50 ? 70  LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 1 70  ? 1.346   20.632 20.905  1.00 21.46 ? 70  LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 1 70  ? 1.532   22.034 21.416  1.00 26.50 ? 70  LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 1 70  ? 1.949   23.007 20.344  1.00 34.30 ? 70  LYS   B NZ  1 
ATOM   1294 N  N   . VAL   B 1 71  ? 0.453   17.099 24.265  1.00 12.43 ? 71  VAL   B N   1 
ATOM   1295 C  CA  . VAL   B 1 71  ? 1.493   16.359 24.907  1.00 12.72 ? 71  VAL   B CA  1 
ATOM   1296 C  C   . VAL   B 1 71  ? 2.645   16.215 23.907  1.00 11.73 ? 71  VAL   B C   1 
ATOM   1297 O  O   . VAL   B 1 71  ? 2.500   15.503 22.932  1.00 14.30 ? 71  VAL   B O   1 
ATOM   1298 C  CB  . VAL   B 1 71  ? 0.989   14.987 25.423  1.00 13.67 ? 71  VAL   B CB  1 
ATOM   1299 C  CG1 . VAL   B 1 71  ? 2.086   14.193 26.048  1.00 14.32 ? 71  VAL   B CG1 1 
ATOM   1300 C  CG2 . VAL   B 1 71  ? -0.178  15.209 26.370  1.00 13.99 ? 71  VAL   B CG2 1 
ATOM   1301 N  N   . GLU   B 1 72  ? 3.790   16.814 24.199  1.00 12.92 ? 72  GLU   B N   1 
ATOM   1302 C  CA  . GLU   B 1 72  ? 4.976   16.766 23.293  1.00 14.68 ? 72  GLU   B CA  1 
ATOM   1303 C  C   . GLU   B 1 72  ? 6.009   15.809 23.935  1.00 12.96 ? 72  GLU   B C   1 
ATOM   1304 O  O   . GLU   B 1 72  ? 6.527   16.104 24.990  1.00 14.43 ? 72  GLU   B O   1 
ATOM   1305 C  CB  . GLU   B 1 72  ? 5.599   18.185 23.154  1.00 15.65 ? 72  GLU   B CB  1 
ATOM   1306 C  CG  . GLU   B 1 72  ? 4.677   19.337 22.684  1.00 18.68 ? 72  GLU   B CG  1 
ATOM   1307 C  CD  . GLU   B 1 72  ? 5.358   20.650 22.338  1.00 21.45 ? 72  GLU   B CD  1 
ATOM   1308 O  OE1 . GLU   B 1 72  ? 6.573   20.748 22.446  1.00 22.18 ? 72  GLU   B OE1 1 
ATOM   1309 O  OE2 . GLU   B 1 72  ? 4.653   21.592 21.874  0.50 21.16 ? 72  GLU   B OE2 1 
ATOM   1310 N  N   . ILE   B 1 73  ? 6.234   14.694 23.279  1.00 13.47 ? 73  ILE   B N   1 
ATOM   1311 C  CA  . ILE   B 1 73  ? 7.142   13.671 23.731  1.00 12.61 ? 73  ILE   B CA  1 
ATOM   1312 C  C   . ILE   B 1 73  ? 8.449   13.769 22.946  1.00 11.82 ? 73  ILE   B C   1 
ATOM   1313 O  O   . ILE   B 1 73  ? 8.423   13.683 21.722  1.00 13.23 ? 73  ILE   B O   1 
ATOM   1314 C  CB  . ILE   B 1 73  ? 6.510   12.274 23.550  1.00 14.07 ? 73  ILE   B CB  1 
ATOM   1315 C  CG1 . ILE   B 1 73  ? 5.102   12.217 24.225  1.00 14.26 ? 73  ILE   B CG1 1 
ATOM   1316 C  CG2 . ILE   B 1 73  ? 7.467   11.222 24.108  1.00 14.54 ? 73  ILE   B CG2 1 
ATOM   1317 C  CD1 . ILE   B 1 73  ? 4.342   10.943 23.957  1.00 16.83 ? 73  ILE   B CD1 1 
ATOM   1318 N  N   . ASP   B 1 74  ? 9.552   13.983 23.648  1.00 13.31 ? 74  ASP   B N   1 
ATOM   1319 C  CA  . ASP   B 1 74  ? 10.853  14.170 22.984  1.00 13.62 ? 74  ASP   B CA  1 
ATOM   1320 C  C   . ASP   B 1 74  ? 11.446  12.811 22.589  1.00 13.38 ? 74  ASP   B C   1 
ATOM   1321 O  O   . ASP   B 1 74  ? 12.391  12.327 23.186  1.00 15.12 ? 74  ASP   B O   1 
ATOM   1322 C  CB  . ASP   B 1 74  ? 11.805  15.020 23.826  1.00 16.00 ? 74  ASP   B CB  1 
ATOM   1323 C  CG  . ASP   B 1 74  ? 13.074  15.377 23.076  1.00 18.08 ? 74  ASP   B CG  1 
ATOM   1324 O  OD1 . ASP   B 1 74  ? 13.209  14.962 21.909  1.00 19.21 ? 74  ASP   B OD1 1 
ATOM   1325 O  OD2 . ASP   B 1 74  ? 13.942  16.018 23.716  1.00 24.89 ? 74  ASP   B OD2 1 
ATOM   1326 N  N   . THR   B 1 75  ? 10.894  12.213 21.557  1.00 12.42 ? 75  THR   B N   1 
ATOM   1327 C  CA  . THR   B 1 75  ? 11.317  10.941 21.097  1.00 12.57 ? 75  THR   B CA  1 
ATOM   1328 C  C   . THR   B 1 75  ? 12.681  11.006 20.426  1.00 12.69 ? 75  THR   B C   1 
ATOM   1329 O  O   . THR   B 1 75  ? 13.440  10.044 20.484  1.00 13.00 ? 75  THR   B O   1 
ATOM   1330 C  CB  . THR   B 1 75  ? 10.320  10.377 20.122  1.00 11.99 ? 75  THR   B CB  1 
ATOM   1331 O  OG1 . THR   B 1 75  ? 10.127  11.233 19.030  1.00 12.52 ? 75  THR   B OG1 1 
ATOM   1332 C  CG2 . THR   B 1 75  ? 8.955   10.161 20.775  1.00 13.81 ? 75  THR   B CG2 1 
ATOM   1333 N  N   . LYS   B 1 76  ? 13.045  12.139 19.800  1.00 13.28 ? 76  LYS   B N   1 
ATOM   1334 C  CA  . LYS   B 1 76  ? 14.315  12.224 19.119  1.00 13.09 ? 76  LYS   B CA  1 
ATOM   1335 C  C   . LYS   B 1 76  ? 15.453  12.107 20.101  1.00 13.61 ? 76  LYS   B C   1 
ATOM   1336 O  O   . LYS   B 1 76  ? 16.418  11.382 19.860  1.00 14.34 ? 76  LYS   B O   1 
ATOM   1337 C  CB  . LYS   B 1 76  ? 14.382  13.527 18.315  1.00 15.48 ? 76  LYS   B CB  1 
ATOM   1338 C  CG  . LYS   B 1 76  ? 15.549  13.594 17.331  1.00 19.55 ? 76  LYS   B CG  1 
ATOM   1339 C  CD  . LYS   B 1 76  ? 15.567  14.951 16.618  1.00 21.04 ? 76  LYS   B CD  1 
ATOM   1340 C  CE  . LYS   B 1 76  ? 16.585  14.889 15.501  1.00 23.61 ? 76  LYS   B CE  1 
ATOM   1341 N  NZ  . LYS   B 1 76  ? 16.660  16.073 14.613  1.00 26.55 ? 76  LYS   B NZ  1 
ATOM   1342 N  N   . SER   B 1 77  ? 15.379  12.854 21.229  1.00 14.44 ? 77  SER   B N   1 
ATOM   1343 C  CA  . SER   B 1 77  ? 16.462  12.758 22.229  1.00 16.49 ? 77  SER   B CA  1 
ATOM   1344 C  C   . SER   B 1 77  ? 16.496  11.359 22.798  1.00 14.05 ? 77  SER   B C   1 
ATOM   1345 O  O   . SER   B 1 77  ? 17.570  10.891 23.104  1.00 16.17 ? 77  SER   B O   1 
ATOM   1346 C  CB  . SER   B 1 77  ? 16.168  13.723 23.325  1.00 19.10 ? 77  SER   B CB  1 
ATOM   1347 O  OG  . SER   B 1 77  ? 16.323  15.050 22.867  1.00 22.11 ? 77  SER   B OG  1 
ATOM   1348 N  N   . TYR   B 1 78  ? 15.344  10.698 22.973  1.00 13.65 ? 78  TYR   B N   1 
ATOM   1349 C  CA  . TYR   B 1 78  ? 15.320  9.343  23.504  1.00 13.16 ? 78  TYR   B CA  1 
ATOM   1350 C  C   . TYR   B 1 78  ? 16.121  8.368  22.620  1.00 13.04 ? 78  TYR   B C   1 
ATOM   1351 O  O   . TYR   B 1 78  ? 16.999  7.629  23.086  1.00 14.13 ? 78  TYR   B O   1 
ATOM   1352 C  CB  . TYR   B 1 78  ? 13.873  8.867  23.644  1.00 13.59 ? 78  TYR   B CB  1 
ATOM   1353 C  CG  . TYR   B 1 78  ? 13.714  7.397  24.070  1.00 13.08 ? 78  TYR   B CG  1 
ATOM   1354 C  CD1 . TYR   B 1 78  ? 13.952  7.018  25.345  1.00 14.50 ? 78  TYR   B CD1 1 
ATOM   1355 C  CD2 . TYR   B 1 78  ? 13.444  6.408  23.162  1.00 13.95 ? 78  TYR   B CD2 1 
ATOM   1356 C  CE1 . TYR   B 1 78  ? 13.900  5.738  25.759  1.00 14.99 ? 78  TYR   B CE1 1 
ATOM   1357 C  CE2 . TYR   B 1 78  ? 13.379  5.115  23.525  1.00 13.37 ? 78  TYR   B CE2 1 
ATOM   1358 C  CZ  . TYR   B 1 78  ? 13.606  4.771  24.846  1.00 14.87 ? 78  TYR   B CZ  1 
ATOM   1359 O  OH  . TYR   B 1 78  ? 13.518  3.481  25.304  1.00 15.45 ? 78  TYR   B OH  1 
ATOM   1360 N  N   . TRP   B 1 79  ? 15.833  8.362  21.323  1.00 12.17 ? 79  TRP   B N   1 
ATOM   1361 C  CA  . TRP   B 1 79  ? 16.520  7.462  20.409  1.00 12.20 ? 79  TRP   B CA  1 
ATOM   1362 C  C   . TRP   B 1 79  ? 17.972  7.789  20.300  1.00 13.67 ? 79  TRP   B C   1 
ATOM   1363 O  O   . TRP   B 1 79  ? 18.838  6.931  20.317  1.00 16.07 ? 79  TRP   B O   1 
ATOM   1364 C  CB  . TRP   B 1 79  ? 15.858  7.465  19.040  1.00 12.45 ? 79  TRP   B CB  1 
ATOM   1365 C  CG  . TRP   B 1 79  ? 14.503  6.836  19.031  1.00 11.21 ? 79  TRP   B CG  1 
ATOM   1366 C  CD1 . TRP   B 1 79  ? 13.315  7.433  18.767  1.00 10.00 ? 79  TRP   B CD1 1 
ATOM   1367 C  CD2 . TRP   B 1 79  ? 14.169  5.446  19.368  1.00 11.51 ? 79  TRP   B CD2 1 
ATOM   1368 N  NE1 . TRP   B 1 79  ? 12.277  6.537  18.886  1.00 11.50 ? 79  TRP   B NE1 1 
ATOM   1369 C  CE2 . TRP   B 1 79  ? 12.775  5.334  19.263  1.00 10.97 ? 79  TRP   B CE2 1 
ATOM   1370 C  CE3 . TRP   B 1 79  ? 14.922  4.315  19.731  1.00 12.39 ? 79  TRP   B CE3 1 
ATOM   1371 C  CZ2 . TRP   B 1 79  ? 12.120  4.133  19.544  1.00 11.57 ? 79  TRP   B CZ2 1 
ATOM   1372 C  CZ3 . TRP   B 1 79  ? 14.250  3.191  20.016  1.00 13.27 ? 79  TRP   B CZ3 1 
ATOM   1373 C  CH2 . TRP   B 1 79  ? 12.891  3.061  19.919  1.00 12.59 ? 79  TRP   B CH2 1 
ATOM   1374 N  N   . LYS   B 1 80  ? 18.313  9.061  20.261  1.00 14.55 ? 80  LYS   B N   1 
ATOM   1375 C  CA  . LYS   B 1 80  ? 19.739  9.410  20.109  1.00 17.04 ? 80  LYS   B CA  1 
ATOM   1376 C  C   . LYS   B 1 80  ? 20.541  9.013  21.310  1.00 16.12 ? 80  LYS   B C   1 
ATOM   1377 O  O   . LYS   B 1 80  ? 21.687  8.617  21.179  1.00 19.45 ? 80  LYS   B O   1 
ATOM   1378 C  CB  . LYS   B 1 80  ? 19.891  10.840 19.759  1.00 20.57 ? 80  LYS   B CB  1 
ATOM   1379 C  CG  . LYS   B 1 80  ? 19.447  11.029 18.344  1.00 22.38 ? 80  LYS   B CG  1 
ATOM   1380 C  CD  . LYS   B 1 80  ? 19.829  12.406 17.773  1.00 25.79 ? 80  LYS   B CD  1 
ATOM   1381 C  CE  . LYS   B 1 80  ? 19.325  12.523 16.376  1.00 27.30 ? 80  LYS   B CE  1 
ATOM   1382 N  N   . ALA   B 1 81  ? 19.947  9.078  22.519  1.00 17.23 ? 81  ALA   B N   1 
ATOM   1383 C  CA  . ALA   B 1 81  ? 20.694  8.675  23.740  1.00 20.25 ? 81  ALA   B CA  1 
ATOM   1384 C  C   . ALA   B 1 81  ? 20.978  7.189  23.735  1.00 21.12 ? 81  ALA   B C   1 
ATOM   1385 O  O   . ALA   B 1 81  ? 21.918  6.717  24.371  1.00 24.35 ? 81  ALA   B O   1 
ATOM   1386 C  CB  . ALA   B 1 81  ? 19.947  9.091  25.001  1.00 22.68 ? 81  ALA   B CB  1 
ATOM   1387 N  N   . LEU   B 1 82  ? 20.178  6.433  22.959  1.00 19.07 ? 82  LEU   B N   1 
ATOM   1388 C  CA  . LEU   B 1 82  ? 20.403  5.022  22.725  1.00 21.98 ? 82  LEU   B CA  1 
ATOM   1389 C  C   . LEU   B 1 82  ? 21.244  4.732  21.522  1.00 22.32 ? 82  LEU   B C   1 
ATOM   1390 O  O   . LEU   B 1 82  ? 21.476  3.577  21.202  1.00 25.56 ? 82  LEU   B O   1 
ATOM   1391 C  CB  . LEU   B 1 82  ? 19.091  4.304  22.556  1.00 20.23 ? 82  LEU   B CB  1 
ATOM   1392 C  CG  . LEU   B 1 82  ? 18.155  4.316  23.737  1.00 25.88 ? 82  LEU   B CG  1 
ATOM   1393 C  CD1 . LEU   B 1 82  ? 16.810  3.729  23.406  1.00 27.74 ? 82  LEU   B CD1 1 
ATOM   1394 C  CD2 . LEU   B 1 82  ? 18.769  3.438  24.824  1.00 34.53 ? 82  LEU   B CD2 1 
ATOM   1395 N  N   . GLY   B 1 83  ? 21.750  5.750  20.843  1.00 19.50 ? 83  GLY   B N   1 
ATOM   1396 C  CA  . GLY   B 1 83  ? 22.560  5.521  19.662  1.00 20.14 ? 83  GLY   B CA  1 
ATOM   1397 C  C   . GLY   B 1 83  ? 21.817  5.158  18.376  1.00 22.98 ? 83  GLY   B C   1 
ATOM   1398 O  O   . GLY   B 1 83  ? 22.429  4.570  17.458  1.00 21.29 ? 83  GLY   B O   1 
ATOM   1399 N  N   . ILE   B 1 84  ? 20.558  5.462  18.283  1.00 17.90 ? 84  ILE   B N   1 
ATOM   1400 C  CA  . ILE   B 1 84  ? 19.711  5.048  17.206  1.00 17.94 ? 84  ILE   B CA  1 
ATOM   1401 C  C   . ILE   B 1 84  ? 19.208  6.296  16.452  1.00 17.72 ? 84  ILE   B C   1 
ATOM   1402 O  O   . ILE   B 1 84  ? 18.742  7.225  17.114  1.00 16.88 ? 84  ILE   B O   1 
ATOM   1403 C  CB  . ILE   B 1 84  ? 18.514  4.227  17.759  1.00 22.27 ? 84  ILE   B CB  1 
ATOM   1404 C  CG1 . ILE   B 1 84  ? 19.062  2.914  18.313  1.00 22.80 ? 84  ILE   B CG1 1 
ATOM   1405 C  CG2 . ILE   B 1 84  ? 17.488  3.936  16.632  1.00 23.91 ? 84  ILE   B CG2 1 
ATOM   1406 C  CD1 . ILE   B 1 84  ? 18.102  2.196  19.228  1.00 22.99 ? 84  ILE   B CD1 1 
ATOM   1407 N  N   . SER   B 1 85  ? 19.228  6.296  15.104  1.00 20.06 ? 85  SER   B N   1 
ATOM   1408 C  CA  . SER   B 1 85  ? 18.804  7.438  14.295  1.00 21.66 ? 85  SER   B CA  1 
ATOM   1409 C  C   . SER   B 1 85  ? 17.298  7.303  14.223  1.00 18.71 ? 85  SER   B C   1 
ATOM   1410 O  O   . SER   B 1 85  ? 16.692  6.330  13.762  1.00 23.23 ? 85  SER   B O   1 
ATOM   1411 C  CB  . SER   B 1 85  ? 19.400  7.409  12.817  1.00 20.74 ? 85  SER   B CB  1 
ATOM   1412 O  OG  . SER   B 1 85  ? 18.942  8.584  12.142  1.00 26.36 ? 85  SER   B OG  1 
ATOM   1413 N  N   . PRO   B 1 86  ? 16.655  8.366  14.629  1.00 15.74 ? 86  PRO   B N   1 
ATOM   1414 C  CA  . PRO   B 1 86  ? 15.229  8.397  14.614  1.00 15.13 ? 86  PRO   B CA  1 
ATOM   1415 C  C   . PRO   B 1 86  ? 14.671  9.160  13.397  1.00 15.98 ? 86  PRO   B C   1 
ATOM   1416 O  O   . PRO   B 1 86  ? 15.301  10.121 12.945  1.00 16.75 ? 86  PRO   B O   1 
ATOM   1417 C  CB  . PRO   B 1 86  ? 14.909  9.198  15.910  1.00 20.17 ? 86  PRO   B CB  1 
ATOM   1418 C  CG  . PRO   B 1 86  ? 16.051  10.164 16.047  1.00 23.51 ? 86  PRO   B CG  1 
ATOM   1419 C  CD  . PRO   B 1 86  ? 17.211  9.415  15.532  1.00 19.33 ? 86  PRO   B CD  1 
ATOM   1420 N  N   . PHE   B 1 87  ? 13.461  8.835  12.976  1.00 11.73 ? 87  PHE   B N   1 
ATOM   1421 C  CA  . PHE   B 1 87  ? 12.806  9.570  11.929  1.00 12.10 ? 87  PHE   B CA  1 
ATOM   1422 C  C   . PHE   B 1 87  ? 12.190  10.893 12.407  1.00 11.87 ? 87  PHE   B C   1 
ATOM   1423 O  O   . PHE   B 1 87  ? 12.268  11.869 11.677  1.00 11.72 ? 87  PHE   B O   1 
ATOM   1424 C  CB  . PHE   B 1 87  ? 11.717  8.668  11.314  1.00 13.26 ? 87  PHE   B CB  1 
ATOM   1425 C  CG  . PHE   B 1 87  ? 10.966  9.273  10.215  1.00 12.30 ? 87  PHE   B CG  1 
ATOM   1426 C  CD1 . PHE   B 1 87  ? 11.569  9.486  8.965   1.00 12.97 ? 87  PHE   B CD1 1 
ATOM   1427 C  CD2 . PHE   B 1 87  ? 9.630   9.667  10.371  1.00 12.25 ? 87  PHE   B CD2 1 
ATOM   1428 C  CE1 . PHE   B 1 87  ? 10.837  10.090 7.947   1.00 12.56 ? 87  PHE   B CE1 1 
ATOM   1429 C  CE2 . PHE   B 1 87  ? 8.948   10.287 9.362   1.00 13.63 ? 87  PHE   B CE2 1 
ATOM   1430 C  CZ  . PHE   B 1 87  ? 9.555   10.456 8.140   1.00 12.65 ? 87  PHE   B CZ  1 
ATOM   1431 N  N   . HIS   B 1 88  ? 11.462  10.879 13.502  1.00 12.52 ? 88  HIS   B N   1 
ATOM   1432 C  CA  . HIS   B 1 88  ? 10.649  12.016 13.861  1.00 12.59 ? 88  HIS   B CA  1 
ATOM   1433 C  C   . HIS   B 1 88  ? 11.398  13.020 14.662  1.00 12.04 ? 88  HIS   B C   1 
ATOM   1434 O  O   . HIS   B 1 88  ? 12.350  12.729 15.393  1.00 14.21 ? 88  HIS   B O   1 
ATOM   1435 C  CB  . HIS   B 1 88  ? 9.474   11.597 14.664  1.00 12.75 ? 88  HIS   B CB  1 
ATOM   1436 C  CG  . HIS   B 1 88  ? 8.651   10.528 14.108  1.00 12.98 ? 88  HIS   B CG  1 
ATOM   1437 N  ND1 . HIS   B 1 88  ? 7.663   10.666 13.199  1.00 15.98 ? 88  HIS   B ND1 1 
ATOM   1438 C  CD2 . HIS   B 1 88  ? 8.786   9.218  14.310  1.00 14.14 ? 88  HIS   B CD2 1 
ATOM   1439 C  CE1 . HIS   B 1 88  ? 7.176   9.470  12.873  1.00 11.76 ? 88  HIS   B CE1 1 
ATOM   1440 N  NE2 . HIS   B 1 88  ? 7.847   8.613  13.576  1.00 16.72 ? 88  HIS   B NE2 1 
ATOM   1441 N  N   . GLU   B 1 89  ? 10.978  14.279 14.532  1.00 11.82 ? 89  GLU   B N   1 
ATOM   1442 C  CA  . GLU   B 1 89  ? 11.446  15.302 15.410  1.00 13.26 ? 89  GLU   B CA  1 
ATOM   1443 C  C   . GLU   B 1 89  ? 10.969  15.165 16.855  1.00 13.06 ? 89  GLU   B C   1 
ATOM   1444 O  O   . GLU   B 1 89  ? 11.628  15.612 17.755  1.00 15.33 ? 89  GLU   B O   1 
ATOM   1445 C  CB  . GLU   B 1 89  ? 11.022  16.666 14.879  1.00 14.12 ? 89  GLU   B CB  1 
ATOM   1446 C  CG  . GLU   B 1 89  ? 11.798  17.133 13.669  1.00 15.22 ? 89  GLU   B CG  1 
ATOM   1447 C  CD  . GLU   B 1 89  ? 13.300  17.248 13.971  1.00 18.11 ? 89  GLU   B CD  1 
ATOM   1448 O  OE1 . GLU   B 1 89  ? 13.646  18.111 14.730  1.00 23.75 ? 89  GLU   B OE1 1 
ATOM   1449 O  OE2 . GLU   B 1 89  ? 14.062  16.468 13.458  1.00 21.87 ? 89  GLU   B OE2 1 
ATOM   1450 N  N   . HIS   B 1 90  ? 9.799   14.562 17.029  1.00 12.11 ? 90  HIS   B N   1 
ATOM   1451 C  CA  . HIS   B 1 90  ? 9.094   14.430 18.319  1.00 12.91 ? 90  HIS   B CA  1 
ATOM   1452 C  C   . HIS   B 1 90  ? 7.844   13.687 18.026  1.00 11.68 ? 90  HIS   B C   1 
ATOM   1453 O  O   . HIS   B 1 90  ? 7.552   13.349 16.862  1.00 13.74 ? 90  HIS   B O   1 
ATOM   1454 C  CB  . HIS   B 1 90  ? 8.748   15.778 18.968  1.00 13.94 ? 90  HIS   B CB  1 
ATOM   1455 C  CG  . HIS   B 1 90  ? 8.359   16.860 18.030  1.00 17.28 ? 90  HIS   B CG  1 
ATOM   1456 N  ND1 . HIS   B 1 90  ? 7.218   16.833 17.309  1.00 20.41 ? 90  HIS   B ND1 1 
ATOM   1457 C  CD2 . HIS   B 1 90  ? 9.006   18.003 17.682  1.00 21.54 ? 90  HIS   B CD2 1 
ATOM   1458 C  CE1 . HIS   B 1 90  ? 7.127   17.952 16.573  1.00 18.19 ? 90  HIS   B CE1 1 
ATOM   1459 N  NE2 . HIS   B 1 90  ? 8.242   18.654 16.753  1.00 22.33 ? 90  HIS   B NE2 1 
ATOM   1460 N  N   . ALA   B 1 91  ? 7.063   13.389 19.055  1.00 12.66 ? 91  ALA   B N   1 
ATOM   1461 C  CA  . ALA   B 1 91  ? 5.731   12.885 18.927  1.00 12.96 ? 91  ALA   B CA  1 
ATOM   1462 C  C   . ALA   B 1 91  ? 4.816   13.768 19.709  1.00 13.40 ? 91  ALA   B C   1 
ATOM   1463 O  O   . ALA   B 1 91  ? 4.963   13.870 20.910  1.00 15.75 ? 91  ALA   B O   1 
ATOM   1464 C  CB  . ALA   B 1 91  ? 5.621   11.421 19.416  1.00 14.51 ? 91  ALA   B CB  1 
ATOM   1465 N  N   . GLU   B 1 92  ? 3.885   14.452 19.039  1.00 16.17 ? 92  GLU   B N   1 
ATOM   1466 C  CA  . GLU   B 1 92  ? 2.988   15.426 19.714  1.00 15.89 ? 92  GLU   B CA  1 
ATOM   1467 C  C   . GLU   B 1 92  ? 1.603   14.911 19.558  1.00 17.70 ? 92  GLU   B C   1 
ATOM   1468 O  O   . GLU   B 1 92  ? 1.150   14.682 18.456  1.00 23.71 ? 92  GLU   B O   1 
ATOM   1469 C  CB  . GLU   B 1 92  ? 3.244   16.925 19.176  1.00 19.94 ? 92  GLU   B CB  1 
ATOM   1470 C  CG  . GLU   B 1 92  ? 4.655   17.516 19.400  1.00 19.19 ? 92  GLU   B CG  1 
ATOM   1471 C  CD  . GLU   B 1 92  ? 4.841   19.013 19.020  0.50 14.03 ? 92  GLU   B CD  1 
ATOM   1472 O  OE1 . GLU   B 1 92  ? 3.920   19.723 18.638  0.50 15.18 ? 92  GLU   B OE1 1 
ATOM   1473 O  OE2 . GLU   B 1 92  ? 5.996   19.457 19.130  0.50 16.04 ? 92  GLU   B OE2 1 
ATOM   1474 N  N   . VAL   B 1 93  ? 0.905   14.774 20.717  1.00 13.58 ? 93  VAL   B N   1 
ATOM   1475 C  CA  . VAL   B 1 93  ? -0.449  14.204 20.824  1.00 13.05 ? 93  VAL   B CA  1 
ATOM   1476 C  C   . VAL   B 1 93  ? -1.428  15.287 21.303  1.00 12.42 ? 93  VAL   B C   1 
ATOM   1477 O  O   . VAL   B 1 93  ? -1.172  15.904 22.322  1.00 12.90 ? 93  VAL   B O   1 
ATOM   1478 C  CB  . VAL   B 1 93  ? -0.485  13.020 21.815  1.00 14.79 ? 93  VAL   B CB  1 
ATOM   1479 C  CG1 . VAL   B 1 93  ? -1.849  12.457 21.933  1.00 14.82 ? 93  VAL   B CG1 1 
ATOM   1480 C  CG2 . VAL   B 1 93  ? 0.510   11.939 21.431  1.00 17.45 ? 93  VAL   B CG2 1 
ATOM   1481 N  N   . VAL   B 1 94  ? -2.438  15.604 20.508  1.00 12.42 ? 94  VAL   B N   1 
ATOM   1482 C  CA  . VAL   B 1 94  ? -3.307  16.778 20.745  1.00 11.97 ? 94  VAL   B CA  1 
ATOM   1483 C  C   . VAL   B 1 94  ? -4.747  16.277 20.861  1.00 12.38 ? 94  VAL   B C   1 
ATOM   1484 O  O   . VAL   B 1 94  ? -5.246  15.529 20.016  1.00 13.00 ? 94  VAL   B O   1 
ATOM   1485 C  CB  . VAL   B 1 94  ? -3.159  17.809 19.607  1.00 12.90 ? 94  VAL   B CB  1 
ATOM   1486 C  CG1 . VAL   B 1 94  ? -3.949  19.026 19.933  1.00 15.80 ? 94  VAL   B CG1 1 
ATOM   1487 C  CG2 . VAL   B 1 94  ? -1.713  18.194 19.427  1.00 15.46 ? 94  VAL   B CG2 1 
ATOM   1488 N  N   . PHE   B 1 95  ? -5.410  16.683 21.940  1.00 13.41 ? 95  PHE   B N   1 
ATOM   1489 C  CA  . PHE   B 1 95  ? -6.752  16.171 22.250  1.00 13.49 ? 95  PHE   B CA  1 
ATOM   1490 C  C   . PHE   B 1 95  ? -7.547  17.193 23.077  1.00 14.45 ? 95  PHE   B C   1 
ATOM   1491 O  O   . PHE   B 1 95  ? -6.999  18.026 23.736  1.00 14.70 ? 95  PHE   B O   1 
ATOM   1492 C  CB  . PHE   B 1 95  ? -6.665  14.854 23.020  1.00 14.95 ? 95  PHE   B CB  1 
ATOM   1493 C  CG  . PHE   B 1 95  ? -6.045  14.961 24.406  1.00 15.07 ? 95  PHE   B CG  1 
ATOM   1494 C  CD1 . PHE   B 1 95  ? -4.681  15.001 24.579  1.00 21.63 ? 95  PHE   B CD1 1 
ATOM   1495 C  CD2 . PHE   B 1 95  ? -6.870  15.035 25.523  1.00 19.34 ? 95  PHE   B CD2 1 
ATOM   1496 C  CE1 . PHE   B 1 95  ? -4.146  15.077 25.897  1.00 19.16 ? 95  PHE   B CE1 1 
ATOM   1497 C  CE2 . PHE   B 1 95  ? -6.359  15.152 26.808  1.00 20.51 ? 95  PHE   B CE2 1 
ATOM   1498 C  CZ  . PHE   B 1 95  ? -5.040  15.173 26.946  1.00 21.37 ? 95  PHE   B CZ  1 
ATOM   1499 N  N   . THR   B 1 96  ? -8.872  17.106 22.991  1.00 16.74 ? 96  THR   B N   1 
ATOM   1500 C  CA  . THR   B 1 96  ? -9.732  17.880 23.846  1.00 17.02 ? 96  THR   B CA  1 
ATOM   1501 C  C   . THR   B 1 96  ? -10.042 17.068 25.090  1.00 19.07 ? 96  THR   B C   1 
ATOM   1502 O  O   . THR   B 1 96  ? -10.442 15.934 25.056  1.00 21.62 ? 96  THR   B O   1 
ATOM   1503 C  CB  . THR   B 1 96  ? -11.055 18.287 23.105  1.00 19.03 ? 96  THR   B CB  1 
ATOM   1504 O  OG1 . THR   B 1 96  ? -10.697 19.062 21.972  1.00 19.93 ? 96  THR   B OG1 1 
ATOM   1505 C  CG2 . THR   B 1 96  ? -11.975 19.092 24.033  1.00 20.67 ? 96  THR   B CG2 1 
ATOM   1506 N  N   . ALA   B 1 97  ? -9.928  17.734 26.231  1.00 20.10 ? 97  ALA   B N   1 
ATOM   1507 C  CA  . ALA   B 1 97  ? -10.479 17.190 27.475  1.00 20.58 ? 97  ALA   B CA  1 
ATOM   1508 C  C   . ALA   B 1 97  ? -11.964 17.709 27.689  1.00 30.65 ? 97  ALA   B C   1 
ATOM   1509 O  O   . ALA   B 1 97  ? -12.229 18.885 27.603  1.00 23.47 ? 97  ALA   B O   1 
ATOM   1510 C  CB  . ALA   B 1 97  ? -9.589  17.624 28.564  1.00 32.86 ? 97  ALA   B CB  1 
ATOM   1511 N  N   . ASN   B 1 98  ? -12.949 16.818 27.869  1.00 27.43 ? 98  ASN   B N   1 
ATOM   1512 C  CA  . ASN   B 1 98  ? -14.393 17.165 27.954  1.00 25.42 ? 98  ASN   B CA  1 
ATOM   1513 C  C   . ASN   B 1 98  ? -15.001 16.751 29.272  1.00 38.12 ? 98  ASN   B C   1 
ATOM   1514 O  O   . ASN   B 1 98  ? -14.757 15.615 29.666  1.00 25.20 ? 98  ASN   B O   1 
ATOM   1515 C  CB  . ASN   B 1 98  ? -15.140 16.608 26.717  1.00 30.19 ? 98  ASN   B CB  1 
ATOM   1516 N  N   . ARG   B 1 104 ? -10.315 10.642 34.110  1.00 32.91 ? 104 ARG   B N   1 
ATOM   1517 C  CA  . ARG   B 1 104 ? -8.891  10.374 34.235  1.00 27.64 ? 104 ARG   B CA  1 
ATOM   1518 C  C   . ARG   B 1 104 ? -8.415  9.915  32.834  1.00 24.01 ? 104 ARG   B C   1 
ATOM   1519 O  O   . ARG   B 1 104 ? -8.980  8.967  32.257  1.00 25.25 ? 104 ARG   B O   1 
ATOM   1520 C  CB  . ARG   B 1 104 ? -8.589  9.230  35.200  1.00 31.00 ? 104 ARG   B CB  1 
ATOM   1521 N  N   . TYR   B 1 105 ? -7.325  10.540 32.355  1.00 19.58 ? 105 TYR   B N   1 
ATOM   1522 C  CA  . TYR   B 1 105 ? -6.827  10.348 31.006  1.00 17.36 ? 105 TYR   B CA  1 
ATOM   1523 C  C   . TYR   B 1 105 ? -5.447  9.750  31.141  1.00 16.30 ? 105 TYR   B C   1 
ATOM   1524 O  O   . TYR   B 1 105 ? -4.575  10.358 31.761  1.00 18.96 ? 105 TYR   B O   1 
ATOM   1525 C  CB  . TYR   B 1 105 ? -6.720  11.655 30.232  1.00 18.61 ? 105 TYR   B CB  1 
ATOM   1526 C  CG  . TYR   B 1 105 ? -7.982  12.445 29.996  1.00 18.92 ? 105 TYR   B CG  1 
ATOM   1527 C  CD1 . TYR   B 1 105 ? -8.647  13.136 31.005  1.00 25.37 ? 105 TYR   B CD1 1 
ATOM   1528 C  CD2 . TYR   B 1 105 ? -8.600  12.429 28.725  1.00 22.26 ? 105 TYR   B CD2 1 
ATOM   1529 C  CE1 . TYR   B 1 105 ? -9.822  13.799 30.753  1.00 24.01 ? 105 TYR   B CE1 1 
ATOM   1530 C  CE2 . TYR   B 1 105 ? -9.782  13.123 28.531  1.00 19.37 ? 105 TYR   B CE2 1 
ATOM   1531 C  CZ  . TYR   B 1 105 ? -10.384 13.768 29.538  1.00 22.02 ? 105 TYR   B CZ  1 
ATOM   1532 O  OH  . TYR   B 1 105 ? -11.524 14.476 29.296  1.00 24.34 ? 105 TYR   B OH  1 
ATOM   1533 N  N   . THR   B 1 106 ? -5.232  8.632  30.439  1.00 15.07 ? 106 THR   B N   1 
ATOM   1534 C  CA  . THR   B 1 106 ? -3.915  8.136  30.215  1.00 14.47 ? 106 THR   B CA  1 
ATOM   1535 C  C   . THR   B 1 106 ? -3.611  8.230  28.714  1.00 13.06 ? 106 THR   B C   1 
ATOM   1536 O  O   . THR   B 1 106 ? -4.405  7.732  27.901  1.00 14.79 ? 106 THR   B O   1 
ATOM   1537 C  CB  . THR   B 1 106 ? -3.779  6.732  30.676  1.00 16.83 ? 106 THR   B CB  1 
ATOM   1538 O  OG1 . THR   B 1 106 ? -3.971  6.622  32.079  1.00 21.75 ? 106 THR   B OG1 1 
ATOM   1539 C  CG2 . THR   B 1 106 ? -2.409  6.145  30.364  1.00 19.19 ? 106 THR   B CG2 1 
ATOM   1540 N  N   . ILE   B 1 107 ? -2.493  8.879  28.393  1.00 12.96 ? 107 ILE   B N   1 
ATOM   1541 C  CA  . ILE   B 1 107 ? -1.983  8.956  27.045  1.00 12.01 ? 107 ILE   B CA  1 
ATOM   1542 C  C   . ILE   B 1 107 ? -0.826  7.989  26.955  1.00 11.34 ? 107 ILE   B C   1 
ATOM   1543 O  O   . ILE   B 1 107 ? 0.180   8.174  27.603  1.00 13.22 ? 107 ILE   B O   1 
ATOM   1544 C  CB  . ILE   B 1 107 ? -1.517  10.364 26.730  1.00 13.10 ? 107 ILE   B CB  1 
ATOM   1545 C  CG1 . ILE   B 1 107 ? -2.624  11.443 26.895  1.00 16.14 ? 107 ILE   B CG1 1 
ATOM   1546 C  CG2 . ILE   B 1 107 ? -0.882  10.421 25.350  1.00 14.12 ? 107 ILE   B CG2 1 
ATOM   1547 C  CD1 . ILE   B 1 107 ? -3.903  11.207 26.085  1.00 17.70 ? 107 ILE   B CD1 1 
ATOM   1548 N  N   . ALA   B 1 108 ? -1.018  6.929  26.182  1.00 11.81 ? 108 ALA   B N   1 
ATOM   1549 C  CA  . ALA   B 1 108 ? 0.013   5.925  26.073  1.00 12.93 ? 108 ALA   B CA  1 
ATOM   1550 C  C   . ALA   B 1 108 ? 0.631   5.985  24.674  1.00 13.32 ? 108 ALA   B C   1 
ATOM   1551 O  O   . ALA   B 1 108 ? -0.072  6.207  23.681  1.00 12.80 ? 108 ALA   B O   1 
ATOM   1552 C  CB  . ALA   B 1 108 ? -0.605  4.595  26.281  1.00 15.98 ? 108 ALA   B CB  1 
ATOM   1553 N  N   . ALA   B 1 109 ? 1.938   5.808  24.612  1.00 12.94 ? 109 ALA   B N   1 
ATOM   1554 C  CA  . ALA   B 1 109 ? 2.662   5.827  23.327  1.00 13.79 ? 109 ALA   B CA  1 
ATOM   1555 C  C   . ALA   B 1 109 ? 3.633   4.655  23.256  1.00 11.99 ? 109 ALA   B C   1 
ATOM   1556 O  O   . ALA   B 1 109 ? 4.288   4.307  24.210  1.00 15.43 ? 109 ALA   B O   1 
ATOM   1557 C  CB  . ALA   B 1 109 ? 3.426   7.137  23.180  1.00 14.68 ? 109 ALA   B CB  1 
ATOM   1558 N  N   . LEU   B 1 110 ? 3.676   4.021  22.075  1.00 10.29 ? 110 LEU   B N   1 
ATOM   1559 C  CA  . LEU   B 1 110 ? 4.570   2.899  21.766  1.00 10.16 ? 110 LEU   B CA  1 
ATOM   1560 C  C   . LEU   B 1 110 ? 5.483   3.383  20.657  1.00 9.15  ? 110 LEU   B C   1 
ATOM   1561 O  O   . LEU   B 1 110 ? 5.039   3.743  19.585  1.00 10.03 ? 110 LEU   B O   1 
ATOM   1562 C  CB  . LEU   B 1 110 ? 3.729   1.695  21.312  1.00 10.09 ? 110 LEU   B CB  1 
ATOM   1563 C  CG  . LEU   B 1 110 ? 4.574   0.454  20.914  1.00 11.06 ? 110 LEU   B CG  1 
ATOM   1564 C  CD1 . LEU   B 1 110 ? 5.385   -0.089 22.092  1.00 11.14 ? 110 LEU   B CD1 1 
ATOM   1565 C  CD2 . LEU   B 1 110 ? 3.653   -0.651 20.366  1.00 13.42 ? 110 LEU   B CD2 1 
ATOM   1566 N  N   . LEU   B 1 111 ? 6.790   3.389  20.937  1.00 9.37  ? 111 LEU   B N   1 
ATOM   1567 C  CA  . LEU   B 1 111 ? 7.798   3.988  20.074  1.00 9.53  ? 111 LEU   B CA  1 
ATOM   1568 C  C   . LEU   B 1 111 ? 8.655   2.968  19.337  1.00 9.61  ? 111 LEU   B C   1 
ATOM   1569 O  O   . LEU   B 1 111 ? 9.159   2.036  19.926  1.00 9.80  ? 111 LEU   B O   1 
ATOM   1570 C  CB  . LEU   B 1 111 ? 8.732   4.878  20.887  1.00 9.77  ? 111 LEU   B CB  1 
ATOM   1571 C  CG  . LEU   B 1 111 ? 8.126   5.929  21.820  1.00 11.47 ? 111 LEU   B CG  1 
ATOM   1572 C  CD1 . LEU   B 1 111 ? 9.276   6.732  22.436  1.00 12.19 ? 111 LEU   B CD1 1 
ATOM   1573 C  CD2 . LEU   B 1 111 ? 7.119   6.836  21.104  1.00 10.59 ? 111 LEU   B CD2 1 
ATOM   1574 N  N   . SER   B 1 112 ? 8.853   3.265  18.060  1.00 9.70  ? 112 SER   B N   1 
ATOM   1575 C  CA  . SER   B 1 112 ? 9.891   2.682  17.232  1.00 9.76  ? 112 SER   B CA  1 
ATOM   1576 C  C   . SER   B 1 112 ? 10.585  3.840  16.494  1.00 9.44  ? 112 SER   B C   1 
ATOM   1577 O  O   . SER   B 1 112 ? 10.129  4.922  16.396  1.00 9.79  ? 112 SER   B O   1 
ATOM   1578 C  CB  . SER   B 1 112 ? 9.293   1.671  16.229  1.00 10.56 ? 112 SER   B CB  1 
ATOM   1579 O  OG  . SER   B 1 112 ? 8.579   0.659  16.891  1.00 13.12 ? 112 SER   B OG  1 
ATOM   1580 N  N   . PRO   B 1 113 ? 11.770  3.504  15.902  1.00 9.33  ? 113 PRO   B N   1 
ATOM   1581 C  CA  . PRO   B 1 113 ? 12.557  4.600  15.287  1.00 9.06  ? 113 PRO   B CA  1 
ATOM   1582 C  C   . PRO   B 1 113 ? 11.822  5.320  14.160  1.00 9.61  ? 113 PRO   B C   1 
ATOM   1583 O  O   . PRO   B 1 113 ? 12.028  6.519  14.021  1.00 10.56 ? 113 PRO   B O   1 
ATOM   1584 C  CB  . PRO   B 1 113 ? 13.854  3.927  14.866  1.00 11.19 ? 113 PRO   B CB  1 
ATOM   1585 C  CG  . PRO   B 1 113 ? 14.022  2.892  15.968  1.00 12.37 ? 113 PRO   B CG  1 
ATOM   1586 C  CD  . PRO   B 1 113 ? 12.654  2.339  16.167  1.00 10.76 ? 113 PRO   B CD  1 
ATOM   1587 N  N   . TYR   B 1 114 ? 11.027  4.579  13.345  1.00 9.35  ? 114 TYR   B N   1 
ATOM   1588 C  CA  . TYR   B 1 114 ? 10.314  5.151  12.220  1.00 8.91  ? 114 TYR   B CA  1 
ATOM   1589 C  C   . TYR   B 1 114 ? 8.785   5.160  12.426  1.00 9.30  ? 114 TYR   B C   1 
ATOM   1590 O  O   . TYR   B 1 114 ? 8.083   5.456  11.498  1.00 12.06 ? 114 TYR   B O   1 
ATOM   1591 C  CB  . TYR   B 1 114 ? 10.672  4.479  10.907  1.00 9.99  ? 114 TYR   B CB  1 
ATOM   1592 C  CG  . TYR   B 1 114 ? 12.033  4.887  10.394  1.00 10.14 ? 114 TYR   B CG  1 
ATOM   1593 C  CD1 . TYR   B 1 114 ? 13.143  4.245  10.924  1.00 15.60 ? 114 TYR   B CD1 1 
ATOM   1594 C  CD2 . TYR   B 1 114 ? 12.180  5.783  9.374   1.00 10.59 ? 114 TYR   B CD2 1 
ATOM   1595 C  CE1 . TYR   B 1 114 ? 14.391  4.541  10.461  1.00 19.92 ? 114 TYR   B CE1 1 
ATOM   1596 C  CE2 . TYR   B 1 114 ? 13.443  6.186  8.913   1.00 12.84 ? 114 TYR   B CE2 1 
ATOM   1597 C  CZ  . TYR   B 1 114 ? 14.552  5.553  9.435   1.00 18.28 ? 114 TYR   B CZ  1 
ATOM   1598 O  OH  . TYR   B 1 114 ? 15.836  5.801  9.009   1.00 24.05 ? 114 TYR   B OH  1 
ATOM   1599 N  N   . SER   B 1 115 ? 8.318   4.892  13.635  1.00 9.65  ? 115 SER   B N   1 
ATOM   1600 C  CA  . SER   B 1 115 ? 6.875   4.764  13.843  1.00 9.02  ? 115 SER   B CA  1 
ATOM   1601 C  C   . SER   B 1 115 ? 6.528   5.055  15.265  1.00 9.74  ? 115 SER   B C   1 
ATOM   1602 O  O   . SER   B 1 115 ? 7.313   4.785  16.159  1.00 12.30 ? 115 SER   B O   1 
ATOM   1603 C  CB  . SER   B 1 115 ? 6.484   3.333  13.481  1.00 10.76 ? 115 SER   B CB  1 
ATOM   1604 O  OG  . SER   B 1 115 ? 5.167   3.031  13.716  1.00 15.56 ? 115 SER   B OG  1 
ATOM   1605 N  N   . TYR   B 1 116 ? 5.322   5.565  15.508  1.00 9.49  ? 116 TYR   B N   1 
ATOM   1606 C  CA  . TYR   B 1 116 ? 4.772   5.526  16.858  1.00 9.78  ? 116 TYR   B CA  1 
ATOM   1607 C  C   . TYR   B 1 116 ? 3.293   5.367  16.798  1.00 9.62  ? 116 TYR   B C   1 
ATOM   1608 O  O   . TYR   B 1 116 ? 2.635   5.741  15.835  1.00 9.73  ? 116 TYR   B O   1 
ATOM   1609 C  CB  . TYR   B 1 116 ? 5.155   6.723  17.711  1.00 11.42 ? 116 TYR   B CB  1 
ATOM   1610 C  CG  . TYR   B 1 116 ? 4.606   8.068  17.262  1.00 12.33 ? 116 TYR   B CG  1 
ATOM   1611 C  CD1 . TYR   B 1 116 ? 5.322   8.832  16.321  1.00 14.67 ? 116 TYR   B CD1 1 
ATOM   1612 C  CD2 . TYR   B 1 116 ? 3.479   8.589  17.759  1.00 13.68 ? 116 TYR   B CD2 1 
ATOM   1613 C  CE1 . TYR   B 1 116 ? 4.932   10.045 15.942  1.00 19.03 ? 116 TYR   B CE1 1 
ATOM   1614 C  CE2 . TYR   B 1 116 ? 3.052   9.895  17.322  1.00 17.07 ? 116 TYR   B CE2 1 
ATOM   1615 C  CZ  . TYR   B 1 116 ? 3.845   10.557 16.410  1.00 16.83 ? 116 TYR   B CZ  1 
ATOM   1616 O  OH  . TYR   B 1 116 ? 3.552   11.861 16.132  1.00 21.26 ? 116 TYR   B OH  1 
ATOM   1617 N  N   . SER   B 1 117 ? 2.766   4.775  17.854  1.00 10.44 ? 117 SER   B N   1 
ATOM   1618 C  CA  . SER   B 1 117 ? 1.343   4.575  18.049  1.00 10.57 ? 117 SER   B CA  1 
ATOM   1619 C  C   . SER   B 1 117 ? 0.948   5.169  19.368  1.00 10.45 ? 117 SER   B C   1 
ATOM   1620 O  O   . SER   B 1 117 ? 1.675   5.090  20.331  1.00 12.91 ? 117 SER   B O   1 
ATOM   1621 C  CB  . SER   B 1 117 ? 1.035   3.040  18.047  1.00 15.14 ? 117 SER   B CB  1 
ATOM   1622 O  OG  . SER   B 1 117 ? -0.305  2.739  18.359  1.00 17.10 ? 117 SER   B OG  1 
ATOM   1623 N  N   . THR   B 1 118 ? -0.237  5.761  19.400  1.00 10.61 ? 118 THR   B N   1 
ATOM   1624 C  CA  . THR   B 1 118 ? -0.728  6.288  20.658  1.00 10.78 ? 118 THR   B CA  1 
ATOM   1625 C  C   . THR   B 1 118 ? -2.182  5.947  20.862  1.00 10.44 ? 118 THR   B C   1 
ATOM   1626 O  O   . THR   B 1 118 ? -2.931  5.899  19.925  1.00 12.15 ? 118 THR   B O   1 
ATOM   1627 C  CB  . THR   B 1 118 ? -0.457  7.801  20.715  1.00 11.68 ? 118 THR   B CB  1 
ATOM   1628 O  OG1 . THR   B 1 118 ? -0.753  8.327  21.980  1.00 11.71 ? 118 THR   B OG1 1 
ATOM   1629 C  CG2 . THR   B 1 118 ? -1.267  8.663  19.691  1.00 12.21 ? 118 THR   B CG2 1 
ATOM   1630 N  N   . THR   B 1 119 ? -2.559  5.720  22.107  1.00 10.67 ? 119 THR   B N   1 
ATOM   1631 C  CA  . THR   B 1 119 ? -3.973  5.462  22.433  1.00 11.43 ? 119 THR   B CA  1 
ATOM   1632 C  C   . THR   B 1 119 ? -4.272  6.260  23.705  1.00 10.40 ? 119 THR   B C   1 
ATOM   1633 O  O   . THR   B 1 119 ? -3.401  6.686  24.419  1.00 13.23 ? 119 THR   B O   1 
ATOM   1634 C  CB  . THR   B 1 119 ? -4.343  3.961  22.539  1.00 14.26 ? 119 THR   B CB  1 
ATOM   1635 O  OG1 . THR   B 1 119 ? -5.761  3.813  22.442  1.00 14.45 ? 119 THR   B OG1 1 
ATOM   1636 C  CG2 . THR   B 1 119 ? -3.769  3.387  23.758  1.00 15.08 ? 119 THR   B CG2 1 
ATOM   1637 N  N   . ALA   B 1 120 ? -5.548  6.446  23.886  1.00 11.02 ? 120 ALA   B N   1 
ATOM   1638 C  CA  . ALA   B 1 120 ? -6.073  7.132  25.067  1.00 11.50 ? 120 ALA   B CA  1 
ATOM   1639 C  C   . ALA   B 1 120 ? -6.889  6.155  25.873  1.00 12.56 ? 120 ALA   B C   1 
ATOM   1640 O  O   . ALA   B 1 120 ? -7.687  5.428  25.318  1.00 14.73 ? 120 ALA   B O   1 
ATOM   1641 C  CB  . ALA   B 1 120 ? -6.877  8.360  24.691  1.00 15.61 ? 120 ALA   B CB  1 
ATOM   1642 N  N   . VAL   B 1 121 ? -6.715  6.147  27.166  1.00 14.30 ? 121 VAL   B N   1 
ATOM   1643 C  CA  . VAL   B 1 121 ? -7.497  5.351  28.110  1.00 18.71 ? 121 VAL   B CA  1 
ATOM   1644 C  C   . VAL   B 1 121 ? -8.152  6.319  29.056  1.00 20.58 ? 121 VAL   B C   1 
ATOM   1645 O  O   . VAL   B 1 121 ? -7.448  7.031  29.754  1.00 23.09 ? 121 VAL   B O   1 
ATOM   1646 C  CB  . VAL   B 1 121 ? -6.636  4.274  28.843  1.00 21.75 ? 121 VAL   B CB  1 
ATOM   1647 C  CG1 . VAL   B 1 121 ? -7.470  3.315  29.666  1.00 27.41 ? 121 VAL   B CG1 1 
ATOM   1648 C  CG2 . VAL   B 1 121 ? -5.701  3.515  27.912  1.00 24.23 ? 121 VAL   B CG2 1 
ATOM   1649 N  N   . VAL   B 1 122 ? -9.448  6.421  28.925  1.00 21.01 ? 122 VAL   B N   1 
ATOM   1650 C  CA  . VAL   B 1 122 ? -10.221 7.425  29.649  1.00 24.02 ? 122 VAL   B CA  1 
ATOM   1651 C  C   . VAL   B 1 122 ? -11.173 6.698  30.524  1.00 27.45 ? 122 VAL   B C   1 
ATOM   1652 O  O   . VAL   B 1 122 ? -12.051 6.089  30.032  1.00 24.78 ? 122 VAL   B O   1 
ATOM   1653 C  CB  . VAL   B 1 122 ? -10.944 8.440  28.681  1.00 26.35 ? 122 VAL   B CB  1 
ATOM   1654 C  CG1 . VAL   B 1 122 ? -11.557 9.595  29.522  1.00 33.66 ? 122 VAL   B CG1 1 
ATOM   1655 C  CG2 . VAL   B 1 122 ? -9.961  8.943  27.583  1.00 23.08 ? 122 VAL   B CG2 1 
ATOM   1656 N  N   . THR   B 1 123 ? -10.982 6.803  31.848  1.00 27.99 ? 123 THR   B N   1 
ATOM   1657 C  CA  . THR   B 1 123 ? -11.749 6.000  32.818  1.00 26.44 ? 123 THR   B CA  1 
ATOM   1658 C  C   . THR   B 1 123 ? -12.386 6.829  33.907  1.00 39.13 ? 123 THR   B C   1 
ATOM   1659 O  O   . THR   B 1 123 ? -12.090 8.024  33.975  1.00 32.54 ? 123 THR   B O   1 
ATOM   1660 C  CB  . THR   B 1 123 ? -10.848 4.922  33.486  1.00 23.61 ? 123 THR   B CB  1 
ATOM   1661 O  OG1 . THR   B 1 123 ? -9.716  5.515  34.079  1.00 35.43 ? 123 THR   B OG1 1 
ATOM   1662 C  CG2 . THR   B 1 123 ? -10.350 3.828  32.558  1.00 26.91 ? 123 THR   B CG2 1 
HETATM 1663 CA CA  . CA    C 2 .   ? 21.814  18.396 4.193   0.80 19.17 ? 201 CA    A CA  1 
HETATM 1664 C  C5  . A1IS0 D 3 .   ? -0.282  0.478  7.673   0.50 16.45 ? 202 A1IS0 A C5  1 
HETATM 1665 C  C6  . A1IS0 D 3 .   ? -1.113  1.628  7.440   0.50 17.79 ? 202 A1IS0 A C6  1 
HETATM 1666 C  C4  . A1IS0 D 3 .   ? 0.395   1.847  9.241   0.50 18.96 ? 202 A1IS0 A C4  1 
HETATM 1667 C  C3  . A1IS0 D 3 .   ? 0.066   0.484  9.078   0.50 21.26 ? 202 A1IS0 A C3  1 
HETATM 1668 C  C2  . A1IS0 D 3 .   ? -0.106  -0.248 10.312  0.50 15.99 ? 202 A1IS0 A C2  1 
HETATM 1669 C  C1  . A1IS0 D 3 .   ? 0.146   0.392  11.597  0.50 15.85 ? 202 A1IS0 A C1  1 
HETATM 1670 C  C9  . A1IS0 D 3 .   ? -0.009  0.013  5.325   0.50 22.11 ? 202 A1IS0 A C9  1 
HETATM 1671 C  C11 . A1IS0 D 3 .   ? -0.385  -1.592 10.761  0.50 14.22 ? 202 A1IS0 A C11 1 
HETATM 1672 C  C10 . A1IS0 D 3 .   ? 0.231   -0.226 6.646   0.50 15.65 ? 202 A1IS0 A C10 1 
HETATM 1673 N  N3  . A1IS0 D 3 .   ? -0.725  -2.627 9.996   0.50 15.72 ? 202 A1IS0 A N3  1 
HETATM 1674 N  N1  . A1IS0 D 3 .   ? -0.427  -1.702 12.051  0.50 14.39 ? 202 A1IS0 A N1  1 
HETATM 1675 N  N2  . A1IS0 D 3 .   ? -0.059  -0.441 12.579  0.50 16.69 ? 202 A1IS0 A N2  1 
HETATM 1676 N  N   . A1IS0 D 3 .   ? 0.486   1.684  11.667  0.50 14.12 ? 202 A1IS0 A N   1 
HETATM 1677 C  C   . A1IS0 D 3 .   ? 0.578   2.392  10.517  0.50 17.50 ? 202 A1IS0 A C   1 
HETATM 1678 C  C8  . A1IS0 D 3 .   ? -0.864  1.266  5.132   0.50 19.94 ? 202 A1IS0 A C8  1 
HETATM 1679 C  C7  . A1IS0 D 3 .   ? -1.332  2.055  6.159   0.50 17.25 ? 202 A1IS0 A C7  1 
HETATM 1680 CA CA  . CA    E 2 .   ? -18.273 20.026 27.598  0.80 37.59 ? 201 CA    B CA  1 
HETATM 1681 C  C5  . A1IS0 F 3 .   ? -0.540  -0.744 24.864  0.50 20.82 ? 202 A1IS0 B C5  1 
HETATM 1682 C  C6  . A1IS0 F 3 .   ? -1.514  -1.709 25.151  0.50 20.76 ? 202 A1IS0 B C6  1 
HETATM 1683 C  C4  . A1IS0 F 3 .   ? -0.244  -2.235 23.225  0.50 20.50 ? 202 A1IS0 B C4  1 
HETATM 1684 C  C3  . A1IS0 F 3 .   ? -0.240  -0.865 23.483  0.50 21.90 ? 202 A1IS0 B C3  1 
HETATM 1685 C  C2  . A1IS0 F 3 .   ? -0.006  0.007  22.372  0.50 17.24 ? 202 A1IS0 B C2  1 
HETATM 1686 C  C1  . A1IS0 F 3 .   ? 0.040   -0.573 21.080  0.50 17.36 ? 202 A1IS0 B C1  1 
HETATM 1687 C  C9  . A1IS0 F 3 .   ? -0.308  -0.192 27.121  0.50 23.54 ? 202 A1IS0 B C9  1 
HETATM 1688 C  C11 . A1IS0 F 3 .   ? -0.050  1.498  21.964  0.50 15.16 ? 202 A1IS0 B C11 1 
HETATM 1689 C  C10 . A1IS0 F 3 .   ? 0.008   0.003  25.802  0.50 20.80 ? 202 A1IS0 B C10 1 
HETATM 1690 N  N3  . A1IS0 F 3 .   ? -0.086  2.647  22.627  0.50 17.19 ? 202 A1IS0 B N3  1 
HETATM 1691 N  N1  . A1IS0 F 3 .   ? 0.079   1.610  20.676  0.50 19.17 ? 202 A1IS0 B N1  1 
HETATM 1692 N  N2  . A1IS0 F 3 .   ? 0.086   0.320  20.157  0.50 17.37 ? 202 A1IS0 B N2  1 
HETATM 1693 N  N   . A1IS0 F 3 .   ? 0.079   -1.867 20.942  0.50 19.30 ? 202 A1IS0 B N   1 
HETATM 1694 C  C   . A1IS0 F 3 .   ? -0.049  -2.708 21.970  0.50 20.41 ? 202 A1IS0 B C   1 
HETATM 1695 C  C8  . A1IS0 F 3 .   ? -1.261  -1.162 27.434  0.50 25.00 ? 202 A1IS0 B C8  1 
HETATM 1696 C  C7  . A1IS0 F 3 .   ? -1.870  -1.941 26.448  0.50 22.74 ? 202 A1IS0 B C7  1 
HETATM 1697 O  O   . HOH   G 4 .   ? 22.944  17.271 4.745   1.00 21.24 ? 301 HOH   A O   1 
HETATM 1698 O  O   . HOH   G 4 .   ? -10.210 16.403 20.569  1.00 26.99 ? 302 HOH   A O   1 
HETATM 1699 O  O   . HOH   G 4 .   ? 0.873   12.995 16.406  1.00 19.67 ? 303 HOH   A O   1 
HETATM 1700 O  O   . HOH   G 4 .   ? 0.018   20.371 14.239  1.00 29.84 ? 304 HOH   A O   1 
HETATM 1701 O  O   . HOH   G 4 .   ? 21.100  19.619 7.889   1.00 11.98 ? 305 HOH   A O   1 
HETATM 1702 O  O   . HOH   G 4 .   ? 1.117   12.978 -2.148  1.00 15.41 ? 306 HOH   A O   1 
HETATM 1703 O  O   . HOH   G 4 .   ? 15.552  11.058 5.388   1.00 17.92 ? 307 HOH   A O   1 
HETATM 1704 O  O   . HOH   G 4 .   ? -6.620  11.972 -3.640  1.00 23.07 ? 308 HOH   A O   1 
HETATM 1705 O  O   . HOH   G 4 .   ? -2.598  13.931 18.207  1.00 17.67 ? 309 HOH   A O   1 
HETATM 1706 O  O   . HOH   G 4 .   ? -16.645 7.738  20.107  1.00 20.04 ? 310 HOH   A O   1 
HETATM 1707 O  O   . HOH   G 4 .   ? 5.609   8.099  11.073  1.00 23.06 ? 311 HOH   A O   1 
HETATM 1708 O  O   . HOH   G 4 .   ? 4.856   15.593 16.317  1.00 19.06 ? 312 HOH   A O   1 
HETATM 1709 O  O   . HOH   G 4 .   ? 12.436  23.621 7.212   1.00 18.99 ? 313 HOH   A O   1 
HETATM 1710 O  O   . HOH   G 4 .   ? 20.927  22.258 3.943   1.00 15.84 ? 314 HOH   A O   1 
HETATM 1711 O  O   . HOH   G 4 .   ? -9.314  12.077 15.766  1.00 12.75 ? 315 HOH   A O   1 
HETATM 1712 O  O   . HOH   G 4 .   ? 16.586  19.048 11.372  1.00 21.99 ? 316 HOH   A O   1 
HETATM 1713 O  O   . HOH   G 4 .   ? 14.312  16.410 -4.993  1.00 23.70 ? 317 HOH   A O   1 
HETATM 1714 O  O   . HOH   G 4 .   ? 12.770  14.029 -2.479  1.00 21.34 ? 318 HOH   A O   1 
HETATM 1715 O  O   . HOH   G 4 .   ? -4.174  24.210 1.952   1.00 15.27 ? 319 HOH   A O   1 
HETATM 1716 O  O   . HOH   G 4 .   ? -2.601  18.287 -3.638  1.00 16.22 ? 320 HOH   A O   1 
HETATM 1717 O  O   . HOH   G 4 .   ? 7.827   1.582  8.060   1.00 12.44 ? 321 HOH   A O   1 
HETATM 1718 O  O   . HOH   G 4 .   ? -8.570  9.962  17.412  1.00 12.96 ? 322 HOH   A O   1 
HETATM 1719 O  O   . HOH   G 4 .   ? 18.175  12.288 3.051   1.00 20.53 ? 323 HOH   A O   1 
HETATM 1720 O  O   . HOH   G 4 .   ? -13.511 5.688  4.992   1.00 17.97 ? 324 HOH   A O   1 
HETATM 1721 O  O   . HOH   G 4 .   ? 14.693  16.632 -2.266  1.00 16.11 ? 325 HOH   A O   1 
HETATM 1722 O  O   . HOH   G 4 .   ? 13.991  12.209 9.377   1.00 17.40 ? 326 HOH   A O   1 
HETATM 1723 O  O   . HOH   G 4 .   ? -14.740 8.624  4.927   1.00 21.63 ? 327 HOH   A O   1 
HETATM 1724 O  O   . HOH   G 4 .   ? 9.434   24.679 -1.887  1.00 19.64 ? 328 HOH   A O   1 
HETATM 1725 O  O   . HOH   G 4 .   ? 17.278  18.382 5.551   1.00 14.23 ? 329 HOH   A O   1 
HETATM 1726 O  O   . HOH   G 4 .   ? -7.812  8.446  14.798  1.00 11.82 ? 330 HOH   A O   1 
HETATM 1727 O  O   . HOH   G 4 .   ? -10.471 14.536 7.263   1.00 14.69 ? 331 HOH   A O   1 
HETATM 1728 O  O   . HOH   G 4 .   ? 4.194   14.125 -3.720  1.00 15.50 ? 332 HOH   A O   1 
HETATM 1729 O  O   . HOH   G 4 .   ? -11.921 15.861 4.079   1.00 18.23 ? 333 HOH   A O   1 
HETATM 1730 O  O   . HOH   G 4 .   ? -0.499  23.555 3.673   1.00 14.47 ? 334 HOH   A O   1 
HETATM 1731 O  O   . HOH   G 4 .   ? -19.088 8.559  19.214  1.00 25.93 ? 335 HOH   A O   1 
HETATM 1732 O  O   . HOH   G 4 .   ? 8.702   5.631  0.154   1.00 25.93 ? 336 HOH   A O   1 
HETATM 1733 O  O   . HOH   G 4 .   ? 14.644  3.539  5.130   1.00 18.59 ? 337 HOH   A O   1 
HETATM 1734 O  O   . HOH   G 4 .   ? 15.359  26.688 3.121   1.00 14.43 ? 338 HOH   A O   1 
HETATM 1735 O  O   . HOH   G 4 .   ? -3.352  15.771 -4.385  1.00 18.00 ? 339 HOH   A O   1 
HETATM 1736 O  O   . HOH   G 4 .   ? -15.240 10.505 6.868   1.00 24.86 ? 340 HOH   A O   1 
HETATM 1737 O  O   . HOH   G 4 .   ? 16.417  13.680 6.298   1.00 16.28 ? 341 HOH   A O   1 
HETATM 1738 O  O   . HOH   G 4 .   ? 8.173   15.115 -9.166  1.00 28.34 ? 342 HOH   A O   1 
HETATM 1739 O  O   . HOH   G 4 .   ? -4.341  11.033 -4.706  1.00 19.25 ? 343 HOH   A O   1 
HETATM 1740 O  O   . HOH   G 4 .   ? 8.784   26.687 4.623   1.00 17.40 ? 344 HOH   A O   1 
HETATM 1741 O  O   . HOH   G 4 .   ? 23.104  18.559 7.839   1.00 26.77 ? 345 HOH   A O   1 
HETATM 1742 O  O   . HOH   G 4 .   ? 21.258  17.507 1.564   1.00 30.85 ? 346 HOH   A O   1 
HETATM 1743 O  O   . HOH   G 4 .   ? 22.300  20.410 5.745   1.00 28.13 ? 347 HOH   A O   1 
HETATM 1744 O  O   . HOH   G 4 .   ? -0.607  24.482 1.057   1.00 29.96 ? 348 HOH   A O   1 
HETATM 1745 O  O   . HOH   G 4 .   ? 16.672  20.719 6.809   1.00 21.95 ? 349 HOH   A O   1 
HETATM 1746 O  O   . HOH   G 4 .   ? 17.792  9.884  4.473   1.00 21.35 ? 350 HOH   A O   1 
HETATM 1747 O  O   . HOH   G 4 .   ? 16.467  23.023 5.307   1.00 23.28 ? 351 HOH   A O   1 
HETATM 1748 O  O   . HOH   G 4 .   ? -5.933  20.315 14.954  1.00 26.33 ? 352 HOH   A O   1 
HETATM 1749 O  O   . HOH   G 4 .   ? 6.931   25.961 2.327   1.00 25.28 ? 353 HOH   A O   1 
HETATM 1750 O  O   . HOH   G 4 .   ? -2.999  24.048 4.576   1.00 15.73 ? 354 HOH   A O   1 
HETATM 1751 O  O   . HOH   G 4 .   ? 15.069  24.517 6.938   1.00 24.62 ? 355 HOH   A O   1 
HETATM 1752 O  O   . HOH   G 4 .   ? -9.278  11.537 -4.934  1.00 21.51 ? 356 HOH   A O   1 
HETATM 1753 O  O   . HOH   G 4 .   ? 16.813  21.122 9.525   1.00 23.75 ? 357 HOH   A O   1 
HETATM 1754 O  O   . HOH   G 4 .   ? -5.255  22.452 18.256  1.00 26.66 ? 358 HOH   A O   1 
HETATM 1755 O  O   . HOH   G 4 .   ? -3.625  25.779 6.785   1.00 27.15 ? 359 HOH   A O   1 
HETATM 1756 O  O   . HOH   G 4 .   ? 14.166  21.865 -12.553 1.00 25.07 ? 360 HOH   A O   1 
HETATM 1757 O  O   . HOH   H 4 .   ? 11.799  14.701 20.108  1.00 22.01 ? 301 HOH   B O   1 
HETATM 1758 O  O   . HOH   H 4 .   ? 3.635   2.399  15.549  1.00 26.19 ? 302 HOH   B O   1 
HETATM 1759 O  O   . HOH   H 4 .   ? 7.301   23.070 21.660  1.00 27.81 ? 303 HOH   B O   1 
HETATM 1760 O  O   . HOH   H 4 .   ? -11.332 14.345 23.115  1.00 26.01 ? 304 HOH   B O   1 
HETATM 1761 O  O   . HOH   H 4 .   ? -12.133 21.203 21.292  1.00 27.35 ? 305 HOH   B O   1 
HETATM 1762 O  O   . HOH   H 4 .   ? 8.129   19.158 20.733  1.00 23.99 ? 306 HOH   B O   1 
HETATM 1763 O  O   . HOH   H 4 .   ? 13.663  14.317 11.878  1.00 18.31 ? 307 HOH   B O   1 
HETATM 1764 O  O   . HOH   H 4 .   ? 11.995  10.565 17.196  1.00 14.03 ? 308 HOH   B O   1 
HETATM 1765 O  O   . HOH   H 4 .   ? -7.847  25.061 25.566  1.00 28.24 ? 309 HOH   B O   1 
HETATM 1766 O  O   . HOH   H 4 .   ? 8.382   20.196 24.387  1.00 22.60 ? 310 HOH   B O   1 
HETATM 1767 O  O   . HOH   H 4 .   ? 16.019  -5.152 19.631  1.00 20.01 ? 311 HOH   B O   1 
HETATM 1768 O  O   . HOH   H 4 .   ? 22.199  2.833  15.346  1.00 29.62 ? 312 HOH   B O   1 
HETATM 1769 O  O   . HOH   H 4 .   ? -3.254  9.257  22.690  1.00 13.00 ? 313 HOH   B O   1 
HETATM 1770 O  O   . HOH   H 4 .   ? 11.132  8.632  15.565  1.00 16.37 ? 314 HOH   B O   1 
HETATM 1771 O  O   . HOH   H 4 .   ? -1.741  14.253 36.721  1.00 27.07 ? 315 HOH   B O   1 
HETATM 1772 O  O   . HOH   H 4 .   ? 25.059  3.757  17.799  1.00 23.77 ? 316 HOH   B O   1 
HETATM 1773 O  O   . HOH   H 4 .   ? 8.589   10.601 36.560  1.00 26.85 ? 317 HOH   B O   1 
HETATM 1774 O  O   . HOH   H 4 .   ? 9.489   7.021  18.114  1.00 11.38 ? 318 HOH   B O   1 
HETATM 1775 O  O   . HOH   H 4 .   ? 13.456  12.551 25.754  1.00 17.66 ? 319 HOH   B O   1 
HETATM 1776 O  O   . HOH   H 4 .   ? 6.057   1.573  17.687  1.00 19.00 ? 320 HOH   B O   1 
HETATM 1777 O  O   . HOH   H 4 .   ? 5.725   13.367 14.727  1.00 12.96 ? 321 HOH   B O   1 
HETATM 1778 O  O   . HOH   H 4 .   ? 8.408   9.519  17.598  1.00 16.36 ? 322 HOH   B O   1 
HETATM 1779 O  O   . HOH   H 4 .   ? 19.940  12.475 23.158  1.00 25.10 ? 323 HOH   B O   1 
HETATM 1780 O  O   . HOH   H 4 .   ? 13.511  -6.044 27.503  1.00 25.47 ? 324 HOH   B O   1 
HETATM 1781 O  O   . HOH   H 4 .   ? 6.072   9.801  37.463  1.00 29.14 ? 325 HOH   B O   1 
HETATM 1782 O  O   . HOH   H 4 .   ? 14.348  3.130  28.030  1.00 21.27 ? 326 HOH   B O   1 
HETATM 1783 O  O   . HOH   H 4 .   ? 20.499  4.347  13.399  1.00 27.02 ? 327 HOH   B O   1 
HETATM 1784 O  O   . HOH   H 4 .   ? 17.859  4.102  10.189  1.00 27.68 ? 328 HOH   B O   1 
HETATM 1785 O  O   . HOH   H 4 .   ? 16.085  19.571 14.022  1.00 28.04 ? 329 HOH   B O   1 
HETATM 1786 O  O   . HOH   H 4 .   ? 9.121   17.471 24.652  1.00 19.63 ? 330 HOH   B O   1 
HETATM 1787 O  O   . HOH   H 4 .   ? 9.861   14.248 36.099  1.00 26.41 ? 331 HOH   B O   1 
HETATM 1788 O  O   . HOH   H 4 .   ? 17.296  7.300  26.051  1.00 25.86 ? 332 HOH   B O   1 
HETATM 1789 O  O   . HOH   H 4 .   ? 7.240   -2.633 24.493  1.00 15.46 ? 333 HOH   B O   1 
HETATM 1790 O  O   . HOH   H 4 .   ? 12.155  6.315  38.240  1.00 26.73 ? 334 HOH   B O   1 
HETATM 1791 O  O   . HOH   H 4 .   ? 9.200   21.370 15.259  1.00 27.39 ? 335 HOH   B O   1 
HETATM 1792 O  O   . HOH   H 4 .   ? -10.589 17.579 32.147  1.00 32.41 ? 336 HOH   B O   1 
HETATM 1793 O  O   . HOH   H 4 .   ? 9.778   17.350 21.908  1.00 25.36 ? 337 HOH   B O   1 
HETATM 1794 O  O   . HOH   H 4 .   ? 5.241   23.729 17.897  1.00 21.28 ? 338 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    C  C   . CYS   A 10  ? 0.4736 0.1850 0.4413 -0.0257 0.1350  -0.0791 10  CYS   A C   
2    O  O   . CYS   A 10  ? 0.5770 0.1945 0.5327 -0.0692 0.1859  -0.1010 10  CYS   A O   
3    N  N   . PRO   A 11  ? 0.2650 0.2268 0.2164 -0.0119 0.0415  0.0224  11  PRO   A N   
4    C  CA  . PRO   A 11  ? 0.1970 0.1688 0.2291 0.0616  0.0421  0.0786  11  PRO   A CA  
5    C  C   . PRO   A 11  ? 0.1473 0.1504 0.2002 0.0151  0.0234  0.0564  11  PRO   A C   
6    O  O   . PRO   A 11  ? 0.1755 0.1471 0.2092 0.0018  0.0304  0.0563  11  PRO   A O   
7    C  CB  . PRO   A 11  ? 0.2863 0.3118 0.1900 -0.0323 0.0708  0.0585  11  PRO   A CB  
8    C  CG  . PRO   A 11  ? 0.2999 0.1548 0.4279 -0.0277 0.0805  0.0989  11  PRO   A CG  
9    C  CD  . PRO   A 11  ? 0.3002 0.3107 0.1748 0.0263  0.0394  0.0740  11  PRO   A CD  
10   N  N   . LEU   A 12  ? 0.1623 0.1439 0.1833 -0.0006 0.0254  0.0592  12  LEU   A N   
11   C  CA  . LEU   A 12  ? 0.1508 0.1450 0.1798 0.0081  0.0241  0.0590  12  LEU   A CA  
12   C  C   . LEU   A 12  ? 0.1662 0.1596 0.1714 0.0012  -0.0070 0.0596  12  LEU   A C   
13   O  O   . LEU   A 12  ? 0.1922 0.2465 0.2542 -0.0267 -0.0311 0.1298  12  LEU   A O   
14   C  CB  . LEU   A 12  ? 0.2029 0.1442 0.2147 0.0217  0.0173  0.0714  12  LEU   A CB  
15   C  CG  . LEU   A 12  ? 0.1396 0.1648 0.2407 0.0214  0.0025  0.0474  12  LEU   A CG  
16   C  CD1 . LEU   A 12  ? 0.1937 0.1602 0.2109 0.0335  0.0057  0.0175  12  LEU   A CD1 
17   C  CD2 . LEU   A 12  ? 0.2111 0.1710 0.2754 0.0331  0.0182  0.0116  12  LEU   A CD2 
18   N  N   . MET   A 13  ? 0.1398 0.1371 0.1562 0.0035  0.0161  0.0444  13  MET   A N   
19   C  CA  . MET   A 13  ? 0.1483 0.1692 0.1592 -0.0100 0.0185  0.0559  13  MET   A CA  
20   C  C   . MET   A 13  ? 0.1145 0.1095 0.1566 0.0130  0.0053  0.0090  13  MET   A C   
21   O  O   . MET   A 13  ? 0.1327 0.1394 0.1688 0.0091  0.0081  0.0336  13  MET   A O   
22   C  CB  . MET   A 13  ? 0.2160 0.2689 0.1544 -0.0487 0.0526  0.0001  13  MET   A CB  
23   C  CG  . MET   A 13  ? 0.2301 0.1836 0.1951 0.0262  0.0003  0.0297  13  MET   A CG  
24   S  SD  . MET   A 13  ? 0.3132 0.1595 0.1962 -0.0313 0.0106  0.0050  13  MET   A SD  
25   C  CE  . MET   A 13  ? 0.4174 0.1806 0.3153 0.0085  0.0878  -0.0287 13  MET   A CE  
26   N  N   . VAL   A 14  ? 0.1353 0.1167 0.1381 -0.0025 -0.0031 0.0205  14  VAL   A N   
27   C  CA  . VAL   A 14  ? 0.1099 0.1338 0.1381 0.0018  -0.0034 0.0176  14  VAL   A CA  
28   C  C   . VAL   A 14  ? 0.1253 0.1658 0.1455 -0.0270 -0.0269 0.0297  14  VAL   A C   
29   O  O   . VAL   A 14  ? 0.1577 0.1791 0.1717 -0.0539 -0.0237 0.0630  14  VAL   A O   
30   C  CB  . VAL   A 14  ? 0.1312 0.1423 0.1675 0.0238  -0.0121 0.0176  14  VAL   A CB  
31   C  CG1 . VAL   A 14  ? 0.1317 0.1853 0.1997 0.0126  0.0387  0.0270  14  VAL   A CG1 
32   C  CG2 . VAL   A 14  ? 0.1871 0.1234 0.1364 0.0293  -0.0011 -0.0042 14  VAL   A CG2 
33   N  N   . LYS   A 15  ? 0.1303 0.1466 0.1288 -0.0254 0.0038  0.0296  15  LYS   A N   
34   C  CA  . LYS   A 15  ? 0.1325 0.1943 0.1329 -0.0210 -0.0015 0.0349  15  LYS   A CA  
35   C  C   . LYS   A 15  ? 0.1168 0.1724 0.1346 -0.0301 -0.0004 0.0024  15  LYS   A C   
36   O  O   . LYS   A 15  ? 0.1394 0.2251 0.1378 -0.0549 -0.0045 0.0422  15  LYS   A O   
37   C  CB  . LYS   A 15  ? 0.2179 0.1860 0.1535 -0.0637 0.0434  0.0142  15  LYS   A CB  
38   C  CG  . LYS   A 15  ? 0.2895 0.2388 0.3134 -0.0296 0.0836  -0.0069 15  LYS   A CG  
39   C  CD  . LYS   A 15  ? 0.4466 0.2906 0.3532 -0.0015 0.1052  -0.0015 15  LYS   A CD  
40   C  CE  . LYS   A 15  ? 0.3914 0.2192 0.3046 -0.0622 0.0660  -0.0152 15  LYS   A CE  
41   N  N   . VAL   A 16  ? 0.1399 0.1454 0.1206 -0.0326 -0.0047 0.0238  16  VAL   A N   
42   C  CA  . VAL   A 16  ? 0.1299 0.1420 0.1270 -0.0392 -0.0074 0.0185  16  VAL   A CA  
43   C  C   . VAL   A 16  ? 0.1214 0.1376 0.1185 -0.0078 -0.0169 0.0193  16  VAL   A C   
44   O  O   . VAL   A 16  ? 0.1281 0.1561 0.1242 -0.0309 -0.0179 0.0249  16  VAL   A O   
45   C  CB  . VAL   A 16  ? 0.1420 0.1490 0.1363 -0.0376 -0.0009 0.0197  16  VAL   A CB  
46   C  CG1 . VAL   A 16  ? 0.1406 0.1364 0.1331 -0.0264 0.0007  0.0085  16  VAL   A CG1 
47   C  CG2 . VAL   A 16  ? 0.1476 0.1399 0.1445 -0.0367 -0.0056 0.0211  16  VAL   A CG2 
48   N  N   . LEU   A 17  ? 0.1313 0.1229 0.1171 -0.0331 -0.0134 0.0085  17  LEU   A N   
49   C  CA  . LEU   A 17  ? 0.1171 0.1177 0.1351 -0.0281 -0.0031 0.0060  17  LEU   A CA  
50   C  C   . LEU   A 17  ? 0.1072 0.1106 0.1202 -0.0166 -0.0193 -0.0018 17  LEU   A C   
51   O  O   . LEU   A 17  ? 0.1213 0.1211 0.1322 -0.0357 -0.0217 0.0058  17  LEU   A O   
52   C  CB  . LEU   A 17  ? 0.1106 0.1286 0.1309 -0.0310 -0.0075 0.0099  17  LEU   A CB  
53   C  CG  . LEU   A 17  ? 0.1210 0.1578 0.1555 -0.0168 -0.0083 0.0254  17  LEU   A CG  
54   C  CD1 . LEU   A 17  ? 0.1452 0.1495 0.1756 0.0217  0.0138  0.0076  17  LEU   A CD1 
55   C  CD2 . LEU   A 17  ? 0.2012 0.1990 0.1537 0.0274  0.0106  -0.0178 17  LEU   A CD2 
56   N  N   . ASP   A 18  ? 0.1179 0.1146 0.1207 -0.0304 -0.0044 0.0016  18  ASP   A N   
57   C  CA  . ASP   A 18  ? 0.1090 0.1012 0.1254 -0.0130 0.0047  -0.0029 18  ASP   A CA  
58   C  C   . ASP   A 18  ? 0.0970 0.0990 0.1247 -0.0233 0.0028  -0.0026 18  ASP   A C   
59   O  O   . ASP   A 18  ? 0.1141 0.0990 0.1386 -0.0059 0.0058  0.0000  18  ASP   A O   
60   C  CB  . ASP   A 18  ? 0.1308 0.1061 0.1245 -0.0064 -0.0009 -0.0007 18  ASP   A CB  
61   C  CG  . ASP   A 18  ? 0.1409 0.1160 0.1517 0.0129  0.0056  -0.0116 18  ASP   A CG  
62   O  OD1 . ASP   A 18  ? 0.1521 0.1257 0.1521 0.0166  0.0238  0.0127  18  ASP   A OD1 
63   O  OD2 . ASP   A 18  ? 0.1717 0.1810 0.1858 0.0512  0.0438  0.0275  18  ASP   A OD2 
64   N  N   . ALA   A 19  ? 0.1209 0.1079 0.1222 -0.0118 -0.0010 -0.0048 19  ALA   A N   
65   C  CA  . ALA   A 19  ? 0.1367 0.1120 0.1328 0.0042  0.0124  -0.0167 19  ALA   A CA  
66   C  C   . ALA   A 19  ? 0.1488 0.1040 0.1410 -0.0214 0.0099  -0.0120 19  ALA   A C   
67   O  O   . ALA   A 19  ? 0.1961 0.1153 0.1404 -0.0158 0.0051  -0.0040 19  ALA   A O   
68   C  CB  . ALA   A 19  ? 0.1509 0.1251 0.1317 0.0091  0.0074  -0.0060 19  ALA   A CB  
69   N  N   . VAL   A 20  ? 0.1372 0.0987 0.1629 -0.0230 0.0169  0.0013  20  VAL   A N   
70   C  CA  . VAL   A 20  ? 0.1714 0.1230 0.1580 -0.0421 0.0382  -0.0120 20  VAL   A CA  
71   C  C   . VAL   A 20  ? 0.1516 0.1399 0.1982 -0.0379 0.0505  -0.0185 20  VAL   A C   
72   O  O   . VAL   A 20  ? 0.1967 0.1929 0.2325 -0.0942 0.0613  -0.0423 20  VAL   A O   
73   C  CB  . VAL   A 20  ? 0.1766 0.1825 0.1849 -0.0239 0.0717  -0.0150 20  VAL   A CB  
74   C  CG1 . VAL   A 20  ? 0.2470 0.2165 0.2937 -0.0097 0.0996  -0.0472 20  VAL   A CG1 
75   C  CG2 . VAL   A 20  ? 0.2830 0.1878 0.1885 -0.0624 0.0788  -0.0230 20  VAL   A CG2 
76   N  N   . ARG   A 21  ? 0.1332 0.1721 0.1826 -0.0009 -0.0025 -0.0217 21  ARG   A N   
77   C  CA  . ARG   A 21  ? 0.1132 0.2734 0.2259 -0.0004 0.0096  -0.0600 21  ARG   A CA  
78   C  C   . ARG   A 21  ? 0.1345 0.1990 0.1690 -0.0479 -0.0101 -0.0291 21  ARG   A C   
79   O  O   . ARG   A 21  ? 0.1414 0.2710 0.2085 -0.0525 -0.0170 -0.0746 21  ARG   A O   
80   C  CB  . ARG   A 21  ? 0.1796 0.2860 0.2557 0.0632  -0.0093 -0.0430 21  ARG   A CB  
81   C  CG  . ARG   A 21  ? 0.2494 0.2860 0.3801 0.0856  0.0099  -0.0725 21  ARG   A CG  
82   C  CD  . ARG   A 21  ? 0.2189 0.2868 0.3471 0.0837  0.0405  0.0034  21  ARG   A CD  
83   N  NE  . ARG   A 21  ? 0.3572 0.5386 0.4821 0.1618  -0.0017 -0.0416 21  ARG   A NE  
84   N  N   . GLY   A 22  ? 0.1294 0.1159 0.1422 -0.0301 -0.0067 0.0052  22  GLY   A N   
85   C  CA  . GLY   A 22  ? 0.1412 0.0916 0.1446 0.0118  0.0002  -0.0055 22  GLY   A CA  
86   C  C   . GLY   A 22  ? 0.1294 0.0886 0.1385 0.0007  0.0142  -0.0055 22  GLY   A C   
87   O  O   . GLY   A 22  ? 0.1405 0.0982 0.1524 0.0052  -0.0057 -0.0028 22  GLY   A O   
88   N  N   . SER   A 23  ? 0.1339 0.0999 0.1341 -0.0161 -0.0139 0.0054  23  SER   A N   
89   C  CA  . SER   A 23  ? 0.1219 0.1329 0.1525 -0.0206 -0.0138 0.0119  23  SER   A CA  
90   C  C   . SER   A 23  ? 0.1244 0.1102 0.1399 -0.0008 0.0070  0.0179  23  SER   A C   
91   O  O   . SER   A 23  ? 0.1432 0.1211 0.1334 -0.0194 -0.0211 -0.0084 23  SER   A O   
92   C  CB  . SER   A 23  ? 0.1612 0.1419 0.1801 -0.0379 -0.0103 0.0095  23  SER   A CB  
93   O  OG  . SER   A 23  ? 0.1501 0.1606 0.2323 0.0119  -0.0184 0.0029  23  SER   A OG  
94   N  N   . PRO   A 24  ? 0.1371 0.1016 0.1361 -0.0146 -0.0176 -0.0071 24  PRO   A N   
95   C  CA  . PRO   A 24  ? 0.1420 0.0983 0.1659 -0.0124 -0.0110 0.0028  24  PRO   A CA  
96   C  C   . PRO   A 24  ? 0.0990 0.1238 0.1598 -0.0247 0.0046  0.0172  24  PRO   A C   
97   O  O   . PRO   A 24  ? 0.1313 0.0946 0.1889 -0.0216 0.0047  0.0085  24  PRO   A O   
98   C  CB  . PRO   A 24  ? 0.2033 0.1294 0.1777 -0.0110 0.0065  0.0213  24  PRO   A CB  
99   C  CG  . PRO   A 24  ? 0.4983 0.2500 0.1366 -0.1443 -0.0163 0.0180  24  PRO   A CG  
100  C  CD  . PRO   A 24  ? 0.1924 0.0895 0.1713 0.0127  -0.0281 0.0011  24  PRO   A CD  
101  N  N   . ALA   A 25  ? 0.1214 0.1119 0.1516 -0.0358 0.0054  0.0029  25  ALA   A N   
102  C  CA  . ALA   A 25  ? 0.1402 0.1062 0.1367 -0.0185 0.0070  0.0024  25  ALA   A CA  
103  C  C   . ALA   A 25  ? 0.1303 0.0948 0.1347 -0.0147 0.0052  -0.0155 25  ALA   A C   
104  O  O   . ALA   A 25  ? 0.1354 0.1077 0.1625 -0.0056 -0.0027 0.0240  25  ALA   A O   
105  C  CB  . ALA   A 25  ? 0.1790 0.1054 0.1540 -0.0268 0.0133  0.0028  25  ALA   A CB  
106  N  N   . ILE   A 26  ? 0.1185 0.1029 0.1578 -0.0152 -0.0002 0.0091  26  ILE   A N   
107  C  CA  . ILE   A 26  ? 0.1483 0.1454 0.1351 0.0180  -0.0241 0.0061  26  ILE   A CA  
108  C  C   . ILE   A 26  ? 0.1244 0.1445 0.1541 -0.0053 0.0107  0.0021  26  ILE   A C   
109  O  O   . ILE   A 26  ? 0.1406 0.1224 0.1686 -0.0029 0.0041  0.0251  26  ILE   A O   
110  C  CB  . ILE   A 26  ? 0.2187 0.1507 0.1851 -0.0204 -0.0440 -0.0222 26  ILE   A CB  
111  C  CG1 . ILE   A 26  ? 0.2175 0.1530 0.1833 0.0096  -0.0371 -0.0201 26  ILE   A CG1 
112  C  CG2 . ILE   A 26  ? 0.2603 0.2139 0.2817 -0.0266 -0.0568 -0.0165 26  ILE   A CG2 
113  C  CD1 . ILE   A 26  ? 0.4033 0.3041 0.3141 -0.1190 -0.0511 -0.0383 26  ILE   A CD1 
114  N  N   . ASN   A 27  ? 0.1554 0.1371 0.1587 -0.0227 0.0081  0.0064  27  ASN   A N   
115  C  CA  . ASN   A 27  ? 0.1873 0.1218 0.2086 0.0010  -0.0202 0.0154  27  ASN   A CA  
116  C  C   . ASN   A 27  ? 0.1626 0.1174 0.1918 -0.0223 0.0122  -0.0004 27  ASN   A C   
117  O  O   . ASN   A 27  ? 0.1800 0.1448 0.2098 -0.0147 0.0128  -0.0169 27  ASN   A O   
118  C  CB  . ASN   A 27  ? 0.2194 0.1217 0.2669 0.0169  -0.0486 0.0272  27  ASN   A CB  
119  C  CG  . ASN   A 27  ? 0.1633 0.1319 0.2586 0.0294  -0.0006 0.0294  27  ASN   A CG  
120  O  OD1 . ASN   A 27  ? 0.1877 0.3265 0.1901 -0.0158 -0.0217 0.0014  27  ASN   A OD1 
121  N  ND2 . ASN   A 27  ? 0.1601 0.2364 0.1915 0.0031  -0.0342 0.0097  27  ASN   A ND2 
122  N  N   . VAL   A 28  ? 0.1776 0.0978 0.1671 -0.0315 0.0146  0.0103  28  VAL   A N   
123  C  CA  . VAL   A 28  ? 0.1826 0.1144 0.1542 -0.0429 0.0220  0.0009  28  VAL   A CA  
124  C  C   . VAL   A 28  ? 0.1657 0.1275 0.1289 -0.0258 0.0151  0.0017  28  VAL   A C   
125  O  O   . VAL   A 28  ? 0.1750 0.1093 0.1422 -0.0205 0.0136  0.0022  28  VAL   A O   
126  C  CB  . VAL   A 28  ? 0.2211 0.0977 0.1551 -0.0315 0.0125  0.0092  28  VAL   A CB  
127  C  CG1 . VAL   A 28  ? 0.2220 0.1286 0.1583 -0.0308 -0.0048 0.0198  28  VAL   A CG1 
128  C  CG2 . VAL   A 28  ? 0.2556 0.1278 0.1920 -0.0544 0.0280  0.0063  28  VAL   A CG2 
129  N  N   . ALA   A 29  ? 0.1336 0.1315 0.1383 -0.0229 0.0257  0.0150  29  ALA   A N   
130  C  CA  . ALA   A 29  ? 0.1434 0.1003 0.1274 -0.0135 0.0232  0.0200  29  ALA   A CA  
131  C  C   . ALA   A 29  ? 0.1497 0.1040 0.1261 -0.0197 0.0248  -0.0025 29  ALA   A C   
132  O  O   . ALA   A 29  ? 0.1633 0.1203 0.1305 -0.0164 0.0082  0.0131  29  ALA   A O   
133  C  CB  . ALA   A 29  ? 0.1443 0.1065 0.1715 -0.0108 0.0065  0.0128  29  ALA   A CB  
134  N  N   . VAL   A 30  ? 0.1282 0.0926 0.1455 -0.0106 -0.0084 0.0159  30  VAL   A N   
135  C  CA  . VAL   A 30  ? 0.1342 0.1071 0.1254 0.0058  0.0089  0.0232  30  VAL   A CA  
136  C  C   . VAL   A 30  ? 0.1133 0.1171 0.1346 -0.0199 0.0004  0.0230  30  VAL   A C   
137  O  O   . VAL   A 30  ? 0.1456 0.1076 0.1362 -0.0142 0.0001  0.0189  30  VAL   A O   
138  C  CB  . VAL   A 30  ? 0.1324 0.1155 0.1478 0.0131  0.0046  0.0311  30  VAL   A CB  
139  C  CG1 . VAL   A 30  ? 0.1489 0.1275 0.1881 0.0333  0.0209  0.0190  30  VAL   A CG1 
140  C  CG2 . VAL   A 30  ? 0.1751 0.1057 0.1576 -0.0026 0.0025  0.0144  30  VAL   A CG2 
141  N  N   . HIS   A 31  ? 0.1186 0.1073 0.1490 -0.0080 0.0037  0.0248  31  HIS   A N   
142  C  CA  . HIS   A 31  ? 0.1355 0.0971 0.1538 0.0043  0.0038  0.0141  31  HIS   A CA  
143  C  C   . HIS   A 31  ? 0.1305 0.0988 0.1275 -0.0111 0.0002  0.0276  31  HIS   A C   
144  O  O   . HIS   A 31  ? 0.1345 0.1416 0.1558 -0.0133 0.0030  0.0350  31  HIS   A O   
145  C  CB  . HIS   A 31  ? 0.1221 0.1420 0.1730 -0.0198 -0.0046 -0.0059 31  HIS   A CB  
146  C  CG  . HIS   A 31  ? 0.1283 0.1180 0.1899 0.0015  0.0104  -0.0074 31  HIS   A CG  
147  N  ND1 . HIS   A 31  ? 0.1841 0.1696 0.2322 0.0213  0.0066  0.0157  31  HIS   A ND1 
148  C  CD2 . HIS   A 31  ? 0.1409 0.1037 0.1988 0.0167  0.0037  0.0250  31  HIS   A CD2 
149  C  CE1 . HIS   A 31  ? 0.1207 0.1293 0.2388 -0.0165 0.0088  0.0087  31  HIS   A CE1 
150  N  NE2 . HIS   A 31  ? 0.1716 0.2410 0.2663 0.0724  -0.0133 0.0145  31  HIS   A NE2 
151  N  N   . VAL   A 32  ? 0.1216 0.0986 0.1491 -0.0067 -0.0027 0.0186  32  VAL   A N   
152  C  CA  . VAL   A 32  ? 0.1201 0.0920 0.1704 0.0074  0.0051  0.0004  32  VAL   A CA  
153  C  C   . VAL   A 32  ? 0.1084 0.1051 0.1708 -0.0010 0.0030  0.0130  32  VAL   A C   
154  O  O   . VAL   A 32  ? 0.1230 0.1234 0.1572 -0.0063 -0.0028 0.0111  32  VAL   A O   
155  C  CB  . VAL   A 32  ? 0.1355 0.1031 0.1420 -0.0031 -0.0141 0.0149  32  VAL   A CB  
156  C  CG1 . VAL   A 32  ? 0.1314 0.1290 0.1650 -0.0053 0.0089  0.0172  32  VAL   A CG1 
157  C  CG2 . VAL   A 32  ? 0.1503 0.1139 0.1698 0.0018  -0.0075 0.0076  32  VAL   A CG2 
158  N  N   . PHE   A 33  ? 0.1415 0.0931 0.1700 -0.0168 -0.0199 0.0162  33  PHE   A N   
159  C  CA  . PHE   A 33  ? 0.1242 0.1132 0.1883 0.0019  -0.0128 -0.0114 33  PHE   A CA  
160  C  C   . PHE   A 33  ? 0.1366 0.1220 0.1720 -0.0148 -0.0292 0.0158  33  PHE   A C   
161  O  O   . PHE   A 33  ? 0.1363 0.0987 0.1864 -0.0026 -0.0114 0.0208  33  PHE   A O   
162  C  CB  . PHE   A 33  ? 0.1431 0.1327 0.1808 -0.0184 -0.0133 -0.0155 33  PHE   A CB  
163  C  CG  . PHE   A 33  ? 0.1588 0.1456 0.2143 0.0125  -0.0034 -0.0166 33  PHE   A CG  
164  C  CD1 . PHE   A 33  ? 0.1422 0.1557 0.2463 -0.0298 0.0266  -0.0341 33  PHE   A CD1 
165  C  CD2 . PHE   A 33  ? 0.1407 0.1725 0.2288 0.0228  0.0068  0.0044  33  PHE   A CD2 
166  C  CE1 . PHE   A 33  ? 0.1710 0.1652 0.2156 -0.0233 0.0192  -0.0097 33  PHE   A CE1 
167  C  CE2 . PHE   A 33  ? 0.1379 0.1833 0.2660 0.0458  -0.0030 -0.0156 33  PHE   A CE2 
168  C  CZ  . PHE   A 33  ? 0.1124 0.2347 0.2593 0.0135  0.0140  -0.0292 33  PHE   A CZ  
169  N  N   . ARG   A 34  ? 0.1360 0.0863 0.2158 -0.0065 -0.0250 -0.0018 34  ARG   A N   
170  C  CA  . ARG   A 34  ? 0.1230 0.1010 0.1928 -0.0087 -0.0376 0.0062  34  ARG   A CA  
171  C  C   . ARG   A 34  ? 0.1258 0.0944 0.2156 -0.0071 -0.0218 0.0008  34  ARG   A C   
172  O  O   . ARG   A 34  ? 0.1677 0.1052 0.2596 0.0061  -0.0481 0.0041  34  ARG   A O   
173  C  CB  . ARG   A 34  ? 0.1658 0.1150 0.2024 -0.0005 -0.0250 0.0033  34  ARG   A CB  
174  C  CG  . ARG   A 34  ? 0.1364 0.1150 0.2254 -0.0095 -0.0200 -0.0061 34  ARG   A CG  
175  C  CD  . ARG   A 34  ? 0.1679 0.1494 0.2060 -0.0137 -0.0138 -0.0123 34  ARG   A CD  
176  N  NE  . ARG   A 34  ? 0.1939 0.1213 0.2079 -0.0094 0.0048  0.0054  34  ARG   A NE  
177  C  CZ  . ARG   A 34  ? 0.1521 0.1246 0.2085 0.0075  0.0028  0.0207  34  ARG   A CZ  
178  N  NH1 . ARG   A 34  ? 0.1821 0.1345 0.2172 -0.0037 0.0040  0.0036  34  ARG   A NH1 
179  N  NH2 . ARG   A 34  ? 0.1918 0.1322 0.2221 0.0034  -0.0145 0.0212  34  ARG   A NH2 
180  N  N   . LYS   A 35  ? 0.1444 0.1026 0.1881 0.0017  -0.0103 0.0045  35  LYS   A N   
181  C  CA  . LYS   A 35  ? 0.1491 0.1508 0.1883 -0.0062 -0.0122 -0.0369 35  LYS   A CA  
182  C  C   . LYS   A 35  ? 0.1608 0.1167 0.2146 -0.0181 0.0019  -0.0361 35  LYS   A C   
183  O  O   . LYS   A 35  ? 0.2100 0.1264 0.2433 -0.0303 0.0099  -0.0049 35  LYS   A O   
184  C  CB  . LYS   A 35  ? 0.1982 0.1811 0.2141 0.0251  -0.0234 0.0234  35  LYS   A CB  
185  C  CG  . LYS   A 35  ? 0.3199 0.3799 0.3049 0.0723  -0.1114 -0.0455 35  LYS   A CG  
186  C  CD  . LYS   A 35  ? 0.3891 0.3537 0.3125 0.0011  -0.0481 -0.0073 35  LYS   A CD  
187  N  N   . ALA   A 36  ? 0.1984 0.1344 0.2075 -0.0128 0.0207  -0.0126 36  ALA   A N   
188  C  CA  . ALA   A 36  ? 0.2123 0.1531 0.2026 -0.0385 0.0042  -0.0104 36  ALA   A CA  
189  C  C   . ALA   A 36  ? 0.2523 0.1491 0.2238 -0.0584 -0.0081 -0.0230 36  ALA   A C   
190  O  O   . ALA   A 36  ? 0.2465 0.1843 0.2238 -0.0573 -0.0299 -0.0292 36  ALA   A O   
191  C  CB  . ALA   A 36  ? 0.3287 0.1549 0.2604 -0.0236 -0.0127 0.0044  36  ALA   A CB  
192  N  N   . ALA   A 37  ? 0.2998 0.2101 0.2436 -0.1026 0.0301  -0.0493 37  ALA   A N   
193  C  CA  . ALA   A 37  ? 0.3183 0.3609 0.3524 -0.1883 0.0902  -0.1100 37  ALA   A CA  
194  C  C   . ALA   A 37  ? 0.2932 0.3482 0.2955 -0.1272 0.0174  -0.1063 37  ALA   A C   
195  O  O   . ALA   A 37  ? 0.3257 0.4120 0.3766 -0.1715 -0.0285 -0.0816 37  ALA   A O   
196  C  CB  . ALA   A 37  ? 0.3840 0.3607 0.3095 -0.2236 0.1072  -0.0993 37  ALA   A CB  
197  N  N   . ASP   A 38  ? 0.3701 0.1927 0.2583 -0.0925 -0.0177 -0.0493 38  ASP   A N   
198  C  CA  . ASP   A 38  ? 0.2724 0.2492 0.2844 -0.0651 0.0160  -0.0897 38  ASP   A CA  
199  C  C   . ASP   A 38  ? 0.4021 0.2940 0.2787 -0.1496 0.0575  -0.1175 38  ASP   A C   
200  O  O   . ASP   A 38  ? 0.4772 0.3624 0.3690 -0.1302 0.0926  -0.1968 38  ASP   A O   
201  C  CB  . ASP   A 38  ? 0.4574 0.2077 0.4865 -0.0448 0.0130  -0.0759 38  ASP   A CB  
202  C  CG  . ASP   A 38  ? 0.4737 0.3112 0.5601 -0.0160 -0.0523 0.0656  38  ASP   A CG  
203  O  OD1 . ASP   A 38  ? 0.4143 0.2104 0.3983 0.0275  0.0510  -0.0360 38  ASP   A OD1 
204  O  OD2 . ASP   A 38  ? 0.8749 0.3038 0.7510 0.0989  -0.1597 0.0158  38  ASP   A OD2 
205  N  N   . ASP   A 39  ? 0.3343 0.2859 0.2400 -0.0747 0.0221  -0.0880 39  ASP   A N   
206  C  CA  . ASP   A 39  ? 0.4061 0.3319 0.2385 -0.0466 0.0086  -0.0572 39  ASP   A CA  
207  C  C   . ASP   A 39  ? 0.4464 0.2418 0.3266 -0.0655 0.1269  -0.0897 39  ASP   A C   
208  O  O   . ASP   A 39  ? 0.6688 0.3438 0.4654 -0.0541 0.2439  0.0247  39  ASP   A O   
209  C  CB  . ASP   A 39  ? 0.5210 0.5134 0.2371 -0.0972 -0.0494 -0.0697 39  ASP   A CB  
210  N  N   . THR   A 40  ? 0.3064 0.2835 0.3596 -0.0713 0.0871  -0.1163 40  THR   A N   
211  C  CA  . THR   A 40  ? 0.3328 0.2489 0.3917 -0.0161 0.0856  -0.1217 40  THR   A CA  
212  C  C   . THR   A 40  ? 0.2641 0.2530 0.3642 0.0132  0.0712  -0.1134 40  THR   A C   
213  O  O   . THR   A 40  ? 0.2279 0.1832 0.2768 0.0362  0.0083  -0.0368 40  THR   A O   
214  C  CB  . THR   A 40  ? 0.4144 0.2129 0.5091 0.0539  0.0173  -0.2230 40  THR   A CB  
215  O  OG1 . THR   A 40  ? 0.4315 0.2061 0.5020 0.0416  -0.0159 -0.0655 40  THR   A OG1 
216  N  N   . TRP   A 41  ? 0.3350 0.1959 0.3761 -0.0031 0.1295  -0.0979 41  TRP   A N   
217  C  CA  . TRP   A 41  ? 0.1609 0.2202 0.3036 0.0746  0.0180  -0.0447 41  TRP   A CA  
218  C  C   . TRP   A 41  ? 0.1936 0.2020 0.4112 0.0669  0.0278  -0.0140 41  TRP   A C   
219  O  O   . TRP   A 41  ? 0.3218 0.6296 1.1244 0.3766  0.1493  0.0190  41  TRP   A O   
220  C  CB  . TRP   A 41  ? 0.1539 0.2440 0.3343 0.0659  0.0352  -0.0820 41  TRP   A CB  
221  C  CG  . TRP   A 41  ? 0.1981 0.2319 0.2451 0.0185  -0.0014 -0.0666 41  TRP   A CG  
222  C  CD1 . TRP   A 41  ? 0.3741 0.3037 0.2546 0.0898  0.0087  -0.0724 41  TRP   A CD1 
223  C  CD2 . TRP   A 41  ? 0.1949 0.1768 0.2380 0.0175  -0.0219 -0.0313 41  TRP   A CD2 
224  N  NE1 . TRP   A 41  ? 0.3972 0.3841 0.2207 0.0941  0.0146  0.0233  41  TRP   A NE1 
225  C  CE2 . TRP   A 41  ? 0.3119 0.2925 0.1911 0.0023  0.0146  -0.0403 41  TRP   A CE2 
226  C  CE3 . TRP   A 41  ? 0.1576 0.1583 0.2522 -0.0091 0.0104  -0.0395 41  TRP   A CE3 
227  C  CZ2 . TRP   A 41  ? 0.2922 0.3028 0.2555 -0.0196 0.0142  0.0322  41  TRP   A CZ2 
228  C  CZ3 . TRP   A 41  ? 0.1750 0.1461 0.2468 -0.0019 -0.0022 -0.0072 41  TRP   A CZ3 
229  C  CH2 . TRP   A 41  ? 0.1632 0.2320 0.3083 0.0438  -0.0065 0.0218  41  TRP   A CH2 
230  N  N   . GLU   A 42  ? 0.1522 0.1229 0.3076 0.0078  -0.0303 -0.0227 42  GLU   A N   
231  C  CA  . GLU   A 42  ? 0.1602 0.1284 0.3679 0.0103  -0.0532 -0.0093 42  GLU   A CA  
232  C  C   . GLU   A 42  ? 0.1297 0.1335 0.2944 -0.0057 -0.0454 0.0154  42  GLU   A C   
233  O  O   . GLU   A 42  ? 0.1608 0.0892 0.3107 0.0076  -0.0193 0.0177  42  GLU   A O   
234  C  CB  . GLU   A 42  ? 0.2679 0.1759 0.3700 -0.0901 -0.0844 -0.0003 42  GLU   A CB  
235  N  N   . PRO   A 43  ? 0.1802 0.1017 0.2758 0.0056  -0.0418 -0.0044 43  PRO   A N   
236  C  CA  . PRO   A 43  ? 0.1735 0.1289 0.2893 0.0128  -0.0422 -0.0050 43  PRO   A CA  
237  C  C   . PRO   A 43  ? 0.2287 0.1314 0.2938 -0.0444 0.0189  0.0118  43  PRO   A C   
238  O  O   . PRO   A 43  ? 0.4442 0.1560 0.3374 -0.1070 0.1147  -0.0074 43  PRO   A O   
239  C  CB  . PRO   A 43  ? 0.2391 0.1304 0.3465 0.0264  -0.1208 -0.0279 43  PRO   A CB  
240  C  CG  . PRO   A 43  ? 0.2589 0.2316 0.4330 0.1019  -0.1740 -0.0603 43  PRO   A CG  
241  C  CD  . PRO   A 43  ? 0.1783 0.1552 0.3757 0.0414  -0.0883 -0.0221 43  PRO   A CD  
242  N  N   . PHE   A 44  ? 0.1476 0.1130 0.2118 -0.0257 0.0081  0.0210  44  PHE   A N   
243  C  CA  . PHE   A 44  ? 0.1382 0.1347 0.1843 -0.0347 -0.0003 0.0274  44  PHE   A CA  
244  C  C   . PHE   A 44  ? 0.1341 0.1392 0.1798 -0.0363 0.0019  0.0425  44  PHE   A C   
245  O  O   . PHE   A 44  ? 0.1595 0.1838 0.1895 -0.0525 0.0068  0.0602  44  PHE   A O   
246  C  CB  . PHE   A 44  ? 0.1318 0.1307 0.1647 -0.0374 0.0066  0.0266  44  PHE   A CB  
247  C  CG  . PHE   A 44  ? 0.1403 0.1807 0.1585 -0.0211 0.0091  0.0434  44  PHE   A CG  
248  C  CD1 . PHE   A 44  ? 0.1512 0.1863 0.1835 -0.0307 0.0157  0.0120  44  PHE   A CD1 
249  C  CD2 . PHE   A 44  ? 0.1348 0.1811 0.1612 -0.0077 0.0104  0.0022  44  PHE   A CD2 
250  C  CE1 . PHE   A 44  ? 0.1799 0.1544 0.1727 -0.0086 0.0249  0.0438  44  PHE   A CE1 
251  C  CE2 . PHE   A 44  ? 0.2082 0.1181 0.1638 -0.0043 0.0130  0.0296  44  PHE   A CE2 
252  C  CZ  . PHE   A 44  ? 0.1929 0.2665 0.1076 0.0356  0.0179  -0.0774 44  PHE   A CZ  
253  N  N   . ALA   A 45  ? 0.1215 0.1299 0.1713 -0.0165 0.0061  0.0317  45  ALA   A N   
254  C  CA  . ALA   A 45  ? 0.1332 0.1546 0.1574 -0.0235 0.0057  -0.0324 45  ALA   A CA  
255  C  C   . ALA   A 45  ? 0.1369 0.1234 0.1502 -0.0290 -0.0116 0.0272  45  ALA   A C   
256  O  O   . ALA   A 45  ? 0.1562 0.1671 0.1504 -0.0463 -0.0109 0.0293  45  ALA   A O   
257  C  CB  . ALA   A 45  ? 0.1742 0.1056 0.1751 -0.0194 0.0162  -0.0058 45  ALA   A CB  
258  N  N   . SER   A 46  ? 0.1442 0.0918 0.1401 -0.0140 0.0027  0.0655  46  SER   A N   
259  C  CA  . SER   A 46  ? 0.1192 0.0940 0.1540 0.0011  -0.0064 0.0352  46  SER   A CA  
260  C  C   . SER   A 46  ? 0.1193 0.0869 0.1513 0.0051  -0.0028 0.0338  46  SER   A C   
261  O  O   . SER   A 46  ? 0.1669 0.1139 0.1292 -0.0088 -0.0035 0.0270  46  SER   A O   
262  C  CB  . SER   A 46  ? 0.1281 0.0993 0.1591 0.0007  -0.0057 0.0257  46  SER   A CB  
263  O  OG  . SER   A 46  ? 0.1408 0.1153 0.1532 0.0069  -0.0104 0.0213  46  SER   A OG  
264  N  N   . GLY   A 47  ? 0.1263 0.0941 0.1498 -0.0031 0.0065  0.0338  47  GLY   A N   
265  C  CA  . GLY   A 47  ? 0.1468 0.0922 0.1413 -0.0070 0.0098  0.0237  47  GLY   A CA  
266  C  C   . GLY   A 47  ? 0.1403 0.0892 0.1301 0.0117  -0.0015 0.0202  47  GLY   A C   
267  O  O   . GLY   A 47  ? 0.1369 0.1102 0.1518 -0.0095 0.0034  0.0244  47  GLY   A O   
268  N  N   . LYS   A 48  ? 0.1471 0.0971 0.1375 -0.0186 0.0143  0.0114  48  LYS   A N   
269  C  CA  . LYS   A 48  ? 0.1680 0.0913 0.1658 -0.0232 0.0166  -0.0070 48  LYS   A CA  
270  C  C   . LYS   A 48  ? 0.1503 0.1143 0.1273 -0.0121 0.0095  0.0036  48  LYS   A C   
271  O  O   . LYS   A 48  ? 0.1947 0.1175 0.1447 -0.0138 0.0296  0.0143  48  LYS   A O   
272  C  CB  . LYS   A 48  ? 0.1972 0.1353 0.2528 -0.0063 0.0407  0.0133  48  LYS   A CB  
273  C  CG  . LYS   A 48  ? 0.1911 0.2383 0.2350 -0.0167 -0.0075 0.0472  48  LYS   A CG  
274  C  CD  . LYS   A 48  ? 0.3467 0.3785 0.3298 0.0156  -0.0065 0.0686  48  LYS   A CD  
275  C  CE  . LYS   A 48  ? 0.3375 0.3022 0.4303 -0.0450 -0.0549 0.0614  48  LYS   A CE  
276  N  N   . THR   A 49  ? 0.1713 0.1061 0.1364 -0.0096 0.0025  0.0140  49  THR   A N   
277  C  CA  . THR   A 49  ? 0.1289 0.1087 0.1403 -0.0239 0.0129  -0.0050 49  THR   A CA  
278  C  C   . THR   A 49  ? 0.1248 0.1113 0.1809 -0.0236 0.0011  0.0158  49  THR   A C   
279  O  O   . THR   A 49  ? 0.1462 0.1358 0.1601 -0.0105 -0.0005 0.0118  49  THR   A O   
280  C  CB  . THR   A 49  ? 0.1522 0.1211 0.1491 -0.0173 0.0105  0.0162  49  THR   A CB  
281  O  OG1 . THR   A 49  ? 0.1663 0.1012 0.1503 -0.0096 0.0063  0.0120  49  THR   A OG1 
282  C  CG2 . THR   A 49  ? 0.1663 0.1187 0.1534 -0.0152 0.0046  0.0178  49  THR   A CG2 
283  N  N   . SER   A 50  ? 0.1590 0.1068 0.1574 -0.0038 -0.0123 0.0099  50  SER   A N   
284  C  CA  . SER   A 50  ? 0.1627 0.1420 0.1488 -0.0330 -0.0196 0.0257  50  SER   A CA  
285  C  C   . SER   A 50  ? 0.1594 0.1463 0.1585 -0.0043 -0.0218 -0.0029 50  SER   A C   
286  O  O   . SER   A 50  ? 0.1782 0.1513 0.1554 -0.0228 -0.0312 0.0075  50  SER   A O   
287  C  CB  . SER   A 50  ? 0.1743 0.1994 0.1656 -0.0337 -0.0088 0.0143  50  SER   A CB  
288  O  OG  . SER   A 50  ? 0.2169 0.1802 0.2082 -0.0041 -0.0100 -0.0278 50  SER   A OG  
289  N  N   . GLU   A 51  ? 0.1920 0.1761 0.1447 -0.0294 -0.0179 0.0139  51  GLU   A N   
290  C  CA  . GLU   A 51  ? 0.1757 0.2044 0.2000 -0.0670 0.0052  -0.0289 51  GLU   A CA  
291  C  C   . GLU   A 51  ? 0.2207 0.1279 0.1994 -0.0735 -0.0298 -0.0218 51  GLU   A C   
292  O  O   . GLU   A 51  ? 0.2723 0.1370 0.2331 -0.0531 0.0124  -0.0134 51  GLU   A O   
293  C  CB  . GLU   A 51  ? 0.3352 0.3018 0.3207 -0.1371 -0.0680 -0.0543 51  GLU   A CB  
294  N  N   . SER   A 52  ? 0.2130 0.1498 0.1503 -0.0522 -0.0146 -0.0187 52  SER   A N   
295  C  CA  . SER   A 52  ? 0.2165 0.1537 0.1868 -0.0256 -0.0315 -0.0155 52  SER   A CA  
296  C  C   . SER   A 52  ? 0.1732 0.1287 0.1548 -0.0425 0.0063  0.0050  52  SER   A C   
297  O  O   . SER   A 52  ? 0.1879 0.1231 0.1798 -0.0208 -0.0023 0.0007  52  SER   A O   
298  C  CB  . SER   A 52  ? 0.2801 0.2108 0.1869 0.0573  -0.0131 -0.0434 52  SER   A CB  
299  O  OG  . SER   A 52  ? 0.3928 0.2646 0.2739 0.0893  0.1089  0.0741  52  SER   A OG  
300  N  N   . GLY   A 53  ? 0.1638 0.1217 0.1499 -0.0317 0.0023  0.0065  53  GLY   A N   
301  C  CA  . GLY   A 53  ? 0.1552 0.1130 0.1393 -0.0308 -0.0072 0.0057  53  GLY   A CA  
302  C  C   . GLY   A 53  ? 0.1524 0.1082 0.1338 -0.0161 -0.0122 0.0011  53  GLY   A C   
303  O  O   . GLY   A 53  ? 0.1491 0.1471 0.1486 -0.0137 -0.0115 0.0162  53  GLY   A O   
304  N  N   . GLU   A 54  ? 0.1676 0.1409 0.1390 -0.0325 -0.0055 -0.0070 54  GLU   A N   
305  C  CA  . GLU   A 54  ? 0.1521 0.1067 0.1775 -0.0052 0.0135  -0.0109 54  GLU   A CA  
306  C  C   . GLU   A 54  ? 0.1135 0.1261 0.1325 -0.0062 -0.0135 -0.0029 54  GLU   A C   
307  O  O   . GLU   A 54  ? 0.1395 0.1544 0.1509 -0.0201 -0.0079 0.0065  54  GLU   A O   
308  C  CB  . GLU   A 54  ? 0.2066 0.1635 0.2441 -0.0264 0.0710  -0.0018 54  GLU   A CB  
309  C  CG  . GLU   A 54  ? 0.2812 0.1084 0.3459 -0.0318 0.0069  -0.0105 54  GLU   A CG  
310  C  CD  . GLU   A 54  ? 0.4043 0.1174 0.4999 0.0098  -0.0029 -0.0433 54  GLU   A CD  
311  O  OE1 . GLU   A 54  ? 1.1217 0.1779 0.7321 -0.0085 0.5942  -0.1574 54  GLU   A OE1 
312  O  OE2 . GLU   A 54  ? 0.5712 0.1778 0.5604 0.0629  -0.0692 -0.0406 54  GLU   A OE2 
313  N  N   . LEU   A 55  ? 0.1398 0.1122 0.1380 -0.0022 -0.0019 0.0132  55  LEU   A N   
314  C  CA  . LEU   A 55  ? 0.1322 0.1093 0.1289 -0.0024 -0.0066 0.0293  55  LEU   A CA  
315  C  C   . LEU   A 55  ? 0.1347 0.1190 0.1716 0.0013  -0.0106 0.0105  55  LEU   A C   
316  O  O   . LEU   A 55  ? 0.1502 0.1292 0.1673 -0.0177 0.0149  0.0083  55  LEU   A O   
317  C  CB  . LEU   A 55  ? 0.1392 0.1208 0.1380 -0.0032 -0.0007 0.0094  55  LEU   A CB  
318  C  CG  . LEU   A 55  ? 0.1291 0.1175 0.1594 -0.0056 -0.0041 0.0133  55  LEU   A CG  
319  C  CD1 . LEU   A 55  ? 0.1750 0.1298 0.1678 0.0076  0.0069  0.0154  55  LEU   A CD1 
320  C  CD2 . LEU   A 55  ? 0.1544 0.1249 0.1688 -0.0119 0.0216  0.0018  55  LEU   A CD2 
321  N  N   . HIS   A 56  ? 0.2109 0.1355 0.1496 -0.0268 0.0157  0.0111  56  HIS   A N   
322  C  CA  . HIS   A 56  ? 0.2344 0.1486 0.2149 -0.0447 0.0588  -0.0168 56  HIS   A CA  
323  C  C   . HIS   A 56  ? 0.2131 0.1800 0.1563 0.0008  0.0253  0.0233  56  HIS   A C   
324  O  O   . HIS   A 56  ? 0.2356 0.1776 0.2121 -0.0125 0.0116  0.0275  56  HIS   A O   
325  C  CB  . HIS   A 56  ? 0.2897 0.1785 0.2340 -0.0907 0.0681  -0.0117 56  HIS   A CB  
326  C  CG  . HIS   A 56  ? 0.2560 0.2066 0.2478 -0.0228 0.0519  -0.0502 56  HIS   A CG  
327  N  ND1 . HIS   A 56  ? 0.2990 0.2024 0.4144 0.0177  0.0783  -0.0397 56  HIS   A ND1 
328  C  CD2 . HIS   A 56  ? 0.3051 0.2531 0.3319 0.0071  0.1131  -0.0068 56  HIS   A CD2 
329  C  CE1 . HIS   A 56  ? 0.3520 0.2113 0.3683 0.0103  0.0859  -0.0544 56  HIS   A CE1 
330  N  NE2 . HIS   A 56  ? 0.4609 0.1691 0.6394 0.0639  -0.0332 -0.0924 56  HIS   A NE2 
331  N  N   . GLY   A 57  ? 0.2152 0.1910 0.1738 -0.0336 -0.0013 0.0214  57  GLY   A N   
332  C  CA  . GLY   A 57  ? 0.2461 0.2034 0.1779 -0.0498 -0.0113 0.0320  57  GLY   A CA  
333  C  C   . GLY   A 57  ? 0.1867 0.1657 0.1855 -0.0244 -0.0167 0.0344  57  GLY   A C   
334  O  O   . GLY   A 57  ? 0.2374 0.1747 0.2161 -0.0283 -0.0436 0.0523  57  GLY   A O   
335  N  N   . LEU   A 58  ? 0.1616 0.1276 0.1771 -0.0132 -0.0016 0.0408  58  LEU   A N   
336  C  CA  . LEU   A 58  ? 0.1178 0.1348 0.1910 -0.0052 -0.0090 0.0246  58  LEU   A CA  
337  C  C   . LEU   A 58  ? 0.1540 0.1239 0.1639 -0.0102 0.0057  0.0047  58  LEU   A C   
338  O  O   . LEU   A 58  ? 0.1585 0.1304 0.2083 0.0005  0.0142  0.0183  58  LEU   A O   
339  C  CB  . LEU   A 58  ? 0.1097 0.1185 0.1909 -0.0076 -0.0037 0.0176  58  LEU   A CB  
340  C  CG  . LEU   A 58  ? 0.1411 0.1216 0.1968 -0.0092 -0.0137 0.0084  58  LEU   A CG  
341  C  CD1 . LEU   A 58  ? 0.1470 0.1405 0.2394 -0.0250 0.0026  0.0482  58  LEU   A CD1 
342  C  CD2 . LEU   A 58  ? 0.1709 0.1520 0.2582 0.0059  0.0390  0.0444  58  LEU   A CD2 
343  N  N   . THR   A 59  ? 0.1534 0.1291 0.1744 -0.0105 0.0042  0.0265  59  THR   A N   
344  C  CA  . THR   A 59  ? 0.1490 0.1339 0.1660 -0.0158 0.0131  0.0244  59  THR   A CA  
345  C  C   . THR   A 59  ? 0.1607 0.1327 0.1541 -0.0161 0.0039  0.0297  59  THR   A C   
346  O  O   . THR   A 59  ? 0.2302 0.1653 0.1878 -0.0561 0.0323  -0.0264 59  THR   A O   
347  C  CB  . THR   A 59  ? 0.1594 0.1228 0.1761 -0.0238 -0.0066 0.0227  59  THR   A CB  
348  O  OG1 . THR   A 59  ? 0.1497 0.1299 0.1904 -0.0203 -0.0099 0.0178  59  THR   A OG1 
349  C  CG2 . THR   A 59  ? 0.1694 0.1193 0.1821 -0.0251 0.0031  0.0185  59  THR   A CG2 
350  N  N   . THR   A 60  ? 0.1722 0.1470 0.1929 -0.0441 0.0412  0.0022  60  THR   A N   
351  C  CA  . THR   A 60  ? 0.1756 0.1544 0.1693 0.0030  0.0353  0.0053  60  THR   A CA  
352  C  C   . THR   A 60  ? 0.1888 0.1142 0.1776 -0.0203 0.0308  0.0309  60  THR   A C   
353  O  O   . THR   A 60  ? 0.2050 0.1385 0.1622 -0.0290 0.0169  0.0158  60  THR   A O   
354  C  CB  . THR   A 60  ? 0.1817 0.1785 0.1521 -0.0119 0.0107  0.0031  60  THR   A CB  
355  O  OG1 . THR   A 60  ? 0.1910 0.1767 0.1844 -0.0330 -0.0175 0.0291  60  THR   A OG1 
356  C  CG2 . THR   A 60  ? 0.1831 0.2719 0.2588 -0.0476 -0.0226 -0.0098 60  THR   A CG2 
357  N  N   . GLU   A 61  ? 0.1923 0.1451 0.1679 -0.0037 0.0128  -0.0081 61  GLU   A N   
358  C  CA  . GLU   A 61  ? 0.2159 0.1581 0.2160 0.0167  0.0000  0.0173  61  GLU   A CA  
359  C  C   . GLU   A 61  ? 0.1669 0.1686 0.1940 0.0120  0.0191  0.0141  61  GLU   A C   
360  O  O   . GLU   A 61  ? 0.2243 0.1400 0.2944 0.0134  -0.0485 0.0188  61  GLU   A O   
361  C  CB  . GLU   A 61  ? 0.2090 0.1650 0.3985 -0.0134 0.0489  -0.1039 61  GLU   A CB  
362  N  N   . GLU   A 62  ? 0.1676 0.1671 0.1691 0.0002  0.0228  0.0110  62  GLU   A N   
363  C  CA  . GLU   A 62  ? 0.1748 0.1596 0.2155 -0.0193 0.0456  0.0254  62  GLU   A CA  
364  C  C   . GLU   A 62  ? 0.1460 0.1215 0.2045 -0.0351 0.0133  0.0293  62  GLU   A C   
365  O  O   . GLU   A 62  ? 0.1386 0.1297 0.2508 -0.0126 0.0002  0.0250  62  GLU   A O   
366  C  CB  . GLU   A 62  ? 0.2695 0.1646 0.2470 -0.0443 0.0376  0.0778  62  GLU   A CB  
367  C  CG  . GLU   A 62  ? 0.3318 0.2869 0.2777 -0.0112 0.1354  0.0865  62  GLU   A CG  
368  C  CD  . GLU   A 62  ? 0.4212 0.3113 0.2810 -0.0757 0.0558  0.0816  62  GLU   A CD  
369  O  OE1 . GLU   A 62  ? 0.2970 0.3647 0.2026 0.0243  -0.0013 0.0100  62  GLU   A OE1 
370  N  N   . GLU   A 63  ? 0.1330 0.1209 0.1606 -0.0080 -0.0055 0.0364  63  GLU   A N   
371  C  CA  A GLU   A 63  ? 0.1357 0.1402 0.1808 -0.0026 -0.0138 0.0635  63  GLU   A CA  
372  C  CA  B GLU   A 63  ? 0.1544 0.1378 0.1860 -0.0251 -0.0107 0.0547  63  GLU   A CA  
373  C  C   . GLU   A 63  ? 0.1110 0.1146 0.1720 -0.0046 0.0047  0.0468  63  GLU   A C   
374  O  O   . GLU   A 63  ? 0.1419 0.1186 0.1533 -0.0057 -0.0126 0.0128  63  GLU   A O   
375  C  CB  A GLU   A 63  ? 0.1566 0.1729 0.1678 0.0483  -0.0187 0.0096  63  GLU   A CB  
376  C  CB  B GLU   A 63  ? 0.1548 0.1538 0.1429 0.0099  -0.0321 0.0409  63  GLU   A CB  
377  C  CG  A GLU   A 63  ? 0.1119 0.1544 0.2297 -0.0391 -0.0071 0.0339  63  GLU   A CG  
378  C  CG  B GLU   A 63  ? 0.1383 0.1435 0.2098 -0.0320 0.0075  0.0464  63  GLU   A CG  
379  C  CD  A GLU   A 63  ? 0.1305 0.2254 0.2280 -0.0022 -0.0016 -0.0150 63  GLU   A CD  
380  C  CD  B GLU   A 63  ? 0.1453 0.1361 0.1947 -0.0062 0.0130  0.0471  63  GLU   A CD  
381  O  OE1 A GLU   A 63  ? 0.1325 0.2373 0.3086 -0.0015 0.0111  0.0739  63  GLU   A OE1 
382  O  OE1 B GLU   A 63  ? 0.1501 0.1383 0.2446 0.0066  0.0010  0.0632  63  GLU   A OE1 
383  O  OE2 A GLU   A 63  ? 0.1278 0.2266 0.1584 0.0100  -0.0024 0.0249  63  GLU   A OE2 
384  O  OE2 B GLU   A 63  ? 0.1009 0.0869 0.1753 0.0060  -0.0028 0.0378  63  GLU   A OE2 
385  N  N   . PHE   A 64  ? 0.1353 0.1215 0.1556 -0.0026 -0.0039 0.0259  64  PHE   A N   
386  C  CA  . PHE   A 64  ? 0.1238 0.1182 0.1301 -0.0082 -0.0027 0.0119  64  PHE   A CA  
387  C  C   . PHE   A 64  ? 0.1239 0.0980 0.1589 0.0087  -0.0126 0.0214  64  PHE   A C   
388  O  O   . PHE   A 64  ? 0.1266 0.1109 0.1800 -0.0031 -0.0003 0.0322  64  PHE   A O   
389  C  CB  . PHE   A 64  ? 0.1400 0.1314 0.1398 -0.0230 -0.0155 0.0237  64  PHE   A CB  
390  C  CG  . PHE   A 64  ? 0.1331 0.1313 0.1483 -0.0122 -0.0190 0.0324  64  PHE   A CG  
391  C  CD1 . PHE   A 64  ? 0.1528 0.1177 0.1591 -0.0023 -0.0009 0.0385  64  PHE   A CD1 
392  C  CD2 . PHE   A 64  ? 0.2132 0.1253 0.1969 -0.0033 -0.0159 0.0438  64  PHE   A CD2 
393  C  CE1 . PHE   A 64  ? 0.1674 0.1501 0.1443 -0.0213 -0.0132 0.0165  64  PHE   A CE1 
394  C  CE2 . PHE   A 64  ? 0.2179 0.1474 0.2106 0.0277  -0.0259 0.0658  64  PHE   A CE2 
395  C  CZ  . PHE   A 64  ? 0.2212 0.1653 0.1698 -0.0272 -0.0123 0.0670  64  PHE   A CZ  
396  N  N   . VAL   A 65  ? 0.1171 0.1165 0.1583 -0.0030 -0.0068 0.0299  65  VAL   A N   
397  C  CA  . VAL   A 65  ? 0.1207 0.1012 0.1226 -0.0110 -0.0013 0.0011  65  VAL   A CA  
398  C  C   . VAL   A 65  ? 0.1057 0.0964 0.1626 -0.0017 -0.0002 0.0360  65  VAL   A C   
399  O  O   . VAL   A 65  ? 0.1225 0.1325 0.1646 -0.0168 0.0078  0.0397  65  VAL   A O   
400  C  CB  . VAL   A 65  ? 0.1288 0.1282 0.1624 -0.0255 -0.0128 0.0234  65  VAL   A CB  
401  C  CG1 . VAL   A 65  ? 0.1607 0.1433 0.1821 -0.0273 -0.0419 0.0536  65  VAL   A CG1 
402  C  CG2 . VAL   A 65  ? 0.1492 0.1060 0.1733 -0.0128 -0.0153 0.0324  65  VAL   A CG2 
403  N  N   . GLU   A 66  ? 0.1142 0.1211 0.1708 -0.0066 0.0054  0.0365  66  GLU   A N   
404  C  CA  . GLU   A 66  ? 0.1170 0.1047 0.1640 -0.0147 0.0057  0.0351  66  GLU   A CA  
405  C  C   . GLU   A 66  ? 0.1269 0.1207 0.1799 0.0000  -0.0172 0.0395  66  GLU   A C   
406  O  O   . GLU   A 66  ? 0.2037 0.1320 0.1818 0.0125  0.0072  0.0441  66  GLU   A O   
407  C  CB  . GLU   A 66  ? 0.1275 0.1492 0.1793 0.0052  -0.0145 0.0461  66  GLU   A CB  
408  C  CG  . GLU   A 66  ? 0.1361 0.1600 0.1734 0.0127  0.0024  0.0404  66  GLU   A CG  
409  C  CD  . GLU   A 66  ? 0.1141 0.1628 0.2062 -0.0114 -0.0122 0.0589  66  GLU   A CD  
410  O  OE1 . GLU   A 66  ? 0.1365 0.1722 0.1818 -0.0165 -0.0108 0.0562  66  GLU   A OE1 
411  O  OE2 . GLU   A 66  ? 0.1570 0.1959 0.2339 -0.0097 -0.0216 0.0990  66  GLU   A OE2 
412  N  N   . GLY   A 67  ? 0.1499 0.1005 0.1426 0.0098  0.0030  0.0310  67  GLY   A N   
413  C  CA  . GLY   A 67  ? 0.1491 0.1298 0.1643 0.0088  0.0164  0.0020  67  GLY   A CA  
414  C  C   . GLY   A 67  ? 0.1505 0.1005 0.1489 -0.0108 -0.0012 0.0083  67  GLY   A C   
415  O  O   . GLY   A 67  ? 0.1604 0.1136 0.1605 0.0118  0.0008  0.0132  67  GLY   A O   
416  N  N   . ILE   A 68  ? 0.1367 0.1049 0.1515 -0.0049 -0.0040 0.0218  68  ILE   A N   
417  C  CA  . ILE   A 68  ? 0.1417 0.0982 0.1563 -0.0105 -0.0025 0.0248  68  ILE   A CA  
418  C  C   . ILE   A 68  ? 0.1253 0.0981 0.1407 0.0001  -0.0041 0.0136  68  ILE   A C   
419  O  O   . ILE   A 68  ? 0.1499 0.1049 0.1798 0.0003  -0.0060 0.0158  68  ILE   A O   
420  C  CB  . ILE   A 68  ? 0.1564 0.1116 0.1464 -0.0023 -0.0106 0.0056  68  ILE   A CB  
421  C  CG1 . ILE   A 68  ? 0.1636 0.2081 0.2008 0.0275  -0.0291 -0.0247 68  ILE   A CG1 
422  C  CG2 . ILE   A 68  ? 0.2035 0.1405 0.1619 -0.0178 0.0143  0.0045  68  ILE   A CG2 
423  C  CD1 . ILE   A 68  ? 0.1974 0.2211 0.2041 -0.0263 -0.0620 0.0000  68  ILE   A CD1 
424  N  N   . TYR   A 69  ? 0.1215 0.1125 0.1547 -0.0080 -0.0106 0.0178  69  TYR   A N   
425  C  CA  . TYR   A 69  ? 0.1326 0.0977 0.1541 0.0123  -0.0023 0.0223  69  TYR   A CA  
426  C  C   . TYR   A 69  ? 0.1262 0.1034 0.1525 0.0039  0.0015  -0.0009 69  TYR   A C   
427  O  O   . TYR   A 69  ? 0.1331 0.1246 0.1656 0.0039  0.0116  0.0316  69  TYR   A O   
428  C  CB  . TYR   A 69  ? 0.1203 0.1131 0.1592 0.0010  -0.0052 0.0064  69  TYR   A CB  
429  C  CG  . TYR   A 69  ? 0.1294 0.1009 0.1628 -0.0099 -0.0113 0.0263  69  TYR   A CG  
430  C  CD1 . TYR   A 69  ? 0.1308 0.1177 0.1539 -0.0071 -0.0056 0.0037  69  TYR   A CD1 
431  C  CD2 . TYR   A 69  ? 0.1045 0.1323 0.1641 -0.0098 0.0089  0.0125  69  TYR   A CD2 
432  C  CE1 . TYR   A 69  ? 0.1048 0.1286 0.1649 -0.0040 0.0090  0.0151  69  TYR   A CE1 
433  C  CE2 . TYR   A 69  ? 0.1395 0.1302 0.1690 -0.0008 -0.0055 0.0169  69  TYR   A CE2 
434  C  CZ  . TYR   A 69  ? 0.1249 0.1071 0.1656 -0.0040 -0.0015 0.0156  69  TYR   A CZ  
435  O  OH  . TYR   A 69  ? 0.1537 0.1462 0.1653 0.0000  0.0112  0.0490  69  TYR   A OH  
436  N  N   . LYS   A 70  ? 0.1371 0.1024 0.1463 0.0032  -0.0015 0.0218  70  LYS   A N   
437  C  CA  . LYS   A 70  ? 0.1420 0.1193 0.1448 -0.0192 0.0147  0.0140  70  LYS   A CA  
438  C  C   . LYS   A 70  ? 0.1413 0.1347 0.1394 -0.0281 0.0196  0.0226  70  LYS   A C   
439  O  O   . LYS   A 70  ? 0.1587 0.1275 0.1702 -0.0201 -0.0194 0.0221  70  LYS   A O   
440  C  CB  . LYS   A 70  ? 0.1521 0.1990 0.1570 -0.0121 -0.0107 -0.0011 70  LYS   A CB  
441  C  CG  . LYS   A 70  ? 0.1399 0.2405 0.2024 0.0195  0.0387  -0.0225 70  LYS   A CG  
442  C  CD  . LYS   A 70  ? 0.2426 0.3375 0.2654 -0.0100 0.0081  -0.0064 70  LYS   A CD  
443  C  CE  . LYS   A 70  ? 0.2668 0.2789 0.2734 0.0148  0.1176  -0.0375 70  LYS   A CE  
444  N  NZ  . LYS   A 70  ? 0.4990 0.3220 0.3682 -0.0524 0.1047  -0.1332 70  LYS   A NZ  
445  N  N   . VAL   A 71  ? 0.1496 0.1388 0.1682 -0.0339 -0.0208 0.0472  71  VAL   A N   
446  C  CA  . VAL   A 71  ? 0.1689 0.1585 0.1446 -0.0224 -0.0228 0.0466  71  VAL   A CA  
447  C  C   . VAL   A 71  ? 0.1654 0.1330 0.1691 -0.0321 -0.0257 0.0272  71  VAL   A C   
448  O  O   . VAL   A 71  ? 0.1956 0.1625 0.1708 -0.0200 -0.0153 0.0546  71  VAL   A O   
449  C  CB  . VAL   A 71  ? 0.2180 0.1563 0.1535 -0.0249 -0.0266 0.0371  71  VAL   A CB  
450  C  CG1 . VAL   A 71  ? 0.2196 0.1859 0.1651 -0.0457 -0.0235 0.0426  71  VAL   A CG1 
451  C  CG2 . VAL   A 71  ? 0.1850 0.1407 0.1923 -0.0085 -0.0173 0.0308  71  VAL   A CG2 
452  N  N   . GLU   A 72  ? 0.1744 0.1433 0.1576 -0.0456 -0.0172 0.0484  72  GLU   A N   
453  C  CA  . GLU   A 72  ? 0.1981 0.1286 0.1531 -0.0349 -0.0230 0.0050  72  GLU   A CA  
454  C  C   . GLU   A 72  ? 0.1725 0.1369 0.1210 -0.0300 -0.0072 0.0226  72  GLU   A C   
455  O  O   . GLU   A 72  ? 0.1779 0.1424 0.1568 -0.0486 -0.0185 0.0380  72  GLU   A O   
456  C  CB  . GLU   A 72  ? 0.2527 0.1682 0.1746 -0.0585 -0.0190 -0.0203 72  GLU   A CB  
457  C  CG  . GLU   A 72  ? 0.3429 0.2393 0.2556 0.0410  0.0451  -0.0072 72  GLU   A CG  
458  C  CD  . GLU   A 72  ? 0.6711 0.2592 0.2930 0.0459  -0.0284 -0.0663 72  GLU   A CD  
459  O  OE1 . GLU   A 72  ? 0.5948 0.4736 0.4057 0.2798  0.1347  0.0758  72  GLU   A OE1 
460  O  OE2 . GLU   A 72  ? 0.3948 0.2884 0.4041 0.0590  0.0031  -0.0510 72  GLU   A OE2 
461  N  N   . ILE   A 73  ? 0.1829 0.1372 0.1280 -0.0261 -0.0099 0.0247  73  ILE   A N   
462  C  CA  . ILE   A 73  ? 0.1774 0.1414 0.1154 -0.0160 0.0021  0.0128  73  ILE   A CA  
463  C  C   . ILE   A 73  ? 0.2078 0.1036 0.1379 -0.0221 0.0201  -0.0024 73  ILE   A C   
464  O  O   . ILE   A 73  ? 0.2160 0.1520 0.1270 -0.0248 0.0209  -0.0030 73  ILE   A O   
465  C  CB  . ILE   A 73  ? 0.1970 0.1239 0.1292 -0.0183 0.0114  0.0195  73  ILE   A CB  
466  C  CG1 . ILE   A 73  ? 0.1659 0.1593 0.1531 -0.0382 -0.0068 0.0095  73  ILE   A CG1 
467  C  CG2 . ILE   A 73  ? 0.1984 0.1409 0.1704 -0.0511 0.0413  -0.0135 73  ILE   A CG2 
468  C  CD1 . ILE   A 73  ? 0.2463 0.1583 0.2172 -0.0126 0.0200  0.0154  73  ILE   A CD1 
469  N  N   . ASP   A 74  ? 0.1993 0.1024 0.1631 -0.0148 0.0406  0.0083  74  ASP   A N   
470  C  CA  . ASP   A 74  ? 0.2338 0.1205 0.1597 -0.0020 0.0410  0.0068  74  ASP   A CA  
471  C  C   . ASP   A 74  ? 0.2390 0.1075 0.1419 0.0143  0.0372  -0.0110 74  ASP   A C   
472  O  O   . ASP   A 74  ? 0.2027 0.1302 0.1577 0.0114  0.0236  0.0213  74  ASP   A O   
473  C  CB  . ASP   A 74  ? 0.2343 0.1333 0.2213 0.0399  0.0491  0.0450  74  ASP   A CB  
474  C  CG  . ASP   A 74  ? 0.4163 0.1337 0.3084 0.0771  0.1205  0.0599  74  ASP   A CG  
475  O  OD1 . ASP   A 74  ? 0.3794 0.1226 0.2778 -0.0095 0.1503  -0.0185 74  ASP   A OD1 
476  O  OD2 . ASP   A 74  ? 0.4756 0.2154 0.4097 0.1619  0.1900  0.1385  74  ASP   A OD2 
477  N  N   . THR   A 75  ? 0.1776 0.1133 0.1574 -0.0070 0.0245  0.0057  75  THR   A N   
478  C  CA  . THR   A 75  ? 0.1657 0.1110 0.1335 -0.0024 0.0364  -0.0085 75  THR   A CA  
479  C  C   . THR   A 75  ? 0.1702 0.1030 0.1731 0.0109  0.0241  0.0316  75  THR   A C   
480  O  O   . THR   A 75  ? 0.1635 0.1276 0.1436 0.0098  0.0156  0.0099  75  THR   A O   
481  C  CB  . THR   A 75  ? 0.1687 0.1194 0.1518 0.0143  0.0267  0.0320  75  THR   A CB  
482  O  OG1 . THR   A 75  ? 0.1552 0.1219 0.1632 0.0019  0.0157  0.0095  75  THR   A OG1 
483  C  CG2 . THR   A 75  ? 0.1610 0.1211 0.1795 0.0102  0.0538  -0.0100 75  THR   A CG2 
484  N  N   . LYS   A 76  ? 0.1654 0.1164 0.1617 0.0059  0.0215  0.0068  76  LYS   A N   
485  C  CA  . LYS   A 76  ? 0.1735 0.1638 0.1632 0.0097  0.0262  -0.0077 76  LYS   A CA  
486  C  C   . LYS   A 76  ? 0.1915 0.1811 0.1608 0.0460  0.0198  -0.0104 76  LYS   A C   
487  O  O   . LYS   A 76  ? 0.1901 0.1989 0.1976 0.0647  -0.0284 -0.0361 76  LYS   A O   
488  C  CB  . LYS   A 76  ? 0.1911 0.1800 0.1824 0.0387  0.0133  -0.0221 76  LYS   A CB  
489  C  CG  . LYS   A 76  ? 0.2134 0.2389 0.1648 0.0380  0.0044  -0.0479 76  LYS   A CG  
490  C  CD  . LYS   A 76  ? 0.2015 0.2629 0.2295 0.0387  -0.0248 -0.0465 76  LYS   A CD  
491  C  CE  . LYS   A 76  ? 0.2260 0.3158 0.2943 0.0658  -0.0088 -0.1241 76  LYS   A CE  
492  N  NZ  . LYS   A 76  ? 0.3237 0.3054 0.3014 0.0756  -0.0482 -0.0859 76  LYS   A NZ  
493  N  N   . SER   A 77  ? 0.2407 0.1617 0.1878 0.0802  0.0253  -0.0251 77  SER   A N   
494  C  CA  . SER   A 77  ? 0.2760 0.2156 0.2040 0.1133  -0.0182 -0.0336 77  SER   A CA  
495  C  C   . SER   A 77  ? 0.2463 0.2321 0.2001 0.1205  -0.0420 -0.0459 77  SER   A C   
496  O  O   . SER   A 77  ? 0.2754 0.2520 0.2204 0.1466  -0.0509 -0.0155 77  SER   A O   
497  C  CB  . SER   A 77  ? 0.4538 0.2562 0.2084 0.1864  0.0029  0.0287  77  SER   A CB  
498  O  OG  . SER   A 77  ? 0.5615 0.2049 0.3238 0.1839  0.0702  0.0453  77  SER   A OG  
499  N  N   . TYR   A 78  ? 0.3051 0.1901 0.1854 0.1280  -0.0381 -0.0121 78  TYR   A N   
500  C  CA  . TYR   A 78  ? 0.2385 0.2569 0.1756 0.1233  -0.0742 -0.0256 78  TYR   A CA  
501  C  C   . TYR   A 78  ? 0.2086 0.2361 0.2052 0.0897  -0.0490 -0.0717 78  TYR   A C   
502  O  O   . TYR   A 78  ? 0.2299 0.2438 0.2033 0.1110  -0.0635 -0.0569 78  TYR   A O   
503  C  CB  . TYR   A 78  ? 0.2076 0.2083 0.1544 0.0801  -0.0165 -0.0172 78  TYR   A CB  
504  C  CG  . TYR   A 78  ? 0.2146 0.2167 0.1642 0.0777  -0.0321 -0.0196 78  TYR   A CG  
505  C  CD1 . TYR   A 78  ? 0.2392 0.1692 0.1645 0.0695  -0.0192 -0.0020 78  TYR   A CD1 
506  C  CD2 . TYR   A 78  ? 0.1614 0.2048 0.1631 0.0835  -0.0043 0.0051  78  TYR   A CD2 
507  C  CE1 . TYR   A 78  ? 0.2447 0.1655 0.1387 0.0785  -0.0061 -0.0026 78  TYR   A CE1 
508  C  CE2 . TYR   A 78  ? 0.1792 0.1880 0.1630 0.0823  -0.0001 0.0167  78  TYR   A CE2 
509  C  CZ  . TYR   A 78  ? 0.1715 0.1769 0.1636 0.0687  -0.0134 -0.0051 78  TYR   A CZ  
510  O  OH  . TYR   A 78  ? 0.2171 0.1676 0.1728 0.0566  0.0071  0.0032  78  TYR   A OH  
511  N  N   . TRP   A 79  ? 0.1898 0.1851 0.1698 0.0717  -0.0315 -0.0235 79  TRP   A N   
512  C  CA  . TRP   A 79  ? 0.1854 0.1892 0.1485 0.0622  -0.0180 -0.0215 79  TRP   A CA  
513  C  C   . TRP   A 79  ? 0.1850 0.1859 0.2268 0.0300  0.0111  -0.0595 79  TRP   A C   
514  O  O   . TRP   A 79  ? 0.1638 0.2415 0.2839 0.0614  -0.0427 -0.0577 79  TRP   A O   
515  C  CB  . TRP   A 79  ? 0.1427 0.1733 0.1733 0.0274  0.0392  -0.0047 79  TRP   A CB  
516  C  CG  . TRP   A 79  ? 0.1404 0.1559 0.1512 0.0051  -0.0091 -0.0083 79  TRP   A CG  
517  C  CD1 . TRP   A 79  ? 0.1515 0.1393 0.1358 -0.0016 0.0189  -0.0353 79  TRP   A CD1 
518  C  CD2 . TRP   A 79  ? 0.1389 0.1781 0.1541 -0.0068 0.0040  -0.0315 79  TRP   A CD2 
519  N  NE1 . TRP   A 79  ? 0.1315 0.1316 0.1550 -0.0148 0.0277  0.0092  79  TRP   A NE1 
520  C  CE2 . TRP   A 79  ? 0.0943 0.1631 0.1656 -0.0112 0.0129  -0.0139 79  TRP   A CE2 
521  C  CE3 . TRP   A 79  ? 0.0987 0.1887 0.2085 0.0214  -0.0353 -0.0226 79  TRP   A CE3 
522  C  CZ2 . TRP   A 79  ? 0.1197 0.1688 0.1599 0.0178  0.0001  -0.0089 79  TRP   A CZ2 
523  C  CZ3 . TRP   A 79  ? 0.1495 0.1915 0.2218 -0.0055 0.0086  -0.0485 79  TRP   A CZ3 
524  C  CH2 . TRP   A 79  ? 0.1461 0.1517 0.1922 0.0369  -0.0126 -0.0112 79  TRP   A CH2 
525  N  N   . LYS   A 80  ? 0.1740 0.1889 0.2364 0.0637  -0.0549 -0.0616 80  LYS   A N   
526  C  CA  . LYS   A 80  ? 0.2201 0.2726 0.2801 0.0908  -0.0363 -0.1051 80  LYS   A CA  
527  C  C   . LYS   A 80  ? 0.1825 0.3088 0.3536 0.1061  -0.0760 -0.1103 80  LYS   A C   
528  O  O   . LYS   A 80  ? 0.2109 0.2956 0.4160 0.1334  -0.1259 -0.1167 80  LYS   A O   
529  C  CB  . LYS   A 80  ? 0.2088 0.2296 0.2544 0.0843  -0.0366 -0.0612 80  LYS   A CB  
530  C  CG  . LYS   A 80  ? 0.2915 0.2624 0.2570 0.0817  -0.0046 -0.0462 80  LYS   A CG  
531  C  CD  . LYS   A 80  ? 0.2559 0.2798 0.4215 0.0455  0.0005  -0.0189 80  LYS   A CD  
532  N  N   . ALA   A 81  ? 0.3089 0.2902 0.2579 0.1919  -0.1293 -0.0701 81  ALA   A N   
533  C  CA  . ALA   A 81  ? 0.2327 0.3284 0.3500 0.1418  -0.1381 -0.1026 81  ALA   A CA  
534  C  C   . ALA   A 81  ? 0.4026 0.3159 0.3721 0.1552  -0.1830 -0.1972 81  ALA   A C   
535  O  O   . ALA   A 81  ? 0.5781 0.3770 0.6919 0.0977  -0.2729 -0.2064 81  ALA   A O   
536  C  CB  . ALA   A 81  ? 0.4195 0.4313 0.3222 0.2165  -0.2016 -0.0841 81  ALA   A CB  
537  N  N   . LEU   A 82  ? 0.2173 0.3340 0.2834 0.1177  -0.1033 -0.0534 82  LEU   A N   
538  C  CA  . LEU   A 82  ? 0.1406 0.3809 0.3733 0.1003  -0.0292 -0.0666 82  LEU   A CA  
539  C  C   . LEU   A 82  ? 0.2110 0.2728 0.2171 0.1165  -0.0615 -0.0489 82  LEU   A C   
540  O  O   . LEU   A 82  ? 0.2881 0.3463 0.4266 0.1373  0.0423  -0.0685 82  LEU   A O   
541  C  CB  . LEU   A 82  ? 0.2154 0.3039 0.3178 0.0988  -0.0622 -0.1031 82  LEU   A CB  
542  C  CG  . LEU   A 82  ? 0.2469 0.2820 0.3181 0.0887  -0.0680 -0.0994 82  LEU   A CG  
543  C  CD1 . LEU   A 82  ? 0.2305 0.3171 0.2741 0.0692  -0.0354 -0.1078 82  LEU   A CD1 
544  C  CD2 . LEU   A 82  ? 0.2909 0.3153 0.3843 0.0920  -0.0469 -0.1586 82  LEU   A CD2 
545  N  N   . GLY   A 83  ? 0.2224 0.3713 0.3444 0.1497  -0.1062 -0.1403 83  GLY   A N   
546  C  CA  . GLY   A 83  ? 0.2133 0.3170 0.3565 0.0810  -0.1013 -0.1165 83  GLY   A CA  
547  C  C   . GLY   A 83  ? 0.1646 0.3113 0.3103 0.0375  -0.0960 -0.0721 83  GLY   A C   
548  O  O   . GLY   A 83  ? 0.1982 0.5338 0.3907 0.0152  -0.0429 -0.1857 83  GLY   A O   
549  N  N   . ILE   A 84  ? 0.1680 0.3134 0.3201 0.0557  -0.0981 -0.0959 84  ILE   A N   
550  C  CA  . ILE   A 84  ? 0.1880 0.2696 0.2496 -0.0013 -0.0186 -0.0210 84  ILE   A CA  
551  C  C   . ILE   A 84  ? 0.1425 0.3262 0.2785 -0.0478 0.0094  -0.0280 84  ILE   A C   
552  O  O   . ILE   A 84  ? 0.2365 0.3410 0.2899 -0.0548 -0.0722 -0.0044 84  ILE   A O   
553  C  CB  . ILE   A 84  ? 0.1679 0.2786 0.2520 0.0312  -0.0102 -0.0617 84  ILE   A CB  
554  C  CG1 . ILE   A 84  ? 0.2881 0.1959 0.3353 0.0422  -0.0445 -0.0045 84  ILE   A CG1 
555  C  CG2 . ILE   A 84  ? 0.1821 0.2832 0.2459 0.0118  -0.0233 -0.0149 84  ILE   A CG2 
556  C  CD1 . ILE   A 84  ? 0.3329 0.2440 0.6110 -0.0165 0.0678  -0.0418 84  ILE   A CD1 
557  N  N   . SER   A 85  ? 0.1669 0.2191 0.2365 0.0030  0.0079  -0.0464 85  SER   A N   
558  C  CA  A SER   A 85  ? 0.1413 0.2164 0.2410 0.0144  0.0144  -0.0295 85  SER   A CA  
559  C  CA  B SER   A 85  ? 0.1425 0.2124 0.2509 0.0098  0.0099  -0.0267 85  SER   A CA  
560  C  C   . SER   A 85  ? 0.1183 0.2086 0.2372 -0.0071 0.0080  -0.0382 85  SER   A C   
561  O  O   . SER   A 85  ? 0.1793 0.2523 0.2892 0.0080  -0.0246 0.0723  85  SER   A O   
562  C  CB  A SER   A 85  ? 0.1272 0.3065 0.2785 0.0526  0.0074  -0.0709 85  SER   A CB  
563  C  CB  B SER   A 85  ? 0.1300 0.3255 0.2614 0.0345  -0.0068 -0.0675 85  SER   A CB  
564  O  OG  A SER   A 85  ? 0.3541 0.3570 0.3643 -0.0636 0.0465  -0.1446 85  SER   A OG  
565  O  OG  B SER   A 85  ? 0.1069 0.2907 0.3201 0.0339  0.0278  -0.0906 85  SER   A OG  
566  N  N   . PRO   A 86  ? 0.1611 0.2082 0.1847 0.0056  0.0076  -0.0145 86  PRO   A N   
567  C  CA  . PRO   A 86  ? 0.1364 0.1981 0.1893 0.0049  -0.0068 -0.0210 86  PRO   A CA  
568  C  C   . PRO   A 86  ? 0.1691 0.2106 0.1725 0.0043  0.0169  -0.0502 86  PRO   A C   
569  O  O   . PRO   A 86  ? 0.1649 0.1932 0.1895 0.0070  0.0035  -0.0210 86  PRO   A O   
570  C  CB  . PRO   A 86  ? 0.1784 0.3084 0.2066 -0.0047 0.0612  -0.0621 86  PRO   A CB  
571  C  CG  . PRO   A 86  ? 0.2442 0.2294 0.2641 -0.0963 0.0011  -0.0247 86  PRO   A CG  
572  C  CD  . PRO   A 86  ? 0.2302 0.1693 0.2484 -0.0241 -0.0094 -0.0315 86  PRO   A CD  
573  N  N   . PHE   A 87  ? 0.1530 0.1456 0.1663 -0.0086 0.0109  -0.0369 87  PHE   A N   
574  C  CA  . PHE   A 87  ? 0.1599 0.1758 0.1470 -0.0051 0.0333  -0.0160 87  PHE   A CA  
575  C  C   . PHE   A 87  ? 0.1402 0.1708 0.1397 0.0118  -0.0013 -0.0296 87  PHE   A C   
576  O  O   . PHE   A 87  ? 0.1654 0.1557 0.1675 -0.0063 0.0172  -0.0437 87  PHE   A O   
577  C  CB  . PHE   A 87  ? 0.1472 0.1713 0.1558 -0.0018 -0.0072 -0.0233 87  PHE   A CB  
578  C  CG  . PHE   A 87  ? 0.1816 0.1340 0.1682 0.0043  -0.0052 -0.0149 87  PHE   A CG  
579  C  CD1 . PHE   A 87  ? 0.1699 0.1998 0.1556 -0.0157 0.0138  -0.0222 87  PHE   A CD1 
580  C  CD2 . PHE   A 87  ? 0.1638 0.2135 0.2063 -0.0392 -0.0061 -0.0510 87  PHE   A CD2 
581  C  CE1 . PHE   A 87  ? 0.2383 0.1926 0.1633 -0.0062 -0.0149 -0.0262 87  PHE   A CE1 
582  C  CE2 . PHE   A 87  ? 0.2121 0.1728 0.2339 0.0369  -0.0494 -0.0491 87  PHE   A CE2 
583  C  CZ  . PHE   A 87  ? 0.2397 0.2008 0.2038 0.0116  -0.0757 -0.0524 87  PHE   A CZ  
584  N  N   . HIS   A 88  ? 0.1499 0.1540 0.1393 -0.0089 0.0163  -0.0294 88  HIS   A N   
585  C  CA  . HIS   A 88  ? 0.1363 0.1507 0.1282 -0.0066 0.0022  -0.0192 88  HIS   A CA  
586  C  C   . HIS   A 88  ? 0.1463 0.1911 0.1502 0.0000  0.0076  -0.0064 88  HIS   A C   
587  O  O   . HIS   A 88  ? 0.1489 0.1773 0.1627 -0.0009 0.0009  -0.0294 88  HIS   A O   
588  C  CB  . HIS   A 88  ? 0.1344 0.1289 0.1642 -0.0236 0.0028  -0.0174 88  HIS   A CB  
589  C  CG  . HIS   A 88  ? 0.1519 0.1336 0.1570 0.0049  0.0059  -0.0180 88  HIS   A CG  
590  N  ND1 . HIS   A 88  ? 0.1520 0.1481 0.1690 -0.0065 -0.0209 -0.0134 88  HIS   A ND1 
591  C  CD2 . HIS   A 88  ? 0.1310 0.1590 0.1767 -0.0141 0.0186  -0.0056 88  HIS   A CD2 
592  C  CE1 . HIS   A 88  ? 0.1195 0.1586 0.1999 0.0004  -0.0095 0.0035  88  HIS   A CE1 
593  N  NE2 . HIS   A 88  ? 0.1539 0.1589 0.1791 0.0313  0.0034  0.0063  88  HIS   A NE2 
594  N  N   . GLU   A 89  ? 0.1427 0.1578 0.1462 0.0143  -0.0018 -0.0231 89  GLU   A N   
595  C  CA  . GLU   A 89  ? 0.1684 0.1739 0.1929 0.0256  -0.0158 -0.0030 89  GLU   A CA  
596  C  C   . GLU   A 89  ? 0.1465 0.1689 0.2014 0.0177  -0.0123 0.0144  89  GLU   A C   
597  O  O   . GLU   A 89  ? 0.1784 0.2764 0.2135 0.0224  -0.0163 0.0633  89  GLU   A O   
598  C  CB  . GLU   A 89  ? 0.1941 0.1884 0.1892 0.0120  -0.0338 -0.0319 89  GLU   A CB  
599  C  CG  . GLU   A 89  ? 0.2006 0.2006 0.2458 -0.0130 -0.0029 -0.0512 89  GLU   A CG  
600  C  CD  . GLU   A 89  ? 0.2518 0.2610 0.2407 0.0315  0.0352  -0.0761 89  GLU   A CD  
601  O  OE1 . GLU   A 89  ? 0.2630 0.4086 0.3149 0.0804  -0.0233 -0.0632 89  GLU   A OE1 
602  O  OE2 . GLU   A 89  ? 0.2272 0.3030 0.3251 0.0470  0.0330  -0.1335 89  GLU   A OE2 
603  N  N   . HIS   A 90  ? 0.1622 0.1382 0.1580 -0.0049 -0.0012 0.0076  90  HIS   A N   
604  C  CA  . HIS   A 90  ? 0.1539 0.1477 0.1402 -0.0221 0.0089  0.0021  90  HIS   A CA  
605  C  C   . HIS   A 90  ? 0.1725 0.1769 0.1321 0.0007  0.0021  0.0183  90  HIS   A C   
606  O  O   . HIS   A 90  ? 0.1704 0.1907 0.1304 0.0028  0.0053  0.0224  90  HIS   A O   
607  C  CB  . HIS   A 90  ? 0.1862 0.1664 0.1604 -0.0025 0.0189  0.0030  90  HIS   A CB  
608  C  CG  . HIS   A 90  ? 0.2052 0.1630 0.1891 -0.0069 0.0152  0.0302  90  HIS   A CG  
609  N  ND1 . HIS   A 90  ? 0.2716 0.2212 0.3794 -0.0457 -0.0638 -0.0201 90  HIS   A ND1 
610  C  CD2 . HIS   A 90  ? 0.2232 0.1744 0.2049 -0.0099 0.0062  -0.0001 90  HIS   A CD2 
611  C  CE1 . HIS   A 90  ? 0.2207 0.2084 0.2716 -0.0147 -0.0360 -0.0132 90  HIS   A CE1 
612  N  NE2 . HIS   A 90  ? 0.2469 0.2113 0.3525 -0.0602 -0.0282 -0.0086 90  HIS   A NE2 
613  N  N   . ALA   A 91  ? 0.1704 0.1635 0.1305 -0.0093 0.0131  0.0088  91  ALA   A N   
614  C  CA  . ALA   A 91  ? 0.1893 0.1851 0.1275 -0.0122 0.0206  0.0029  91  ALA   A CA  
615  C  C   . ALA   A 91  ? 0.1706 0.2324 0.1152 -0.0131 0.0223  0.0240  91  ALA   A C   
616  O  O   . ALA   A 91  ? 0.2045 0.2268 0.1395 -0.0200 -0.0060 0.0460  91  ALA   A O   
617  C  CB  . ALA   A 91  ? 0.1893 0.1654 0.1672 -0.0206 0.0181  0.0275  91  ALA   A CB  
618  N  N   . GLU   A 92  ? 0.1786 0.2502 0.1590 -0.0189 0.0092  0.0188  92  GLU   A N   
619  C  CA  . GLU   A 92  ? 0.1322 0.2679 0.1780 -0.0039 -0.0101 0.0364  92  GLU   A CA  
620  C  C   . GLU   A 92  ? 0.2013 0.2686 0.1450 0.0030  -0.0187 0.0583  92  GLU   A C   
621  O  O   . GLU   A 92  ? 0.2164 0.3135 0.1783 0.0054  0.0138  0.0783  92  GLU   A O   
622  C  CB  . GLU   A 92  ? 0.2474 0.2403 0.2201 0.0000  -0.0251 0.0461  92  GLU   A CB  
623  C  CG  . GLU   A 92  ? 0.2706 0.2093 0.2340 -0.0274 0.0190  -0.0352 92  GLU   A CG  
624  C  CD  . GLU   A 92  ? 0.2310 0.1350 0.2034 0.0336  -0.0138 -0.0366 92  GLU   A CD  
625  O  OE1 . GLU   A 92  ? 0.1751 0.1475 0.3094 -0.0034 -0.0675 -0.0343 92  GLU   A OE1 
626  O  OE2 . GLU   A 92  ? 0.1685 0.1692 0.1450 -0.0458 0.0435  0.0036  92  GLU   A OE2 
627  N  N   . VAL   A 93  ? 0.1612 0.2095 0.1404 -0.0347 -0.0048 0.0502  93  VAL   A N   
628  C  CA  . VAL   A 93  ? 0.1723 0.1721 0.1734 -0.0327 -0.0151 0.0145  93  VAL   A CA  
629  C  C   . VAL   A 93  ? 0.1404 0.1522 0.1854 -0.0323 -0.0114 0.0411  93  VAL   A C   
630  O  O   . VAL   A 93  ? 0.2128 0.1996 0.2120 -0.0467 -0.0732 0.0772  93  VAL   A O   
631  C  CB  . VAL   A 93  ? 0.2540 0.1617 0.1754 -0.0520 0.0011  0.0003  93  VAL   A CB  
632  C  CG1 . VAL   A 93  ? 0.2784 0.2661 0.2352 -0.0514 0.0138  0.0309  93  VAL   A CG1 
633  C  CG2 . VAL   A 93  ? 0.2815 0.1646 0.2320 -0.0650 -0.0065 -0.0004 93  VAL   A CG2 
634  N  N   . VAL   A 94  ? 0.1669 0.1209 0.1296 -0.0151 0.0015  0.0167  94  VAL   A N   
635  C  CA  . VAL   A 94  ? 0.1439 0.1218 0.1404 -0.0021 -0.0025 0.0130  94  VAL   A CA  
636  C  C   . VAL   A 94  ? 0.1460 0.1146 0.1319 0.0051  -0.0070 0.0095  94  VAL   A C   
637  O  O   . VAL   A 94  ? 0.1584 0.1126 0.1441 0.0195  0.0056  0.0039  94  VAL   A O   
638  C  CB  . VAL   A 94  ? 0.1411 0.1543 0.1507 -0.0077 -0.0077 -0.0047 94  VAL   A CB  
639  C  CG1 . VAL   A 94  ? 0.1699 0.1328 0.1718 0.0206  -0.0127 -0.0300 94  VAL   A CG1 
640  C  CG2 . VAL   A 94  ? 0.1710 0.2103 0.1661 0.0199  0.0016  -0.0040 94  VAL   A CG2 
641  N  N   . PHE   A 95  ? 0.1310 0.0980 0.1530 0.0081  0.0074  0.0118  95  PHE   A N   
642  C  CA  . PHE   A 95  ? 0.1486 0.0983 0.1379 0.0058  0.0147  0.0081  95  PHE   A CA  
643  C  C   . PHE   A 95  ? 0.1233 0.1033 0.1361 -0.0009 -0.0070 0.0135  95  PHE   A C   
644  O  O   . PHE   A 95  ? 0.1544 0.1026 0.1597 0.0097  -0.0123 0.0258  95  PHE   A O   
645  C  CB  . PHE   A 95  ? 0.1697 0.0977 0.1438 0.0182  0.0053  0.0085  95  PHE   A CB  
646  C  CG  . PHE   A 95  ? 0.1499 0.0842 0.1834 -0.0119 -0.0035 0.0066  95  PHE   A CG  
647  C  CD1 . PHE   A 95  ? 0.1548 0.1514 0.1878 0.0020  -0.0191 -0.0156 95  PHE   A CD1 
648  C  CD2 . PHE   A 95  ? 0.1796 0.1116 0.1613 -0.0119 0.0006  0.0252  95  PHE   A CD2 
649  C  CE1 . PHE   A 95  ? 0.1568 0.1949 0.2443 0.0239  -0.0166 -0.0375 95  PHE   A CE1 
650  C  CE2 . PHE   A 95  ? 0.2388 0.1315 0.1858 -0.0218 -0.0139 0.0266  95  PHE   A CE2 
651  C  CZ  . PHE   A 95  ? 0.2414 0.1207 0.2068 0.0037  -0.0548 -0.0103 95  PHE   A CZ  
652  N  N   . THR   A 96  ? 0.1505 0.1032 0.1338 0.0088  -0.0023 0.0188  96  THR   A N   
653  C  CA  . THR   A 96  ? 0.1572 0.1137 0.1445 0.0166  0.0142  0.0315  96  THR   A CA  
654  C  C   . THR   A 96  ? 0.1564 0.1017 0.1510 0.0165  0.0166  0.0222  96  THR   A C   
655  O  O   . THR   A 96  ? 0.2369 0.1139 0.1688 0.0400  0.0174  0.0293  96  THR   A O   
656  C  CB  . THR   A 96  ? 0.1531 0.1316 0.1785 0.0183  0.0138  0.0341  96  THR   A CB  
657  O  OG1 . THR   A 96  ? 0.1812 0.1730 0.1797 -0.0205 -0.0027 0.0062  96  THR   A OG1 
658  C  CG2 . THR   A 96  ? 0.1581 0.1557 0.2082 -0.0124 0.0069  0.0208  96  THR   A CG2 
659  N  N   . ALA   A 97  ? 0.1632 0.1087 0.1386 0.0079  0.0093  0.0251  97  ALA   A N   
660  C  CA  . ALA   A 97  ? 0.1570 0.0964 0.1531 0.0037  0.0064  0.0197  97  ALA   A CA  
661  C  C   . ALA   A 97  ? 0.1668 0.0976 0.1642 0.0000  0.0295  0.0341  97  ALA   A C   
662  O  O   . ALA   A 97  ? 0.1500 0.1014 0.1780 0.0022  0.0161  0.0307  97  ALA   A O   
663  C  CB  . ALA   A 97  ? 0.1521 0.1526 0.1451 0.0150  0.0137  0.0129  97  ALA   A CB  
664  N  N   . ASN   A 98  ? 0.1368 0.0900 0.1684 -0.0024 0.0159  0.0187  98  ASN   A N   
665  C  CA  . ASN   A 98  ? 0.1640 0.1015 0.1775 0.0022  0.0357  0.0108  98  ASN   A CA  
666  C  C   . ASN   A 98  ? 0.1379 0.1244 0.2151 -0.0148 0.0476  0.0175  98  ASN   A C   
667  O  O   . ASN   A 98  ? 0.1731 0.1616 0.2109 -0.0287 0.0356  0.0259  98  ASN   A O   
668  C  CB  . ASN   A 98  ? 0.1903 0.1381 0.1597 -0.0239 0.0307  0.0215  98  ASN   A CB  
669  C  CG  . ASN   A 98  ? 0.1607 0.1288 0.1573 0.0038  0.0247  0.0173  98  ASN   A CG  
670  O  OD1 . ASN   A 98  ? 0.1778 0.1643 0.1980 0.0167  0.0124  0.0367  98  ASN   A OD1 
671  N  ND2 . ASN   A 98  ? 0.1327 0.1181 0.1602 -0.0009 0.0180  0.0184  98  ASN   A ND2 
672  N  N   . ASP   A 99  ? 0.1480 0.1508 0.2145 -0.0036 0.0405  0.0313  99  ASP   A N   
673  C  CA  . ASP   A 99  ? 0.1389 0.1686 0.2247 -0.0124 0.0253  0.0434  99  ASP   A CA  
674  C  C   . ASP   A 99  ? 0.1429 0.2063 0.2344 0.0028  0.0021  0.0459  99  ASP   A C   
675  O  O   . ASP   A 99  ? 0.1397 0.2450 0.2328 0.0097  -0.0069 0.0063  99  ASP   A O   
676  C  CB  . ASP   A 99  ? 0.1561 0.2446 0.2403 0.0081  0.0304  0.0288  99  ASP   A CB  
677  C  CG  . ASP   A 99  ? 0.4928 0.3186 0.2608 -0.1273 -0.0192 0.0559  99  ASP   A CG  
678  O  OD1 . ASP   A 99  ? 0.2387 0.3502 0.2908 -0.0187 -0.0500 0.0074  99  ASP   A OD1 
679  O  OD2 . ASP   A 99  ? 0.3216 0.3494 0.3059 -0.0176 -0.0160 -0.0016 99  ASP   A OD2 
680  N  N   . SER   A 100 ? 0.1628 0.1969 0.3242 0.0308  0.0299  0.0472  100 SER   A N   
681  C  CA  . SER   A 100 ? 0.2153 0.1794 0.4078 0.0447  0.0481  0.0219  100 SER   A CA  
682  C  C   . SER   A 100 ? 0.1854 0.1992 0.3568 0.0205  0.0710  -0.0101 100 SER   A C   
683  O  O   . SER   A 100 ? 0.3744 0.2553 0.4468 0.0676  0.0869  -0.0400 100 SER   A O   
684  C  CB  . SER   A 100 ? 0.5142 0.4484 0.6578 0.4540  0.2881  0.2407  100 SER   A CB  
685  N  N   . GLY   A 101 ? 0.1787 0.1831 0.3353 0.0141  0.0574  -0.0031 101 GLY   A N   
686  C  CA  . GLY   A 101 ? 0.1911 0.1722 0.3350 -0.0068 0.0973  -0.0248 101 GLY   A CA  
687  C  C   . GLY   A 101 ? 0.1969 0.1466 0.2555 -0.0184 0.0755  0.0078  101 GLY   A C   
688  O  O   . GLY   A 101 ? 0.1977 0.1554 0.2471 -0.0099 0.0654  0.0087  101 GLY   A O   
689  N  N   . PRO   A 102 ? 0.2060 0.1644 0.2621 -0.0258 0.1102  0.0238  102 PRO   A N   
690  C  CA  . PRO   A 102 ? 0.1768 0.1235 0.2364 0.0045  0.0925  0.0207  102 PRO   A CA  
691  C  C   . PRO   A 102 ? 0.1897 0.1274 0.2406 -0.0092 0.0929  0.0085  102 PRO   A C   
692  O  O   . PRO   A 102 ? 0.1965 0.1325 0.2825 -0.0101 0.1083  -0.0072 102 PRO   A O   
693  C  CB  . PRO   A 102 ? 0.2168 0.1784 0.2548 -0.0052 0.0824  0.0039  102 PRO   A CB  
694  C  CG  . PRO   A 102 ? 0.3264 0.2724 0.2316 -0.0874 0.0651  0.0439  102 PRO   A CG  
695  C  CD  . PRO   A 102 ? 0.2184 0.2038 0.2355 -0.0547 0.0725  0.0168  102 PRO   A CD  
696  N  N   . ARG   A 103 ? 0.1868 0.1173 0.2342 0.0109  0.0849  0.0214  103 ARG   A N   
697  C  CA  . ARG   A 103 ? 0.1614 0.1318 0.2002 -0.0135 0.0673  -0.0022 103 ARG   A CA  
698  C  C   . ARG   A 103 ? 0.1589 0.1584 0.2133 0.0335  0.0603  0.0419  103 ARG   A C   
699  O  O   . ARG   A 103 ? 0.1564 0.1710 0.2231 0.0043  0.0305  0.0349  103 ARG   A O   
700  C  CB  . ARG   A 103 ? 0.1569 0.1477 0.2349 -0.0119 0.0578  0.0131  103 ARG   A CB  
701  C  CG  . ARG   A 103 ? 0.1681 0.1664 0.2626 0.0204  0.0408  0.0372  103 ARG   A CG  
702  C  CD  . ARG   A 103 ? 0.2149 0.1406 0.3033 0.0356  0.0243  0.0196  103 ARG   A CD  
703  N  NE  . ARG   A 103 ? 0.1917 0.2058 0.4319 0.0732  0.0361  0.0397  103 ARG   A NE  
704  C  CZ  . ARG   A 103 ? 0.1837 0.2655 0.4515 0.0780  0.0692  0.0240  103 ARG   A CZ  
705  N  NH1 . ARG   A 103 ? 0.2478 0.2001 0.4267 -0.0071 0.0297  0.0025  103 ARG   A NH1 
706  N  NH2 . ARG   A 103 ? 0.2426 0.2694 0.5712 0.1004  -0.0200 -0.0130 103 ARG   A NH2 
707  N  N   . ARG   A 104 ? 0.1744 0.1712 0.1898 -0.0120 0.0566  0.0083  104 ARG   A N   
708  C  CA  . ARG   A 104 ? 0.1722 0.1232 0.1875 -0.0123 0.0394  0.0176  104 ARG   A CA  
709  C  C   . ARG   A 104 ? 0.1643 0.1156 0.1698 0.0013  0.0279  0.0174  104 ARG   A C   
710  O  O   . ARG   A 104 ? 0.1953 0.1336 0.1829 0.0280  0.0459  0.0343  104 ARG   A O   
711  C  CB  . ARG   A 104 ? 0.1950 0.1887 0.2066 -0.0139 0.0428  0.0106  104 ARG   A CB  
712  C  CG  . ARG   A 104 ? 0.2770 0.3272 0.2063 0.0254  0.0745  -0.0036 104 ARG   A CG  
713  C  CD  . ARG   A 104 ? 0.4907 0.3476 0.2407 0.0056  0.0524  -0.0211 104 ARG   A CD  
714  N  N   . TYR   A 105 ? 0.1355 0.1131 0.1652 0.0079  0.0281  0.0284  105 TYR   A N   
715  C  CA  . TYR   A 105 ? 0.1290 0.1167 0.1372 -0.0017 0.0105  0.0303  105 TYR   A CA  
716  C  C   . TYR   A 105 ? 0.1306 0.1018 0.1456 0.0122  0.0224  0.0276  105 TYR   A C   
717  O  O   . TYR   A 105 ? 0.1383 0.1296 0.1939 -0.0011 0.0023  0.0554  105 TYR   A O   
718  C  CB  . TYR   A 105 ? 0.1374 0.1076 0.1601 0.0198  0.0344  0.0158  105 TYR   A CB  
719  C  CG  . TYR   A 105 ? 0.1372 0.0943 0.1558 0.0139  0.0306  0.0043  105 TYR   A CG  
720  C  CD1 . TYR   A 105 ? 0.1372 0.1182 0.1686 0.0032  0.0204  0.0368  105 TYR   A CD1 
721  C  CD2 . TYR   A 105 ? 0.1413 0.1104 0.1657 -0.0119 0.0220  0.0360  105 TYR   A CD2 
722  C  CE1 . TYR   A 105 ? 0.1594 0.1074 0.1735 -0.0018 0.0111  0.0284  105 TYR   A CE1 
723  C  CE2 . TYR   A 105 ? 0.1546 0.1074 0.1766 -0.0065 0.0190  0.0246  105 TYR   A CE2 
724  C  CZ  . TYR   A 105 ? 0.1406 0.0932 0.1809 0.0033  0.0210  0.0173  105 TYR   A CZ  
725  O  OH  . TYR   A 105 ? 0.1463 0.1039 0.2206 -0.0176 0.0177  0.0181  105 TYR   A OH  
726  N  N   . THR   A 106 ? 0.1297 0.1036 0.1561 0.0098  0.0159  0.0396  106 THR   A N   
727  C  CA  . THR   A 106 ? 0.1422 0.1051 0.1591 0.0016  0.0019  0.0155  106 THR   A CA  
728  C  C   . THR   A 106 ? 0.1159 0.1036 0.1575 -0.0029 0.0017  0.0392  106 THR   A C   
729  O  O   . THR   A 106 ? 0.1433 0.1384 0.1602 0.0395  0.0224  0.0416  106 THR   A O   
730  C  CB  . THR   A 106 ? 0.1744 0.1088 0.1892 0.0000  0.0021  0.0155  106 THR   A CB  
731  O  OG1 . THR   A 106 ? 0.2459 0.1409 0.1920 0.0062  0.0235  -0.0210 106 THR   A OG1 
732  C  CG2 . THR   A 106 ? 0.1859 0.1453 0.2218 -0.0259 -0.0260 0.0100  106 THR   A CG2 
733  N  N   . ILE   A 107 ? 0.1228 0.1191 0.1426 0.0092  0.0233  0.0434  107 ILE   A N   
734  C  CA  . ILE   A 107 ? 0.1002 0.1356 0.1513 0.0029  -0.0067 0.0122  107 ILE   A CA  
735  C  C   . ILE   A 107 ? 0.1064 0.1558 0.1466 -0.0014 0.0046  0.0469  107 ILE   A C   
736  O  O   . ILE   A 107 ? 0.1242 0.1486 0.1579 -0.0046 -0.0026 0.0392  107 ILE   A O   
737  C  CB  . ILE   A 107 ? 0.1275 0.1637 0.1657 0.0188  -0.0223 0.0062  107 ILE   A CB  
738  C  CG1 . ILE   A 107 ? 0.1542 0.1355 0.2131 0.0115  -0.0242 -0.0131 107 ILE   A CG1 
739  C  CG2 . ILE   A 107 ? 0.1687 0.2092 0.1751 0.0532  -0.0230 -0.0060 107 ILE   A CG2 
740  C  CD1 . ILE   A 107 ? 0.1695 0.1627 0.2412 -0.0103 -0.0193 0.0173  107 ILE   A CD1 
741  N  N   . ALA   A 108 ? 0.1076 0.1688 0.1390 -0.0149 -0.0032 0.0524  108 ALA   A N   
742  C  CA  . ALA   A 108 ? 0.1368 0.1874 0.1507 -0.0392 0.0001  0.0474  108 ALA   A CA  
743  C  C   . ALA   A 108 ? 0.1162 0.2166 0.1444 -0.0504 -0.0166 0.0714  108 ALA   A C   
744  O  O   . ALA   A 108 ? 0.1173 0.3669 0.1490 -0.0295 -0.0146 0.0797  108 ALA   A O   
745  C  CB  . ALA   A 108 ? 0.1855 0.2055 0.1903 -0.0672 -0.0026 0.0672  108 ALA   A CB  
746  N  N   . ALA   A 109 ? 0.1148 0.1899 0.1501 -0.0463 -0.0029 0.0501  109 ALA   A N   
747  C  CA  . ALA   A 109 ? 0.1046 0.1457 0.1569 -0.0161 -0.0108 0.0269  109 ALA   A CA  
748  C  C   . ALA   A 109 ? 0.0987 0.1566 0.1242 -0.0316 -0.0174 0.0265  109 ALA   A C   
749  O  O   . ALA   A 109 ? 0.1332 0.1995 0.1358 -0.0474 -0.0211 0.0421  109 ALA   A O   
750  C  CB  . ALA   A 109 ? 0.1170 0.1844 0.1788 -0.0273 -0.0063 0.0394  109 ALA   A CB  
751  N  N   . LEU   A 110 ? 0.1100 0.1308 0.1109 -0.0274 -0.0007 -0.0030 110 LEU   A N   
752  C  CA  . LEU   A 110 ? 0.0958 0.1003 0.1262 -0.0144 0.0070  -0.0056 110 LEU   A CA  
753  C  C   . LEU   A 110 ? 0.0991 0.0935 0.1162 -0.0214 -0.0056 -0.0095 110 LEU   A C   
754  O  O   . LEU   A 110 ? 0.1176 0.1247 0.1288 -0.0093 -0.0074 -0.0236 110 LEU   A O   
755  C  CB  . LEU   A 110 ? 0.1011 0.1271 0.1119 -0.0101 0.0064  -0.0053 110 LEU   A CB  
756  C  CG  . LEU   A 110 ? 0.1089 0.1138 0.1436 -0.0030 0.0219  -0.0035 110 LEU   A CG  
757  C  CD1 . LEU   A 110 ? 0.1296 0.0947 0.1427 -0.0307 0.0154  -0.0061 110 LEU   A CD1 
758  C  CD2 . LEU   A 110 ? 0.1516 0.1419 0.1553 0.0194  -0.0055 0.0102  110 LEU   A CD2 
759  N  N   . LEU   A 111 ? 0.0983 0.0910 0.1135 -0.0237 0.0017  -0.0070 111 LEU   A N   
760  C  CA  . LEU   A 111 ? 0.1028 0.1005 0.1254 -0.0078 -0.0015 -0.0185 111 LEU   A CA  
761  C  C   . LEU   A 111 ? 0.0970 0.1089 0.1079 -0.0083 -0.0062 0.0020  111 LEU   A C   
762  O  O   . LEU   A 111 ? 0.1158 0.1163 0.1245 -0.0171 -0.0012 -0.0074 111 LEU   A O   
763  C  CB  . LEU   A 111 ? 0.1207 0.1014 0.1337 -0.0043 -0.0080 -0.0074 111 LEU   A CB  
764  C  CG  . LEU   A 111 ? 0.1212 0.1070 0.1262 -0.0120 0.0180  -0.0093 111 LEU   A CG  
765  C  CD1 . LEU   A 111 ? 0.1565 0.1233 0.1295 0.0091  -0.0045 0.0072  111 LEU   A CD1 
766  C  CD2 . LEU   A 111 ? 0.1287 0.1087 0.1428 -0.0045 0.0135  0.0011  111 LEU   A CD2 
767  N  N   . SER   A 112 ? 0.1182 0.1200 0.1169 -0.0205 0.0129  -0.0150 112 SER   A N   
768  C  CA  . SER   A 112 ? 0.1309 0.1470 0.1034 -0.0157 0.0045  -0.0040 112 SER   A CA  
769  C  C   . SER   A 112 ? 0.0952 0.1682 0.1288 -0.0137 0.0253  -0.0190 112 SER   A C   
770  O  O   . SER   A 112 ? 0.1200 0.1230 0.1589 -0.0353 0.0174  -0.0134 112 SER   A O   
771  C  CB  . SER   A 112 ? 0.1578 0.1394 0.1250 -0.0198 0.0305  -0.0183 112 SER   A CB  
772  O  OG  . SER   A 112 ? 0.2308 0.1481 0.1452 0.0162  0.0365  -0.0045 112 SER   A OG  
773  N  N   . PRO   A 113 ? 0.1221 0.1342 0.1405 -0.0213 0.0099  -0.0217 113 PRO   A N   
774  C  CA  . PRO   A 113 ? 0.1066 0.1624 0.1583 -0.0131 0.0141  -0.0266 113 PRO   A CA  
775  C  C   . PRO   A 113 ? 0.1374 0.1720 0.1525 -0.0324 0.0285  -0.0115 113 PRO   A C   
776  O  O   . PRO   A 113 ? 0.1432 0.1512 0.1755 -0.0174 0.0218  -0.0271 113 PRO   A O   
777  C  CB  . PRO   A 113 ? 0.1201 0.1828 0.1988 0.0105  0.0081  -0.0405 113 PRO   A CB  
778  C  CG  . PRO   A 113 ? 0.1336 0.2333 0.1982 -0.0243 0.0244  -0.0710 113 PRO   A CG  
779  C  CD  . PRO   A 113 ? 0.1244 0.1705 0.1736 -0.0318 0.0190  -0.0255 113 PRO   A CD  
780  N  N   . TYR   A 114 ? 0.1118 0.1265 0.1532 -0.0085 0.0145  -0.0350 114 TYR   A N   
781  C  CA  . TYR   A 114 ? 0.1330 0.1627 0.1477 -0.0050 0.0058  -0.0197 114 TYR   A CA  
782  C  C   . TYR   A 114 ? 0.1244 0.1624 0.1708 0.0072  0.0037  -0.0610 114 TYR   A C   
783  O  O   . TYR   A 114 ? 0.1108 0.2111 0.1598 -0.0141 0.0091  -0.0389 114 TYR   A O   
784  C  CB  . TYR   A 114 ? 0.1261 0.1625 0.1649 -0.0151 0.0024  -0.0326 114 TYR   A CB  
785  C  CG  . TYR   A 114 ? 0.1242 0.1649 0.1483 -0.0192 0.0216  -0.0117 114 TYR   A CG  
786  C  CD1 . TYR   A 114 ? 0.1465 0.2314 0.1986 -0.0095 0.0225  -0.0556 114 TYR   A CD1 
787  C  CD2 . TYR   A 114 ? 0.1378 0.1696 0.1721 -0.0183 0.0163  -0.0127 114 TYR   A CD2 
788  C  CE1 . TYR   A 114 ? 0.1467 0.4307 0.1894 0.0074  0.0412  -0.0653 114 TYR   A CE1 
789  C  CE2 . TYR   A 114 ? 0.1566 0.1967 0.1845 -0.0077 0.0429  -0.0266 114 TYR   A CE2 
790  C  CZ  . TYR   A 114 ? 0.1581 0.2846 0.2215 0.0429  0.0144  -0.0263 114 TYR   A CZ  
791  O  OH  . TYR   A 114 ? 0.1695 0.4248 0.2640 0.0778  0.0528  -0.0558 114 TYR   A OH  
792  N  N   . SER   A 115 ? 0.1032 0.1690 0.1719 -0.0289 0.0095  -0.0437 115 SER   A N   
793  C  CA  . SER   A 115 ? 0.0989 0.1474 0.1776 -0.0210 -0.0013 -0.0515 115 SER   A CA  
794  C  C   . SER   A 115 ? 0.0978 0.1960 0.1578 0.0152  0.0005  -0.0546 115 SER   A C   
795  O  O   . SER   A 115 ? 0.1086 0.2646 0.1712 -0.0004 -0.0030 -0.0647 115 SER   A O   
796  C  CB  . SER   A 115 ? 0.1658 0.1723 0.1761 -0.0012 -0.0405 -0.0472 115 SER   A CB  
797  O  OG  . SER   A 115 ? 0.2776 0.1718 0.2443 0.0077  0.0097  -0.0197 115 SER   A OG  
798  N  N   . TYR   A 116 ? 0.0995 0.1579 0.1487 0.0050  0.0110  -0.0550 116 TYR   A N   
799  C  CA  . TYR   A 116 ? 0.0998 0.1671 0.1425 0.0102  -0.0124 -0.0411 116 TYR   A CA  
800  C  C   . TYR   A 116 ? 0.0953 0.1243 0.1350 -0.0073 -0.0107 -0.0207 116 TYR   A C   
801  O  O   . TYR   A 116 ? 0.1074 0.1358 0.1326 0.0098  -0.0077 -0.0263 116 TYR   A O   
802  C  CB  . TYR   A 116 ? 0.1315 0.2009 0.1441 0.0644  -0.0210 -0.0098 116 TYR   A CB  
803  C  CG  . TYR   A 116 ? 0.1438 0.1633 0.1209 0.0285  -0.0002 0.0058  116 TYR   A CG  
804  C  CD1 . TYR   A 116 ? 0.1516 0.1533 0.1681 0.0105  0.0138  0.0106  116 TYR   A CD1 
805  C  CD2 . TYR   A 116 ? 0.1680 0.1417 0.1870 0.0306  0.0156  0.0025  116 TYR   A CD2 
806  C  CE1 . TYR   A 116 ? 0.1520 0.1648 0.1803 0.0078  0.0233  0.0088  116 TYR   A CE1 
807  C  CE2 . TYR   A 116 ? 0.2146 0.1404 0.1852 0.0439  0.0030  -0.0105 116 TYR   A CE2 
808  C  CZ  . TYR   A 116 ? 0.1828 0.1441 0.1696 0.0234  0.0137  0.0038  116 TYR   A CZ  
809  O  OH  . TYR   A 116 ? 0.2803 0.1434 0.1863 0.0123  0.0111  -0.0058 116 TYR   A OH  
810  N  N   . SER   A 117 ? 0.1010 0.1420 0.1376 0.0012  -0.0065 -0.0405 117 SER   A N   
811  C  CA  . SER   A 117 ? 0.1091 0.1616 0.1381 0.0060  -0.0073 -0.0054 117 SER   A CA  
812  C  C   . SER   A 117 ? 0.0961 0.1337 0.1601 -0.0251 -0.0039 -0.0217 117 SER   A C   
813  O  O   . SER   A 117 ? 0.1085 0.1642 0.1381 -0.0271 -0.0071 -0.0119 117 SER   A O   
814  C  CB  . SER   A 117 ? 0.1252 0.1462 0.1754 0.0374  0.0216  -0.0031 117 SER   A CB  
815  O  OG  . SER   A 117 ? 0.1630 0.1877 0.1842 0.0402  0.0012  0.0099  117 SER   A OG  
816  N  N   . THR   A 118 ? 0.1155 0.1457 0.1390 0.0017  0.0166  -0.0275 118 THR   A N   
817  C  CA  A THR   A 118 ? 0.1101 0.1314 0.1959 0.0243  -0.0229 0.0065  118 THR   A CA  
818  C  CA  B THR   A 118 ? 0.1160 0.1301 0.1882 0.0204  -0.0023 -0.0064 118 THR   A CA  
819  C  C   . THR   A 118 ? 0.1086 0.1196 0.1657 -0.0064 0.0126  0.0151  118 THR   A C   
820  O  O   . THR   A 118 ? 0.1212 0.1692 0.1354 0.0190  0.0077  0.0190  118 THR   A O   
821  C  CB  A THR   A 118 ? 0.1340 0.1669 0.3003 -0.0239 -0.0294 -0.0018 118 THR   A CB  
822  C  CB  B THR   A 118 ? 0.1049 0.1653 0.2029 0.0605  -0.0444 -0.0097 118 THR   A CB  
823  O  OG1 A THR   A 118 ? 0.1898 0.1874 0.2403 0.0442  -0.0130 0.0516  118 THR   A OG1 
824  O  OG1 B THR   A 118 ? 0.0877 0.1342 0.2832 0.0433  -0.0242 -0.0126 118 THR   A OG1 
825  C  CG2 A THR   A 118 ? 0.2230 0.1550 0.4095 -0.0991 -0.1075 0.0790  118 THR   A CG2 
826  C  CG2 B THR   A 118 ? 0.0535 0.1081 0.2111 -0.0002 -0.0228 0.0318  118 THR   A CG2 
827  N  N   . THR   A 119 ? 0.1001 0.1514 0.1307 0.0020  -0.0023 0.0180  119 THR   A N   
828  C  CA  . THR   A 119 ? 0.1242 0.1227 0.1468 0.0069  0.0028  0.0250  119 THR   A CA  
829  C  C   . THR   A 119 ? 0.0979 0.1224 0.1347 -0.0016 -0.0036 0.0073  119 THR   A C   
830  O  O   . THR   A 119 ? 0.1084 0.1727 0.1636 -0.0122 -0.0021 0.0530  119 THR   A O   
831  C  CB  . THR   A 119 ? 0.1117 0.1063 0.1816 -0.0011 -0.0171 0.0238  119 THR   A CB  
832  O  OG1 . THR   A 119 ? 0.1397 0.1106 0.1718 0.0112  -0.0094 0.0187  119 THR   A OG1 
833  C  CG2 . THR   A 119 ? 0.1632 0.1270 0.1789 0.0031  -0.0003 0.0283  119 THR   A CG2 
834  N  N   . ALA   A 120 ? 0.1139 0.1209 0.1313 0.0040  0.0075  0.0188  120 ALA   A N   
835  C  CA  . ALA   A 120 ? 0.1263 0.1004 0.1470 0.0111  0.0125  0.0204  120 ALA   A CA  
836  C  C   . ALA   A 120 ? 0.1134 0.0943 0.1656 0.0187  0.0135  0.0221  120 ALA   A C   
837  O  O   . ALA   A 120 ? 0.1324 0.1216 0.1677 0.0218  0.0215  0.0286  120 ALA   A O   
838  C  CB  . ALA   A 120 ? 0.1457 0.1131 0.1831 -0.0135 0.0344  0.0070  120 ALA   A CB  
839  N  N   . VAL   A 121 ? 0.1342 0.0971 0.1478 0.0123  0.0324  0.0227  121 VAL   A N   
840  C  CA  . VAL   A 121 ? 0.1399 0.1066 0.1473 0.0072  0.0210  0.0289  121 VAL   A CA  
841  C  C   . VAL   A 121 ? 0.1309 0.1015 0.1570 0.0379  0.0399  0.0169  121 VAL   A C   
842  O  O   . VAL   A 121 ? 0.1516 0.1281 0.2100 0.0346  0.0297  0.0563  121 VAL   A O   
843  C  CB  . VAL   A 121 ? 0.1653 0.1105 0.1684 0.0227  0.0169  0.0091  121 VAL   A CB  
844  C  CG1 . VAL   A 121 ? 0.2290 0.1322 0.2219 0.0293  -0.0228 -0.0246 121 VAL   A CG1 
845  C  CG2 . VAL   A 121 ? 0.2503 0.1912 0.2105 -0.0808 -0.0223 -0.0023 121 VAL   A CG2 
846  N  N   . VAL   A 122 ? 0.1283 0.1043 0.1875 0.0240  0.0315  0.0268  122 VAL   A N   
847  C  CA  . VAL   A 122 ? 0.1652 0.0983 0.1776 0.0130  0.0390  0.0238  122 VAL   A CA  
848  C  C   . VAL   A 122 ? 0.2087 0.1069 0.2209 0.0255  0.0600  0.0403  122 VAL   A C   
849  O  O   . VAL   A 122 ? 0.1817 0.1285 0.2525 0.0291  0.0613  0.0316  122 VAL   A O   
850  C  CB  . VAL   A 122 ? 0.1889 0.1193 0.2416 0.0144  0.0238  0.0500  122 VAL   A CB  
851  C  CG1 . VAL   A 122 ? 0.2307 0.1367 0.2305 -0.0188 0.0376  0.0189  122 VAL   A CG1 
852  C  CG2 . VAL   A 122 ? 0.2157 0.1302 0.1971 0.0019  0.0287  0.0363  122 VAL   A CG2 
853  N  N   . THR   A 123 ? 0.1876 0.1203 0.1930 0.0372  0.0506  0.0080  123 THR   A N   
854  C  CA  . THR   A 123 ? 0.2431 0.1600 0.1846 0.0279  0.0764  0.0143  123 THR   A CA  
855  C  C   . THR   A 123 ? 0.2010 0.1776 0.2319 0.0537  0.0702  0.0221  123 THR   A C   
856  O  O   . THR   A 123 ? 0.2127 0.1703 0.2477 0.0488  0.0786  0.0278  123 THR   A O   
857  C  CB  . THR   A 123 ? 0.2653 0.2442 0.2703 0.0102  0.0573  -0.0103 123 THR   A CB  
858  O  OG1 . THR   A 123 ? 0.3606 0.3162 0.3602 0.0726  0.0171  -0.1093 123 THR   A OG1 
859  C  CG2 . THR   A 123 ? 0.3000 0.2934 0.3230 -0.1066 0.0504  -0.0598 123 THR   A CG2 
860  N  N   . ASN   A 124 ? 0.2892 0.1993 0.3297 0.0762  0.1381  0.0220  124 ASN   A N   
861  C  CA  . ASN   A 124 ? 0.2958 0.2154 0.2920 0.0382  0.1125  0.0545  124 ASN   A CA  
862  C  C   . ASN   A 124 ? 0.5940 0.5801 0.2882 -0.1862 0.0442  0.1357  124 ASN   A C   
863  O  O   . ASN   A 124 ? 0.4775 0.6945 0.2498 -0.0184 0.0338  0.0075  124 ASN   A O   
864  C  CB  . ASN   A 124 ? 0.2893 0.3089 0.4337 0.0661  0.1280  0.0659  124 ASN   A CB  
865  C  CG  . ASN   A 124 ? 0.3106 0.3276 0.4491 0.0688  0.0572  0.1040  124 ASN   A CG  
866  O  OD1 . ASN   A 124 ? 0.3563 0.3604 0.3796 0.0498  0.1001  0.0463  124 ASN   A OD1 
867  N  ND2 . ASN   A 124 ? 0.3828 0.3846 0.5326 0.0312  0.0351  0.0648  124 ASN   A ND2 
868  N  N   . PRO   B 11  ? 0.2708 0.4489 0.2357 -0.0471 0.0928  -0.1554 11  PRO   B N   
869  C  CA  . PRO   B 11  ? 0.3075 0.3279 0.2514 -0.0744 0.0814  -0.1094 11  PRO   B CA  
870  C  C   . PRO   B 11  ? 0.2754 0.2575 0.2443 0.0322  0.0227  -0.1381 11  PRO   B C   
871  O  O   . PRO   B 11  ? 0.2005 0.3399 0.2779 -0.0113 0.0216  -0.1416 11  PRO   B O   
872  C  CB  . PRO   B 11  ? 0.4491 0.4163 0.4948 -0.0053 -0.0021 -0.0461 11  PRO   B CB  
873  C  CG  . PRO   B 11  ? 0.3873 0.3269 0.5855 -0.0336 0.2176  -0.2147 11  PRO   B CG  
874  C  CD  . PRO   B 11  ? 0.3496 0.4355 0.3638 -0.1196 0.0674  -0.1591 11  PRO   B CD  
875  N  N   . LEU   B 12  ? 0.2123 0.3066 0.2399 0.0303  0.0236  -0.1155 12  LEU   B N   
876  C  CA  . LEU   B 12  ? 0.1985 0.2687 0.2353 0.0123  0.0249  -0.0834 12  LEU   B CA  
877  C  C   . LEU   B 12  ? 0.1543 0.2771 0.2031 -0.0060 0.0169  -0.1002 12  LEU   B C   
878  O  O   . LEU   B 12  ? 0.2376 0.3581 0.2634 0.0328  -0.0234 -0.1550 12  LEU   B O   
879  C  CB  . LEU   B 12  ? 0.1896 0.2994 0.2485 0.0071  0.0209  -0.0527 12  LEU   B CB  
880  C  CG  . LEU   B 12  ? 0.1891 0.2617 0.2534 0.0015  0.0309  -0.0124 12  LEU   B CG  
881  C  CD1 . LEU   B 12  ? 0.2908 0.2833 0.2190 -0.0144 0.0055  -0.0161 12  LEU   B CD1 
882  C  CD2 . LEU   B 12  ? 0.1799 0.2584 0.3872 0.0217  -0.0223 -0.0294 12  LEU   B CD2 
883  N  N   . MET   B 13  ? 0.2160 0.2512 0.1798 0.0153  0.0255  -0.0892 13  MET   B N   
884  C  CA  . MET   B 13  ? 0.2278 0.2154 0.1674 -0.0084 0.0217  -0.0851 13  MET   B CA  
885  C  C   . MET   B 13  ? 0.1718 0.2084 0.1463 0.0105  -0.0077 -0.0588 13  MET   B C   
886  O  O   . MET   B 13  ? 0.1440 0.2364 0.1502 -0.0169 0.0123  -0.0527 13  MET   B O   
887  C  CB  . MET   B 13  ? 0.3450 0.2798 0.1922 0.0443  0.1036  -0.0165 13  MET   B CB  
888  C  CG  . MET   B 13  ? 0.4179 0.2873 0.2067 -0.0535 0.0345  -0.0411 13  MET   B CG  
889  S  SD  . MET   B 13  ? 0.3655 0.3604 0.2724 -0.0193 0.0244  -0.0498 13  MET   B SD  
890  C  CE  . MET   B 13  ? 0.3290 0.4625 0.3400 -0.0649 0.0234  0.1289  13  MET   B CE  
891  N  N   . VAL   B 14  ? 0.1702 0.1908 0.1378 0.0301  -0.0293 -0.0574 14  VAL   B N   
892  C  CA  . VAL   B 14  ? 0.1780 0.2073 0.1455 0.0307  -0.0310 -0.0497 14  VAL   B CA  
893  C  C   . VAL   B 14  ? 0.1605 0.2284 0.1378 0.0451  -0.0165 -0.0301 14  VAL   B C   
894  O  O   . VAL   B 14  ? 0.2098 0.2528 0.1784 0.0815  -0.0466 -0.0536 14  VAL   B O   
895  C  CB  . VAL   B 14  ? 0.1459 0.2248 0.1658 0.0157  -0.0167 -0.0442 14  VAL   B CB  
896  C  CG1 . VAL   B 14  ? 0.1784 0.2335 0.1771 0.0181  -0.0003 -0.0374 14  VAL   B CG1 
897  C  CG2 . VAL   B 14  ? 0.1525 0.2159 0.1766 -0.0260 0.0110  -0.0523 14  VAL   B CG2 
898  N  N   . LYS   B 15  ? 0.1682 0.2049 0.1586 0.0273  -0.0046 -0.0508 15  LYS   B N   
899  C  CA  . LYS   B 15  ? 0.1711 0.2352 0.1446 0.0298  -0.0074 -0.0251 15  LYS   B CA  
900  C  C   . LYS   B 15  ? 0.1777 0.2536 0.1551 0.0647  -0.0378 -0.0341 15  LYS   B C   
901  O  O   . LYS   B 15  ? 0.1679 0.2749 0.1485 0.0770  -0.0139 -0.0448 15  LYS   B O   
902  C  CB  . LYS   B 15  ? 0.2583 0.2252 0.1833 0.0436  0.0385  -0.0187 15  LYS   B CB  
903  C  CG  . LYS   B 15  ? 0.2812 0.2656 0.2930 0.0327  0.0610  -0.0190 15  LYS   B CG  
904  C  CD  . LYS   B 15  ? 0.4618 0.2426 0.3965 -0.0298 0.1056  -0.0610 15  LYS   B CD  
905  C  CE  . LYS   B 15  ? 0.3499 0.3710 0.3666 0.0500  0.0444  -0.0457 15  LYS   B CE  
906  N  NZ  . LYS   B 15  ? 0.4674 0.5482 0.5320 0.1646  -0.0108 -0.1586 15  LYS   B NZ  
907  N  N   . VAL   B 16  ? 0.1710 0.2198 0.1159 0.0445  -0.0264 -0.0196 16  VAL   B N   
908  C  CA  . VAL   B 16  ? 0.1623 0.2436 0.1246 0.0749  -0.0062 -0.0141 16  VAL   B CA  
909  C  C   . VAL   B 16  ? 0.1463 0.2205 0.1158 0.0647  -0.0177 0.0011  16  VAL   B C   
910  O  O   . VAL   B 16  ? 0.1652 0.2174 0.1336 0.0543  -0.0119 -0.0186 16  VAL   B O   
911  C  CB  . VAL   B 16  ? 0.1389 0.2372 0.1453 0.0742  -0.0204 -0.0112 16  VAL   B CB  
912  C  CG1 . VAL   B 16  ? 0.2127 0.1933 0.1673 0.0484  0.0029  -0.0040 16  VAL   B CG1 
913  C  CG2 . VAL   B 16  ? 0.2014 0.2267 0.1666 0.0778  -0.0189 -0.0321 16  VAL   B CG2 
914  N  N   . LEU   B 17  ? 0.1608 0.2020 0.1284 0.0800  -0.0099 -0.0159 17  LEU   B N   
915  C  CA  . LEU   B 17  ? 0.1332 0.1887 0.1308 0.0272  -0.0136 0.0034  17  LEU   B CA  
916  C  C   . LEU   B 17  ? 0.1437 0.1314 0.1487 0.0356  -0.0012 -0.0024 17  LEU   B C   
917  O  O   . LEU   B 17  ? 0.1381 0.1780 0.1441 0.0444  -0.0157 0.0065  17  LEU   B O   
918  C  CB  . LEU   B 17  ? 0.1414 0.1954 0.1445 0.0133  -0.0044 -0.0208 17  LEU   B CB  
919  C  CG  . LEU   B 17  ? 0.1488 0.2662 0.1684 0.0346  0.0027  -0.0085 17  LEU   B CG  
920  C  CD1 . LEU   B 17  ? 0.1746 0.3913 0.2817 -0.0321 0.0301  -0.0331 17  LEU   B CD1 
921  C  CD2 . LEU   B 17  ? 0.2039 0.3083 0.1768 -0.0159 0.0108  0.0299  17  LEU   B CD2 
922  N  N   . ASP   B 18  ? 0.1347 0.1479 0.1245 0.0330  -0.0041 0.0000  18  ASP   B N   
923  C  CA  . ASP   B 18  ? 0.1029 0.1449 0.1488 0.0280  0.0040  -0.0037 18  ASP   B CA  
924  C  C   . ASP   B 18  ? 0.1169 0.1463 0.1344 0.0135  0.0017  0.0109  18  ASP   B C   
925  O  O   . ASP   B 18  ? 0.1432 0.1526 0.1416 0.0204  -0.0058 0.0161  18  ASP   B O   
926  C  CB  . ASP   B 18  ? 0.1214 0.1411 0.1658 0.0176  -0.0093 0.0082  18  ASP   B CB  
927  C  CG  . ASP   B 18  ? 0.1012 0.1576 0.1710 0.0126  -0.0128 0.0066  18  ASP   B CG  
928  O  OD1 . ASP   B 18  ? 0.1375 0.1500 0.1720 0.0125  0.0190  0.0046  18  ASP   B OD1 
929  O  OD2 . ASP   B 18  ? 0.1187 0.1940 0.2213 0.0037  0.0031  0.0034  18  ASP   B OD2 
930  N  N   . ALA   B 19  ? 0.1297 0.1328 0.1354 0.0254  0.0047  0.0237  19  ALA   B N   
931  C  CA  . ALA   B 19  ? 0.1351 0.1246 0.1535 0.0027  0.0104  0.0090  19  ALA   B CA  
932  C  C   . ALA   B 19  ? 0.1581 0.1355 0.1263 0.0095  0.0145  -0.0009 19  ALA   B C   
933  O  O   . ALA   B 19  ? 0.1992 0.1301 0.1535 0.0117  -0.0002 0.0076  19  ALA   B O   
934  C  CB  . ALA   B 19  ? 0.1353 0.1476 0.1475 0.0046  0.0085  -0.0189 19  ALA   B CB  
935  N  N   . VAL   B 20  ? 0.1421 0.1462 0.1480 0.0262  0.0302  0.0123  20  VAL   B N   
936  C  CA  . VAL   B 20  ? 0.1514 0.1320 0.1494 0.0401  0.0323  0.0252  20  VAL   B CA  
937  C  C   . VAL   B 20  ? 0.1351 0.1540 0.1854 0.0335  0.0456  0.0251  20  VAL   B C   
938  O  O   . VAL   B 20  ? 0.2046 0.1542 0.2324 0.0625  0.0512  0.0406  20  VAL   B O   
939  C  CB  . VAL   B 20  ? 0.1713 0.1756 0.1650 0.0629  0.0679  0.0127  20  VAL   B CB  
940  C  CG1 . VAL   B 20  ? 0.2152 0.2118 0.2572 0.0645  0.0975  0.0530  20  VAL   B CG1 
941  C  CG2 . VAL   B 20  ? 0.2173 0.1926 0.1825 0.0323  0.0195  0.0225  20  VAL   B CG2 
942  N  N   . ARG   B 21  ? 0.1496 0.1648 0.1862 0.0271  0.0286  0.0323  21  ARG   B N   
943  C  CA  . ARG   B 21  ? 0.1646 0.2198 0.1940 0.0264  -0.0115 0.0632  21  ARG   B CA  
944  C  C   . ARG   B 21  ? 0.1599 0.1877 0.1817 0.0490  -0.0098 0.0459  21  ARG   B C   
945  O  O   . ARG   B 21  ? 0.1919 0.2228 0.2165 0.0517  -0.0085 0.0709  21  ARG   B O   
946  C  CB  . ARG   B 21  ? 0.1827 0.3205 0.2355 -0.0427 -0.0675 0.0970  21  ARG   B CB  
947  N  N   . GLY   B 22  ? 0.1501 0.1459 0.1815 0.0102  -0.0113 0.0171  22  GLY   B N   
948  C  CA  . GLY   B 22  ? 0.1617 0.1636 0.1867 -0.0114 -0.0073 0.0073  22  GLY   B CA  
949  C  C   . GLY   B 22  ? 0.1464 0.1895 0.1864 0.0007  -0.0132 0.0128  22  GLY   B C   
950  O  O   . GLY   B 22  ? 0.1597 0.1993 0.1964 -0.0080 0.0187  0.0279  22  GLY   B O   
951  N  N   . SER   B 23  ? 0.2169 0.1997 0.1407 0.0135  -0.0082 0.0190  23  SER   B N   
952  C  CA  . SER   B 23  ? 0.1878 0.1884 0.1505 0.0032  -0.0071 0.0158  23  SER   B CA  
953  C  C   . SER   B 23  ? 0.1687 0.1742 0.1433 -0.0026 -0.0130 -0.0118 23  SER   B C   
954  O  O   . SER   B 23  ? 0.1920 0.2008 0.1415 -0.0033 -0.0258 0.0140  23  SER   B O   
955  C  CB  . SER   B 23  ? 0.1908 0.1882 0.2312 0.0321  -0.0363 0.0153  23  SER   B CB  
956  O  OG  . SER   B 23  ? 0.1820 0.2808 0.2485 -0.0135 -0.0267 -0.0010 23  SER   B OG  
957  N  N   . PRO   B 24  ? 0.1881 0.1679 0.1385 -0.0001 -0.0276 0.0102  24  PRO   B N   
958  C  CA  . PRO   B 24  ? 0.1274 0.1935 0.1681 0.0405  -0.0139 -0.0182 24  PRO   B CA  
959  C  C   . PRO   B 24  ? 0.1315 0.2008 0.1773 0.0388  0.0019  0.0114  24  PRO   B C   
960  O  O   . PRO   B 24  ? 0.1442 0.1794 0.2167 0.0277  -0.0060 0.0203  24  PRO   B O   
961  C  CB  . PRO   B 24  ? 0.2152 0.1938 0.1535 -0.0023 0.0273  0.0128  24  PRO   B CB  
962  C  CG  . PRO   B 24  ? 0.5501 0.2773 0.1729 0.1290  0.0172  0.0207  24  PRO   B CG  
963  C  CD  . PRO   B 24  ? 0.1945 0.2107 0.1682 0.0212  -0.0098 0.0244  24  PRO   B CD  
964  N  N   . ALA   B 25  ? 0.1344 0.1805 0.1641 0.0310  0.0032  0.0013  25  ALA   B N   
965  C  CA  . ALA   B 25  ? 0.1605 0.1815 0.1522 0.0221  0.0074  0.0011  25  ALA   B CA  
966  C  C   . ALA   B 25  ? 0.1241 0.1781 0.1661 0.0196  0.0131  0.0134  25  ALA   B C   
967  O  O   . ALA   B 25  ? 0.1474 0.1898 0.1798 0.0403  -0.0209 -0.0300 25  ALA   B O   
968  C  CB  . ALA   B 25  ? 0.2016 0.1829 0.1471 0.0233  -0.0006 -0.0290 25  ALA   B CB  
969  N  N   . ILE   B 26  ? 0.1483 0.1975 0.1675 0.0479  0.0105  -0.0032 26  ILE   B N   
970  C  CA  . ILE   B 26  ? 0.1639 0.2373 0.1757 0.0340  -0.0041 0.0021  26  ILE   B CA  
971  C  C   . ILE   B 26  ? 0.1504 0.2532 0.1893 0.0139  -0.0219 -0.0060 26  ILE   B C   
972  O  O   . ILE   B 26  ? 0.1949 0.2071 0.2247 -0.0099 -0.0068 -0.0076 26  ILE   B O   
973  C  CB  . ILE   B 26  ? 0.2092 0.2966 0.2259 0.0387  -0.0206 0.0307  26  ILE   B CB  
974  C  CG1 . ILE   B 26  ? 0.2583 0.2741 0.2053 0.0322  -0.0269 0.0491  26  ILE   B CG1 
975  C  CG2 . ILE   B 26  ? 0.2654 0.2770 0.2939 0.0360  -0.0324 0.0288  26  ILE   B CG2 
976  C  CD1 . ILE   B 26  ? 0.2940 0.4357 0.3018 0.0901  -0.0764 0.0069  26  ILE   B CD1 
977  N  N   . ASN   B 27  ? 0.1676 0.2322 0.1940 0.0272  -0.0062 -0.0057 27  ASN   B N   
978  C  CA  A ASN   B 27  ? 0.1634 0.2327 0.2103 0.0135  -0.0231 -0.0305 27  ASN   B CA  
979  C  CA  B ASN   B 27  ? 0.1934 0.2323 0.2155 0.0081  -0.0102 -0.0332 27  ASN   B CA  
980  C  C   . ASN   B 27  ? 0.1675 0.1962 0.2201 -0.0134 -0.0227 -0.0266 27  ASN   B C   
981  O  O   . ASN   B 27  ? 0.1887 0.2857 0.2542 -0.0319 0.0033  -0.0092 27  ASN   B O   
982  C  CB  A ASN   B 27  ? 0.1755 0.2486 0.2459 0.0311  -0.0542 -0.0322 27  ASN   B CB  
983  C  CB  B ASN   B 27  ? 0.2102 0.2312 0.2876 0.0033  -0.0183 -0.0515 27  ASN   B CB  
984  C  CG  A ASN   B 27  ? 0.2198 0.2715 0.2684 0.0138  -0.0608 -0.0389 27  ASN   B CG  
985  C  CG  B ASN   B 27  ? 0.2366 0.3347 0.2900 0.0112  -0.0096 -0.0082 27  ASN   B CG  
986  O  OD1 A ASN   B 27  ? 0.2599 0.3054 0.3277 0.0057  -0.0348 -0.0659 27  ASN   B OD1 
987  O  OD1 B ASN   B 27  ? 0.2131 0.3939 0.2640 -0.0597 -0.0486 -0.0689 27  ASN   B OD1 
988  N  ND2 A ASN   B 27  ? 0.2778 0.3511 0.4027 -0.0250 -0.0285 -0.0364 27  ASN   B ND2 
989  N  ND2 B ASN   B 27  ? 0.2692 0.3365 0.3530 0.0449  -0.0153 -0.0088 27  ASN   B ND2 
990  N  N   . VAL   B 28  ? 0.1941 0.1893 0.1852 0.0167  -0.0100 -0.0265 28  VAL   B N   
991  C  CA  . VAL   B 28  ? 0.1717 0.1977 0.1622 0.0056  0.0016  -0.0310 28  VAL   B CA  
992  C  C   . VAL   B 28  ? 0.1580 0.1877 0.1693 -0.0035 0.0004  -0.0367 28  VAL   B C   
993  O  O   . VAL   B 28  ? 0.1823 0.1841 0.1609 0.0072  0.0113  -0.0283 28  VAL   B O   
994  C  CB  . VAL   B 28  ? 0.2244 0.1773 0.1739 0.0158  -0.0166 -0.0428 28  VAL   B CB  
995  C  CG1 . VAL   B 28  ? 0.2434 0.1915 0.2176 0.0325  -0.0479 -0.0728 28  VAL   B CG1 
996  C  CG2 . VAL   B 28  ? 0.2365 0.2035 0.1746 0.0195  0.0154  -0.0374 28  VAL   B CG2 
997  N  N   . ALA   B 29  ? 0.1575 0.1991 0.1689 0.0040  0.0232  -0.0402 29  ALA   B N   
998  C  CA  . ALA   B 29  ? 0.1713 0.1851 0.2115 0.0042  0.0058  -0.0622 29  ALA   B CA  
999  C  C   . ALA   B 29  ? 0.1731 0.1769 0.1797 -0.0334 -0.0160 -0.0408 29  ALA   B C   
1000 O  O   . ALA   B 29  ? 0.1845 0.1979 0.1791 0.0292  -0.0137 -0.0482 29  ALA   B O   
1001 C  CB  . ALA   B 29  ? 0.1927 0.1968 0.2426 -0.0325 -0.0247 -0.0288 29  ALA   B CB  
1002 N  N   . VAL   B 30  ? 0.1772 0.1946 0.1608 0.0054  -0.0144 -0.0477 30  VAL   B N   
1003 C  CA  . VAL   B 30  ? 0.1789 0.1818 0.1565 0.0106  -0.0343 -0.0324 30  VAL   B CA  
1004 C  C   . VAL   B 30  ? 0.1764 0.1959 0.1650 -0.0038 -0.0134 -0.0274 30  VAL   B C   
1005 O  O   . VAL   B 30  ? 0.2014 0.2598 0.1850 0.0536  -0.0259 -0.0907 30  VAL   B O   
1006 C  CB  . VAL   B 30  ? 0.2041 0.2112 0.1570 0.0087  0.0088  -0.0482 30  VAL   B CB  
1007 C  CG1 . VAL   B 30  ? 0.2062 0.2374 0.2012 0.0254  -0.0096 -0.0468 30  VAL   B CG1 
1008 C  CG2 . VAL   B 30  ? 0.1633 0.2289 0.1843 0.0072  -0.0172 -0.0538 30  VAL   B CG2 
1009 N  N   . HIS   B 31  ? 0.1869 0.2342 0.1563 0.0283  -0.0114 -0.0253 31  HIS   B N   
1010 C  CA  . HIS   B 31  ? 0.1705 0.2103 0.1945 0.0329  0.0015  -0.0192 31  HIS   B CA  
1011 C  C   . HIS   B 31  ? 0.1851 0.2242 0.1812 0.0071  0.0011  -0.0435 31  HIS   B C   
1012 O  O   . HIS   B 31  ? 0.1764 0.2505 0.2160 0.0323  -0.0141 -0.0659 31  HIS   B O   
1013 C  CB  . HIS   B 31  ? 0.1794 0.2673 0.2747 0.0297  -0.0109 0.0105  31  HIS   B CB  
1014 C  CG  . HIS   B 31  ? 0.2062 0.2916 0.3974 -0.0123 -0.0244 0.0148  31  HIS   B CG  
1015 N  ND1 . HIS   B 31  ? 0.2390 0.3428 0.3458 -0.0418 -0.0688 -0.0243 31  HIS   B ND1 
1016 C  CD2 . HIS   B 31  ? 0.2169 0.1848 0.5921 -0.0272 -0.1012 -0.0775 31  HIS   B CD2 
1017 C  CE1 . HIS   B 31  ? 0.1927 0.2877 0.4110 -0.0668 0.0055  -0.1177 31  HIS   B CE1 
1018 N  NE2 . HIS   B 31  ? 0.2073 0.3131 0.5198 -0.0081 0.0017  -0.0927 31  HIS   B NE2 
1019 N  N   . VAL   B 32  ? 0.1524 0.2550 0.1859 0.0080  -0.0107 -0.0641 32  VAL   B N   
1020 C  CA  . VAL   B 32  ? 0.1478 0.2107 0.1812 0.0115  0.0040  -0.0740 32  VAL   B CA  
1021 C  C   . VAL   B 32  ? 0.1898 0.2016 0.1832 0.0261  -0.0155 -0.0803 32  VAL   B C   
1022 O  O   . VAL   B 32  ? 0.2006 0.2229 0.2462 -0.0027 -0.0055 -0.0933 32  VAL   B O   
1023 C  CB  . VAL   B 32  ? 0.1433 0.2459 0.1781 -0.0088 0.0025  -0.0804 32  VAL   B CB  
1024 C  CG1 . VAL   B 32  ? 0.1578 0.2473 0.1768 -0.0258 0.0082  -0.0679 32  VAL   B CG1 
1025 C  CG2 . VAL   B 32  ? 0.1729 0.2667 0.2030 -0.0115 -0.0160 -0.0583 32  VAL   B CG2 
1026 N  N   . PHE   B 33  ? 0.1872 0.1744 0.2330 0.0056  -0.0348 -0.0633 33  PHE   B N   
1027 C  CA  . PHE   B 33  ? 0.2139 0.2120 0.2643 -0.0234 -0.0703 -0.0757 33  PHE   B CA  
1028 C  C   . PHE   B 33  ? 0.2036 0.1813 0.2456 0.0022  -0.0473 -0.0692 33  PHE   B C   
1029 O  O   . PHE   B 33  ? 0.1680 0.1911 0.2408 0.0185  -0.0378 -0.0796 33  PHE   B O   
1030 C  CB  . PHE   B 33  ? 0.2064 0.2318 0.2628 0.0237  -0.0494 -0.0236 33  PHE   B CB  
1031 C  CG  . PHE   B 33  ? 0.1925 0.2483 0.3097 0.0017  -0.0411 -0.0088 33  PHE   B CG  
1032 C  CD1 . PHE   B 33  ? 0.2145 0.3144 0.3706 0.0571  -0.0022 0.0312  33  PHE   B CD1 
1033 C  CD2 . PHE   B 33  ? 0.1981 0.3304 0.3984 -0.0141 -0.0093 -0.0638 33  PHE   B CD2 
1034 C  CE1 . PHE   B 33  ? 0.2316 0.2794 0.3722 0.0773  0.0059  0.0582  33  PHE   B CE1 
1035 C  CE2 . PHE   B 33  ? 0.1981 0.3308 0.4727 -0.0042 -0.0874 0.0108  33  PHE   B CE2 
1036 C  CZ  . PHE   B 33  ? 0.2443 0.3139 0.4149 0.0033  0.0534  0.0648  33  PHE   B CZ  
1037 N  N   . ARG   B 34  ? 0.1830 0.1887 0.2944 -0.0126 -0.0275 -0.1045 34  ARG   B N   
1038 C  CA  . ARG   B 34  ? 0.1673 0.2190 0.3035 0.0116  0.0064  -0.0739 34  ARG   B CA  
1039 C  C   . ARG   B 34  ? 0.3023 0.1822 0.3277 0.0272  -0.0383 -0.1050 34  ARG   B C   
1040 O  O   . ARG   B 34  ? 0.2907 0.2150 0.3926 0.0178  -0.0481 -0.0862 34  ARG   B O   
1041 C  CB  . ARG   B 34  ? 0.2213 0.2540 0.2721 0.0138  -0.0244 -0.0780 34  ARG   B CB  
1042 C  CG  . ARG   B 34  ? 0.2351 0.2304 0.3502 0.0338  0.0266  -0.0447 34  ARG   B CG  
1043 C  CD  . ARG   B 34  ? 0.3209 0.3778 0.3475 0.0292  -0.0091 -0.0861 34  ARG   B CD  
1044 N  NE  . ARG   B 34  ? 0.3227 0.3779 0.3337 0.0534  0.0452  -0.0697 34  ARG   B NE  
1045 N  N   . LYS   B 35  ? 0.2460 0.2042 0.2950 0.0281  -0.0501 -0.0776 35  LYS   B N   
1046 C  CA  . LYS   B 35  ? 0.2543 0.2408 0.3135 0.0596  -0.0422 -0.0620 35  LYS   B CA  
1047 C  C   . LYS   B 35  ? 0.2782 0.2253 0.2605 0.0180  0.0095  -0.0524 35  LYS   B C   
1048 O  O   . LYS   B 35  ? 0.2862 0.2269 0.3543 0.0181  0.0612  -0.0815 35  LYS   B O   
1049 C  CB  . LYS   B 35  ? 0.3095 0.2273 0.2853 0.0254  -0.0108 -0.0555 35  LYS   B CB  
1050 C  CG  . LYS   B 35  ? 0.2700 0.3195 0.3354 0.0423  -0.0525 -0.0276 35  LYS   B CG  
1051 C  CD  . LYS   B 35  ? 0.3361 0.3540 0.4624 0.0189  -0.1657 -0.0888 35  LYS   B CD  
1052 N  N   . ALA   B 36  ? 0.3710 0.2254 0.4073 0.0451  0.0215  -0.0624 36  ALA   B N   
1053 C  CA  . ALA   B 36  ? 0.3821 0.2495 0.3701 0.0501  0.0609  -0.0302 36  ALA   B CA  
1054 C  C   . ALA   B 36  ? 0.3854 0.2626 0.3824 0.1087  0.0221  -0.0314 36  ALA   B C   
1055 O  O   . ALA   B 36  ? 0.3877 0.2986 0.4138 0.0575  0.0268  -0.0550 36  ALA   B O   
1056 C  CB  . ALA   B 36  ? 0.3833 0.2481 0.3743 0.0102  0.1301  0.0195  36  ALA   B CB  
1057 N  N   . ALA   B 37  ? 0.4650 0.2981 0.4962 0.1463  0.0210  -0.0520 37  ALA   B N   
1058 C  CA  . ALA   B 37  ? 0.4144 0.4343 0.3378 0.1044  0.0868  -0.0172 37  ALA   B CA  
1059 C  C   . ALA   B 37  ? 0.4557 0.3903 0.3670 0.0953  0.0584  0.0088  37  ALA   B C   
1060 O  O   . ALA   B 37  ? 0.5071 0.5605 0.4367 0.1794  -0.0129 -0.0693 37  ALA   B O   
1061 C  CB  . ALA   B 37  ? 0.3785 0.3107 0.5184 -0.0113 0.1156  -0.0228 37  ALA   B CB  
1062 N  N   . ASP   B 38  ? 0.4903 0.2296 0.4713 0.0901  0.0246  -0.0314 38  ASP   B N   
1063 C  CA  . ASP   B 38  ? 0.4543 0.4697 0.4514 0.0392  0.0304  -0.0287 38  ASP   B CA  
1064 C  C   . ASP   B 38  ? 0.3904 0.3275 0.4665 0.0727  0.0924  0.0752  38  ASP   B C   
1065 O  O   . ASP   B 38  ? 0.5431 0.4378 0.3863 0.0334  0.1224  0.0348  38  ASP   B O   
1066 C  CB  . ASP   B 38  ? 0.5700 0.3136 0.5708 0.0638  -0.0115 -0.0062 38  ASP   B CB  
1067 C  CG  . ASP   B 38  ? 0.5016 0.4249 0.5714 -0.1254 -0.0379 0.0750  38  ASP   B CG  
1068 O  OD1 . ASP   B 38  ? 0.6285 0.2987 0.5684 -0.0209 -0.0581 0.0116  38  ASP   B OD1 
1069 O  OD2 . ASP   B 38  ? 0.6287 0.3677 0.6052 -0.1081 -0.0230 -0.0155 38  ASP   B OD2 
1070 N  N   . ASP   B 39  ? 0.4617 0.3071 0.3766 0.0295  0.0901  -0.0136 39  ASP   B N   
1071 C  CA  . ASP   B 39  ? 0.4577 0.3776 0.3828 0.0242  0.0078  -0.1172 39  ASP   B CA  
1072 C  C   . ASP   B 39  ? 0.5078 0.4249 0.3807 0.0952  0.0050  -0.0443 39  ASP   B C   
1073 O  O   . ASP   B 39  ? 0.4906 0.3444 0.5719 0.0136  0.0825  -0.0612 39  ASP   B O   
1074 C  CB  . ASP   B 39  ? 0.5250 0.4576 0.4248 0.0981  -0.0316 0.0117  39  ASP   B CB  
1075 N  N   . THR   B 40  ? 0.4346 0.3469 0.4073 0.1030  0.0952  -0.0186 40  THR   B N   
1076 C  CA  . THR   B 40  ? 0.4587 0.4135 0.4348 0.0387  0.0057  0.0679  40  THR   B CA  
1077 C  C   . THR   B 40  ? 0.3532 0.2506 0.4400 0.0160  0.0747  -0.0056 40  THR   B C   
1078 O  O   . THR   B 40  ? 0.3864 0.2485 0.3956 -0.0266 0.0873  -0.0220 40  THR   B O   
1079 C  CB  . THR   B 40  ? 0.3335 0.5044 0.5235 0.0768  0.0218  -0.0617 40  THR   B CB  
1080 O  OG1 . THR   B 40  ? 0.5990 0.3153 0.4973 -0.1158 -0.0046 0.0410  40  THR   B OG1 
1081 N  N   . TRP   B 41  ? 0.3995 0.3806 0.4768 -0.0101 -0.0940 -0.0779 41  TRP   B N   
1082 C  CA  . TRP   B 41  ? 0.3749 0.2534 0.4081 -0.0385 -0.0251 -0.0822 41  TRP   B CA  
1083 C  C   . TRP   B 41  ? 0.3303 0.3174 0.4104 -0.0549 -0.0548 0.0615  41  TRP   B C   
1084 O  O   . TRP   B 41  ? 0.4199 0.5343 0.7491 -0.1311 -0.1818 -0.0961 41  TRP   B O   
1085 C  CB  . TRP   B 41  ? 0.3735 0.3736 0.3143 -0.0171 -0.0084 -0.0942 41  TRP   B CB  
1086 C  CG  . TRP   B 41  ? 0.3271 0.3489 0.3023 -0.0351 0.0088  -0.0503 41  TRP   B CG  
1087 C  CD1 . TRP   B 41  ? 0.2583 0.5102 0.3083 -0.0738 0.0189  -0.0826 41  TRP   B CD1 
1088 C  CD2 . TRP   B 41  ? 0.2348 0.3652 0.3261 -0.0101 -0.0382 -0.0031 41  TRP   B CD2 
1089 N  NE1 . TRP   B 41  ? 0.3853 0.4262 0.3209 -0.0895 -0.0582 -0.0457 41  TRP   B NE1 
1090 C  CE2 . TRP   B 41  ? 0.2803 0.3420 0.3340 0.0020  -0.0019 -0.0466 41  TRP   B CE2 
1091 C  CE3 . TRP   B 41  ? 0.1969 0.2222 0.3894 -0.0109 0.0464  -0.0014 41  TRP   B CE3 
1092 C  CZ2 . TRP   B 41  ? 0.2467 0.4247 0.3527 -0.0426 -0.1003 -0.0069 41  TRP   B CZ2 
1093 C  CZ3 . TRP   B 41  ? 0.2452 0.2186 0.3350 0.0415  -0.0299 -0.0278 41  TRP   B CZ3 
1094 C  CH2 . TRP   B 41  ? 0.2874 0.2736 0.3463 0.0528  -0.0735 -0.0425 41  TRP   B CH2 
1095 N  N   . GLU   B 42  ? 0.3254 0.3233 0.3761 -0.0670 -0.0516 -0.0500 42  GLU   B N   
1096 C  CA  . GLU   B 42  ? 0.3545 0.3321 0.3438 -0.0602 -0.0366 -0.0367 42  GLU   B CA  
1097 C  C   . GLU   B 42  ? 0.3091 0.3319 0.3778 -0.0602 -0.1119 -0.0335 42  GLU   B C   
1098 O  O   . GLU   B 42  ? 0.2730 0.2500 0.3903 -0.0287 0.0000  -0.1385 42  GLU   B O   
1099 C  CB  . GLU   B 42  ? 0.2908 0.3040 0.4082 0.0245  -0.0100 0.0119  42  GLU   B CB  
1100 N  N   . PRO   B 43  ? 0.2793 0.3600 0.4078 -0.1051 -0.0596 -0.0294 43  PRO   B N   
1101 C  CA  . PRO   B 43  ? 0.3034 0.3834 0.2918 -0.1231 -0.0543 -0.0472 43  PRO   B CA  
1102 C  C   . PRO   B 43  ? 0.2816 0.3221 0.3460 0.0041  -0.0375 -0.0368 43  PRO   B C   
1103 O  O   . PRO   B 43  ? 0.3412 0.2576 0.3977 -0.0275 -0.0062 -0.1034 43  PRO   B O   
1104 C  CB  . PRO   B 43  ? 0.2937 0.4255 0.2677 -0.1008 -0.0717 0.0184  43  PRO   B CB  
1105 C  CG  . PRO   B 43  ? 0.3135 0.4810 0.3774 -0.2007 -0.1275 0.1048  43  PRO   B CG  
1106 C  CD  . PRO   B 43  ? 0.3491 0.4500 0.5621 -0.1629 -0.2173 0.1322  43  PRO   B CD  
1107 N  N   . PHE   B 44  ? 0.1676 0.2566 0.3066 0.0293  -0.0237 -0.0609 44  PHE   B N   
1108 C  CA  . PHE   B 44  ? 0.1687 0.2704 0.3030 0.0168  -0.0123 -0.1113 44  PHE   B CA  
1109 C  C   . PHE   B 44  ? 0.1932 0.2825 0.2504 -0.0208 0.0338  -0.1189 44  PHE   B C   
1110 O  O   . PHE   B 44  ? 0.2499 0.3108 0.2548 0.0092  0.0003  -0.1079 44  PHE   B O   
1111 C  CB  . PHE   B 44  ? 0.1615 0.2958 0.2758 0.0003  -0.0198 -0.1158 44  PHE   B CB  
1112 C  CG  . PHE   B 44  ? 0.1394 0.3111 0.2589 0.0155  -0.0098 -0.1035 44  PHE   B CG  
1113 C  CD1 . PHE   B 44  ? 0.2144 0.3344 0.2758 0.0292  -0.0057 -0.1110 44  PHE   B CD1 
1114 C  CD2 . PHE   B 44  ? 0.1982 0.3508 0.1595 -0.0020 0.0060  -0.0814 44  PHE   B CD2 
1115 C  CE1 . PHE   B 44  ? 0.1929 0.4171 0.4039 0.0210  0.0497  -0.0998 44  PHE   B CE1 
1116 C  CE2 . PHE   B 44  ? 0.3189 0.2108 0.3165 -0.0245 0.0218  -0.1004 44  PHE   B CE2 
1117 C  CZ  . PHE   B 44  ? 0.2789 0.5088 0.1100 -0.0383 0.0317  -0.1032 44  PHE   B CZ  
1118 N  N   . ALA   B 45  ? 0.2256 0.2612 0.1531 0.0390  0.0048  -0.0613 45  ALA   B N   
1119 C  CA  . ALA   B 45  ? 0.2412 0.1439 0.3844 0.0168  -0.0345 -0.1331 45  ALA   B CA  
1120 C  C   . ALA   B 45  ? 0.1868 0.2468 0.2277 0.0573  -0.0469 -0.1027 45  ALA   B C   
1121 O  O   . ALA   B 45  ? 0.1700 0.3708 0.2241 0.0298  -0.0425 -0.1085 45  ALA   B O   
1122 C  CB  . ALA   B 45  ? 0.1596 0.2776 0.2774 0.0093  -0.0128 -0.1009 45  ALA   B CB  
1123 N  N   . SER   B 46  ? 0.1840 0.2822 0.2048 0.0096  -0.0355 -0.0930 46  SER   B N   
1124 C  CA  . SER   B 46  ? 0.1646 0.2233 0.2124 -0.0279 -0.0225 -0.0748 46  SER   B CA  
1125 C  C   . SER   B 46  ? 0.1781 0.2150 0.1720 -0.0259 -0.0180 -0.0721 46  SER   B C   
1126 O  O   . SER   B 46  ? 0.2650 0.2478 0.1832 -0.0318 -0.0081 -0.0773 46  SER   B O   
1127 C  CB  . SER   B 46  ? 0.2137 0.2025 0.2422 0.0120  -0.0329 -0.0930 46  SER   B CB  
1128 O  OG  . SER   B 46  ? 0.2028 0.1982 0.2635 -0.0167 -0.0329 -0.1072 46  SER   B OG  
1129 N  N   . GLY   B 47  ? 0.2097 0.2094 0.2050 -0.0329 -0.0250 -0.0605 47  GLY   B N   
1130 C  CA  . GLY   B 47  ? 0.2050 0.2144 0.2029 -0.0275 -0.0313 -0.0488 47  GLY   B CA  
1131 C  C   . GLY   B 47  ? 0.2098 0.1907 0.1857 -0.0208 -0.0180 -0.0669 47  GLY   B C   
1132 O  O   . GLY   B 47  ? 0.2100 0.2406 0.1779 0.0030  -0.0186 -0.0531 47  GLY   B O   
1133 N  N   . LYS   B 48  ? 0.2926 0.1971 0.1708 -0.0026 -0.0434 -0.0620 48  LYS   B N   
1134 C  CA  . LYS   B 48  ? 0.3082 0.2411 0.1765 0.0163  -0.0373 -0.0636 48  LYS   B CA  
1135 C  C   . LYS   B 48  ? 0.2391 0.2232 0.1562 0.0061  -0.0037 -0.0472 48  LYS   B C   
1136 O  O   . LYS   B 48  ? 0.2604 0.2184 0.1918 0.0152  -0.0126 -0.0502 48  LYS   B O   
1137 C  CB  . LYS   B 48  ? 0.2661 0.2570 0.4479 -0.0502 0.0863  -0.0516 48  LYS   B CB  
1138 N  N   . THR   B 49  ? 0.1873 0.2046 0.1607 0.0065  -0.0223 -0.0288 49  THR   B N   
1139 C  CA  . THR   B 49  ? 0.1643 0.2080 0.1556 0.0248  -0.0015 -0.0193 49  THR   B CA  
1140 C  C   . THR   B 49  ? 0.1496 0.2384 0.1875 0.0169  -0.0064 -0.0475 49  THR   B C   
1141 O  O   . THR   B 49  ? 0.1832 0.2422 0.1675 -0.0031 -0.0217 -0.0309 49  THR   B O   
1142 C  CB  . THR   B 49  ? 0.1422 0.2169 0.1654 0.0375  -0.0127 -0.0385 49  THR   B CB  
1143 O  OG1 . THR   B 49  ? 0.1440 0.1890 0.1932 0.0320  -0.0105 -0.0556 49  THR   B OG1 
1144 C  CG2 . THR   B 49  ? 0.1626 0.1719 0.1677 0.0251  -0.0108 -0.0256 49  THR   B CG2 
1145 N  N   . SER   B 50  ? 0.1567 0.2262 0.1777 0.0187  -0.0240 -0.0207 50  SER   B N   
1146 C  CA  . SER   B 50  ? 0.1876 0.2632 0.1709 0.0357  -0.0152 -0.0278 50  SER   B CA  
1147 C  C   . SER   B 50  ? 0.2116 0.2284 0.1617 0.0015  -0.0165 -0.0042 50  SER   B C   
1148 O  O   . SER   B 50  ? 0.2057 0.2328 0.1650 0.0226  -0.0114 0.0017  50  SER   B O   
1149 C  CB  . SER   B 50  ? 0.1901 0.2779 0.1791 0.0000  -0.0134 -0.0016 50  SER   B CB  
1150 O  OG  . SER   B 50  ? 0.2523 0.2703 0.2071 0.0140  -0.0157 0.0027  50  SER   B OG  
1151 N  N   . GLU   B 51  ? 0.2302 0.2584 0.1822 0.0275  -0.0526 0.0081  51  GLU   B N   
1152 C  CA  . GLU   B 51  ? 0.2362 0.2517 0.2419 0.0427  -0.0402 0.0332  51  GLU   B CA  
1153 C  C   . GLU   B 51  ? 0.2048 0.2740 0.1712 0.0333  0.0120  0.0119  51  GLU   B C   
1154 O  O   . GLU   B 51  ? 0.2646 0.2852 0.2423 0.0484  0.0053  -0.0303 51  GLU   B O   
1155 C  CB  . GLU   B 51  ? 0.3688 0.3680 0.3582 0.1011  -0.1731 0.0188  51  GLU   B CB  
1156 N  N   . SER   B 52  ? 0.2510 0.2812 0.1557 0.0174  -0.0226 -0.0069 52  SER   B N   
1157 C  CA  . SER   B 52  ? 0.2495 0.2274 0.1754 0.0196  0.0082  -0.0063 52  SER   B CA  
1158 C  C   . SER   B 52  ? 0.2193 0.2517 0.1928 -0.0076 -0.0075 -0.0061 52  SER   B C   
1159 O  O   . SER   B 52  ? 0.2455 0.2668 0.1807 -0.0095 0.0302  0.0092  52  SER   B O   
1160 C  CB  . SER   B 52  ? 0.2626 0.3168 0.2097 -0.0337 -0.0050 0.0667  52  SER   B CB  
1161 O  OG  . SER   B 52  ? 0.3042 0.4040 0.2172 0.0241  0.0295  -0.0103 52  SER   B OG  
1162 N  N   . GLY   B 53  ? 0.2052 0.2517 0.1366 -0.0054 -0.0159 -0.0233 53  GLY   B N   
1163 C  CA  . GLY   B 53  ? 0.1585 0.2491 0.1445 -0.0020 -0.0193 -0.0049 53  GLY   B CA  
1164 C  C   . GLY   B 53  ? 0.1953 0.2227 0.1223 0.0074  -0.0318 -0.0038 53  GLY   B C   
1165 O  O   . GLY   B 53  ? 0.1895 0.2424 0.1480 0.0215  -0.0223 -0.0310 53  GLY   B O   
1166 N  N   . GLU   B 54  ? 0.1880 0.3539 0.1290 0.0217  -0.0121 0.0018  54  GLU   B N   
1167 C  CA  . GLU   B 54  ? 0.2177 0.2748 0.1548 0.0409  -0.0149 -0.0356 54  GLU   B CA  
1168 C  C   . GLU   B 54  ? 0.1658 0.2854 0.1394 0.0368  -0.0104 -0.0201 54  GLU   B C   
1169 O  O   . GLU   B 54  ? 0.1700 0.3738 0.1714 0.0291  -0.0174 -0.0508 54  GLU   B O   
1170 C  CB  . GLU   B 54  ? 0.2758 0.3037 0.2171 0.0601  0.0793  0.0044  54  GLU   B CB  
1171 C  CG  . GLU   B 54  ? 0.2385 0.3647 0.2674 0.0513  -0.0118 -0.0059 54  GLU   B CG  
1172 C  CD  . GLU   B 54  ? 0.3928 0.2811 0.4062 -0.0744 0.0370  -0.0390 54  GLU   B CD  
1173 O  OE1 . GLU   B 54  ? 0.5371 0.5008 0.3993 -0.1559 0.1630  -0.0573 54  GLU   B OE1 
1174 O  OE2 . GLU   B 54  ? 0.4222 0.3127 0.5303 -0.0653 -0.0228 0.0396  54  GLU   B OE2 
1175 N  N   . LEU   B 55  ? 0.1997 0.2518 0.1680 0.0228  -0.0170 -0.0361 55  LEU   B N   
1176 C  CA  . LEU   B 55  ? 0.1620 0.2736 0.1465 0.0014  -0.0078 -0.0380 55  LEU   B CA  
1177 C  C   . LEU   B 55  ? 0.2001 0.3286 0.2089 0.0076  -0.0102 -0.0666 55  LEU   B C   
1178 O  O   . LEU   B 55  ? 0.2408 0.2861 0.2467 0.0294  -0.0188 -0.0680 55  LEU   B O   
1179 C  CB  . LEU   B 55  ? 0.2022 0.2492 0.1871 0.0036  0.0108  -0.0669 55  LEU   B CB  
1180 C  CG  . LEU   B 55  ? 0.2060 0.2738 0.1744 0.0239  0.0057  -0.0299 55  LEU   B CG  
1181 C  CD1 . LEU   B 55  ? 0.2517 0.2763 0.2171 -0.0271 0.0042  -0.0871 55  LEU   B CD1 
1182 C  CD2 . LEU   B 55  ? 0.2703 0.2169 0.2048 0.0253  0.0375  -0.0156 55  LEU   B CD2 
1183 N  N   . HIS   B 56  ? 0.2779 0.3487 0.1965 -0.0121 0.0613  -0.1176 56  HIS   B N   
1184 C  CA  . HIS   B 56  ? 0.2758 0.4591 0.2696 -0.0507 0.0939  -0.1322 56  HIS   B CA  
1185 C  C   . HIS   B 56  ? 0.3397 0.3666 0.2161 -0.0090 0.0993  -0.0941 56  HIS   B C   
1186 O  O   . HIS   B 56  ? 0.3326 0.3451 0.2815 -0.0047 0.0469  -0.0850 56  HIS   B O   
1187 C  CB  . HIS   B 56  ? 0.3768 0.6517 0.2799 0.0645  0.1923  -0.1387 56  HIS   B CB  
1188 C  CG  . HIS   B 56  ? 0.4541 0.5902 0.4034 -0.0176 0.0337  0.1551  56  HIS   B CG  
1189 N  ND1 . HIS   B 56  ? 0.4762 0.5475 0.8634 -0.1455 0.2601  0.0912  56  HIS   B ND1 
1190 C  CD2 . HIS   B 56  ? 0.4704 0.3435 0.6684 -0.0065 0.0851  0.1354  56  HIS   B CD2 
1191 C  CE1 . HIS   B 56  ? 0.6235 0.3947 0.6350 -0.0299 0.3039  -0.0518 56  HIS   B CE1 
1192 N  NE2 . HIS   B 56  ? 0.5976 0.4584 0.6675 0.0705  0.1446  0.1048  56  HIS   B NE2 
1193 N  N   . GLY   B 57  ? 0.3684 0.3715 0.2506 0.0336  0.0674  -0.1125 57  GLY   B N   
1194 C  CA  . GLY   B 57  ? 0.3219 0.3763 0.2591 0.0292  0.0320  -0.1306 57  GLY   B CA  
1195 C  C   . GLY   B 57  ? 0.2689 0.3431 0.2689 0.0212  -0.0001 -0.1137 57  GLY   B C   
1196 O  O   . GLY   B 57  ? 0.3769 0.3463 0.2987 0.0209  -0.0506 -0.1320 57  GLY   B O   
1197 N  N   . LEU   B 58  ? 0.1902 0.3299 0.2674 0.0117  -0.0099 -0.1221 58  LEU   B N   
1198 C  CA  . LEU   B 58  ? 0.2428 0.3234 0.2868 0.0351  0.0065  -0.1401 58  LEU   B CA  
1199 C  C   . LEU   B 58  ? 0.2470 0.2832 0.2231 0.0153  0.0130  -0.0351 58  LEU   B C   
1200 O  O   . LEU   B 58  ? 0.2785 0.3034 0.3081 -0.0189 0.0411  -0.0747 58  LEU   B O   
1201 C  CB  . LEU   B 58  ? 0.1917 0.2790 0.2653 0.0378  -0.0222 -0.0790 58  LEU   B CB  
1202 C  CG  . LEU   B 58  ? 0.2365 0.2608 0.2641 0.0671  -0.0365 -0.0608 58  LEU   B CG  
1203 C  CD1 . LEU   B 58  ? 0.2981 0.3218 0.2833 0.0448  -0.0090 -0.1474 58  LEU   B CD1 
1204 C  CD2 . LEU   B 58  ? 0.2895 0.2592 0.3961 0.0725  0.0203  -0.0343 58  LEU   B CD2 
1205 N  N   . THR   B 59  ? 0.2057 0.3409 0.2823 0.0156  -0.0123 -0.1331 59  THR   B N   
1206 C  CA  . THR   B 59  ? 0.2412 0.3489 0.2500 -0.0085 -0.0053 -0.1417 59  THR   B CA  
1207 C  C   . THR   B 59  ? 0.2372 0.2331 0.2681 0.0205  -0.0396 -0.0705 59  THR   B C   
1208 O  O   . THR   B 59  ? 0.2980 0.3522 0.2287 0.0361  0.0396  -0.0751 59  THR   B O   
1209 C  CB  . THR   B 59  ? 0.2407 0.3140 0.2690 0.0356  0.0121  -0.1142 59  THR   B CB  
1210 O  OG1 . THR   B 59  ? 0.3556 0.3774 0.2610 0.0578  -0.0445 -0.1338 59  THR   B OG1 
1211 C  CG2 . THR   B 59  ? 0.2379 0.3708 0.2631 0.0172  -0.0761 -0.1200 59  THR   B CG2 
1212 N  N   . THR   B 60  ? 0.2740 0.4063 0.3143 0.0749  0.0444  -0.1026 60  THR   B N   
1213 C  CA  . THR   B 60  ? 0.1585 0.4390 0.3538 0.0339  0.0060  -0.1483 60  THR   B CA  
1214 C  C   . THR   B 60  ? 0.2302 0.2968 0.2646 0.0321  0.0256  -0.0925 60  THR   B C   
1215 O  O   . THR   B 60  ? 0.2482 0.2716 0.2578 0.0510  0.0104  -0.1003 60  THR   B O   
1216 C  CB  . THR   B 60  ? 0.2788 0.4902 0.2864 -0.0489 -0.0149 -0.1195 60  THR   B CB  
1217 O  OG1 . THR   B 60  ? 0.3423 0.4290 0.3683 -0.0276 0.0038  -0.2194 60  THR   B OG1 
1218 C  CG2 . THR   B 60  ? 0.3487 0.5115 0.3345 0.0585  -0.1121 -0.0520 60  THR   B CG2 
1219 N  N   . GLU   B 61  ? 0.2026 0.3672 0.2882 0.0294  0.0361  -0.1114 61  GLU   B N   
1220 C  CA  . GLU   B 61  ? 0.1904 0.2590 0.3210 0.0209  0.0142  -0.0546 61  GLU   B CA  
1221 C  C   . GLU   B 61  ? 0.1949 0.3081 0.2973 0.0357  0.0129  -0.1033 61  GLU   B C   
1222 O  O   . GLU   B 61  ? 0.2854 0.2486 0.2745 0.0165  -0.0389 -0.0996 61  GLU   B O   
1223 C  CB  . GLU   B 61  ? 0.2462 0.3434 0.3691 0.0159  0.0235  -0.0213 61  GLU   B CB  
1224 N  N   . GLU   B 62  ? 0.2316 0.3352 0.2826 0.0523  0.0010  -0.1537 62  GLU   B N   
1225 C  CA  . GLU   B 62  ? 0.2132 0.3033 0.3393 0.0212  0.0427  -0.1300 62  GLU   B CA  
1226 C  C   . GLU   B 62  ? 0.1842 0.1598 0.3419 0.0297  0.0067  -0.1106 62  GLU   B C   
1227 O  O   . GLU   B 62  ? 0.2104 0.2129 0.4739 0.0377  0.0559  -0.0582 62  GLU   B O   
1228 C  CB  . GLU   B 62  ? 0.3895 0.2729 0.3564 0.0441  -0.0472 -0.1231 62  GLU   B CB  
1229 N  N   . GLU   B 63  ? 0.1807 0.2845 0.3241 0.0311  0.0124  -0.1496 63  GLU   B N   
1230 C  CA  . GLU   B 63  ? 0.2204 0.2505 0.3445 -0.0137 0.0259  -0.1705 63  GLU   B CA  
1231 C  C   . GLU   B 63  ? 0.1678 0.2958 0.2963 -0.0004 0.0458  -0.1093 63  GLU   B C   
1232 O  O   . GLU   B 63  ? 0.2490 0.2774 0.3634 -0.0316 0.0810  -0.1087 63  GLU   B O   
1233 C  CB  . GLU   B 63  ? 0.2182 0.4798 0.3020 -0.0119 -0.0504 -0.1717 63  GLU   B CB  
1234 N  N   . PHE   B 64  ? 0.1746 0.3185 0.2846 0.0169  -0.0041 -0.1042 64  PHE   B N   
1235 C  CA  . PHE   B 64  ? 0.1930 0.2733 0.2470 0.0267  -0.0278 -0.0772 64  PHE   B CA  
1236 C  C   . PHE   B 64  ? 0.1775 0.2434 0.2441 0.0221  0.0468  -0.0419 64  PHE   B C   
1237 O  O   . PHE   B 64  ? 0.1801 0.3148 0.3655 0.0006  0.0065  -0.0180 64  PHE   B O   
1238 C  CB  . PHE   B 64  ? 0.2192 0.2773 0.1984 0.0238  -0.0511 -0.0541 64  PHE   B CB  
1239 C  CG  . PHE   B 64  ? 0.2158 0.2878 0.2326 0.0271  -0.0107 -0.0534 64  PHE   B CG  
1240 C  CD1 . PHE   B 64  ? 0.2143 0.2788 0.2301 0.0129  -0.0297 -0.1034 64  PHE   B CD1 
1241 C  CD2 . PHE   B 64  ? 0.5076 0.3543 0.3090 -0.0834 0.0875  -0.0746 64  PHE   B CD2 
1242 C  CE1 . PHE   B 64  ? 0.2440 0.3333 0.2490 0.0439  -0.0579 -0.1002 64  PHE   B CE1 
1243 C  CE2 . PHE   B 64  ? 0.4552 0.2999 0.3180 -0.0147 0.0021  -0.1150 64  PHE   B CE2 
1244 C  CZ  . PHE   B 64  ? 0.3717 0.2727 0.2243 0.0424  -0.0129 -0.1000 64  PHE   B CZ  
1245 N  N   . VAL   B 65  ? 0.1647 0.2487 0.2529 0.0139  0.0097  -0.1110 65  VAL   B N   
1246 C  CA  . VAL   B 65  ? 0.1710 0.2476 0.2467 0.0246  0.0125  -0.1333 65  VAL   B CA  
1247 C  C   . VAL   B 65  ? 0.1938 0.3054 0.2067 0.0708  -0.0043 -0.0860 65  VAL   B C   
1248 O  O   . VAL   B 65  ? 0.1958 0.2663 0.2514 0.0555  0.0267  -0.1071 65  VAL   B O   
1249 C  CB  . VAL   B 65  ? 0.1934 0.2933 0.2977 0.0077  0.0163  -0.1401 65  VAL   B CB  
1250 C  CG1 . VAL   B 65  ? 0.2153 0.2756 0.3310 0.0807  -0.0198 -0.1141 65  VAL   B CG1 
1251 C  CG2 . VAL   B 65  ? 0.2364 0.2748 0.4436 -0.0176 0.0442  -0.1004 65  VAL   B CG2 
1252 N  N   . GLU   B 66  ? 0.2062 0.3873 0.2366 0.0616  0.0204  -0.1533 66  GLU   B N   
1253 C  CA  . GLU   B 66  ? 0.2395 0.3236 0.2351 0.0458  0.0010  -0.0857 66  GLU   B CA  
1254 C  C   . GLU   B 66  ? 0.2632 0.3689 0.2193 0.0902  -0.0100 -0.0867 66  GLU   B C   
1255 O  O   . GLU   B 66  ? 0.2740 0.3589 0.2968 0.0875  -0.0021 -0.0843 66  GLU   B O   
1256 C  CB  . GLU   B 66  ? 0.2067 0.2886 0.2824 0.0173  0.0220  -0.0992 66  GLU   B CB  
1257 C  CG  . GLU   B 66  ? 0.1972 0.3212 0.2897 0.0327  0.0477  -0.0681 66  GLU   B CG  
1258 C  CD  . GLU   B 66  ? 0.2127 0.2799 0.3725 0.0248  -0.0395 -0.1299 66  GLU   B CD  
1259 O  OE1 . GLU   B 66  ? 0.2274 0.3268 0.2896 0.0393  0.0056  -0.1229 66  GLU   B OE1 
1260 O  OE2 . GLU   B 66  ? 0.3634 0.3005 0.3965 -0.0352 -0.0126 -0.1404 66  GLU   B OE2 
1261 N  N   . GLY   B 67  ? 0.2745 0.3057 0.2404 0.0928  0.0338  -0.0808 67  GLY   B N   
1262 C  CA  . GLY   B 67  ? 0.3477 0.2794 0.2784 0.1113  0.0178  -0.0454 67  GLY   B CA  
1263 C  C   . GLY   B 67  ? 0.2187 0.2456 0.2637 0.0430  -0.0080 -0.0599 67  GLY   B C   
1264 O  O   . GLY   B 67  ? 0.2098 0.2668 0.2387 0.0203  0.0281  -0.0817 67  GLY   B O   
1265 N  N   . ILE   B 68  ? 0.2142 0.1924 0.2566 0.0831  -0.0196 -0.0566 68  ILE   B N   
1266 C  CA  . ILE   B 68  ? 0.1803 0.1616 0.2334 0.0498  -0.0118 -0.0558 68  ILE   B CA  
1267 C  C   . ILE   B 68  ? 0.1939 0.1870 0.2418 0.0420  -0.0180 -0.0673 68  ILE   B C   
1268 O  O   . ILE   B 68  ? 0.2419 0.1863 0.3058 0.0589  -0.0688 -0.0751 68  ILE   B O   
1269 C  CB  . ILE   B 68  ? 0.2020 0.2221 0.2500 0.0472  -0.0345 -0.0624 68  ILE   B CB  
1270 C  CG1 . ILE   B 68  ? 0.2616 0.2692 0.2727 0.0551  -0.0435 -0.0337 68  ILE   B CG1 
1271 C  CG2 . ILE   B 68  ? 0.2023 0.1846 0.2318 0.0448  -0.0345 -0.0451 68  ILE   B CG2 
1272 C  CD1 . ILE   B 68  ? 0.3212 0.4106 0.3175 0.0887  -0.0856 0.0090  68  ILE   B CD1 
1273 N  N   . TYR   B 69  ? 0.1439 0.1681 0.2047 0.0374  0.0015  -0.0538 69  TYR   B N   
1274 C  CA  . TYR   B 69  ? 0.1368 0.1695 0.2004 0.0284  -0.0072 -0.0504 69  TYR   B CA  
1275 C  C   . TYR   B 69  ? 0.1298 0.1606 0.1955 0.0255  -0.0027 -0.0455 69  TYR   B C   
1276 O  O   . TYR   B 69  ? 0.1505 0.1764 0.2012 0.0063  -0.0053 -0.0612 69  TYR   B O   
1277 C  CB  . TYR   B 69  ? 0.1459 0.1883 0.2026 0.0386  0.0228  -0.0504 69  TYR   B CB  
1278 C  CG  . TYR   B 69  ? 0.1532 0.2033 0.2144 0.0163  -0.0059 -0.0599 69  TYR   B CG  
1279 C  CD1 . TYR   B 69  ? 0.1452 0.2576 0.2240 0.0338  -0.0202 -0.1152 69  TYR   B CD1 
1280 C  CD2 . TYR   B 69  ? 0.1473 0.2176 0.2440 0.0124  0.0248  -0.0853 69  TYR   B CD2 
1281 C  CE1 . TYR   B 69  ? 0.1516 0.2456 0.2274 0.0131  0.0030  -0.0907 69  TYR   B CE1 
1282 C  CE2 . TYR   B 69  ? 0.1596 0.2477 0.2289 0.0035  -0.0065 -0.1083 69  TYR   B CE2 
1283 C  CZ  . TYR   B 69  ? 0.1505 0.2169 0.2579 -0.0015 0.0130  -0.1084 69  TYR   B CZ  
1284 O  OH  . TYR   B 69  ? 0.2416 0.2727 0.2585 0.0241  0.0522  -0.1322 69  TYR   B OH  
1285 N  N   . LYS   B 70  ? 0.1199 0.1666 0.1804 0.0135  -0.0132 -0.0488 70  LYS   B N   
1286 C  CA  . LYS   B 70  ? 0.1643 0.1724 0.1793 0.0209  -0.0025 -0.0387 70  LYS   B CA  
1287 C  C   . LYS   B 70  ? 0.1777 0.1641 0.1679 0.0346  0.0104  -0.0242 70  LYS   B C   
1288 O  O   . LYS   B 70  ? 0.1770 0.2081 0.1923 0.0269  -0.0112 -0.0553 70  LYS   B O   
1289 C  CB  . LYS   B 70  ? 0.1847 0.2058 0.2001 -0.0181 0.0114  -0.0029 70  LYS   B CB  
1290 C  CG  . LYS   B 70  ? 0.1756 0.2201 0.1930 0.0169  0.0077  -0.0082 70  LYS   B CG  
1291 C  CD  . LYS   B 70  ? 0.2509 0.2849 0.2795 0.0109  0.0265  0.0359  70  LYS   B CD  
1292 C  CE  . LYS   B 70  ? 0.2820 0.3876 0.3370 -0.0459 0.0832  -0.0134 70  LYS   B CE  
1293 N  NZ  . LYS   B 70  ? 0.4945 0.3594 0.4492 -0.0838 0.1751  0.0331  70  LYS   B NZ  
1294 N  N   . VAL   B 71  ? 0.1183 0.1741 0.1798 0.0168  -0.0067 -0.0383 71  VAL   B N   
1295 C  CA  . VAL   B 71  ? 0.1636 0.1607 0.1588 0.0165  0.0156  -0.0377 71  VAL   B CA  
1296 C  C   . VAL   B 71  ? 0.1167 0.1693 0.1593 0.0291  -0.0051 -0.0305 71  VAL   B C   
1297 O  O   . VAL   B 71  ? 0.1757 0.2049 0.1625 0.0051  0.0057  -0.0506 71  VAL   B O   
1298 C  CB  . VAL   B 71  ? 0.1718 0.2078 0.1398 -0.0106 0.0014  -0.0295 71  VAL   B CB  
1299 C  CG1 . VAL   B 71  ? 0.1867 0.1960 0.1613 -0.0001 -0.0153 -0.0240 71  VAL   B CG1 
1300 C  CG2 . VAL   B 71  ? 0.1477 0.1928 0.1907 -0.0182 -0.0102 -0.0424 71  VAL   B CG2 
1301 N  N   . GLU   B 72  ? 0.1471 0.1878 0.1559 0.0146  0.0137  -0.0210 72  GLU   B N   
1302 C  CA  . GLU   B 72  ? 0.1656 0.2336 0.1585 0.0070  0.0075  -0.0234 72  GLU   B CA  
1303 C  C   . GLU   B 72  ? 0.1567 0.1817 0.1538 -0.0021 -0.0142 -0.0068 72  GLU   B C   
1304 O  O   . GLU   B 72  ? 0.1624 0.2053 0.1804 0.0284  -0.0011 -0.0381 72  GLU   B O   
1305 C  CB  . GLU   B 72  ? 0.1760 0.2035 0.2150 0.0128  0.0285  0.0099  72  GLU   B CB  
1306 C  CG  . GLU   B 72  ? 0.2061 0.2573 0.2462 -0.0004 -0.0394 0.0002  72  GLU   B CG  
1307 C  CD  . GLU   B 72  ? 0.2220 0.2877 0.3053 -0.0317 -0.0282 -0.0183 72  GLU   B CD  
1308 O  OE1 . GLU   B 72  ? 0.2284 0.3066 0.3076 -0.0303 0.0003  0.0102  72  GLU   B OE1 
1309 O  OE2 . GLU   B 72  ? 0.3403 0.2265 0.2372 0.0172  -0.0968 -0.0376 72  GLU   B OE2 
1310 N  N   . ILE   B 73  ? 0.1731 0.1754 0.1631 0.0268  0.0088  -0.0137 73  ILE   B N   
1311 C  CA  . ILE   B 73  ? 0.1687 0.1713 0.1390 0.0053  0.0190  -0.0372 73  ILE   B CA  
1312 C  C   . ILE   B 73  ? 0.1597 0.1498 0.1395 0.0177  -0.0032 -0.0093 73  ILE   B C   
1313 O  O   . ILE   B 73  ? 0.1719 0.1763 0.1542 0.0186  0.0101  -0.0092 73  ILE   B O   
1314 C  CB  . ILE   B 73  ? 0.1823 0.2079 0.1442 -0.0118 -0.0084 -0.0138 73  ILE   B CB  
1315 C  CG1 . ILE   B 73  ? 0.1661 0.2171 0.1585 -0.0027 0.0127  -0.0139 73  ILE   B CG1 
1316 C  CG2 . ILE   B 73  ? 0.2237 0.1749 0.1538 0.0029  0.0130  -0.0129 73  ILE   B CG2 
1317 C  CD1 . ILE   B 73  ? 0.2260 0.2240 0.1893 -0.0370 0.0065  -0.0021 73  ILE   B CD1 
1318 N  N   . ASP   B 74  ? 0.1538 0.1768 0.1750 0.0143  0.0070  -0.0295 74  ASP   B N   
1319 C  CA  . ASP   B 74  ? 0.1530 0.1831 0.1811 0.0340  0.0310  -0.0427 74  ASP   B CA  
1320 C  C   . ASP   B 74  ? 0.1393 0.1541 0.2147 0.0117  0.0124  -0.0070 74  ASP   B C   
1321 O  O   . ASP   B 74  ? 0.1858 0.1934 0.1951 0.0060  0.0246  -0.0366 74  ASP   B O   
1322 C  CB  . ASP   B 74  ? 0.1535 0.1780 0.2761 0.0060  0.0333  -0.0703 74  ASP   B CB  
1323 C  CG  . ASP   B 74  ? 0.2056 0.1843 0.2969 0.0009  0.0300  -0.0723 74  ASP   B CG  
1324 O  OD1 . ASP   B 74  ? 0.2343 0.1982 0.2974 0.0146  0.0814  -0.0042 74  ASP   B OD1 
1325 O  OD2 . ASP   B 74  ? 0.2361 0.2791 0.4303 -0.0575 0.0655  -0.1861 74  ASP   B OD2 
1326 N  N   . THR   B 75  ? 0.1546 0.1569 0.1604 0.0163  0.0136  -0.0142 75  THR   B N   
1327 C  CA  . THR   B 75  ? 0.1844 0.1527 0.1405 0.0185  0.0242  -0.0064 75  THR   B CA  
1328 C  C   . THR   B 75  ? 0.1901 0.1429 0.1490 0.0265  0.0141  0.0035  75  THR   B C   
1329 O  O   . THR   B 75  ? 0.1660 0.1450 0.1826 0.0103  0.0086  -0.0008 75  THR   B O   
1330 C  CB  . THR   B 75  ? 0.1634 0.1186 0.1734 0.0101  0.0231  -0.0006 75  THR   B CB  
1331 O  OG1 . THR   B 75  ? 0.1797 0.1314 0.1647 0.0308  0.0044  0.0008  75  THR   B OG1 
1332 C  CG2 . THR   B 75  ? 0.1745 0.1412 0.2087 0.0027  0.0231  -0.0258 75  THR   B CG2 
1333 N  N   . LYS   B 76  ? 0.1736 0.1458 0.1851 0.0151  0.0276  -0.0180 76  LYS   B N   
1334 C  CA  . LYS   B 76  ? 0.1626 0.1643 0.1703 -0.0105 0.0241  -0.0125 76  LYS   B CA  
1335 C  C   . LYS   B 76  ? 0.1689 0.1349 0.2131 -0.0048 0.0367  -0.0123 76  LYS   B C   
1336 O  O   . LYS   B 76  ? 0.1843 0.1612 0.1993 0.0003  0.0282  0.0097  76  LYS   B O   
1337 C  CB  . LYS   B 76  ? 0.1832 0.2018 0.2030 0.0188  0.0111  0.0158  76  LYS   B CB  
1338 C  CG  . LYS   B 76  ? 0.2061 0.2976 0.2391 0.0077  0.0406  0.1067  76  LYS   B CG  
1339 C  CD  . LYS   B 76  ? 0.2021 0.3048 0.2923 -0.0325 0.0389  0.0709  76  LYS   B CD  
1340 C  CE  . LYS   B 76  ? 0.2327 0.3333 0.3311 -0.0233 0.0214  0.0952  76  LYS   B CE  
1341 N  NZ  . LYS   B 76  ? 0.3079 0.3423 0.3584 -0.0678 0.0322  0.1396  76  LYS   B NZ  
1342 N  N   . SER   B 77  ? 0.1854 0.1377 0.2254 -0.0100 0.0280  -0.0065 77  SER   B N   
1343 C  CA  . SER   B 77  ? 0.2170 0.1847 0.2248 -0.0403 0.0077  -0.0154 77  SER   B CA  
1344 C  C   . SER   B 77  ? 0.1308 0.1797 0.2231 0.0051  0.0024  -0.0381 77  SER   B C   
1345 O  O   . SER   B 77  ? 0.1667 0.2143 0.2332 -0.0187 0.0120  -0.0371 77  SER   B O   
1346 C  CB  . SER   B 77  ? 0.2702 0.2007 0.2546 -0.0089 0.0226  -0.0294 77  SER   B CB  
1347 O  OG  . SER   B 77  ? 0.2294 0.2480 0.3627 -0.0350 0.0599  -0.0680 77  SER   B OG  
1348 N  N   . TYR   B 78  ? 0.1535 0.1824 0.1826 -0.0229 0.0158  -0.0075 78  TYR   B N   
1349 C  CA  . TYR   B 78  ? 0.1260 0.2007 0.1732 -0.0154 -0.0023 0.0143  78  TYR   B CA  
1350 C  C   . TYR   B 78  ? 0.1158 0.1841 0.1954 -0.0071 -0.0227 0.0018  78  TYR   B C   
1351 O  O   . TYR   B 78  ? 0.1469 0.1990 0.1907 -0.0237 -0.0262 -0.0059 78  TYR   B O   
1352 C  CB  . TYR   B 78  ? 0.1230 0.2176 0.1755 -0.0066 0.0141  -0.0212 78  TYR   B CB  
1353 C  CG  . TYR   B 78  ? 0.1295 0.1934 0.1740 -0.0152 0.0172  -0.0083 78  TYR   B CG  
1354 C  CD1 . TYR   B 78  ? 0.1527 0.2194 0.1787 -0.0362 0.0145  -0.0078 78  TYR   B CD1 
1355 C  CD2 . TYR   B 78  ? 0.1372 0.1989 0.1936 -0.0036 0.0078  -0.0140 78  TYR   B CD2 
1356 C  CE1 . TYR   B 78  ? 0.1814 0.2288 0.1592 -0.0527 -0.0054 0.0024  78  TYR   B CE1 
1357 C  CE2 . TYR   B 78  ? 0.1544 0.1789 0.1745 -0.0221 -0.0030 -0.0238 78  TYR   B CE2 
1358 C  CZ  . TYR   B 78  ? 0.1725 0.2123 0.1801 -0.0367 -0.0006 -0.0006 78  TYR   B CZ  
1359 O  OH  . TYR   B 78  ? 0.1854 0.2181 0.1833 -0.0304 0.0052  -0.0214 78  TYR   B OH  
1360 N  N   . TRP   B 79  ? 0.1234 0.1635 0.1753 -0.0012 -0.0042 0.0049  79  TRP   B N   
1361 C  CA  . TRP   B 79  ? 0.1030 0.1594 0.2011 0.0092  0.0017  0.0021  79  TRP   B CA  
1362 C  C   . TRP   B 79  ? 0.1018 0.1995 0.2178 -0.0013 -0.0089 0.0082  79  TRP   B C   
1363 O  O   . TRP   B 79  ? 0.1154 0.2462 0.2488 0.0245  -0.0114 -0.0219 79  TRP   B O   
1364 C  CB  . TRP   B 79  ? 0.1206 0.1576 0.1948 0.0071  0.0144  0.0054  79  TRP   B CB  
1365 C  CG  . TRP   B 79  ? 0.1196 0.1464 0.1600 0.0084  0.0001  -0.0207 79  TRP   B CG  
1366 C  CD1 . TRP   B 79  ? 0.1102 0.1351 0.1344 0.0221  0.0031  -0.0194 79  TRP   B CD1 
1367 C  CD2 . TRP   B 79  ? 0.1214 0.1475 0.1682 0.0222  -0.0265 -0.0032 79  TRP   B CD2 
1368 N  NE1 . TRP   B 79  ? 0.1086 0.1749 0.1532 0.0273  -0.0120 -0.0051 79  TRP   B NE1 
1369 C  CE2 . TRP   B 79  ? 0.1150 0.1562 0.1454 0.0179  -0.0141 -0.0133 79  TRP   B CE2 
1370 C  CE3 . TRP   B 79  ? 0.1105 0.1437 0.2165 -0.0017 -0.0345 -0.0036 79  TRP   B CE3 
1371 C  CZ2 . TRP   B 79  ? 0.1197 0.1728 0.1470 0.0276  -0.0064 -0.0141 79  TRP   B CZ2 
1372 C  CZ3 . TRP   B 79  ? 0.1480 0.1405 0.2154 0.0260  -0.0307 -0.0095 79  TRP   B CZ3 
1373 C  CH2 . TRP   B 79  ? 0.1577 0.1315 0.1891 -0.0107 -0.0240 -0.0027 79  TRP   B CH2 
1374 N  N   . LYS   B 80  ? 0.1269 0.2101 0.2157 -0.0224 0.0041  -0.0034 80  LYS   B N   
1375 C  CA  . LYS   B 80  ? 0.0947 0.2512 0.3013 -0.0274 0.0133  -0.0056 80  LYS   B CA  
1376 C  C   . LYS   B 80  ? 0.1310 0.2362 0.2453 -0.0085 -0.0033 -0.0335 80  LYS   B C   
1377 O  O   . LYS   B 80  ? 0.1166 0.3081 0.3140 -0.0026 -0.0032 -0.0385 80  LYS   B O   
1378 C  CB  . LYS   B 80  ? 0.1773 0.2986 0.3054 -0.0524 0.0102  0.0073  80  LYS   B CB  
1379 C  CG  . LYS   B 80  ? 0.2398 0.2912 0.3192 -0.0508 0.0515  0.0041  80  LYS   B CG  
1380 C  CD  . LYS   B 80  ? 0.3199 0.3126 0.3473 -0.0364 0.0436  0.0137  80  LYS   B CD  
1381 C  CE  . LYS   B 80  ? 0.3638 0.3231 0.3500 -0.0107 -0.0054 0.0140  80  LYS   B CE  
1382 N  N   . ALA   B 81  ? 0.1520 0.2486 0.2541 -0.0074 -0.0254 -0.0077 81  ALA   B N   
1383 C  CA  . ALA   B 81  ? 0.1915 0.3258 0.2519 -0.0253 -0.0448 -0.0066 81  ALA   B CA  
1384 C  C   . ALA   B 81  ? 0.1515 0.3286 0.3220 0.0003  -0.0662 -0.0515 81  ALA   B C   
1385 O  O   . ALA   B 81  ? 0.1757 0.3529 0.3963 0.0107  -0.0833 0.0080  81  ALA   B O   
1386 C  CB  . ALA   B 81  ? 0.2360 0.3468 0.2786 -0.0290 -0.0241 0.0104  81  ALA   B CB  
1387 N  N   . LEU   B 82  ? 0.2092 0.2647 0.2504 -0.0344 -0.0727 0.0172  82  LEU   B N   
1388 C  CA  . LEU   B 82  ? 0.1635 0.3245 0.3471 -0.0397 -0.0717 -0.0345 82  LEU   B CA  
1389 C  C   . LEU   B 82  ? 0.2155 0.2796 0.3526 0.0577  -0.0902 0.0082  82  LEU   B C   
1390 O  O   . LEU   B 82  ? 0.1824 0.2976 0.4909 0.0864  -0.0444 -0.0396 82  LEU   B O   
1391 C  CB  . LEU   B 82  ? 0.1708 0.2226 0.3749 0.0140  -0.0982 0.0120  82  LEU   B CB  
1392 C  CG  . LEU   B 82  ? 0.2694 0.3564 0.3574 -0.0270 -0.0672 0.0657  82  LEU   B CG  
1393 C  CD1 . LEU   B 82  ? 0.2170 0.4218 0.4149 0.0121  -0.0400 0.0419  82  LEU   B CD1 
1394 C  CD2 . LEU   B 82  ? 0.3489 0.5453 0.4177 -0.0156 -0.0778 0.1805  82  LEU   B CD2 
1395 N  N   . GLY   B 83  ? 0.1469 0.2505 0.3435 0.0365  -0.0644 -0.0476 83  GLY   B N   
1396 C  CA  . GLY   B 83  ? 0.1174 0.3395 0.3081 0.0586  -0.0417 -0.0950 83  GLY   B CA  
1397 C  C   . GLY   B 83  ? 0.0939 0.3675 0.4117 0.0347  -0.0349 -0.1333 83  GLY   B C   
1398 O  O   . GLY   B 83  ? 0.1113 0.2976 0.3999 0.0434  -0.0466 -0.1255 83  GLY   B O   
1399 N  N   . ILE   B 84  ? 0.1250 0.2491 0.3059 0.0460  -0.0615 -0.1013 84  ILE   B N   
1400 C  CA  . ILE   B 84  ? 0.1134 0.2997 0.2686 0.0678  -0.0491 -0.1298 84  ILE   B CA  
1401 C  C   . ILE   B 84  ? 0.0884 0.2761 0.3085 0.0319  -0.0341 -0.1295 84  ILE   B C   
1402 O  O   . ILE   B 84  ? 0.1328 0.2711 0.2373 0.0209  -0.0038 -0.0885 84  ILE   B O   
1403 C  CB  . ILE   B 84  ? 0.1268 0.2607 0.4584 0.0820  -0.0713 -0.1393 84  ILE   B CB  
1404 C  CG1 . ILE   B 84  ? 0.1619 0.2361 0.4682 0.0201  -0.0514 -0.1001 84  ILE   B CG1 
1405 C  CG2 . ILE   B 84  ? 0.1513 0.3133 0.4435 0.0055  -0.0513 -0.1466 84  ILE   B CG2 
1406 C  CD1 . ILE   B 84  ? 0.2142 0.2359 0.4233 0.0722  -0.0843 -0.0359 84  ILE   B CD1 
1407 N  N   . SER   B 85  ? 0.1562 0.3416 0.2642 0.0683  -0.0131 -0.1537 85  SER   B N   
1408 C  CA  . SER   B 85  ? 0.1208 0.4026 0.2994 0.0316  0.0160  -0.1523 85  SER   B CA  
1409 C  C   . SER   B 85  ? 0.1122 0.2931 0.3054 0.0740  -0.0394 -0.0861 85  SER   B C   
1410 O  O   . SER   B 85  ? 0.1614 0.3358 0.3853 0.0643  -0.0573 -0.1522 85  SER   B O   
1411 C  CB  . SER   B 85  ? 0.1193 0.3975 0.2711 0.0678  0.0089  -0.0448 85  SER   B CB  
1412 O  OG  . SER   B 85  ? 0.1747 0.5425 0.2842 0.0673  -0.0031 -0.0411 85  SER   B OG  
1413 N  N   . PRO   B 86  ? 0.1438 0.2432 0.2109 0.0028  0.0306  -0.0324 86  PRO   B N   
1414 C  CA  . PRO   B 86  ? 0.1503 0.2082 0.2161 0.0502  0.0413  0.0709  86  PRO   B CA  
1415 C  C   . PRO   B 86  ? 0.2185 0.2001 0.1884 0.0005  0.0616  0.0272  86  PRO   B C   
1416 O  O   . PRO   B 86  ? 0.2096 0.2148 0.2120 -0.0182 0.0436  0.0471  86  PRO   B O   
1417 C  CB  . PRO   B 86  ? 0.1911 0.3897 0.1853 0.1181  0.0665  0.0473  86  PRO   B CB  
1418 C  CG  . PRO   B 86  ? 0.3639 0.3478 0.1815 0.1270  0.0265  0.0564  86  PRO   B CG  
1419 C  CD  . PRO   B 86  ? 0.2718 0.2837 0.1789 0.0144  0.0328  0.0104  86  PRO   B CD  
1420 N  N   . PHE   B 87  ? 0.1795 0.1026 0.1635 0.0209  0.0430  0.0126  87  PHE   B N   
1421 C  CA  . PHE   B 87  ? 0.1871 0.1228 0.1496 0.0262  0.0470  0.0041  87  PHE   B CA  
1422 C  C   . PHE   B 87  ? 0.2072 0.1106 0.1330 0.0280  0.0155  0.0063  87  PHE   B C   
1423 O  O   . PHE   B 87  ? 0.1944 0.1086 0.1423 0.0046  0.0204  -0.0024 87  PHE   B O   
1424 C  CB  . PHE   B 87  ? 0.2241 0.1196 0.1601 0.0128  0.0530  0.0045  87  PHE   B CB  
1425 C  CG  . PHE   B 87  ? 0.2049 0.1002 0.1620 -0.0132 0.0224  -0.0034 87  PHE   B CG  
1426 C  CD1 . PHE   B 87  ? 0.2164 0.1201 0.1562 0.0118  0.0288  0.0090  87  PHE   B CD1 
1427 C  CD2 . PHE   B 87  ? 0.1958 0.0965 0.1730 -0.0151 0.0352  0.0103  87  PHE   B CD2 
1428 C  CE1 . PHE   B 87  ? 0.1908 0.1193 0.1668 -0.0121 0.0153  0.0205  87  PHE   B CE1 
1429 C  CE2 . PHE   B 87  ? 0.2063 0.0984 0.2130 -0.0198 0.0022  -0.0010 87  PHE   B CE2 
1430 C  CZ  . PHE   B 87  ? 0.1908 0.0951 0.1945 -0.0233 -0.0177 0.0110  87  PHE   B CZ  
1431 N  N   . HIS   B 88  ? 0.2316 0.1143 0.1295 0.0587  0.0310  0.0312  88  HIS   B N   
1432 C  CA  . HIS   B 88  ? 0.1664 0.1572 0.1544 0.0653  0.0128  -0.0085 88  HIS   B CA  
1433 C  C   . HIS   B 88  ? 0.1613 0.1629 0.1331 0.0713  -0.0034 -0.0122 88  HIS   B C   
1434 O  O   . HIS   B 88  ? 0.2144 0.1566 0.1690 0.0717  0.0092  -0.0028 88  HIS   B O   
1435 C  CB  . HIS   B 88  ? 0.1754 0.1365 0.1726 0.0692  0.0072  0.0041  88  HIS   B CB  
1436 C  CG  . HIS   B 88  ? 0.1583 0.1692 0.1656 0.0267  0.0298  0.0173  88  HIS   B CG  
1437 N  ND1 . HIS   B 88  ? 0.2579 0.1275 0.2217 0.0178  0.0198  -0.0199 88  HIS   B ND1 
1438 C  CD2 . HIS   B 88  ? 0.1770 0.1477 0.2125 0.0909  0.0690  0.0802  88  HIS   B CD2 
1439 C  CE1 . HIS   B 88  ? 0.1405 0.1151 0.1909 0.0128  0.0428  -0.0024 88  HIS   B CE1 
1440 N  NE2 . HIS   B 88  ? 0.2143 0.1637 0.2572 0.0303  0.0739  0.0713  88  HIS   B NE2 
1441 N  N   . GLU   B 89  ? 0.1935 0.1119 0.1436 0.0376  0.0119  0.0017  89  GLU   B N   
1442 C  CA  . GLU   B 89  ? 0.1976 0.1309 0.1750 0.0386  0.0257  -0.0022 89  GLU   B CA  
1443 C  C   . GLU   B 89  ? 0.1992 0.1467 0.1501 0.0366  -0.0194 -0.0250 89  GLU   B C   
1444 O  O   . GLU   B 89  ? 0.2052 0.2124 0.1645 0.0290  0.0042  -0.0206 89  GLU   B O   
1445 C  CB  . GLU   B 89  ? 0.2086 0.1427 0.1852 0.0384  0.0035  -0.0092 89  GLU   B CB  
1446 C  CG  . GLU   B 89  ? 0.2403 0.1680 0.1698 0.0132  0.0093  -0.0199 89  GLU   B CG  
1447 C  CD  . GLU   B 89  ? 0.2783 0.1865 0.2233 -0.0302 0.0419  -0.0092 89  GLU   B CD  
1448 O  OE1 . GLU   B 89  ? 0.2839 0.3869 0.2313 -0.0889 0.0000  -0.0143 89  GLU   B OE1 
1449 O  OE2 . GLU   B 89  ? 0.2860 0.2081 0.3366 0.0091  0.0472  0.0584  89  GLU   B OE2 
1450 N  N   . HIS   B 90  ? 0.1793 0.1332 0.1475 0.0166  0.0095  -0.0121 90  HIS   B N   
1451 C  CA  . HIS   B 90  ? 0.2136 0.1311 0.1458 0.0124  0.0091  -0.0195 90  HIS   B CA  
1452 C  C   . HIS   B 90  ? 0.1728 0.1259 0.1450 0.0406  0.0140  -0.0137 90  HIS   B C   
1453 O  O   . HIS   B 90  ? 0.1974 0.1842 0.1402 0.0164  0.0019  -0.0320 90  HIS   B O   
1454 C  CB  . HIS   B 90  ? 0.2064 0.1719 0.1513 0.0364  -0.0025 -0.0326 90  HIS   B CB  
1455 C  CG  . HIS   B 90  ? 0.2368 0.2243 0.1954 0.0915  -0.0157 -0.0541 90  HIS   B CG  
1456 N  ND1 . HIS   B 90  ? 0.2672 0.2035 0.3047 0.0975  -0.0530 -0.0699 90  HIS   B ND1 
1457 C  CD2 . HIS   B 90  ? 0.3738 0.2389 0.2053 0.1310  0.0220  0.0034  90  HIS   B CD2 
1458 C  CE1 . HIS   B 90  ? 0.2410 0.1755 0.2745 0.0360  -0.0319 -0.0486 90  HIS   B CE1 
1459 N  NE2 . HIS   B 90  ? 0.3269 0.2275 0.2938 0.0457  -0.0309 -0.0197 90  HIS   B NE2 
1460 N  N   . ALA   B 91  ? 0.1892 0.1608 0.1309 0.0089  0.0054  -0.0180 91  ALA   B N   
1461 C  CA  . ALA   B 91  ? 0.1743 0.1778 0.1403 0.0007  0.0240  -0.0402 91  ALA   B CA  
1462 C  C   . ALA   B 91  ? 0.1883 0.1710 0.1497 -0.0104 0.0230  -0.0382 91  ALA   B C   
1463 O  O   . ALA   B 91  ? 0.2054 0.2378 0.1551 0.0488  -0.0008 -0.0570 91  ALA   B O   
1464 C  CB  . ALA   B 91  ? 0.2122 0.1936 0.1453 -0.0087 0.0183  -0.0206 91  ALA   B CB  
1465 N  N   . GLU   B 92  ? 0.1721 0.2929 0.1494 0.0267  0.0123  -0.0617 92  GLU   B N   
1466 C  CA  . GLU   B 92  ? 0.1796 0.2614 0.1627 0.0216  0.0299  -0.0365 92  GLU   B CA  
1467 C  C   . GLU   B 92  ? 0.1921 0.3219 0.1585 0.0443  0.0191  -0.0763 92  GLU   B C   
1468 O  O   . GLU   B 92  ? 0.1830 0.5492 0.1685 0.0391  -0.0148 -0.0981 92  GLU   B O   
1469 C  CB  . GLU   B 92  ? 0.2476 0.2460 0.2638 0.0326  0.0155  0.0027  92  GLU   B CB  
1470 C  CG  . GLU   B 92  ? 0.2683 0.2184 0.2422 0.0094  -0.0095 0.0076  92  GLU   B CG  
1471 C  CD  . GLU   B 92  ? 0.2136 0.2038 0.1155 -0.0158 0.0013  -0.0340 92  GLU   B CD  
1472 O  OE1 . GLU   B 92  ? 0.1573 0.1845 0.2350 -0.0327 -0.0135 0.0027  92  GLU   B OE1 
1473 O  OE2 . GLU   B 92  ? 0.2212 0.1403 0.2479 0.0210  0.0097  -0.0519 92  GLU   B OE2 
1474 N  N   . VAL   B 93  ? 0.1606 0.2028 0.1527 0.0374  0.0037  -0.0459 93  VAL   B N   
1475 C  CA  . VAL   B 93  ? 0.1634 0.1758 0.1567 0.0185  -0.0084 -0.0486 93  VAL   B CA  
1476 C  C   . VAL   B 93  ? 0.1500 0.1801 0.1415 0.0300  -0.0014 -0.0391 93  VAL   B C   
1477 O  O   . VAL   B 93  ? 0.1543 0.1829 0.1527 0.0367  -0.0124 -0.0354 93  VAL   B O   
1478 C  CB  . VAL   B 93  ? 0.1650 0.1787 0.2182 -0.0006 -0.0148 -0.0395 93  VAL   B CB  
1479 C  CG1 . VAL   B 93  ? 0.1799 0.1697 0.2135 0.0201  -0.0187 0.0052  93  VAL   B CG1 
1480 C  CG2 . VAL   B 93  ? 0.2174 0.1753 0.2701 0.0325  -0.0406 -0.0565 93  VAL   B CG2 
1481 N  N   . VAL   B 94  ? 0.1722 0.1523 0.1471 0.0220  -0.0085 -0.0367 94  VAL   B N   
1482 C  CA  . VAL   B 94  ? 0.1604 0.1483 0.1461 0.0091  -0.0068 -0.0480 94  VAL   B CA  
1483 C  C   . VAL   B 94  ? 0.1551 0.1473 0.1679 0.0309  -0.0095 -0.0208 94  VAL   B C   
1484 O  O   . VAL   B 94  ? 0.1614 0.1582 0.1742 -0.0011 -0.0275 -0.0307 94  VAL   B O   
1485 C  CB  . VAL   B 94  ? 0.1749 0.1525 0.1625 0.0039  -0.0122 -0.0128 94  VAL   B CB  
1486 C  CG1 . VAL   B 94  ? 0.2190 0.1591 0.2221 0.0173  -0.0325 0.0022  94  VAL   B CG1 
1487 C  CG2 . VAL   B 94  ? 0.2090 0.1729 0.2052 -0.0144 -0.0259 0.0179  94  VAL   B CG2 
1488 N  N   . PHE   B 95  ? 0.1555 0.1737 0.1802 0.0096  -0.0121 -0.0334 95  PHE   B N   
1489 C  CA  . PHE   B 95  ? 0.1388 0.1760 0.1976 0.0166  -0.0094 -0.0454 95  PHE   B CA  
1490 C  C   . PHE   B 95  ? 0.1518 0.2065 0.1905 0.0093  -0.0174 -0.0311 95  PHE   B C   
1491 O  O   . PHE   B 95  ? 0.1727 0.1563 0.2292 0.0148  -0.0009 -0.0251 95  PHE   B O   
1492 C  CB  . PHE   B 95  ? 0.1766 0.1987 0.1925 -0.0046 -0.0033 -0.0389 95  PHE   B CB  
1493 C  CG  . PHE   B 95  ? 0.2202 0.1245 0.2279 0.0254  -0.0476 -0.0173 95  PHE   B CG  
1494 C  CD1 . PHE   B 95  ? 0.2566 0.1841 0.3809 -0.0180 -0.1313 0.0330  95  PHE   B CD1 
1495 C  CD2 . PHE   B 95  ? 0.3430 0.1638 0.2280 0.0327  -0.0459 -0.0906 95  PHE   B CD2 
1496 C  CE1 . PHE   B 95  ? 0.2100 0.1836 0.3343 -0.0325 -0.0683 0.0195  95  PHE   B CE1 
1497 C  CE2 . PHE   B 95  ? 0.3421 0.1954 0.2417 -0.0208 -0.0380 -0.0402 95  PHE   B CE2 
1498 C  CZ  . PHE   B 95  ? 0.3221 0.1847 0.3049 -0.0698 -0.0694 -0.0190 95  PHE   B CZ  
1499 N  N   . THR   B 96  ? 0.1539 0.2665 0.2155 0.0157  0.0013  -0.0693 96  THR   B N   
1500 C  CA  . THR   B 96  ? 0.1506 0.2770 0.2189 0.0399  0.0172  -0.0446 96  THR   B CA  
1501 C  C   . THR   B 96  ? 0.2190 0.2517 0.2536 0.0600  0.0397  -0.0540 96  THR   B C   
1502 O  O   . THR   B 96  ? 0.3326 0.2817 0.2071 0.0269  0.0391  -0.0538 96  THR   B O   
1503 C  CB  . THR   B 96  ? 0.1583 0.3294 0.2352 0.0228  -0.0283 -0.0836 96  THR   B CB  
1504 O  OG1 . THR   B 96  ? 0.2156 0.3273 0.2144 0.0521  -0.0118 -0.0404 96  THR   B OG1 
1505 C  CG2 . THR   B 96  ? 0.1821 0.3298 0.2733 0.0941  0.0221  -0.0416 96  THR   B CG2 
1506 N  N   . ALA   B 97  ? 0.1916 0.3169 0.2550 0.0400  0.0531  -0.0790 97  ALA   B N   
1507 C  CA  . ALA   B 97  ? 0.2871 0.2410 0.2539 0.0036  0.0454  -0.0850 97  ALA   B CA  
1508 C  C   . ALA   B 97  ? 0.3788 0.3207 0.4649 0.0530  0.2130  -0.0452 97  ALA   B C   
1509 O  O   . ALA   B 97  ? 0.2384 0.3523 0.3010 -0.0218 0.0138  -0.0318 97  ALA   B O   
1510 C  CB  . ALA   B 97  ? 0.6567 0.3217 0.2700 -0.1924 -0.0632 -0.0224 97  ALA   B CB  
1511 N  N   . ASN   B 98  ? 0.2180 0.4712 0.3527 -0.0254 0.0571  -0.1216 98  ASN   B N   
1512 C  CA  . ASN   B 98  ? 0.2694 0.2822 0.4140 -0.0554 0.0010  -0.1394 98  ASN   B CA  
1513 C  C   . ASN   B 98  ? 0.4700 0.4567 0.5213 -0.1371 -0.0899 0.1517  98  ASN   B C   
1514 O  O   . ASN   B 98  ? 0.2549 0.3724 0.3298 0.0235  0.0912  -0.0399 98  ASN   B O   
1515 C  CB  . ASN   B 98  ? 0.2321 0.5280 0.3868 -0.0106 -0.0573 -0.1672 98  ASN   B CB  
1516 N  N   . ARG   B 104 ? 0.2647 0.7456 0.2401 -0.0176 0.0394  -0.1618 104 ARG   B N   
1517 C  CA  . ARG   B 104 ? 0.2111 0.5604 0.2783 -0.0163 0.0750  -0.1394 104 ARG   B CA  
1518 C  C   . ARG   B 104 ? 0.2590 0.3450 0.3082 -0.0375 0.1247  -0.1249 104 ARG   B C   
1519 O  O   . ARG   B 104 ? 0.3052 0.4412 0.2127 -0.0990 0.0804  -0.0761 104 ARG   B O   
1520 C  CB  . ARG   B 104 ? 0.3340 0.5883 0.2556 -0.0336 0.0455  -0.1197 104 ARG   B CB  
1521 N  N   . TYR   B 105 ? 0.1709 0.3983 0.1745 -0.0135 0.0196  -0.0907 105 TYR   B N   
1522 C  CA  . TYR   B 105 ? 0.1897 0.2738 0.1961 -0.0021 0.0177  -0.0797 105 TYR   B CA  
1523 C  C   . TYR   B 105 ? 0.1570 0.2723 0.1899 -0.0121 0.0201  -0.0864 105 TYR   B C   
1524 O  O   . TYR   B 105 ? 0.1768 0.2907 0.2528 -0.0145 0.0182  -0.1254 105 TYR   B O   
1525 C  CB  . TYR   B 105 ? 0.1933 0.2813 0.2325 -0.0059 0.0495  -0.0499 105 TYR   B CB  
1526 C  CG  . TYR   B 105 ? 0.1960 0.2461 0.2767 0.0197  -0.0268 -0.0480 105 TYR   B CG  
1527 C  CD1 . TYR   B 105 ? 0.2843 0.3358 0.3435 0.0921  -0.0839 -0.1485 105 TYR   B CD1 
1528 C  CD2 . TYR   B 105 ? 0.2563 0.3120 0.2776 0.0643  -0.0278 -0.0160 105 TYR   B CD2 
1529 C  CE1 . TYR   B 105 ? 0.2729 0.3834 0.2557 0.1033  -0.0341 -0.0457 105 TYR   B CE1 
1530 C  CE2 . TYR   B 105 ? 0.2877 0.2078 0.2401 0.0186  -0.0566 -0.0444 105 TYR   B CE2 
1531 C  CZ  . TYR   B 105 ? 0.2022 0.3339 0.3003 0.0535  -0.0315 -0.0749 105 TYR   B CZ  
1532 O  OH  . TYR   B 105 ? 0.2421 0.3389 0.3436 0.0419  -0.0037 -0.0630 105 TYR   B OH  
1533 N  N   . THR   B 106 ? 0.1701 0.2362 0.1660 -0.0419 0.0415  -0.0660 106 THR   B N   
1534 C  CA  . THR   B 106 ? 0.1789 0.2113 0.1596 -0.0081 0.0218  -0.0435 106 THR   B CA  
1535 C  C   . THR   B 106 ? 0.1285 0.2179 0.1496 -0.0099 0.0092  -0.0497 106 THR   B C   
1536 O  O   . THR   B 106 ? 0.1448 0.2393 0.1779 -0.0504 0.0100  -0.0738 106 THR   B O   
1537 C  CB  . THR   B 106 ? 0.2274 0.2216 0.1903 -0.0009 -0.0112 -0.0430 106 THR   B CB  
1538 O  OG1 . THR   B 106 ? 0.3248 0.3135 0.1881 -0.0590 0.0229  -0.0380 106 THR   B OG1 
1539 C  CG2 . THR   B 106 ? 0.2256 0.2454 0.2579 0.0190  -0.0305 -0.0268 106 THR   B CG2 
1540 N  N   . ILE   B 107 ? 0.1201 0.2148 0.1575 -0.0117 0.0118  -0.0692 107 ILE   B N   
1541 C  CA  . ILE   B 107 ? 0.1204 0.1989 0.1368 0.0064  0.0000  -0.0230 107 ILE   B CA  
1542 C  C   . ILE   B 107 ? 0.1295 0.1700 0.1313 0.0013  -0.0221 -0.0291 107 ILE   B C   
1543 O  O   . ILE   B 107 ? 0.1274 0.2198 0.1548 0.0102  -0.0206 -0.0300 107 ILE   B O   
1544 C  CB  . ILE   B 107 ? 0.1345 0.1900 0.1731 -0.0175 -0.0035 -0.0237 107 ILE   B CB  
1545 C  CG1 . ILE   B 107 ? 0.1506 0.2591 0.2033 0.0343  -0.0091 -0.0584 107 ILE   B CG1 
1546 C  CG2 . ILE   B 107 ? 0.1464 0.2046 0.1853 -0.0073 -0.0292 -0.0206 107 ILE   B CG2 
1547 C  CD1 . ILE   B 107 ? 0.1809 0.1781 0.3134 0.0634  -0.0427 -0.0615 107 ILE   B CD1 
1548 N  N   . ALA   B 108 ? 0.1390 0.1832 0.1265 0.0046  0.0023  -0.0311 108 ALA   B N   
1549 C  CA  . ALA   B 108 ? 0.1794 0.1767 0.1352 0.0245  -0.0065 -0.0180 108 ALA   B CA  
1550 C  C   . ALA   B 108 ? 0.1652 0.2034 0.1372 0.0480  -0.0214 -0.0183 108 ALA   B C   
1551 O  O   . ALA   B 108 ? 0.1479 0.2091 0.1291 0.0299  0.0000  -0.0080 108 ALA   B O   
1552 C  CB  . ALA   B 108 ? 0.2248 0.2026 0.1796 0.0330  0.0215  0.0000  108 ALA   B CB  
1553 N  N   . ALA   B 109 ? 0.1687 0.2089 0.1137 0.0695  -0.0198 -0.0323 109 ALA   B N   
1554 C  CA  . ALA   B 109 ? 0.1607 0.2131 0.1502 0.0687  0.0034  -0.0141 109 ALA   B CA  
1555 C  C   . ALA   B 109 ? 0.1356 0.1821 0.1375 0.0543  -0.0239 -0.0174 109 ALA   B C   
1556 O  O   . ALA   B 109 ? 0.1985 0.2624 0.1252 0.1097  -0.0427 -0.0514 109 ALA   B O   
1557 C  CB  . ALA   B 109 ? 0.1720 0.2239 0.1616 0.0570  0.0322  -0.0057 109 ALA   B CB  
1558 N  N   . LEU   B 110 ? 0.1314 0.1378 0.1218 0.0436  -0.0147 -0.0055 110 LEU   B N   
1559 C  CA  . LEU   B 110 ? 0.1179 0.1441 0.1239 0.0288  -0.0042 0.0089  110 LEU   B CA  
1560 C  C   . LEU   B 110 ? 0.1008 0.1190 0.1278 0.0217  -0.0076 -0.0033 110 LEU   B C   
1561 O  O   . LEU   B 110 ? 0.1068 0.1500 0.1242 0.0176  -0.0074 0.0052  110 LEU   B O   
1562 C  CB  . LEU   B 110 ? 0.0978 0.1435 0.1420 0.0035  -0.0002 0.0013  110 LEU   B CB  
1563 C  CG  . LEU   B 110 ? 0.1162 0.1546 0.1492 0.0258  0.0120  0.0011  110 LEU   B CG  
1564 C  CD1 . LEU   B 110 ? 0.1263 0.1457 0.1512 0.0112  0.0118  0.0156  110 LEU   B CD1 
1565 C  CD2 . LEU   B 110 ? 0.1490 0.1609 0.2000 -0.0136 -0.0178 -0.0102 110 LEU   B CD2 
1566 N  N   . LEU   B 111 ? 0.1061 0.1270 0.1228 0.0081  -0.0002 0.0067  111 LEU   B N   
1567 C  CA  . LEU   B 111 ? 0.0998 0.1328 0.1294 0.0056  -0.0032 0.0032  111 LEU   B CA  
1568 C  C   . LEU   B 111 ? 0.1168 0.1353 0.1128 0.0106  -0.0016 0.0109  111 LEU   B C   
1569 O  O   . LEU   B 111 ? 0.1218 0.1214 0.1292 0.0143  -0.0009 0.0081  111 LEU   B O   
1570 C  CB  . LEU   B 111 ? 0.1071 0.1318 0.1321 0.0051  0.0170  0.0177  111 LEU   B CB  
1571 C  CG  . LEU   B 111 ? 0.1383 0.1402 0.1571 0.0147  0.0004  -0.0212 111 LEU   B CG  
1572 C  CD1 . LEU   B 111 ? 0.1430 0.1468 0.1730 0.0049  -0.0022 -0.0273 111 LEU   B CD1 
1573 C  CD2 . LEU   B 111 ? 0.1274 0.1228 0.1521 0.0061  -0.0108 -0.0009 111 LEU   B CD2 
1574 N  N   . SER   B 112 ? 0.1118 0.1369 0.1198 0.0153  0.0050  0.0012  112 SER   B N   
1575 C  CA  . SER   B 112 ? 0.1072 0.1339 0.1297 0.0162  -0.0076 -0.0068 112 SER   B CA  
1576 C  C   . SER   B 112 ? 0.1108 0.1410 0.1065 0.0239  0.0142  -0.0131 112 SER   B C   
1577 O  O   . SER   B 112 ? 0.1212 0.1026 0.1480 0.0249  0.0006  -0.0098 112 SER   B O   
1578 C  CB  . SER   B 112 ? 0.1380 0.1416 0.1215 -0.0133 0.0174  -0.0045 112 SER   B CB  
1579 O  OG  . SER   B 112 ? 0.1863 0.1556 0.1565 -0.0220 0.0099  -0.0102 112 SER   B OG  
1580 N  N   . PRO   B 113 ? 0.1122 0.1034 0.1389 0.0143  -0.0001 -0.0061 113 PRO   B N   
1581 C  CA  . PRO   B 113 ? 0.0959 0.1007 0.1475 -0.0074 -0.0017 -0.0128 113 PRO   B CA  
1582 C  C   . PRO   B 113 ? 0.1168 0.1116 0.1367 0.0183  0.0201  -0.0043 113 PRO   B C   
1583 O  O   . PRO   B 113 ? 0.1345 0.1080 0.1586 0.0023  0.0114  -0.0004 113 PRO   B O   
1584 C  CB  . PRO   B 113 ? 0.1174 0.1497 0.1579 0.0203  -0.0010 -0.0068 113 PRO   B CB  
1585 C  CG  . PRO   B 113 ? 0.1322 0.1457 0.1919 0.0264  -0.0129 0.0100  113 PRO   B CG  
1586 C  CD  . PRO   B 113 ? 0.1146 0.1356 0.1585 0.0000  -0.0095 -0.0041 113 PRO   B CD  
1587 N  N   . TYR   B 114 ? 0.1166 0.1033 0.1353 0.0024  0.0167  -0.0019 114 TYR   B N   
1588 C  CA  . TYR   B 114 ? 0.1085 0.1065 0.1233 0.0002  0.0096  0.0007  114 TYR   B CA  
1589 C  C   . TYR   B 114 ? 0.1046 0.1054 0.1433 -0.0039 0.0022  0.0227  114 TYR   B C   
1590 O  O   . TYR   B 114 ? 0.1200 0.1960 0.1420 0.0041  -0.0087 0.0338  114 TYR   B O   
1591 C  CB  . TYR   B 114 ? 0.1168 0.1098 0.1527 0.0134  0.0041  0.0088  114 TYR   B CB  
1592 C  CG  . TYR   B 114 ? 0.1397 0.1207 0.1247 0.0136  0.0166  -0.0048 114 TYR   B CG  
1593 C  CD1 . TYR   B 114 ? 0.1379 0.2778 0.1770 0.0546  0.0185  0.0437  114 TYR   B CD1 
1594 C  CD2 . TYR   B 114 ? 0.1428 0.1155 0.1440 0.0125  0.0324  -0.0072 114 TYR   B CD2 
1595 C  CE1 . TYR   B 114 ? 0.1536 0.3625 0.2408 0.0369  0.0291  0.0509  114 TYR   B CE1 
1596 C  CE2 . TYR   B 114 ? 0.1579 0.1772 0.1525 -0.0164 0.0243  -0.0071 114 TYR   B CE2 
1597 C  CZ  . TYR   B 114 ? 0.1326 0.3269 0.2349 -0.0023 0.0138  0.0533  114 TYR   B CZ  
1598 O  OH  . TYR   B 114 ? 0.1805 0.3899 0.3432 -0.0389 0.0878  -0.0134 114 TYR   B OH  
1599 N  N   . SER   B 115 ? 0.0956 0.1291 0.1417 0.0118  0.0074  0.0223  115 SER   B N   
1600 C  CA  . SER   B 115 ? 0.1053 0.1158 0.1216 0.0124  0.0081  0.0107  115 SER   B CA  
1601 C  C   . SER   B 115 ? 0.0907 0.1362 0.1429 0.0124  -0.0007 0.0270  115 SER   B C   
1602 O  O   . SER   B 115 ? 0.1141 0.2040 0.1491 0.0204  0.0013  0.0313  115 SER   B O   
1603 C  CB  . SER   B 115 ? 0.1370 0.1300 0.1418 0.0219  -0.0225 0.0053  115 SER   B CB  
1604 O  OG  . SER   B 115 ? 0.1824 0.1648 0.2439 -0.0265 -0.0217 0.0130  115 SER   B OG  
1605 N  N   . TYR   B 116 ? 0.1054 0.1365 0.1186 0.0184  0.0015  0.0221  116 TYR   B N   
1606 C  CA  . TYR   B 116 ? 0.0917 0.1552 0.1246 0.0029  -0.0010 0.0115  116 TYR   B CA  
1607 C  C   . TYR   B 116 ? 0.0947 0.1326 0.1382 0.0231  -0.0071 -0.0072 116 TYR   B C   
1608 O  O   . TYR   B 116 ? 0.1042 0.1414 0.1241 0.0125  -0.0025 0.0029  116 TYR   B O   
1609 C  CB  . TYR   B 116 ? 0.1001 0.1861 0.1476 0.0098  -0.0178 0.0151  116 TYR   B CB  
1610 C  CG  . TYR   B 116 ? 0.1483 0.1612 0.1588 -0.0222 -0.0070 -0.0102 116 TYR   B CG  
1611 C  CD1 . TYR   B 116 ? 0.2214 0.1576 0.1781 -0.0374 0.0071  -0.0129 116 TYR   B CD1 
1612 C  CD2 . TYR   B 116 ? 0.1763 0.1618 0.1815 0.0060  -0.0011 -0.0045 116 TYR   B CD2 
1613 C  CE1 . TYR   B 116 ? 0.3128 0.1892 0.2208 -0.0210 0.0283  0.0230  116 TYR   B CE1 
1614 C  CE2 . TYR   B 116 ? 0.2299 0.2040 0.2145 0.0231  0.0440  0.0415  116 TYR   B CE2 
1615 C  CZ  . TYR   B 116 ? 0.2275 0.1792 0.2327 0.0395  0.0341  0.0438  116 TYR   B CZ  
1616 O  OH  . TYR   B 116 ? 0.3104 0.1968 0.3004 0.0520  0.0444  0.0717  116 TYR   B OH  
1617 N  N   . SER   B 117 ? 0.1125 0.1549 0.1290 0.0029  0.0103  0.0075  117 SER   B N   
1618 C  CA  . SER   B 117 ? 0.0726 0.1969 0.1321 0.0104  0.0094  -0.0043 117 SER   B CA  
1619 C  C   . SER   B 117 ? 0.1108 0.1594 0.1266 0.0300  -0.0036 -0.0032 117 SER   B C   
1620 O  O   . SER   B 117 ? 0.1202 0.2396 0.1305 0.0686  -0.0081 -0.0080 117 SER   B O   
1621 C  CB  . SER   B 117 ? 0.1328 0.2217 0.2206 -0.0626 0.0397  -0.0963 117 SER   B CB  
1622 O  OG  . SER   B 117 ? 0.1672 0.2513 0.2312 -0.0371 0.0009  -0.0276 117 SER   B OG  
1623 N  N   . THR   B 118 ? 0.0956 0.1640 0.1434 0.0209  0.0085  -0.0113 118 THR   B N   
1624 C  CA  . THR   B 118 ? 0.1122 0.1568 0.1405 0.0241  -0.0005 -0.0116 118 THR   B CA  
1625 C  C   . THR   B 118 ? 0.1087 0.1591 0.1289 0.0370  -0.0118 -0.0089 118 THR   B C   
1626 O  O   . THR   B 118 ? 0.1014 0.2092 0.1507 0.0274  0.0084  -0.0062 118 THR   B O   
1627 C  CB  . THR   B 118 ? 0.1069 0.1830 0.1538 0.0125  0.0146  -0.0023 118 THR   B CB  
1628 O  OG1 . THR   B 118 ? 0.1398 0.1474 0.1578 0.0103  -0.0067 -0.0225 118 THR   B OG1 
1629 C  CG2 . THR   B 118 ? 0.1456 0.1650 0.1534 0.0201  -0.0084 -0.0001 118 THR   B CG2 
1630 N  N   . THR   B 119 ? 0.1117 0.1453 0.1483 0.0161  0.0057  -0.0046 119 THR   B N   
1631 C  CA  . THR   B 119 ? 0.1438 0.1403 0.1502 0.0122  0.0330  -0.0234 119 THR   B CA  
1632 C  C   . THR   B 119 ? 0.1016 0.1403 0.1532 -0.0063 0.0068  -0.0193 119 THR   B C   
1633 O  O   . THR   B 119 ? 0.1193 0.2198 0.1636 0.0054  0.0115  -0.0397 119 THR   B O   
1634 C  CB  . THR   B 119 ? 0.1275 0.1723 0.2417 0.0323  0.0072  -0.0260 119 THR   B CB  
1635 O  OG1 . THR   B 119 ? 0.1500 0.2008 0.1982 0.0086  -0.0016 -0.0424 119 THR   B OG1 
1636 C  CG2 . THR   B 119 ? 0.1724 0.1872 0.2131 0.0587  -0.0232 -0.0531 119 THR   B CG2 
1637 N  N   . ALA   B 120 ? 0.1204 0.1534 0.1449 -0.0056 0.0140  -0.0420 120 ALA   B N   
1638 C  CA  . ALA   B 120 ? 0.1156 0.1590 0.1620 -0.0011 0.0247  -0.0476 120 ALA   B CA  
1639 C  C   . ALA   B 120 ? 0.1324 0.1765 0.1682 -0.0271 0.0231  -0.0463 120 ALA   B C   
1640 O  O   . ALA   B 120 ? 0.1560 0.2207 0.1827 -0.0641 0.0378  -0.0493 120 ALA   B O   
1641 C  CB  . ALA   B 120 ? 0.1588 0.2023 0.2318 0.0306  0.0273  -0.0376 120 ALA   B CB  
1642 N  N   . VAL   B 121 ? 0.1520 0.2487 0.1426 -0.0748 0.0288  -0.0452 121 VAL   B N   
1643 C  CA  . VAL   B 121 ? 0.2256 0.3141 0.1709 -0.1341 0.0267  -0.0622 121 VAL   B CA  
1644 C  C   . VAL   B 121 ? 0.2184 0.3866 0.1766 -0.1305 0.0633  -0.0837 121 VAL   B C   
1645 O  O   . VAL   B 121 ? 0.2431 0.4135 0.2207 -0.1339 0.0732  -0.1363 121 VAL   B O   
1646 C  CB  . VAL   B 121 ? 0.2842 0.3384 0.2037 -0.1355 0.0023  0.0221  121 VAL   B CB  
1647 C  CG1 . VAL   B 121 ? 0.4485 0.3460 0.2467 -0.1517 0.0467  0.0127  121 VAL   B CG1 
1648 C  CG2 . VAL   B 121 ? 0.3140 0.3366 0.2700 -0.0377 -0.0708 0.0911  121 VAL   B CG2 
1649 N  N   . VAL   B 122 ? 0.2413 0.3776 0.1792 -0.1363 0.0627  -0.0906 122 VAL   B N   
1650 C  CA  . VAL   B 122 ? 0.2422 0.4105 0.2598 -0.1367 0.0139  -0.1273 122 VAL   B CA  
1651 C  C   . VAL   B 122 ? 0.2897 0.4278 0.3252 -0.1201 0.0696  -0.0629 122 VAL   B C   
1652 O  O   . VAL   B 122 ? 0.2293 0.4402 0.2719 -0.0881 0.0772  -0.0402 122 VAL   B O   
1653 C  CB  . VAL   B 122 ? 0.2696 0.4227 0.3087 -0.0856 0.0959  -0.0844 122 VAL   B CB  
1654 C  CG1 . VAL   B 122 ? 0.4303 0.4345 0.4139 0.0541  0.0755  -0.1066 122 VAL   B CG1 
1655 C  CG2 . VAL   B 122 ? 0.2254 0.3548 0.2964 -0.0413 0.0644  -0.0425 122 VAL   B CG2 
1656 N  N   . THR   B 123 ? 0.2979 0.4814 0.2843 -0.1278 0.0888  -0.0510 123 THR   B N   
1657 C  CA  . THR   B 123 ? 0.3226 0.3672 0.3146 -0.0137 0.0667  0.0066  123 THR   B CA  
1658 C  C   . THR   B 123 ? 0.7228 0.2738 0.4899 0.1065  -0.0254 -0.1720 123 THR   B C   
1659 O  O   . THR   B 123 ? 0.4603 0.4310 0.3451 -0.1059 0.2164  -0.1213 123 THR   B O   
1660 C  CB  . THR   B 123 ? 0.2924 0.2733 0.3312 -0.0114 0.0819  -0.0175 123 THR   B CB  
1661 O  OG1 . THR   B 123 ? 0.4708 0.4759 0.3993 -0.0116 0.0352  -0.1178 123 THR   B OG1 
1662 C  CG2 . THR   B 123 ? 0.3409 0.3263 0.3549 -0.0020 0.1103  -0.0535 123 THR   B CG2 
1663 CA CA  . CA    C .   ? 0.1905 0.2481 0.2895 -0.0059 -0.0179 0.0441  201 CA    A CA  
1664 C  C5  . A1IS0 D .   ? 0.2286 0.1776 0.2186 -0.0263 -0.0598 -0.0489 202 A1IS0 A C5  
1665 C  C6  . A1IS0 D .   ? 0.1971 0.2190 0.2597 -0.0325 -0.0055 -0.0521 202 A1IS0 A C6  
1666 C  C4  . A1IS0 D .   ? 0.2666 0.2575 0.1963 -0.0296 0.0228  0.0262  202 A1IS0 A C4  
1667 C  C3  . A1IS0 D .   ? 0.2745 0.2915 0.2415 0.0823  0.0183  0.0010  202 A1IS0 A C3  
1668 C  C2  . A1IS0 D .   ? 0.1170 0.2279 0.2627 -0.0510 0.0594  -0.0016 202 A1IS0 A C2  
1669 C  C1  . A1IS0 D .   ? 0.1424 0.2049 0.2547 0.0464  0.0338  0.0042  202 A1IS0 A C1  
1670 C  C9  . A1IS0 D .   ? 0.2252 0.3535 0.2612 0.0031  -0.0013 0.0014  202 A1IS0 A C9  
1671 C  C11 . A1IS0 D .   ? 0.1543 0.1842 0.2016 -0.0024 -0.0234 -0.0122 202 A1IS0 A C11 
1672 C  C10 . A1IS0 D .   ? 0.1662 0.2062 0.2222 -0.0026 0.0485  0.0042  202 A1IS0 A C10 
1673 N  N3  . A1IS0 D .   ? 0.1965 0.1839 0.2167 -0.0488 -0.0241 0.0246  202 A1IS0 A N3  
1674 N  N1  . A1IS0 D .   ? 0.1654 0.1739 0.2074 0.0177  -0.0142 0.0031  202 A1IS0 A N1  
1675 N  N2  . A1IS0 D .   ? 0.1710 0.2134 0.2498 0.0306  -0.0011 -0.0130 202 A1IS0 A N2  
1676 N  N   . A1IS0 D .   ? 0.1358 0.1632 0.2373 0.0006  0.0443  0.0065  202 A1IS0 A N   
1677 C  C   . A1IS0 D .   ? 0.2025 0.2489 0.2133 0.0590  0.0272  -0.0396 202 A1IS0 A C   
1678 C  C8  . A1IS0 D .   ? 0.2195 0.2966 0.2413 -0.0708 0.0714  0.0178  202 A1IS0 A C8  
1679 C  C7  . A1IS0 D .   ? 0.1380 0.2314 0.2860 -0.0822 -0.0712 0.0350  202 A1IS0 A C7  
1680 CA CA  . CA    E .   ? 0.4664 0.5831 0.3784 0.0102  0.0109  -0.1210 201 CA    B CA  
1681 C  C5  . A1IS0 F .   ? 0.1783 0.3605 0.2520 0.0147  0.0186  -0.0295 202 A1IS0 B C5  
1682 C  C6  . A1IS0 F .   ? 0.2184 0.2659 0.3044 0.0466  -0.0106 -0.0534 202 A1IS0 B C6  
1683 C  C4  . A1IS0 F .   ? 0.2177 0.2495 0.3114 0.0641  -0.0328 0.0457  202 A1IS0 B C4  
1684 C  C3  . A1IS0 F .   ? 0.3017 0.3080 0.2225 -0.0190 -0.0226 -0.0074 202 A1IS0 B C3  
1685 C  C2  . A1IS0 F .   ? 0.1359 0.2512 0.2677 0.0148  -0.0031 0.0010  202 A1IS0 B C2  
1686 C  C1  . A1IS0 F .   ? 0.1512 0.2419 0.2662 -0.0071 -0.0568 0.0171  202 A1IS0 B C1  
1687 C  C9  . A1IS0 F .   ? 0.2710 0.3340 0.2892 -0.0185 0.0035  0.0026  202 A1IS0 B C9  
1688 C  C11 . A1IS0 F .   ? 0.0990 0.2551 0.2220 0.0020  -0.0300 0.0048  202 A1IS0 B C11 
1689 C  C10 . A1IS0 F .   ? 0.2460 0.2624 0.2819 0.0000  0.0009  0.0001  202 A1IS0 B C10 
1690 N  N3  . A1IS0 F .   ? 0.1603 0.2730 0.2195 0.0289  0.0072  0.0150  202 A1IS0 B N3  
1691 N  N1  . A1IS0 F .   ? 0.2436 0.2221 0.2626 -0.0141 0.0209  0.0166  202 A1IS0 B N1  
1692 N  N2  . A1IS0 F .   ? 0.1697 0.2420 0.2482 -0.0772 0.0359  0.0174  202 A1IS0 B N2  
1693 N  N   . A1IS0 F .   ? 0.2295 0.2265 0.2772 -0.0432 -0.0270 0.0030  202 A1IS0 B N   
1694 C  C   . A1IS0 F .   ? 0.2071 0.3210 0.2474 0.0127  -0.0811 0.0125  202 A1IS0 B C   
1695 C  C8  . A1IS0 F .   ? 0.2893 0.3946 0.2659 -0.0263 -0.0197 -0.0048 202 A1IS0 B C8  
1696 C  C7  . A1IS0 F .   ? 0.2985 0.2659 0.2995 -0.0469 0.0188  0.0195  202 A1IS0 B C7  
1697 O  O   . HOH   G .   ? 0.3545 0.1715 0.2811 0.0622  -0.0274 0.0588  301 HOH   A O   
1698 O  O   . HOH   G .   ? 0.3234 0.3783 0.3235 0.1057  -0.0152 -0.1785 302 HOH   A O   
1699 O  O   . HOH   G .   ? 0.3156 0.2005 0.2310 0.0023  0.0126  0.0000  303 HOH   A O   
1700 O  O   . HOH   G .   ? 0.2998 0.4112 0.4225 0.0261  0.0968  0.0034  304 HOH   A O   
1701 O  O   . HOH   G .   ? 0.1392 0.1478 0.1680 0.0027  0.0000  0.0275  305 HOH   A O   
1702 O  O   . HOH   G .   ? 0.1953 0.1582 0.2318 0.0000  0.0020  0.0295  306 HOH   A O   
1703 O  O   . HOH   G .   ? 0.2283 0.1999 0.2524 0.0030  -0.0257 0.0408  307 HOH   A O   
1704 O  O   . HOH   G .   ? 0.3409 0.3373 0.1983 -0.0149 0.0155  -0.0210 308 HOH   A O   
1705 O  O   . HOH   G .   ? 0.2985 0.1699 0.2028 0.0621  -0.0623 -0.0435 309 HOH   A O   
1706 O  O   . HOH   G .   ? 0.1854 0.1948 0.3813 0.0280  -0.0086 0.0174  310 HOH   A O   
1707 O  O   . HOH   G .   ? 0.2979 0.2208 0.3573 -0.1246 0.1385  -0.1224 311 HOH   A O   
1708 O  O   . HOH   G .   ? 0.2660 0.2219 0.2360 0.0381  -0.0141 -0.0098 312 HOH   A O   
1709 O  O   . HOH   G .   ? 0.2116 0.1168 0.3932 -0.0026 0.0966  0.0065  313 HOH   A O   
1710 O  O   . HOH   G .   ? 0.1868 0.1816 0.2332 -0.0227 0.0038  0.0432  314 HOH   A O   
1711 O  O   . HOH   G .   ? 0.1467 0.1975 0.1401 -0.0180 0.0119  -0.0076 315 HOH   A O   
1712 O  O   . HOH   G .   ? 0.2450 0.2648 0.3256 -0.0562 -0.0024 -0.0218 316 HOH   A O   
1713 O  O   . HOH   G .   ? 0.3518 0.2427 0.3060 0.0728  -0.1089 -0.0173 317 HOH   A O   
1714 O  O   . HOH   G .   ? 0.2467 0.2068 0.3571 -0.0049 0.0260  0.0176  318 HOH   A O   
1715 O  O   . HOH   G .   ? 0.1811 0.1496 0.2495 -0.0012 -0.0009 -0.0140 319 HOH   A O   
1716 O  O   . HOH   G .   ? 0.2138 0.1959 0.2066 -0.0099 0.0049  0.0086  320 HOH   A O   
1717 O  O   . HOH   G .   ? 0.1340 0.1413 0.1974 0.0133  0.0094  -0.0059 321 HOH   A O   
1718 O  O   . HOH   G .   ? 0.1924 0.1495 0.1503 -0.0299 0.0036  -0.0003 322 HOH   A O   
1719 O  O   . HOH   G .   ? 0.3239 0.1572 0.2987 -0.0180 0.0609  0.0416  323 HOH   A O   
1720 O  O   . HOH   G .   ? 0.1634 0.2485 0.2707 -0.0166 -0.0148 0.0981  324 HOH   A O   
1721 O  O   . HOH   G .   ? 0.1773 0.1906 0.2439 0.0256  0.0387  0.0655  325 HOH   A O   
1722 O  O   . HOH   G .   ? 0.2365 0.1783 0.2464 0.0508  0.0785  0.0690  326 HOH   A O   
1723 O  O   . HOH   G .   ? 0.2201 0.3332 0.2684 -0.0353 0.0376  0.0186  327 HOH   A O   
1724 O  O   . HOH   G .   ? 0.3144 0.1323 0.2995 0.0446  0.0638  0.0625  328 HOH   A O   
1725 O  O   . HOH   G .   ? 0.1848 0.1387 0.2171 -0.0076 -0.0049 0.0411  329 HOH   A O   
1726 O  O   . HOH   G .   ? 0.1270 0.1687 0.1532 0.0067  0.0171  0.0103  330 HOH   A O   
1727 O  O   . HOH   G .   ? 0.2448 0.1361 0.1773 -0.0396 0.0350  0.0137  331 HOH   A O   
1728 O  O   . HOH   G .   ? 0.2293 0.1593 0.2003 -0.0158 -0.0034 0.0398  332 HOH   A O   
1729 O  O   . HOH   G .   ? 0.3213 0.1386 0.2324 -0.0145 0.0154  0.0286  333 HOH   A O   
1730 O  O   . HOH   G .   ? 0.1766 0.1518 0.2212 0.0179  -0.0198 0.0083  334 HOH   A O   
1731 O  O   . HOH   G .   ? 0.2537 0.3210 0.4101 -0.0615 0.0783  -0.0331 335 HOH   A O   
1732 O  O   . HOH   G .   ? 0.4791 0.2787 0.2271 -0.1363 -0.0105 -0.0007 336 HOH   A O   
1733 O  O   . HOH   G .   ? 0.1858 0.2433 0.2772 -0.0177 0.0353  0.0680  337 HOH   A O   
1734 O  O   . HOH   G .   ? 0.1967 0.1533 0.1982 -0.0129 -0.0022 0.0147  338 HOH   A O   
1735 O  O   . HOH   G .   ? 0.2268 0.1997 0.2574 0.0107  0.0116  0.0370  339 HOH   A O   
1736 O  O   . HOH   G .   ? 0.3440 0.3274 0.2732 0.1199  -0.0765 -0.0257 340 HOH   A O   
1737 O  O   . HOH   G .   ? 0.2044 0.1875 0.2264 0.0353  0.0287  0.0641  341 HOH   A O   
1738 O  O   . HOH   G .   ? 0.3975 0.3561 0.3232 0.0169  -0.0525 -0.1247 342 HOH   A O   
1739 O  O   . HOH   G .   ? 0.2177 0.3359 0.1776 0.0032  -0.0240 0.0231  343 HOH   A O   
1740 O  O   . HOH   G .   ? 0.2198 0.1781 0.2632 0.0280  0.0054  0.0126  344 HOH   A O   
1741 O  O   . HOH   G .   ? 0.3094 0.3359 0.3715 -0.0260 -0.0843 0.0759  345 HOH   A O   
1742 O  O   . HOH   G .   ? 0.4632 0.3009 0.4081 0.1560  0.2017  0.1630  346 HOH   A O   
1743 O  O   . HOH   G .   ? 0.4411 0.2885 0.3390 0.0673  0.0793  0.1337  347 HOH   A O   
1744 O  O   . HOH   G .   ? 0.6405 0.2213 0.2764 0.0517  -0.1310 0.0267  348 HOH   A O   
1745 O  O   . HOH   G .   ? 0.3891 0.2178 0.2270 0.0225  -0.0463 0.0080  349 HOH   A O   
1746 O  O   . HOH   G .   ? 0.2093 0.2641 0.3376 0.0036  0.0308  0.0507  350 HOH   A O   
1747 O  O   . HOH   G .   ? 0.3346 0.2191 0.3305 -0.0645 0.0828  0.0225  351 HOH   A O   
1748 O  O   . HOH   G .   ? 0.3165 0.2794 0.4045 0.0530  -0.0575 0.0004  352 HOH   A O   
1749 O  O   . HOH   G .   ? 0.3793 0.2656 0.3153 0.0787  -0.0263 0.0719  353 HOH   A O   
1750 O  O   . HOH   G .   ? 0.1815 0.1775 0.2386 0.0015  0.0008  0.0205  354 HOH   A O   
1751 O  O   . HOH   G .   ? 0.2567 0.2378 0.4407 0.0218  0.0318  -0.0423 355 HOH   A O   
1752 O  O   . HOH   G .   ? 0.3712 0.1992 0.2467 0.0121  -0.0810 0.0539  356 HOH   A O   
1753 O  O   . HOH   G .   ? 0.3179 0.3031 0.2814 -0.0611 0.0115  0.0317  357 HOH   A O   
1754 O  O   . HOH   G .   ? 0.2983 0.3692 0.3456 0.0060  -0.0510 0.0965  358 HOH   A O   
1755 O  O   . HOH   G .   ? 0.4542 0.2937 0.2836 0.1455  0.0800  0.0537  359 HOH   A O   
1756 O  O   . HOH   G .   ? 0.3916 0.2414 0.3196 0.0018  0.0454  -0.0304 360 HOH   A O   
1757 O  O   . HOH   H .   ? 0.3151 0.2459 0.2750 -0.0210 -0.0179 0.0176  301 HOH   B O   
1758 O  O   . HOH   H .   ? 0.3167 0.3320 0.3462 -0.0136 0.0839  -0.1303 302 HOH   B O   
1759 O  O   . HOH   H .   ? 0.3300 0.2856 0.4409 -0.0121 0.0329  0.0577  303 HOH   B O   
1760 O  O   . HOH   H .   ? 0.3434 0.3097 0.3350 0.0058  0.1012  -0.1037 304 HOH   B O   
1761 O  O   . HOH   H .   ? 0.3053 0.3575 0.3764 0.0815  -0.0427 -0.0204 305 HOH   B O   
1762 O  O   . HOH   H .   ? 0.3061 0.2681 0.3371 -0.0205 0.0491  -0.0465 306 HOH   B O   
1763 O  O   . HOH   H .   ? 0.2220 0.2316 0.2420 0.0100  -0.0160 0.0863  307 HOH   B O   
1764 O  O   . HOH   H .   ? 0.1847 0.1985 0.1496 0.0882  0.0226  0.0286  308 HOH   B O   
1765 O  O   . HOH   H .   ? 0.3570 0.2404 0.4753 0.0627  0.0297  -0.1057 309 HOH   B O   
1766 O  O   . HOH   H .   ? 0.2648 0.3002 0.2934 0.0020  0.0086  -0.0350 310 HOH   B O   
1767 O  O   . HOH   H .   ? 0.1504 0.2003 0.4096 0.0464  0.0333  0.0103  311 HOH   B O   
1768 O  O   . HOH   H .   ? 0.2840 0.3126 0.5285 0.0260  0.0107  -0.1523 312 HOH   B O   
1769 O  O   . HOH   H .   ? 0.1576 0.1509 0.1853 0.0365  0.0137  -0.0025 313 HOH   B O   
1770 O  O   . HOH   H .   ? 0.2859 0.1700 0.1660 0.1039  0.0356  0.0097  314 HOH   B O   
1771 O  O   . HOH   H .   ? 0.3151 0.4110 0.3024 -0.0078 0.0064  -0.1916 315 HOH   B O   
1772 O  O   . HOH   H .   ? 0.1792 0.2403 0.4835 0.0604  -0.0788 -0.0418 316 HOH   B O   
1773 O  O   . HOH   H .   ? 0.3541 0.4206 0.2453 0.0175  -0.0018 -0.0424 317 HOH   B O   
1774 O  O   . HOH   H .   ? 0.1329 0.1370 0.1625 0.0192  0.0115  -0.0106 318 HOH   B O   
1775 O  O   . HOH   H .   ? 0.1993 0.2315 0.2401 -0.0220 0.0188  -0.0440 319 HOH   B O   
1776 O  O   . HOH   H .   ? 0.2030 0.2845 0.2343 0.0239  0.0350  -0.0108 320 HOH   B O   
1777 O  O   . HOH   H .   ? 0.1954 0.1391 0.1577 -0.0119 0.0117  0.0263  321 HOH   B O   
1778 O  O   . HOH   H .   ? 0.2293 0.1848 0.2075 0.0168  0.0036  0.0168  322 HOH   B O   
1779 O  O   . HOH   H .   ? 0.2368 0.2763 0.4407 -0.0706 -0.0190 -0.0692 323 HOH   B O   
1780 O  O   . HOH   H .   ? 0.2299 0.4272 0.3103 -0.0016 -0.0564 0.1134  324 HOH   B O   
1781 O  O   . HOH   H .   ? 0.2896 0.5713 0.2463 0.0776  -0.0174 -0.0422 325 HOH   B O   
1782 O  O   . HOH   H .   ? 0.1862 0.3040 0.3179 0.0636  -0.0314 -0.0692 326 HOH   B O   
1783 O  O   . HOH   H .   ? 0.2608 0.3946 0.3712 0.0847  -0.0114 -0.1573 327 HOH   B O   
1784 O  O   . HOH   H .   ? 0.2031 0.4243 0.4242 0.0011  0.0062  -0.0964 328 HOH   B O   
1785 O  O   . HOH   H .   ? 0.3975 0.3345 0.3331 0.0205  -0.0739 -0.0089 329 HOH   B O   
1786 O  O   . HOH   H .   ? 0.1644 0.2734 0.3080 -0.0213 0.0021  -0.0964 330 HOH   B O   
1787 O  O   . HOH   H .   ? 0.3818 0.4187 0.2029 0.0434  -0.0461 -0.0874 331 HOH   B O   
1788 O  O   . HOH   H .   ? 0.2905 0.4215 0.2704 0.0206  -0.0742 -0.0256 332 HOH   B O   
1789 O  O   . HOH   H .   ? 0.1757 0.2094 0.2021 -0.0143 -0.0008 0.0296  333 HOH   B O   
1790 O  O   . HOH   H .   ? 0.3577 0.3818 0.2761 0.0009  -0.0759 -0.0169 334 HOH   B O   
1791 O  O   . HOH   H .   ? 0.3934 0.2694 0.3778 -0.0974 -0.1774 0.1329  335 HOH   B O   
1792 O  O   . HOH   H .   ? 0.3399 0.5681 0.3234 0.0893  0.0082  -0.1239 336 HOH   B O   
1793 O  O   . HOH   H .   ? 0.4230 0.2602 0.2802 0.0317  -0.0135 -0.1211 337 HOH   B O   
1794 O  O   . HOH   H .   ? 0.3397 0.1827 0.2860 -0.0347 -0.0159 0.0025  338 HOH   B O   
# 
