data_9DA3
# 
_entry.id   9DA3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DA3         pdb_00009da3 10.2210/pdb9da3/pdb 
WWPDB D_1000287621 ?            ?                   
# 
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 2025-02-05 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_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 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DA3 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'CRYSTAL STRUCTURE OF HUMAN DNPH1 (RCL) WITH 6-NAPHTHYL-PURINE-RIBOSIDE-MONOPHOSPHATE' 4P5E unspecified 
PDB 'Crystal structure of human DNPH1 bound to hmdUMP'                                     8QHQ unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              agnidipta.ghosh@einsteinmed.edu 
_pdbx_contact_author.name_first         Agnidipta 
_pdbx_contact_author.name_last          Ghosh 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7753-0240 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wagner, A.G.'  1 0000-0003-4786-7747 
'Schramm, V.L.' 2 0000-0002-8056-1929 
'Almo, S.C.'    3 0000-0003-2591-5234 
'Ghosh, A.'     4 0000-0002-7753-0240 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                3653 
_citation.page_last                 3672 
_citation.title                     'Transition State Analogs of Human DNPH1 Reveal Two Electrophile Migration Mechanisms.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02778 
_citation.pdbx_database_id_PubMed   39818772 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wagner, A.G.'         1  ? 
primary 'Lang, T.B.D.'         2  ? 
primary 'Ledingham, E.T.'      3  ? 
primary 'Ghosh, A.'            4  ? 
primary 'Brooks, D.'           5  ? 
primary 'Eskandari, R.'        6  ? 
primary 'Suthagar, K.'         7  ? 
primary 'Almo, S.C.'           8  ? 
primary 'Lamiable-Oulaidi, F.' 9  ? 
primary 'Tyler, P.C.'          10 ? 
primary 'Schramm, V.L.'        11 ? 
# 
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 '5-hydroxymethyl-dUMP N-hydrolase' 16224.247 2   3.2.2.- ? ? ? 
2 non-polymer syn 
'[(3R,4R)-4-hydroxy-1-{[5-(hydroxymethyl)-6-oxo-1,6-dihydropyridin-3-yl]methyl}pyrrolidin-3-yl]methyl dihydrogen phosphate' 
334.262   2   ?       ? ? ? 
3 water       nat water 18.015    166 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;2'-deoxynucleoside 5'-phosphate N-hydrolase 1,c-Myc-responsive protein RCL
;
# 
_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       
;SMRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQP
SLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQP
SLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_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 '[(3R,4R)-4-hydroxy-1-{[5-(hydroxymethyl)-6-oxo-1,6-dihydropyridin-3-yl]methyl}pyrrolidin-3-yl]methyl dihydrogen phosphate' 
A1BBD 
3 water                                                                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   ARG n 
1 4   PRO n 
1 5   ALA n 
1 6   LEU n 
1 7   TYR n 
1 8   PHE n 
1 9   CYS n 
1 10  GLY n 
1 11  SER n 
1 12  ILE n 
1 13  ARG n 
1 14  GLY n 
1 15  GLY n 
1 16  ARG n 
1 17  GLU n 
1 18  ASP n 
1 19  ARG n 
1 20  THR n 
1 21  LEU n 
1 22  TYR n 
1 23  GLU n 
1 24  ARG n 
1 25  ILE n 
1 26  VAL n 
1 27  SER n 
1 28  ARG n 
1 29  LEU n 
1 30  ARG n 
1 31  ARG n 
1 32  PHE n 
1 33  GLY n 
1 34  THR n 
1 35  VAL n 
1 36  LEU n 
1 37  THR n 
1 38  GLU n 
1 39  HIS n 
1 40  VAL n 
1 41  ALA n 
1 42  ALA n 
1 43  ALA n 
1 44  GLU n 
1 45  LEU n 
1 46  GLY n 
1 47  ALA n 
1 48  ARG n 
1 49  GLY n 
1 50  GLU n 
1 51  GLU n 
1 52  ALA n 
1 53  ALA n 
1 54  GLY n 
1 55  GLY n 
1 56  ASP n 
1 57  ARG n 
1 58  LEU n 
1 59  ILE n 
1 60  HIS n 
1 61  GLU n 
1 62  GLN n 
1 63  ASP n 
1 64  LEU n 
1 65  GLU n 
1 66  TRP n 
1 67  LEU n 
1 68  GLN n 
1 69  GLN n 
1 70  ALA n 
1 71  ASP n 
1 72  VAL n 
1 73  VAL n 
1 74  VAL n 
1 75  ALA n 
1 76  GLU n 
1 77  VAL n 
1 78  THR n 
1 79  GLN n 
1 80  PRO n 
1 81  SER n 
1 82  LEU n 
1 83  GLY n 
1 84  VAL n 
1 85  GLY n 
1 86  TYR n 
1 87  GLU n 
1 88  LEU n 
1 89  GLY n 
1 90  ARG n 
1 91  ALA n 
1 92  VAL n 
1 93  ALA n 
1 94  PHE n 
1 95  ASN n 
1 96  LYS n 
1 97  ARG n 
1 98  ILE n 
1 99  LEU n 
1 100 CYS n 
1 101 LEU n 
1 102 PHE n 
1 103 ARG n 
1 104 PRO n 
1 105 GLN n 
1 106 SER n 
1 107 GLY n 
1 108 ARG n 
1 109 VAL n 
1 110 LEU n 
1 111 SER n 
1 112 ALA n 
1 113 MET n 
1 114 ILE n 
1 115 ARG n 
1 116 GLY n 
1 117 ALA n 
1 118 ALA n 
1 119 ASP n 
1 120 GLY n 
1 121 SER n 
1 122 ARG n 
1 123 PHE n 
1 124 GLN n 
1 125 VAL n 
1 126 TRP n 
1 127 ASP n 
1 128 TYR n 
1 129 GLU n 
1 130 GLU n 
1 131 GLY n 
1 132 GLU n 
1 133 VAL n 
1 134 GLU n 
1 135 ALA n 
1 136 LEU n 
1 137 LEU n 
1 138 ASP n 
1 139 ARG n 
1 140 TYR n 
1 141 PHE n 
1 142 GLU n 
1 143 ALA n 
1 144 ASP n 
1 145 PRO 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                   145 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DNPH1, C6orf108, RCL' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              pRIL 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   LIC 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET-28a(+)' 
_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 
A1BBD non-polymer         . 
'[(3R,4R)-4-hydroxy-1-{[5-(hydroxymethyl)-6-oxo-1,6-dihydropyridin-3-yl]methyl}pyrrolidin-3-yl]methyl dihydrogen phosphate' ? 
'C12 H19 N2 O7 P' 334.262 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
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   SER 1   18  ?   ?   ?   A . n 
A 1 2   MET 2   19  ?   ?   ?   A . n 
A 1 3   ARG 3   20  20  ARG ARG A . n 
A 1 4   PRO 4   21  21  PRO PRO A . n 
A 1 5   ALA 5   22  22  ALA ALA A . n 
A 1 6   LEU 6   23  23  LEU LEU A . n 
A 1 7   TYR 7   24  24  TYR TYR A . n 
A 1 8   PHE 8   25  25  PHE PHE A . n 
A 1 9   CYS 9   26  26  CYS CYS A . n 
A 1 10  GLY 10  27  27  GLY GLY A . n 
A 1 11  SER 11  28  28  SER SER A . n 
A 1 12  ILE 12  29  29  ILE ILE A . n 
A 1 13  ARG 13  30  30  ARG ARG A . n 
A 1 14  GLY 14  31  31  GLY GLY A . n 
A 1 15  GLY 15  32  32  GLY GLY A . n 
A 1 16  ARG 16  33  33  ARG ARG A . n 
A 1 17  GLU 17  34  34  GLU GLU A . n 
A 1 18  ASP 18  35  35  ASP ASP A . n 
A 1 19  ARG 19  36  36  ARG ARG A . n 
A 1 20  THR 20  37  37  THR THR A . n 
A 1 21  LEU 21  38  38  LEU LEU A . n 
A 1 22  TYR 22  39  39  TYR TYR A . n 
A 1 23  GLU 23  40  40  GLU GLU A . n 
A 1 24  ARG 24  41  41  ARG ARG A . n 
A 1 25  ILE 25  42  42  ILE ILE A . n 
A 1 26  VAL 26  43  43  VAL VAL A . n 
A 1 27  SER 27  44  44  SER SER A . n 
A 1 28  ARG 28  45  45  ARG ARG A . n 
A 1 29  LEU 29  46  46  LEU LEU A . n 
A 1 30  ARG 30  47  47  ARG ARG A . n 
A 1 31  ARG 31  48  48  ARG ARG A . n 
A 1 32  PHE 32  49  49  PHE PHE A . n 
A 1 33  GLY 33  50  50  GLY GLY A . n 
A 1 34  THR 34  51  51  THR THR A . n 
A 1 35  VAL 35  52  52  VAL VAL A . n 
A 1 36  LEU 36  53  53  LEU LEU A . n 
A 1 37  THR 37  54  54  THR THR A . n 
A 1 38  GLU 38  55  55  GLU GLU A . n 
A 1 39  HIS 39  56  ?   ?   ?   A . n 
A 1 40  VAL 40  57  ?   ?   ?   A . n 
A 1 41  ALA 41  58  ?   ?   ?   A . n 
A 1 42  ALA 42  59  ?   ?   ?   A . n 
A 1 43  ALA 43  60  ?   ?   ?   A . n 
A 1 44  GLU 44  61  ?   ?   ?   A . n 
A 1 45  LEU 45  62  ?   ?   ?   A . n 
A 1 46  GLY 46  63  ?   ?   ?   A . n 
A 1 47  ALA 47  64  ?   ?   ?   A . n 
A 1 48  ARG 48  65  ?   ?   ?   A . n 
A 1 49  GLY 49  66  ?   ?   ?   A . n 
A 1 50  GLU 50  67  ?   ?   ?   A . n 
A 1 51  GLU 51  68  ?   ?   ?   A . n 
A 1 52  ALA 52  69  ?   ?   ?   A . n 
A 1 53  ALA 53  70  ?   ?   ?   A . n 
A 1 54  GLY 54  71  71  GLY GLY A . n 
A 1 55  GLY 55  72  72  GLY GLY A . n 
A 1 56  ASP 56  73  73  ASP ASP A . n 
A 1 57  ARG 57  74  74  ARG ARG A . n 
A 1 58  LEU 58  75  75  LEU LEU A . n 
A 1 59  ILE 59  76  76  ILE ILE A . n 
A 1 60  HIS 60  77  77  HIS HIS A . n 
A 1 61  GLU 61  78  78  GLU GLU A . n 
A 1 62  GLN 62  79  79  GLN GLN A . n 
A 1 63  ASP 63  80  80  ASP ASP A . n 
A 1 64  LEU 64  81  81  LEU LEU A . n 
A 1 65  GLU 65  82  82  GLU GLU A . n 
A 1 66  TRP 66  83  83  TRP TRP A . n 
A 1 67  LEU 67  84  84  LEU LEU A . n 
A 1 68  GLN 68  85  85  GLN GLN A . n 
A 1 69  GLN 69  86  86  GLN GLN A . n 
A 1 70  ALA 70  87  87  ALA ALA A . n 
A 1 71  ASP 71  88  88  ASP ASP A . n 
A 1 72  VAL 72  89  89  VAL VAL A . n 
A 1 73  VAL 73  90  90  VAL VAL A . n 
A 1 74  VAL 74  91  91  VAL VAL A . n 
A 1 75  ALA 75  92  92  ALA ALA A . n 
A 1 76  GLU 76  93  93  GLU GLU A . n 
A 1 77  VAL 77  94  94  VAL VAL A . n 
A 1 78  THR 78  95  95  THR THR A . n 
A 1 79  GLN 79  96  96  GLN GLN A . n 
A 1 80  PRO 80  97  97  PRO PRO A . n 
A 1 81  SER 81  98  98  SER SER A . n 
A 1 82  LEU 82  99  99  LEU LEU A . n 
A 1 83  GLY 83  100 100 GLY GLY A . n 
A 1 84  VAL 84  101 101 VAL VAL A . n 
A 1 85  GLY 85  102 102 GLY GLY A . n 
A 1 86  TYR 86  103 103 TYR TYR A . n 
A 1 87  GLU 87  104 104 GLU GLU A . n 
A 1 88  LEU 88  105 105 LEU LEU A . n 
A 1 89  GLY 89  106 106 GLY GLY A . n 
A 1 90  ARG 90  107 107 ARG ARG A . n 
A 1 91  ALA 91  108 108 ALA ALA A . n 
A 1 92  VAL 92  109 109 VAL VAL A . n 
A 1 93  ALA 93  110 110 ALA ALA A . n 
A 1 94  PHE 94  111 111 PHE PHE A . n 
A 1 95  ASN 95  112 112 ASN ASN A . n 
A 1 96  LYS 96  113 113 LYS LYS A . n 
A 1 97  ARG 97  114 114 ARG ARG A . n 
A 1 98  ILE 98  115 115 ILE ILE A . n 
A 1 99  LEU 99  116 116 LEU LEU A . n 
A 1 100 CYS 100 117 117 CYS CYS A . n 
A 1 101 LEU 101 118 118 LEU LEU A . n 
A 1 102 PHE 102 119 119 PHE PHE A . n 
A 1 103 ARG 103 120 120 ARG ARG A . n 
A 1 104 PRO 104 121 121 PRO PRO A . n 
A 1 105 GLN 105 122 122 GLN GLN A . n 
A 1 106 SER 106 123 123 SER SER A . n 
A 1 107 GLY 107 124 124 GLY GLY A . n 
A 1 108 ARG 108 125 125 ARG ARG A . n 
A 1 109 VAL 109 126 126 VAL VAL A . n 
A 1 110 LEU 110 127 127 LEU LEU A . n 
A 1 111 SER 111 128 128 SER SER A . n 
A 1 112 ALA 112 129 129 ALA ALA A . n 
A 1 113 MET 113 130 130 MET MET A . n 
A 1 114 ILE 114 131 131 ILE ILE A . n 
A 1 115 ARG 115 132 132 ARG ARG A . n 
A 1 116 GLY 116 133 133 GLY GLY A . n 
A 1 117 ALA 117 134 134 ALA ALA A . n 
A 1 118 ALA 118 135 135 ALA ALA A . n 
A 1 119 ASP 119 136 136 ASP ASP A . n 
A 1 120 GLY 120 137 137 GLY GLY A . n 
A 1 121 SER 121 138 138 SER SER A . n 
A 1 122 ARG 122 139 139 ARG ARG A . n 
A 1 123 PHE 123 140 140 PHE PHE A . n 
A 1 124 GLN 124 141 141 GLN GLN A . n 
A 1 125 VAL 125 142 142 VAL VAL A . n 
A 1 126 TRP 126 143 143 TRP TRP A . n 
A 1 127 ASP 127 144 144 ASP ASP A . n 
A 1 128 TYR 128 145 145 TYR TYR A . n 
A 1 129 GLU 129 146 146 GLU GLU A . n 
A 1 130 GLU 130 147 147 GLU GLU A . n 
A 1 131 GLY 131 148 148 GLY GLY A . n 
A 1 132 GLU 132 149 149 GLU GLU A . n 
A 1 133 VAL 133 150 150 VAL VAL A . n 
A 1 134 GLU 134 151 151 GLU GLU A . n 
A 1 135 ALA 135 152 152 ALA ALA A . n 
A 1 136 LEU 136 153 153 LEU LEU A . n 
A 1 137 LEU 137 154 154 LEU LEU A . n 
A 1 138 ASP 138 155 155 ASP ASP A . n 
A 1 139 ARG 139 156 156 ARG ARG A . n 
A 1 140 TYR 140 157 157 TYR TYR A . n 
A 1 141 PHE 141 158 158 PHE PHE A . n 
A 1 142 GLU 142 159 159 GLU GLU A . n 
A 1 143 ALA 143 160 ?   ?   ?   A . n 
A 1 144 ASP 144 161 ?   ?   ?   A . n 
A 1 145 PRO 145 162 ?   ?   ?   A . n 
B 1 1   SER 1   18  ?   ?   ?   B . n 
B 1 2   MET 2   19  ?   ?   ?   B . n 
B 1 3   ARG 3   20  20  ARG ARG B . n 
B 1 4   PRO 4   21  21  PRO PRO B . n 
B 1 5   ALA 5   22  22  ALA ALA B . n 
B 1 6   LEU 6   23  23  LEU LEU B . n 
B 1 7   TYR 7   24  24  TYR TYR B . n 
B 1 8   PHE 8   25  25  PHE PHE B . n 
B 1 9   CYS 9   26  26  CYS CYS B . n 
B 1 10  GLY 10  27  27  GLY GLY B . n 
B 1 11  SER 11  28  28  SER SER B . n 
B 1 12  ILE 12  29  29  ILE ILE B . n 
B 1 13  ARG 13  30  30  ARG ARG B . n 
B 1 14  GLY 14  31  31  GLY GLY B . n 
B 1 15  GLY 15  32  32  GLY GLY B . n 
B 1 16  ARG 16  33  33  ARG ARG B . n 
B 1 17  GLU 17  34  34  GLU GLU B . n 
B 1 18  ASP 18  35  35  ASP ASP B . n 
B 1 19  ARG 19  36  36  ARG ARG B . n 
B 1 20  THR 20  37  37  THR THR B . n 
B 1 21  LEU 21  38  38  LEU LEU B . n 
B 1 22  TYR 22  39  39  TYR TYR B . n 
B 1 23  GLU 23  40  40  GLU GLU B . n 
B 1 24  ARG 24  41  41  ARG ARG B . n 
B 1 25  ILE 25  42  42  ILE ILE B . n 
B 1 26  VAL 26  43  43  VAL VAL B . n 
B 1 27  SER 27  44  44  SER SER B . n 
B 1 28  ARG 28  45  45  ARG ARG B . n 
B 1 29  LEU 29  46  46  LEU LEU B . n 
B 1 30  ARG 30  47  47  ARG ARG B . n 
B 1 31  ARG 31  48  48  ARG ARG B . n 
B 1 32  PHE 32  49  49  PHE PHE B . n 
B 1 33  GLY 33  50  50  GLY GLY B . n 
B 1 34  THR 34  51  51  THR THR B . n 
B 1 35  VAL 35  52  52  VAL VAL B . n 
B 1 36  LEU 36  53  53  LEU LEU B . n 
B 1 37  THR 37  54  ?   ?   ?   B . n 
B 1 38  GLU 38  55  ?   ?   ?   B . n 
B 1 39  HIS 39  56  ?   ?   ?   B . n 
B 1 40  VAL 40  57  ?   ?   ?   B . n 
B 1 41  ALA 41  58  ?   ?   ?   B . n 
B 1 42  ALA 42  59  ?   ?   ?   B . n 
B 1 43  ALA 43  60  ?   ?   ?   B . n 
B 1 44  GLU 44  61  ?   ?   ?   B . n 
B 1 45  LEU 45  62  ?   ?   ?   B . n 
B 1 46  GLY 46  63  ?   ?   ?   B . n 
B 1 47  ALA 47  64  ?   ?   ?   B . n 
B 1 48  ARG 48  65  ?   ?   ?   B . n 
B 1 49  GLY 49  66  ?   ?   ?   B . n 
B 1 50  GLU 50  67  ?   ?   ?   B . n 
B 1 51  GLU 51  68  ?   ?   ?   B . n 
B 1 52  ALA 52  69  ?   ?   ?   B . n 
B 1 53  ALA 53  70  ?   ?   ?   B . n 
B 1 54  GLY 54  71  71  GLY GLY B . n 
B 1 55  GLY 55  72  72  GLY GLY B . n 
B 1 56  ASP 56  73  73  ASP ASP B . n 
B 1 57  ARG 57  74  74  ARG ARG B . n 
B 1 58  LEU 58  75  75  LEU LEU B . n 
B 1 59  ILE 59  76  76  ILE ILE B . n 
B 1 60  HIS 60  77  77  HIS HIS B . n 
B 1 61  GLU 61  78  78  GLU GLU B . n 
B 1 62  GLN 62  79  79  GLN GLN B . n 
B 1 63  ASP 63  80  80  ASP ASP B . n 
B 1 64  LEU 64  81  81  LEU LEU B . n 
B 1 65  GLU 65  82  82  GLU GLU B . n 
B 1 66  TRP 66  83  83  TRP TRP B . n 
B 1 67  LEU 67  84  84  LEU LEU B . n 
B 1 68  GLN 68  85  85  GLN GLN B . n 
B 1 69  GLN 69  86  86  GLN GLN B . n 
B 1 70  ALA 70  87  87  ALA ALA B . n 
B 1 71  ASP 71  88  88  ASP ASP B . n 
B 1 72  VAL 72  89  89  VAL VAL B . n 
B 1 73  VAL 73  90  90  VAL VAL B . n 
B 1 74  VAL 74  91  91  VAL VAL B . n 
B 1 75  ALA 75  92  92  ALA ALA B . n 
B 1 76  GLU 76  93  93  GLU GLU B . n 
B 1 77  VAL 77  94  94  VAL VAL B . n 
B 1 78  THR 78  95  95  THR THR B . n 
B 1 79  GLN 79  96  96  GLN GLN B . n 
B 1 80  PRO 80  97  97  PRO PRO B . n 
B 1 81  SER 81  98  98  SER SER B . n 
B 1 82  LEU 82  99  99  LEU LEU B . n 
B 1 83  GLY 83  100 100 GLY GLY B . n 
B 1 84  VAL 84  101 101 VAL VAL B . n 
B 1 85  GLY 85  102 102 GLY GLY B . n 
B 1 86  TYR 86  103 103 TYR TYR B . n 
B 1 87  GLU 87  104 104 GLU GLU B . n 
B 1 88  LEU 88  105 105 LEU LEU B . n 
B 1 89  GLY 89  106 106 GLY GLY B . n 
B 1 90  ARG 90  107 107 ARG ARG B . n 
B 1 91  ALA 91  108 108 ALA ALA B . n 
B 1 92  VAL 92  109 109 VAL VAL B . n 
B 1 93  ALA 93  110 110 ALA ALA B . n 
B 1 94  PHE 94  111 111 PHE PHE B . n 
B 1 95  ASN 95  112 112 ASN ASN B . n 
B 1 96  LYS 96  113 113 LYS LYS B . n 
B 1 97  ARG 97  114 114 ARG ARG B . n 
B 1 98  ILE 98  115 115 ILE ILE B . n 
B 1 99  LEU 99  116 116 LEU LEU B . n 
B 1 100 CYS 100 117 117 CYS CYS B . n 
B 1 101 LEU 101 118 118 LEU LEU B . n 
B 1 102 PHE 102 119 119 PHE PHE B . n 
B 1 103 ARG 103 120 120 ARG ARG B . n 
B 1 104 PRO 104 121 121 PRO PRO B . n 
B 1 105 GLN 105 122 122 GLN GLN B . n 
B 1 106 SER 106 123 123 SER SER B . n 
B 1 107 GLY 107 124 124 GLY GLY B . n 
B 1 108 ARG 108 125 125 ARG ARG B . n 
B 1 109 VAL 109 126 126 VAL VAL B . n 
B 1 110 LEU 110 127 127 LEU LEU B . n 
B 1 111 SER 111 128 128 SER SER B . n 
B 1 112 ALA 112 129 129 ALA ALA B . n 
B 1 113 MET 113 130 130 MET MET B . n 
B 1 114 ILE 114 131 131 ILE ILE B . n 
B 1 115 ARG 115 132 132 ARG ARG B . n 
B 1 116 GLY 116 133 133 GLY GLY B . n 
B 1 117 ALA 117 134 134 ALA ALA B . n 
B 1 118 ALA 118 135 135 ALA ALA B . n 
B 1 119 ASP 119 136 136 ASP ASP B . n 
B 1 120 GLY 120 137 137 GLY GLY B . n 
B 1 121 SER 121 138 138 SER SER B . n 
B 1 122 ARG 122 139 139 ARG ARG B . n 
B 1 123 PHE 123 140 140 PHE PHE B . n 
B 1 124 GLN 124 141 141 GLN GLN B . n 
B 1 125 VAL 125 142 142 VAL VAL B . n 
B 1 126 TRP 126 143 143 TRP TRP B . n 
B 1 127 ASP 127 144 144 ASP ASP B . n 
B 1 128 TYR 128 145 145 TYR TYR B . n 
B 1 129 GLU 129 146 146 GLU GLU B . n 
B 1 130 GLU 130 147 147 GLU GLU B . n 
B 1 131 GLY 131 148 148 GLY GLY B . n 
B 1 132 GLU 132 149 149 GLU GLU B . n 
B 1 133 VAL 133 150 150 VAL VAL B . n 
B 1 134 GLU 134 151 151 GLU GLU B . n 
B 1 135 ALA 135 152 152 ALA ALA B . n 
B 1 136 LEU 136 153 153 LEU LEU B . n 
B 1 137 LEU 137 154 154 LEU LEU B . n 
B 1 138 ASP 138 155 155 ASP ASP B . n 
B 1 139 ARG 139 156 156 ARG ARG B . n 
B 1 140 TYR 140 157 157 TYR TYR B . n 
B 1 141 PHE 141 158 158 PHE PHE B . n 
B 1 142 GLU 142 159 159 GLU GLU B . n 
B 1 143 ALA 143 160 ?   ?   ?   B . n 
B 1 144 ASP 144 161 ?   ?   ?   B . n 
B 1 145 PRO 145 162 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BBD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BBD 
_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 A1BBD 1  201 203 A1BBD T40 A . 
D 2 A1BBD 1  201 201 A1BBD T40 B . 
E 3 HOH   1  301 134 HOH   HOH A . 
E 3 HOH   2  302 51  HOH   HOH A . 
E 3 HOH   3  303 153 HOH   HOH A . 
E 3 HOH   4  304 103 HOH   HOH A . 
E 3 HOH   5  305 57  HOH   HOH A . 
E 3 HOH   6  306 108 HOH   HOH A . 
E 3 HOH   7  307 96  HOH   HOH A . 
E 3 HOH   8  308 33  HOH   HOH A . 
E 3 HOH   9  309 24  HOH   HOH A . 
E 3 HOH   10 310 25  HOH   HOH A . 
E 3 HOH   11 311 157 HOH   HOH A . 
E 3 HOH   12 312 41  HOH   HOH A . 
E 3 HOH   13 313 52  HOH   HOH A . 
E 3 HOH   14 314 152 HOH   HOH A . 
E 3 HOH   15 315 21  HOH   HOH A . 
E 3 HOH   16 316 81  HOH   HOH A . 
E 3 HOH   17 317 2   HOH   HOH A . 
E 3 HOH   18 318 165 HOH   HOH A . 
E 3 HOH   19 319 13  HOH   HOH A . 
E 3 HOH   20 320 31  HOH   HOH A . 
E 3 HOH   21 321 112 HOH   HOH A . 
E 3 HOH   22 322 84  HOH   HOH A . 
E 3 HOH   23 323 162 HOH   HOH A . 
E 3 HOH   24 324 150 HOH   HOH A . 
E 3 HOH   25 325 16  HOH   HOH A . 
E 3 HOH   26 326 10  HOH   HOH A . 
E 3 HOH   27 327 63  HOH   HOH A . 
E 3 HOH   28 328 60  HOH   HOH A . 
E 3 HOH   29 329 22  HOH   HOH A . 
E 3 HOH   30 330 163 HOH   HOH A . 
E 3 HOH   31 331 101 HOH   HOH A . 
E 3 HOH   32 332 7   HOH   HOH A . 
E 3 HOH   33 333 128 HOH   HOH A . 
E 3 HOH   34 334 54  HOH   HOH A . 
E 3 HOH   35 335 4   HOH   HOH A . 
E 3 HOH   36 336 15  HOH   HOH A . 
E 3 HOH   37 337 32  HOH   HOH A . 
E 3 HOH   38 338 100 HOH   HOH A . 
E 3 HOH   39 339 19  HOH   HOH A . 
E 3 HOH   40 340 166 HOH   HOH A . 
E 3 HOH   41 341 135 HOH   HOH A . 
E 3 HOH   42 342 56  HOH   HOH A . 
E 3 HOH   43 343 9   HOH   HOH A . 
E 3 HOH   44 344 27  HOH   HOH A . 
E 3 HOH   45 345 26  HOH   HOH A . 
E 3 HOH   46 346 89  HOH   HOH A . 
E 3 HOH   47 347 104 HOH   HOH A . 
E 3 HOH   48 348 74  HOH   HOH A . 
E 3 HOH   49 349 97  HOH   HOH A . 
E 3 HOH   50 350 88  HOH   HOH A . 
E 3 HOH   51 351 85  HOH   HOH A . 
E 3 HOH   52 352 121 HOH   HOH A . 
E 3 HOH   53 353 40  HOH   HOH A . 
E 3 HOH   54 354 45  HOH   HOH A . 
E 3 HOH   55 355 37  HOH   HOH A . 
E 3 HOH   56 356 91  HOH   HOH A . 
E 3 HOH   57 357 130 HOH   HOH A . 
E 3 HOH   58 358 1   HOH   HOH A . 
E 3 HOH   59 359 95  HOH   HOH A . 
E 3 HOH   60 360 30  HOH   HOH A . 
E 3 HOH   61 361 71  HOH   HOH A . 
E 3 HOH   62 362 145 HOH   HOH A . 
E 3 HOH   63 363 39  HOH   HOH A . 
E 3 HOH   64 364 161 HOH   HOH A . 
E 3 HOH   65 365 65  HOH   HOH A . 
E 3 HOH   66 366 29  HOH   HOH A . 
E 3 HOH   67 367 118 HOH   HOH A . 
E 3 HOH   68 368 53  HOH   HOH A . 
E 3 HOH   69 369 58  HOH   HOH A . 
E 3 HOH   70 370 11  HOH   HOH A . 
E 3 HOH   71 371 35  HOH   HOH A . 
E 3 HOH   72 372 105 HOH   HOH A . 
E 3 HOH   73 373 43  HOH   HOH A . 
E 3 HOH   74 374 124 HOH   HOH A . 
E 3 HOH   75 375 106 HOH   HOH A . 
E 3 HOH   76 376 113 HOH   HOH A . 
E 3 HOH   77 377 138 HOH   HOH A . 
E 3 HOH   78 378 42  HOH   HOH A . 
E 3 HOH   79 379 155 HOH   HOH A . 
E 3 HOH   80 380 110 HOH   HOH A . 
E 3 HOH   81 381 154 HOH   HOH A . 
E 3 HOH   82 382 80  HOH   HOH A . 
E 3 HOH   83 383 132 HOH   HOH A . 
E 3 HOH   84 384 83  HOH   HOH A . 
E 3 HOH   85 385 125 HOH   HOH A . 
E 3 HOH   86 386 59  HOH   HOH A . 
E 3 HOH   87 387 123 HOH   HOH A . 
F 3 HOH   1  301 131 HOH   HOH B . 
F 3 HOH   2  302 78  HOH   HOH B . 
F 3 HOH   3  303 79  HOH   HOH B . 
F 3 HOH   4  304 61  HOH   HOH B . 
F 3 HOH   5  305 139 HOH   HOH B . 
F 3 HOH   6  306 50  HOH   HOH B . 
F 3 HOH   7  307 72  HOH   HOH B . 
F 3 HOH   8  308 147 HOH   HOH B . 
F 3 HOH   9  309 151 HOH   HOH B . 
F 3 HOH   10 310 158 HOH   HOH B . 
F 3 HOH   11 311 23  HOH   HOH B . 
F 3 HOH   12 312 48  HOH   HOH B . 
F 3 HOH   13 313 44  HOH   HOH B . 
F 3 HOH   14 314 115 HOH   HOH B . 
F 3 HOH   15 315 69  HOH   HOH B . 
F 3 HOH   16 316 107 HOH   HOH B . 
F 3 HOH   17 317 86  HOH   HOH B . 
F 3 HOH   18 318 14  HOH   HOH B . 
F 3 HOH   19 319 70  HOH   HOH B . 
F 3 HOH   20 320 34  HOH   HOH B . 
F 3 HOH   21 321 129 HOH   HOH B . 
F 3 HOH   22 322 137 HOH   HOH B . 
F 3 HOH   23 323 12  HOH   HOH B . 
F 3 HOH   24 324 156 HOH   HOH B . 
F 3 HOH   25 325 49  HOH   HOH B . 
F 3 HOH   26 326 6   HOH   HOH B . 
F 3 HOH   27 327 76  HOH   HOH B . 
F 3 HOH   28 328 3   HOH   HOH B . 
F 3 HOH   29 329 46  HOH   HOH B . 
F 3 HOH   30 330 67  HOH   HOH B . 
F 3 HOH   31 331 8   HOH   HOH B . 
F 3 HOH   32 332 143 HOH   HOH B . 
F 3 HOH   33 333 144 HOH   HOH B . 
F 3 HOH   34 334 93  HOH   HOH B . 
F 3 HOH   35 335 120 HOH   HOH B . 
F 3 HOH   36 336 117 HOH   HOH B . 
F 3 HOH   37 337 159 HOH   HOH B . 
F 3 HOH   38 338 92  HOH   HOH B . 
F 3 HOH   39 339 77  HOH   HOH B . 
F 3 HOH   40 340 17  HOH   HOH B . 
F 3 HOH   41 341 18  HOH   HOH B . 
F 3 HOH   42 342 75  HOH   HOH B . 
F 3 HOH   43 343 90  HOH   HOH B . 
F 3 HOH   44 344 68  HOH   HOH B . 
F 3 HOH   45 345 38  HOH   HOH B . 
F 3 HOH   46 346 47  HOH   HOH B . 
F 3 HOH   47 347 73  HOH   HOH B . 
F 3 HOH   48 348 20  HOH   HOH B . 
F 3 HOH   49 349 136 HOH   HOH B . 
F 3 HOH   50 350 114 HOH   HOH B . 
F 3 HOH   51 351 102 HOH   HOH B . 
F 3 HOH   52 352 28  HOH   HOH B . 
F 3 HOH   53 353 5   HOH   HOH B . 
F 3 HOH   54 354 66  HOH   HOH B . 
F 3 HOH   55 355 87  HOH   HOH B . 
F 3 HOH   56 356 98  HOH   HOH B . 
F 3 HOH   57 357 64  HOH   HOH B . 
F 3 HOH   58 358 133 HOH   HOH B . 
F 3 HOH   59 359 160 HOH   HOH B . 
F 3 HOH   60 360 164 HOH   HOH B . 
F 3 HOH   61 361 149 HOH   HOH B . 
F 3 HOH   62 362 36  HOH   HOH B . 
F 3 HOH   63 363 55  HOH   HOH B . 
F 3 HOH   64 364 116 HOH   HOH B . 
F 3 HOH   65 365 127 HOH   HOH B . 
F 3 HOH   66 366 119 HOH   HOH B . 
F 3 HOH   67 367 62  HOH   HOH B . 
F 3 HOH   68 368 122 HOH   HOH B . 
F 3 HOH   69 369 140 HOH   HOH B . 
F 3 HOH   70 370 82  HOH   HOH B . 
F 3 HOH   71 371 141 HOH   HOH B . 
F 3 HOH   72 372 142 HOH   HOH B . 
F 3 HOH   73 373 146 HOH   HOH B . 
F 3 HOH   74 374 148 HOH   HOH B . 
F 3 HOH   75 375 109 HOH   HOH B . 
F 3 HOH   76 376 126 HOH   HOH B . 
F 3 HOH   77 377 94  HOH   HOH B . 
F 3 HOH   78 378 111 HOH   HOH B . 
F 3 HOH   79 379 99  HOH   HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           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                     9DA3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.972 
_cell.length_a_esd                 ? 
_cell.length_b                     64.585 
_cell.length_b_esd                 ? 
_cell.length_c                     128.640 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9DA3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DA3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.97 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.0 
_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    '20% (w/v) PEG 3350 and 0.2 M Sodium malonate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DA3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.51 
_reflns.d_resolution_low                               24.85 
_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                                     38634 
_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                           96.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_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                                0.080 
_reflns.pdbx_Rpim_I_all                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       263117 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_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                                    1.51 
_reflns_shell.d_res_low                                     1.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           5459 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1441 
_reflns_shell.percent_possible_obs                          74.5 
_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                               3.8 
_reflns_shell.pdbx_chi_squared                              1.10 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.2 
_reflns_shell.pdbx_Rrim_I_all                               0.601 
_reflns_shell.pdbx_Rpim_I_all                               0.284 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.817 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.526 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9DA3 
_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                            1.51 
_refine.ls_d_res_low                             24.85 
_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                     38586 
_refine.ls_number_reflns_R_free                  1949 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.67 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1818 
_refine.ls_R_factor_R_free                       0.1982 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1809 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 21.45 
_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                             ? 
_refine.overall_SU_ML                            0.16 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        1996 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             166 
_refine_hist.number_atoms_total               2206 
_refine_hist.d_res_high                       1.51 
_refine_hist.d_res_low                        24.85 
# 
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' ? 0.007 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.072 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.863 ? 306 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059 ? 296 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.018 ? 369 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.51 1.55  . . 100 1997 75.00  . . . . 0.2455 . . . . . . . . . . . 0.2502 
'X-RAY DIFFRACTION' 1.55 1.59  . . 116 2318 86.00  . . . . 0.2192 . . . . . . . . . . . 0.2810 
'X-RAY DIFFRACTION' 1.59 1.64  . . 117 2602 95.00  . . . . 0.2004 . . . . . . . . . . . 0.2689 
'X-RAY DIFFRACTION' 1.64 1.69  . . 126 2601 97.00  . . . . 0.1919 . . . . . . . . . . . 0.2288 
'X-RAY DIFFRACTION' 1.69 1.75  . . 159 2630 100.00 . . . . 0.1876 . . . . . . . . . . . 0.2570 
'X-RAY DIFFRACTION' 1.75 1.82  . . 142 2673 100.00 . . . . 0.1851 . . . . . . . . . . . 0.1822 
'X-RAY DIFFRACTION' 1.82 1.91  . . 131 2727 100.00 . . . . 0.1961 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 1.91 2.01  . . 132 2701 100.00 . . . . 0.1814 . . . . . . . . . . . 0.2313 
'X-RAY DIFFRACTION' 2.01 2.13  . . 135 2693 100.00 . . . . 0.1860 . . . . . . . . . . . 0.2142 
'X-RAY DIFFRACTION' 2.13 2.30  . . 170 2671 100.00 . . . . 0.1769 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.30 2.53  . . 149 2704 100.00 . . . . 0.1825 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 2.53 2.89  . . 154 2726 100.00 . . . . 0.1901 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.90 3.64  . . 168 2735 100.00 . . . . 0.1782 . . . . . . . . . . . 0.1831 
'X-RAY DIFFRACTION' 3.65 24.85 . . 150 2859 100.00 . . . . 0.1647 . . . . . . . . . . . 0.1711 
# 
_struct.entry_id                     9DA3 
_struct.title                        'Crystal structure of human DNPH1 bound to inhibitor 2a' 
_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        9DA3 
_struct_keywords.text            'Inhibitor, Complex, HYDROLASE, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DNPH1_HUMAN 
_struct_ref.pdbx_db_accession          O43598 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQPSL
GVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_struct_ref.pdbx_align_begin           20 
# 
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 9DA3 A 3 ? 145 ? O43598 20 ? 162 ? 20 162 
2 1 9DA3 B 3 ? 145 ? O43598 20 ? 162 ? 20 162 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DA3 SER A 1 ? UNP O43598 ? ? 'expression tag' 18 1 
1 9DA3 MET A 2 ? UNP O43598 ? ? 'expression tag' 19 2 
2 9DA3 SER B 1 ? UNP O43598 ? ? 'expression tag' 18 3 
2 9DA3 MET B 2 ? UNP O43598 ? ? 'expression tag' 19 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4260  ? 
1 MORE         -34   ? 
1 'SSA (A^2)'  10700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'Superdex S200' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            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 18  ? GLY A 33  ? ASP A 35  GLY A 50  1 ? 16 
HELX_P HELX_P2  AA2 GLY A 55  ? ALA A 70  ? GLY A 72  ALA A 87  1 ? 16 
HELX_P HELX_P3  AA3 SER A 81  ? PHE A 94  ? SER A 98  PHE A 111 1 ? 14 
HELX_P HELX_P4  AA4 ARG A 103 ? GLY A 107 ? ARG A 120 GLY A 124 5 ? 5  
HELX_P HELX_P5  AA5 SER A 111 ? GLY A 116 ? SER A 128 GLY A 133 1 ? 6  
HELX_P HELX_P6  AA6 GLU A 129 ? GLY A 131 ? GLU A 146 GLY A 148 5 ? 3  
HELX_P HELX_P7  AA7 GLU A 132 ? GLU A 142 ? GLU A 149 GLU A 159 1 ? 11 
HELX_P HELX_P8  AA8 ASP B 18  ? ARG B 31  ? ASP B 35  ARG B 48  1 ? 14 
HELX_P HELX_P9  AA9 GLY B 55  ? ALA B 70  ? GLY B 72  ALA B 87  1 ? 16 
HELX_P HELX_P10 AB1 SER B 81  ? PHE B 94  ? SER B 98  PHE B 111 1 ? 14 
HELX_P HELX_P11 AB2 ARG B 103 ? GLY B 107 ? ARG B 120 GLY B 124 5 ? 5  
HELX_P HELX_P12 AB3 SER B 111 ? GLY B 116 ? SER B 128 GLY B 133 1 ? 6  
HELX_P HELX_P13 AB4 GLU B 129 ? GLY B 131 ? GLU B 146 GLY B 148 5 ? 3  
HELX_P HELX_P14 AB5 GLU B 132 ? PHE B 141 ? GLU B 149 PHE B 158 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? 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 THR A 34  ? VAL A 35  ? THR A 51  VAL A 52  
AA1 2 ALA A 5   ? CYS A 9   ? ALA A 22  CYS A 26  
AA1 3 VAL A 72  ? GLU A 76  ? VAL A 89  GLU A 93  
AA1 4 ARG A 97  ? PHE A 102 ? ARG A 114 PHE A 119 
AA1 5 PHE A 123 ? ASP A 127 ? PHE A 140 ASP A 144 
AA2 1 THR B 34  ? VAL B 35  ? THR B 51  VAL B 52  
AA2 2 ALA B 5   ? CYS B 9   ? ALA B 22  CYS B 26  
AA2 3 VAL B 72  ? GLU B 76  ? VAL B 89  GLU B 93  
AA2 4 ARG B 97  ? PHE B 102 ? ARG B 114 PHE B 119 
AA2 5 PHE B 123 ? ASP B 127 ? PHE B 140 ASP B 144 
# 
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 THR A 34  ? O THR A 51  N LEU A 6   ? N LEU A 23  
AA1 2 3 N TYR A 7   ? N TYR A 24  O VAL A 74  ? O VAL A 91  
AA1 3 4 N VAL A 73  ? N VAL A 90  O LEU A 99  ? O LEU A 116 
AA1 4 5 N CYS A 100 ? N CYS A 117 O GLN A 124 ? O GLN A 141 
AA2 1 2 O THR B 34  ? O THR B 51  N LEU B 6   ? N LEU B 23  
AA2 2 3 N TYR B 7   ? N TYR B 24  O VAL B 74  ? O VAL B 91  
AA2 3 4 N VAL B 73  ? N VAL B 90  O ARG B 97  ? O ARG B 114 
AA2 4 5 N CYS B 100 ? N CYS B 117 O GLN B 124 ? O GLN B 141 
# 
_pdbx_entry_details.entry_id                   9DA3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 29  ? ? -123.99 -74.98 
2 1 SER A 128 ? ? -35.81  132.38 
3 1 SER A 138 ? ? -130.90 -76.12 
4 1 ILE B 29  ? ? -123.25 -76.66 
5 1 SER B 128 ? ? -32.99  129.21 
6 1 SER B 138 ? ? -125.04 -86.23 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.111 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 HOH 369 ? E HOH . 
2 1 A HOH 379 ? E HOH . 
3 1 B HOH 334 ? F HOH . 
4 1 B HOH 370 ? F HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -21.4235 -4.3992  -6.8048  0.1818 ? 0.0047  ? 0.0155  ? 0.1644 ? -0.0226 ? 0.1305 ? 0.7085 ? 
0.4113  ? 0.3829  ? 3.2344 ? 0.0447  ? 1.3250 ? -0.0423 ? -0.0427 ? 0.0648  ? 0.1096  ? 0.0838  ? 0.1481  ? -0.2288 ? -0.0321 ? 
-0.0190 ? 
2  'X-RAY DIFFRACTION' ? refined -29.1798 -11.5604 -12.6337 0.1613 ? 0.0104  ? 0.0126  ? 0.1938 ? -0.0153 ? 0.2267 ? 1.0419 ? 
-0.2818 ? 0.2105  ? 1.9578 ? 0.0338  ? 1.2509 ? -0.0347 ? -0.0597 ? -0.0845 ? 0.0631  ? 0.0279  ? 0.5126  ? -0.1060 ? -0.2610 ? 
0.0200  ? 
3  'X-RAY DIFFRACTION' ? refined -15.7298 -9.7954  -18.7067 0.1924 ? -0.0258 ? 0.0445  ? 0.1774 ? -0.0141 ? 0.1320 ? 2.5772 ? 
0.6060  ? -0.0778 ? 2.8708 ? 0.5364  ? 1.9264 ? -0.0565 ? 0.1881  ? 0.1197  ? -0.3943 ? 0.0951  ? -0.2507 ? -0.2538 ? 0.0971  ? 
-0.0665 ? 
4  'X-RAY DIFFRACTION' ? refined -13.2728 3.6262   -12.0290 0.3732 ? -0.0917 ? 0.0793  ? 0.1953 ? -0.0301 ? 0.2494 ? 3.6617 ? 
0.5384  ? 0.5499  ? 3.3014 ? 0.1259  ? 3.9690 ? -0.2020 ? 0.0041  ? 0.3528  ? -0.2864 ? 0.4582  ? -0.4787 ? -0.9079 ? 0.4581  ? 
-0.0291 ? 
5  'X-RAY DIFFRACTION' ? refined -21.5912 -32.7577 -27.8296 0.3000 ? 0.0215  ? -0.0448 ? 0.3653 ? -0.2216 ? 0.3643 ? 0.3210 ? 
0.5686  ? 0.4760  ? 2.7493 ? 0.5960  ? 3.1665 ? 0.0924  ? 0.7830  ? -0.8473 ? -0.6533 ? -0.2215 ? 0.4316  ? 0.1887  ? -0.1231 ? 
-0.2394 ? 
6  'X-RAY DIFFRACTION' ? refined -10.5539 -26.9309 -14.7314 0.1372 ? -0.0064 ? 0.0312  ? 0.2111 ? -0.0528 ? 0.2216 ? 2.4039 ? 
-0.7192 ? 0.4110  ? 4.2216 ? -0.4281 ? 2.7125 ? 0.0579  ? 0.1140  ? -0.2481 ? 0.1302  ? 0.0269  ? -0.4299 ? -0.0163 ? 0.2159  ? 
-0.1077 ? 
7  'X-RAY DIFFRACTION' ? refined -16.2838 -37.1326 -23.3093 0.2644 ? 0.0238  ? 0.0642  ? 0.2923 ? -0.1301 ? 0.4542 ? 1.0990 ? 
-0.6377 ? 0.5636  ? 2.4090 ? 0.9050  ? 3.3180 ? -0.0702 ? 0.4656  ? -0.4667 ? -0.3462 ? -0.1059 ? -0.1101 ? 0.1281  ? 0.1248  ? 
0.1294  ? 
8  'X-RAY DIFFRACTION' ? refined -15.8431 -20.4884 -31.1000 0.4376 ? 0.0283  ? 0.0599  ? 0.4541 ? -0.0749 ? 0.2240 ? 4.5264 ? 
0.9219  ? 0.8437  ? 2.3680 ? 0.0975  ? 3.1772 ? 0.0417  ? 1.0070  ? -0.3595 ? -0.9149 ? 0.2537  ? -0.2688 ? -0.3086 ? 0.4400  ? 
-0.2020 ? 
9  'X-RAY DIFFRACTION' ? refined -23.8907 -25.4299 -20.7951 0.1410 ? 0.0006  ? -0.0017 ? 0.1730 ? -0.0406 ? 0.1329 ? 2.1172 ? 
-0.0456 ? 0.0095  ? 3.3362 ? 0.1347  ? 2.4943 ? 0.0088  ? 0.3124  ? -0.2040 ? -0.4060 ? -0.0162 ? 0.1281  ? -0.0759 ? 0.0024  ? 
-0.0072 ? 
10 'X-RAY DIFFRACTION' ? refined -21.6278 -29.6260 -5.3472  0.1452 ? -0.0085 ? 0.0267  ? 0.1799 ? 0.0308  ? 0.2184 ? 3.1665 ? 
-2.1330 ? 0.6219  ? 3.2586 ? -0.4259 ? 2.7444 ? -0.1493 ? -0.1408 ? -0.2659 ? 0.2993  ? 0.0156  ? -0.0542 ? 0.0180  ? 0.1398  ? 
0.0127  ? 
11 'X-RAY DIFFRACTION' ? refined -30.6398 -29.1389 -14.5260 0.1119 ? -0.0247 ? -0.0194 ? 0.1604 ? -0.0186 ? 0.2231 ? 3.2708 ? 
-0.9884 ? -0.4368 ? 2.6540 ? 0.3132  ? 2.4565 ? 0.1036  ? 0.0579  ? -0.4478 ? -0.0971 ? -0.0577 ? 0.4143  ? 0.1004  ? -0.2554 ? 
-0.0385 ? 
12 'X-RAY DIFFRACTION' ? refined -26.1187 -41.5494 -18.2236 0.3225 ? -0.0397 ? -0.0196 ? 0.1911 ? -0.0817 ? 0.3827 ? 4.0479 ? 
-0.9815 ? 1.0225  ? 4.0232 ? -0.8961 ? 8.7614 ? 0.1863  ? 0.0875  ? -0.8121 ? 0.1903  ? 0.0429  ? 0.2524  ? 1.2953  ? -0.1125 ? 
-0.2590 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 20 through 52 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 53 through 98 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 99 through 146 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 147 through 159 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 20 through 26 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 27 through 35 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 36 through 72 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 73 through 86 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 87 through 119 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 120 through 128 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 129 through 146 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 147 through 159 )
;
# 
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 SER 18  ? A SER 1   
2  1 Y 1 A MET 19  ? A MET 2   
3  1 Y 1 A HIS 56  ? A HIS 39  
4  1 Y 1 A VAL 57  ? A VAL 40  
5  1 Y 1 A ALA 58  ? A ALA 41  
6  1 Y 1 A ALA 59  ? A ALA 42  
7  1 Y 1 A ALA 60  ? A ALA 43  
8  1 Y 1 A GLU 61  ? A GLU 44  
9  1 Y 1 A LEU 62  ? A LEU 45  
10 1 Y 1 A GLY 63  ? A GLY 46  
11 1 Y 1 A ALA 64  ? A ALA 47  
12 1 Y 1 A ARG 65  ? A ARG 48  
13 1 Y 1 A GLY 66  ? A GLY 49  
14 1 Y 1 A GLU 67  ? A GLU 50  
15 1 Y 1 A GLU 68  ? A GLU 51  
16 1 Y 1 A ALA 69  ? A ALA 52  
17 1 Y 1 A ALA 70  ? A ALA 53  
18 1 Y 1 A ALA 160 ? A ALA 143 
19 1 Y 1 A ASP 161 ? A ASP 144 
20 1 Y 1 A PRO 162 ? A PRO 145 
21 1 Y 1 B SER 18  ? B SER 1   
22 1 Y 1 B MET 19  ? B MET 2   
23 1 Y 1 B THR 54  ? B THR 37  
24 1 Y 1 B GLU 55  ? B GLU 38  
25 1 Y 1 B HIS 56  ? B HIS 39  
26 1 Y 1 B VAL 57  ? B VAL 40  
27 1 Y 1 B ALA 58  ? B ALA 41  
28 1 Y 1 B ALA 59  ? B ALA 42  
29 1 Y 1 B ALA 60  ? B ALA 43  
30 1 Y 1 B GLU 61  ? B GLU 44  
31 1 Y 1 B LEU 62  ? B LEU 45  
32 1 Y 1 B GLY 63  ? B GLY 46  
33 1 Y 1 B ALA 64  ? B ALA 47  
34 1 Y 1 B ARG 65  ? B ARG 48  
35 1 Y 1 B GLY 66  ? B GLY 49  
36 1 Y 1 B GLU 67  ? B GLU 50  
37 1 Y 1 B GLU 68  ? B GLU 51  
38 1 Y 1 B ALA 69  ? B ALA 52  
39 1 Y 1 B ALA 70  ? B ALA 53  
40 1 Y 1 B ALA 160 ? B ALA 143 
41 1 Y 1 B ASP 161 ? B ASP 144 
42 1 Y 1 B PRO 162 ? B PRO 145 
# 
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 
A1BBD C12  C N N 1   
A1BBD C11  C N N 2   
A1BBD C10  C N N 3   
A1BBD C01  C N R 4   
A1BBD C02  C N R 5   
A1BBD C03  C N N 6   
A1BBD C04  C N N 7   
A1BBD C05  C N N 8   
A1BBD C06  C N N 9   
A1BBD C07  C N N 10  
A1BBD C08  C N N 11  
A1BBD C09  C N N 12  
A1BBD N01  N N N 13  
A1BBD N02  N N N 14  
A1BBD O01  O N N 15  
A1BBD O02  O N N 16  
A1BBD O03  O N N 17  
A1BBD O04  O N N 18  
A1BBD O05  O N N 19  
A1BBD O06  O N N 20  
A1BBD O07  O N N 21  
A1BBD P01  P N N 22  
A1BBD H1   H N N 23  
A1BBD H2   H N N 24  
A1BBD H3   H N N 25  
A1BBD H4   H N N 26  
A1BBD H5   H N N 27  
A1BBD H6   H N N 28  
A1BBD H7   H N N 29  
A1BBD H8   H N N 30  
A1BBD H9   H N N 31  
A1BBD H10  H N N 32  
A1BBD H11  H N N 33  
A1BBD H12  H N N 34  
A1BBD H13  H N N 35  
A1BBD H14  H N N 36  
A1BBD H15  H N N 37  
A1BBD H17  H N N 38  
A1BBD H18  H N N 39  
A1BBD H19  H N N 40  
A1BBD H20  H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
HIS   N    N N N 178 
HIS   CA   C N S 179 
HIS   C    C N N 180 
HIS   O    O N N 181 
HIS   CB   C N N 182 
HIS   CG   C Y N 183 
HIS   ND1  N Y N 184 
HIS   CD2  C Y N 185 
HIS   CE1  C Y N 186 
HIS   NE2  N Y N 187 
HIS   OXT  O N N 188 
HIS   H    H N N 189 
HIS   H2   H N N 190 
HIS   HA   H N N 191 
HIS   HB2  H N N 192 
HIS   HB3  H N N 193 
HIS   HD1  H N N 194 
HIS   HD2  H N N 195 
HIS   HE1  H N N 196 
HIS   HE2  H N N 197 
HIS   HXT  H N N 198 
HOH   O    O N N 199 
HOH   H1   H N N 200 
HOH   H2   H N N 201 
ILE   N    N N N 202 
ILE   CA   C N S 203 
ILE   C    C N N 204 
ILE   O    O N N 205 
ILE   CB   C N S 206 
ILE   CG1  C N N 207 
ILE   CG2  C N N 208 
ILE   CD1  C N N 209 
ILE   OXT  O N N 210 
ILE   H    H N N 211 
ILE   H2   H N N 212 
ILE   HA   H N N 213 
ILE   HB   H N N 214 
ILE   HG12 H N N 215 
ILE   HG13 H N N 216 
ILE   HG21 H N N 217 
ILE   HG22 H N N 218 
ILE   HG23 H N N 219 
ILE   HD11 H N N 220 
ILE   HD12 H N N 221 
ILE   HD13 H N N 222 
ILE   HXT  H N N 223 
LEU   N    N N N 224 
LEU   CA   C N S 225 
LEU   C    C N N 226 
LEU   O    O N N 227 
LEU   CB   C N N 228 
LEU   CG   C N N 229 
LEU   CD1  C N N 230 
LEU   CD2  C N N 231 
LEU   OXT  O N N 232 
LEU   H    H N N 233 
LEU   H2   H N N 234 
LEU   HA   H N N 235 
LEU   HB2  H N N 236 
LEU   HB3  H N N 237 
LEU   HG   H N N 238 
LEU   HD11 H N N 239 
LEU   HD12 H N N 240 
LEU   HD13 H N N 241 
LEU   HD21 H N N 242 
LEU   HD22 H N N 243 
LEU   HD23 H N N 244 
LEU   HXT  H N N 245 
LYS   N    N N N 246 
LYS   CA   C N S 247 
LYS   C    C N N 248 
LYS   O    O N N 249 
LYS   CB   C N N 250 
LYS   CG   C N N 251 
LYS   CD   C N N 252 
LYS   CE   C N N 253 
LYS   NZ   N N N 254 
LYS   OXT  O N N 255 
LYS   H    H N N 256 
LYS   H2   H N N 257 
LYS   HA   H N N 258 
LYS   HB2  H N N 259 
LYS   HB3  H N N 260 
LYS   HG2  H N N 261 
LYS   HG3  H N N 262 
LYS   HD2  H N N 263 
LYS   HD3  H N N 264 
LYS   HE2  H N N 265 
LYS   HE3  H N N 266 
LYS   HZ1  H N N 267 
LYS   HZ2  H N N 268 
LYS   HZ3  H N N 269 
LYS   HXT  H N N 270 
MET   N    N N N 271 
MET   CA   C N S 272 
MET   C    C N N 273 
MET   O    O N N 274 
MET   CB   C N N 275 
MET   CG   C N N 276 
MET   SD   S N N 277 
MET   CE   C N N 278 
MET   OXT  O N N 279 
MET   H    H N N 280 
MET   H2   H N N 281 
MET   HA   H N N 282 
MET   HB2  H N N 283 
MET   HB3  H N N 284 
MET   HG2  H N N 285 
MET   HG3  H N N 286 
MET   HE1  H N N 287 
MET   HE2  H N N 288 
MET   HE3  H N N 289 
MET   HXT  H N N 290 
PHE   N    N N N 291 
PHE   CA   C N S 292 
PHE   C    C N N 293 
PHE   O    O N N 294 
PHE   CB   C N N 295 
PHE   CG   C Y N 296 
PHE   CD1  C Y N 297 
PHE   CD2  C Y N 298 
PHE   CE1  C Y N 299 
PHE   CE2  C Y N 300 
PHE   CZ   C Y N 301 
PHE   OXT  O N N 302 
PHE   H    H N N 303 
PHE   H2   H N N 304 
PHE   HA   H N N 305 
PHE   HB2  H N N 306 
PHE   HB3  H N N 307 
PHE   HD1  H N N 308 
PHE   HD2  H N N 309 
PHE   HE1  H N N 310 
PHE   HE2  H N N 311 
PHE   HZ   H N N 312 
PHE   HXT  H N N 313 
PRO   N    N N N 314 
PRO   CA   C N S 315 
PRO   C    C N N 316 
PRO   O    O N N 317 
PRO   CB   C N N 318 
PRO   CG   C N N 319 
PRO   CD   C N N 320 
PRO   OXT  O N N 321 
PRO   H    H N N 322 
PRO   HA   H N N 323 
PRO   HB2  H N N 324 
PRO   HB3  H N N 325 
PRO   HG2  H N N 326 
PRO   HG3  H N N 327 
PRO   HD2  H N N 328 
PRO   HD3  H N N 329 
PRO   HXT  H N N 330 
SER   N    N N N 331 
SER   CA   C N S 332 
SER   C    C N N 333 
SER   O    O N N 334 
SER   CB   C N N 335 
SER   OG   O N N 336 
SER   OXT  O N N 337 
SER   H    H N N 338 
SER   H2   H N N 339 
SER   HA   H N N 340 
SER   HB2  H N N 341 
SER   HB3  H N N 342 
SER   HG   H N N 343 
SER   HXT  H N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
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 
A1BBD C04 C02  sing N N 1   
A1BBD C04 N01  sing N N 2   
A1BBD O01 C01  sing N N 3   
A1BBD C02 C01  sing N N 4   
A1BBD C02 C03  sing N N 5   
A1BBD N01 C05  sing N N 6   
A1BBD N01 C12  sing N N 7   
A1BBD C05 C06  sing N N 8   
A1BBD O03 P01  doub N N 9   
A1BBD O02 C03  sing N N 10  
A1BBD O02 P01  sing N N 11  
A1BBD C01 C12  sing N N 12  
A1BBD P01 O04  sing N N 13  
A1BBD P01 O05  sing N N 14  
A1BBD C06 C11  sing N N 15  
A1BBD C06 C07  doub N N 16  
A1BBD C11 C09  doub N N 17  
A1BBD O07 C10  sing N N 18  
A1BBD C07 N02  sing N N 19  
A1BBD C09 C10  sing N N 20  
A1BBD C09 C08  sing N N 21  
A1BBD N02 C08  sing N N 22  
A1BBD C08 O06  doub N N 23  
A1BBD C12 H1   sing N N 24  
A1BBD C12 H2   sing N N 25  
A1BBD C11 H3   sing N N 26  
A1BBD C10 H4   sing N N 27  
A1BBD C10 H5   sing N N 28  
A1BBD C01 H6   sing N N 29  
A1BBD C02 H7   sing N N 30  
A1BBD C03 H8   sing N N 31  
A1BBD C03 H9   sing N N 32  
A1BBD C04 H10  sing N N 33  
A1BBD C04 H11  sing N N 34  
A1BBD C05 H12  sing N N 35  
A1BBD C05 H13  sing N N 36  
A1BBD C07 H15  sing N N 37  
A1BBD O01 H17  sing N N 38  
A1BBD O04 H18  sing N N 39  
A1BBD O05 H19  sing N N 40  
A1BBD O07 H20  sing N N 41  
A1BBD N02 H14  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM041916       1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'S10 OD020068' 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   4P5E 
_pdbx_initial_refinement_model.details          
'CRYSTAL STRUCTURE OF HUMAN DNPH1 (RCL) WITH 6-NAPHTHYL-PURINE-RIBOSIDE-MONOPHOSPHATE' 
# 
_atom_sites.entry_id                    9DA3 
_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]   0.016401 
_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]   0.015483 
_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]   0.007774 
_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 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ARG   A 1 3   ? -29.801 8.896   -16.118 1.00 32.95 ? 20  ARG   A N   1 
ATOM   2    C CA  . ARG   A 1 3   ? -29.036 7.980   -15.265 1.00 30.59 ? 20  ARG   A CA  1 
ATOM   3    C C   . ARG   A 1 3   ? -29.279 6.524   -15.672 1.00 28.93 ? 20  ARG   A C   1 
ATOM   4    O O   . ARG   A 1 3   ? -30.422 6.089   -15.787 1.00 32.03 ? 20  ARG   A O   1 
ATOM   5    C CB  . ARG   A 1 3   ? -29.401 8.188   -13.789 1.00 33.36 ? 20  ARG   A CB  1 
ATOM   6    C CG  . ARG   A 1 3   ? -28.785 9.438   -13.150 1.00 37.16 ? 20  ARG   A CG  1 
ATOM   7    C CD  . ARG   A 1 3   ? -29.406 9.724   -11.776 1.00 40.08 ? 20  ARG   A CD  1 
ATOM   8    N NE  . ARG   A 1 3   ? -29.137 8.689   -10.785 1.00 38.99 ? 20  ARG   A NE  1 
ATOM   9    C CZ  . ARG   A 1 3   ? -28.014 8.569   -10.090 1.00 36.80 ? 20  ARG   A CZ  1 
ATOM   10   N NH1 . ARG   A 1 3   ? -27.010 9.419   -10.246 1.00 38.29 ? 20  ARG   A NH1 1 
ATOM   11   N NH2 . ARG   A 1 3   ? -27.896 7.573   -9.212  1.00 37.19 ? 20  ARG   A NH2 1 
ATOM   12   N N   . PRO   A 1 4   ? -28.208 5.776   -15.901 1.00 26.34 ? 21  PRO   A N   1 
ATOM   13   C CA  . PRO   A 1 4   ? -28.371 4.405   -16.390 1.00 24.27 ? 21  PRO   A CA  1 
ATOM   14   C C   . PRO   A 1 4   ? -28.848 3.448   -15.310 1.00 26.90 ? 21  PRO   A C   1 
ATOM   15   O O   . PRO   A 1 4   ? -28.649 3.665   -14.110 1.00 27.42 ? 21  PRO   A O   1 
ATOM   16   C CB  . PRO   A 1 4   ? -26.961 4.051   -16.869 1.00 25.47 ? 21  PRO   A CB  1 
ATOM   17   C CG  . PRO   A 1 4   ? -26.098 4.765   -15.848 1.00 26.03 ? 21  PRO   A CG  1 
ATOM   18   C CD  . PRO   A 1 4   ? -26.787 6.102   -15.665 1.00 28.84 ? 21  PRO   A CD  1 
ATOM   19   N N   . ALA   A 1 5   ? -29.520 2.385   -15.763 1.00 22.56 ? 22  ALA   A N   1 
ATOM   20   C CA  . ALA   A 1 5   ? -29.802 1.226   -14.932 1.00 21.32 ? 22  ALA   A CA  1 
ATOM   21   C C   . ALA   A 1 5   ? -28.610 0.290   -15.025 1.00 21.71 ? 22  ALA   A C   1 
ATOM   22   O O   . ALA   A 1 5   ? -28.118 0.014   -16.122 1.00 22.37 ? 22  ALA   A O   1 
ATOM   23   C CB  . ALA   A 1 5   ? -31.073 0.516   -15.390 1.00 23.84 ? 22  ALA   A CB  1 
ATOM   24   N N   . LEU   A 1 6   ? -28.145 -0.195  -13.881 1.00 18.68 ? 23  LEU   A N   1 
ATOM   25   C CA  . LEU   A 1 6   ? -26.915 -0.965  -13.811 1.00 18.57 ? 23  LEU   A CA  1 
ATOM   26   C C   . LEU   A 1 6   ? -27.183 -2.338  -13.211 1.00 18.56 ? 23  LEU   A C   1 
ATOM   27   O O   . LEU   A 1 6   ? -28.056 -2.509  -12.352 1.00 21.54 ? 23  LEU   A O   1 
ATOM   28   C CB  . LEU   A 1 6   ? -25.855 -0.206  -12.998 1.00 17.56 ? 23  LEU   A CB  1 
ATOM   29   C CG  . LEU   A 1 6   ? -25.679 1.237   -13.462 1.00 20.51 ? 23  LEU   A CG  1 
ATOM   30   C CD1 . LEU   A 1 6   ? -24.815 2.017   -12.492 1.00 20.62 ? 23  LEU   A CD1 1 
ATOM   31   C CD2 . LEU   A 1 6   ? -25.016 1.192   -14.832 1.00 20.29 ? 23  LEU   A CD2 1 
ATOM   32   N N   . TYR   A 1 7   ? -26.447 -3.321  -13.707 1.00 16.63 ? 24  TYR   A N   1 
ATOM   33   C CA  . TYR   A 1 7   ? -26.558 -4.700  -13.267 1.00 15.37 ? 24  TYR   A CA  1 
ATOM   34   C C   . TYR   A 1 7   ? -25.159 -5.113  -12.829 1.00 15.23 ? 24  TYR   A C   1 
ATOM   35   O O   . TYR   A 1 7   ? -24.223 -5.027  -13.630 1.00 17.88 ? 24  TYR   A O   1 
ATOM   36   C CB  . TYR   A 1 7   ? -26.996 -5.607  -14.420 1.00 15.04 ? 24  TYR   A CB  1 
ATOM   37   C CG  . TYR   A 1 7   ? -27.361 -7.011  -14.009 1.00 17.14 ? 24  TYR   A CG  1 
ATOM   38   C CD1 . TYR   A 1 7   ? -26.373 -7.966  -13.824 1.00 16.55 ? 24  TYR   A CD1 1 
ATOM   39   C CD2 . TYR   A 1 7   ? -28.682 -7.431  -14.032 1.00 18.32 ? 24  TYR   A CD2 1 
ATOM   40   C CE1 . TYR   A 1 7   ? -26.702 -9.257  -13.488 1.00 17.06 ? 24  TYR   A CE1 1 
ATOM   41   C CE2 . TYR   A 1 7   ? -29.027 -8.723  -13.730 1.00 18.54 ? 24  TYR   A CE2 1 
ATOM   42   C CZ  . TYR   A 1 7   ? -28.021 -9.628  -13.454 1.00 16.63 ? 24  TYR   A CZ  1 
ATOM   43   O OH  . TYR   A 1 7   ? -28.341 -10.944 -13.156 1.00 18.57 ? 24  TYR   A OH  1 
ATOM   44   N N   . PHE   A 1 8   ? -25.001 -5.551  -11.582 1.00 14.31 ? 25  PHE   A N   1 
ATOM   45   C CA  . PHE   A 1 8   ? -23.691 -5.992  -11.099 1.00 12.81 ? 25  PHE   A CA  1 
ATOM   46   C C   . PHE   A 1 8   ? -23.612 -7.508  -10.961 1.00 13.65 ? 25  PHE   A C   1 
ATOM   47   O O   . PHE   A 1 8   ? -24.525 -8.136  -10.413 1.00 15.91 ? 25  PHE   A O   1 
ATOM   48   C CB  . PHE   A 1 8   ? -23.341 -5.357  -9.748  1.00 14.53 ? 25  PHE   A CB  1 
ATOM   49   C CG  . PHE   A 1 8   ? -22.049 -5.887  -9.191  1.00 13.84 ? 25  PHE   A CG  1 
ATOM   50   C CD1 . PHE   A 1 8   ? -20.835 -5.503  -9.742  1.00 13.96 ? 25  PHE   A CD1 1 
ATOM   51   C CD2 . PHE   A 1 8   ? -22.061 -6.875  -8.209  1.00 15.29 ? 25  PHE   A CD2 1 
ATOM   52   C CE1 . PHE   A 1 8   ? -19.644 -6.045  -9.284  1.00 15.95 ? 25  PHE   A CE1 1 
ATOM   53   C CE2 . PHE   A 1 8   ? -20.867 -7.415  -7.737  1.00 14.72 ? 25  PHE   A CE2 1 
ATOM   54   C CZ  . PHE   A 1 8   ? -19.657 -6.992  -8.283  1.00 15.93 ? 25  PHE   A CZ  1 
ATOM   55   N N   . CYS   A 1 9   ? -22.483 -8.080  -11.397 1.00 12.98 ? 26  CYS   A N   1 
ATOM   56   C CA  . CYS   A 1 9   ? -22.216 -9.522  -11.295 1.00 12.80 ? 26  CYS   A CA  1 
ATOM   57   C C   . CYS   A 1 9   ? -20.954 -9.790  -10.480 1.00 13.41 ? 26  CYS   A C   1 
ATOM   58   O O   . CYS   A 1 9   ? -19.895 -9.209  -10.748 1.00 15.14 ? 26  CYS   A O   1 
ATOM   59   C CB  . CYS   A 1 9   ? -22.029 -10.199 -12.664 1.00 14.06 ? 26  CYS   A CB  1 
ATOM   60   S SG  . CYS   A 1 9   ? -23.108 -9.677  -14.009 1.00 15.28 ? 26  CYS   A SG  1 
ATOM   61   N N   . GLY   A 1 10  ? -21.053 -10.717 -9.523  1.00 12.46 ? 27  GLY   A N   1 
ATOM   62   C CA  . GLY   A 1 10  ? -19.901 -11.161 -8.757  1.00 12.81 ? 27  GLY   A CA  1 
ATOM   63   C C   . GLY   A 1 10  ? -20.228 -12.475 -8.080  1.00 12.04 ? 27  GLY   A C   1 
ATOM   64   O O   . GLY   A 1 10  ? -21.373 -12.715 -7.690  1.00 12.32 ? 27  GLY   A O   1 
ATOM   65   N N   . SER   A 1 11  ? -19.216 -13.342 -7.961  1.00 12.20 ? 28  SER   A N   1 
ATOM   66   C CA  . SER   A 1 11  ? -19.397 -14.678 -7.392  1.00 12.31 ? 28  SER   A CA  1 
ATOM   67   C C   . SER   A 1 11  ? -20.111 -14.651 -6.046  1.00 14.13 ? 28  SER   A C   1 
ATOM   68   O O   . SER   A 1 11  ? -19.793 -13.842 -5.165  1.00 13.31 ? 28  SER   A O   1 
ATOM   69   C CB  . SER   A 1 11  ? -18.026 -15.340 -7.221  1.00 12.61 ? 28  SER   A CB  1 
ATOM   70   O OG  . SER   A 1 11  ? -18.128 -16.666 -6.707  1.00 13.20 ? 28  SER   A OG  1 
ATOM   71   N N   . ILE   A 1 12  ? -21.051 -15.596 -5.877  1.00 13.50 ? 29  ILE   A N   1 
ATOM   72   C CA  . ILE   A 1 12  ? -21.684 -15.843 -4.585  1.00 13.17 ? 29  ILE   A CA  1 
ATOM   73   C C   . ILE   A 1 12  ? -21.478 -17.317 -4.241  1.00 14.83 ? 29  ILE   A C   1 
ATOM   74   O O   . ILE   A 1 12  ? -20.625 -17.647 -3.405  1.00 14.75 ? 29  ILE   A O   1 
ATOM   75   C CB  . ILE   A 1 12  ? -23.172 -15.445 -4.577  1.00 13.17 ? 29  ILE   A CB  1 
ATOM   76   C CG1 . ILE   A 1 12  ? -23.303 -13.942 -4.901  1.00 14.75 ? 29  ILE   A CG1 1 
ATOM   77   C CG2 . ILE   A 1 12  ? -23.806 -15.773 -3.200  1.00 16.81 ? 29  ILE   A CG2 1 
ATOM   78   C CD1 . ILE   A 1 12  ? -24.748 -13.464 -5.011  1.00 17.51 ? 29  ILE   A CD1 1 
ATOM   79   N N   . ARG   A 1 13  ? -22.222 -18.216 -4.895  1.00 13.18 ? 30  ARG   A N   1 
ATOM   80   C CA  . ARG   A 1 13  ? -21.994 -19.640 -4.613  1.00 13.65 ? 30  ARG   A CA  1 
ATOM   81   C C   . ARG   A 1 13  ? -20.674 -20.140 -5.182  1.00 14.05 ? 30  ARG   A C   1 
ATOM   82   O O   . ARG   A 1 13  ? -20.165 -21.162 -4.714  1.00 16.71 ? 30  ARG   A O   1 
ATOM   83   C CB  . ARG   A 1 13  ? -23.170 -20.483 -5.095  1.00 14.06 ? 30  ARG   A CB  1 
ATOM   84   C CG  . ARG   A 1 13  ? -24.448 -20.116 -4.343  1.00 15.13 ? 30  ARG   A CG  1 
ATOM   85   C CD  . ARG   A 1 13  ? -25.594 -20.997 -4.711  1.00 13.94 ? 30  ARG   A CD  1 
ATOM   86   N NE  . ARG   A 1 13  ? -26.820 -20.601 -4.027  1.00 16.52 ? 30  ARG   A NE  1 
ATOM   87   C CZ  . ARG   A 1 13  ? -28.035 -20.998 -4.388  1.00 18.57 ? 30  ARG   A CZ  1 
ATOM   88   N NH1 . ARG   A 1 13  ? -28.216 -21.891 -5.349  1.00 17.64 ? 30  ARG   A NH1 1 
ATOM   89   N NH2 . ARG   A 1 13  ? -29.101 -20.465 -3.787  1.00 19.53 ? 30  ARG   A NH2 1 
ATOM   90   N N   . GLY   A 1 14  ? -20.070 -19.422 -6.124  1.00 13.45 ? 31  GLY   A N   1 
ATOM   91   C CA  . GLY   A 1 14  ? -18.699 -19.767 -6.471  1.00 14.27 ? 31  GLY   A CA  1 
ATOM   92   C C   . GLY   A 1 14  ? -17.691 -19.430 -5.390  1.00 16.79 ? 31  GLY   A C   1 
ATOM   93   O O   . GLY   A 1 14  ? -16.539 -19.873 -5.478  1.00 17.84 ? 31  GLY   A O   1 
ATOM   94   N N   . GLY   A 1 15  ? -18.108 -18.698 -4.363  1.00 15.88 ? 32  GLY   A N   1 
ATOM   95   C CA  . GLY   A 1 15  ? -17.230 -18.253 -3.304  1.00 16.08 ? 32  GLY   A CA  1 
ATOM   96   C C   . GLY   A 1 15  ? -17.367 -16.757 -3.104  1.00 15.57 ? 32  GLY   A C   1 
ATOM   97   O O   . GLY   A 1 15  ? -17.524 -16.010 -4.072  1.00 15.44 ? 32  GLY   A O   1 
ATOM   98   N N   . ARG   A 1 16  ? -17.313 -16.299 -1.858  1.00 15.49 ? 33  ARG   A N   1 
ATOM   99   C CA  . ARG   A 1 16  ? -17.500 -14.891 -1.534  1.00 16.47 ? 33  ARG   A CA  1 
ATOM   100  C C   . ARG   A 1 16  ? -16.188 -14.213 -1.141  1.00 16.37 ? 33  ARG   A C   1 
ATOM   101  O O   . ARG   A 1 16  ? -16.196 -13.223 -0.399  1.00 18.72 ? 33  ARG   A O   1 
ATOM   102  C CB  . ARG   A 1 16  ? -18.546 -14.757 -0.427  1.00 18.17 ? 33  ARG   A CB  1 
ATOM   103  C CG  . ARG   A 1 16  ? -19.860 -15.518 -0.746  1.00 16.89 ? 33  ARG   A CG  1 
ATOM   104  C CD  . ARG   A 1 16  ? -21.099 -14.971 -0.046  1.00 20.13 ? 33  ARG   A CD  1 
ATOM   105  N NE  . ARG   A 1 16  ? -21.514 -13.676 -0.568  1.00 18.81 ? 33  ARG   A NE  1 
ATOM   106  C CZ  . ARG   A 1 16  ? -22.552 -12.979 -0.114  1.00 20.17 ? 33  ARG   A CZ  1 
ATOM   107  N NH1 . ARG   A 1 16  ? -23.268 -13.400 0.920   1.00 23.92 ? 33  ARG   A NH1 1 
ATOM   108  N NH2 . ARG   A 1 16  ? -22.889 -11.843 -0.725  1.00 22.66 ? 33  ARG   A NH2 1 
ATOM   109  N N   . GLU   A 1 17  ? -15.062 -14.720 -1.657  1.00 16.98 ? 34  GLU   A N   1 
ATOM   110  C CA  . GLU   A 1 17  ? -13.752 -14.150 -1.326  1.00 16.31 ? 34  GLU   A CA  1 
ATOM   111  C C   . GLU   A 1 17  ? -13.686 -12.644 -1.571  1.00 16.42 ? 34  GLU   A C   1 
ATOM   112  O O   . GLU   A 1 17  ? -13.028 -11.923 -0.810  1.00 17.66 ? 34  GLU   A O   1 
ATOM   113  C CB  . GLU   A 1 17  ? -12.659 -14.850 -2.142  1.00 18.42 ? 34  GLU   A CB  1 
ATOM   114  C CG  . GLU   A 1 17  ? -12.320 -16.293 -1.748  1.00 20.65 ? 34  GLU   A CG  1 
ATOM   115  C CD  . GLU   A 1 17  ? -13.199 -17.351 -2.410  1.00 23.06 ? 34  GLU   A CD  1 
ATOM   116  O OE1 . GLU   A 1 17  ? -14.294 -17.048 -2.926  1.00 19.77 ? 34  GLU   A OE1 1 
ATOM   117  O OE2 . GLU   A 1 17  ? -12.759 -18.516 -2.455  1.00 21.50 ? 34  GLU   A OE2 1 
ATOM   118  N N   . ASP   A 1 18  ? -14.324 -12.153 -2.642  1.00 14.84 ? 35  ASP   A N   1 
ATOM   119  C CA  . ASP   A 1 18  ? -14.210 -10.761 -3.074  1.00 14.68 ? 35  ASP   A CA  1 
ATOM   120  C C   . ASP   A 1 18  ? -15.422 -9.909  -2.691  1.00 15.86 ? 35  ASP   A C   1 
ATOM   121  O O   . ASP   A 1 18  ? -15.589 -8.808  -3.237  1.00 15.08 ? 35  ASP   A O   1 
ATOM   122  C CB  . ASP   A 1 18  ? -13.983 -10.688 -4.590  1.00 16.57 ? 35  ASP   A CB  1 
ATOM   123  C CG  . ASP   A 1 18  ? -12.601 -11.161 -5.025  1.00 17.67 ? 35  ASP   A CG  1 
ATOM   124  O OD1 . ASP   A 1 18  ? -11.666 -11.190 -4.198  1.00 19.82 ? 35  ASP   A OD1 1 
ATOM   125  O OD2 . ASP   A 1 18  ? -12.450 -11.494 -6.221  1.00 18.14 ? 35  ASP   A OD2 1 
ATOM   126  N N   . ARG   A 1 19  ? -16.242 -10.381 -1.744  1.00 15.19 ? 36  ARG   A N   1 
ATOM   127  C CA  . ARG   A 1 19  ? -17.463 -9.675  -1.344  1.00 14.83 ? 36  ARG   A CA  1 
ATOM   128  C C   . ARG   A 1 19  ? -17.233 -8.208  -0.950  1.00 16.20 ? 36  ARG   A C   1 
ATOM   129  O O   . ARG   A 1 19  ? -18.029 -7.336  -1.323  1.00 16.28 ? 36  ARG   A O   1 
ATOM   130  C CB  . ARG   A 1 19  ? -18.132 -10.446 -0.215  1.00 16.88 ? 36  ARG   A CB  1 
ATOM   131  C CG  . ARG   A 1 19  ? -19.368 -9.797  0.365   1.00 19.90 ? 36  ARG   A CG  1 
ATOM   132  C CD  . ARG   A 1 19  ? -19.987 -10.733 1.384   1.00 19.74 ? 36  ARG   A CD  1 
ATOM   133  N NE  . ARG   A 1 19  ? -21.359 -10.358 1.715   1.00 22.85 ? 36  ARG   A NE  1 
ATOM   134  C CZ  . ARG   A 1 19  ? -21.931 -10.636 2.878   1.00 25.62 ? 36  ARG   A CZ  1 
ATOM   135  N NH1 . ARG   A 1 19  ? -21.364 -11.459 3.741   1.00 26.34 ? 36  ARG   A NH1 1 
ATOM   136  N NH2 . ARG   A 1 19  ? -23.123 -10.115 3.161   1.00 28.58 ? 36  ARG   A NH2 1 
ATOM   137  N N   . THR   A 1 20  ? -16.163 -7.904  -0.200  1.00 15.52 ? 37  THR   A N   1 
ATOM   138  C CA  . THR   A 1 20  ? -15.919 -6.512  0.189   1.00 16.78 ? 37  THR   A CA  1 
ATOM   139  C C   . THR   A 1 20  ? -15.624 -5.641  -1.025  1.00 15.25 ? 37  THR   A C   1 
ATOM   140  O O   . THR   A 1 20  ? -16.102 -4.503  -1.118  1.00 15.61 ? 37  THR   A O   1 
ATOM   141  C CB  . THR   A 1 20  ? -14.768 -6.424  1.201   1.00 16.41 ? 37  THR   A CB  1 
ATOM   142  O OG1 . THR   A 1 20  ? -15.069 -7.251  2.329   1.00 19.16 ? 37  THR   A OG1 1 
ATOM   143  C CG2 . THR   A 1 20  ? -14.538 -4.964  1.650   1.00 18.90 ? 37  THR   A CG2 1 
ATOM   144  N N   . LEU   A 1 21  ? -14.847 -6.164  -1.972  1.00 15.25 ? 38  LEU   A N   1 
ATOM   145  C CA  . LEU   A 1 21  ? -14.629 -5.465  -3.232  1.00 16.46 ? 38  LEU   A CA  1 
ATOM   146  C C   . LEU   A 1 21  ? -15.932 -5.272  -3.991  1.00 17.08 ? 38  LEU   A C   1 
ATOM   147  O O   . LEU   A 1 21  ? -16.165 -4.200  -4.568  1.00 16.42 ? 38  LEU   A O   1 
ATOM   148  C CB  . LEU   A 1 21  ? -13.628 -6.248  -4.079  1.00 17.34 ? 38  LEU   A CB  1 
ATOM   149  C CG  . LEU   A 1 21  ? -13.352 -5.752  -5.497  1.00 20.77 ? 38  LEU   A CG  1 
ATOM   150  C CD1 . LEU   A 1 21  ? -12.716 -4.379  -5.488  1.00 20.80 ? 38  LEU   A CD1 1 
ATOM   151  C CD2 . LEU   A 1 21  ? -12.437 -6.734  -6.217  1.00 22.19 ? 38  LEU   A CD2 1 
ATOM   152  N N   . TYR   A 1 22  ? -16.796 -6.296  -4.021  1.00 15.22 ? 39  TYR   A N   1 
ATOM   153  C CA  . TYR   A 1 22  ? -18.068 -6.109  -4.707  1.00 14.83 ? 39  TYR   A CA  1 
ATOM   154  C C   . TYR   A 1 22  ? -18.873 -4.993  -4.067  1.00 16.64 ? 39  TYR   A C   1 
ATOM   155  O O   . TYR   A 1 22  ? -19.530 -4.216  -4.770  1.00 17.17 ? 39  TYR   A O   1 
ATOM   156  C CB  . TYR   A 1 22  ? -18.909 -7.388  -4.728  1.00 13.30 ? 39  TYR   A CB  1 
ATOM   157  C CG  . TYR   A 1 22  ? -18.251 -8.619  -5.263  1.00 13.28 ? 39  TYR   A CG  1 
ATOM   158  C CD1 . TYR   A 1 22  ? -17.183 -8.547  -6.149  1.00 13.09 ? 39  TYR   A CD1 1 
ATOM   159  C CD2 . TYR   A 1 22  ? -18.762 -9.877  -4.940  1.00 13.63 ? 39  TYR   A CD2 1 
ATOM   160  C CE1 . TYR   A 1 22  ? -16.582 -9.721  -6.652  1.00 15.19 ? 39  TYR   A CE1 1 
ATOM   161  C CE2 . TYR   A 1 22  ? -18.190 -11.040 -5.443  1.00 13.29 ? 39  TYR   A CE2 1 
ATOM   162  C CZ  . TYR   A 1 22  ? -17.115 -10.957 -6.293  1.00 14.19 ? 39  TYR   A CZ  1 
ATOM   163  O OH  . TYR   A 1 22  ? -16.559 -12.119 -6.771  1.00 14.57 ? 39  TYR   A OH  1 
ATOM   164  N N   . GLU   A 1 23  ? -18.833 -4.898  -2.737  1.00 14.19 ? 40  GLU   A N   1 
ATOM   165  C CA  . GLU   A 1 23  ? -19.563 -3.824  -2.069  1.00 15.32 ? 40  GLU   A CA  1 
ATOM   166  C C   . GLU   A 1 23  ? -19.007 -2.460  -2.469  1.00 16.56 ? 40  GLU   A C   1 
ATOM   167  O O   . GLU   A 1 23  ? -19.769 -1.496  -2.640  1.00 16.38 ? 40  GLU   A O   1 
ATOM   168  C CB  . GLU   A 1 23  ? -19.527 -3.980  -0.545  1.00 17.17 ? 40  GLU   A CB  1 
ATOM   169  C CG  . GLU   A 1 23  ? -20.495 -5.046  0.014   1.00 15.43 ? 40  GLU   A CG  1 
ATOM   170  C CD  . GLU   A 1 23  ? -20.003 -5.749  1.266   1.00 19.14 ? 40  GLU   A CD  1 
ATOM   171  O OE1 . GLU   A 1 23  ? -18.878 -5.473  1.744   1.00 18.59 ? 40  GLU   A OE1 1 
ATOM   172  O OE2 . GLU   A 1 23  ? -20.827 -6.473  1.869   1.00 18.73 ? 40  GLU   A OE2 1 
ATOM   173  N N   . ARG   A 1 24  ? -17.678 -2.354  -2.624  1.00 16.09 ? 41  ARG   A N   1 
ATOM   174  C CA  . ARG   A 1 24  ? -17.088 -1.103  -3.104  1.00 16.28 ? 41  ARG   A CA  1 
ATOM   175  C C   . ARG   A 1 24  ? -17.544 -0.786  -4.516  1.00 15.94 ? 41  ARG   A C   1 
ATOM   176  O O   . ARG   A 1 24  ? -17.836 0.371   -4.845  1.00 17.50 ? 41  ARG   A O   1 
ATOM   177  C CB  . ARG   A 1 24  ? -15.565 -1.192  -3.063  1.00 16.20 ? 41  ARG   A CB  1 
ATOM   178  C CG  . ARG   A 1 24  ? -14.980 -1.001  -1.687  1.00 17.67 ? 41  ARG   A CG  1 
ATOM   179  C CD  . ARG   A 1 24  ? -13.501 -1.378  -1.693  1.00 21.67 ? 41  ARG   A CD  1 
ATOM   180  N NE  . ARG   A 1 24  ? -12.721 -0.639  -2.680  1.00 20.25 ? 41  ARG   A NE  1 
ATOM   181  C CZ  . ARG   A 1 24  ? -11.534 -1.036  -3.123  1.00 24.85 ? 41  ARG   A CZ  1 
ATOM   182  N NH1 . ARG   A 1 24  ? -10.993 -2.173  -2.714  1.00 24.44 ? 41  ARG   A NH1 1 
ATOM   183  N NH2 . ARG   A 1 24  ? -10.872 -0.270  -3.990  1.00 24.79 ? 41  ARG   A NH2 1 
ATOM   184  N N   . ILE   A 1 25  ? -17.597 -1.799  -5.377  1.00 15.72 ? 42  ILE   A N   1 
ATOM   185  C CA  . ILE   A 1 25  ? -18.010 -1.560  -6.755  1.00 16.23 ? 42  ILE   A CA  1 
ATOM   186  C C   . ILE   A 1 25  ? -19.452 -1.082  -6.796  1.00 16.64 ? 42  ILE   A C   1 
ATOM   187  O O   . ILE   A 1 25  ? -19.783 -0.108  -7.480  1.00 16.30 ? 42  ILE   A O   1 
ATOM   188  C CB  . ILE   A 1 25  ? -17.811 -2.834  -7.594  1.00 15.27 ? 42  ILE   A CB  1 
ATOM   189  C CG1 . ILE   A 1 25  ? -16.327 -3.105  -7.765  1.00 14.98 ? 42  ILE   A CG1 1 
ATOM   190  C CG2 . ILE   A 1 25  ? -18.520 -2.693  -8.919  1.00 17.44 ? 42  ILE   A CG2 1 
ATOM   191  C CD1 . ILE   A 1 25  ? -16.007 -4.497  -8.316  1.00 15.79 ? 42  ILE   A CD1 1 
ATOM   192  N N   . VAL   A 1 26  ? -20.325 -1.748  -6.039  1.00 15.33 ? 43  VAL   A N   1 
ATOM   193  C CA  . VAL   A 1 26  ? -21.731 -1.357  -6.014  1.00 16.30 ? 43  VAL   A CA  1 
ATOM   194  C C   . VAL   A 1 26  ? -21.897 0.038   -5.423  1.00 15.73 ? 43  VAL   A C   1 
ATOM   195  O O   . VAL   A 1 26  ? -22.718 0.836   -5.902  1.00 17.03 ? 43  VAL   A O   1 
ATOM   196  C CB  . VAL   A 1 26  ? -22.546 -2.415  -5.256  1.00 14.44 ? 43  VAL   A CB  1 
ATOM   197  C CG1 . VAL   A 1 26  ? -23.951 -1.914  -4.951  1.00 20.50 ? 43  VAL   A CG1 1 
ATOM   198  C CG2 . VAL   A 1 26  ? -22.601 -3.689  -6.112  1.00 17.61 ? 43  VAL   A CG2 1 
ATOM   199  N N   . SER   A 1 27  ? -21.115 0.369   -4.390  1.00 16.47 ? 44  SER   A N   1 
ATOM   200  C CA  . SER   A 1 27  ? -21.199 1.712   -3.819  1.00 15.44 ? 44  SER   A CA  1 
ATOM   201  C C   . SER   A 1 27  ? -20.861 2.761   -4.863  1.00 16.89 ? 44  SER   A C   1 
ATOM   202  O O   . SER   A 1 27  ? -21.521 3.805   -4.945  1.00 17.71 ? 44  SER   A O   1 
ATOM   203  C CB  . SER   A 1 27  ? -20.242 1.831   -2.635  1.00 19.14 ? 44  SER   A CB  1 
ATOM   204  O OG  . SER   A 1 27  ? -20.753 1.124   -1.514  1.00 19.68 ? 44  SER   A OG  1 
ATOM   205  N N   . ARG   A 1 28  ? -19.833 2.502   -5.674  1.00 16.88 ? 45  ARG   A N   1 
ATOM   206  C CA  . ARG   A 1 28  ? -19.466 3.477   -6.693  1.00 18.98 ? 45  ARG   A CA  1 
ATOM   207  C C   . ARG   A 1 28  ? -20.495 3.501   -7.819  1.00 19.48 ? 45  ARG   A C   1 
ATOM   208  O O   . ARG   A 1 28  ? -20.849 4.574   -8.319  1.00 21.15 ? 45  ARG   A O   1 
ATOM   209  C CB  . ARG   A 1 28  ? -18.056 3.184   -7.219  1.00 17.73 ? 45  ARG   A CB  1 
ATOM   210  C CG  . ARG   A 1 28  ? -17.554 4.152   -8.307  1.00 18.23 ? 45  ARG   A CG  1 
ATOM   211  C CD  . ARG   A 1 28  ? -17.770 5.625   -7.923  1.00 21.52 ? 45  ARG   A CD  1 
ATOM   212  N NE  . ARG   A 1 28  ? -17.170 5.956   -6.638  1.00 21.20 ? 45  ARG   A NE  1 
ATOM   213  C CZ  . ARG   A 1 28  ? -16.049 6.645   -6.457  1.00 25.85 ? 45  ARG   A CZ  1 
ATOM   214  N NH1 . ARG   A 1 28  ? -15.420 7.235   -7.466  1.00 23.88 ? 45  ARG   A NH1 1 
ATOM   215  N NH2 . ARG   A 1 28  ? -15.571 6.788   -5.222  1.00 21.17 ? 45  ARG   A NH2 1 
ATOM   216  N N   . LEU   A 1 29  ? -21.009 2.331   -8.214  1.00 17.73 ? 46  LEU   A N   1 
ATOM   217  C CA  . LEU   A 1 29  ? -22.015 2.306   -9.270  1.00 17.40 ? 46  LEU   A CA  1 
ATOM   218  C C   . LEU   A 1 29  ? -23.254 3.106   -8.879  1.00 20.97 ? 46  LEU   A C   1 
ATOM   219  O O   . LEU   A 1 29  ? -23.854 3.775   -9.723  1.00 21.25 ? 46  LEU   A O   1 
ATOM   220  C CB  . LEU   A 1 29  ? -22.399 0.871   -9.624  1.00 16.02 ? 46  LEU   A CB  1 
ATOM   221  C CG  . LEU   A 1 29  ? -21.323 0.038   -10.305 1.00 17.14 ? 46  LEU   A CG  1 
ATOM   222  C CD1 . LEU   A 1 29  ? -21.890 -1.357  -10.490 1.00 17.37 ? 46  LEU   A CD1 1 
ATOM   223  C CD2 . LEU   A 1 29  ? -20.878 0.647   -11.626 1.00 18.96 ? 46  LEU   A CD2 1 
ATOM   224  N N   . ARG   A 1 30  ? -23.645 3.059   -7.602  1.00 20.51 ? 47  ARG   A N   1 
ATOM   225  C CA  . ARG   A 1 30  ? -24.793 3.837   -7.125  1.00 20.61 ? 47  ARG   A CA  1 
ATOM   226  C C   . ARG   A 1 30  ? -24.610 5.340   -7.278  1.00 23.41 ? 47  ARG   A C   1 
ATOM   227  O O   . ARG   A 1 30  ? -25.611 6.059   -7.355  1.00 27.03 ? 47  ARG   A O   1 
ATOM   228  C CB  . ARG   A 1 30  ? -25.090 3.488   -5.670  1.00 20.63 ? 47  ARG   A CB  1 
ATOM   229  C CG  . ARG   A 1 30  ? -25.788 2.159   -5.577  1.00 22.77 ? 47  ARG   A CG  1 
ATOM   230  C CD  . ARG   A 1 30  ? -26.056 1.667   -4.180  1.00 31.14 ? 47  ARG   A CD  1 
ATOM   231  N NE  . ARG   A 1 30  ? -26.897 0.480   -4.268  1.00 37.84 ? 47  ARG   A NE  1 
ATOM   232  C CZ  . ARG   A 1 30  ? -27.182 -0.333  -3.262  1.00 44.82 ? 47  ARG   A CZ  1 
ATOM   233  N NH1 . ARG   A 1 30  ? -26.484 -0.315  -2.137  1.00 46.12 ? 47  ARG   A NH1 1 
ATOM   234  N NH2 . ARG   A 1 30  ? -28.173 -1.205  -3.399  1.00 46.26 ? 47  ARG   A NH2 1 
ATOM   235  N N   . ARG   A 1 31  ? -23.368 5.827   -7.329  1.00 22.18 ? 48  ARG   A N   1 
ATOM   236  C CA  . ARG   A 1 31  ? -23.155 7.240   -7.616  1.00 21.67 ? 48  ARG   A CA  1 
ATOM   237  C C   . ARG   A 1 31  ? -23.643 7.606   -9.011  1.00 25.32 ? 48  ARG   A C   1 
ATOM   238  O O   . ARG   A 1 31  ? -24.010 8.759   -9.257  1.00 26.47 ? 48  ARG   A O   1 
ATOM   239  C CB  . ARG   A 1 31  ? -21.678 7.606   -7.497  1.00 23.23 ? 48  ARG   A CB  1 
ATOM   240  C CG  . ARG   A 1 31  ? -21.003 7.143   -6.232  1.00 28.85 ? 48  ARG   A CG  1 
ATOM   241  C CD  . ARG   A 1 31  ? -20.514 8.311   -5.474  1.00 24.34 ? 48  ARG   A CD  1 
ATOM   242  N NE  . ARG   A 1 31  ? -19.790 7.944   -4.268  1.00 22.81 ? 48  ARG   A NE  1 
ATOM   243  C CZ  . ARG   A 1 31  ? -18.603 8.444   -3.958  1.00 20.72 ? 48  ARG   A CZ  1 
ATOM   244  N NH1 . ARG   A 1 31  ? -18.015 9.351   -4.726  1.00 24.51 ? 48  ARG   A NH1 1 
ATOM   245  N NH2 . ARG   A 1 31  ? -18.000 8.040   -2.848  1.00 19.91 ? 48  ARG   A NH2 1 
ATOM   246  N N   . PHE   A 1 32  ? -23.639 6.649   -9.937  1.00 23.93 ? 49  PHE   A N   1 
ATOM   247  C CA  . PHE   A 1 32  ? -23.938 6.922   -11.336 1.00 25.84 ? 49  PHE   A CA  1 
ATOM   248  C C   . PHE   A 1 32  ? -25.339 6.524   -11.761 1.00 26.74 ? 49  PHE   A C   1 
ATOM   249  O O   . PHE   A 1 32  ? -25.880 7.124   -12.694 1.00 27.79 ? 49  PHE   A O   1 
ATOM   250  C CB  . PHE   A 1 32  ? -22.935 6.202   -12.239 1.00 25.08 ? 49  PHE   A CB  1 
ATOM   251  C CG  . PHE   A 1 32  ? -21.508 6.548   -11.955 1.00 27.66 ? 49  PHE   A CG  1 
ATOM   252  C CD1 . PHE   A 1 32  ? -21.069 7.859   -12.040 1.00 35.03 ? 49  PHE   A CD1 1 
ATOM   253  C CD2 . PHE   A 1 32  ? -20.611 5.571   -11.562 1.00 32.55 ? 49  PHE   A CD2 1 
ATOM   254  C CE1 . PHE   A 1 32  ? -19.748 8.178   -11.778 1.00 37.07 ? 49  PHE   A CE1 1 
ATOM   255  C CE2 . PHE   A 1 32  ? -19.295 5.893   -11.283 1.00 30.88 ? 49  PHE   A CE2 1 
ATOM   256  C CZ  . PHE   A 1 32  ? -18.870 7.184   -11.389 1.00 33.59 ? 49  PHE   A CZ  1 
ATOM   257  N N   . GLY   A 1 33  ? -25.926 5.514   -11.139 1.00 25.08 ? 50  GLY   A N   1 
ATOM   258  C CA  . GLY   A 1 33  ? -27.246 5.097   -11.557 1.00 27.02 ? 50  GLY   A CA  1 
ATOM   259  C C   . GLY   A 1 33  ? -27.845 4.142   -10.555 1.00 27.24 ? 50  GLY   A C   1 
ATOM   260  O O   . GLY   A 1 33  ? -27.349 3.989   -9.442  1.00 30.08 ? 50  GLY   A O   1 
ATOM   261  N N   . THR   A 1 34  ? -28.918 3.490   -10.982 1.00 28.88 ? 51  THR   A N   1 
ATOM   262  C CA  . THR   A 1 34  ? -29.669 2.564   -10.144 1.00 26.39 ? 51  THR   A CA  1 
ATOM   263  C C   . THR   A 1 34  ? -29.107 1.163   -10.347 1.00 21.92 ? 51  THR   A C   1 
ATOM   264  O O   . THR   A 1 34  ? -29.028 0.695   -11.483 1.00 23.94 ? 51  THR   A O   1 
ATOM   265  C CB  . THR   A 1 34  ? -31.146 2.614   -10.534 1.00 25.93 ? 51  THR   A CB  1 
ATOM   266  O OG1 . THR   A 1 34  ? -31.682 3.896   -10.177 1.00 31.67 ? 51  THR   A OG1 1 
ATOM   267  C CG2 . THR   A 1 34  ? -31.936 1.527   -9.836  1.00 29.51 ? 51  THR   A CG2 1 
ATOM   268  N N   . VAL   A 1 35  ? -28.702 0.499   -9.265  1.00 21.12 ? 52  VAL   A N   1 
ATOM   269  C CA  . VAL   A 1 35  ? -28.176 -0.866  -9.355  1.00 21.41 ? 52  VAL   A CA  1 
ATOM   270  C C   . VAL   A 1 35  ? -29.343 -1.827  -9.158  1.00 25.76 ? 52  VAL   A C   1 
ATOM   271  O O   . VAL   A 1 35  ? -29.770 -2.078  -8.028  1.00 25.43 ? 52  VAL   A O   1 
ATOM   272  C CB  . VAL   A 1 35  ? -27.048 -1.114  -8.355  1.00 21.02 ? 52  VAL   A CB  1 
ATOM   273  C CG1 . VAL   A 1 35  ? -26.499 -2.533  -8.501  1.00 24.31 ? 52  VAL   A CG1 1 
ATOM   274  C CG2 . VAL   A 1 35  ? -25.933 -0.105  -8.597  1.00 21.36 ? 52  VAL   A CG2 1 
ATOM   275  N N   . LEU   A 1 36  ? -29.838 -2.392  -10.273 1.00 21.75 ? 53  LEU   A N   1 
ATOM   276  C CA  . LEU   A 1 36  ? -31.048 -3.214  -10.236 1.00 23.29 ? 53  LEU   A CA  1 
ATOM   277  C C   . LEU   A 1 36  ? -30.867 -4.479  -9.417  1.00 24.10 ? 53  LEU   A C   1 
ATOM   278  O O   . LEU   A 1 36  ? -31.838 -4.984  -8.839  1.00 25.57 ? 53  LEU   A O   1 
ATOM   279  C CB  . LEU   A 1 36  ? -31.496 -3.600  -11.652 1.00 21.84 ? 53  LEU   A CB  1 
ATOM   280  C CG  . LEU   A 1 36  ? -31.766 -2.508  -12.687 1.00 21.77 ? 53  LEU   A CG  1 
ATOM   281  C CD1 . LEU   A 1 36  ? -31.883 -3.165  -14.058 1.00 26.14 ? 53  LEU   A CD1 1 
ATOM   282  C CD2 . LEU   A 1 36  ? -33.038 -1.759  -12.320 1.00 26.25 ? 53  LEU   A CD2 1 
ATOM   283  N N   . THR   A 1 37  ? -29.657 -5.012  -9.371  1.00 22.95 ? 54  THR   A N   1 
ATOM   284  C CA  . THR   A 1 37  ? -29.428 -6.303  -8.741  1.00 26.85 ? 54  THR   A CA  1 
ATOM   285  C C   . THR   A 1 37  ? -29.363 -6.217  -7.224  1.00 29.73 ? 54  THR   A C   1 
ATOM   286  O O   . THR   A 1 37  ? -29.261 -7.256  -6.562  1.00 31.73 ? 54  THR   A O   1 
ATOM   287  C CB  . THR   A 1 37  ? -28.136 -6.921  -9.284  1.00 23.61 ? 54  THR   A CB  1 
ATOM   288  O OG1 . THR   A 1 37  ? -27.115 -5.910  -9.387  1.00 21.10 ? 54  THR   A OG1 1 
ATOM   289  C CG2 . THR   A 1 37  ? -28.381 -7.465  -10.663 1.00 22.21 ? 54  THR   A CG2 1 
ATOM   290  N N   . GLU   A 1 38  ? -29.433 -5.019  -6.656  1.00 34.52 ? 55  GLU   A N   1 
ATOM   291  C CA  . GLU   A 1 38  ? -29.340 -4.868  -5.211  1.00 39.51 ? 55  GLU   A CA  1 
ATOM   292  C C   . GLU   A 1 38  ? -30.702 -4.577  -4.603  1.00 42.20 ? 55  GLU   A C   1 
ATOM   293  O O   . GLU   A 1 38  ? -31.725 -4.714  -5.273  1.00 50.51 ? 55  GLU   A O   1 
ATOM   294  C CB  . GLU   A 1 38  ? -28.357 -3.760  -4.867  1.00 40.75 ? 55  GLU   A CB  1 
ATOM   295  C CG  . GLU   A 1 38  ? -26.897 -4.092  -5.125  1.00 39.62 ? 55  GLU   A CG  1 
ATOM   296  C CD  . GLU   A 1 38  ? -26.294 -5.007  -4.071  1.00 43.46 ? 55  GLU   A CD  1 
ATOM   297  O OE1 . GLU   A 1 38  ? -26.084 -4.541  -2.923  1.00 43.47 ? 55  GLU   A OE1 1 
ATOM   298  O OE2 . GLU   A 1 38  ? -26.032 -6.189  -4.391  1.00 45.29 ? 55  GLU   A OE2 1 
ATOM   299  N N   . GLY   A 1 54  ? -39.737 -18.877 -4.032  1.00 50.18 ? 71  GLY   A N   1 
ATOM   300  C CA  . GLY   A 1 54  ? -39.472 -19.081 -5.446  1.00 46.95 ? 71  GLY   A CA  1 
ATOM   301  C C   . GLY   A 1 54  ? -38.211 -19.885 -5.730  1.00 42.07 ? 71  GLY   A C   1 
ATOM   302  O O   . GLY   A 1 54  ? -37.993 -20.348 -6.854  1.00 40.19 ? 71  GLY   A O   1 
ATOM   303  N N   . GLY   A 1 55  ? -37.380 -20.045 -4.701  1.00 42.99 ? 72  GLY   A N   1 
ATOM   304  C CA  . GLY   A 1 55  ? -36.142 -20.782 -4.814  1.00 32.32 ? 72  GLY   A CA  1 
ATOM   305  C C   . GLY   A 1 55  ? -35.190 -20.175 -5.829  1.00 30.39 ? 72  GLY   A C   1 
ATOM   306  O O   . GLY   A 1 55  ? -35.129 -18.957 -6.051  1.00 30.10 ? 72  GLY   A O   1 
ATOM   307  N N   . ASP   A 1 56  ? -34.428 -21.051 -6.472  1.00 28.72 ? 73  ASP   A N   1 
ATOM   308  C CA  . ASP   A 1 56  ? -33.469 -20.583 -7.453  1.00 24.18 ? 73  ASP   A CA  1 
ATOM   309  C C   . ASP   A 1 56  ? -34.133 -20.156 -8.752  1.00 22.56 ? 73  ASP   A C   1 
ATOM   310  O O   . ASP   A 1 56  ? -33.567 -19.327 -9.478  1.00 20.69 ? 73  ASP   A O   1 
ATOM   311  C CB  . ASP   A 1 56  ? -32.423 -21.663 -7.714  1.00 23.74 ? 73  ASP   A CB  1 
ATOM   312  C CG  . ASP   A 1 56  ? -31.515 -21.884 -6.512  1.00 27.07 ? 73  ASP   A CG  1 
ATOM   313  O OD1 . ASP   A 1 56  ? -31.508 -21.030 -5.592  1.00 27.70 ? 73  ASP   A OD1 1 
ATOM   314  O OD2 . ASP   A 1 56  ? -30.738 -22.854 -6.535  1.00 29.10 ? 73  ASP   A OD2 1 
ATOM   315  N N   . ARG   A 1 57  ? -35.303 -20.706 -9.077  1.00 25.72 ? 74  ARG   A N   1 
ATOM   316  C CA  A ARG   A 1 57  ? -36.026 -20.256 -10.263 0.67 24.87 ? 74  ARG   A CA  1 
ATOM   317  C CA  B ARG   A 1 57  ? -36.010 -20.254 -10.268 0.11 24.93 ? 74  ARG   A CA  1 
ATOM   318  C CA  C ARG   A 1 57  ? -36.008 -20.250 -10.271 0.22 24.91 ? 74  ARG   A CA  1 
ATOM   319  C C   . ARG   A 1 57  ? -36.383 -18.777 -10.174 1.00 23.31 ? 74  ARG   A C   1 
ATOM   320  O O   . ARG   A 1 57  ? -36.246 -18.041 -11.152 1.00 22.73 ? 74  ARG   A O   1 
ATOM   321  C CB  A ARG   A 1 57  ? -37.292 -21.087 -10.457 0.67 27.25 ? 74  ARG   A CB  1 
ATOM   322  C CB  B ARG   A 1 57  ? -37.226 -21.160 -10.516 0.11 27.27 ? 74  ARG   A CB  1 
ATOM   323  C CB  C ARG   A 1 57  ? -37.255 -21.090 -10.520 0.22 27.27 ? 74  ARG   A CB  1 
ATOM   324  C CG  A ARG   A 1 57  ? -38.102 -20.692 -11.678 0.67 29.59 ? 74  ARG   A CG  1 
ATOM   325  C CG  B ARG   A 1 57  ? -38.134 -20.771 -11.677 0.11 29.56 ? 74  ARG   A CG  1 
ATOM   326  C CG  C ARG   A 1 57  ? -36.992 -22.548 -10.802 0.22 27.73 ? 74  ARG   A CG  1 
ATOM   327  C CD  A ARG   A 1 57  ? -37.429 -21.145 -12.950 0.67 29.48 ? 74  ARG   A CD  1 
ATOM   328  C CD  B ARG   A 1 57  ? -37.405 -20.782 -13.001 0.11 29.05 ? 74  ARG   A CD  1 
ATOM   329  C CD  C ARG   A 1 57  ? -38.300 -23.241 -11.115 0.22 30.46 ? 74  ARG   A CD  1 
ATOM   330  N NE  A ARG   A 1 57  ? -38.307 -21.015 -14.107 0.67 31.65 ? 74  ARG   A NE  1 
ATOM   331  N NE  B ARG   A 1 57  ? -38.071 -21.478 -14.094 0.11 30.97 ? 74  ARG   A NE  1 
ATOM   332  N NE  C ARG   A 1 57  ? -38.140 -24.670 -11.345 0.22 33.06 ? 74  ARG   A NE  1 
ATOM   333  C CZ  A ARG   A 1 57  ? -37.901 -21.121 -15.364 0.67 31.24 ? 74  ARG   A CZ  1 
ATOM   334  C CZ  B ARG   A 1 57  ? -38.807 -20.916 -15.044 0.11 31.87 ? 74  ARG   A CZ  1 
ATOM   335  C CZ  C ARG   A 1 57  ? -37.767 -25.205 -12.499 0.22 31.28 ? 74  ARG   A CZ  1 
ATOM   336  N NH1 A ARG   A 1 57  ? -36.666 -21.495 -15.663 0.67 30.52 ? 74  ARG   A NH1 1 
ATOM   337  N NH1 B ARG   A 1 57  ? -39.432 -19.766 -14.850 0.11 33.48 ? 74  ARG   A NH1 1 
ATOM   338  N NH1 C ARG   A 1 57  ? -37.421 -24.451 -13.529 0.22 30.14 ? 74  ARG   A NH1 1 
ATOM   339  N NH2 A ARG   A 1 57  ? -38.755 -20.847 -16.346 0.67 31.90 ? 74  ARG   A NH2 1 
ATOM   340  N NH2 B ARG   A 1 57  ? -38.969 -21.556 -16.201 0.11 33.08 ? 74  ARG   A NH2 1 
ATOM   341  N NH2 C ARG   A 1 57  ? -37.758 -26.529 -12.629 0.22 30.82 ? 74  ARG   A NH2 1 
ATOM   342  N N   . LEU   A 1 58  ? -36.849 -18.330 -9.003  1.00 24.05 ? 75  LEU   A N   1 
ATOM   343  C CA  . LEU   A 1 58  ? -37.177 -16.914 -8.848  1.00 24.93 ? 75  LEU   A CA  1 
ATOM   344  C C   . LEU   A 1 58  ? -35.944 -16.043 -9.054  1.00 24.71 ? 75  LEU   A C   1 
ATOM   345  O O   . LEU   A 1 58  ? -36.012 -15.015 -9.739  1.00 24.29 ? 75  LEU   A O   1 
ATOM   346  C CB  . LEU   A 1 58  ? -37.796 -16.654 -7.472  1.00 25.31 ? 75  LEU   A CB  1 
ATOM   347  C CG  . LEU   A 1 58  ? -38.027 -15.183 -7.091  1.00 33.33 ? 75  LEU   A CG  1 
ATOM   348  C CD1 . LEU   A 1 58  ? -38.888 -14.480 -8.130  1.00 36.69 ? 75  LEU   A CD1 1 
ATOM   349  C CD2 . LEU   A 1 58  ? -38.651 -15.043 -5.694  1.00 40.23 ? 75  LEU   A CD2 1 
ATOM   350  N N   . ILE   A 1 59  ? -34.803 -16.448 -8.492  1.00 22.91 ? 76  ILE   A N   1 
ATOM   351  C CA  . ILE   A 1 59  ? -33.563 -15.704 -8.704  1.00 21.02 ? 76  ILE   A CA  1 
ATOM   352  C C   . ILE   A 1 59  ? -33.254 -15.603 -10.191 1.00 23.22 ? 76  ILE   A C   1 
ATOM   353  O O   . ILE   A 1 59  ? -32.989 -14.518 -10.715 1.00 19.89 ? 76  ILE   A O   1 
ATOM   354  C CB  . ILE   A 1 59  ? -32.403 -16.362 -7.928  1.00 23.60 ? 76  ILE   A CB  1 
ATOM   355  C CG1 . ILE   A 1 59  ? -32.644 -16.257 -6.414  1.00 24.67 ? 76  ILE   A CG1 1 
ATOM   356  C CG2 . ILE   A 1 59  ? -31.068 -15.769 -8.338  1.00 22.25 ? 76  ILE   A CG2 1 
ATOM   357  C CD1 . ILE   A 1 59  ? -31.742 -17.158 -5.578  1.00 24.66 ? 76  ILE   A CD1 1 
ATOM   358  N N   . HIS   A 1 60  ? -33.325 -16.726 -10.902 1.00 19.48 ? 77  HIS   A N   1 
ATOM   359  C CA  . HIS   A 1 60  ? -32.979 -16.721 -12.321 1.00 19.38 ? 77  HIS   A CA  1 
ATOM   360  C C   . HIS   A 1 60  ? -33.915 -15.808 -13.110 1.00 20.64 ? 77  HIS   A C   1 
ATOM   361  O O   . HIS   A 1 60  ? -33.468 -14.973 -13.904 1.00 19.37 ? 77  HIS   A O   1 
ATOM   362  C CB  . HIS   A 1 60  ? -33.036 -18.153 -12.863 1.00 19.19 ? 77  HIS   A CB  1 
ATOM   363  C CG  . HIS   A 1 60  ? -32.780 -18.252 -14.335 1.00 18.89 ? 77  HIS   A CG  1 
ATOM   364  N ND1 . HIS   A 1 60  ? -33.776 -18.120 -15.283 1.00 21.34 ? 77  HIS   A ND1 1 
ATOM   365  C CD2 . HIS   A 1 60  ? -31.628 -18.449 -15.020 1.00 17.86 ? 77  HIS   A CD2 1 
ATOM   366  C CE1 . HIS   A 1 60  ? -33.242 -18.244 -16.488 1.00 20.88 ? 77  HIS   A CE1 1 
ATOM   367  N NE2 . HIS   A 1 60  ? -31.941 -18.444 -16.354 1.00 20.16 ? 77  HIS   A NE2 1 
ATOM   368  N N   . GLU   A 1 61  ? -35.223 -15.947 -12.891 1.00 20.90 ? 78  GLU   A N   1 
ATOM   369  C CA  . GLU   A 1 61  ? -36.191 -15.190 -13.683 1.00 21.73 ? 78  GLU   A CA  1 
ATOM   370  C C   . GLU   A 1 61  ? -36.126 -13.706 -13.378 1.00 24.20 ? 78  GLU   A C   1 
ATOM   371  O O   . GLU   A 1 61  ? -36.193 -12.883 -14.296 1.00 21.45 ? 78  GLU   A O   1 
ATOM   372  C CB  . GLU   A 1 61  ? -37.603 -15.713 -13.449 1.00 23.42 ? 78  GLU   A CB  1 
ATOM   373  C CG  . GLU   A 1 61  ? -37.770 -17.188 -13.837 1.00 23.87 ? 78  GLU   A CG  1 
ATOM   374  C CD  . GLU   A 1 61  ? -37.629 -17.406 -15.332 1.00 29.40 ? 78  GLU   A CD  1 
ATOM   375  O OE1 . GLU   A 1 61  ? -38.625 -17.213 -16.058 1.00 37.23 ? 78  GLU   A OE1 1 
ATOM   376  O OE2 . GLU   A 1 61  ? -36.519 -17.776 -15.785 1.00 28.55 ? 78  GLU   A OE2 1 
ATOM   377  N N   . GLN   A 1 62  ? -36.016 -13.354 -12.098 1.00 21.78 ? 79  GLN   A N   1 
ATOM   378  C CA  . GLN   A 1 62  ? -35.921 -11.952 -11.722 1.00 23.26 ? 79  GLN   A CA  1 
ATOM   379  C C   . GLN   A 1 62  ? -34.644 -11.338 -12.279 1.00 24.71 ? 79  GLN   A C   1 
ATOM   380  O O   . GLN   A 1 62  ? -34.664 -10.230 -12.828 1.00 23.48 ? 79  GLN   A O   1 
ATOM   381  C CB  . GLN   A 1 62  ? -36.004 -11.843 -10.196 1.00 27.03 ? 79  GLN   A CB  1 
ATOM   382  C CG  . GLN   A 1 62  ? -35.925 -10.451 -9.604  1.00 37.75 ? 79  GLN   A CG  1 
ATOM   383  C CD  . GLN   A 1 62  ? -36.244 -10.449 -8.107  1.00 42.87 ? 79  GLN   A CD  1 
ATOM   384  O OE1 . GLN   A 1 62  ? -36.204 -11.491 -7.444  1.00 42.36 ? 79  GLN   A OE1 1 
ATOM   385  N NE2 . GLN   A 1 62  ? -36.594 -9.281  -7.579  1.00 44.89 ? 79  GLN   A NE2 1 
ATOM   386  N N   . ASP   A 1 63  ? -33.532 -12.068 -12.220 1.00 20.86 ? 80  ASP   A N   1 
ATOM   387  C CA  . ASP   A 1 63  ? -32.290 -11.488 -12.697 1.00 21.21 ? 80  ASP   A CA  1 
ATOM   388  C C   . ASP   A 1 63  ? -32.290 -11.364 -14.216 1.00 21.68 ? 80  ASP   A C   1 
ATOM   389  O O   . ASP   A 1 63  ? -31.727 -10.408 -14.762 1.00 23.47 ? 80  ASP   A O   1 
ATOM   390  C CB  . ASP   A 1 63  ? -31.116 -12.320 -12.182 1.00 21.99 ? 80  ASP   A CB  1 
ATOM   391  C CG  . ASP   A 1 63  ? -30.689 -11.880 -10.798 1.00 26.09 ? 80  ASP   A CG  1 
ATOM   392  O OD1 . ASP   A 1 63  ? -30.914 -12.641 -9.833  1.00 31.08 ? 80  ASP   A OD1 1 
ATOM   393  O OD2 . ASP   A 1 63  ? -30.148 -10.769 -10.658 1.00 31.98 ? 80  ASP   A OD2 1 
ATOM   394  N N   . LEU   A 1 64  ? -32.955 -12.281 -14.915 1.00 22.00 ? 81  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 64  ? -33.021 -12.185 -16.369 1.00 22.43 ? 81  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 64  ? -33.850 -10.967 -16.784 1.00 26.34 ? 81  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 64  ? -33.587 -10.328 -17.815 1.00 25.88 ? 81  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 64  ? -33.633 -13.478 -16.906 1.00 24.83 ? 81  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 64  ? -32.800 -14.397 -17.800 1.00 26.69 ? 81  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 64  ? -33.726 -15.453 -18.418 1.00 31.19 ? 81  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 64  ? -31.968 -13.660 -18.839 1.00 30.42 ? 81  LEU   A CD2 1 
ATOM   402  N N   . GLU   A 1 65  ? -34.853 -10.632 -15.978 1.00 24.10 ? 82  GLU   A N   1 
ATOM   403  C CA  . GLU   A 1 65  ? -35.651 -9.431  -16.189 1.00 24.30 ? 82  GLU   A CA  1 
ATOM   404  C C   . GLU   A 1 65  ? -34.779 -8.183  -16.045 1.00 24.77 ? 82  GLU   A C   1 
ATOM   405  O O   . GLU   A 1 65  ? -34.802 -7.283  -16.898 1.00 25.32 ? 82  GLU   A O   1 
ATOM   406  C CB  . GLU   A 1 65  ? -36.777 -9.446  -15.159 1.00 25.16 ? 82  GLU   A CB  1 
ATOM   407  C CG  . GLU   A 1 65  ? -38.105 -10.002 -15.658 1.00 29.26 ? 82  GLU   A CG  1 
ATOM   408  C CD  . GLU   A 1 65  ? -38.976 -10.524 -14.510 1.00 35.99 ? 82  GLU   A CD  1 
ATOM   409  O OE1 . GLU   A 1 65  ? -38.795 -10.084 -13.352 1.00 36.97 ? 82  GLU   A OE1 1 
ATOM   410  O OE2 . GLU   A 1 65  ? -39.872 -11.358 -14.772 1.00 42.76 ? 82  GLU   A OE2 1 
ATOM   411  N N   . TRP   A 1 66  ? -33.986 -8.126  -14.973 1.00 20.76 ? 83  TRP   A N   1 
ATOM   412  C CA  . TRP   A 1 66  ? -33.120 -6.969  -14.760 1.00 21.52 ? 83  TRP   A CA  1 
ATOM   413  C C   . TRP   A 1 66  ? -32.028 -6.889  -15.814 1.00 20.48 ? 83  TRP   A C   1 
ATOM   414  O O   . TRP   A 1 66  ? -31.605 -5.790  -16.197 1.00 22.38 ? 83  TRP   A O   1 
ATOM   415  C CB  . TRP   A 1 66  ? -32.478 -7.024  -13.377 1.00 20.62 ? 83  TRP   A CB  1 
ATOM   416  C CG  . TRP   A 1 66  ? -33.427 -6.850  -12.256 1.00 21.23 ? 83  TRP   A CG  1 
ATOM   417  C CD1 . TRP   A 1 66  ? -34.515 -6.029  -12.218 1.00 25.38 ? 83  TRP   A CD1 1 
ATOM   418  C CD2 . TRP   A 1 66  ? -33.302 -7.415  -10.954 1.00 24.26 ? 83  TRP   A CD2 1 
ATOM   419  N NE1 . TRP   A 1 66  ? -35.116 -6.102  -10.982 1.00 28.73 ? 83  TRP   A NE1 1 
ATOM   420  C CE2 . TRP   A 1 66  ? -34.379 -6.943  -10.186 1.00 28.62 ? 83  TRP   A CE2 1 
ATOM   421  C CE3 . TRP   A 1 66  ? -32.385 -8.293  -10.366 1.00 25.45 ? 83  TRP   A CE3 1 
ATOM   422  C CZ2 . TRP   A 1 66  ? -34.570 -7.325  -8.858  1.00 32.59 ? 83  TRP   A CZ2 1 
ATOM   423  C CZ3 . TRP   A 1 66  ? -32.580 -8.670  -9.056  1.00 28.79 ? 83  TRP   A CZ3 1 
ATOM   424  C CH2 . TRP   A 1 66  ? -33.659 -8.188  -8.316  1.00 30.87 ? 83  TRP   A CH2 1 
ATOM   425  N N   . LEU   A 1 67  ? -31.549 -8.035  -16.279 1.00 22.11 ? 84  LEU   A N   1 
ATOM   426  C CA  . LEU   A 1 67  ? -30.421 -8.022  -17.190 1.00 22.84 ? 84  LEU   A CA  1 
ATOM   427  C C   . LEU   A 1 67  ? -30.836 -7.363  -18.507 1.00 22.24 ? 84  LEU   A C   1 
ATOM   428  O O   . LEU   A 1 67  ? -30.079 -6.577  -19.093 1.00 25.75 ? 84  LEU   A O   1 
ATOM   429  C CB  . LEU   A 1 67  ? -29.952 -9.469  -17.381 1.00 23.74 ? 84  LEU   A CB  1 
ATOM   430  C CG  . LEU   A 1 67  ? -28.748 -9.836  -18.213 1.00 24.81 ? 84  LEU   A CG  1 
ATOM   431  C CD1 . LEU   A 1 67  ? -27.568 -9.136  -17.569 1.00 23.01 ? 84  LEU   A CD1 1 
ATOM   432  C CD2 . LEU   A 1 67  ? -28.563 -11.346 -18.262 1.00 22.80 ? 84  LEU   A CD2 1 
ATOM   433  N N   . GLN   A 1 68  ? -32.083 -7.609  -18.940 1.00 24.66 ? 85  GLN   A N   1 
ATOM   434  C CA  . GLN   A 1 68  ? -32.628 -6.983  -20.142 1.00 25.95 ? 85  GLN   A CA  1 
ATOM   435  C C   . GLN   A 1 68  ? -32.918 -5.503  -19.949 1.00 25.43 ? 85  GLN   A C   1 
ATOM   436  O O   . GLN   A 1 68  ? -32.934 -4.741  -20.925 1.00 27.85 ? 85  GLN   A O   1 
ATOM   437  C CB  . GLN   A 1 68  ? -33.907 -7.707  -20.566 1.00 30.08 ? 85  GLN   A CB  1 
ATOM   438  C CG  . GLN   A 1 68  ? -33.656 -9.112  -21.086 1.00 32.09 ? 85  GLN   A CG  1 
ATOM   439  C CD  . GLN   A 1 68  ? -34.913 -9.947  -21.158 1.00 33.30 ? 85  GLN   A CD  1 
ATOM   440  O OE1 . GLN   A 1 68  ? -35.544 -10.040 -22.205 1.00 34.20 ? 85  GLN   A OE1 1 
ATOM   441  N NE2 . GLN   A 1 68  ? -35.243 -10.622 -20.061 1.00 34.69 ? 85  GLN   A NE2 1 
ATOM   442  N N   . GLN   A 1 69  ? -33.165 -5.081  -18.714 1.00 25.71 ? 86  GLN   A N   1 
ATOM   443  C CA  . GLN   A 1 69  ? -33.451 -3.688  -18.417 1.00 23.34 ? 86  GLN   A CA  1 
ATOM   444  C C   . GLN   A 1 69  ? -32.182 -2.861  -18.326 1.00 20.79 ? 86  GLN   A C   1 
ATOM   445  O O   . GLN   A 1 69  ? -32.233 -1.640  -18.511 1.00 23.66 ? 86  GLN   A O   1 
ATOM   446  C CB  . GLN   A 1 69  ? -34.201 -3.621  -17.090 1.00 22.61 ? 86  GLN   A CB  1 
ATOM   447  C CG  . GLN   A 1 69  ? -35.620 -4.112  -17.224 1.00 24.23 ? 86  GLN   A CG  1 
ATOM   448  C CD  . GLN   A 1 69  ? -36.339 -4.196  -15.907 1.00 24.49 ? 86  GLN   A CD  1 
ATOM   449  O OE1 . GLN   A 1 69  ? -35.842 -3.738  -14.876 1.00 23.89 ? 86  GLN   A OE1 1 
ATOM   450  N NE2 . GLN   A 1 69  ? -37.481 -4.877  -15.912 1.00 25.37 ? 86  GLN   A NE2 1 
ATOM   451  N N   . ALA   A 1 70  ? -31.051 -3.501  -18.051 1.00 21.86 ? 87  ALA   A N   1 
ATOM   452  C CA  . ALA   A 1 70  ? -29.844 -2.768  -17.714 1.00 19.50 ? 87  ALA   A CA  1 
ATOM   453  C C   . ALA   A 1 70  ? -29.282 -2.027  -18.926 1.00 21.38 ? 87  ALA   A C   1 
ATOM   454  O O   . ALA   A 1 70  ? -29.314 -2.519  -20.056 1.00 22.63 ? 87  ALA   A O   1 
ATOM   455  C CB  . ALA   A 1 70  ? -28.799 -3.725  -17.152 1.00 20.97 ? 87  ALA   A CB  1 
ATOM   456  N N   . ASP   A 1 71  ? -28.771 -0.821  -18.671 1.00 19.54 ? 88  ASP   A N   1 
ATOM   457  C CA  . ASP   A 1 71  ? -27.995 -0.076  -19.660 1.00 22.28 ? 88  ASP   A CA  1 
ATOM   458  C C   . ASP   A 1 71  ? -26.545 -0.552  -19.716 1.00 22.26 ? 88  ASP   A C   1 
ATOM   459  O O   . ASP   A 1 71  ? -25.946 -0.604  -20.800 1.00 24.04 ? 88  ASP   A O   1 
ATOM   460  C CB  . ASP   A 1 71  ? -28.095 1.414   -19.344 1.00 23.84 ? 88  ASP   A CB  1 
ATOM   461  C CG  . ASP   A 1 71  ? -29.532 1.929   -19.432 1.00 25.19 ? 88  ASP   A CG  1 
ATOM   462  O OD1 . ASP   A 1 71  ? -30.194 1.660   -20.456 1.00 27.39 ? 88  ASP   A OD1 1 
ATOM   463  O OD2 . ASP   A 1 71  ? -30.051 2.475   -18.444 1.00 26.53 ? 88  ASP   A OD2 1 
ATOM   464  N N   . VAL   A 1 72  ? -25.966 -0.925  -18.571 1.00 18.68 ? 89  VAL   A N   1 
ATOM   465  C CA  . VAL   A 1 72  ? -24.613 -1.470  -18.516 1.00 17.12 ? 89  VAL   A CA  1 
ATOM   466  C C   . VAL   A 1 72  ? -24.606 -2.633  -17.540 1.00 18.34 ? 89  VAL   A C   1 
ATOM   467  O O   . VAL   A 1 72  ? -25.222 -2.557  -16.472 1.00 18.42 ? 89  VAL   A O   1 
ATOM   468  C CB  . VAL   A 1 72  ? -23.573 -0.411  -18.084 1.00 19.06 ? 89  VAL   A CB  1 
ATOM   469  C CG1 . VAL   A 1 72  ? -22.175 -0.987  -18.128 1.00 20.24 ? 89  VAL   A CG1 1 
ATOM   470  C CG2 . VAL   A 1 72  ? -23.642 0.818   -18.989 1.00 20.20 ? 89  VAL   A CG2 1 
ATOM   471  N N   . VAL   A 1 73  ? -23.894 -3.696  -17.908 1.00 17.69 ? 90  VAL   A N   1 
ATOM   472  C CA  . VAL   A 1 73  ? -23.661 -4.862  -17.067 1.00 17.66 ? 90  VAL   A CA  1 
ATOM   473  C C   . VAL   A 1 73  ? -22.205 -4.812  -16.624 1.00 18.75 ? 90  VAL   A C   1 
ATOM   474  O O   . VAL   A 1 73  ? -21.298 -4.806  -17.465 1.00 19.42 ? 90  VAL   A O   1 
ATOM   475  C CB  . VAL   A 1 73  ? -23.967 -6.159  -17.829 1.00 15.16 ? 90  VAL   A CB  1 
ATOM   476  C CG1 . VAL   A 1 73  ? -23.603 -7.381  -16.991 1.00 16.97 ? 90  VAL   A CG1 1 
ATOM   477  C CG2 . VAL   A 1 73  ? -25.436 -6.207  -18.240 1.00 16.67 ? 90  VAL   A CG2 1 
ATOM   478  N N   . VAL   A 1 74  ? -21.974 -4.768  -15.317 1.00 14.42 ? 91  VAL   A N   1 
ATOM   479  C CA  . VAL   A 1 74  ? -20.631 -4.691  -14.748 1.00 14.98 ? 91  VAL   A CA  1 
ATOM   480  C C   . VAL   A 1 74  ? -20.367 -5.982  -13.981 1.00 16.23 ? 91  VAL   A C   1 
ATOM   481  O O   . VAL   A 1 74  ? -21.151 -6.362  -13.106 1.00 15.84 ? 91  VAL   A O   1 
ATOM   482  C CB  . VAL   A 1 74  ? -20.478 -3.460  -13.838 1.00 15.83 ? 91  VAL   A CB  1 
ATOM   483  C CG1 . VAL   A 1 74  ? -19.054 -3.402  -13.256 1.00 17.36 ? 91  VAL   A CG1 1 
ATOM   484  C CG2 . VAL   A 1 74  ? -20.824 -2.155  -14.616 1.00 18.12 ? 91  VAL   A CG2 1 
ATOM   485  N N   . ALA   A 1 75  ? -19.269 -6.663  -14.305 1.00 13.68 ? 92  ALA   A N   1 
ATOM   486  C CA  . ALA   A 1 75  ? -18.955 -7.939  -13.684 1.00 13.11 ? 92  ALA   A CA  1 
ATOM   487  C C   . ALA   A 1 75  ? -17.526 -7.922  -13.169 1.00 14.39 ? 92  ALA   A C   1 
ATOM   488  O O   . ALA   A 1 75  ? -16.606 -7.522  -13.892 1.00 17.27 ? 92  ALA   A O   1 
ATOM   489  C CB  . ALA   A 1 75  ? -19.139 -9.091  -14.677 1.00 14.07 ? 92  ALA   A CB  1 
ATOM   490  N N   . GLU   A 1 76  ? -17.340 -8.349  -11.930 1.00 12.36 ? 93  GLU   A N   1 
ATOM   491  C CA  . GLU   A 1 76  ? -16.009 -8.584  -11.381 1.00 14.47 ? 93  GLU   A CA  1 
ATOM   492  C C   . GLU   A 1 76  ? -15.764 -10.070 -11.567 1.00 16.41 ? 93  GLU   A C   1 
ATOM   493  O O   . GLU   A 1 76  ? -16.427 -10.887 -10.924 1.00 14.51 ? 93  GLU   A O   1 
ATOM   494  C CB  . GLU   A 1 76  ? -15.913 -8.161  -9.912  1.00 13.31 ? 93  GLU   A CB  1 
ATOM   495  C CG  . GLU   A 1 76  ? -14.529 -7.566  -9.536  1.00 15.67 ? 93  GLU   A CG  1 
ATOM   496  C CD  . GLU   A 1 76  ? -13.391 -8.576  -9.617  1.00 17.82 ? 93  GLU   A CD  1 
ATOM   497  O OE1 . GLU   A 1 76  ? -13.654 -9.792  -9.697  1.00 15.65 ? 93  GLU   A OE1 1 
ATOM   498  O OE2 . GLU   A 1 76  ? -12.213 -8.144  -9.621  1.00 17.71 ? 93  GLU   A OE2 1 
ATOM   499  N N   . VAL   A 1 77  ? -14.823 -10.407 -12.452 1.00 14.87 ? 94  VAL   A N   1 
ATOM   500  C CA  . VAL   A 1 77  ? -14.674 -11.765 -12.975 1.00 14.64 ? 94  VAL   A CA  1 
ATOM   501  C C   . VAL   A 1 77  ? -13.412 -12.450 -12.451 1.00 15.78 ? 94  VAL   A C   1 
ATOM   502  O O   . VAL   A 1 77  ? -12.944 -13.427 -13.054 1.00 15.86 ? 94  VAL   A O   1 
ATOM   503  C CB  . VAL   A 1 77  ? -14.692 -11.786 -14.514 1.00 16.10 ? 94  VAL   A CB  1 
ATOM   504  C CG1 . VAL   A 1 77  ? -16.033 -11.346 -15.047 1.00 16.30 ? 94  VAL   A CG1 1 
ATOM   505  C CG2 . VAL   A 1 77  ? -13.552 -10.912 -15.098 1.00 15.74 ? 94  VAL   A CG2 1 
ATOM   506  N N   . THR   A 1 78  ? -12.866 -11.995 -11.326 1.00 14.96 ? 95  THR   A N   1 
ATOM   507  C CA  . THR   A 1 78  ? -11.663 -12.629 -10.793 1.00 15.19 ? 95  THR   A CA  1 
ATOM   508  C C   . THR   A 1 78  ? -11.964 -13.986 -10.160 1.00 15.44 ? 95  THR   A C   1 
ATOM   509  O O   . THR   A 1 78  ? -11.247 -14.963 -10.415 1.00 16.73 ? 95  THR   A O   1 
ATOM   510  C CB  . THR   A 1 78  ? -10.993 -11.696 -9.793  1.00 15.97 ? 95  THR   A CB  1 
ATOM   511  O OG1 . THR   A 1 78  ? -10.692 -10.469 -10.463 1.00 17.02 ? 95  THR   A OG1 1 
ATOM   512  C CG2 . THR   A 1 78  ? -9.706  -12.310 -9.274  1.00 16.51 ? 95  THR   A CG2 1 
ATOM   513  N N   . GLN   A 1 79  ? -13.022 -14.082 -9.353  1.00 16.20 ? 96  GLN   A N   1 
ATOM   514  C CA  . GLN   A 1 79  ? -13.396 -15.344 -8.723  1.00 14.32 ? 96  GLN   A CA  1 
ATOM   515  C C   . GLN   A 1 79  ? -14.244 -16.178 -9.675  1.00 14.87 ? 96  GLN   A C   1 
ATOM   516  O O   . GLN   A 1 79  ? -15.301 -15.713 -10.109 1.00 15.61 ? 96  GLN   A O   1 
ATOM   517  C CB  . GLN   A 1 79  ? -14.176 -15.069 -7.430  1.00 15.56 ? 96  GLN   A CB  1 
ATOM   518  C CG  . GLN   A 1 79  ? -14.463 -16.316 -6.582  1.00 15.07 ? 96  GLN   A CG  1 
ATOM   519  C CD  . GLN   A 1 79  ? -13.195 -16.921 -6.003  1.00 19.21 ? 96  GLN   A CD  1 
ATOM   520  O OE1 . GLN   A 1 79  ? -12.298 -16.200 -5.569  1.00 20.13 ? 96  GLN   A OE1 1 
ATOM   521  N NE2 . GLN   A 1 79  ? -13.132 -18.245 -5.957  1.00 21.76 ? 96  GLN   A NE2 1 
ATOM   522  N N   . PRO   A 1 80  ? -13.825 -17.390 -10.040 1.00 13.90 ? 97  PRO   A N   1 
ATOM   523  C CA  . PRO   A 1 80  ? -14.630 -18.183 -10.984 1.00 13.73 ? 97  PRO   A CA  1 
ATOM   524  C C   . PRO   A 1 80  ? -16.013 -18.514 -10.439 1.00 13.90 ? 97  PRO   A C   1 
ATOM   525  O O   . PRO   A 1 80  ? -16.180 -18.872 -9.273  1.00 14.33 ? 97  PRO   A O   1 
ATOM   526  C CB  . PRO   A 1 80  ? -13.793 -19.452 -11.190 1.00 14.29 ? 97  PRO   A CB  1 
ATOM   527  C CG  . PRO   A 1 80  ? -12.377 -18.979 -10.915 1.00 16.70 ? 97  PRO   A CG  1 
ATOM   528  C CD  . PRO   A 1 80  ? -12.512 -18.010 -9.772  1.00 14.10 ? 97  PRO   A CD  1 
ATOM   529  N N   . SER   A 1 81  ? -17.012 -18.407 -11.317 1.00 12.91 ? 98  SER   A N   1 
ATOM   530  C CA  . SER   A 1 81  ? -18.403 -18.531 -10.896 1.00 11.84 ? 98  SER   A CA  1 
ATOM   531  C C   . SER   A 1 81  ? -19.246 -18.898 -12.106 1.00 12.30 ? 98  SER   A C   1 
ATOM   532  O O   . SER   A 1 81  ? -19.178 -18.214 -13.134 1.00 13.37 ? 98  SER   A O   1 
ATOM   533  C CB  . SER   A 1 81  ? -18.887 -17.204 -10.281 1.00 13.42 ? 98  SER   A CB  1 
ATOM   534  O OG  . SER   A 1 81  ? -20.315 -17.119 -10.325 1.00 13.05 ? 98  SER   A OG  1 
ATOM   535  N N   . LEU   A 1 82  ? -20.044 -19.963 -11.980 1.00 11.74 ? 99  LEU   A N   1 
ATOM   536  C CA  . LEU   A 1 82  ? -20.976 -20.313 -13.056 1.00 12.72 ? 99  LEU   A CA  1 
ATOM   537  C C   . LEU   A 1 82  ? -22.007 -19.222 -13.263 1.00 13.61 ? 99  LEU   A C   1 
ATOM   538  O O   . LEU   A 1 82  ? -22.358 -18.904 -14.402 1.00 12.24 ? 99  LEU   A O   1 
ATOM   539  C CB  . LEU   A 1 82  ? -21.694 -21.619 -12.737 1.00 13.52 ? 99  LEU   A CB  1 
ATOM   540  C CG  . LEU   A 1 82  ? -20.831 -22.866 -12.586 1.00 13.11 ? 99  LEU   A CG  1 
ATOM   541  C CD1 . LEU   A 1 82  ? -21.676 -23.897 -11.882 1.00 15.73 ? 99  LEU   A CD1 1 
ATOM   542  C CD2 . LEU   A 1 82  ? -20.372 -23.376 -13.932 1.00 14.85 ? 99  LEU   A CD2 1 
ATOM   543  N N   . GLY   A 1 83  ? -22.521 -18.660 -12.168 1.00 12.04 ? 100 GLY   A N   1 
ATOM   544  C CA  . GLY   A 1 83  ? -23.581 -17.671 -12.289 1.00 12.36 ? 100 GLY   A CA  1 
ATOM   545  C C   . GLY   A 1 83  ? -23.115 -16.403 -12.973 1.00 12.61 ? 100 GLY   A C   1 
ATOM   546  O O   . GLY   A 1 83  ? -23.842 -15.828 -13.791 1.00 13.19 ? 100 GLY   A O   1 
ATOM   547  N N   . VAL   A 1 84  ? -21.894 -15.959 -12.662 1.00 11.79 ? 101 VAL   A N   1 
ATOM   548  C CA  . VAL   A 1 84  ? -21.360 -14.780 -13.333 1.00 12.28 ? 101 VAL   A CA  1 
ATOM   549  C C   . VAL   A 1 84  ? -21.152 -15.073 -14.816 1.00 14.33 ? 101 VAL   A C   1 
ATOM   550  O O   . VAL   A 1 84  ? -21.512 -14.268 -15.684 1.00 14.06 ? 101 VAL   A O   1 
ATOM   551  C CB  . VAL   A 1 84  ? -20.053 -14.333 -12.659 1.00 10.79 ? 101 VAL   A CB  1 
ATOM   552  C CG1 . VAL   A 1 84  ? -19.387 -13.196 -13.469 1.00 13.40 ? 101 VAL   A CG1 1 
ATOM   553  C CG2 . VAL   A 1 84  ? -20.328 -13.890 -11.209 1.00 13.33 ? 101 VAL   A CG2 1 
ATOM   554  N N   . GLY   A 1 85  ? -20.599 -16.238 -15.139 1.00 11.85 ? 102 GLY   A N   1 
ATOM   555  C CA  . GLY   A 1 85  ? -20.404 -16.560 -16.543 1.00 12.56 ? 102 GLY   A CA  1 
ATOM   556  C C   . GLY   A 1 85  ? -21.719 -16.639 -17.295 1.00 12.69 ? 102 GLY   A C   1 
ATOM   557  O O   . GLY   A 1 85  ? -21.832 -16.156 -18.425 1.00 14.45 ? 102 GLY   A O   1 
ATOM   558  N N   . TYR   A 1 86  ? -22.735 -17.237 -16.665 1.00 13.24 ? 103 TYR   A N   1 
ATOM   559  C CA  . TYR   A 1 86  ? -24.043 -17.361 -17.300 1.00 14.02 ? 103 TYR   A CA  1 
ATOM   560  C C   . TYR   A 1 86  ? -24.665 -15.991 -17.544 1.00 13.55 ? 103 TYR   A C   1 
ATOM   561  O O   . TYR   A 1 86  ? -25.243 -15.736 -18.618 1.00 14.02 ? 103 TYR   A O   1 
ATOM   562  C CB  . TYR   A 1 86  ? -24.947 -18.218 -16.412 1.00 15.19 ? 103 TYR   A CB  1 
ATOM   563  C CG  . TYR   A 1 86  ? -26.343 -18.388 -16.934 1.00 12.72 ? 103 TYR   A CG  1 
ATOM   564  C CD1 . TYR   A 1 86  ? -26.648 -19.408 -17.822 1.00 15.24 ? 103 TYR   A CD1 1 
ATOM   565  C CD2 . TYR   A 1 86  ? -27.362 -17.534 -16.528 1.00 14.35 ? 103 TYR   A CD2 1 
ATOM   566  C CE1 . TYR   A 1 86  ? -27.922 -19.572 -18.302 1.00 17.06 ? 103 TYR   A CE1 1 
ATOM   567  C CE2 . TYR   A 1 86  ? -28.642 -17.686 -17.001 1.00 16.99 ? 103 TYR   A CE2 1 
ATOM   568  C CZ  . TYR   A 1 86  ? -28.918 -18.709 -17.888 1.00 16.66 ? 103 TYR   A CZ  1 
ATOM   569  O OH  . TYR   A 1 86  ? -30.197 -18.875 -18.360 1.00 18.98 ? 103 TYR   A OH  1 
ATOM   570  N N   . GLU   A 1 87  ? -24.593 -15.109 -16.536 1.00 13.44 ? 104 GLU   A N   1 
ATOM   571  C CA  . GLU   A 1 87  ? -25.074 -13.735 -16.702 1.00 13.47 ? 104 GLU   A CA  1 
ATOM   572  C C   . GLU   A 1 87  ? -24.395 -13.054 -17.878 1.00 14.65 ? 104 GLU   A C   1 
ATOM   573  O O   . GLU   A 1 87  ? -25.055 -12.369 -18.670 1.00 16.27 ? 104 GLU   A O   1 
ATOM   574  C CB  . GLU   A 1 87  ? -24.838 -12.932 -15.416 1.00 12.21 ? 104 GLU   A CB  1 
ATOM   575  C CG  . GLU   A 1 87  ? -25.832 -13.297 -14.320 1.00 14.67 ? 104 GLU   A CG  1 
ATOM   576  C CD  . GLU   A 1 87  ? -25.500 -12.748 -12.935 1.00 14.39 ? 104 GLU   A CD  1 
ATOM   577  O OE1 . GLU   A 1 87  ? -24.308 -12.603 -12.584 1.00 15.02 ? 104 GLU   A OE1 1 
ATOM   578  O OE2 . GLU   A 1 87  ? -26.455 -12.496 -12.178 1.00 17.15 ? 104 GLU   A OE2 1 
ATOM   579  N N   . LEU   A 1 88  ? -23.079 -13.233 -18.011 1.00 13.68 ? 105 LEU   A N   1 
ATOM   580  C CA  . LEU   A 1 88  ? -22.369 -12.605 -19.120 1.00 13.92 ? 105 LEU   A CA  1 
ATOM   581  C C   . LEU   A 1 88  ? -22.776 -13.211 -20.462 1.00 15.77 ? 105 LEU   A C   1 
ATOM   582  O O   . LEU   A 1 88  ? -22.944 -12.478 -21.442 1.00 15.31 ? 105 LEU   A O   1 
ATOM   583  C CB  . LEU   A 1 88  ? -20.854 -12.702 -18.900 1.00 13.88 ? 105 LEU   A CB  1 
ATOM   584  C CG  . LEU   A 1 88  ? -20.331 -11.796 -17.768 1.00 14.25 ? 105 LEU   A CG  1 
ATOM   585  C CD1 . LEU   A 1 88  ? -18.915 -12.149 -17.347 1.00 14.53 ? 105 LEU   A CD1 1 
ATOM   586  C CD2 . LEU   A 1 88  ? -20.418 -10.310 -18.158 1.00 14.64 ? 105 LEU   A CD2 1 
ATOM   587  N N   . GLY   A 1 89  ? -22.969 -14.540 -20.528 1.00 15.94 ? 106 GLY   A N   1 
ATOM   588  C CA  . GLY   A 1 89  ? -23.429 -15.149 -21.771 1.00 14.68 ? 106 GLY   A CA  1 
ATOM   589  C C   . GLY   A 1 89  ? -24.805 -14.659 -22.190 1.00 16.13 ? 106 GLY   A C   1 
ATOM   590  O O   . GLY   A 1 89  ? -25.036 -14.337 -23.358 1.00 17.06 ? 106 GLY   A O   1 
ATOM   591  N N   . ARG   A 1 90  ? -25.747 -14.606 -21.240 1.00 16.47 ? 107 ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 90  ? -27.062 -14.058 -21.564 1.00 18.32 ? 107 ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 90  ? -26.962 -12.593 -21.968 1.00 19.47 ? 107 ARG   A C   1 
ATOM   594  O O   . ARG   A 1 90  ? -27.659 -12.153 -22.887 1.00 18.99 ? 107 ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 90  ? -28.017 -14.229 -20.382 1.00 16.33 ? 107 ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 90  ? -28.351 -15.708 -20.022 1.00 16.30 ? 107 ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 90  ? -28.954 -16.522 -21.172 1.00 19.36 ? 107 ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 90  ? -30.199 -15.963 -21.689 1.00 20.43 ? 107 ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 90  ? -31.411 -16.342 -21.304 1.00 22.34 ? 107 ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 90  ? -31.587 -17.207 -20.320 1.00 23.62 ? 107 ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 90  ? -32.477 -15.834 -21.915 1.00 22.91 ? 107 ARG   A NH2 1 
ATOM   602  N N   . ALA   A 1 91  ? -26.088 -11.830 -21.302 1.00 18.42 ? 108 ALA   A N   1 
ATOM   603  C CA  . ALA   A 1 91  ? -25.984 -10.399 -21.598 1.00 17.93 ? 108 ALA   A CA  1 
ATOM   604  C C   . ALA   A 1 91  ? -25.445 -10.156 -23.005 1.00 19.92 ? 108 ALA   A C   1 
ATOM   605  O O   . ALA   A 1 91  ? -25.917 -9.248  -23.708 1.00 19.85 ? 108 ALA   A O   1 
ATOM   606  C CB  . ALA   A 1 91  ? -25.102 -9.709  -20.555 1.00 17.46 ? 108 ALA   A CB  1 
ATOM   607  N N   . VAL   A 1 92  ? -24.453 -10.944 -23.430 1.00 18.40 ? 109 VAL   A N   1 
ATOM   608  C CA  . VAL   A 1 92  ? -23.931 -10.811 -24.788 1.00 20.41 ? 109 VAL   A CA  1 
ATOM   609  C C   . VAL   A 1 92  ? -25.038 -11.062 -25.796 1.00 22.86 ? 109 VAL   A C   1 
ATOM   610  O O   . VAL   A 1 92  ? -25.169 -10.350 -26.801 1.00 24.50 ? 109 VAL   A O   1 
ATOM   611  C CB  . VAL   A 1 92  ? -22.748 -11.775 -25.010 1.00 22.91 ? 109 VAL   A CB  1 
ATOM   612  C CG1 . VAL   A 1 92  ? -22.408 -11.876 -26.496 1.00 23.77 ? 109 VAL   A CG1 1 
ATOM   613  C CG2 . VAL   A 1 92  ? -21.542 -11.330 -24.216 1.00 22.17 ? 109 VAL   A CG2 1 
ATOM   614  N N   . ALA   A 1 93  ? -25.854 -12.082 -25.545 1.00 22.95 ? 110 ALA   A N   1 
ATOM   615  C CA  . ALA   A 1 93  ? -26.918 -12.406 -26.484 1.00 23.66 ? 110 ALA   A CA  1 
ATOM   616  C C   . ALA   A 1 93  ? -28.010 -11.352 -26.477 1.00 24.31 ? 110 ALA   A C   1 
ATOM   617  O O   . ALA   A 1 93  ? -28.706 -11.179 -27.481 1.00 27.37 ? 110 ALA   A O   1 
ATOM   618  C CB  . ALA   A 1 93  ? -27.491 -13.776 -26.150 1.00 24.01 ? 110 ALA   A CB  1 
ATOM   619  N N   . PHE   A 1 94  ? -28.177 -10.643 -25.361 1.00 24.07 ? 111 PHE   A N   1 
ATOM   620  C CA  . PHE   A 1 94  ? -29.078 -9.502  -25.281 1.00 24.39 ? 111 PHE   A CA  1 
ATOM   621  C C   . PHE   A 1 94  ? -28.464 -8.232  -25.842 1.00 27.61 ? 111 PHE   A C   1 
ATOM   622  O O   . PHE   A 1 94  ? -29.112 -7.183  -25.783 1.00 29.49 ? 111 PHE   A O   1 
ATOM   623  C CB  . PHE   A 1 94  ? -29.481 -9.242  -23.830 1.00 23.89 ? 111 PHE   A CB  1 
ATOM   624  C CG  . PHE   A 1 94  ? -30.471 -10.227 -23.288 1.00 26.58 ? 111 PHE   A CG  1 
ATOM   625  C CD1 . PHE   A 1 94  ? -31.504 -10.710 -24.076 1.00 27.26 ? 111 PHE   A CD1 1 
ATOM   626  C CD2 . PHE   A 1 94  ? -30.357 -10.679 -21.980 1.00 27.01 ? 111 PHE   A CD2 1 
ATOM   627  C CE1 . PHE   A 1 94  ? -32.412 -11.617 -23.567 1.00 29.24 ? 111 PHE   A CE1 1 
ATOM   628  C CE2 . PHE   A 1 94  ? -31.260 -11.588 -21.471 1.00 26.87 ? 111 PHE   A CE2 1 
ATOM   629  C CZ  . PHE   A 1 94  ? -32.286 -12.058 -22.266 1.00 26.96 ? 111 PHE   A CZ  1 
ATOM   630  N N   . ASN   A 1 95  ? -27.228 -8.291  -26.344 1.00 25.56 ? 112 ASN   A N   1 
ATOM   631  C CA  . ASN   A 1 95  ? -26.575 -7.131  -26.949 1.00 29.76 ? 112 ASN   A CA  1 
ATOM   632  C C   . ASN   A 1 95  ? -26.353 -6.022  -25.921 1.00 27.56 ? 112 ASN   A C   1 
ATOM   633  O O   . ASN   A 1 95  ? -26.476 -4.828  -26.225 1.00 31.21 ? 112 ASN   A O   1 
ATOM   634  C CB  . ASN   A 1 95  ? -27.377 -6.625  -28.156 1.00 33.85 ? 112 ASN   A CB  1 
ATOM   635  C CG  . ASN   A 1 95  ? -26.624 -5.599  -28.973 1.00 46.49 ? 112 ASN   A CG  1 
ATOM   636  O OD1 . ASN   A 1 95  ? -25.443 -5.774  -29.279 1.00 50.64 ? 112 ASN   A OD1 1 
ATOM   637  N ND2 . ASN   A 1 95  ? -27.308 -4.515  -29.333 1.00 45.88 ? 112 ASN   A ND2 1 
ATOM   638  N N   . LYS   A 1 96  ? -26.027 -6.414  -24.693 1.00 23.36 ? 113 LYS   A N   1 
ATOM   639  C CA  . LYS   A 1 96  ? -25.769 -5.453  -23.631 1.00 23.48 ? 113 LYS   A CA  1 
ATOM   640  C C   . LYS   A 1 96  ? -24.347 -4.910  -23.694 1.00 25.94 ? 113 LYS   A C   1 
ATOM   641  O O   . LYS   A 1 96  ? -23.401 -5.606  -24.079 1.00 26.45 ? 113 LYS   A O   1 
ATOM   642  C CB  . LYS   A 1 96  ? -26.006 -6.096  -22.263 1.00 23.81 ? 113 LYS   A CB  1 
ATOM   643  C CG  . LYS   A 1 96  ? -27.449 -6.452  -22.010 1.00 26.46 ? 113 LYS   A CG  1 
ATOM   644  C CD  . LYS   A 1 96  ? -28.288 -5.207  -22.177 1.00 28.91 ? 113 LYS   A CD  1 
ATOM   645  C CE  . LYS   A 1 96  ? -29.756 -5.463  -21.967 1.00 31.68 ? 113 LYS   A CE  1 
ATOM   646  N NZ  . LYS   A 1 96  ? -30.496 -4.188  -22.079 1.00 29.46 ? 113 LYS   A NZ  1 
ATOM   647  N N   . ARG   A 1 97  ? -24.203 -3.650  -23.296 1.00 22.10 ? 114 ARG   A N   1 
ATOM   648  C CA  . ARG   A 1 97  ? -22.884 -3.102  -23.028 1.00 22.63 ? 114 ARG   A CA  1 
ATOM   649  C C   . ARG   A 1 97  ? -22.352 -3.705  -21.735 1.00 21.31 ? 114 ARG   A C   1 
ATOM   650  O O   . ARG   A 1 97  ? -23.042 -3.710  -20.710 1.00 20.55 ? 114 ARG   A O   1 
ATOM   651  C CB  . ARG   A 1 97  ? -22.939 -1.576  -22.929 1.00 24.60 ? 114 ARG   A CB  1 
ATOM   652  C CG  . ARG   A 1 97  ? -21.547 -0.970  -22.799 1.00 29.83 ? 114 ARG   A CG  1 
ATOM   653  C CD  . ARG   A 1 97  ? -21.448 0.453   -23.346 1.00 36.69 ? 114 ARG   A CD  1 
ATOM   654  N NE  . ARG   A 1 97  ? -22.085 1.444   -22.489 1.00 43.58 ? 114 ARG   A NE  1 
ATOM   655  C CZ  . ARG   A 1 97  ? -21.594 2.654   -22.251 1.00 46.54 ? 114 ARG   A CZ  1 
ATOM   656  N NH1 . ARG   A 1 97  ? -20.457 3.060   -22.795 1.00 51.90 ? 114 ARG   A NH1 1 
ATOM   657  N NH2 . ARG   A 1 97  ? -22.265 3.484   -21.454 1.00 49.17 ? 114 ARG   A NH2 1 
ATOM   658  N N   . ILE   A 1 98  ? -21.132 -4.237  -21.785 1.00 18.68 ? 115 ILE   A N   1 
ATOM   659  C CA  . ILE   A 1 98  ? -20.589 -5.066  -20.716 1.00 18.22 ? 115 ILE   A CA  1 
ATOM   660  C C   . ILE   A 1 98  ? -19.200 -4.575  -20.338 1.00 19.97 ? 115 ILE   A C   1 
ATOM   661  O O   . ILE   A 1 98  ? -18.360 -4.328  -21.211 1.00 20.01 ? 115 ILE   A O   1 
ATOM   662  C CB  . ILE   A 1 98  ? -20.528 -6.543  -21.138 1.00 17.45 ? 115 ILE   A CB  1 
ATOM   663  C CG1 . ILE   A 1 98  ? -21.936 -7.111  -21.231 1.00 19.05 ? 115 ILE   A CG1 1 
ATOM   664  C CG2 . ILE   A 1 98  ? -19.671 -7.347  -20.168 1.00 17.99 ? 115 ILE   A CG2 1 
ATOM   665  C CD1 . ILE   A 1 98  ? -21.996 -8.354  -22.103 1.00 20.62 ? 115 ILE   A CD1 1 
ATOM   666  N N   . LEU   A 1 99  ? -18.960 -4.442  -19.038 1.00 19.83 ? 116 LEU   A N   1 
ATOM   667  C CA  . LEU   A 1 99  ? -17.649 -4.117  -18.492 1.00 17.56 ? 116 LEU   A CA  1 
ATOM   668  C C   . LEU   A 1 99  ? -17.249 -5.226  -17.530 1.00 16.69 ? 116 LEU   A C   1 
ATOM   669  O O   . LEU   A 1 99  ? -17.911 -5.424  -16.507 1.00 15.68 ? 116 LEU   A O   1 
ATOM   670  C CB  . LEU   A 1 99  ? -17.675 -2.766  -17.770 1.00 18.89 ? 116 LEU   A CB  1 
ATOM   671  C CG  . LEU   A 1 99  ? -16.401 -2.445  -16.980 1.00 21.10 ? 116 LEU   A CG  1 
ATOM   672  C CD1 . LEU   A 1 99  ? -15.187 -2.369  -17.901 1.00 23.90 ? 116 LEU   A CD1 1 
ATOM   673  C CD2 . LEU   A 1 99  ? -16.559 -1.167  -16.167 1.00 21.97 ? 116 LEU   A CD2 1 
ATOM   674  N N   . CYS   A 1 100 ? -16.178 -5.946  -17.852 1.00 15.99 ? 117 CYS   A N   1 
ATOM   675  C CA  . CYS   A 1 100 ? -15.615 -6.956  -16.966 1.00 15.35 ? 117 CYS   A CA  1 
ATOM   676  C C   . CYS   A 1 100 ? -14.327 -6.442  -16.342 1.00 18.49 ? 117 CYS   A C   1 
ATOM   677  O O   . CYS   A 1 100 ? -13.509 -5.804  -17.013 1.00 19.98 ? 117 CYS   A O   1 
ATOM   678  C CB  . CYS   A 1 100 ? -15.337 -8.279  -17.697 1.00 15.95 ? 117 CYS   A CB  1 
ATOM   679  S SG  . CYS   A 1 100 ? -16.818 -9.138  -18.215 1.00 17.61 ? 117 CYS   A SG  1 
ATOM   680  N N   . LEU   A 1 101 ? -14.152 -6.742  -15.060 1.00 17.16 ? 118 LEU   A N   1 
ATOM   681  C CA  . LEU   A 1 101 ? -13.029 -6.270  -14.259 1.00 17.34 ? 118 LEU   A CA  1 
ATOM   682  C C   . LEU   A 1 101 ? -12.309 -7.487  -13.706 1.00 17.36 ? 118 LEU   A C   1 
ATOM   683  O O   . LEU   A 1 101 ? -12.933 -8.311  -13.027 1.00 17.02 ? 118 LEU   A O   1 
ATOM   684  C CB  . LEU   A 1 101 ? -13.534 -5.396  -13.120 1.00 19.48 ? 118 LEU   A CB  1 
ATOM   685  C CG  . LEU   A 1 101 ? -14.444 -4.250  -13.560 1.00 20.49 ? 118 LEU   A CG  1 
ATOM   686  C CD1 . LEU   A 1 101 ? -15.050 -3.566  -12.341 1.00 23.15 ? 118 LEU   A CD1 1 
ATOM   687  C CD2 . LEU   A 1 101 ? -13.637 -3.272  -14.385 1.00 26.08 ? 118 LEU   A CD2 1 
ATOM   688  N N   . PHE   A 1 102 ? -11.015 -7.607  -13.995 1.00 17.12 ? 119 PHE   A N   1 
ATOM   689  C CA  . PHE   A 1 102 ? -10.213 -8.760  -13.598 1.00 17.48 ? 119 PHE   A CA  1 
ATOM   690  C C   . PHE   A 1 102 ? -8.927  -8.320  -12.903 1.00 17.16 ? 119 PHE   A C   1 
ATOM   691  O O   . PHE   A 1 102 ? -8.262  -7.376  -13.346 1.00 18.96 ? 119 PHE   A O   1 
ATOM   692  C CB  . PHE   A 1 102 ? -9.849  -9.618  -14.813 1.00 16.47 ? 119 PHE   A CB  1 
ATOM   693  C CG  . PHE   A 1 102 ? -9.000  -10.811 -14.472 1.00 16.94 ? 119 PHE   A CG  1 
ATOM   694  C CD1 . PHE   A 1 102 ? -9.561  -11.911 -13.819 1.00 17.34 ? 119 PHE   A CD1 1 
ATOM   695  C CD2 . PHE   A 1 102 ? -7.650  -10.834 -14.778 1.00 19.73 ? 119 PHE   A CD2 1 
ATOM   696  C CE1 . PHE   A 1 102 ? -8.772  -13.025 -13.503 1.00 19.21 ? 119 PHE   A CE1 1 
ATOM   697  C CE2 . PHE   A 1 102 ? -6.855  -11.922 -14.459 1.00 20.24 ? 119 PHE   A CE2 1 
ATOM   698  C CZ  . PHE   A 1 102 ? -7.411  -13.025 -13.816 1.00 19.42 ? 119 PHE   A CZ  1 
ATOM   699  N N   . ARG   A 1 103 ? -8.547  -9.048  -11.839 1.00 17.26 ? 120 ARG   A N   1 
ATOM   700  C CA  . ARG   A 1 103 ? -7.323  -8.751  -11.092 1.00 20.11 ? 120 ARG   A CA  1 
ATOM   701  C C   . ARG   A 1 103 ? -6.234  -9.787  -11.343 1.00 20.62 ? 120 ARG   A C   1 
ATOM   702  O O   . ARG   A 1 103 ? -6.248  -10.859 -10.720 1.00 21.94 ? 120 ARG   A O   1 
ATOM   703  C CB  . ARG   A 1 103 ? -7.622  -8.657  -9.593  1.00 19.88 ? 120 ARG   A CB  1 
ATOM   704  C CG  . ARG   A 1 103 ? -8.691  -7.640  -9.280  1.00 19.21 ? 120 ARG   A CG  1 
ATOM   705  C CD  . ARG   A 1 103 ? -8.765  -7.252  -7.815  1.00 19.68 ? 120 ARG   A CD  1 
ATOM   706  N NE  . ARG   A 1 103 ? -8.607  -8.399  -6.925  1.00 20.67 ? 120 ARG   A NE  1 
ATOM   707  C CZ  . ARG   A 1 103 ? -9.543  -9.313  -6.675  1.00 16.73 ? 120 ARG   A CZ  1 
ATOM   708  N NH1 . ARG   A 1 103 ? -10.723 -9.291  -7.279  1.00 17.04 ? 120 ARG   A NH1 1 
ATOM   709  N NH2 . ARG   A 1 103 ? -9.283  -10.271 -5.792  1.00 20.07 ? 120 ARG   A NH2 1 
ATOM   710  N N   . PRO   A 1 104 ? -5.251  -9.504  -12.204 1.00 20.26 ? 121 PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 104 ? -4.151  -10.464 -12.414 1.00 21.29 ? 121 PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 104 ? -3.358  -10.776 -11.156 1.00 25.20 ? 121 PRO   A C   1 
ATOM   713  O O   . PRO   A 1 104 ? -2.747  -11.851 -11.070 1.00 27.17 ? 121 PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 104 ? -3.265  -9.752  -13.448 1.00 25.50 ? 121 PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 104 ? -4.158  -8.765  -14.114 1.00 26.07 ? 121 PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 104 ? -5.097  -8.304  -13.045 1.00 21.65 ? 121 PRO   A CD  1 
ATOM   717  N N   . GLN   A 1 105 ? -3.305  -9.858  -10.188 1.00 23.73 ? 122 GLN   A N   1 
ATOM   718  C CA  . GLN   A 1 105 ? -2.530  -10.130 -8.984  1.00 25.08 ? 122 GLN   A CA  1 
ATOM   719  C C   . GLN   A 1 105 ? -3.138  -11.246 -8.141  1.00 27.19 ? 122 GLN   A C   1 
ATOM   720  O O   . GLN   A 1 105 ? -2.480  -11.722 -7.206  1.00 29.49 ? 122 GLN   A O   1 
ATOM   721  C CB  . GLN   A 1 105 ? -2.375  -8.854  -8.148  1.00 28.37 ? 122 GLN   A CB  1 
ATOM   722  C CG  . GLN   A 1 105 ? -1.425  -7.829  -8.753  1.00 29.46 ? 122 GLN   A CG  1 
ATOM   723  C CD  . GLN   A 1 105 ? -1.350  -6.540  -7.940  1.00 31.54 ? 122 GLN   A CD  1 
ATOM   724  O OE1 . GLN   A 1 105 ? -2.228  -6.250  -7.117  0.65 30.39 ? 122 GLN   A OE1 1 
ATOM   725  N NE2 . GLN   A 1 105 ? -0.298  -5.761  -8.172  0.63 33.16 ? 122 GLN   A NE2 1 
ATOM   726  N N   . SER   A 1 106 ? -4.354  -11.682 -8.472  1.00 25.60 ? 123 SER   A N   1 
ATOM   727  C CA  . SER   A 1 106 ? -4.951  -12.858 -7.843  1.00 26.53 ? 123 SER   A CA  1 
ATOM   728  C C   . SER   A 1 106 ? -4.156  -14.123 -8.123  1.00 27.97 ? 123 SER   A C   1 
ATOM   729  O O   . SER   A 1 106 ? -4.300  -15.111 -7.391  1.00 29.63 ? 123 SER   A O   1 
ATOM   730  C CB  . SER   A 1 106 ? -6.377  -13.081 -8.355  1.00 23.87 ? 123 SER   A CB  1 
ATOM   731  O OG  . SER   A 1 106 ? -6.337  -13.441 -9.730  1.00 23.39 ? 123 SER   A OG  1 
ATOM   732  N N   . GLY   A 1 107 ? -3.350  -14.129 -9.181  1.00 25.53 ? 124 GLY   A N   1 
ATOM   733  C CA  . GLY   A 1 107 ? -2.667  -15.327 -9.612  1.00 29.13 ? 124 GLY   A CA  1 
ATOM   734  C C   . GLY   A 1 107 ? -3.467  -16.210 -10.546 1.00 29.83 ? 124 GLY   A C   1 
ATOM   735  O O   . GLY   A 1 107 ? -2.940  -17.232 -11.011 1.00 32.78 ? 124 GLY   A O   1 
ATOM   736  N N   . ARG   A 1 108 ? -4.708  -15.854 -10.839 1.00 28.72 ? 125 ARG   A N   1 
ATOM   737  C CA  . ARG   A 1 108 ? -5.512  -16.642 -11.756 1.00 27.71 ? 125 ARG   A CA  1 
ATOM   738  C C   . ARG   A 1 108 ? -5.285  -16.213 -13.196 1.00 28.97 ? 125 ARG   A C   1 
ATOM   739  O O   . ARG   A 1 108 ? -4.801  -15.116 -13.486 1.00 26.94 ? 125 ARG   A O   1 
ATOM   740  C CB  . ARG   A 1 108 ? -7.000  -16.534 -11.420 1.00 28.20 ? 125 ARG   A CB  1 
ATOM   741  C CG  . ARG   A 1 108 ? -7.310  -16.898 -9.993  1.00 35.12 ? 125 ARG   A CG  1 
ATOM   742  C CD  . ARG   A 1 108 ? -8.783  -17.128 -9.795  1.00 31.49 ? 125 ARG   A CD  1 
ATOM   743  N NE  . ARG   A 1 108 ? -9.085  -17.458 -8.408  1.00 25.42 ? 125 ARG   A NE  1 
ATOM   744  C CZ  . ARG   A 1 108 ? -9.437  -18.665 -7.987  1.00 27.22 ? 125 ARG   A CZ  1 
ATOM   745  N NH1 . ARG   A 1 108 ? -9.491  -19.701 -8.814  1.00 27.73 ? 125 ARG   A NH1 1 
ATOM   746  N NH2 . ARG   A 1 108 ? -9.737  -18.841 -6.704  1.00 33.47 ? 125 ARG   A NH2 1 
ATOM   747  N N   . VAL   A 1 109 ? -5.635  -17.117 -14.102 1.00 26.40 ? 126 VAL   A N   1 
ATOM   748  C CA  . VAL   A 1 109 ? -5.759  -16.818 -15.519 1.00 25.79 ? 126 VAL   A CA  1 
ATOM   749  C C   . VAL   A 1 109 ? -7.241  -16.697 -15.831 1.00 23.23 ? 126 VAL   A C   1 
ATOM   750  O O   . VAL   A 1 109 ? -8.005  -17.637 -15.598 1.00 23.29 ? 126 VAL   A O   1 
ATOM   751  C CB  . VAL   A 1 109 ? -5.093  -17.899 -16.377 1.00 24.87 ? 126 VAL   A CB  1 
ATOM   752  C CG1 . VAL   A 1 109 ? -5.024  -17.437 -17.816 1.00 29.29 ? 126 VAL   A CG1 1 
ATOM   753  C CG2 . VAL   A 1 109 ? -3.696  -18.180 -15.842 1.00 29.56 ? 126 VAL   A CG2 1 
ATOM   754  N N   . LEU   A 1 110 ? -7.653  -15.545 -16.347 1.00 19.03 ? 127 LEU   A N   1 
ATOM   755  C CA  . LEU   A 1 110 ? -9.054  -15.338 -16.679 1.00 20.23 ? 127 LEU   A CA  1 
ATOM   756  C C   . LEU   A 1 110 ? -9.477  -16.262 -17.813 1.00 18.76 ? 127 LEU   A C   1 
ATOM   757  O O   . LEU   A 1 110 ? -8.768  -16.396 -18.812 1.00 20.62 ? 127 LEU   A O   1 
ATOM   758  C CB  . LEU   A 1 110 ? -9.295  -13.877 -17.070 1.00 19.12 ? 127 LEU   A CB  1 
ATOM   759  C CG  . LEU   A 1 110 ? -10.713 -13.567 -17.539 1.00 19.24 ? 127 LEU   A CG  1 
ATOM   760  C CD1 . LEU   A 1 110 ? -11.701 -13.834 -16.417 1.00 19.15 ? 127 LEU   A CD1 1 
ATOM   761  C CD2 . LEU   A 1 110 ? -10.787 -12.084 -17.957 1.00 21.05 ? 127 LEU   A CD2 1 
ATOM   762  N N   . SER   A 1 111 ? -10.641 -16.893 -17.636 1.00 18.38 ? 128 SER   A N   1 
ATOM   763  C CA  . SER   A 1 111 ? -11.295 -17.702 -18.661 1.00 18.48 ? 128 SER   A CA  1 
ATOM   764  C C   . SER   A 1 111 ? -11.109 -17.143 -20.064 1.00 19.50 ? 128 SER   A C   1 
ATOM   765  O O   . SER   A 1 111 ? -11.384 -15.966 -20.316 1.00 19.65 ? 128 SER   A O   1 
ATOM   766  C CB  . SER   A 1 111 ? -12.791 -17.764 -18.363 1.00 17.91 ? 128 SER   A CB  1 
ATOM   767  O OG  . SER   A 1 111 ? -13.436 -18.553 -19.351 1.00 18.21 ? 128 SER   A OG  1 
ATOM   768  N N   . ALA   A 1 112 ? -10.733 -18.019 -20.998 1.00 19.96 ? 129 ALA   A N   1 
ATOM   769  C CA  . ALA   A 1 112 ? -10.659 -17.611 -22.398 1.00 23.62 ? 129 ALA   A CA  1 
ATOM   770  C C   . ALA   A 1 112 ? -12.022 -17.191 -22.942 1.00 22.63 ? 129 ALA   A C   1 
ATOM   771  O O   . ALA   A 1 112 ? -12.088 -16.408 -23.896 1.00 21.73 ? 129 ALA   A O   1 
ATOM   772  C CB  . ALA   A 1 112 ? -10.085 -18.738 -23.259 1.00 22.36 ? 129 ALA   A CB  1 
ATOM   773  N N   . MET   A 1 113 ? -13.121 -17.717 -22.385 1.00 19.64 ? 130 MET   A N   1 
ATOM   774  C CA  . MET   A 1 113 ? -14.440 -17.348 -22.887 1.00 21.75 ? 130 MET   A CA  1 
ATOM   775  C C   . MET   A 1 113 ? -14.823 -15.924 -22.495 1.00 22.79 ? 130 MET   A C   1 
ATOM   776  O O   . MET   A 1 113 ? -15.695 -15.320 -23.139 1.00 23.50 ? 130 MET   A O   1 
ATOM   777  C CB  . MET   A 1 113 ? -15.496 -18.342 -22.387 1.00 21.51 ? 130 MET   A CB  1 
ATOM   778  C CG  . MET   A 1 113 ? -15.304 -19.748 -22.976 1.00 22.47 ? 130 MET   A CG  1 
ATOM   779  S SD  . MET   A 1 113 ? -15.041 -19.840 -24.759 1.00 25.37 ? 130 MET   A SD  1 
ATOM   780  C CE  . MET   A 1 113 ? -16.733 -19.812 -25.346 1.00 26.99 ? 130 MET   A CE  1 
ATOM   781  N N   . ILE   A 1 114 ? -14.218 -15.384 -21.442 1.00 17.21 ? 131 ILE   A N   1 
ATOM   782  C CA  . ILE   A 1 114 ? -14.464 -13.991 -21.065 1.00 20.12 ? 131 ILE   A CA  1 
ATOM   783  C C   . ILE   A 1 114 ? -13.452 -13.070 -21.728 1.00 23.16 ? 131 ILE   A C   1 
ATOM   784  O O   . ILE   A 1 114 ? -13.824 -12.072 -22.353 1.00 21.80 ? 131 ILE   A O   1 
ATOM   785  C CB  . ILE   A 1 114 ? -14.444 -13.833 -19.528 1.00 18.76 ? 131 ILE   A CB  1 
ATOM   786  C CG1 . ILE   A 1 114 ? -15.461 -14.768 -18.859 1.00 22.50 ? 131 ILE   A CG1 1 
ATOM   787  C CG2 . ILE   A 1 114 ? -14.766 -12.381 -19.148 1.00 18.56 ? 131 ILE   A CG2 1 
ATOM   788  C CD1 . ILE   A 1 114 ? -16.848 -14.750 -19.478 1.00 19.21 ? 131 ILE   A CD1 1 
ATOM   789  N N   . ARG   A 1 115 ? -12.162 -13.400 -21.598 1.00 20.92 ? 132 ARG   A N   1 
ATOM   790  C CA  . ARG   A 1 115 ? -11.104 -12.645 -22.270 1.00 21.36 ? 132 ARG   A CA  1 
ATOM   791  C C   . ARG   A 1 115 ? -11.355 -12.551 -23.768 1.00 23.45 ? 132 ARG   A C   1 
ATOM   792  O O   . ARG   A 1 115 ? -11.232 -11.471 -24.360 1.00 26.96 ? 132 ARG   A O   1 
ATOM   793  C CB  . ARG   A 1 115 ? -9.749  -13.299 -21.977 1.00 25.80 ? 132 ARG   A CB  1 
ATOM   794  C CG  . ARG   A 1 115 ? -8.537  -12.583 -22.528 1.00 31.73 ? 132 ARG   A CG  1 
ATOM   795  C CD  . ARG   A 1 115 ? -8.193  -11.421 -21.659 1.00 29.35 ? 132 ARG   A CD  1 
ATOM   796  N NE  . ARG   A 1 115 ? -7.624  -11.756 -20.356 1.00 26.40 ? 132 ARG   A NE  1 
ATOM   797  C CZ  . ARG   A 1 115 ? -7.326  -10.822 -19.459 1.00 24.38 ? 132 ARG   A CZ  1 
ATOM   798  N NH1 . ARG   A 1 115 ? -7.566  -9.544  -19.697 1.00 31.19 ? 132 ARG   A NH1 1 
ATOM   799  N NH2 . ARG   A 1 115 ? -6.799  -11.178 -18.290 1.00 25.46 ? 132 ARG   A NH2 1 
ATOM   800  N N   . GLY   A 1 116 ? -11.724 -13.666 -24.395 1.00 23.77 ? 133 GLY   A N   1 
ATOM   801  C CA  . GLY   A 1 116 ? -11.934 -13.713 -25.829 1.00 24.55 ? 133 GLY   A CA  1 
ATOM   802  C C   . GLY   A 1 116 ? -13.266 -13.189 -26.319 1.00 24.30 ? 133 GLY   A C   1 
ATOM   803  O O   . GLY   A 1 116 ? -13.428 -13.020 -27.530 1.00 25.84 ? 133 GLY   A O   1 
ATOM   804  N N   . ALA   A 1 117 ? -14.220 -12.930 -25.414 1.00 23.26 ? 134 ALA   A N   1 
ATOM   805  C CA  . ALA   A 1 117 ? -15.485 -12.316 -25.802 1.00 25.54 ? 134 ALA   A CA  1 
ATOM   806  C C   . ALA   A 1 117 ? -15.359 -10.813 -26.005 1.00 25.29 ? 134 ALA   A C   1 
ATOM   807  O O   . ALA   A 1 117 ? -16.217 -10.214 -26.661 1.00 27.29 ? 134 ALA   A O   1 
ATOM   808  C CB  . ALA   A 1 117 ? -16.570 -12.592 -24.753 1.00 22.23 ? 134 ALA   A CB  1 
ATOM   809  N N   . ALA   A 1 118 ? -14.304 -10.204 -25.478 1.00 26.30 ? 135 ALA   A N   1 
ATOM   810  C CA  . ALA   A 1 118 ? -14.166 -8.757  -25.542 1.00 26.75 ? 135 ALA   A CA  1 
ATOM   811  C C   . ALA   A 1 118 ? -13.971 -8.301  -26.979 1.00 29.39 ? 135 ALA   A C   1 
ATOM   812  O O   . ALA   A 1 118 ? -13.139 -8.844  -27.714 1.00 34.80 ? 135 ALA   A O   1 
ATOM   813  C CB  . ALA   A 1 118 ? -12.995 -8.292  -24.678 1.00 29.61 ? 135 ALA   A CB  1 
ATOM   814  N N   . ASP   A 1 119 ? -14.753 -7.307  -27.383 1.00 30.18 ? 136 ASP   A N   1 
ATOM   815  C CA  . ASP   A 1 119 ? -14.572 -6.636  -28.662 1.00 28.25 ? 136 ASP   A CA  1 
ATOM   816  C C   . ASP   A 1 119 ? -14.031 -5.219  -28.498 1.00 32.80 ? 136 ASP   A C   1 
ATOM   817  O O   . ASP   A 1 119 ? -13.874 -4.499  -29.493 1.00 33.75 ? 136 ASP   A O   1 
ATOM   818  C CB  . ASP   A 1 119 ? -15.897 -6.647  -29.431 1.00 32.41 ? 136 ASP   A CB  1 
ATOM   819  C CG  . ASP   A 1 119 ? -16.948 -5.732  -28.812 1.00 35.74 ? 136 ASP   A CG  1 
ATOM   820  O OD1 . ASP   A 1 119 ? -18.086 -5.729  -29.324 1.00 45.93 ? 136 ASP   A OD1 1 
ATOM   821  O OD2 . ASP   A 1 119 ? -16.663 -5.032  -27.816 1.00 33.49 ? 136 ASP   A OD2 1 
ATOM   822  N N   . GLY   A 1 120 ? -13.740 -4.808  -27.264 1.00 31.05 ? 137 GLY   A N   1 
ATOM   823  C CA  . GLY   A 1 120 ? -13.128 -3.531  -26.998 1.00 33.80 ? 137 GLY   A CA  1 
ATOM   824  C C   . GLY   A 1 120 ? -14.064 -2.349  -27.028 1.00 32.79 ? 137 GLY   A C   1 
ATOM   825  O O   . GLY   A 1 120 ? -13.609 -1.222  -26.802 1.00 38.25 ? 137 GLY   A O   1 
ATOM   826  N N   . SER   A 1 121 ? -15.350 -2.561  -27.306 1.00 31.74 ? 138 SER   A N   1 
ATOM   827  C CA  . SER   A 1 121 ? -16.321 -1.474  -27.289 1.00 33.27 ? 138 SER   A CA  1 
ATOM   828  C C   . SER   A 1 121 ? -17.550 -1.861  -26.475 1.00 33.83 ? 138 SER   A C   1 
ATOM   829  O O   . SER   A 1 121 ? -17.715 -1.415  -25.331 1.00 31.91 ? 138 SER   A O   1 
ATOM   830  C CB  . SER   A 1 121 ? -16.722 -1.087  -28.715 1.00 34.99 ? 138 SER   A CB  1 
ATOM   831  O OG  . SER   A 1 121 ? -15.924 -0.013  -29.182 1.00 48.85 ? 138 SER   A OG  1 
ATOM   832  N N   . ARG   A 1 122 ? -18.417 -2.699  -27.053 1.00 29.09 ? 139 ARG   A N   1 
ATOM   833  C CA  . ARG   A 1 122 ? -19.600 -3.155  -26.324 1.00 32.88 ? 139 ARG   A CA  1 
ATOM   834  C C   . ARG   A 1 122 ? -19.257 -4.132  -25.203 1.00 28.99 ? 139 ARG   A C   1 
ATOM   835  O O   . ARG   A 1 122 ? -20.016 -4.252  -24.235 1.00 29.57 ? 139 ARG   A O   1 
ATOM   836  C CB  . ARG   A 1 122 ? -20.598 -3.820  -27.271 1.00 34.45 ? 139 ARG   A CB  1 
ATOM   837  C CG  . ARG   A 1 122 ? -22.038 -3.576  -26.858 1.00 40.21 ? 139 ARG   A CG  1 
ATOM   838  C CD  . ARG   A 1 122 ? -22.942 -3.246  -28.043 1.00 43.80 ? 139 ARG   A CD  1 
ATOM   839  N NE  . ARG   A 1 122 ? -24.312 -2.978  -27.615 1.00 45.37 ? 139 ARG   A NE  1 
ATOM   840  C CZ  . ARG   A 1 122 ? -24.676 -1.999  -26.796 1.00 44.31 ? 139 ARG   A CZ  1 
ATOM   841  N NH1 . ARG   A 1 122 ? -23.836 -1.031  -26.451 1.00 47.16 ? 139 ARG   A NH1 1 
ATOM   842  N NH2 . ARG   A 1 122 ? -25.928 -1.962  -26.347 1.00 40.53 ? 139 ARG   A NH2 1 
ATOM   843  N N   . PHE   A 1 123 ? -18.166 -4.876  -25.333 1.00 24.93 ? 140 PHE   A N   1 
ATOM   844  C CA  . PHE   A 1 123 ? -17.741 -5.852  -24.333 1.00 23.15 ? 140 PHE   A CA  1 
ATOM   845  C C   . PHE   A 1 123 ? -16.285 -5.525  -24.053 1.00 23.28 ? 140 PHE   A C   1 
ATOM   846  O O   . PHE   A 1 123 ? -15.425 -5.749  -24.911 1.00 23.64 ? 140 PHE   A O   1 
ATOM   847  C CB  . PHE   A 1 123 ? -17.911 -7.296  -24.839 1.00 24.57 ? 140 PHE   A CB  1 
ATOM   848  C CG  . PHE   A 1 123 ? -17.781 -8.365  -23.764 1.00 22.50 ? 140 PHE   A CG  1 
ATOM   849  C CD1 . PHE   A 1 123 ? -16.646 -8.447  -22.963 1.00 21.23 ? 140 PHE   A CD1 1 
ATOM   850  C CD2 . PHE   A 1 123 ? -18.766 -9.326  -23.599 1.00 22.80 ? 140 PHE   A CD2 1 
ATOM   851  C CE1 . PHE   A 1 123 ? -16.515 -9.432  -21.989 1.00 22.28 ? 140 PHE   A CE1 1 
ATOM   852  C CE2 . PHE   A 1 123 ? -18.638 -10.327 -22.629 1.00 20.43 ? 140 PHE   A CE2 1 
ATOM   853  C CZ  . PHE   A 1 123 ? -17.508 -10.371 -21.821 1.00 20.55 ? 140 PHE   A CZ  1 
ATOM   854  N N   . GLN   A 1 124 ? -16.013 -4.968  -22.876 1.00 22.81 ? 141 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 124 ? -14.662 -4.584  -22.497 1.00 21.07 ? 141 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 124 ? -14.221 -5.417  -21.303 1.00 20.57 ? 141 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 124 ? -15.016 -5.706  -20.404 1.00 20.33 ? 141 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 124 ? -14.585 -3.097  -22.164 1.00 21.46 ? 141 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 124 ? -14.789 -2.227  -23.388 1.00 21.90 ? 141 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 124 ? -14.788 -0.751  -23.057 1.00 30.02 ? 141 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 124 ? -14.084 -0.308  -22.149 1.00 30.69 ? 141 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 124 ? -15.581 0.021   -23.790 1.00 35.49 ? 141 GLN   A NE2 1 
ATOM   863  N N   . VAL   A 1 125 ? -12.955 -5.812  -21.306 1.00 21.63 ? 142 VAL   A N   1 
ATOM   864  C CA  . VAL   A 1 125 ? -12.331 -6.500  -20.184 1.00 20.16 ? 142 VAL   A CA  1 
ATOM   865  C C   . VAL   A 1 125 ? -11.138 -5.662  -19.753 1.00 22.11 ? 142 VAL   A C   1 
ATOM   866  O O   . VAL   A 1 125 ? -10.210 -5.444  -20.541 1.00 26.34 ? 142 VAL   A O   1 
ATOM   867  C CB  . VAL   A 1 125 ? -11.890 -7.923  -20.556 1.00 23.19 ? 142 VAL   A CB  1 
ATOM   868  C CG1 . VAL   A 1 125 ? -11.188 -8.579  -19.384 1.00 25.41 ? 142 VAL   A CG1 1 
ATOM   869  C CG2 . VAL   A 1 125 ? -13.083 -8.768  -21.012 1.00 22.78 ? 142 VAL   A CG2 1 
ATOM   870  N N   . TRP   A 1 126 ? -11.163 -5.186  -18.514 1.00 19.40 ? 143 TRP   A N   1 
ATOM   871  C CA  . TRP   A 1 126 ? -10.071 -4.384  -17.969 1.00 21.16 ? 143 TRP   A CA  1 
ATOM   872  C C   . TRP   A 1 126 ? -9.343  -5.154  -16.879 1.00 20.54 ? 143 TRP   A C   1 
ATOM   873  O O   . TRP   A 1 126 ? -9.970  -5.628  -15.928 1.00 21.87 ? 143 TRP   A O   1 
ATOM   874  C CB  . TRP   A 1 126 ? -10.574 -3.060  -17.386 1.00 23.75 ? 143 TRP   A CB  1 
ATOM   875  C CG  . TRP   A 1 126 ? -11.257 -2.100  -18.334 1.00 26.64 ? 143 TRP   A CG  1 
ATOM   876  C CD1 . TRP   A 1 126 ? -12.191 -2.388  -19.287 1.00 27.69 ? 143 TRP   A CD1 1 
ATOM   877  C CD2 . TRP   A 1 126 ? -11.105 -0.683  -18.341 1.00 28.06 ? 143 TRP   A CD2 1 
ATOM   878  N NE1 . TRP   A 1 126 ? -12.596 -1.229  -19.920 1.00 29.24 ? 143 TRP   A NE1 1 
ATOM   879  C CE2 . TRP   A 1 126 ? -11.935 -0.171  -19.356 1.00 26.52 ? 143 TRP   A CE2 1 
ATOM   880  C CE3 . TRP   A 1 126 ? -10.308 0.204   -17.613 1.00 30.26 ? 143 TRP   A CE3 1 
ATOM   881  C CZ2 . TRP   A 1 126 ? -12.020 1.185   -19.635 1.00 27.40 ? 143 TRP   A CZ2 1 
ATOM   882  C CZ3 . TRP   A 1 126 ? -10.386 1.558   -17.900 1.00 33.48 ? 143 TRP   A CZ3 1 
ATOM   883  C CH2 . TRP   A 1 126 ? -11.231 2.034   -18.907 1.00 32.57 ? 143 TRP   A CH2 1 
ATOM   884  N N   . ASP   A 1 127 ? -8.024  -5.276  -17.023 1.00 22.40 ? 144 ASP   A N   1 
ATOM   885  C CA  A ASP   A 1 127 ? -7.184  -5.756  -15.940 0.59 22.26 ? 144 ASP   A CA  1 
ATOM   886  C CA  B ASP   A 1 127 ? -7.183  -5.759  -15.940 0.41 22.27 ? 144 ASP   A CA  1 
ATOM   887  C C   . ASP   A 1 127 ? -6.864  -4.593  -15.015 1.00 21.78 ? 144 ASP   A C   1 
ATOM   888  O O   . ASP   A 1 127 ? -6.597  -3.479  -15.473 1.00 24.25 ? 144 ASP   A O   1 
ATOM   889  C CB  A ASP   A 1 127 ? -5.898  -6.352  -16.500 0.59 22.78 ? 144 ASP   A CB  1 
ATOM   890  C CB  B ASP   A 1 127 ? -5.877  -6.356  -16.473 0.41 22.79 ? 144 ASP   A CB  1 
ATOM   891  C CG  A ASP   A 1 127 ? -6.148  -7.556  -17.367 0.59 23.98 ? 144 ASP   A CG  1 
ATOM   892  C CG  B ASP   A 1 127 ? -6.071  -7.694  -17.162 0.41 24.18 ? 144 ASP   A CG  1 
ATOM   893  O OD1 A ASP   A 1 127 ? -6.429  -8.635  -16.818 0.59 24.52 ? 144 ASP   A OD1 1 
ATOM   894  O OD1 B ASP   A 1 127 ? -7.059  -8.391  -16.855 0.41 25.23 ? 144 ASP   A OD1 1 
ATOM   895  O OD2 A ASP   A 1 127 ? -6.110  -7.412  -18.604 0.59 26.06 ? 144 ASP   A OD2 1 
ATOM   896  O OD2 B ASP   A 1 127 ? -5.202  -8.063  -17.988 0.41 26.72 ? 144 ASP   A OD2 1 
ATOM   897  N N   . TYR   A 1 128 ? -6.897  -4.844  -13.707 1.00 21.79 ? 145 TYR   A N   1 
ATOM   898  C CA  . TYR   A 1 128 ? -6.705  -3.741  -12.768 1.00 20.81 ? 145 TYR   A CA  1 
ATOM   899  C C   . TYR   A 1 128 ? -6.178  -4.257  -11.433 1.00 21.53 ? 145 TYR   A C   1 
ATOM   900  O O   . TYR   A 1 128 ? -6.219  -5.461  -11.143 1.00 20.32 ? 145 TYR   A O   1 
ATOM   901  C CB  . TYR   A 1 128 ? -8.025  -2.969  -12.574 1.00 20.75 ? 145 TYR   A CB  1 
ATOM   902  C CG  . TYR   A 1 128 ? -8.998  -3.668  -11.650 1.00 20.89 ? 145 TYR   A CG  1 
ATOM   903  C CD1 . TYR   A 1 128 ? -9.681  -4.801  -12.071 1.00 20.68 ? 145 TYR   A CD1 1 
ATOM   904  C CD2 . TYR   A 1 128 ? -9.242  -3.195  -10.369 1.00 20.94 ? 145 TYR   A CD2 1 
ATOM   905  C CE1 . TYR   A 1 128 ? -10.559 -5.456  -11.234 1.00 19.22 ? 145 TYR   A CE1 1 
ATOM   906  C CE2 . TYR   A 1 128 ? -10.118 -3.832  -9.526  1.00 20.46 ? 145 TYR   A CE2 1 
ATOM   907  C CZ  . TYR   A 1 128 ? -10.775 -4.962  -9.957  1.00 19.20 ? 145 TYR   A CZ  1 
ATOM   908  O OH  . TYR   A 1 128 ? -11.648 -5.602  -9.109  1.00 19.44 ? 145 TYR   A OH  1 
ATOM   909  N N   . GLU   A 1 129 ? -5.683  -3.320  -10.617 1.00 23.01 ? 146 GLU   A N   1 
ATOM   910  C CA  . GLU   A 1 129 ? -5.286  -3.579  -9.236  1.00 22.85 ? 146 GLU   A CA  1 
ATOM   911  C C   . GLU   A 1 129 ? -6.389  -3.093  -8.305  1.00 24.92 ? 146 GLU   A C   1 
ATOM   912  O O   . GLU   A 1 129 ? -6.993  -2.044  -8.552  1.00 23.33 ? 146 GLU   A O   1 
ATOM   913  C CB  . GLU   A 1 129 ? -3.972  -2.874  -8.905  1.00 25.97 ? 146 GLU   A CB  1 
ATOM   914  C CG  . GLU   A 1 129 ? -2.798  -3.385  -9.705  1.00 27.06 ? 146 GLU   A CG  1 
ATOM   915  C CD  . GLU   A 1 129 ? -1.546  -2.562  -9.427  1.00 30.72 ? 146 GLU   A CD  1 
ATOM   916  O OE1 . GLU   A 1 129 ? -1.518  -1.837  -8.412  1.00 36.69 ? 146 GLU   A OE1 1 
ATOM   917  O OE2 . GLU   A 1 129 ? -0.625  -2.555  -10.256 1.00 34.26 ? 146 GLU   A OE2 1 
ATOM   918  N N   . GLU   A 1 130 ? -6.626  -3.846  -7.220  1.00 24.81 ? 147 GLU   A N   1 
ATOM   919  C CA  . GLU   A 1 130 ? -7.838  -3.682  -6.411  1.00 24.47 ? 147 GLU   A CA  1 
ATOM   920  C C   . GLU   A 1 130 ? -8.057  -2.260  -5.908  1.00 24.23 ? 147 GLU   A C   1 
ATOM   921  O O   . GLU   A 1 130 ? -9.206  -1.806  -5.831  1.00 27.21 ? 147 GLU   A O   1 
ATOM   922  C CB  . GLU   A 1 130 ? -7.824  -4.661  -5.224  1.00 27.41 ? 147 GLU   A CB  1 
ATOM   923  C CG  . GLU   A 1 130 ? -6.698  -4.482  -4.200  1.00 30.93 ? 147 GLU   A CG  1 
ATOM   924  C CD  . GLU   A 1 130 ? -6.923  -3.378  -3.159  0.65 26.83 ? 147 GLU   A CD  1 
ATOM   925  O OE1 . GLU   A 1 130 ? -8.086  -2.979  -2.904  0.74 31.68 ? 147 GLU   A OE1 1 
ATOM   926  O OE2 . GLU   A 1 130 ? -5.909  -2.916  -2.584  0.70 31.91 ? 147 GLU   A OE2 1 
ATOM   927  N N   . GLY   A 1 131 ? -6.981  -1.541  -5.574  1.00 25.49 ? 148 GLY   A N   1 
ATOM   928  C CA  . GLY   A 1 131 ? -7.124  -0.208  -5.006  1.00 26.24 ? 148 GLY   A CA  1 
ATOM   929  C C   . GLY   A 1 131 ? -7.703  0.810   -5.962  1.00 25.66 ? 148 GLY   A C   1 
ATOM   930  O O   . GLY   A 1 131 ? -8.252  1.826   -5.516  1.00 28.36 ? 148 GLY   A O   1 
ATOM   931  N N   . GLU   A 1 132 ? -7.618  0.547   -7.261  1.00 27.21 ? 149 GLU   A N   1 
ATOM   932  C CA  . GLU   A 1 132 ? -7.981  1.488   -8.309  1.00 25.24 ? 149 GLU   A CA  1 
ATOM   933  C C   . GLU   A 1 132 ? -9.421  1.347   -8.794  1.00 25.61 ? 149 GLU   A C   1 
ATOM   934  O O   . GLU   A 1 132 ? -9.795  2.041   -9.740  1.00 25.69 ? 149 GLU   A O   1 
ATOM   935  C CB  . GLU   A 1 132 ? -7.040  1.308   -9.512  1.00 29.38 ? 149 GLU   A CB  1 
ATOM   936  C CG  . GLU   A 1 132 ? -5.558  1.636   -9.287  1.00 33.93 ? 149 GLU   A CG  1 
ATOM   937  C CD  . GLU   A 1 132 ? -5.305  3.088   -8.899  1.00 42.59 ? 149 GLU   A CD  1 
ATOM   938  O OE1 . GLU   A 1 132 ? -4.272  3.358   -8.246  1.00 50.37 ? 149 GLU   A OE1 1 
ATOM   939  O OE2 . GLU   A 1 132 ? -6.124  3.965   -9.260  1.00 38.84 ? 149 GLU   A OE2 1 
ATOM   940  N N   . VAL   A 1 133 ? -10.239 0.478   -8.191  1.00 21.78 ? 150 VAL   A N   1 
ATOM   941  C CA  . VAL   A 1 133 ? -11.502 0.118   -8.838  1.00 19.88 ? 150 VAL   A CA  1 
ATOM   942  C C   . VAL   A 1 133 ? -12.446 1.318   -8.930  1.00 21.36 ? 150 VAL   A C   1 
ATOM   943  O O   . VAL   A 1 133 ? -13.126 1.494   -9.945  1.00 21.44 ? 150 VAL   A O   1 
ATOM   944  C CB  . VAL   A 1 133 ? -12.166 -1.098  -8.151  1.00 19.03 ? 150 VAL   A CB  1 
ATOM   945  C CG1 . VAL   A 1 133 ? -12.885 -0.727  -6.852  1.00 22.36 ? 150 VAL   A CG1 1 
ATOM   946  C CG2 . VAL   A 1 133 ? -13.131 -1.762  -9.123  1.00 21.18 ? 150 VAL   A CG2 1 
ATOM   947  N N   . GLU   A 1 134 ? -12.493 2.168   -7.896  1.00 20.52 ? 151 GLU   A N   1 
ATOM   948  C CA  . GLU   A 1 134 ? -13.350 3.354   -7.946  1.00 22.16 ? 151 GLU   A CA  1 
ATOM   949  C C   . GLU   A 1 134 ? -12.918 4.286   -9.066  1.00 25.00 ? 151 GLU   A C   1 
ATOM   950  O O   . GLU   A 1 134 ? -13.747 4.810   -9.818  1.00 22.85 ? 151 GLU   A O   1 
ATOM   951  C CB  . GLU   A 1 134 ? -13.315 4.093   -6.608  1.00 22.23 ? 151 GLU   A CB  1 
ATOM   952  C CG  . GLU   A 1 134 ? -14.089 3.419   -5.487  1.00 21.32 ? 151 GLU   A CG  1 
ATOM   953  C CD  . GLU   A 1 134 ? -13.259 2.404   -4.717  1.00 21.26 ? 151 GLU   A CD  1 
ATOM   954  O OE1 . GLU   A 1 134 ? -12.076 2.186   -5.072  1.00 21.90 ? 151 GLU   A OE1 1 
ATOM   955  O OE2 . GLU   A 1 134 ? -13.794 1.830   -3.744  1.00 20.89 ? 151 GLU   A OE2 1 
ATOM   956  N N   . ALA   A 1 135 ? -11.611 4.523   -9.169  1.00 24.95 ? 152 ALA   A N   1 
ATOM   957  C CA  . ALA   A 1 135 ? -11.074 5.374   -10.218 1.00 25.54 ? 152 ALA   A CA  1 
ATOM   958  C C   . ALA   A 1 135 ? -11.360 4.810   -11.601 1.00 25.75 ? 152 ALA   A C   1 
ATOM   959  O O   . ALA   A 1 135 ? -11.701 5.559   -12.526 1.00 30.00 ? 152 ALA   A O   1 
ATOM   960  C CB  . ALA   A 1 135 ? -9.579  5.533   -10.009 1.00 27.49 ? 152 ALA   A CB  1 
ATOM   961  N N   . LEU   A 1 136 ? -11.206 3.494   -11.770 1.00 24.57 ? 153 LEU   A N   1 
ATOM   962  C CA  . LEU   A 1 136 ? -11.469 2.899   -13.073 1.00 22.82 ? 153 LEU   A CA  1 
ATOM   963  C C   . LEU   A 1 136 ? -12.932 3.061   -13.451 1.00 22.68 ? 153 LEU   A C   1 
ATOM   964  O O   . LEU   A 1 136 ? -13.250 3.396   -14.597 1.00 26.32 ? 153 LEU   A O   1 
ATOM   965  C CB  . LEU   A 1 136 ? -11.044 1.419   -13.075 1.00 23.86 ? 153 LEU   A CB  1 
ATOM   966  C CG  . LEU   A 1 136 ? -11.191 0.479   -14.283 1.00 29.88 ? 153 LEU   A CG  1 
ATOM   967  C CD1 . LEU   A 1 136 ? -10.526 -0.821  -13.929 1.00 30.78 ? 153 LEU   A CD1 1 
ATOM   968  C CD2 . LEU   A 1 136 ? -12.643 0.148   -14.681 1.00 29.49 ? 153 LEU   A CD2 1 
ATOM   969  N N   . LEU   A 1 137 ? -13.840 2.812   -12.503 1.00 22.58 ? 154 LEU   A N   1 
ATOM   970  C CA  . LEU   A 1 137 ? -15.254 3.028   -12.767 1.00 21.99 ? 154 LEU   A CA  1 
ATOM   971  C C   . LEU   A 1 137 ? -15.534 4.488   -13.104 1.00 24.05 ? 154 LEU   A C   1 
ATOM   972  O O   . LEU   A 1 137 ? -16.351 4.780   -13.984 1.00 25.62 ? 154 LEU   A O   1 
ATOM   973  C CB  . LEU   A 1 137 ? -16.077 2.572   -11.568 1.00 19.04 ? 154 LEU   A CB  1 
ATOM   974  C CG  . LEU   A 1 137 ? -16.058 1.062   -11.316 1.00 17.43 ? 154 LEU   A CG  1 
ATOM   975  C CD1 . LEU   A 1 137 ? -16.696 0.760   -9.963  1.00 22.38 ? 154 LEU   A CD1 1 
ATOM   976  C CD2 . LEU   A 1 137 ? -16.789 0.337   -12.456 1.00 20.76 ? 154 LEU   A CD2 1 
ATOM   977  N N   . ASP   A 1 138 ? -14.851 5.423   -12.428 1.00 23.60 ? 155 ASP   A N   1 
ATOM   978  C CA  . ASP   A 1 138 ? -14.973 6.834   -12.783 1.00 28.18 ? 155 ASP   A CA  1 
ATOM   979  C C   . ASP   A 1 138 ? -14.615 7.052   -14.247 1.00 29.44 ? 155 ASP   A C   1 
ATOM   980  O O   . ASP   A 1 138 ? -15.331 7.745   -14.978 1.00 30.26 ? 155 ASP   A O   1 
ATOM   981  C CB  . ASP   A 1 138 ? -14.065 7.689   -11.898 1.00 29.00 ? 155 ASP   A CB  1 
ATOM   982  C CG  . ASP   A 1 138 ? -14.639 7.935   -10.509 1.00 30.58 ? 155 ASP   A CG  1 
ATOM   983  O OD1 . ASP   A 1 138 ? -15.777 7.505   -10.235 1.00 29.83 ? 155 ASP   A OD1 1 
ATOM   984  O OD2 . ASP   A 1 138 ? -13.954 8.590   -9.690  1.00 32.49 ? 155 ASP   A OD2 1 
ATOM   985  N N   . ARG   A 1 139 ? -13.503 6.457   -14.691 1.00 27.15 ? 156 ARG   A N   1 
ATOM   986  C CA  . ARG   A 1 139 ? -13.078 6.631   -16.075 1.00 28.47 ? 156 ARG   A CA  1 
ATOM   987  C C   . ARG   A 1 139 ? -14.123 6.076   -17.040 1.00 27.79 ? 156 ARG   A C   1 
ATOM   988  O O   . ARG   A 1 139 ? -14.402 6.683   -18.083 1.00 33.51 ? 156 ARG   A O   1 
ATOM   989  C CB  . ARG   A 1 139 ? -11.725 5.951   -16.308 1.00 32.43 ? 156 ARG   A CB  1 
ATOM   990  C CG  . ARG   A 1 139 ? -10.537 6.476   -15.477 1.00 32.88 ? 156 ARG   A CG  1 
ATOM   991  C CD  . ARG   A 1 139 ? -10.083 7.875   -15.886 1.00 35.56 ? 156 ARG   A CD  1 
ATOM   992  N NE  . ARG   A 1 139 ? -10.833 8.979   -15.289 1.00 41.15 ? 156 ARG   A NE  1 
ATOM   993  C CZ  . ARG   A 1 139 ? -11.064 9.155   -13.991 1.00 38.62 ? 156 ARG   A CZ  1 
ATOM   994  N NH1 . ARG   A 1 139 ? -10.494 8.394   -13.067 1.00 37.63 ? 156 ARG   A NH1 1 
ATOM   995  N NH2 . ARG   A 1 139 ? -11.861 10.150  -13.606 1.00 41.43 ? 156 ARG   A NH2 1 
ATOM   996  N N   . TYR   A 1 140 ? -14.715 4.926   -16.712 1.00 29.37 ? 157 TYR   A N   1 
ATOM   997  C CA  . TYR   A 1 140 ? -15.662 4.304   -17.631 1.00 29.90 ? 157 TYR   A CA  1 
ATOM   998  C C   . TYR   A 1 140 ? -16.981 5.071   -17.686 1.00 29.53 ? 157 TYR   A C   1 
ATOM   999  O O   . TYR   A 1 140 ? -17.565 5.232   -18.763 1.00 32.73 ? 157 TYR   A O   1 
ATOM   1000 C CB  . TYR   A 1 140 ? -15.909 2.849   -17.226 1.00 27.45 ? 157 TYR   A CB  1 
ATOM   1001 C CG  . TYR   A 1 140 ? -16.807 2.091   -18.178 1.00 28.62 ? 157 TYR   A CG  1 
ATOM   1002 C CD1 . TYR   A 1 140 ? -18.191 2.106   -18.033 1.00 27.66 ? 157 TYR   A CD1 1 
ATOM   1003 C CD2 . TYR   A 1 140 ? -16.265 1.323   -19.200 1.00 29.55 ? 157 TYR   A CD2 1 
ATOM   1004 C CE1 . TYR   A 1 140 ? -19.011 1.414   -18.900 1.00 28.38 ? 157 TYR   A CE1 1 
ATOM   1005 C CE2 . TYR   A 1 140 ? -17.080 0.610   -20.063 1.00 27.44 ? 157 TYR   A CE2 1 
ATOM   1006 C CZ  . TYR   A 1 140 ? -18.449 0.658   -19.905 1.00 28.59 ? 157 TYR   A CZ  1 
ATOM   1007 O OH  . TYR   A 1 140 ? -19.266 -0.038  -20.770 1.00 31.02 ? 157 TYR   A OH  1 
ATOM   1008 N N   . PHE   A 1 141 ? -17.476 5.546   -16.545 1.00 29.15 ? 158 PHE   A N   1 
ATOM   1009 C CA  . PHE   A 1 141 ? -18.798 6.162   -16.491 1.00 30.21 ? 158 PHE   A CA  1 
ATOM   1010 C C   . PHE   A 1 141 ? -18.788 7.685   -16.621 1.00 40.38 ? 158 PHE   A C   1 
ATOM   1011 O O   . PHE   A 1 141 ? -19.845 8.304   -16.469 1.00 41.27 ? 158 PHE   A O   1 
ATOM   1012 C CB  . PHE   A 1 141 ? -19.512 5.753   -15.198 1.00 28.92 ? 158 PHE   A CB  1 
ATOM   1013 C CG  . PHE   A 1 141 ? -20.020 4.342   -15.223 1.00 29.35 ? 158 PHE   A CG  1 
ATOM   1014 C CD1 . PHE   A 1 141 ? -21.160 4.026   -15.940 1.00 30.29 ? 158 PHE   A CD1 1 
ATOM   1015 C CD2 . PHE   A 1 141 ? -19.333 3.326   -14.585 1.00 25.84 ? 158 PHE   A CD2 1 
ATOM   1016 C CE1 . PHE   A 1 141 ? -21.628 2.733   -15.989 1.00 27.03 ? 158 PHE   A CE1 1 
ATOM   1017 C CE2 . PHE   A 1 141 ? -19.787 2.023   -14.643 1.00 26.53 ? 158 PHE   A CE2 1 
ATOM   1018 C CZ  . PHE   A 1 141 ? -20.941 1.728   -15.347 1.00 27.38 ? 158 PHE   A CZ  1 
ATOM   1019 N N   . GLU   A 1 142 ? -17.648 8.301   -16.922 1.00 41.87 ? 159 GLU   A N   1 
ATOM   1020 C CA  . GLU   A 1 142 ? -17.608 9.759   -17.096 1.00 44.09 ? 159 GLU   A CA  1 
ATOM   1021 C C   . GLU   A 1 142 ? -17.238 10.172  -18.513 1.00 52.40 ? 159 GLU   A C   1 
ATOM   1022 O O   . GLU   A 1 142 ? -17.409 9.405   -19.458 1.00 55.43 ? 159 GLU   A O   1 
ATOM   1023 C CB  . GLU   A 1 142 ? -16.628 10.385  -16.110 1.00 46.91 ? 159 GLU   A CB  1 
ATOM   1024 C CG  . GLU   A 1 142 ? -17.248 10.735  -14.768 1.00 57.75 ? 159 GLU   A CG  1 
ATOM   1025 C CD  . GLU   A 1 142 ? -16.248 10.692  -13.627 1.00 56.42 ? 159 GLU   A CD  1 
ATOM   1026 O OE1 . GLU   A 1 142 ? -15.121 11.209  -13.798 1.00 62.55 ? 159 GLU   A OE1 1 
ATOM   1027 O OE2 . GLU   A 1 142 ? -16.603 10.167  -12.550 1.00 57.94 ? 159 GLU   A OE2 1 
ATOM   1028 N N   . ARG   B 1 3   ? -27.479 -39.290 -34.929 1.00 55.49 ? 20  ARG   B N   1 
ATOM   1029 C CA  . ARG   B 1 3   ? -26.363 -39.098 -34.011 1.00 49.17 ? 20  ARG   B CA  1 
ATOM   1030 C C   . ARG   B 1 3   ? -26.079 -37.604 -33.832 1.00 46.39 ? 20  ARG   B C   1 
ATOM   1031 O O   . ARG   B 1 3   ? -25.659 -36.914 -34.765 1.00 44.09 ? 20  ARG   B O   1 
ATOM   1032 C CB  . ARG   B 1 3   ? -25.122 -39.852 -34.510 1.00 50.32 ? 20  ARG   B CB  1 
ATOM   1033 C CG  . ARG   B 1 3   ? -25.019 -41.268 -33.935 1.00 52.08 ? 20  ARG   B CG  1 
ATOM   1034 C CD  . ARG   B 1 3   ? -23.769 -42.000 -34.385 1.00 51.41 ? 20  ARG   B CD  1 
ATOM   1035 N NE  . ARG   B 1 3   ? -22.800 -42.120 -33.304 1.00 49.31 ? 20  ARG   B NE  1 
ATOM   1036 C CZ  . ARG   B 1 3   ? -21.613 -41.527 -33.293 1.00 47.84 ? 20  ARG   B CZ  1 
ATOM   1037 N NH1 . ARG   B 1 3   ? -21.180 -40.828 -34.329 1.00 48.98 ? 20  ARG   B NH1 1 
ATOM   1038 N NH2 . ARG   B 1 3   ? -20.838 -41.646 -32.219 1.00 47.94 ? 20  ARG   B NH2 1 
ATOM   1039 N N   . PRO   B 1 4   ? -26.306 -37.099 -32.629 1.00 52.96 ? 21  PRO   B N   1 
ATOM   1040 C CA  . PRO   B 1 4   ? -26.202 -35.662 -32.398 1.00 45.44 ? 21  PRO   B CA  1 
ATOM   1041 C C   . PRO   B 1 4   ? -24.776 -35.141 -32.499 1.00 42.33 ? 21  PRO   B C   1 
ATOM   1042 O O   . PRO   B 1 4   ? -23.793 -35.874 -32.364 1.00 43.97 ? 21  PRO   B O   1 
ATOM   1043 C CB  . PRO   B 1 4   ? -26.739 -35.545 -30.955 1.00 48.64 ? 21  PRO   B CB  1 
ATOM   1044 C CG  . PRO   B 1 4   ? -27.713 -36.719 -30.962 1.00 61.02 ? 21  PRO   B CG  1 
ATOM   1045 C CD  . PRO   B 1 4   ? -26.703 -37.718 -31.362 1.00 53.14 ? 21  PRO   B CD  1 
ATOM   1046 N N   . ALA   B 1 5   ? -24.683 -33.845 -32.781 1.00 37.13 ? 22  ALA   B N   1 
ATOM   1047 C CA  . ALA   B 1 5   ? -23.461 -33.081 -32.570 1.00 35.25 ? 22  ALA   B CA  1 
ATOM   1048 C C   . ALA   B 1 5   ? -23.478 -32.601 -31.126 1.00 32.66 ? 22  ALA   B C   1 
ATOM   1049 O O   . ALA   B 1 5   ? -24.428 -31.929 -30.705 1.00 32.14 ? 22  ALA   B O   1 
ATOM   1050 C CB  . ALA   B 1 5   ? -23.377 -31.900 -33.536 1.00 35.68 ? 22  ALA   B CB  1 
ATOM   1051 N N   . LEU   B 1 6   ? -22.436 -32.947 -30.375 1.00 31.24 ? 23  LEU   B N   1 
ATOM   1052 C CA  . LEU   B 1 6   ? -22.405 -32.760 -28.930 1.00 29.10 ? 23  LEU   B CA  1 
ATOM   1053 C C   . LEU   B 1 6   ? -21.289 -31.806 -28.534 1.00 28.54 ? 23  LEU   B C   1 
ATOM   1054 O O   . LEU   B 1 6   ? -20.151 -31.946 -28.995 1.00 31.17 ? 23  LEU   B O   1 
ATOM   1055 C CB  . LEU   B 1 6   ? -22.218 -34.101 -28.220 1.00 29.85 ? 23  LEU   B CB  1 
ATOM   1056 C CG  . LEU   B 1 6   ? -23.240 -35.181 -28.561 1.00 34.84 ? 23  LEU   B CG  1 
ATOM   1057 C CD1 . LEU   B 1 6   ? -22.730 -36.541 -28.129 1.00 36.04 ? 23  LEU   B CD1 1 
ATOM   1058 C CD2 . LEU   B 1 6   ? -24.593 -34.876 -27.936 1.00 36.13 ? 23  LEU   B CD2 1 
ATOM   1059 N N   . TYR   B 1 7   ? -21.609 -30.863 -27.658 1.00 26.07 ? 24  TYR   B N   1 
ATOM   1060 C CA  . TYR   B 1 7   ? -20.651 -29.897 -27.157 1.00 23.24 ? 24  TYR   B CA  1 
ATOM   1061 C C   . TYR   B 1 7   ? -20.486 -30.154 -25.665 1.00 22.06 ? 24  TYR   B C   1 
ATOM   1062 O O   . TYR   B 1 7   ? -21.469 -30.072 -24.919 1.00 24.56 ? 24  TYR   B O   1 
ATOM   1063 C CB  . TYR   B 1 7   ? -21.171 -28.477 -27.418 1.00 22.76 ? 24  TYR   B CB  1 
ATOM   1064 C CG  . TYR   B 1 7   ? -20.214 -27.356 -27.093 1.00 22.14 ? 24  TYR   B CG  1 
ATOM   1065 C CD1 . TYR   B 1 7   ? -20.005 -26.954 -25.785 1.00 21.29 ? 24  TYR   B CD1 1 
ATOM   1066 C CD2 . TYR   B 1 7   ? -19.546 -26.679 -28.114 1.00 25.12 ? 24  TYR   B CD2 1 
ATOM   1067 C CE1 . TYR   B 1 7   ? -19.124 -25.906 -25.483 1.00 21.75 ? 24  TYR   B CE1 1 
ATOM   1068 C CE2 . TYR   B 1 7   ? -18.674 -25.634 -27.826 1.00 25.54 ? 24  TYR   B CE2 1 
ATOM   1069 C CZ  . TYR   B 1 7   ? -18.466 -25.262 -26.517 1.00 25.21 ? 24  TYR   B CZ  1 
ATOM   1070 O OH  . TYR   B 1 7   ? -17.604 -24.223 -26.246 1.00 23.66 ? 24  TYR   B OH  1 
ATOM   1071 N N   . PHE   B 1 8   ? -19.262 -30.448 -25.219 1.00 20.83 ? 25  PHE   B N   1 
ATOM   1072 C CA  . PHE   B 1 8   ? -19.023 -30.713 -23.800 1.00 20.24 ? 25  PHE   B CA  1 
ATOM   1073 C C   . PHE   B 1 8   ? -18.396 -29.508 -23.099 1.00 18.80 ? 25  PHE   B C   1 
ATOM   1074 O O   . PHE   B 1 8   ? -17.440 -28.917 -23.608 1.00 20.09 ? 25  PHE   B O   1 
ATOM   1075 C CB  . PHE   B 1 8   ? -18.107 -31.925 -23.583 1.00 23.79 ? 25  PHE   B CB  1 
ATOM   1076 C CG  . PHE   B 1 8   ? -17.780 -32.137 -22.133 1.00 21.21 ? 25  PHE   B CG  1 
ATOM   1077 C CD1 . PHE   B 1 8   ? -18.732 -32.680 -21.278 1.00 24.78 ? 25  PHE   B CD1 1 
ATOM   1078 C CD2 . PHE   B 1 8   ? -16.582 -31.683 -21.598 1.00 22.00 ? 25  PHE   B CD2 1 
ATOM   1079 C CE1 . PHE   B 1 8   ? -18.473 -32.831 -19.934 1.00 23.00 ? 25  PHE   B CE1 1 
ATOM   1080 C CE2 . PHE   B 1 8   ? -16.313 -31.817 -20.248 1.00 21.95 ? 25  PHE   B CE2 1 
ATOM   1081 C CZ  . PHE   B 1 8   ? -17.256 -32.391 -19.412 1.00 22.16 ? 25  PHE   B CZ  1 
ATOM   1082 N N   . CYS   B 1 9   ? -18.900 -29.196 -21.900 1.00 17.73 ? 26  CYS   B N   1 
ATOM   1083 C CA  . CYS   B 1 9   ? -18.409 -28.106 -21.057 1.00 17.17 ? 26  CYS   B CA  1 
ATOM   1084 C C   . CYS   B 1 9   ? -17.895 -28.641 -19.729 1.00 15.27 ? 26  CYS   B C   1 
ATOM   1085 O O   . CYS   B 1 9   ? -18.597 -29.399 -19.053 1.00 18.75 ? 26  CYS   B O   1 
ATOM   1086 C CB  . CYS   B 1 9   ? -19.509 -27.078 -20.750 1.00 16.53 ? 26  CYS   B CB  1 
ATOM   1087 S SG  . CYS   B 1 9   ? -20.523 -26.570 -22.117 1.00 18.93 ? 26  CYS   B SG  1 
ATOM   1088 N N   . GLY   B 1 10  ? -16.700 -28.202 -19.331 1.00 16.50 ? 27  GLY   B N   1 
ATOM   1089 C CA  . GLY   B 1 10  ? -16.199 -28.488 -18.000 1.00 16.18 ? 27  GLY   B CA  1 
ATOM   1090 C C   . GLY   B 1 10  ? -15.048 -27.561 -17.680 1.00 16.00 ? 27  GLY   B C   1 
ATOM   1091 O O   . GLY   B 1 10  ? -14.306 -27.144 -18.572 1.00 18.31 ? 27  GLY   B O   1 
ATOM   1092 N N   . SER   B 1 11  ? -14.917 -27.213 -16.396 1.00 16.16 ? 28  SER   B N   1 
ATOM   1093 C CA  . SER   B 1 11  ? -13.930 -26.224 -15.952 1.00 15.17 ? 28  SER   B CA  1 
ATOM   1094 C C   . SER   B 1 11  ? -12.507 -26.529 -16.420 1.00 17.13 ? 28  SER   B C   1 
ATOM   1095 O O   . SER   B 1 11  ? -12.040 -27.672 -16.352 1.00 17.62 ? 28  SER   B O   1 
ATOM   1096 C CB  . SER   B 1 11  ? -13.951 -26.147 -14.422 1.00 15.78 ? 28  SER   B CB  1 
ATOM   1097 O OG  . SER   B 1 11  ? -12.986 -25.215 -13.935 1.00 16.92 ? 28  SER   B OG  1 
ATOM   1098 N N   . ILE   B 1 12  ? -11.796 -25.472 -16.851 1.00 14.95 ? 29  ILE   B N   1 
ATOM   1099 C CA  . ILE   B 1 12  ? -10.366 -25.543 -17.161 1.00 17.10 ? 29  ILE   B CA  1 
ATOM   1100 C C   . ILE   B 1 12  ? -9.651  -24.500 -16.303 1.00 18.63 ? 29  ILE   B C   1 
ATOM   1101 O O   . ILE   B 1 12  ? -9.032  -24.836 -15.287 1.00 18.31 ? 29  ILE   B O   1 
ATOM   1102 C CB  . ILE   B 1 12  ? -10.084 -25.342 -18.662 1.00 16.73 ? 29  ILE   B CB  1 
ATOM   1103 C CG1 . ILE   B 1 12  ? -10.804 -26.410 -19.507 1.00 17.64 ? 29  ILE   B CG1 1 
ATOM   1104 C CG2 . ILE   B 1 12  ? -8.580  -25.438 -18.922 1.00 19.56 ? 29  ILE   B CG2 1 
ATOM   1105 C CD1 . ILE   B 1 12  ? -10.639 -26.206 -20.988 1.00 18.99 ? 29  ILE   B CD1 1 
ATOM   1106 N N   . ARG   B 1 13  ? -9.743  -23.217 -16.681 1.00 18.15 ? 30  ARG   B N   1 
ATOM   1107 C CA  . ARG   B 1 13  ? -9.113  -22.171 -15.875 1.00 19.02 ? 30  ARG   B CA  1 
ATOM   1108 C C   . ARG   B 1 13  ? -9.838  -21.928 -14.554 1.00 18.56 ? 30  ARG   B C   1 
ATOM   1109 O O   . ARG   B 1 13  ? -9.248  -21.341 -13.638 1.00 19.80 ? 30  ARG   B O   1 
ATOM   1110 C CB  . ARG   B 1 13  ? -9.002  -20.884 -16.687 1.00 17.66 ? 30  ARG   B CB  1 
ATOM   1111 C CG  . ARG   B 1 13  ? -8.073  -21.036 -17.872 1.00 19.65 ? 30  ARG   B CG  1 
ATOM   1112 C CD  . ARG   B 1 13  ? -7.885  -19.780 -18.668 1.00 18.59 ? 30  ARG   B CD  1 
ATOM   1113 N NE  . ARG   B 1 13  ? -7.053  -20.043 -19.844 1.00 21.89 ? 30  ARG   B NE  1 
ATOM   1114 C CZ  . ARG   B 1 13  ? -6.909  -19.215 -20.867 1.00 25.17 ? 30  ARG   B CZ  1 
ATOM   1115 N NH1 . ARG   B 1 13  ? -7.470  -18.016 -20.872 1.00 22.66 ? 30  ARG   B NH1 1 
ATOM   1116 N NH2 . ARG   B 1 13  ? -6.184  -19.598 -21.913 1.00 24.91 ? 30  ARG   B NH2 1 
ATOM   1117 N N   . GLY   B 1 14  ? -11.084 -22.394 -14.414 1.00 15.78 ? 31  GLY   B N   1 
ATOM   1118 C CA  . GLY   B 1 14  ? -11.672 -22.394 -13.085 1.00 15.68 ? 31  GLY   B CA  1 
ATOM   1119 C C   . GLY   B 1 14  ? -11.093 -23.450 -12.164 1.00 18.02 ? 31  GLY   B C   1 
ATOM   1120 O O   . GLY   B 1 14  ? -11.374 -23.424 -10.962 1.00 21.04 ? 31  GLY   B O   1 
ATOM   1121 N N   . GLY   B 1 15  ? -10.276 -24.359 -12.702 1.00 19.02 ? 32  GLY   B N   1 
ATOM   1122 C CA  . GLY   B 1 15  ? -9.712  -25.459 -11.942 1.00 20.17 ? 32  GLY   B CA  1 
ATOM   1123 C C   . GLY   B 1 15  ? -9.916  -26.772 -12.669 1.00 17.94 ? 32  GLY   B C   1 
ATOM   1124 O O   . GLY   B 1 15  ? -10.966 -26.981 -13.277 1.00 18.62 ? 32  GLY   B O   1 
ATOM   1125 N N   . ARG   B 1 16  ? -8.915  -27.658 -12.630 1.00 19.63 ? 33  ARG   B N   1 
ATOM   1126 C CA  . ARG   B 1 16  ? -8.939  -28.921 -13.356 1.00 19.05 ? 33  ARG   B CA  1 
ATOM   1127 C C   . ARG   B 1 16  ? -9.145  -30.116 -12.430 1.00 19.22 ? 33  ARG   B C   1 
ATOM   1128 O O   . ARG   B 1 16  ? -8.772  -31.243 -12.765 1.00 21.51 ? 33  ARG   B O   1 
ATOM   1129 C CB  . ARG   B 1 16  ? -7.657  -29.079 -14.171 1.00 22.08 ? 33  ARG   B CB  1 
ATOM   1130 C CG  . ARG   B 1 16  ? -7.445  -27.867 -15.058 1.00 23.01 ? 33  ARG   B CG  1 
ATOM   1131 C CD  . ARG   B 1 16  ? -6.605  -28.168 -16.248 1.00 25.86 ? 33  ARG   B CD  1 
ATOM   1132 N NE  . ARG   B 1 16  ? -7.359  -28.897 -17.262 1.00 22.50 ? 33  ARG   B NE  1 
ATOM   1133 C CZ  . ARG   B 1 16  ? -6.841  -29.323 -18.399 1.00 25.83 ? 33  ARG   B CZ  1 
ATOM   1134 N NH1 . ARG   B 1 16  ? -5.601  -29.021 -18.744 1.00 27.05 ? 33  ARG   B NH1 1 
ATOM   1135 N NH2 . ARG   B 1 16  ? -7.588  -30.051 -19.218 1.00 27.14 ? 33  ARG   B NH2 1 
ATOM   1136 N N   . GLU   B 1 17  ? -9.766  -29.880 -11.274 1.00 20.84 ? 34  GLU   B N   1 
ATOM   1137 C CA  . GLU   B 1 17  ? -9.949  -30.935 -10.281 1.00 20.54 ? 34  GLU   B CA  1 
ATOM   1138 C C   . GLU   B 1 17  ? -10.670 -32.151 -10.868 1.00 21.16 ? 34  GLU   B C   1 
ATOM   1139 O O   . GLU   B 1 17  ? -10.331 -33.301 -10.553 1.00 21.73 ? 34  GLU   B O   1 
ATOM   1140 C CB  . GLU   B 1 17  ? -10.734 -30.378 -9.088  1.00 22.31 ? 34  GLU   B CB  1 
ATOM   1141 C CG  . GLU   B 1 17  ? -9.963  -29.426 -8.159  1.00 24.61 ? 34  GLU   B CG  1 
ATOM   1142 C CD  . GLU   B 1 17  ? -9.914  -27.975 -8.641  1.00 24.16 ? 34  GLU   B CD  1 
ATOM   1143 O OE1 . GLU   B 1 17  ? -10.241 -27.677 -9.806  1.00 21.55 ? 34  GLU   B OE1 1 
ATOM   1144 O OE2 . GLU   B 1 17  ? -9.568  -27.104 -7.820  1.00 30.91 ? 34  GLU   B OE2 1 
ATOM   1145 N N   . ASP   B 1 18  ? -11.661 -31.921 -11.735 1.00 18.82 ? 35  ASP   B N   1 
ATOM   1146 C CA  . ASP   B 1 18  ? -12.513 -32.978 -12.265 1.00 18.95 ? 35  ASP   B CA  1 
ATOM   1147 C C   . ASP   B 1 18  ? -12.094 -33.442 -13.656 1.00 19.48 ? 35  ASP   B C   1 
ATOM   1148 O O   . ASP   B 1 18  ? -12.892 -34.060 -14.366 1.00 19.39 ? 35  ASP   B O   1 
ATOM   1149 C CB  . ASP   B 1 18  ? -13.975 -32.516 -12.291 1.00 19.03 ? 35  ASP   B CB  1 
ATOM   1150 C CG  . ASP   B 1 18  ? -14.576 -32.364 -10.898 1.00 20.45 ? 35  ASP   B CG  1 
ATOM   1151 O OD1 . ASP   B 1 18  ? -14.028 -32.939 -9.944  1.00 21.96 ? 35  ASP   B OD1 1 
ATOM   1152 O OD2 . ASP   B 1 18  ? -15.615 -31.676 -10.751 1.00 20.14 ? 35  ASP   B OD2 1 
ATOM   1153 N N   . ARG   B 1 19  ? -10.849 -33.187 -14.043 1.00 22.27 ? 36  ARG   B N   1 
ATOM   1154 C CA  . ARG   B 1 19  ? -10.380 -33.533 -15.378 1.00 23.21 ? 36  ARG   B CA  1 
ATOM   1155 C C   . ARG   B 1 19  ? -10.580 -35.017 -15.721 1.00 24.33 ? 36  ARG   B C   1 
ATOM   1156 O O   . ARG   B 1 19  ? -11.022 -35.352 -16.828 1.00 24.12 ? 36  ARG   B O   1 
ATOM   1157 C CB  . ARG   B 1 19  ? -8.926  -33.096 -15.474 1.00 25.06 ? 36  ARG   B CB  1 
ATOM   1158 C CG  . ARG   B 1 19  ? -8.235  -33.439 -16.721 1.00 30.37 ? 36  ARG   B CG  1 
ATOM   1159 C CD  . ARG   B 1 19  ? -6.757  -33.151 -16.574 1.00 27.63 ? 36  ARG   B CD  1 
ATOM   1160 N NE  . ARG   B 1 19  ? -6.157  -32.997 -17.887 1.00 28.30 ? 36  ARG   B NE  1 
ATOM   1161 C CZ  . ARG   B 1 19  ? -5.000  -32.406 -18.115 1.00 29.64 ? 36  ARG   B CZ  1 
ATOM   1162 N NH1 . ARG   B 1 19  ? -4.311  -31.834 -17.137 1.00 31.04 ? 36  ARG   B NH1 1 
ATOM   1163 N NH2 . ARG   B 1 19  ? -4.523  -32.380 -19.355 1.00 33.26 ? 36  ARG   B NH2 1 
ATOM   1164 N N   . THR   B 1 20  ? -10.286 -35.926 -14.787 1.00 24.60 ? 37  THR   B N   1 
ATOM   1165 C CA  . THR   B 1 20  ? -10.460 -37.350 -15.082 1.00 24.89 ? 37  THR   B CA  1 
ATOM   1166 C C   . THR   B 1 20  ? -11.915 -37.689 -15.348 1.00 24.31 ? 37  THR   B C   1 
ATOM   1167 O O   . THR   B 1 20  ? -12.230 -38.496 -16.232 1.00 26.91 ? 37  THR   B O   1 
ATOM   1168 C CB  . THR   B 1 20  ? -9.926  -38.198 -13.934 1.00 26.94 ? 37  THR   B CB  1 
ATOM   1169 O OG1 . THR   B 1 20  ? -8.551  -37.876 -13.717 1.00 29.25 ? 37  THR   B OG1 1 
ATOM   1170 C CG2 . THR   B 1 20  ? -10.028 -39.682 -14.258 1.00 28.59 ? 37  THR   B CG2 1 
ATOM   1171 N N   . LEU   B 1 21  ? -12.816 -37.094 -14.581 1.00 24.90 ? 38  LEU   B N   1 
ATOM   1172 C CA  . LEU   B 1 21  ? -14.232 -37.356 -14.782 1.00 23.57 ? 38  LEU   B CA  1 
ATOM   1173 C C   . LEU   B 1 21  ? -14.702 -36.821 -16.129 1.00 25.41 ? 38  LEU   B C   1 
ATOM   1174 O O   . LEU   B 1 21  ? -15.527 -37.450 -16.800 1.00 26.60 ? 38  LEU   B O   1 
ATOM   1175 C CB  . LEU   B 1 21  ? -15.016 -36.729 -13.634 1.00 24.78 ? 38  LEU   B CB  1 
ATOM   1176 C CG  . LEU   B 1 21  ? -16.534 -36.777 -13.674 1.00 25.71 ? 38  LEU   B CG  1 
ATOM   1177 C CD1 . LEU   B 1 21  ? -17.107 -38.188 -13.584 1.00 28.71 ? 38  LEU   B CD1 1 
ATOM   1178 C CD2 . LEU   B 1 21  ? -17.051 -35.900 -12.545 1.00 28.52 ? 38  LEU   B CD2 1 
ATOM   1179 N N   . TYR   B 1 22  ? -14.194 -35.656 -16.537 1.00 22.64 ? 39  TYR   B N   1 
ATOM   1180 C CA  . TYR   B 1 22  ? -14.564 -35.094 -17.836 1.00 22.88 ? 39  TYR   B CA  1 
ATOM   1181 C C   . TYR   B 1 22  ? -14.189 -36.053 -18.959 1.00 23.90 ? 39  TYR   B C   1 
ATOM   1182 O O   . TYR   B 1 22  ? -14.950 -36.223 -19.919 1.00 24.51 ? 39  TYR   B O   1 
ATOM   1183 C CB  . TYR   B 1 22  ? -13.873 -33.742 -18.061 1.00 22.52 ? 39  TYR   B CB  1 
ATOM   1184 C CG  . TYR   B 1 22  ? -14.203 -32.653 -17.068 1.00 21.53 ? 39  TYR   B CG  1 
ATOM   1185 C CD1 . TYR   B 1 22  ? -15.300 -32.741 -16.225 1.00 20.80 ? 39  TYR   B CD1 1 
ATOM   1186 C CD2 . TYR   B 1 22  ? -13.364 -31.552 -16.946 1.00 21.56 ? 39  TYR   B CD2 1 
ATOM   1187 C CE1 . TYR   B 1 22  ? -15.581 -31.714 -15.315 1.00 20.98 ? 39  TYR   B CE1 1 
ATOM   1188 C CE2 . TYR   B 1 22  ? -13.621 -30.538 -16.039 1.00 20.82 ? 39  TYR   B CE2 1 
ATOM   1189 C CZ  . TYR   B 1 22  ? -14.720 -30.622 -15.229 1.00 20.04 ? 39  TYR   B CZ  1 
ATOM   1190 O OH  . TYR   B 1 22  ? -14.930 -29.607 -14.344 1.00 19.47 ? 39  TYR   B OH  1 
ATOM   1191 N N   . GLU   B 1 23  ? -13.017 -36.691 -18.847 1.00 24.65 ? 40  GLU   B N   1 
ATOM   1192 C CA  . GLU   B 1 23  ? -12.571 -37.656 -19.848 1.00 27.02 ? 40  GLU   B CA  1 
ATOM   1193 C C   . GLU   B 1 23  ? -13.539 -38.836 -19.927 1.00 30.35 ? 40  GLU   B C   1 
ATOM   1194 O O   . GLU   B 1 23  ? -13.853 -39.330 -21.017 1.00 29.26 ? 40  GLU   B O   1 
ATOM   1195 C CB  . GLU   B 1 23  ? -11.154 -38.112 -19.486 1.00 27.25 ? 40  GLU   B CB  1 
ATOM   1196 C CG  . GLU   B 1 23  ? -10.352 -38.864 -20.538 1.00 43.66 ? 40  GLU   B CG  1 
ATOM   1197 C CD  . GLU   B 1 23  ? -10.709 -38.494 -21.969 1.00 50.44 ? 40  GLU   B CD  1 
ATOM   1198 O OE1 . GLU   B 1 23  ? -10.585 -37.296 -22.317 1.00 47.35 ? 40  GLU   B OE1 1 
ATOM   1199 O OE2 . GLU   B 1 23  ? -11.071 -39.401 -22.755 1.00 51.00 ? 40  GLU   B OE2 1 
ATOM   1200 N N   . ARG   B 1 24  ? -14.053 -39.279 -18.780 1.00 27.22 ? 41  ARG   B N   1 
ATOM   1201 C CA  . ARG   B 1 24  ? -15.032 -40.364 -18.783 1.00 29.82 ? 41  ARG   B CA  1 
ATOM   1202 C C   . ARG   B 1 24  ? -16.319 -39.951 -19.483 1.00 28.27 ? 41  ARG   B C   1 
ATOM   1203 O O   . ARG   B 1 24  ? -16.916 -40.742 -20.223 1.00 31.17 ? 41  ARG   B O   1 
ATOM   1204 C CB  . ARG   B 1 24  ? -15.345 -40.804 -17.358 1.00 29.73 ? 41  ARG   B CB  1 
ATOM   1205 C CG  . ARG   B 1 24  ? -14.344 -41.758 -16.777 1.00 36.85 ? 41  ARG   B CG  1 
ATOM   1206 C CD  . ARG   B 1 24  ? -14.614 -41.970 -15.305 1.00 39.51 ? 41  ARG   B CD  1 
ATOM   1207 N NE  . ARG   B 1 24  ? -15.928 -42.557 -15.074 1.00 34.37 ? 41  ARG   B NE  1 
ATOM   1208 C CZ  . ARG   B 1 24  ? -16.587 -42.478 -13.927 1.00 34.32 ? 41  ARG   B CZ  1 
ATOM   1209 N NH1 . ARG   B 1 24  ? -16.101 -41.802 -12.898 1.00 39.12 ? 41  ARG   B NH1 1 
ATOM   1210 N NH2 . ARG   B 1 24  ? -17.762 -43.090 -13.808 1.00 35.74 ? 41  ARG   B NH2 1 
ATOM   1211 N N   . ILE   B 1 25  ? -16.773 -38.722 -19.239 1.00 26.56 ? 42  ILE   B N   1 
ATOM   1212 C CA  . ILE   B 1 25  ? -18.002 -38.242 -19.857 1.00 25.56 ? 42  ILE   B CA  1 
ATOM   1213 C C   . ILE   B 1 25  ? -17.828 -38.144 -21.368 1.00 28.14 ? 42  ILE   B C   1 
ATOM   1214 O O   . ILE   B 1 25  ? -18.686 -38.587 -22.139 1.00 27.14 ? 42  ILE   B O   1 
ATOM   1215 C CB  . ILE   B 1 25  ? -18.413 -36.890 -19.240 1.00 24.19 ? 42  ILE   B CB  1 
ATOM   1216 C CG1 . ILE   B 1 25  ? -18.818 -37.100 -17.787 1.00 23.20 ? 42  ILE   B CG1 1 
ATOM   1217 C CG2 . ILE   B 1 25  ? -19.572 -36.254 -20.020 1.00 25.61 ? 42  ILE   B CG2 1 
ATOM   1218 C CD1 . ILE   B 1 25  ? -18.884 -35.814 -16.968 1.00 23.28 ? 42  ILE   B CD1 1 
ATOM   1219 N N   . VAL   B 1 26  ? -16.725 -37.544 -21.814 1.00 26.74 ? 43  VAL   B N   1 
ATOM   1220 C CA  . VAL   B 1 26  ? -16.527 -37.353 -23.246 1.00 27.40 ? 43  VAL   B CA  1 
ATOM   1221 C C   . VAL   B 1 26  ? -16.401 -38.698 -23.940 1.00 30.26 ? 43  VAL   B C   1 
ATOM   1222 O O   . VAL   B 1 26  ? -16.939 -38.901 -25.036 1.00 30.24 ? 43  VAL   B O   1 
ATOM   1223 C CB  . VAL   B 1 26  ? -15.303 -36.456 -23.496 1.00 26.87 ? 43  VAL   B CB  1 
ATOM   1224 C CG1 . VAL   B 1 26  ? -14.923 -36.458 -24.971 1.00 30.75 ? 43  VAL   B CG1 1 
ATOM   1225 C CG2 . VAL   B 1 26  ? -15.604 -35.043 -23.011 1.00 28.53 ? 43  VAL   B CG2 1 
ATOM   1226 N N   . SER   B 1 27  ? -15.710 -39.644 -23.295 1.00 30.07 ? 44  SER   B N   1 
ATOM   1227 C CA  . SER   B 1 27  ? -15.614 -41.001 -23.820 1.00 30.57 ? 44  SER   B CA  1 
ATOM   1228 C C   . SER   B 1 27  ? -16.991 -41.609 -24.032 1.00 32.69 ? 44  SER   B C   1 
ATOM   1229 O O   . SER   B 1 27  ? -17.239 -42.266 -25.053 1.00 33.99 ? 44  SER   B O   1 
ATOM   1230 C CB  . SER   B 1 27  ? -14.793 -41.875 -22.866 1.00 32.36 ? 44  SER   B CB  1 
ATOM   1231 O OG  . SER   B 1 27  ? -13.423 -41.498 -22.851 1.00 38.28 ? 44  SER   B OG  1 
ATOM   1232 N N   . ARG   B 1 28  ? -17.904 -41.409 -23.078 1.00 30.71 ? 45  ARG   B N   1 
ATOM   1233 C CA  . ARG   B 1 28  ? -19.222 -42.004 -23.247 1.00 33.03 ? 45  ARG   B CA  1 
ATOM   1234 C C   . ARG   B 1 28  ? -20.031 -41.224 -24.280 1.00 34.17 ? 45  ARG   B C   1 
ATOM   1235 O O   . ARG   B 1 28  ? -20.774 -41.825 -25.062 1.00 35.31 ? 45  ARG   B O   1 
ATOM   1236 C CB  . ARG   B 1 28  ? -19.952 -42.090 -21.902 1.00 31.90 ? 45  ARG   B CB  1 
ATOM   1237 C CG  . ARG   B 1 28  ? -21.395 -42.582 -21.994 1.00 37.61 ? 45  ARG   B CG  1 
ATOM   1238 C CD  . ARG   B 1 28  ? -21.543 -44.054 -22.364 1.00 44.59 ? 45  ARG   B CD  1 
ATOM   1239 N NE  . ARG   B 1 28  ? -20.485 -44.918 -21.858 1.00 42.15 ? 45  ARG   B NE  1 
ATOM   1240 C CZ  . ARG   B 1 28  ? -20.706 -46.065 -21.222 1.00 47.65 ? 45  ARG   B CZ  1 
ATOM   1241 N NH1 . ARG   B 1 28  ? -21.931 -46.521 -21.021 1.00 50.74 ? 45  ARG   B NH1 1 
ATOM   1242 N NH2 . ARG   B 1 28  ? -19.673 -46.777 -20.783 1.00 44.50 ? 45  ARG   B NH2 1 
ATOM   1243 N N   . LEU   B 1 29  ? -19.863 -39.897 -24.338 1.00 29.69 ? 46  LEU   B N   1 
ATOM   1244 C CA  . LEU   B 1 29  ? -20.607 -39.106 -25.317 1.00 29.31 ? 46  LEU   B CA  1 
ATOM   1245 C C   . LEU   B 1 29  ? -20.270 -39.512 -26.751 1.00 30.89 ? 46  LEU   B C   1 
ATOM   1246 O O   . LEU   B 1 29  ? -21.137 -39.465 -27.631 1.00 32.83 ? 46  LEU   B O   1 
ATOM   1247 C CB  . LEU   B 1 29  ? -20.341 -37.611 -25.111 1.00 28.13 ? 46  LEU   B CB  1 
ATOM   1248 C CG  . LEU   B 1 29  ? -20.871 -37.009 -23.811 1.00 27.29 ? 46  LEU   B CG  1 
ATOM   1249 C CD1 . LEU   B 1 29  ? -20.502 -35.528 -23.699 1.00 25.95 ? 46  LEU   B CD1 1 
ATOM   1250 C CD2 . LEU   B 1 29  ? -22.380 -37.191 -23.672 1.00 27.60 ? 46  LEU   B CD2 1 
ATOM   1251 N N   . ARG   B 1 30  ? -19.023 -39.928 -27.007 1.00 33.95 ? 47  ARG   B N   1 
ATOM   1252 C CA  . ARG   B 1 30  ? -18.641 -40.296 -28.369 1.00 32.67 ? 47  ARG   B CA  1 
ATOM   1253 C C   . ARG   B 1 30  ? -19.444 -41.485 -28.870 1.00 35.59 ? 47  ARG   B C   1 
ATOM   1254 O O   . ARG   B 1 30  ? -19.634 -41.641 -30.083 1.00 38.85 ? 47  ARG   B O   1 
ATOM   1255 C CB  . ARG   B 1 30  ? -17.145 -40.609 -28.433 1.00 37.52 ? 47  ARG   B CB  1 
ATOM   1256 C CG  . ARG   B 1 30  ? -16.291 -39.369 -28.572 1.00 37.31 ? 47  ARG   B CG  1 
ATOM   1257 C CD  . ARG   B 1 30  ? -14.821 -39.697 -28.758 1.00 47.25 ? 47  ARG   B CD  1 
ATOM   1258 N NE  . ARG   B 1 30  ? -14.179 -40.033 -27.493 1.00 46.89 ? 47  ARG   B NE  1 
ATOM   1259 C CZ  . ARG   B 1 30  ? -13.166 -39.358 -26.966 1.00 47.42 ? 47  ARG   B CZ  1 
ATOM   1260 N NH1 . ARG   B 1 30  ? -12.723 -38.235 -27.512 1.00 51.20 ? 47  ARG   B NH1 1 
ATOM   1261 N NH2 . ARG   B 1 30  ? -12.594 -39.811 -25.854 1.00 46.46 ? 47  ARG   B NH2 1 
ATOM   1262 N N   . ARG   B 1 31  ? -19.917 -42.332 -27.951 1.00 38.03 ? 48  ARG   B N   1 
ATOM   1263 C CA  . ARG   B 1 31  ? -20.789 -43.443 -28.316 1.00 38.17 ? 48  ARG   B CA  1 
ATOM   1264 C C   . ARG   B 1 31  ? -22.084 -42.951 -28.959 1.00 35.96 ? 48  ARG   B C   1 
ATOM   1265 O O   . ARG   B 1 31  ? -22.703 -43.678 -29.745 1.00 39.25 ? 48  ARG   B O   1 
ATOM   1266 C CB  . ARG   B 1 31  ? -21.096 -44.271 -27.063 1.00 37.68 ? 48  ARG   B CB  1 
ATOM   1267 C CG  . ARG   B 1 31  ? -19.909 -45.036 -26.503 1.00 38.36 ? 48  ARG   B CG  1 
ATOM   1268 C CD  . ARG   B 1 31  ? -20.295 -46.456 -26.123 1.00 53.47 ? 48  ARG   B CD  1 
ATOM   1269 N NE  . ARG   B 1 31  ? -19.607 -46.940 -24.930 1.00 54.11 ? 48  ARG   B NE  1 
ATOM   1270 C CZ  . ARG   B 1 31  ? -20.109 -47.832 -24.087 1.00 53.63 ? 48  ARG   B CZ  1 
ATOM   1271 N NH1 . ARG   B 1 31  ? -21.367 -48.233 -24.175 1.00 51.68 ? 48  ARG   B NH1 1 
ATOM   1272 N NH2 . ARG   B 1 31  ? -19.330 -48.335 -23.132 1.00 56.04 ? 48  ARG   B NH2 1 
ATOM   1273 N N   . PHE   B 1 32  ? -22.514 -41.723 -28.638 1.00 36.02 ? 49  PHE   B N   1 
ATOM   1274 C CA  . PHE   B 1 32  ? -23.808 -41.234 -29.090 1.00 35.25 ? 49  PHE   B CA  1 
ATOM   1275 C C   . PHE   B 1 32  ? -23.741 -40.205 -30.209 1.00 40.17 ? 49  PHE   B C   1 
ATOM   1276 O O   . PHE   B 1 32  ? -24.746 -40.017 -30.900 1.00 42.35 ? 49  PHE   B O   1 
ATOM   1277 C CB  . PHE   B 1 32  ? -24.608 -40.632 -27.920 1.00 34.09 ? 49  PHE   B CB  1 
ATOM   1278 C CG  . PHE   B 1 32  ? -24.536 -41.436 -26.648 1.00 34.76 ? 49  PHE   B CG  1 
ATOM   1279 C CD1 . PHE   B 1 32  ? -25.118 -42.690 -26.577 1.00 40.03 ? 49  PHE   B CD1 1 
ATOM   1280 C CD2 . PHE   B 1 32  ? -23.962 -40.906 -25.502 1.00 40.69 ? 49  PHE   B CD2 1 
ATOM   1281 C CE1 . PHE   B 1 32  ? -25.074 -43.424 -25.412 1.00 41.62 ? 49  PHE   B CE1 1 
ATOM   1282 C CE2 . PHE   B 1 32  ? -23.923 -41.640 -24.328 1.00 39.76 ? 49  PHE   B CE2 1 
ATOM   1283 C CZ  . PHE   B 1 32  ? -24.479 -42.895 -24.287 1.00 35.62 ? 49  PHE   B CZ  1 
ATOM   1284 N N   . GLY   B 1 33  ? -22.617 -39.527 -30.406 1.00 34.81 ? 50  GLY   B N   1 
ATOM   1285 C CA  . GLY   B 1 33  ? -22.546 -38.602 -31.520 1.00 36.86 ? 50  GLY   B CA  1 
ATOM   1286 C C   . GLY   B 1 33  ? -21.182 -37.961 -31.650 1.00 36.85 ? 50  GLY   B C   1 
ATOM   1287 O O   . GLY   B 1 33  ? -20.234 -38.318 -30.949 1.00 38.12 ? 50  GLY   B O   1 
ATOM   1288 N N   . THR   B 1 34  ? -21.105 -37.011 -32.585 1.00 37.09 ? 51  THR   B N   1 
ATOM   1289 C CA  . THR   B 1 34  ? -19.891 -36.232 -32.821 1.00 35.38 ? 51  THR   B CA  1 
ATOM   1290 C C   . THR   B 1 34  ? -19.653 -35.276 -31.660 1.00 35.31 ? 51  THR   B C   1 
ATOM   1291 O O   . THR   B 1 34  ? -20.504 -34.434 -31.373 1.00 34.66 ? 51  THR   B O   1 
ATOM   1292 C CB  . THR   B 1 34  ? -20.027 -35.424 -34.109 1.00 36.79 ? 51  THR   B CB  1 
ATOM   1293 O OG1 . THR   B 1 34  ? -20.107 -36.296 -35.236 1.00 38.62 ? 51  THR   B OG1 1 
ATOM   1294 C CG2 . THR   B 1 34  ? -18.845 -34.483 -34.278 1.00 39.86 ? 51  THR   B CG2 1 
ATOM   1295 N N   . VAL   B 1 35  ? -18.494 -35.368 -31.015 1.00 32.92 ? 52  VAL   B N   1 
ATOM   1296 C CA  . VAL   B 1 35  ? -18.139 -34.443 -29.942 1.00 32.37 ? 52  VAL   B CA  1 
ATOM   1297 C C   . VAL   B 1 35  ? -17.265 -33.344 -30.539 1.00 36.27 ? 52  VAL   B C   1 
ATOM   1298 O O   . VAL   B 1 35  ? -16.100 -33.575 -30.878 1.00 38.93 ? 52  VAL   B O   1 
ATOM   1299 C CB  . VAL   B 1 35  ? -17.436 -35.157 -28.782 1.00 32.28 ? 52  VAL   B CB  1 
ATOM   1300 C CG1 . VAL   B 1 35  ? -17.184 -34.174 -27.641 1.00 34.71 ? 52  VAL   B CG1 1 
ATOM   1301 C CG2 . VAL   B 1 35  ? -18.283 -36.320 -28.297 1.00 35.09 ? 52  VAL   B CG2 1 
ATOM   1302 N N   . LEU   B 1 36  ? -17.823 -32.141 -30.665 1.00 33.86 ? 53  LEU   B N   1 
ATOM   1303 C CA  . LEU   B 1 36  ? -17.137 -31.048 -31.349 1.00 32.85 ? 53  LEU   B CA  1 
ATOM   1304 C C   . LEU   B 1 36  ? -15.971 -30.468 -30.537 1.00 32.68 ? 53  LEU   B C   1 
ATOM   1305 O O   . LEU   B 1 36  ? -16.001 -30.445 -29.305 1.00 39.27 ? 53  LEU   B O   1 
ATOM   1306 C CB  . LEU   B 1 36  ? -18.140 -29.940 -31.702 1.00 33.45 ? 53  LEU   B CB  1 
ATOM   1307 C CG  . LEU   B 1 36  ? -19.480 -30.400 -32.292 1.00 34.41 ? 53  LEU   B CG  1 
ATOM   1308 C CD1 . LEU   B 1 36  ? -20.618 -29.452 -31.925 1.00 33.22 ? 53  LEU   B CD1 1 
ATOM   1309 C CD2 . LEU   B 1 36  ? -19.380 -30.554 -33.807 1.00 37.76 ? 53  LEU   B CD2 1 
ATOM   1310 N N   . GLY   B 1 54  ? -7.161  -13.854 -32.520 1.00 78.78 ? 71  GLY   B N   1 
ATOM   1311 C CA  . GLY   B 1 54  ? -6.009  -14.563 -31.990 1.00 78.65 ? 71  GLY   B CA  1 
ATOM   1312 C C   . GLY   B 1 54  ? -6.059  -14.868 -30.502 1.00 70.50 ? 71  GLY   B C   1 
ATOM   1313 O O   . GLY   B 1 54  ? -6.680  -14.135 -29.724 1.00 73.06 ? 71  GLY   B O   1 
ATOM   1314 N N   . GLY   B 1 55  ? -5.402  -15.960 -30.111 1.00 54.72 ? 72  GLY   B N   1 
ATOM   1315 C CA  . GLY   B 1 55  ? -5.255  -16.271 -28.694 1.00 49.41 ? 72  GLY   B CA  1 
ATOM   1316 C C   . GLY   B 1 55  ? -6.572  -16.694 -28.074 1.00 44.71 ? 72  GLY   B C   1 
ATOM   1317 O O   . GLY   B 1 55  ? -7.259  -17.595 -28.568 1.00 43.56 ? 72  GLY   B O   1 
ATOM   1318 N N   . ASP   B 1 56  ? -6.932  -16.046 -26.961 1.00 36.73 ? 73  ASP   B N   1 
ATOM   1319 C CA  . ASP   B 1 56  ? -8.221  -16.339 -26.342 1.00 32.16 ? 73  ASP   B CA  1 
ATOM   1320 C C   . ASP   B 1 56  ? -9.378  -15.950 -27.251 1.00 33.00 ? 73  ASP   B C   1 
ATOM   1321 O O   . ASP   B 1 56  ? -10.440 -16.575 -27.198 1.00 28.27 ? 73  ASP   B O   1 
ATOM   1322 C CB  . ASP   B 1 56  ? -8.341  -15.640 -24.986 1.00 30.48 ? 73  ASP   B CB  1 
ATOM   1323 C CG  . ASP   B 1 56  ? -7.541  -16.343 -23.898 1.00 30.56 ? 73  ASP   B CG  1 
ATOM   1324 O OD1 . ASP   B 1 56  ? -6.956  -17.409 -24.197 1.00 35.87 ? 73  ASP   B OD1 1 
ATOM   1325 O OD2 . ASP   B 1 56  ? -7.522  -15.860 -22.747 1.00 32.23 ? 73  ASP   B OD2 1 
ATOM   1326 N N   . ARG   B 1 57  ? -9.198  -14.935 -28.099 1.00 31.66 ? 74  ARG   B N   1 
ATOM   1327 C CA  . ARG   B 1 57  ? -10.256 -14.609 -29.048 1.00 32.50 ? 74  ARG   B CA  1 
ATOM   1328 C C   . ARG   B 1 57  ? -10.514 -15.761 -30.007 1.00 33.06 ? 74  ARG   B C   1 
ATOM   1329 O O   . ARG   B 1 57  ? -11.673 -16.072 -30.304 1.00 32.16 ? 74  ARG   B O   1 
ATOM   1330 C CB  . ARG   B 1 57  ? -9.937  -13.317 -29.807 1.00 36.98 ? 74  ARG   B CB  1 
ATOM   1331 C CG  . ARG   B 1 57  ? -10.797 -13.141 -31.054 1.00 42.67 ? 74  ARG   B CG  1 
ATOM   1332 C CD  . ARG   B 1 57  ? -12.210 -12.593 -30.790 1.00 39.04 ? 74  ARG   B CD  1 
ATOM   1333 N NE  . ARG   B 1 57  ? -12.760 -11.709 -31.825 1.00 45.12 ? 74  ARG   B NE  1 
ATOM   1334 C CZ  . ARG   B 1 57  ? -12.816 -11.943 -33.138 1.00 46.62 ? 74  ARG   B CZ  1 
ATOM   1335 N NH1 . ARG   B 1 57  ? -12.176 -12.956 -33.707 1.00 46.79 ? 74  ARG   B NH1 1 
ATOM   1336 N NH2 . ARG   B 1 57  ? -13.526 -11.126 -33.910 1.00 47.93 ? 74  ARG   B NH2 1 
ATOM   1337 N N   . LEU   B 1 58  ? -9.452  -16.416 -30.491 1.00 34.68 ? 75  LEU   B N   1 
ATOM   1338 C CA  . LEU   B 1 58  ? -9.636  -17.555 -31.387 1.00 35.78 ? 75  LEU   B CA  1 
ATOM   1339 C C   . LEU   B 1 58  ? -10.375 -18.693 -30.691 1.00 33.48 ? 75  LEU   B C   1 
ATOM   1340 O O   . LEU   B 1 58  ? -11.237 -19.341 -31.298 1.00 33.62 ? 75  LEU   B O   1 
ATOM   1341 C CB  . LEU   B 1 58  ? -8.286  -18.041 -31.912 1.00 38.36 ? 75  LEU   B CB  1 
ATOM   1342 C CG  . LEU   B 1 58  ? -8.326  -19.185 -32.933 1.00 43.14 ? 75  LEU   B CG  1 
ATOM   1343 C CD1 . LEU   B 1 58  ? -9.433  -18.995 -33.969 1.00 43.50 ? 75  LEU   B CD1 1 
ATOM   1344 C CD2 . LEU   B 1 58  ? -6.978  -19.365 -33.601 1.00 43.60 ? 75  LEU   B CD2 1 
ATOM   1345 N N   . ILE   B 1 59  ? -10.050 -18.955 -29.419 1.00 31.62 ? 76  ILE   B N   1 
ATOM   1346 C CA  . ILE   B 1 59  ? -10.778 -19.972 -28.659 1.00 29.61 ? 76  ILE   B CA  1 
ATOM   1347 C C   . ILE   B 1 59  ? -12.247 -19.603 -28.555 1.00 28.14 ? 76  ILE   B C   1 
ATOM   1348 O O   . ILE   B 1 59  ? -13.132 -20.424 -28.817 1.00 27.62 ? 76  ILE   B O   1 
ATOM   1349 C CB  . ILE   B 1 59  ? -10.163 -20.161 -27.262 1.00 28.20 ? 76  ILE   B CB  1 
ATOM   1350 C CG1 . ILE   B 1 59  ? -8.750  -20.726 -27.357 1.00 30.20 ? 76  ILE   B CG1 1 
ATOM   1351 C CG2 . ILE   B 1 59  ? -11.066 -21.038 -26.381 1.00 27.93 ? 76  ILE   B CG2 1 
ATOM   1352 C CD1 . ILE   B 1 59  ? -7.921  -20.438 -26.140 1.00 34.38 ? 76  ILE   B CD1 1 
ATOM   1353 N N   . HIS   B 1 60  ? -12.529 -18.363 -28.160 1.00 27.23 ? 77  HIS   B N   1 
ATOM   1354 C CA  . HIS   B 1 60  ? -13.920 -17.948 -28.021 1.00 25.98 ? 77  HIS   B CA  1 
ATOM   1355 C C   . HIS   B 1 60  ? -14.663 -18.067 -29.343 1.00 27.44 ? 77  HIS   B C   1 
ATOM   1356 O O   . HIS   B 1 60  ? -15.786 -18.579 -29.387 1.00 26.67 ? 77  HIS   B O   1 
ATOM   1357 C CB  . HIS   B 1 60  ? -13.982 -16.519 -27.489 1.00 25.64 ? 77  HIS   B CB  1 
ATOM   1358 C CG  . HIS   B 1 60  ? -15.363 -15.949 -27.438 1.00 24.94 ? 77  HIS   B CG  1 
ATOM   1359 N ND1 . HIS   B 1 60  ? -15.950 -15.317 -28.511 1.00 26.50 ? 77  HIS   B ND1 1 
ATOM   1360 C CD2 . HIS   B 1 60  ? -16.284 -15.944 -26.447 1.00 23.15 ? 77  HIS   B CD2 1 
ATOM   1361 C CE1 . HIS   B 1 60  ? -17.169 -14.929 -28.178 1.00 25.68 ? 77  HIS   B CE1 1 
ATOM   1362 N NE2 . HIS   B 1 60  ? -17.394 -15.295 -26.928 1.00 23.65 ? 77  HIS   B NE2 1 
ATOM   1363 N N   . GLU   B 1 61  ? -14.045 -17.616 -30.432 1.00 29.81 ? 78  GLU   B N   1 
ATOM   1364 C CA  . GLU   B 1 61  ? -14.718 -17.648 -31.725 1.00 31.61 ? 78  GLU   B CA  1 
ATOM   1365 C C   . GLU   B 1 61  ? -14.900 -19.078 -32.215 1.00 32.11 ? 78  GLU   B C   1 
ATOM   1366 O O   . GLU   B 1 61  ? -15.989 -19.448 -32.669 1.00 32.20 ? 78  GLU   B O   1 
ATOM   1367 C CB  . GLU   B 1 61  ? -13.937 -16.813 -32.734 1.00 34.41 ? 78  GLU   B CB  1 
ATOM   1368 C CG  . GLU   B 1 61  ? -13.940 -15.324 -32.393 1.00 36.84 ? 78  GLU   B CG  1 
ATOM   1369 C CD  . GLU   B 1 61  ? -15.341 -14.733 -32.298 1.00 38.37 ? 78  GLU   B CD  1 
ATOM   1370 O OE1 . GLU   B 1 61  ? -16.018 -14.633 -33.347 1.00 41.74 ? 78  GLU   B OE1 1 
ATOM   1371 O OE2 . GLU   B 1 61  ? -15.773 -14.390 -31.174 1.00 34.33 ? 78  GLU   B OE2 1 
ATOM   1372 N N   . GLN   B 1 62  ? -13.840 -19.894 -32.135 1.00 32.74 ? 79  GLN   B N   1 
ATOM   1373 C CA  . GLN   B 1 62  ? -13.943 -21.316 -32.473 1.00 33.43 ? 79  GLN   B CA  1 
ATOM   1374 C C   . GLN   B 1 62  ? -15.051 -22.005 -31.684 1.00 31.19 ? 79  GLN   B C   1 
ATOM   1375 O O   . GLN   B 1 62  ? -15.916 -22.678 -32.253 1.00 31.82 ? 79  GLN   B O   1 
ATOM   1376 C CB  . GLN   B 1 62  ? -12.605 -22.018 -32.203 1.00 34.29 ? 79  GLN   B CB  1 
ATOM   1377 C CG  . GLN   B 1 62  ? -12.541 -23.484 -32.648 1.00 41.91 ? 79  GLN   B CG  1 
ATOM   1378 C CD  . GLN   B 1 62  ? -13.035 -23.729 -34.067 1.00 49.44 ? 79  GLN   B CD  1 
ATOM   1379 O OE1 . GLN   B 1 62  ? -12.396 -23.329 -35.042 1.00 53.21 ? 79  GLN   B OE1 1 
ATOM   1380 N NE2 . GLN   B 1 62  ? -14.213 -24.338 -34.189 1.00 47.68 ? 79  GLN   B NE2 1 
ATOM   1381 N N   . ASP   B 1 63  ? -15.028 -21.864 -30.358 1.00 28.84 ? 80  ASP   B N   1 
ATOM   1382 C CA  . ASP   B 1 63  ? -15.986 -22.598 -29.542 1.00 28.16 ? 80  ASP   B CA  1 
ATOM   1383 C C   . ASP   B 1 63  ? -17.399 -22.061 -29.725 1.00 26.36 ? 80  ASP   B C   1 
ATOM   1384 O O   . ASP   B 1 63  ? -18.361 -22.833 -29.672 1.00 27.02 ? 80  ASP   B O   1 
ATOM   1385 C CB  . ASP   B 1 63  ? -15.564 -22.563 -28.070 1.00 29.29 ? 80  ASP   B CB  1 
ATOM   1386 C CG  . ASP   B 1 63  ? -14.559 -23.661 -27.721 1.00 35.49 ? 80  ASP   B CG  1 
ATOM   1387 O OD1 . ASP   B 1 63  ? -14.973 -24.829 -27.569 1.00 37.25 ? 80  ASP   B OD1 1 
ATOM   1388 O OD2 . ASP   B 1 63  ? -13.350 -23.363 -27.592 1.00 37.99 ? 80  ASP   B OD2 1 
ATOM   1389 N N   . LEU   B 1 64  ? -17.543 -20.754 -29.976 1.00 26.51 ? 81  LEU   B N   1 
ATOM   1390 C CA  . LEU   B 1 64  ? -18.863 -20.205 -30.265 1.00 26.68 ? 81  LEU   B CA  1 
ATOM   1391 C C   . LEU   B 1 64  ? -19.418 -20.749 -31.575 1.00 28.56 ? 81  LEU   B C   1 
ATOM   1392 O O   . LEU   B 1 64  ? -20.634 -20.940 -31.704 1.00 28.31 ? 81  LEU   B O   1 
ATOM   1393 C CB  . LEU   B 1 64  ? -18.800 -18.675 -30.305 1.00 26.69 ? 81  LEU   B CB  1 
ATOM   1394 C CG  . LEU   B 1 64  ? -20.118 -17.938 -30.074 1.00 29.84 ? 81  LEU   B CG  1 
ATOM   1395 C CD1 . LEU   B 1 64  ? -20.506 -18.020 -28.617 1.00 26.58 ? 81  LEU   B CD1 1 
ATOM   1396 C CD2 . LEU   B 1 64  ? -20.063 -16.477 -30.559 1.00 29.90 ? 81  LEU   B CD2 1 
ATOM   1397 N N   . GLU   B 1 65  ? -18.549 -21.005 -32.554 1.00 30.58 ? 82  GLU   B N   1 
ATOM   1398 C CA  . GLU   B 1 65  ? -18.991 -21.647 -33.788 1.00 32.87 ? 82  GLU   B CA  1 
ATOM   1399 C C   . GLU   B 1 65  ? -19.457 -23.072 -33.532 1.00 32.48 ? 82  GLU   B C   1 
ATOM   1400 O O   . GLU   B 1 65  ? -20.522 -23.475 -34.009 1.00 33.18 ? 82  GLU   B O   1 
ATOM   1401 C CB  . GLU   B 1 65  ? -17.868 -21.625 -34.822 1.00 37.36 ? 82  GLU   B CB  1 
ATOM   1402 C CG  . GLU   B 1 65  ? -17.538 -20.233 -35.327 1.00 43.45 ? 82  GLU   B CG  1 
ATOM   1403 C CD  . GLU   B 1 65  ? -16.605 -20.246 -36.523 1.00 51.17 ? 82  GLU   B CD  1 
ATOM   1404 O OE1 . GLU   B 1 65  ? -16.930 -20.902 -37.537 1.00 53.45 ? 82  GLU   B OE1 1 
ATOM   1405 O OE2 . GLU   B 1 65  ? -15.547 -19.581 -36.445 1.00 55.73 ? 82  GLU   B OE2 1 
ATOM   1406 N N   . TRP   B 1 66  ? -18.659 -23.864 -32.804 1.00 31.70 ? 83  TRP   B N   1 
ATOM   1407 C CA  . TRP   B 1 66  ? -19.098 -25.218 -32.460 1.00 31.59 ? 83  TRP   B CA  1 
ATOM   1408 C C   . TRP   B 1 66  ? -20.392 -25.197 -31.672 1.00 29.58 ? 83  TRP   B C   1 
ATOM   1409 O O   . TRP   B 1 66  ? -21.256 -26.060 -31.854 1.00 30.18 ? 83  TRP   B O   1 
ATOM   1410 C CB  . TRP   B 1 66  ? -18.044 -25.976 -31.648 1.00 31.05 ? 83  TRP   B CB  1 
ATOM   1411 C CG  . TRP   B 1 66  ? -16.757 -26.350 -32.331 1.00 33.86 ? 83  TRP   B CG  1 
ATOM   1412 C CD1 . TRP   B 1 66  ? -16.573 -26.671 -33.650 1.00 39.11 ? 83  TRP   B CD1 1 
ATOM   1413 C CD2 . TRP   B 1 66  ? -15.480 -26.509 -31.698 1.00 37.24 ? 83  TRP   B CD2 1 
ATOM   1414 N NE1 . TRP   B 1 66  ? -15.255 -26.999 -33.873 1.00 41.95 ? 83  TRP   B NE1 1 
ATOM   1415 C CE2 . TRP   B 1 66  ? -14.564 -26.897 -32.692 1.00 42.87 ? 83  TRP   B CE2 1 
ATOM   1416 C CE3 . TRP   B 1 66  ? -15.020 -26.338 -30.385 1.00 39.61 ? 83  TRP   B CE3 1 
ATOM   1417 C CZ2 . TRP   B 1 66  ? -13.214 -27.122 -32.416 1.00 45.23 ? 83  TRP   B CZ2 1 
ATOM   1418 C CZ3 . TRP   B 1 66  ? -13.679 -26.563 -30.115 1.00 37.85 ? 83  TRP   B CZ3 1 
ATOM   1419 C CH2 . TRP   B 1 66  ? -12.795 -26.952 -31.124 1.00 44.42 ? 83  TRP   B CH2 1 
ATOM   1420 N N   . LEU   B 1 67  ? -20.535 -24.244 -30.758 1.00 27.50 ? 84  LEU   B N   1 
ATOM   1421 C CA  . LEU   B 1 67  ? -21.699 -24.313 -29.894 1.00 25.88 ? 84  LEU   B CA  1 
ATOM   1422 C C   . LEU   B 1 67  ? -22.954 -24.004 -30.701 1.00 27.85 ? 84  LEU   B C   1 
ATOM   1423 O O   . LEU   B 1 67  ? -24.001 -24.623 -30.487 1.00 27.97 ? 84  LEU   B O   1 
ATOM   1424 C CB  . LEU   B 1 67  ? -21.487 -23.383 -28.697 1.00 25.56 ? 84  LEU   B CB  1 
ATOM   1425 C CG  . LEU   B 1 67  ? -22.614 -23.039 -27.753 1.00 27.23 ? 84  LEU   B CG  1 
ATOM   1426 C CD1 . LEU   B 1 67  ? -22.602 -24.167 -26.764 1.00 26.79 ? 84  LEU   B CD1 1 
ATOM   1427 C CD2 . LEU   B 1 67  ? -22.266 -21.761 -27.016 1.00 26.36 ? 84  LEU   B CD2 1 
ATOM   1428 N N   . GLN   B 1 68  ? -22.831 -23.120 -31.694 1.00 28.28 ? 85  GLN   B N   1 
ATOM   1429 C CA  . GLN   B 1 68  ? -23.915 -22.879 -32.643 1.00 29.87 ? 85  GLN   B CA  1 
ATOM   1430 C C   . GLN   B 1 68  ? -24.207 -24.103 -33.510 1.00 31.85 ? 85  GLN   B C   1 
ATOM   1431 O O   . GLN   B 1 68  ? -25.333 -24.256 -34.001 1.00 33.88 ? 85  GLN   B O   1 
ATOM   1432 C CB  . GLN   B 1 68  ? -23.567 -21.691 -33.538 1.00 32.15 ? 85  GLN   B CB  1 
ATOM   1433 C CG  . GLN   B 1 68  ? -24.145 -20.386 -33.074 1.00 35.71 ? 85  GLN   B CG  1 
ATOM   1434 C CD  . GLN   B 1 68  ? -23.586 -19.214 -33.847 1.00 36.84 ? 85  GLN   B CD  1 
ATOM   1435 O OE1 . GLN   B 1 68  ? -24.315 -18.515 -34.549 1.00 41.98 ? 85  GLN   B OE1 1 
ATOM   1436 N NE2 . GLN   B 1 68  ? -22.285 -18.992 -33.724 1.00 40.95 ? 85  GLN   B NE2 1 
ATOM   1437 N N   . GLN   B 1 69  ? -23.211 -24.966 -33.728 1.00 32.68 ? 86  GLN   B N   1 
ATOM   1438 C CA  . GLN   B 1 69  ? -23.372 -26.171 -34.537 1.00 34.95 ? 86  GLN   B CA  1 
ATOM   1439 C C   . GLN   B 1 69  ? -23.907 -27.352 -33.746 1.00 34.16 ? 86  GLN   B C   1 
ATOM   1440 O O   . GLN   B 1 69  ? -24.148 -28.409 -34.341 1.00 36.19 ? 86  GLN   B O   1 
ATOM   1441 C CB  . GLN   B 1 69  ? -22.036 -26.608 -35.141 1.00 37.38 ? 86  GLN   B CB  1 
ATOM   1442 C CG  . GLN   B 1 69  ? -21.656 -25.984 -36.453 1.00 44.24 ? 86  GLN   B CG  1 
ATOM   1443 C CD  . GLN   B 1 69  ? -20.166 -26.146 -36.734 1.00 55.25 ? 86  GLN   B CD  1 
ATOM   1444 O OE1 . GLN   B 1 69  ? -19.496 -25.204 -37.151 1.00 56.78 ? 86  GLN   B OE1 1 
ATOM   1445 N NE2 . GLN   B 1 69  ? -19.646 -27.354 -36.507 1.00 58.82 ? 86  GLN   B NE2 1 
ATOM   1446 N N   . ALA   B 1 70  ? -24.052 -27.218 -32.432 1.00 30.72 ? 87  ALA   B N   1 
ATOM   1447 C CA  . ALA   B 1 70  ? -24.359 -28.358 -31.584 1.00 29.49 ? 87  ALA   B CA  1 
ATOM   1448 C C   . ALA   B 1 70  ? -25.846 -28.681 -31.604 1.00 32.87 ? 87  ALA   B C   1 
ATOM   1449 O O   . ALA   B 1 70  ? -26.692 -27.808 -31.823 1.00 31.29 ? 87  ALA   B O   1 
ATOM   1450 C CB  . ALA   B 1 70  ? -23.911 -28.098 -30.144 1.00 28.28 ? 87  ALA   B CB  1 
ATOM   1451 N N   . ASP   B 1 71  ? -26.152 -29.963 -31.401 1.00 29.33 ? 88  ASP   B N   1 
ATOM   1452 C CA  . ASP   B 1 71  ? -27.517 -30.399 -31.129 1.00 31.05 ? 88  ASP   B CA  1 
ATOM   1453 C C   . ASP   B 1 71  ? -27.788 -30.509 -29.636 1.00 32.00 ? 88  ASP   B C   1 
ATOM   1454 O O   . ASP   B 1 71  ? -28.898 -30.193 -29.186 1.00 33.69 ? 88  ASP   B O   1 
ATOM   1455 C CB  . ASP   B 1 71  ? -27.811 -31.746 -31.795 1.00 31.88 ? 88  ASP   B CB  1 
ATOM   1456 C CG  . ASP   B 1 71  ? -27.644 -31.705 -33.299 1.00 35.23 ? 88  ASP   B CG  1 
ATOM   1457 O OD1 . ASP   B 1 71  ? -28.221 -30.804 -33.941 1.00 37.57 ? 88  ASP   B OD1 1 
ATOM   1458 O OD2 . ASP   B 1 71  ? -26.976 -32.606 -33.845 1.00 37.74 ? 88  ASP   B OD2 1 
ATOM   1459 N N   . VAL   B 1 72  ? -26.802 -30.952 -28.856 1.00 25.04 ? 89  VAL   B N   1 
ATOM   1460 C CA  . VAL   B 1 72  ? -26.919 -31.047 -27.408 1.00 25.00 ? 89  VAL   B CA  1 
ATOM   1461 C C   . VAL   B 1 72  ? -25.650 -30.478 -26.782 1.00 22.96 ? 89  VAL   B C   1 
ATOM   1462 O O   . VAL   B 1 72  ? -24.539 -30.755 -27.247 1.00 21.26 ? 89  VAL   B O   1 
ATOM   1463 C CB  . VAL   B 1 72  ? -27.148 -32.496 -26.936 1.00 26.55 ? 89  VAL   B CB  1 
ATOM   1464 C CG1 . VAL   B 1 72  ? -27.346 -32.538 -25.436 1.00 26.26 ? 89  VAL   B CG1 1 
ATOM   1465 C CG2 . VAL   B 1 72  ? -28.334 -33.121 -27.651 1.00 29.27 ? 89  VAL   B CG2 1 
ATOM   1466 N N   . VAL   B 1 73  ? -25.823 -29.691 -25.722 1.00 20.29 ? 90  VAL   B N   1 
ATOM   1467 C CA  . VAL   B 1 73  ? -24.736 -29.184 -24.893 1.00 19.68 ? 90  VAL   B CA  1 
ATOM   1468 C C   . VAL   B 1 73  ? -24.784 -29.916 -23.560 1.00 18.31 ? 90  VAL   B C   1 
ATOM   1469 O O   . VAL   B 1 73  ? -25.819 -29.915 -22.881 1.00 22.14 ? 90  VAL   B O   1 
ATOM   1470 C CB  . VAL   B 1 73  ? -24.862 -27.664 -24.684 1.00 18.40 ? 90  VAL   B CB  1 
ATOM   1471 C CG1 . VAL   B 1 73  ? -23.776 -27.151 -23.726 1.00 19.21 ? 90  VAL   B CG1 1 
ATOM   1472 C CG2 . VAL   B 1 73  ? -24.786 -26.960 -26.028 1.00 20.97 ? 90  VAL   B CG2 1 
ATOM   1473 N N   . VAL   B 1 74  ? -23.673 -30.537 -23.185 1.00 18.77 ? 91  VAL   B N   1 
ATOM   1474 C CA  . VAL   B 1 74  ? -23.562 -31.292 -21.945 1.00 17.79 ? 91  VAL   B CA  1 
ATOM   1475 C C   . VAL   B 1 74  ? -22.511 -30.609 -21.087 1.00 18.12 ? 91  VAL   B C   1 
ATOM   1476 O O   . VAL   B 1 74  ? -21.360 -30.461 -21.519 1.00 18.84 ? 91  VAL   B O   1 
ATOM   1477 C CB  . VAL   B 1 74  ? -23.175 -32.757 -22.208 1.00 20.02 ? 91  VAL   B CB  1 
ATOM   1478 C CG1 . VAL   B 1 74  ? -23.026 -33.529 -20.897 1.00 19.87 ? 91  VAL   B CG1 1 
ATOM   1479 C CG2 . VAL   B 1 74  ? -24.190 -33.425 -23.135 1.00 19.96 ? 91  VAL   B CG2 1 
ATOM   1480 N N   . ALA   B 1 75  ? -22.879 -30.246 -19.862 1.00 15.97 ? 92  ALA   B N   1 
ATOM   1481 C CA  . ALA   B 1 75  ? -21.958 -29.524 -18.991 1.00 15.54 ? 92  ALA   B CA  1 
ATOM   1482 C C   . ALA   B 1 75  ? -21.848 -30.215 -17.644 1.00 15.64 ? 92  ALA   B C   1 
ATOM   1483 O O   . ALA   B 1 75  ? -22.858 -30.539 -17.019 1.00 17.76 ? 92  ALA   B O   1 
ATOM   1484 C CB  . ALA   B 1 75  ? -22.412 -28.074 -18.790 1.00 15.32 ? 92  ALA   B CB  1 
ATOM   1485 N N   . GLU   B 1 76  ? -20.624 -30.440 -17.196 1.00 15.02 ? 93  GLU   B N   1 
ATOM   1486 C CA  . GLU   B 1 76  ? -20.391 -30.886 -15.830 1.00 14.93 ? 93  GLU   B CA  1 
ATOM   1487 C C   . GLU   B 1 76  ? -20.156 -29.630 -15.004 1.00 15.79 ? 93  GLU   B C   1 
ATOM   1488 O O   . GLU   B 1 76  ? -19.159 -28.920 -15.213 1.00 17.00 ? 93  GLU   B O   1 
ATOM   1489 C CB  . GLU   B 1 76  ? -19.216 -31.856 -15.757 1.00 16.35 ? 93  GLU   B CB  1 
ATOM   1490 C CG  . GLU   B 1 76  ? -19.378 -32.959 -14.707 1.00 17.22 ? 93  GLU   B CG  1 
ATOM   1491 C CD  . GLU   B 1 76  ? -19.368 -32.457 -13.261 1.00 18.51 ? 93  GLU   B CD  1 
ATOM   1492 O OE1 . GLU   B 1 76  ? -18.990 -31.300 -13.021 1.00 16.71 ? 93  GLU   B OE1 1 
ATOM   1493 O OE2 . GLU   B 1 76  ? -19.713 -33.240 -12.360 1.00 18.04 ? 93  GLU   B OE2 1 
ATOM   1494 N N   . VAL   B 1 77  ? -21.087 -29.335 -14.098 1.00 14.82 ? 94  VAL   B N   1 
ATOM   1495 C CA  . VAL   B 1 77  ? -21.172 -28.021 -13.463 1.00 14.50 ? 94  VAL   B CA  1 
ATOM   1496 C C   . VAL   B 1 77  ? -20.771 -28.059 -11.989 1.00 15.45 ? 94  VAL   B C   1 
ATOM   1497 O O   . VAL   B 1 77  ? -21.107 -27.148 -11.235 1.00 16.01 ? 94  VAL   B O   1 
ATOM   1498 C CB  . VAL   B 1 77  ? -22.571 -27.406 -13.633 1.00 13.40 ? 94  VAL   B CB  1 
ATOM   1499 C CG1 . VAL   B 1 77  ? -22.830 -27.092 -15.104 1.00 14.61 ? 94  VAL   B CG1 1 
ATOM   1500 C CG2 . VAL   B 1 77  ? -23.679 -28.315 -13.041 1.00 14.80 ? 94  VAL   B CG2 1 
ATOM   1501 N N   . THR   B 1 78  ? -20.024 -29.072 -11.563 1.00 14.54 ? 95  THR   B N   1 
ATOM   1502 C CA  . THR   B 1 78  ? -19.648 -29.155 -10.155 1.00 13.75 ? 95  THR   B CA  1 
ATOM   1503 C C   . THR   B 1 78  ? -18.574 -28.133 -9.785  1.00 14.70 ? 95  THR   B C   1 
ATOM   1504 O O   . THR   B 1 78  ? -18.665 -27.486 -8.734  1.00 14.66 ? 95  THR   B O   1 
ATOM   1505 C CB  . THR   B 1 78  ? -19.187 -30.575 -9.843  1.00 14.29 ? 95  THR   B CB  1 
ATOM   1506 O OG1 . THR   B 1 78  ? -20.264 -31.456 -10.186 1.00 16.16 ? 95  THR   B OG1 1 
ATOM   1507 C CG2 . THR   B 1 78  ? -18.864 -30.730 -8.378  1.00 16.14 ? 95  THR   B CG2 1 
ATOM   1508 N N   . GLN   B 1 79  ? -17.540 -27.990 -10.612 1.00 14.66 ? 96  GLN   B N   1 
ATOM   1509 C CA  . GLN   B 1 79  ? -16.468 -27.021 -10.357 1.00 14.25 ? 96  GLN   B CA  1 
ATOM   1510 C C   . GLN   B 1 79  ? -16.868 -25.653 -10.893 1.00 14.36 ? 96  GLN   B C   1 
ATOM   1511 O O   . GLN   B 1 79  ? -17.120 -25.524 -12.091 1.00 14.84 ? 96  GLN   B O   1 
ATOM   1512 C CB  . GLN   B 1 79  ? -15.179 -27.489 -11.020 1.00 14.58 ? 96  GLN   B CB  1 
ATOM   1513 C CG  . GLN   B 1 79  ? -13.940 -26.678 -10.676 1.00 16.75 ? 96  GLN   B CG  1 
ATOM   1514 C CD  . GLN   B 1 79  ? -13.537 -26.832 -9.227  1.00 18.17 ? 96  GLN   B CD  1 
ATOM   1515 O OE1 . GLN   B 1 79  ? -13.612 -27.917 -8.646  1.00 20.77 ? 96  GLN   B OE1 1 
ATOM   1516 N NE2 . GLN   B 1 79  ? -13.064 -25.744 -8.642  1.00 22.69 ? 96  GLN   B NE2 1 
ATOM   1517 N N   . PRO   B 1 80  ? -16.941 -24.616 -10.060 1.00 13.17 ? 97  PRO   B N   1 
ATOM   1518 C CA  . PRO   B 1 80  ? -17.356 -23.298 -10.573 1.00 12.66 ? 97  PRO   B CA  1 
ATOM   1519 C C   . PRO   B 1 80  ? -16.393 -22.777 -11.629 1.00 12.89 ? 97  PRO   B C   1 
ATOM   1520 O O   . PRO   B 1 80  ? -15.172 -22.867 -11.477 1.00 14.97 ? 97  PRO   B O   1 
ATOM   1521 C CB  . PRO   B 1 80  ? -17.358 -22.415 -9.321  1.00 13.86 ? 97  PRO   B CB  1 
ATOM   1522 C CG  . PRO   B 1 80  ? -17.592 -23.384 -8.181  1.00 14.69 ? 97  PRO   B CG  1 
ATOM   1523 C CD  . PRO   B 1 80  ? -16.803 -24.629 -8.596  1.00 14.18 ? 97  PRO   B CD  1 
ATOM   1524 N N   . SER   B 1 81  ? -16.960 -22.217 -12.708 1.00 11.74 ? 98  SER   B N   1 
ATOM   1525 C CA  . SER   B 1 81  ? -16.173 -21.839 -13.874 1.00 13.75 ? 98  SER   B CA  1 
ATOM   1526 C C   . SER   B 1 81  ? -16.913 -20.767 -14.657 1.00 12.47 ? 98  SER   B C   1 
ATOM   1527 O O   . SER   B 1 81  ? -18.081 -20.965 -15.014 1.00 13.55 ? 98  SER   B O   1 
ATOM   1528 C CB  . SER   B 1 81  ? -15.922 -23.064 -14.773 1.00 14.42 ? 98  SER   B CB  1 
ATOM   1529 O OG  . SER   B 1 81  ? -15.564 -22.667 -16.083 1.00 14.27 ? 98  SER   B OG  1 
ATOM   1530 N N   . LEU   B 1 82  ? -16.237 -19.646 -14.926 1.00 13.35 ? 99  LEU   B N   1 
ATOM   1531 C CA  . LEU   B 1 82  ? -16.839 -18.613 -15.763 1.00 14.23 ? 99  LEU   B CA  1 
ATOM   1532 C C   . LEU   B 1 82  ? -17.113 -19.123 -17.164 1.00 15.03 ? 99  LEU   B C   1 
ATOM   1533 O O   . LEU   B 1 82  ? -18.153 -18.807 -17.753 1.00 13.78 ? 99  LEU   B O   1 
ATOM   1534 C CB  . LEU   B 1 82  ? -15.917 -17.399 -15.852 1.00 13.85 ? 99  LEU   B CB  1 
ATOM   1535 C CG  . LEU   B 1 82  ? -15.606 -16.652 -14.563 1.00 16.19 ? 99  LEU   B CG  1 
ATOM   1536 C CD1 . LEU   B 1 82  ? -14.394 -15.766 -14.727 1.00 17.23 ? 99  LEU   B CD1 1 
ATOM   1537 C CD2 . LEU   B 1 82  ? -16.796 -15.818 -14.157 1.00 16.14 ? 99  LEU   B CD2 1 
ATOM   1538 N N   . GLY   B 1 83  ? -16.170 -19.892 -17.729 1.00 14.09 ? 100 GLY   B N   1 
ATOM   1539 C CA  . GLY   B 1 83  ? -16.312 -20.329 -19.110 1.00 15.89 ? 100 GLY   B CA  1 
ATOM   1540 C C   . GLY   B 1 83  ? -17.475 -21.281 -19.288 1.00 15.28 ? 100 GLY   B C   1 
ATOM   1541 O O   . GLY   B 1 83  ? -18.230 -21.181 -20.262 1.00 15.56 ? 100 GLY   B O   1 
ATOM   1542 N N   . VAL   B 1 84  ? -17.641 -22.217 -18.350 1.00 14.01 ? 101 VAL   B N   1 
ATOM   1543 C CA  . VAL   B 1 84  ? -18.786 -23.122 -18.404 1.00 13.88 ? 101 VAL   B CA  1 
ATOM   1544 C C   . VAL   B 1 84  ? -20.091 -22.347 -18.287 1.00 15.08 ? 101 VAL   B C   1 
ATOM   1545 O O   . VAL   B 1 84  ? -21.052 -22.601 -19.025 1.00 14.78 ? 101 VAL   B O   1 
ATOM   1546 C CB  . VAL   B 1 84  ? -18.677 -24.193 -17.309 1.00 13.42 ? 101 VAL   B CB  1 
ATOM   1547 C CG1 . VAL   B 1 84  ? -19.953 -25.025 -17.259 1.00 13.88 ? 101 VAL   B CG1 1 
ATOM   1548 C CG2 . VAL   B 1 84  ? -17.475 -25.093 -17.597 1.00 13.34 ? 101 VAL   B CG2 1 
ATOM   1549 N N   . GLY   B 1 85  ? -20.155 -21.400 -17.348 1.00 12.91 ? 102 GLY   B N   1 
ATOM   1550 C CA  . GLY   B 1 85  ? -21.372 -20.620 -17.211 1.00 14.65 ? 102 GLY   B CA  1 
ATOM   1551 C C   . GLY   B 1 85  ? -21.675 -19.829 -18.469 1.00 13.82 ? 102 GLY   B C   1 
ATOM   1552 O O   . GLY   B 1 85  ? -22.826 -19.781 -18.924 1.00 14.26 ? 102 GLY   B O   1 
ATOM   1553 N N   . TYR   B 1 86  ? -20.636 -19.246 -19.077 1.00 13.74 ? 103 TYR   B N   1 
ATOM   1554 C CA  . TYR   B 1 86  ? -20.801 -18.467 -20.301 1.00 14.57 ? 103 TYR   B CA  1 
ATOM   1555 C C   . TYR   B 1 86  ? -21.284 -19.344 -21.448 1.00 14.79 ? 103 TYR   B C   1 
ATOM   1556 O O   . TYR   B 1 86  ? -22.178 -18.948 -22.202 1.00 15.26 ? 103 TYR   B O   1 
ATOM   1557 C CB  . TYR   B 1 86  ? -19.475 -17.776 -20.651 1.00 13.36 ? 103 TYR   B CB  1 
ATOM   1558 C CG  . TYR   B 1 86  ? -19.501 -16.987 -21.926 1.00 15.50 ? 103 TYR   B CG  1 
ATOM   1559 C CD1 . TYR   B 1 86  ? -19.926 -15.660 -21.924 1.00 16.26 ? 103 TYR   B CD1 1 
ATOM   1560 C CD2 . TYR   B 1 86  ? -19.074 -17.545 -23.126 1.00 17.21 ? 103 TYR   B CD2 1 
ATOM   1561 C CE1 . TYR   B 1 86  ? -19.939 -14.915 -23.099 1.00 17.95 ? 103 TYR   B CE1 1 
ATOM   1562 C CE2 . TYR   B 1 86  ? -19.087 -16.813 -24.300 1.00 19.52 ? 103 TYR   B CE2 1 
ATOM   1563 C CZ  . TYR   B 1 86  ? -19.517 -15.501 -24.288 1.00 19.47 ? 103 TYR   B CZ  1 
ATOM   1564 O OH  . TYR   B 1 86  ? -19.532 -14.756 -25.450 1.00 22.09 ? 103 TYR   B OH  1 
ATOM   1565 N N   . GLU   B 1 87  ? -20.702 -20.539 -21.586 1.00 15.26 ? 104 GLU   B N   1 
ATOM   1566 C CA  . GLU   B 1 87  ? -21.161 -21.466 -22.614 1.00 15.23 ? 104 GLU   B CA  1 
ATOM   1567 C C   . GLU   B 1 87  ? -22.634 -21.799 -22.430 1.00 16.04 ? 104 GLU   B C   1 
ATOM   1568 O O   . GLU   B 1 87  ? -23.399 -21.831 -23.406 1.00 17.72 ? 104 GLU   B O   1 
ATOM   1569 C CB  . GLU   B 1 87  ? -20.304 -22.737 -22.579 1.00 14.87 ? 104 GLU   B CB  1 
ATOM   1570 C CG  . GLU   B 1 87  ? -18.948 -22.510 -23.238 1.00 17.71 ? 104 GLU   B CG  1 
ATOM   1571 C CD  . GLU   B 1 87  ? -17.922 -23.585 -22.956 1.00 15.85 ? 104 GLU   B CD  1 
ATOM   1572 O OE1 . GLU   B 1 87  ? -17.966 -24.216 -21.880 1.00 18.13 ? 104 GLU   B OE1 1 
ATOM   1573 O OE2 . GLU   B 1 87  ? -17.039 -23.741 -23.817 1.00 20.12 ? 104 GLU   B OE2 1 
ATOM   1574 N N   . LEU   B 1 88  ? -23.059 -22.021 -21.183 1.00 15.30 ? 105 LEU   B N   1 
ATOM   1575 C CA  . LEU   B 1 88  ? -24.459 -22.350 -20.934 1.00 16.01 ? 105 LEU   B CA  1 
ATOM   1576 C C   . LEU   B 1 88  ? -25.367 -21.163 -21.245 1.00 15.38 ? 105 LEU   B C   1 
ATOM   1577 O O   . LEU   B 1 88  ? -26.454 -21.341 -21.808 1.00 16.90 ? 105 LEU   B O   1 
ATOM   1578 C CB  . LEU   B 1 88  ? -24.619 -22.818 -19.484 1.00 14.72 ? 105 LEU   B CB  1 
ATOM   1579 C CG  . LEU   B 1 88  ? -24.040 -24.219 -19.251 1.00 15.27 ? 105 LEU   B CG  1 
ATOM   1580 C CD1 . LEU   B 1 88  ? -23.979 -24.525 -17.753 1.00 15.84 ? 105 LEU   B CD1 1 
ATOM   1581 C CD2 . LEU   B 1 88  ? -24.856 -25.289 -19.999 1.00 17.18 ? 105 LEU   B CD2 1 
ATOM   1582 N N   . GLY   B 1 89  ? -24.937 -19.942 -20.903 1.00 14.30 ? 106 GLY   B N   1 
ATOM   1583 C CA  . GLY   B 1 89  ? -25.738 -18.774 -21.238 1.00 16.44 ? 106 GLY   B CA  1 
ATOM   1584 C C   . GLY   B 1 89  ? -25.870 -18.563 -22.734 1.00 17.78 ? 106 GLY   B C   1 
ATOM   1585 O O   . GLY   B 1 89  ? -26.969 -18.301 -23.236 1.00 18.66 ? 106 GLY   B O   1 
ATOM   1586 N N   . ARG   B 1 90  ? -24.765 -18.702 -23.475 1.00 17.29 ? 107 ARG   B N   1 
ATOM   1587 C CA  . ARG   B 1 90  ? -24.852 -18.591 -24.930 1.00 19.23 ? 107 ARG   B CA  1 
ATOM   1588 C C   . ARG   B 1 90  ? -25.675 -19.728 -25.520 1.00 20.52 ? 107 ARG   B C   1 
ATOM   1589 O O   . ARG   B 1 90  ? -26.428 -19.522 -26.479 1.00 21.26 ? 107 ARG   B O   1 
ATOM   1590 C CB  . ARG   B 1 90  ? -23.454 -18.559 -25.561 1.00 20.72 ? 107 ARG   B CB  1 
ATOM   1591 C CG  . ARG   B 1 90  ? -22.581 -17.341 -25.180 1.00 19.97 ? 107 ARG   B CG  1 
ATOM   1592 C CD  . ARG   B 1 90  ? -23.237 -15.999 -25.494 1.00 20.44 ? 107 ARG   B CD  1 
ATOM   1593 N NE  . ARG   B 1 90  ? -23.560 -15.798 -26.904 1.00 21.81 ? 107 ARG   B NE  1 
ATOM   1594 C CZ  . ARG   B 1 90  ? -22.748 -15.252 -27.804 1.00 24.79 ? 107 ARG   B CZ  1 
ATOM   1595 N NH1 . ARG   B 1 90  ? -21.510 -14.890 -27.499 1.00 23.48 ? 107 ARG   B NH1 1 
ATOM   1596 N NH2 . ARG   B 1 90  ? -23.196 -15.042 -29.040 1.00 24.60 ? 107 ARG   B NH2 1 
ATOM   1597 N N   . ALA   B 1 91  ? -25.560 -20.929 -24.947 1.00 18.13 ? 108 ALA   B N   1 
ATOM   1598 C CA  . ALA   B 1 91  ? -26.320 -22.064 -25.456 1.00 19.18 ? 108 ALA   B CA  1 
ATOM   1599 C C   . ALA   B 1 91  ? -27.816 -21.842 -25.314 1.00 20.80 ? 108 ALA   B C   1 
ATOM   1600 O O   . ALA   B 1 91  ? -28.592 -22.180 -26.222 1.00 20.90 ? 108 ALA   B O   1 
ATOM   1601 C CB  . ALA   B 1 91  ? -25.916 -23.338 -24.726 1.00 18.67 ? 108 ALA   B CB  1 
ATOM   1602 N N   . VAL   B 1 92  ? -28.248 -21.307 -24.170 1.00 18.32 ? 109 VAL   B N   1 
ATOM   1603 C CA  . VAL   B 1 92  ? -29.670 -21.023 -23.990 1.00 20.43 ? 109 VAL   B CA  1 
ATOM   1604 C C   . VAL   B 1 92  ? -30.153 -20.075 -25.072 1.00 22.70 ? 109 VAL   B C   1 
ATOM   1605 O O   . VAL   B 1 92  ? -31.176 -20.307 -25.721 1.00 24.06 ? 109 VAL   B O   1 
ATOM   1606 C CB  . VAL   B 1 92  ? -29.939 -20.443 -22.590 1.00 21.53 ? 109 VAL   B CB  1 
ATOM   1607 C CG1 . VAL   B 1 92  ? -31.328 -19.833 -22.544 1.00 24.31 ? 109 VAL   B CG1 1 
ATOM   1608 C CG2 . VAL   B 1 92  ? -29.828 -21.528 -21.546 1.00 20.11 ? 109 VAL   B CG2 1 
ATOM   1609 N N   . ALA   B 1 93  ? -29.407 -18.998 -25.300 1.00 23.88 ? 110 ALA   B N   1 
ATOM   1610 C CA  . ALA   B 1 93  ? -29.846 -18.013 -26.277 1.00 24.51 ? 110 ALA   B CA  1 
ATOM   1611 C C   . ALA   B 1 93  ? -29.758 -18.543 -27.708 1.00 25.12 ? 110 ALA   B C   1 
ATOM   1612 O O   . ALA   B 1 93  ? -30.467 -18.049 -28.589 1.00 27.58 ? 110 ALA   B O   1 
ATOM   1613 C CB  . ALA   B 1 93  ? -29.034 -16.739 -26.103 1.00 21.69 ? 110 ALA   B CB  1 
ATOM   1614 N N   . PHE   B 1 94  ? -28.885 -19.522 -27.963 1.00 24.03 ? 111 PHE   B N   1 
ATOM   1615 C CA  . PHE   B 1 94  ? -28.836 -20.225 -29.242 1.00 26.22 ? 111 PHE   B CA  1 
ATOM   1616 C C   . PHE   B 1 94  ? -29.912 -21.305 -29.370 1.00 27.39 ? 111 PHE   B C   1 
ATOM   1617 O O   . PHE   B 1 94  ? -29.866 -22.079 -30.335 1.00 28.51 ? 111 PHE   B O   1 
ATOM   1618 C CB  . PHE   B 1 94  ? -27.458 -20.865 -29.468 1.00 24.49 ? 111 PHE   B CB  1 
ATOM   1619 C CG  . PHE   B 1 94  ? -26.348 -19.881 -29.777 1.00 25.32 ? 111 PHE   B CG  1 
ATOM   1620 C CD1 . PHE   B 1 94  ? -26.546 -18.840 -30.672 1.00 27.32 ? 111 PHE   B CD1 1 
ATOM   1621 C CD2 . PHE   B 1 94  ? -25.082 -20.062 -29.242 1.00 26.84 ? 111 PHE   B CD2 1 
ATOM   1622 C CE1 . PHE   B 1 94  ? -25.523 -17.960 -30.976 1.00 31.20 ? 111 PHE   B CE1 1 
ATOM   1623 C CE2 . PHE   B 1 94  ? -24.046 -19.190 -29.548 1.00 27.85 ? 111 PHE   B CE2 1 
ATOM   1624 C CZ  . PHE   B 1 94  ? -24.267 -18.134 -30.412 1.00 30.50 ? 111 PHE   B CZ  1 
ATOM   1625 N N   . ASN   B 1 95  ? -30.864 -21.357 -28.437 1.00 26.88 ? 112 ASN   B N   1 
ATOM   1626 C CA  . ASN   B 1 95  ? -31.924 -22.371 -28.396 1.00 25.76 ? 112 ASN   B CA  1 
ATOM   1627 C C   . ASN   B 1 95  ? -31.383 -23.788 -28.524 1.00 25.99 ? 112 ASN   B C   1 
ATOM   1628 O O   . ASN   B 1 95  ? -31.883 -24.597 -29.303 1.00 28.34 ? 112 ASN   B O   1 
ATOM   1629 C CB  . ASN   B 1 95  ? -33.017 -22.120 -29.443 1.00 29.12 ? 112 ASN   B CB  1 
ATOM   1630 C CG  . ASN   B 1 95  ? -33.736 -20.808 -29.234 1.00 36.95 ? 112 ASN   B CG  1 
ATOM   1631 O OD1 . ASN   B 1 95  ? -33.442 -19.807 -29.888 1.00 37.77 ? 112 ASN   B OD1 1 
ATOM   1632 N ND2 . ASN   B 1 95  ? -34.667 -20.798 -28.279 1.00 40.10 ? 112 ASN   B ND2 1 
ATOM   1633 N N   . LYS   B 1 96  ? -30.398 -24.113 -27.697 1.00 26.65 ? 113 LYS   B N   1 
ATOM   1634 C CA  . LYS   B 1 96  ? -29.834 -25.453 -27.686 1.00 24.98 ? 113 LYS   B CA  1 
ATOM   1635 C C   . LYS   B 1 96  ? -30.458 -26.285 -26.570 1.00 26.26 ? 113 LYS   B C   1 
ATOM   1636 O O   . LYS   B 1 96  ? -30.891 -25.761 -25.539 1.00 26.24 ? 113 LYS   B O   1 
ATOM   1637 C CB  . LYS   B 1 96  ? -28.314 -25.400 -27.504 1.00 23.96 ? 113 LYS   B CB  1 
ATOM   1638 C CG  . LYS   B 1 96  ? -27.583 -24.780 -28.692 1.00 24.67 ? 113 LYS   B CG  1 
ATOM   1639 C CD  . LYS   B 1 96  ? -27.891 -25.488 -30.009 1.00 24.88 ? 113 LYS   B CD  1 
ATOM   1640 C CE  . LYS   B 1 96  ? -27.337 -24.683 -31.184 1.00 29.28 ? 113 LYS   B CE  1 
ATOM   1641 N NZ  . LYS   B 1 96  ? -27.660 -25.288 -32.501 1.00 29.52 ? 113 LYS   B NZ  1 
ATOM   1642 N N   . ARG   B 1 97  ? -30.510 -27.595 -26.804 1.00 22.75 ? 114 ARG   B N   1 
ATOM   1643 C CA  . ARG   B 1 97  ? -30.820 -28.572 -25.764 1.00 20.48 ? 114 ARG   B CA  1 
ATOM   1644 C C   . ARG   B 1 97  ? -29.636 -28.750 -24.814 1.00 22.03 ? 114 ARG   B C   1 
ATOM   1645 O O   . ARG   B 1 97  ? -28.503 -28.956 -25.261 1.00 21.01 ? 114 ARG   B O   1 
ATOM   1646 C CB  . ARG   B 1 97  ? -31.158 -29.900 -26.433 1.00 26.68 ? 114 ARG   B CB  1 
ATOM   1647 C CG  . ARG   B 1 97  ? -31.604 -31.000 -25.514 1.00 25.82 ? 114 ARG   B CG  1 
ATOM   1648 C CD  . ARG   B 1 97  ? -32.780 -31.723 -26.142 1.00 31.04 ? 114 ARG   B CD  1 
ATOM   1649 N NE  . ARG   B 1 97  ? -32.441 -32.377 -27.401 1.00 30.80 ? 114 ARG   B NE  1 
ATOM   1650 C CZ  . ARG   B 1 97  ? -31.832 -33.552 -27.511 1.00 39.96 ? 114 ARG   B CZ  1 
ATOM   1651 N NH1 . ARG   B 1 97  ? -31.397 -34.210 -26.445 1.00 34.81 ? 114 ARG   B NH1 1 
ATOM   1652 N NH2 . ARG   B 1 97  ? -31.659 -34.086 -28.720 1.00 37.31 ? 114 ARG   B NH2 1 
ATOM   1653 N N   . ILE   B 1 98  ? -29.889 -28.687 -23.497 1.00 17.59 ? 115 ILE   B N   1 
ATOM   1654 C CA  . ILE   B 1 98  ? -28.825 -28.605 -22.494 1.00 18.68 ? 115 ILE   B CA  1 
ATOM   1655 C C   . ILE   B 1 98  ? -29.026 -29.669 -21.414 1.00 18.02 ? 115 ILE   B C   1 
ATOM   1656 O O   . ILE   B 1 98  ? -30.142 -29.845 -20.912 1.00 19.91 ? 115 ILE   B O   1 
ATOM   1657 C CB  . ILE   B 1 98  ? -28.771 -27.199 -21.858 1.00 17.94 ? 115 ILE   B CB  1 
ATOM   1658 C CG1 . ILE   B 1 98  ? -28.287 -26.165 -22.872 1.00 19.81 ? 115 ILE   B CG1 1 
ATOM   1659 C CG2 . ILE   B 1 98  ? -27.879 -27.173 -20.619 1.00 19.41 ? 115 ILE   B CG2 1 
ATOM   1660 C CD1 . ILE   B 1 98  ? -28.634 -24.734 -22.468 1.00 20.09 ? 115 ILE   B CD1 1 
ATOM   1661 N N   . LEU   B 1 99  ? -27.947 -30.374 -21.062 1.00 18.37 ? 116 LEU   B N   1 
ATOM   1662 C CA  . LEU   B 1 99  ? -27.904 -31.315 -19.942 1.00 17.28 ? 116 LEU   B CA  1 
ATOM   1663 C C   . LEU   B 1 99  ? -26.766 -30.915 -19.009 1.00 16.66 ? 116 LEU   B C   1 
ATOM   1664 O O   . LEU   B 1 99  ? -25.605 -30.905 -19.420 1.00 17.37 ? 116 LEU   B O   1 
ATOM   1665 C CB  . LEU   B 1 99  ? -27.711 -32.748 -20.441 1.00 20.18 ? 116 LEU   B CB  1 
ATOM   1666 C CG  . LEU   B 1 99  ? -27.420 -33.810 -19.372 1.00 19.14 ? 116 LEU   B CG  1 
ATOM   1667 C CD1 . LEU   B 1 99  ? -28.542 -33.976 -18.337 1.00 20.56 ? 116 LEU   B CD1 1 
ATOM   1668 C CD2 . LEU   B 1 99  ? -27.013 -35.158 -19.981 1.00 21.43 ? 116 LEU   B CD2 1 
ATOM   1669 N N   . CYS   B 1 100 ? -27.098 -30.576 -17.763 1.00 17.06 ? 117 CYS   B N   1 
ATOM   1670 C CA  . CYS   B 1 100 ? -26.097 -30.238 -16.747 1.00 16.36 ? 117 CYS   B CA  1 
ATOM   1671 C C   . CYS   B 1 100 ? -26.014 -31.338 -15.703 1.00 16.54 ? 117 CYS   B C   1 
ATOM   1672 O O   . CYS   B 1 100 ? -27.039 -31.910 -15.300 1.00 19.05 ? 117 CYS   B O   1 
ATOM   1673 C CB  . CYS   B 1 100 ? -26.406 -28.922 -16.046 1.00 17.36 ? 117 CYS   B CB  1 
ATOM   1674 S SG  . CYS   B 1 100 ? -26.254 -27.479 -17.077 1.00 18.06 ? 117 CYS   B SG  1 
ATOM   1675 N N   . LEU   B 1 101 ? -24.791 -31.616 -15.251 1.00 16.23 ? 118 LEU   B N   1 
ATOM   1676 C CA  . LEU   B 1 101 ? -24.501 -32.711 -14.328 1.00 17.80 ? 118 LEU   B CA  1 
ATOM   1677 C C   . LEU   B 1 101 ? -23.770 -32.151 -13.118 1.00 16.89 ? 118 LEU   B C   1 
ATOM   1678 O O   . LEU   B 1 101 ? -22.708 -31.547 -13.270 1.00 16.05 ? 118 LEU   B O   1 
ATOM   1679 C CB  . LEU   B 1 101 ? -23.647 -33.779 -15.012 1.00 19.65 ? 118 LEU   B CB  1 
ATOM   1680 C CG  . LEU   B 1 101 ? -24.189 -34.293 -16.338 1.00 19.48 ? 118 LEU   B CG  1 
ATOM   1681 C CD1 . LEU   B 1 101 ? -23.167 -35.196 -17.038 1.00 23.04 ? 118 LEU   B CD1 1 
ATOM   1682 C CD2 . LEU   B 1 101 ? -25.505 -35.034 -16.125 1.00 22.93 ? 118 LEU   B CD2 1 
ATOM   1683 N N   . PHE   B 1 102 ? -24.322 -32.368 -11.924 1.00 16.66 ? 119 PHE   B N   1 
ATOM   1684 C CA  . PHE   B 1 102 ? -23.804 -31.797 -10.687 1.00 16.75 ? 119 PHE   B CA  1 
ATOM   1685 C C   . PHE   B 1 102 ? -23.630 -32.870 -9.625  1.00 16.74 ? 119 PHE   B C   1 
ATOM   1686 O O   . PHE   B 1 102 ? -24.535 -33.681 -9.413  1.00 18.30 ? 119 PHE   B O   1 
ATOM   1687 C CB  . PHE   B 1 102 ? -24.759 -30.727 -10.133 1.00 15.18 ? 119 PHE   B CB  1 
ATOM   1688 C CG  . PHE   B 1 102 ? -24.289 -30.141 -8.826  1.00 15.44 ? 119 PHE   B CG  1 
ATOM   1689 C CD1 . PHE   B 1 102 ? -23.201 -29.271 -8.798  1.00 16.57 ? 119 PHE   B CD1 1 
ATOM   1690 C CD2 . PHE   B 1 102 ? -24.892 -30.485 -7.637  1.00 16.70 ? 119 PHE   B CD2 1 
ATOM   1691 C CE1 . PHE   B 1 102 ? -22.741 -28.749 -7.586  1.00 17.87 ? 119 PHE   B CE1 1 
ATOM   1692 C CE2 . PHE   B 1 102 ? -24.455 -29.977 -6.433  1.00 17.30 ? 119 PHE   B CE2 1 
ATOM   1693 C CZ  . PHE   B 1 102 ? -23.375 -29.106 -6.396  1.00 16.28 ? 119 PHE   B CZ  1 
ATOM   1694 N N   . ARG   B 1 103 ? -22.493 -32.850 -8.915  1.00 15.82 ? 120 ARG   B N   1 
ATOM   1695 C CA  . ARG   B 1 103 ? -22.241 -33.845 -7.865  1.00 17.05 ? 120 ARG   B CA  1 
ATOM   1696 C C   . ARG   B 1 103 ? -22.420 -33.246 -6.476  1.00 16.88 ? 120 ARG   B C   1 
ATOM   1697 O O   . ARG   B 1 103 ? -21.538 -32.511 -6.009  1.00 17.76 ? 120 ARG   B O   1 
ATOM   1698 C CB  . ARG   B 1 103 ? -20.837 -34.441 -7.987  1.00 18.67 ? 120 ARG   B CB  1 
ATOM   1699 C CG  . ARG   B 1 103 ? -20.534 -35.056 -9.328  1.00 18.86 ? 120 ARG   B CG  1 
ATOM   1700 C CD  . ARG   B 1 103 ? -19.270 -35.911 -9.347  1.00 20.98 ? 120 ARG   B CD  1 
ATOM   1701 N NE  . ARG   B 1 103 ? -18.137 -35.338 -8.622  1.00 19.36 ? 120 ARG   B NE  1 
ATOM   1702 C CZ  . ARG   B 1 103 ? -17.387 -34.334 -9.067  1.00 19.29 ? 120 ARG   B CZ  1 
ATOM   1703 N NH1 . ARG   B 1 103 ? -17.689 -33.683 -10.182 1.00 19.65 ? 120 ARG   B NH1 1 
ATOM   1704 N NH2 . ARG   B 1 103 ? -16.307 -33.976 -8.378  1.00 20.52 ? 120 ARG   B NH2 1 
ATOM   1705 N N   . PRO   B 1 104 ? -23.482 -33.590 -5.752  1.00 18.63 ? 121 PRO   B N   1 
ATOM   1706 C CA  . PRO   B 1 104 ? -23.600 -33.149 -4.351  1.00 19.89 ? 121 PRO   B CA  1 
ATOM   1707 C C   . PRO   B 1 104 ? -22.461 -33.609 -3.459  1.00 20.82 ? 121 PRO   B C   1 
ATOM   1708 O O   . PRO   B 1 104 ? -22.243 -32.989 -2.410  1.00 19.21 ? 121 PRO   B O   1 
ATOM   1709 C CB  . PRO   B 1 104 ? -24.938 -33.754 -3.895  1.00 21.68 ? 121 PRO   B CB  1 
ATOM   1710 C CG  . PRO   B 1 104 ? -25.663 -34.117 -5.152  1.00 23.83 ? 121 PRO   B CG  1 
ATOM   1711 C CD  . PRO   B 1 104 ? -24.654 -34.363 -6.211  1.00 19.53 ? 121 PRO   B CD  1 
ATOM   1712 N N   . GLN   B 1 105 ? -21.730 -34.678 -3.822  1.00 18.25 ? 122 GLN   B N   1 
ATOM   1713 C CA  . GLN   B 1 105 ? -20.609 -35.102 -2.992  1.00 19.87 ? 122 GLN   B CA  1 
ATOM   1714 C C   . GLN   B 1 105 ? -19.528 -34.027 -2.921  1.00 18.65 ? 122 GLN   B C   1 
ATOM   1715 O O   . GLN   B 1 105 ? -18.696 -34.056 -2.012  1.00 18.61 ? 122 GLN   B O   1 
ATOM   1716 C CB  . GLN   B 1 105 ? -20.051 -36.431 -3.521  1.00 19.11 ? 122 GLN   B CB  1 
ATOM   1717 C CG  . GLN   B 1 105 ? -18.932 -37.095 -2.709  1.00 22.23 ? 122 GLN   B CG  1 
ATOM   1718 C CD  . GLN   B 1 105 ? -17.563 -36.487 -2.965  1.00 25.51 ? 122 GLN   B CD  1 
ATOM   1719 O OE1 . GLN   B 1 105 ? -17.266 -36.076 -4.081  1.00 23.06 ? 122 GLN   B OE1 1 
ATOM   1720 N NE2 . GLN   B 1 105 ? -16.702 -36.491 -1.945  0.85 21.80 ? 122 GLN   B NE2 1 
ATOM   1721 N N   . SER   B 1 106 ? -19.551 -33.047 -3.828  1.00 16.86 ? 123 SER   B N   1 
ATOM   1722 C CA  . SER   B 1 106 ? -18.619 -31.925 -3.745  1.00 18.67 ? 123 SER   B CA  1 
ATOM   1723 C C   . SER   B 1 106 ? -18.843 -31.045 -2.519  1.00 18.11 ? 123 SER   B C   1 
ATOM   1724 O O   . SER   B 1 106 ? -17.957 -30.267 -2.157  1.00 19.40 ? 123 SER   B O   1 
ATOM   1725 C CB  . SER   B 1 106 ? -18.751 -31.049 -4.986  1.00 16.65 ? 123 SER   B CB  1 
ATOM   1726 O OG  . SER   B 1 106 ? -20.027 -30.402 -4.998  1.00 16.76 ? 123 SER   B OG  1 
ATOM   1727 N N   . GLY   B 1 107 ? -19.998 -31.142 -1.876  1.00 17.96 ? 124 GLY   B N   1 
ATOM   1728 C CA  . GLY   B 1 107 ? -20.326 -30.281 -0.764  1.00 18.53 ? 124 GLY   B CA  1 
ATOM   1729 C C   . GLY   B 1 107 ? -20.796 -28.901 -1.161  1.00 18.01 ? 124 GLY   B C   1 
ATOM   1730 O O   . GLY   B 1 107 ? -21.178 -28.121 -0.277  1.00 20.10 ? 124 GLY   B O   1 
ATOM   1731 N N   . ARG   B 1 108 ? -20.796 -28.588 -2.450  1.00 17.82 ? 125 ARG   B N   1 
ATOM   1732 C CA  . ARG   B 1 108 ? -21.157 -27.268 -2.931  1.00 18.35 ? 125 ARG   B CA  1 
ATOM   1733 C C   . ARG   B 1 108 ? -22.664 -27.158 -3.077  1.00 17.74 ? 125 ARG   B C   1 
ATOM   1734 O O   . ARG   B 1 108 ? -23.388 -28.158 -3.179  1.00 18.70 ? 125 ARG   B O   1 
ATOM   1735 C CB  . ARG   B 1 108 ? -20.516 -26.968 -4.287  1.00 18.27 ? 125 ARG   B CB  1 
ATOM   1736 C CG  . ARG   B 1 108 ? -19.029 -26.782 -4.226  1.00 21.05 ? 125 ARG   B CG  1 
ATOM   1737 C CD  . ARG   B 1 108 ? -18.496 -26.258 -5.541  1.00 20.52 ? 125 ARG   B CD  1 
ATOM   1738 N NE  . ARG   B 1 108 ? -17.050 -26.145 -5.492  1.00 24.45 ? 125 ARG   B NE  1 
ATOM   1739 C CZ  . ARG   B 1 108 ? -16.222 -27.110 -5.849  1.00 25.92 ? 125 ARG   B CZ  1 
ATOM   1740 N NH1 . ARG   B 1 108 ? -16.668 -28.230 -6.394  1.00 26.08 ? 125 ARG   B NH1 1 
ATOM   1741 N NH2 . ARG   B 1 108 ? -14.914 -26.941 -5.668  1.00 30.13 ? 125 ARG   B NH2 1 
ATOM   1742 N N   . VAL   B 1 109 ? -23.129 -25.915 -3.096  1.00 17.09 ? 126 VAL   B N   1 
ATOM   1743 C CA  . VAL   B 1 109 ? -24.491 -25.582 -3.483  1.00 16.43 ? 126 VAL   B CA  1 
ATOM   1744 C C   . VAL   B 1 109 ? -24.413 -25.019 -4.894  1.00 14.27 ? 126 VAL   B C   1 
ATOM   1745 O O   . VAL   B 1 109 ? -23.765 -23.989 -5.126  1.00 15.55 ? 126 VAL   B O   1 
ATOM   1746 C CB  . VAL   B 1 109 ? -25.124 -24.575 -2.513  1.00 17.57 ? 126 VAL   B CB  1 
ATOM   1747 C CG1 . VAL   B 1 109 ? -26.554 -24.300 -2.931  1.00 18.02 ? 126 VAL   B CG1 1 
ATOM   1748 C CG2 . VAL   B 1 109 ? -25.046 -25.094 -1.075  1.00 21.03 ? 126 VAL   B CG2 1 
ATOM   1749 N N   . LEU   B 1 110 ? -25.024 -25.720 -5.851  1.00 15.46 ? 127 LEU   B N   1 
ATOM   1750 C CA  . LEU   B 1 110 ? -24.934 -25.307 -7.244  1.00 13.91 ? 127 LEU   B CA  1 
ATOM   1751 C C   . LEU   B 1 110 ? -25.558 -23.929 -7.437  1.00 15.75 ? 127 LEU   B C   1 
ATOM   1752 O O   . LEU   B 1 110 ? -26.632 -23.632 -6.896  1.00 16.79 ? 127 LEU   B O   1 
ATOM   1753 C CB  . LEU   B 1 110 ? -25.642 -26.317 -8.146  1.00 14.31 ? 127 LEU   B CB  1 
ATOM   1754 C CG  . LEU   B 1 110 ? -25.740 -25.947 -9.629  1.00 14.36 ? 127 LEU   B CG  1 
ATOM   1755 C CD1 . LEU   B 1 110 ? -24.375 -25.838 -10.266 1.00 16.22 ? 127 LEU   B CD1 1 
ATOM   1756 C CD2 . LEU   B 1 110 ? -26.624 -27.000 -10.343 1.00 15.08 ? 127 LEU   B CD2 1 
ATOM   1757 N N   . SER   B 1 111 ? -24.860 -23.090 -8.207  1.00 13.65 ? 128 SER   B N   1 
ATOM   1758 C CA  . SER   B 1 111 ? -25.331 -21.781 -8.659  1.00 13.11 ? 128 SER   B CA  1 
ATOM   1759 C C   . SER   B 1 111 ? -26.831 -21.720 -8.898  1.00 14.78 ? 128 SER   B C   1 
ATOM   1760 O O   . SER   B 1 111 ? -27.381 -22.554 -9.624  1.00 14.81 ? 128 SER   B O   1 
ATOM   1761 C CB  . SER   B 1 111 ? -24.629 -21.408 -9.957  1.00 13.38 ? 128 SER   B CB  1 
ATOM   1762 O OG  . SER   B 1 111 ? -25.039 -20.122 -10.406 1.00 13.85 ? 128 SER   B OG  1 
ATOM   1763 N N   . ALA   B 1 112 ? -27.492 -20.719 -8.319  1.00 14.61 ? 129 ALA   B N   1 
ATOM   1764 C CA  . ALA   B 1 112 ? -28.914 -20.514 -8.596  1.00 16.40 ? 129 ALA   B CA  1 
ATOM   1765 C C   . ALA   B 1 112 ? -29.167 -20.239 -10.070 1.00 15.83 ? 129 ALA   B C   1 
ATOM   1766 O O   . ALA   B 1 112 ? -30.275 -20.504 -10.560 1.00 16.53 ? 129 ALA   B O   1 
ATOM   1767 C CB  . ALA   B 1 112 ? -29.471 -19.362 -7.757  1.00 15.80 ? 129 ALA   B CB  1 
ATOM   1768 N N   . MET   B 1 113 ? -28.171 -19.700 -10.787 1.00 14.72 ? 130 MET   B N   1 
ATOM   1769 C CA  . MET   B 1 113 ? -28.399 -19.375 -12.183 1.00 16.00 ? 130 MET   B CA  1 
ATOM   1770 C C   . MET   B 1 113 ? -28.487 -20.636 -13.030 1.00 17.41 ? 130 MET   B C   1 
ATOM   1771 O O   . MET   B 1 113 ? -29.156 -20.653 -14.068 1.00 18.98 ? 130 MET   B O   1 
ATOM   1772 C CB  . MET   B 1 113 ? -27.276 -18.474 -12.695 1.00 17.28 ? 130 MET   B CB  1 
ATOM   1773 C CG  . MET   B 1 113 ? -27.308 -17.056 -12.146 1.00 19.62 ? 130 MET   B CG  1 
ATOM   1774 S SD  . MET   B 1 113 ? -28.901 -16.258 -11.995 1.00 19.99 ? 130 MET   B SD  1 
ATOM   1775 C CE  . MET   B 1 113 ? -29.005 -15.434 -13.585 1.00 23.84 ? 130 MET   B CE  1 
ATOM   1776 N N   . ILE   B 1 114 ? -27.817 -21.703 -12.619 1.00 13.70 ? 131 ILE   B N   1 
ATOM   1777 C CA  . ILE   B 1 114 ? -27.892 -22.945 -13.367 1.00 14.78 ? 131 ILE   B CA  1 
ATOM   1778 C C   . ILE   B 1 114 ? -29.071 -23.784 -12.905 1.00 15.63 ? 131 ILE   B C   1 
ATOM   1779 O O   . ILE   B 1 114 ? -29.887 -24.243 -13.713 1.00 15.60 ? 131 ILE   B O   1 
ATOM   1780 C CB  . ILE   B 1 114 ? -26.557 -23.700 -13.236 1.00 12.81 ? 131 ILE   B CB  1 
ATOM   1781 C CG1 . ILE   B 1 114 ? -25.396 -22.803 -13.708 1.00 15.93 ? 131 ILE   B CG1 1 
ATOM   1782 C CG2 . ILE   B 1 114 ? -26.614 -25.011 -14.024 1.00 15.77 ? 131 ILE   B CG2 1 
ATOM   1783 C CD1 . ILE   B 1 114 ? -25.573 -22.158 -15.086 1.00 16.63 ? 131 ILE   B CD1 1 
ATOM   1784 N N   . ARG   B 1 115 ? -29.199 -23.966 -11.593 1.00 15.35 ? 132 ARG   B N   1 
ATOM   1785 C CA  . ARG   B 1 115 ? -30.337 -24.698 -11.048 1.00 18.09 ? 132 ARG   B CA  1 
ATOM   1786 C C   . ARG   B 1 115 ? -31.654 -24.021 -11.440 1.00 18.37 ? 132 ARG   B C   1 
ATOM   1787 O O   . ARG   B 1 115 ? -32.632 -24.697 -11.787 1.00 19.30 ? 132 ARG   B O   1 
ATOM   1788 C CB  . ARG   B 1 115 ? -30.169 -24.796 -9.526  1.00 18.80 ? 132 ARG   B CB  1 
ATOM   1789 C CG  . ARG   B 1 115 ? -31.220 -25.530 -8.776  1.00 23.03 ? 132 ARG   B CG  1 
ATOM   1790 C CD  . ARG   B 1 115 ? -30.977 -27.030 -8.827  1.00 22.34 ? 132 ARG   B CD  1 
ATOM   1791 N NE  . ARG   B 1 115 ? -29.821 -27.481 -8.052  1.00 21.01 ? 132 ARG   B NE  1 
ATOM   1792 C CZ  . ARG   B 1 115 ? -29.409 -28.744 -8.027  1.00 19.90 ? 132 ARG   B CZ  1 
ATOM   1793 N NH1 . ARG   B 1 115 ? -30.015 -29.678 -8.745  1.00 23.15 ? 132 ARG   B NH1 1 
ATOM   1794 N NH2 . ARG   B 1 115 ? -28.369 -29.082 -7.262  1.00 20.67 ? 132 ARG   B NH2 1 
ATOM   1795 N N   . GLY   B 1 116 ? -31.680 -22.680 -11.423 1.00 16.41 ? 133 GLY   B N   1 
ATOM   1796 C CA  . GLY   B 1 116 ? -32.881 -21.924 -11.745 1.00 16.88 ? 133 GLY   B CA  1 
ATOM   1797 C C   . GLY   B 1 116 ? -33.179 -21.765 -13.222 1.00 18.07 ? 133 GLY   B C   1 
ATOM   1798 O O   . GLY   B 1 116 ? -34.308 -21.408 -13.574 1.00 20.70 ? 133 GLY   B O   1 
ATOM   1799 N N   . ALA   B 1 117 ? -32.203 -22.007 -14.091 1.00 16.49 ? 134 ALA   B N   1 
ATOM   1800 C CA  . ALA   B 1 117 ? -32.442 -21.980 -15.533 1.00 17.44 ? 134 ALA   B CA  1 
ATOM   1801 C C   . ALA   B 1 117 ? -33.158 -23.237 -16.012 1.00 21.51 ? 134 ALA   B C   1 
ATOM   1802 O O   . ALA   B 1 117 ? -33.753 -23.228 -17.100 1.00 22.40 ? 134 ALA   B O   1 
ATOM   1803 C CB  . ALA   B 1 117 ? -31.116 -21.841 -16.293 1.00 17.54 ? 134 ALA   B CB  1 
ATOM   1804 N N   . ALA   B 1 118 ? -33.115 -24.308 -15.222 1.00 19.24 ? 135 ALA   B N   1 
ATOM   1805 C CA  . ALA   B 1 118 ? -33.633 -25.597 -15.656 1.00 21.55 ? 135 ALA   B CA  1 
ATOM   1806 C C   . ALA   B 1 118 ? -35.141 -25.543 -15.819 1.00 22.52 ? 135 ALA   B C   1 
ATOM   1807 O O   . ALA   B 1 118 ? -35.849 -24.890 -15.045 1.00 23.62 ? 135 ALA   B O   1 
ATOM   1808 C CB  . ALA   B 1 118 ? -33.262 -26.687 -14.652 1.00 22.61 ? 135 ALA   B CB  1 
ATOM   1809 N N   . ASP   B 1 119 ? -35.636 -26.239 -16.837 1.00 20.69 ? 136 ASP   B N   1 
ATOM   1810 C CA  . ASP   B 1 119 ? -37.067 -26.388 -17.035 1.00 21.95 ? 136 ASP   B CA  1 
ATOM   1811 C C   . ASP   B 1 119 ? -37.488 -27.853 -17.067 1.00 22.90 ? 136 ASP   B C   1 
ATOM   1812 O O   . ASP   B 1 119 ? -38.657 -28.148 -17.325 1.00 23.92 ? 136 ASP   B O   1 
ATOM   1813 C CB  . ASP   B 1 119 ? -37.487 -25.621 -18.299 1.00 25.01 ? 136 ASP   B CB  1 
ATOM   1814 C CG  . ASP   B 1 119 ? -36.885 -26.195 -19.578 1.00 26.70 ? 136 ASP   B CG  1 
ATOM   1815 O OD1 . ASP   B 1 119 ? -36.265 -27.277 -19.536 1.00 24.43 ? 136 ASP   B OD1 1 
ATOM   1816 O OD2 . ASP   B 1 119 ? -36.976 -25.513 -20.624 1.00 30.88 ? 136 ASP   B OD2 1 
ATOM   1817 N N   . GLY   B 1 120 ? -36.562 -28.773 -16.788 1.00 22.89 ? 137 GLY   B N   1 
ATOM   1818 C CA  . GLY   B 1 120 ? -36.864 -30.193 -16.742 1.00 23.03 ? 137 GLY   B CA  1 
ATOM   1819 C C   . GLY   B 1 120 ? -37.002 -30.875 -18.084 1.00 23.33 ? 137 GLY   B C   1 
ATOM   1820 O O   . GLY   B 1 120 ? -37.184 -32.100 -18.121 1.00 27.50 ? 137 GLY   B O   1 
ATOM   1821 N N   . SER   B 1 121 ? -36.944 -30.129 -19.186 1.00 27.45 ? 138 SER   B N   1 
ATOM   1822 C CA  . SER   B 1 121 ? -37.084 -30.705 -20.519 1.00 28.57 ? 138 SER   B CA  1 
ATOM   1823 C C   . SER   B 1 121 ? -35.880 -30.325 -21.371 1.00 26.49 ? 138 SER   B C   1 
ATOM   1824 O O   . SER   B 1 121 ? -34.893 -31.070 -21.432 1.00 26.25 ? 138 SER   B O   1 
ATOM   1825 C CB  . SER   B 1 121 ? -38.389 -30.240 -21.173 1.00 28.99 ? 138 SER   B CB  1 
ATOM   1826 O OG  . SER   B 1 121 ? -38.787 -31.151 -22.179 1.00 39.68 ? 138 SER   B OG  1 
ATOM   1827 N N   . ARG   B 1 122 ? -35.935 -29.159 -22.012 1.00 25.95 ? 139 ARG   B N   1 
ATOM   1828 C CA  . ARG   B 1 122 ? -34.838 -28.747 -22.877 1.00 25.48 ? 139 ARG   B CA  1 
ATOM   1829 C C   . ARG   B 1 122 ? -33.639 -28.193 -22.109 1.00 27.20 ? 139 ARG   B C   1 
ATOM   1830 O O   . ARG   B 1 122 ? -32.563 -28.053 -22.701 1.00 28.05 ? 139 ARG   B O   1 
ATOM   1831 C CB  . ARG   B 1 122 ? -35.353 -27.728 -23.899 1.00 28.90 ? 139 ARG   B CB  1 
ATOM   1832 C CG  . ARG   B 1 122 ? -35.618 -28.355 -25.258 1.00 34.62 ? 139 ARG   B CG  1 
ATOM   1833 C CD  . ARG   B 1 122 ? -35.911 -27.336 -26.360 1.00 36.55 ? 139 ARG   B CD  1 
ATOM   1834 N NE  . ARG   B 1 122 ? -34.731 -26.928 -27.117 1.00 31.31 ? 139 ARG   B NE  1 
ATOM   1835 C CZ  . ARG   B 1 122 ? -34.153 -27.656 -28.065 1.00 30.48 ? 139 ARG   B CZ  1 
ATOM   1836 N NH1 . ARG   B 1 122 ? -34.525 -28.907 -28.307 1.00 34.40 ? 139 ARG   B NH1 1 
ATOM   1837 N NH2 . ARG   B 1 122 ? -33.172 -27.123 -28.787 1.00 33.15 ? 139 ARG   B NH2 1 
ATOM   1838 N N   . PHE   B 1 123 ? -33.783 -27.884 -20.818 1.00 21.00 ? 140 PHE   B N   1 
ATOM   1839 C CA  . PHE   B 1 123 ? -32.654 -27.547 -19.946 1.00 22.43 ? 140 PHE   B CA  1 
ATOM   1840 C C   . PHE   B 1 123 ? -32.819 -28.399 -18.689 1.00 20.91 ? 140 PHE   B C   1 
ATOM   1841 O O   . PHE   B 1 123 ? -33.671 -28.113 -17.843 1.00 20.86 ? 140 PHE   B O   1 
ATOM   1842 C CB  . PHE   B 1 123 ? -32.627 -26.047 -19.627 1.00 19.92 ? 140 PHE   B CB  1 
ATOM   1843 C CG  . PHE   B 1 123 ? -31.332 -25.550 -18.984 1.00 19.73 ? 140 PHE   B CG  1 
ATOM   1844 C CD1 . PHE   B 1 123 ? -30.795 -26.139 -17.844 1.00 18.47 ? 140 PHE   B CD1 1 
ATOM   1845 C CD2 . PHE   B 1 123 ? -30.676 -24.457 -19.524 1.00 18.22 ? 140 PHE   B CD2 1 
ATOM   1846 C CE1 . PHE   B 1 123 ? -29.619 -25.652 -17.262 1.00 19.40 ? 140 PHE   B CE1 1 
ATOM   1847 C CE2 . PHE   B 1 123 ? -29.517 -23.958 -18.950 1.00 19.06 ? 140 PHE   B CE2 1 
ATOM   1848 C CZ  . PHE   B 1 123 ? -28.978 -24.560 -17.825 1.00 18.04 ? 140 PHE   B CZ  1 
ATOM   1849 N N   . GLN   B 1 124 ? -32.019 -29.457 -18.561 1.00 19.77 ? 141 GLN   B N   1 
ATOM   1850 C CA  . GLN   B 1 124 ? -32.117 -30.377 -17.434 1.00 19.97 ? 141 GLN   B CA  1 
ATOM   1851 C C   . GLN   B 1 124 ? -30.878 -30.263 -16.555 1.00 20.17 ? 141 GLN   B C   1 
ATOM   1852 O O   . GLN   B 1 124 ? -29.756 -30.180 -17.065 1.00 19.14 ? 141 GLN   B O   1 
ATOM   1853 C CB  . GLN   B 1 124 ? -32.277 -31.820 -17.922 1.00 19.24 ? 141 GLN   B CB  1 
ATOM   1854 C CG  . GLN   B 1 124 ? -33.656 -32.091 -18.486 1.00 20.27 ? 141 GLN   B CG  1 
ATOM   1855 C CD  . GLN   B 1 124 ? -33.754 -33.476 -19.068 1.00 22.70 ? 141 GLN   B CD  1 
ATOM   1856 O OE1 . GLN   B 1 124 ? -33.222 -34.430 -18.497 1.00 25.62 ? 141 GLN   B OE1 1 
ATOM   1857 N NE2 . GLN   B 1 124 ? -34.440 -33.605 -20.198 1.00 24.52 ? 141 GLN   B NE2 1 
ATOM   1858 N N   . VAL   B 1 125 ? -31.079 -30.259 -15.236 1.00 18.59 ? 142 VAL   B N   1 
ATOM   1859 C CA  . VAL   B 1 125 ? -29.981 -30.274 -14.262 1.00 19.42 ? 142 VAL   B CA  1 
ATOM   1860 C C   . VAL   B 1 125 ? -30.140 -31.516 -13.400 1.00 18.63 ? 142 VAL   B C   1 
ATOM   1861 O O   . VAL   B 1 125 ? -31.117 -31.638 -12.652 1.00 20.97 ? 142 VAL   B O   1 
ATOM   1862 C CB  . VAL   B 1 125 ? -29.953 -29.017 -13.381 1.00 17.81 ? 142 VAL   B CB  1 
ATOM   1863 C CG1 . VAL   B 1 125 ? -28.827 -29.135 -12.357 1.00 18.14 ? 142 VAL   B CG1 1 
ATOM   1864 C CG2 . VAL   B 1 125 ? -29.746 -27.764 -14.235 1.00 19.63 ? 142 VAL   B CG2 1 
ATOM   1865 N N   . TRP   B 1 126 ? -29.179 -32.434 -13.486 1.00 17.63 ? 143 TRP   B N   1 
ATOM   1866 C CA  . TRP   B 1 126 ? -29.233 -33.687 -12.743 1.00 18.86 ? 143 TRP   B CA  1 
ATOM   1867 C C   . TRP   B 1 126 ? -28.156 -33.721 -11.672 1.00 22.36 ? 143 TRP   B C   1 
ATOM   1868 O O   . TRP   B 1 126 ? -26.973 -33.523 -11.967 1.00 21.63 ? 143 TRP   B O   1 
ATOM   1869 C CB  . TRP   B 1 126 ? -29.068 -34.889 -13.673 1.00 18.51 ? 143 TRP   B CB  1 
ATOM   1870 C CG  . TRP   B 1 126 ? -30.308 -35.156 -14.440 1.00 18.01 ? 143 TRP   B CG  1 
ATOM   1871 C CD1 . TRP   B 1 126 ? -30.649 -34.627 -15.647 1.00 23.31 ? 143 TRP   B CD1 1 
ATOM   1872 C CD2 . TRP   B 1 126 ? -31.410 -35.965 -14.027 1.00 19.65 ? 143 TRP   B CD2 1 
ATOM   1873 N NE1 . TRP   B 1 126 ? -31.893 -35.070 -16.023 1.00 21.59 ? 143 TRP   B NE1 1 
ATOM   1874 C CE2 . TRP   B 1 126 ? -32.378 -35.903 -15.050 1.00 21.35 ? 143 TRP   B CE2 1 
ATOM   1875 C CE3 . TRP   B 1 126 ? -31.667 -36.753 -12.899 1.00 20.98 ? 143 TRP   B CE3 1 
ATOM   1876 C CZ2 . TRP   B 1 126 ? -33.590 -36.573 -14.971 1.00 21.90 ? 143 TRP   B CZ2 1 
ATOM   1877 C CZ3 . TRP   B 1 126 ? -32.882 -37.424 -12.820 1.00 25.77 ? 143 TRP   B CZ3 1 
ATOM   1878 C CH2 . TRP   B 1 126 ? -33.821 -37.340 -13.861 1.00 24.71 ? 143 TRP   B CH2 1 
ATOM   1879 N N   . ASP   B 1 127 ? -28.571 -33.965 -10.434 1.00 19.13 ? 144 ASP   B N   1 
ATOM   1880 C CA  . ASP   B 1 127 ? -27.653 -34.409 -9.395  1.00 21.45 ? 144 ASP   B CA  1 
ATOM   1881 C C   . ASP   B 1 127 ? -27.295 -35.869 -9.622  1.00 21.36 ? 144 ASP   B C   1 
ATOM   1882 O O   . ASP   B 1 127 ? -28.167 -36.690 -9.937  1.00 25.13 ? 144 ASP   B O   1 
ATOM   1883 C CB  . ASP   B 1 127 ? -28.283 -34.260 -8.014  1.00 19.82 ? 144 ASP   B CB  1 
ATOM   1884 C CG  . ASP   B 1 127 ? -28.736 -32.854 -7.743  1.00 23.61 ? 144 ASP   B CG  1 
ATOM   1885 O OD1 . ASP   B 1 127 ? -27.876 -32.004 -7.484  1.00 22.06 ? 144 ASP   B OD1 1 
ATOM   1886 O OD2 . ASP   B 1 127 ? -29.954 -32.589 -7.777  1.00 27.56 ? 144 ASP   B OD2 1 
ATOM   1887 N N   . TYR   B 1 128 ? -26.019 -36.208 -9.446  1.00 20.99 ? 145 TYR   B N   1 
ATOM   1888 C CA  . TYR   B 1 128 ? -25.583 -37.583 -9.684  1.00 23.12 ? 145 TYR   B CA  1 
ATOM   1889 C C   . TYR   B 1 128 ? -24.368 -37.941 -8.831  1.00 22.97 ? 145 TYR   B C   1 
ATOM   1890 O O   . TYR   B 1 128 ? -23.618 -37.069 -8.376  1.00 21.44 ? 145 TYR   B O   1 
ATOM   1891 C CB  . TYR   B 1 128 ? -25.262 -37.819 -11.166 1.00 21.52 ? 145 TYR   B CB  1 
ATOM   1892 C CG  . TYR   B 1 128 ? -23.921 -37.270 -11.596 1.00 21.46 ? 145 TYR   B CG  1 
ATOM   1893 C CD1 . TYR   B 1 128 ? -23.734 -35.896 -11.763 1.00 21.75 ? 145 TYR   B CD1 1 
ATOM   1894 C CD2 . TYR   B 1 128 ? -22.848 -38.110 -11.818 1.00 22.69 ? 145 TYR   B CD2 1 
ATOM   1895 C CE1 . TYR   B 1 128 ? -22.512 -35.398 -12.146 1.00 20.71 ? 145 TYR   B CE1 1 
ATOM   1896 C CE2 . TYR   B 1 128 ? -21.627 -37.625 -12.197 1.00 22.15 ? 145 TYR   B CE2 1 
ATOM   1897 C CZ  . TYR   B 1 128 ? -21.458 -36.272 -12.359 1.00 21.28 ? 145 TYR   B CZ  1 
ATOM   1898 O OH  . TYR   B 1 128 ? -20.222 -35.799 -12.744 1.00 22.84 ? 145 TYR   B OH  1 
ATOM   1899 N N   . GLU   B 1 129 ? -24.173 -39.246 -8.629  1.00 25.29 ? 146 GLU   B N   1 
ATOM   1900 C CA  . GLU   B 1 129 ? -22.969 -39.769 -7.996  1.00 28.00 ? 146 GLU   B CA  1 
ATOM   1901 C C   . GLU   B 1 129 ? -21.992 -40.231 -9.069  1.00 28.01 ? 146 GLU   B C   1 
ATOM   1902 O O   . GLU   B 1 129 ? -22.398 -40.824 -10.070 1.00 29.72 ? 146 GLU   B O   1 
ATOM   1903 C CB  . GLU   B 1 129 ? -23.276 -40.928 -7.042  1.00 32.21 ? 146 GLU   B CB  1 
ATOM   1904 C CG  . GLU   B 1 129 ? -24.118 -40.534 -5.839  1.00 36.16 ? 146 GLU   B CG  1 
ATOM   1905 C CD  . GLU   B 1 129 ? -24.733 -41.727 -5.132  1.00 50.81 ? 146 GLU   B CD  1 
ATOM   1906 O OE1 . GLU   B 1 129 ? -25.234 -41.551 -3.998  1.00 58.47 ? 146 GLU   B OE1 1 
ATOM   1907 O OE2 . GLU   B 1 129 ? -24.698 -42.844 -5.697  1.00 55.14 ? 146 GLU   B OE2 1 
ATOM   1908 N N   . GLU   B 1 130 ? -20.698 -39.983 -8.836  1.00 28.10 ? 147 GLU   B N   1 
ATOM   1909 C CA  . GLU   B 1 130 ? -19.693 -40.132 -9.889  1.00 27.85 ? 147 GLU   B CA  1 
ATOM   1910 C C   . GLU   B 1 130 ? -19.719 -41.522 -10.520 1.00 31.60 ? 147 GLU   B C   1 
ATOM   1911 O O   . GLU   B 1 130 ? -19.519 -41.667 -11.732 1.00 32.10 ? 147 GLU   B O   1 
ATOM   1912 C CB  . GLU   B 1 130 ? -18.311 -39.759 -9.310  1.00 29.38 ? 147 GLU   B CB  1 
ATOM   1913 C CG  . GLU   B 1 130 ? -17.646 -40.698 -8.279  1.00 35.22 ? 147 GLU   B CG  1 
ATOM   1914 C CD  . GLU   B 1 130 ? -17.169 -42.055 -8.802  0.77 36.38 ? 147 GLU   B CD  1 
ATOM   1915 O OE1 . GLU   B 1 130 ? -17.075 -42.262 -10.032 0.70 35.75 ? 147 GLU   B OE1 1 
ATOM   1916 O OE2 . GLU   B 1 130 ? -16.895 -42.937 -7.961  0.75 38.90 ? 147 GLU   B OE2 1 
ATOM   1917 N N   . GLY   B 1 131 ? -19.988 -42.555 -9.721  1.00 31.85 ? 148 GLY   B N   1 
ATOM   1918 C CA  . GLY   B 1 131 ? -19.968 -43.909 -10.242 1.00 34.12 ? 148 GLY   B CA  1 
ATOM   1919 C C   . GLY   B 1 131 ? -21.047 -44.203 -11.260 1.00 35.75 ? 148 GLY   B C   1 
ATOM   1920 O O   . GLY   B 1 131 ? -20.937 -45.201 -11.977 1.00 37.28 ? 148 GLY   B O   1 
ATOM   1921 N N   . GLU   B 1 132 ? -22.089 -43.373 -11.339 1.00 33.56 ? 149 GLU   B N   1 
ATOM   1922 C CA  . GLU   B 1 132 ? -23.235 -43.665 -12.193 1.00 35.53 ? 149 GLU   B CA  1 
ATOM   1923 C C   . GLU   B 1 132 ? -23.305 -42.782 -13.430 1.00 32.13 ? 149 GLU   B C   1 
ATOM   1924 O O   . GLU   B 1 132 ? -24.314 -42.828 -14.144 1.00 31.87 ? 149 GLU   B O   1 
ATOM   1925 C CB  . GLU   B 1 132 ? -24.547 -43.542 -11.410 1.00 37.37 ? 149 GLU   B CB  1 
ATOM   1926 C CG  . GLU   B 1 132 ? -25.012 -42.122 -11.159 1.00 36.66 ? 149 GLU   B CG  1 
ATOM   1927 C CD  . GLU   B 1 132 ? -25.964 -42.007 -9.975  1.00 43.62 ? 149 GLU   B CD  1 
ATOM   1928 O OE1 . GLU   B 1 132 ? -26.391 -40.874 -9.665  1.00 34.25 ? 149 GLU   B OE1 1 
ATOM   1929 O OE2 . GLU   B 1 132 ? -26.289 -43.049 -9.358  1.00 47.75 ? 149 GLU   B OE2 1 
ATOM   1930 N N   . VAL   B 1 133 ? -22.263 -41.998 -13.721 1.00 30.38 ? 150 VAL   B N   1 
ATOM   1931 C CA  . VAL   B 1 133 ? -22.379 -41.012 -14.794 1.00 31.62 ? 150 VAL   B CA  1 
ATOM   1932 C C   . VAL   B 1 133 ? -22.581 -41.693 -16.146 1.00 30.29 ? 150 VAL   B C   1 
ATOM   1933 O O   . VAL   B 1 133 ? -23.333 -41.195 -16.990 1.00 31.47 ? 150 VAL   B O   1 
ATOM   1934 C CB  . VAL   B 1 133 ? -21.169 -40.055 -14.796 1.00 30.15 ? 150 VAL   B CB  1 
ATOM   1935 C CG1 . VAL   B 1 133 ? -19.937 -40.699 -15.402 1.00 27.46 ? 150 VAL   B CG1 1 
ATOM   1936 C CG2 . VAL   B 1 133 ? -21.511 -38.785 -15.558 1.00 27.03 ? 150 VAL   B CG2 1 
ATOM   1937 N N   . GLU   B 1 134 ? -21.944 -42.847 -16.374 1.00 33.18 ? 151 GLU   B N   1 
ATOM   1938 C CA  . GLU   B 1 134 ? -22.130 -43.519 -17.655 1.00 30.72 ? 151 GLU   B CA  1 
ATOM   1939 C C   . GLU   B 1 134 ? -23.563 -44.012 -17.813 1.00 34.47 ? 151 GLU   B C   1 
ATOM   1940 O O   . GLU   B 1 134 ? -24.137 -43.929 -18.904 1.00 33.65 ? 151 GLU   B O   1 
ATOM   1941 C CB  . GLU   B 1 134 ? -21.145 -44.681 -17.803 1.00 34.93 ? 151 GLU   B CB  1 
ATOM   1942 C CG  . GLU   B 1 134 ? -19.720 -44.259 -18.139 1.00 34.88 ? 151 GLU   B CG  1 
ATOM   1943 C CD  . GLU   B 1 134 ? -18.863 -44.036 -16.904 1.00 36.06 ? 151 GLU   B CD  1 
ATOM   1944 O OE1 . GLU   B 1 134 ? -19.397 -44.140 -15.775 1.00 36.67 ? 151 GLU   B OE1 1 
ATOM   1945 O OE2 . GLU   B 1 134 ? -17.649 -43.769 -17.066 1.00 39.12 ? 151 GLU   B OE2 1 
ATOM   1946 N N   . ALA   B 1 135 ? -24.155 -44.523 -16.733 1.00 31.85 ? 152 ALA   B N   1 
ATOM   1947 C CA  . ALA   B 1 135 ? -25.533 -44.995 -16.797 1.00 36.20 ? 152 ALA   B CA  1 
ATOM   1948 C C   . ALA   B 1 135 ? -26.503 -43.839 -16.991 1.00 30.93 ? 152 ALA   B C   1 
ATOM   1949 O O   . ALA   B 1 135 ? -27.493 -43.968 -17.724 1.00 33.97 ? 152 ALA   B O   1 
ATOM   1950 C CB  . ALA   B 1 135 ? -25.878 -45.778 -15.532 1.00 35.59 ? 152 ALA   B CB  1 
ATOM   1951 N N   . LEU   B 1 136 ? -26.233 -42.703 -16.344 1.00 31.63 ? 153 LEU   B N   1 
ATOM   1952 C CA  . LEU   B 1 136 ? -27.089 -41.538 -16.516 1.00 30.95 ? 153 LEU   B CA  1 
ATOM   1953 C C   . LEU   B 1 136 ? -27.058 -41.064 -17.967 1.00 29.73 ? 153 LEU   B C   1 
ATOM   1954 O O   . LEU   B 1 136 ? -28.099 -40.758 -18.559 1.00 28.42 ? 153 LEU   B O   1 
ATOM   1955 C CB  . LEU   B 1 136 ? -26.638 -40.427 -15.562 1.00 27.14 ? 153 LEU   B CB  1 
ATOM   1956 C CG  . LEU   B 1 136 ? -27.393 -39.095 -15.566 1.00 29.66 ? 153 LEU   B CG  1 
ATOM   1957 C CD1 . LEU   B 1 136 ? -27.244 -38.429 -14.206 1.00 27.79 ? 153 LEU   B CD1 1 
ATOM   1958 C CD2 . LEU   B 1 136 ? -26.974 -38.150 -16.674 1.00 30.08 ? 153 LEU   B CD2 1 
ATOM   1959 N N   . LEU   B 1 137 ? -25.862 -41.000 -18.560 1.00 27.42 ? 154 LEU   B N   1 
ATOM   1960 C CA  . LEU   B 1 137 ? -25.756 -40.605 -19.959 1.00 28.49 ? 154 LEU   B CA  1 
ATOM   1961 C C   . LEU   B 1 137 ? -26.451 -41.613 -20.871 1.00 30.90 ? 154 LEU   B C   1 
ATOM   1962 O O   . LEU   B 1 137 ? -27.136 -41.224 -21.824 1.00 27.51 ? 154 LEU   B O   1 
ATOM   1963 C CB  . LEU   B 1 137 ? -24.286 -40.445 -20.345 1.00 27.63 ? 154 LEU   B CB  1 
ATOM   1964 C CG  . LEU   B 1 137 ? -23.538 -39.286 -19.660 1.00 25.55 ? 154 LEU   B CG  1 
ATOM   1965 C CD1 . LEU   B 1 137 ? -22.044 -39.429 -19.888 1.00 26.12 ? 154 LEU   B CD1 1 
ATOM   1966 C CD2 . LEU   B 1 137 ? -24.019 -37.903 -20.106 1.00 27.07 ? 154 LEU   B CD2 1 
ATOM   1967 N N   . ASP   B 1 138 ? -26.276 -42.913 -20.599 1.00 29.60 ? 155 ASP   B N   1 
ATOM   1968 C CA  . ASP   B 1 138 ? -26.982 -43.942 -21.364 1.00 33.34 ? 155 ASP   B CA  1 
ATOM   1969 C C   . ASP   B 1 138 ? -28.491 -43.732 -21.328 1.00 34.22 ? 155 ASP   B C   1 
ATOM   1970 O O   . ASP   B 1 138 ? -29.177 -43.938 -22.335 1.00 34.27 ? 155 ASP   B O   1 
ATOM   1971 C CB  . ASP   B 1 138 ? -26.643 -45.340 -20.835 1.00 33.34 ? 155 ASP   B CB  1 
ATOM   1972 C CG  . ASP   B 1 138 ? -25.278 -45.837 -21.287 1.00 40.13 ? 155 ASP   B CG  1 
ATOM   1973 O OD1 . ASP   B 1 138 ? -24.656 -45.180 -22.142 1.00 40.41 ? 155 ASP   B OD1 1 
ATOM   1974 O OD2 . ASP   B 1 138 ? -24.839 -46.909 -20.806 1.00 41.72 ? 155 ASP   B OD2 1 
ATOM   1975 N N   . ARG   B 1 139 ? -29.028 -43.332 -20.173 1.00 33.51 ? 156 ARG   B N   1 
ATOM   1976 C CA  . ARG   B 1 139 ? -30.463 -43.095 -20.068 1.00 33.79 ? 156 ARG   B CA  1 
ATOM   1977 C C   . ARG   B 1 139 ? -30.883 -41.880 -20.883 1.00 28.91 ? 156 ARG   B C   1 
ATOM   1978 O O   . ARG   B 1 139 ? -31.865 -41.939 -21.637 1.00 31.86 ? 156 ARG   B O   1 
ATOM   1979 C CB  . ARG   B 1 139 ? -30.866 -42.912 -18.606 1.00 36.62 ? 156 ARG   B CB  1 
ATOM   1980 C CG  . ARG   B 1 139 ? -32.377 -42.834 -18.391 1.00 41.93 ? 156 ARG   B CG  1 
ATOM   1981 C CD  . ARG   B 1 139 ? -32.699 -42.369 -16.975 1.00 39.43 ? 156 ARG   B CD  1 
ATOM   1982 N NE  . ARG   B 1 139 ? -32.373 -40.959 -16.787 1.00 39.51 ? 156 ARG   B NE  1 
ATOM   1983 C CZ  . ARG   B 1 139 ? -31.525 -40.496 -15.880 1.00 41.99 ? 156 ARG   B CZ  1 
ATOM   1984 N NH1 . ARG   B 1 139 ? -30.858 -41.309 -15.072 1.00 48.56 ? 156 ARG   B NH1 1 
ATOM   1985 N NH2 . ARG   B 1 139 ? -31.340 -39.187 -15.778 1.00 32.50 ? 156 ARG   B NH2 1 
ATOM   1986 N N   . TYR   B 1 140 ? -30.152 -40.771 -20.738 1.00 32.61 ? 157 TYR   B N   1 
ATOM   1987 C CA  . TYR   B 1 140 ? -30.515 -39.538 -21.431 1.00 30.11 ? 157 TYR   B CA  1 
ATOM   1988 C C   . TYR   B 1 140 ? -30.472 -39.721 -22.945 1.00 32.88 ? 157 TYR   B C   1 
ATOM   1989 O O   . TYR   B 1 140 ? -31.343 -39.230 -23.669 1.00 29.39 ? 157 TYR   B O   1 
ATOM   1990 C CB  . TYR   B 1 140 ? -29.580 -38.402 -20.991 1.00 24.23 ? 157 TYR   B CB  1 
ATOM   1991 C CG  . TYR   B 1 140 ? -29.924 -37.051 -21.587 1.00 27.32 ? 157 TYR   B CG  1 
ATOM   1992 C CD1 . TYR   B 1 140 ? -29.403 -36.670 -22.817 1.00 27.89 ? 157 TYR   B CD1 1 
ATOM   1993 C CD2 . TYR   B 1 140 ? -30.758 -36.159 -20.924 1.00 25.53 ? 157 TYR   B CD2 1 
ATOM   1994 C CE1 . TYR   B 1 140 ? -29.711 -35.453 -23.385 1.00 25.20 ? 157 TYR   B CE1 1 
ATOM   1995 C CE2 . TYR   B 1 140 ? -31.072 -34.930 -21.488 1.00 23.80 ? 157 TYR   B CE2 1 
ATOM   1996 C CZ  . TYR   B 1 140 ? -30.539 -34.586 -22.712 1.00 26.94 ? 157 TYR   B CZ  1 
ATOM   1997 O OH  . TYR   B 1 140 ? -30.841 -33.374 -23.293 1.00 24.53 ? 157 TYR   B OH  1 
ATOM   1998 N N   . PHE   B 1 141 ? -29.465 -40.429 -23.441 1.00 33.37 ? 158 PHE   B N   1 
ATOM   1999 C CA  . PHE   B 1 141 ? -29.261 -40.598 -24.868 1.00 33.42 ? 158 PHE   B CA  1 
ATOM   2000 C C   . PHE   B 1 141 ? -29.866 -41.894 -25.387 1.00 39.44 ? 158 PHE   B C   1 
ATOM   2001 O O   . PHE   B 1 141 ? -29.604 -42.271 -26.531 1.00 44.49 ? 158 PHE   B O   1 
ATOM   2002 C CB  . PHE   B 1 141 ? -27.762 -40.523 -25.175 1.00 34.63 ? 158 PHE   B CB  1 
ATOM   2003 C CG  . PHE   B 1 141 ? -27.199 -39.130 -25.060 1.00 32.61 ? 158 PHE   B CG  1 
ATOM   2004 C CD1 . PHE   B 1 141 ? -27.447 -38.180 -26.040 1.00 31.67 ? 158 PHE   B CD1 1 
ATOM   2005 C CD2 . PHE   B 1 141 ? -26.486 -38.751 -23.932 1.00 29.08 ? 158 PHE   B CD2 1 
ATOM   2006 C CE1 . PHE   B 1 141 ? -26.940 -36.889 -25.922 1.00 30.60 ? 158 PHE   B CE1 1 
ATOM   2007 C CE2 . PHE   B 1 141 ? -25.993 -37.457 -23.797 1.00 30.53 ? 158 PHE   B CE2 1 
ATOM   2008 C CZ  . PHE   B 1 141 ? -26.218 -36.526 -24.793 1.00 29.30 ? 158 PHE   B CZ  1 
ATOM   2009 N N   . GLU   B 1 142 ? -30.680 -42.565 -24.572 1.00 49.25 ? 159 GLU   B N   1 
ATOM   2010 C CA  . GLU   B 1 142 ? -31.403 -43.774 -24.967 1.00 49.75 ? 159 GLU   B CA  1 
ATOM   2011 C C   . GLU   B 1 142 ? -30.477 -44.851 -25.518 1.00 59.58 ? 159 GLU   B C   1 
ATOM   2012 O O   . GLU   B 1 142 ? -29.853 -45.594 -24.758 1.00 64.73 ? 159 GLU   B O   1 
ATOM   2013 C CB  . GLU   B 1 142 ? -32.486 -43.434 -25.994 1.00 57.79 ? 159 GLU   B CB  1 
ATOM   2014 C CG  . GLU   B 1 142 ? -33.850 -43.104 -25.393 1.00 67.04 ? 159 GLU   B CG  1 
ATOM   2015 C CD  . GLU   B 1 142 ? -33.955 -41.684 -24.877 1.00 61.73 ? 159 GLU   B CD  1 
ATOM   2016 O OE1 . GLU   B 1 142 ? -33.623 -40.750 -25.637 1.00 67.63 ? 159 GLU   B OE1 1 
ATOM   2017 O OE2 . GLU   B 1 142 ? -34.386 -41.501 -23.716 1.00 61.54 ? 159 GLU   B OE2 1 
HETATM 2018 C C12 . A1BBD C 2 .   ? -25.682 -12.784 -8.835  1.00 15.06 ? 201 A1BBD A C12 1 
HETATM 2019 C C11 . A1BBD C 2 .   ? -27.292 -15.902 -7.642  1.00 14.95 ? 201 A1BBD A C11 1 
HETATM 2020 C C10 . A1BBD C 2 .   ? -26.869 -17.753 -5.909  1.00 16.16 ? 201 A1BBD A C10 1 
HETATM 2021 C C01 . A1BBD C 2 .   ? -24.180 -12.896 -9.155  1.00 13.54 ? 201 A1BBD A C01 1 
HETATM 2022 C C02 . A1BBD C 2 .   ? -24.056 -14.356 -9.758  1.00 13.35 ? 201 A1BBD A C02 1 
HETATM 2023 C C03 . A1BBD C 2 .   ? -23.431 -15.323 -8.650  1.00 13.41 ? 201 A1BBD A C03 1 
HETATM 2024 C C04 . A1BBD C 2 .   ? -25.277 -14.795 -10.092 1.00 12.89 ? 201 A1BBD A C04 1 
HETATM 2025 C C05 . A1BBD C 2 .   ? -27.671 -14.038 -9.360  1.00 15.11 ? 201 A1BBD A C05 1 
HETATM 2026 C C06 . A1BBD C 2 .   ? -27.735 -14.594 -7.909  1.00 16.08 ? 201 A1BBD A C06 1 
HETATM 2027 C C07 . A1BBD C 2 .   ? -28.250 -13.802 -6.882  1.00 16.91 ? 201 A1BBD A C07 1 
HETATM 2028 C C08 . A1BBD C 2 .   ? -27.866 -15.486 -5.377  1.00 16.77 ? 201 A1BBD A C08 1 
HETATM 2029 C C09 . A1BBD C 2 .   ? -27.351 -16.348 -6.333  1.00 14.62 ? 201 A1BBD A C09 1 
HETATM 2030 N N01 . A1BBD C 2 .   ? -26.304 -13.578 -9.737  1.00 14.33 ? 201 A1BBD A N01 1 
HETATM 2031 N N02 . A1BBD C 2 .   ? -28.298 -14.259 -5.635  1.00 18.67 ? 201 A1BBD A N02 1 
HETATM 2032 O O01 . A1BBD C 2 .   ? -23.733 -11.972 -10.046 1.00 13.72 ? 201 A1BBD A O01 1 
HETATM 2033 O O02 . A1BBD C 2 .   ? -23.432 -16.614 -9.233  1.00 13.04 ? 201 A1BBD A O02 1 
HETATM 2034 O O03 . A1BBD C 2 .   ? -22.959 -19.037 -9.275  1.00 13.08 ? 201 A1BBD A O03 1 
HETATM 2035 O O04 . A1BBD C 2 .   ? -21.483 -17.555 -7.896  1.00 13.20 ? 201 A1BBD A O04 1 
HETATM 2036 O O05 . A1BBD C 2 .   ? -23.825 -17.940 -7.139  1.00 12.47 ? 201 A1BBD A O05 1 
HETATM 2037 O O06 . A1BBD C 2 .   ? -27.934 -15.921 -4.051  1.00 20.29 ? 201 A1BBD A O06 1 
HETATM 2038 O O07 . A1BBD C 2 .   ? -26.317 -18.455 -7.007  1.00 14.94 ? 201 A1BBD A O07 1 
HETATM 2039 P P01 . A1BBD C 2 .   ? -22.904 -17.864 -8.336  1.00 12.52 ? 201 A1BBD A P01 1 
HETATM 2040 C C12 . A1BBD D 2 .   ? -14.130 -25.177 -22.546 1.00 20.46 ? 201 A1BBD B C12 1 
HETATM 2041 C C11 . A1BBD D 2 .   ? -11.683 -22.463 -22.618 1.00 23.32 ? 201 A1BBD B C11 1 
HETATM 2042 C C10 . A1BBD D 2 .   ? -9.617  -21.682 -21.278 1.00 21.23 ? 201 A1BBD B C10 1 
HETATM 2043 C C01 . A1BBD D 2 .   ? -14.800 -25.470 -21.186 1.00 16.18 ? 201 A1BBD B C01 1 
HETATM 2044 C C02 . A1BBD D 2 .   ? -14.936 -24.016 -20.553 1.00 15.52 ? 201 A1BBD B C02 1 
HETATM 2045 C C03 . A1BBD D 2 .   ? -13.785 -23.853 -19.453 1.00 15.76 ? 201 A1BBD B C03 1 
HETATM 2046 C C04 . A1BBD D 2 .   ? -14.792 -23.111 -21.511 1.00 18.29 ? 201 A1BBD B C04 1 
HETATM 2047 C C05 . A1BBD D 2 .   ? -13.758 -23.245 -23.928 1.00 21.26 ? 201 A1BBD B C05 1 
HETATM 2048 C C06 . A1BBD D 2 .   ? -12.232 -23.305 -23.595 1.00 21.33 ? 201 A1BBD B C06 1 
HETATM 2049 C C07 . A1BBD D 2 .   ? -11.410 -24.195 -24.288 1.00 22.32 ? 201 A1BBD B C07 1 
HETATM 2050 C C08 . A1BBD D 2 .   ? -9.576  -23.474 -23.080 1.00 23.95 ? 201 A1BBD B C08 1 
HETATM 2051 C C09 . A1BBD D 2 .   ? -10.316 -22.560 -22.345 1.00 20.06 ? 201 A1BBD B C09 1 
HETATM 2052 N N01 . A1BBD D 2 .   ? -14.556 -23.959 -22.897 1.00 18.16 ? 201 A1BBD B N01 1 
HETATM 2053 N N02 . A1BBD D 2 .   ? -10.109 -24.255 -24.012 1.00 25.28 ? 201 A1BBD B N02 1 
HETATM 2054 O O01 . A1BBD D 2 .   ? -16.022 -26.049 -21.322 1.00 17.57 ? 201 A1BBD B O01 1 
HETATM 2055 O O02 . A1BBD D 2 .   ? -13.927 -22.504 -19.019 1.00 15.03 ? 201 A1BBD B O02 1 
HETATM 2056 O O03 . A1BBD D 2 .   ? -13.334 -20.571 -17.605 1.00 15.96 ? 201 A1BBD B O03 1 
HETATM 2057 O O04 . A1BBD D 2 .   ? -12.896 -22.833 -16.696 1.00 13.70 ? 201 A1BBD B O04 1 
HETATM 2058 O O05 . A1BBD D 2 .   ? -11.452 -22.042 -18.536 1.00 16.90 ? 201 A1BBD B O05 1 
HETATM 2059 O O06 . A1BBD D 2 .   ? -8.202  -23.554 -22.796 1.00 27.09 ? 201 A1BBD B O06 1 
HETATM 2060 O O07 . A1BBD D 2 .   ? -10.566 -20.852 -20.627 1.00 19.32 ? 201 A1BBD B O07 1 
HETATM 2061 P P01 . A1BBD D 2 .   ? -12.856 -21.962 -17.909 1.00 15.63 ? 201 A1BBD B P01 1 
HETATM 2062 O O   . HOH   E 3 .   ? -24.134 0.422   -1.731  1.00 31.09 ? 301 HOH   A O   1 
HETATM 2063 O O   . HOH   E 3 .   ? -14.843 -20.141 -7.369  1.00 21.94 ? 302 HOH   A O   1 
HETATM 2064 O O   . HOH   E 3 .   ? -6.786  -0.933  -15.391 1.00 29.27 ? 303 HOH   A O   1 
HETATM 2065 O O   . HOH   E 3 .   ? -9.046  -18.702 -13.480 1.00 28.66 ? 304 HOH   A O   1 
HETATM 2066 O O   . HOH   E 3 .   ? -14.322 -11.788 -8.067  1.00 15.59 ? 305 HOH   A O   1 
HETATM 2067 O O   . HOH   E 3 .   ? -11.472 9.240   -10.319 1.00 34.99 ? 306 HOH   A O   1 
HETATM 2068 O O   . HOH   E 3 .   ? -22.720 -7.500  -25.795 1.00 33.16 ? 307 HOH   A O   1 
HETATM 2069 O O   . HOH   E 3 .   ? -25.668 -6.438  -7.236  1.00 26.88 ? 308 HOH   A O   1 
HETATM 2070 O O   . HOH   E 3 .   ? -26.623 -2.045  -22.915 1.00 27.76 ? 309 HOH   A O   1 
HETATM 2071 O O   . HOH   E 3 .   ? -16.532 -12.852 2.207   1.00 23.35 ? 310 HOH   A O   1 
HETATM 2072 O O   . HOH   E 3 .   ? -10.037 -17.034 -4.457  1.00 31.84 ? 311 HOH   A O   1 
HETATM 2073 O O   . HOH   E 3 .   ? -18.118 -1.809  -22.420 1.00 24.57 ? 312 HOH   A O   1 
HETATM 2074 O O   . HOH   E 3 .   ? -4.534  -7.156  -9.909  1.00 21.93 ? 313 HOH   A O   1 
HETATM 2075 O O   . HOH   E 3 .   ? -12.892 -7.741  3.863   1.00 34.35 ? 314 HOH   A O   1 
HETATM 2076 O O   . HOH   E 3 .   ? -20.063 -12.557 -2.796  1.00 18.46 ? 315 HOH   A O   1 
HETATM 2077 O O   . HOH   E 3 .   ? -10.911 -13.917 -6.043  1.00 23.02 ? 316 HOH   A O   1 
HETATM 2078 O O   . HOH   E 3 .   ? -22.906 5.188   -3.064  1.00 20.89 ? 317 HOH   A O   1 
HETATM 2079 O O   . HOH   E 3 .   ? -32.766 2.373   -18.304 1.00 35.06 ? 318 HOH   A O   1 
HETATM 2080 O O   . HOH   E 3 .   ? -16.448 2.352   -3.433  1.00 16.78 ? 319 HOH   A O   1 
HETATM 2081 O O   . HOH   E 3 .   ? -37.046 -3.015  -12.541 1.00 27.99 ? 320 HOH   A O   1 
HETATM 2082 O O   . HOH   E 3 .   ? -8.760  -15.273 -6.807  1.00 30.59 ? 321 HOH   A O   1 
HETATM 2083 O O   . HOH   E 3 .   ? -10.688 -9.221  -2.579  1.00 28.37 ? 322 HOH   A O   1 
HETATM 2084 O O   . HOH   E 3 .   ? -37.028 -8.599  -11.871 1.00 33.01 ? 323 HOH   A O   1 
HETATM 2085 O O   . HOH   E 3 .   ? -13.698 -5.176  -32.146 1.00 30.92 ? 324 HOH   A O   1 
HETATM 2086 O O   . HOH   E 3 .   ? -11.274 -15.606 -13.116 1.00 21.30 ? 325 HOH   A O   1 
HETATM 2087 O O   . HOH   E 3 .   ? -17.611 -4.765  4.082   1.00 18.65 ? 326 HOH   A O   1 
HETATM 2088 O O   . HOH   E 3 .   ? -4.983  -6.351  -7.158  1.00 24.26 ? 327 HOH   A O   1 
HETATM 2089 O O   . HOH   E 3 .   ? -18.702 -22.973 -3.235  1.00 29.09 ? 328 HOH   A O   1 
HETATM 2090 O O   . HOH   E 3 .   ? -22.473 -8.100  0.361   1.00 23.43 ? 329 HOH   A O   1 
HETATM 2091 O O   . HOH   E 3 .   ? -26.528 -10.042 -10.289 1.00 25.85 ? 330 HOH   A O   1 
HETATM 2092 O O   . HOH   E 3 .   ? -37.332 -13.627 -16.707 1.00 31.52 ? 331 HOH   A O   1 
HETATM 2093 O O   . HOH   E 3 .   ? -16.896 -13.397 -9.851  1.00 14.81 ? 332 HOH   A O   1 
HETATM 2094 O O   . HOH   E 3 .   ? -6.092  -15.207 -5.269  1.00 35.03 ? 333 HOH   A O   1 
HETATM 2095 O O   . HOH   E 3 .   ? -20.826 -19.252 -1.137  1.00 26.55 ? 334 HOH   A O   1 
HETATM 2096 O O   . HOH   E 3 .   ? -20.844 -20.849 -9.346  1.00 13.79 ? 335 HOH   A O   1 
HETATM 2097 O O   . HOH   E 3 .   ? -15.937 -13.744 -4.508  1.00 16.16 ? 336 HOH   A O   1 
HETATM 2098 O O   . HOH   E 3 .   ? -29.845 -14.001 -23.657 1.00 21.29 ? 337 HOH   A O   1 
HETATM 2099 O O   . HOH   E 3 .   ? -5.715  -13.568 -17.306 1.00 23.70 ? 338 HOH   A O   1 
HETATM 2100 O O   . HOH   E 3 .   ? -6.847  -14.683 -19.938 1.00 22.26 ? 339 HOH   A O   1 
HETATM 2101 O O   . HOH   E 3 .   ? -24.290 -10.574 5.679   1.00 37.66 ? 340 HOH   A O   1 
HETATM 2102 O O   . HOH   E 3 .   ? -9.587  -9.175  -24.229 1.00 35.24 ? 341 HOH   A O   1 
HETATM 2103 O O   . HOH   E 3 .   ? -14.450 -20.559 -3.473  1.00 24.91 ? 342 HOH   A O   1 
HETATM 2104 O O   . HOH   E 3 .   ? -22.581 -10.556 -6.293  1.00 17.52 ? 343 HOH   A O   1 
HETATM 2105 O O   . HOH   E 3 .   ? -14.060 -9.805  0.787   1.00 22.18 ? 344 HOH   A O   1 
HETATM 2106 O O   . HOH   E 3 .   ? -5.117  -0.756  -11.737 1.00 24.46 ? 345 HOH   A O   1 
HETATM 2107 O O   . HOH   E 3 .   ? -36.263 -18.938 -18.380 1.00 34.60 ? 346 HOH   A O   1 
HETATM 2108 O O   . HOH   E 3 .   ? -28.452 -7.895  -3.894  1.00 41.73 ? 347 HOH   A O   1 
HETATM 2109 O O   . HOH   E 3 .   ? -29.144 1.584   -6.649  1.00 31.76 ? 348 HOH   A O   1 
HETATM 2110 O O   . HOH   E 3 .   ? -18.972 -10.589 -27.379 1.00 33.86 ? 349 HOH   A O   1 
HETATM 2111 O O   . HOH   E 3 .   ? -22.173 -1.634  -1.074  1.00 22.18 ? 350 HOH   A O   1 
HETATM 2112 O O   . HOH   E 3 .   ? -16.737 -17.918 0.472   1.00 27.40 ? 351 HOH   A O   1 
HETATM 2113 O O   . HOH   E 3 .   ? -27.184 -18.243 -2.380  1.00 31.58 ? 352 HOH   A O   1 
HETATM 2114 O O   . HOH   E 3 .   ? -24.772 -9.319  -7.760  1.00 24.07 ? 353 HOH   A O   1 
HETATM 2115 O O   . HOH   E 3 .   ? -32.735 -14.971 -24.694 1.00 29.17 ? 354 HOH   A O   1 
HETATM 2116 O O   . HOH   E 3 .   ? -11.904 -4.144  -0.729  1.00 29.11 ? 355 HOH   A O   1 
HETATM 2117 O O   . HOH   E 3 .   ? -9.805  3.985   -6.778  1.00 27.43 ? 356 HOH   A O   1 
HETATM 2118 O O   . HOH   E 3 .   ? -17.694 3.965   -21.421 1.00 37.88 ? 357 HOH   A O   1 
HETATM 2119 O O   . HOH   E 3 .   ? -11.200 -17.679 -14.849 1.00 18.18 ? 358 HOH   A O   1 
HETATM 2120 O O   . HOH   E 3 .   ? -6.450  -19.708 -12.928 1.00 32.32 ? 359 HOH   A O   1 
HETATM 2121 O O   . HOH   E 3 .   ? -4.080  -2.137  -5.517  1.00 30.87 ? 360 HOH   A O   1 
HETATM 2122 O O   . HOH   E 3 .   ? -33.997 -18.884 -19.898 1.00 29.06 ? 361 HOH   A O   1 
HETATM 2123 O O   . HOH   E 3 .   ? -23.587 -3.963  -1.411  1.00 27.86 ? 362 HOH   A O   1 
HETATM 2124 O O   . HOH   E 3 .   ? -15.580 10.348  -3.334  1.00 26.95 ? 363 HOH   A O   1 
HETATM 2125 O O   . HOH   E 3 .   ? -22.656 -15.556 2.883   1.00 35.20 ? 364 HOH   A O   1 
HETATM 2126 O O   . HOH   E 3 .   ? -18.957 -13.213 3.496   1.00 29.94 ? 365 HOH   A O   1 
HETATM 2127 O O   . HOH   E 3 .   ? -11.597 -4.940  -23.863 1.00 27.19 ? 366 HOH   A O   1 
HETATM 2128 O O   . HOH   E 3 .   ? -36.123 -23.333 -7.818  1.00 33.07 ? 367 HOH   A O   1 
HETATM 2129 O O   . HOH   E 3 .   ? -6.427  -4.520  -19.480 1.00 30.12 ? 368 HOH   A O   1 
HETATM 2130 O O   . HOH   E 3 .   ? -18.374 0.000   0.000   0.50 17.61 ? 369 HOH   A O   1 
HETATM 2131 O O   . HOH   E 3 .   ? -16.938 -2.227  0.715   1.00 17.81 ? 370 HOH   A O   1 
HETATM 2132 O O   . HOH   E 3 .   ? -21.891 -10.417 -3.244  1.00 21.09 ? 371 HOH   A O   1 
HETATM 2133 O O   . HOH   E 3 .   ? -27.071 -14.098 -1.747  1.00 35.55 ? 372 HOH   A O   1 
HETATM 2134 O O   . HOH   E 3 .   ? -12.641 -8.173  -1.165  1.00 23.73 ? 373 HOH   A O   1 
HETATM 2135 O O   . HOH   E 3 .   ? -34.686 -24.057 -5.777  1.00 35.05 ? 374 HOH   A O   1 
HETATM 2136 O O   . HOH   E 3 .   ? -8.020  -8.126  -22.444 1.00 32.56 ? 375 HOH   A O   1 
HETATM 2137 O O   . HOH   E 3 .   ? -11.635 2.408   -1.435  1.00 30.02 ? 376 HOH   A O   1 
HETATM 2138 O O   . HOH   E 3 .   ? -38.407 -24.084 -8.192  1.00 41.26 ? 377 HOH   A O   1 
HETATM 2139 O O   . HOH   E 3 .   ? -9.302  -13.514 -3.460  1.00 31.89 ? 378 HOH   A O   1 
HETATM 2140 O O   . HOH   E 3 .   ? -10.682 0.000   0.000   0.50 31.82 ? 379 HOH   A O   1 
HETATM 2141 O O   . HOH   E 3 .   ? -15.417 -20.413 -0.696  1.00 35.72 ? 380 HOH   A O   1 
HETATM 2142 O O   . HOH   E 3 .   ? -31.330 -13.706 -26.098 1.00 32.04 ? 381 HOH   A O   1 
HETATM 2143 O O   . HOH   E 3 .   ? -22.552 -21.566 -1.357  1.00 26.67 ? 382 HOH   A O   1 
HETATM 2144 O O   . HOH   E 3 .   ? -24.166 3.581   -1.404  1.00 31.69 ? 383 HOH   A O   1 
HETATM 2145 O O   . HOH   E 3 .   ? -10.250 -6.642  -25.501 1.00 34.58 ? 384 HOH   A O   1 
HETATM 2146 O O   . HOH   E 3 .   ? -25.101 -7.869  -0.234  1.00 36.82 ? 385 HOH   A O   1 
HETATM 2147 O O   . HOH   E 3 .   ? -7.020  0.565   -13.156 1.00 28.08 ? 386 HOH   A O   1 
HETATM 2148 O O   . HOH   E 3 .   ? -24.975 -18.129 -0.492  1.00 44.57 ? 387 HOH   A O   1 
HETATM 2149 O O   . HOH   F 3 .   ? -13.102 -38.912 -23.819 1.00 46.26 ? 301 HOH   B O   1 
HETATM 2150 O O   . HOH   F 3 .   ? -14.533 -26.410 -25.713 1.00 33.62 ? 302 HOH   B O   1 
HETATM 2151 O O   . HOH   F 3 .   ? -15.617 -34.683 -5.406  1.00 30.47 ? 303 HOH   B O   1 
HETATM 2152 O O   . HOH   F 3 .   ? -13.405 -23.000 -9.490  1.00 23.41 ? 304 HOH   B O   1 
HETATM 2153 O O   . HOH   F 3 .   ? -19.413 -38.550 -36.215 1.00 36.92 ? 305 HOH   B O   1 
HETATM 2154 O O   . HOH   F 3 .   ? -34.146 -36.780 -18.989 1.00 29.87 ? 306 HOH   B O   1 
HETATM 2155 O O   . HOH   F 3 .   ? -30.635 -28.394 -29.796 1.00 30.87 ? 307 HOH   B O   1 
HETATM 2156 O O   . HOH   F 3 .   ? -16.752 -29.987 -12.547 1.00 16.63 ? 308 HOH   B O   1 
HETATM 2157 O O   . HOH   F 3 .   ? -16.673 -30.590 -26.807 1.00 30.14 ? 309 HOH   B O   1 
HETATM 2158 O O   . HOH   F 3 .   ? -7.680  -34.247 -19.626 1.00 33.84 ? 310 HOH   B O   1 
HETATM 2159 O O   . HOH   F 3 .   ? -32.061 -31.509 -21.805 1.00 21.79 ? 311 HOH   B O   1 
HETATM 2160 O O   . HOH   F 3 .   ? -15.200 -30.078 -8.379  1.00 21.29 ? 312 HOH   B O   1 
HETATM 2161 O O   . HOH   F 3 .   ? -7.965  -38.698 -11.207 1.00 32.99 ? 313 HOH   B O   1 
HETATM 2162 O O   . HOH   F 3 .   ? -13.181 -35.491 -9.644  1.00 32.18 ? 314 HOH   B O   1 
HETATM 2163 O O   . HOH   F 3 .   ? -16.575 -43.409 -19.892 1.00 29.21 ? 315 HOH   B O   1 
HETATM 2164 O O   . HOH   F 3 .   ? -15.280 -15.191 -35.896 1.00 42.66 ? 316 HOH   B O   1 
HETATM 2165 O O   . HOH   F 3 .   ? -6.388  -32.462 -12.329 1.00 29.17 ? 317 HOH   B O   1 
HETATM 2166 O O   . HOH   F 3 .   ? -21.153 -23.596 -5.750  1.00 16.45 ? 318 HOH   B O   1 
HETATM 2167 O O   . HOH   F 3 .   ? -23.728 -30.534 -1.901  1.00 26.60 ? 319 HOH   B O   1 
HETATM 2168 O O   . HOH   F 3 .   ? -17.758 -37.147 -6.535  1.00 23.93 ? 320 HOH   B O   1 
HETATM 2169 O O   . HOH   F 3 .   ? -13.829 -31.664 -28.203 1.00 38.11 ? 321 HOH   B O   1 
HETATM 2170 O O   . HOH   F 3 .   ? -28.802 -39.277 -10.549 1.00 32.16 ? 322 HOH   B O   1 
HETATM 2171 O O   . HOH   F 3 .   ? -10.095 -29.562 -16.745 1.00 20.36 ? 323 HOH   B O   1 
HETATM 2172 O O   . HOH   F 3 .   ? -17.546 -45.226 -21.546 1.00 39.94 ? 324 HOH   B O   1 
HETATM 2173 O O   . HOH   F 3 .   ? -17.465 -27.882 -0.839  1.00 24.58 ? 325 HOH   B O   1 
HETATM 2174 O O   . HOH   F 3 .   ? -13.357 -19.673 -14.985 1.00 14.74 ? 326 HOH   B O   1 
HETATM 2175 O O   . HOH   F 3 .   ? -25.800 -32.992 -36.326 1.00 33.80 ? 327 HOH   B O   1 
HETATM 2176 O O   . HOH   F 3 .   ? -20.905 -25.732 -8.857  1.00 18.94 ? 328 HOH   B O   1 
HETATM 2177 O O   . HOH   F 3 .   ? -28.787 -25.270 -6.279  1.00 21.45 ? 329 HOH   B O   1 
HETATM 2178 O O   . HOH   F 3 .   ? -9.429  -35.373 -12.171 1.00 24.35 ? 330 HOH   B O   1 
HETATM 2179 O O   . HOH   F 3 .   ? -17.188 -27.098 -14.468 1.00 16.58 ? 331 HOH   B O   1 
HETATM 2180 O O   . HOH   F 3 .   ? -20.718 -25.425 0.338   1.00 27.29 ? 332 HOH   B O   1 
HETATM 2181 O O   . HOH   F 3 .   ? -23.537 -28.377 1.223   1.00 27.40 ? 333 HOH   B O   1 
HETATM 2182 O O   . HOH   F 3 .   ? -30.486 -24.140 -32.160 0.50 27.19 ? 334 HOH   B O   1 
HETATM 2183 O O   . HOH   F 3 .   ? -6.336  -24.270 -14.671 1.00 28.97 ? 335 HOH   B O   1 
HETATM 2184 O O   . HOH   F 3 .   ? -4.516  -31.254 -14.374 1.00 31.87 ? 336 HOH   B O   1 
HETATM 2185 O O   . HOH   F 3 .   ? -34.365 -24.121 -26.987 1.00 34.43 ? 337 HOH   B O   1 
HETATM 2186 O O   . HOH   F 3 .   ? -6.311  -22.710 -20.856 1.00 29.82 ? 338 HOH   B O   1 
HETATM 2187 O O   . HOH   F 3 .   ? -26.052 -16.917 -27.687 1.00 23.06 ? 339 HOH   B O   1 
HETATM 2188 O O   . HOH   F 3 .   ? -22.388 -36.819 -5.817  1.00 21.02 ? 340 HOH   B O   1 
HETATM 2189 O O   . HOH   F 3 .   ? -12.485 -29.393 -12.882 1.00 18.63 ? 341 HOH   B O   1 
HETATM 2190 O O   . HOH   F 3 .   ? -13.404 -29.135 -20.413 1.00 25.72 ? 342 HOH   B O   1 
HETATM 2191 O O   . HOH   F 3 .   ? -32.157 -29.759 -10.650 1.00 29.64 ? 343 HOH   B O   1 
HETATM 2192 O O   . HOH   F 3 .   ? -6.505  -27.070 -11.191 1.00 26.24 ? 344 HOH   B O   1 
HETATM 2193 O O   . HOH   F 3 .   ? -10.333 -33.911 -19.214 1.00 25.31 ? 345 HOH   B O   1 
HETATM 2194 O O   . HOH   F 3 .   ? -20.154 -38.434 -6.445  1.00 23.83 ? 346 HOH   B O   1 
HETATM 2195 O O   . HOH   F 3 .   ? -11.155 -41.012 -17.224 1.00 32.35 ? 347 HOH   B O   1 
HETATM 2196 O O   . HOH   F 3 .   ? -27.026 -27.694 -5.072  1.00 20.51 ? 348 HOH   B O   1 
HETATM 2197 O O   . HOH   F 3 .   ? -17.750 -17.336 -33.672 1.00 37.96 ? 349 HOH   B O   1 
HETATM 2198 O O   . HOH   F 3 .   ? -34.776 -24.205 -22.047 1.00 35.46 ? 350 HOH   B O   1 
HETATM 2199 O O   . HOH   F 3 .   ? -14.542 -28.763 -23.129 1.00 29.23 ? 351 HOH   B O   1 
HETATM 2200 O O   . HOH   F 3 .   ? -21.265 -23.837 -2.151  1.00 21.35 ? 352 HOH   B O   1 
HETATM 2201 O O   . HOH   F 3 .   ? -21.921 -23.328 -8.304  1.00 13.35 ? 353 HOH   B O   1 
HETATM 2202 O O   . HOH   F 3 .   ? -10.357 -31.041 -18.971 1.00 23.42 ? 354 HOH   B O   1 
HETATM 2203 O O   . HOH   F 3 .   ? -33.472 -27.477 -11.253 1.00 29.90 ? 355 HOH   B O   1 
HETATM 2204 O O   . HOH   F 3 .   ? -9.694  -24.256 -8.598  1.00 29.67 ? 356 HOH   B O   1 
HETATM 2205 O O   . HOH   F 3 .   ? -33.980 -30.117 -14.630 1.00 24.81 ? 357 HOH   B O   1 
HETATM 2206 O O   . HOH   F 3 .   ? -40.325 -27.399 -19.672 1.00 30.61 ? 358 HOH   B O   1 
HETATM 2207 O O   . HOH   F 3 .   ? -33.581 -37.950 -26.652 1.00 39.39 ? 359 HOH   B O   1 
HETATM 2208 O O   . HOH   F 3 .   ? -11.704 -25.906 -5.993  1.00 37.34 ? 360 HOH   B O   1 
HETATM 2209 O O   . HOH   F 3 .   ? -16.104 -33.153 -0.794  1.00 26.59 ? 361 HOH   B O   1 
HETATM 2210 O O   . HOH   F 3 .   ? -11.970 -36.497 -11.750 1.00 29.15 ? 362 HOH   B O   1 
HETATM 2211 O O   . HOH   F 3 .   ? -19.931 -12.774 -28.985 1.00 27.62 ? 363 HOH   B O   1 
HETATM 2212 O O   . HOH   F 3 .   ? -26.046 -14.582 -29.979 1.00 35.52 ? 364 HOH   B O   1 
HETATM 2213 O O   . HOH   F 3 .   ? -33.503 -21.596 -19.652 1.00 34.41 ? 365 HOH   B O   1 
HETATM 2214 O O   . HOH   F 3 .   ? -31.198 -37.243 -26.170 1.00 33.05 ? 366 HOH   B O   1 
HETATM 2215 O O   . HOH   F 3 .   ? -32.538 -24.639 -23.085 1.00 31.63 ? 367 HOH   B O   1 
HETATM 2216 O O   . HOH   F 3 .   ? -13.341 -31.936 -6.990  1.00 38.10 ? 368 HOH   B O   1 
HETATM 2217 O O   . HOH   F 3 .   ? -11.925 -42.058 -20.022 1.00 36.13 ? 369 HOH   B O   1 
HETATM 2218 O O   . HOH   F 3 .   ? -30.486 -26.936 -32.160 0.50 29.92 ? 370 HOH   B O   1 
HETATM 2219 O O   . HOH   F 3 .   ? -33.960 -33.145 -13.612 1.00 30.57 ? 371 HOH   B O   1 
HETATM 2220 O O   . HOH   F 3 .   ? -12.042 -34.320 -21.634 1.00 34.65 ? 372 HOH   B O   1 
HETATM 2221 O O   . HOH   F 3 .   ? -25.028 -34.042 -0.417  1.00 36.54 ? 373 HOH   B O   1 
HETATM 2222 O O   . HOH   F 3 .   ? -35.822 -34.701 -23.538 1.00 27.22 ? 374 HOH   B O   1 
HETATM 2223 O O   . HOH   F 3 .   ? -23.417 -38.042 -3.484  1.00 31.81 ? 375 HOH   B O   1 
HETATM 2224 O O   . HOH   F 3 .   ? -14.711 -31.434 -24.736 1.00 34.28 ? 376 HOH   B O   1 
HETATM 2225 O O   . HOH   F 3 .   ? -13.010 -22.026 -7.303  1.00 29.97 ? 377 HOH   B O   1 
HETATM 2226 O O   . HOH   F 3 .   ? -7.489  -22.995 -10.055 1.00 39.40 ? 378 HOH   B O   1 
HETATM 2227 O O   . HOH   F 3 .   ? -21.773 -40.006 -2.536  1.00 30.73 ? 379 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 3   ? 0.5164 0.2927 0.4430 0.0459  -0.1073 0.0189  20  ARG A N   
2    C CA  . ARG A 3   ? 0.4778 0.2785 0.4059 0.0412  -0.0878 0.0133  20  ARG A CA  
3    C C   . ARG A 3   ? 0.4455 0.2678 0.3860 0.0371  -0.0884 0.0152  20  ARG A C   
4    O O   . ARG A 3   ? 0.4707 0.3054 0.4409 0.0449  -0.0963 0.0178  20  ARG A O   
5    C CB  . ARG A 3   ? 0.4997 0.3159 0.4520 0.0532  -0.0733 0.0067  20  ARG A CB  
6    C CG  . ARG A 3   ? 0.5612 0.3567 0.4939 0.0544  -0.0678 0.0025  20  ARG A CG  
7    C CD  . ARG A 3   ? 0.5873 0.3927 0.5427 0.0683  -0.0550 -0.0040 20  ARG A CD  
8    N NE  . ARG A 3   ? 0.5625 0.3927 0.5261 0.0672  -0.0384 -0.0085 20  ARG A NE  
9    C CZ  . ARG A 3   ? 0.5424 0.3716 0.4843 0.0596  -0.0281 -0.0128 20  ARG A CZ  
10   N NH1 . ARG A 3   ? 0.5782 0.3855 0.4911 0.0516  -0.0312 -0.0136 20  ARG A NH1 
11   N NH2 . ARG A 3   ? 0.5376 0.3877 0.4877 0.0594  -0.0153 -0.0161 20  ARG A NH2 
12   N N   . PRO A 4   ? 0.4183 0.2447 0.3378 0.0251  -0.0806 0.0140  21  PRO A N   
13   C CA  . PRO A 4   ? 0.3845 0.2267 0.3109 0.0206  -0.0822 0.0156  21  PRO A CA  
14   C C   . PRO A 4   ? 0.3966 0.2699 0.3555 0.0276  -0.0710 0.0122  21  PRO A C   
15   O O   . PRO A 4   ? 0.3971 0.2803 0.3646 0.0327  -0.0575 0.0073  21  PRO A O   
16   C CB  . PRO A 4   ? 0.4129 0.2481 0.3068 0.0065  -0.0746 0.0140  21  PRO A CB  
17   C CG  . PRO A 4   ? 0.4216 0.2573 0.3103 0.0066  -0.0615 0.0089  21  PRO A CG  
18   C CD  . PRO A 4   ? 0.4617 0.2803 0.3538 0.0152  -0.0694 0.0104  21  PRO A CD  
19   N N   . ALA A 5   ? 0.3320 0.2180 0.3070 0.0272  -0.0775 0.0151  22  ALA A N   
20   C CA  . ALA A 5   ? 0.2989 0.2127 0.2986 0.0298  -0.0667 0.0126  22  ALA A CA  
21   C C   . ALA A 5   ? 0.3098 0.2274 0.2878 0.0194  -0.0582 0.0100  22  ALA A C   
22   O O   . ALA A 5   ? 0.3302 0.2346 0.2851 0.0105  -0.0652 0.0119  22  ALA A O   
23   C CB  . ALA A 5   ? 0.3175 0.2424 0.3461 0.0332  -0.0787 0.0172  22  ALA A CB  
24   N N   . LEU A 6   ? 0.2638 0.1976 0.2483 0.0207  -0.0431 0.0054  23  LEU A N   
25   C CA  . LEU A 6   ? 0.2668 0.2045 0.2342 0.0124  -0.0347 0.0022  23  LEU A CA  
26   C C   . LEU A 6   ? 0.2537 0.2124 0.2389 0.0134  -0.0288 0.0013  23  LEU A C   
27   O O   . LEU A 6   ? 0.2794 0.2511 0.2880 0.0206  -0.0244 0.0016  23  LEU A O   
28   C CB  . LEU A 6   ? 0.2603 0.1931 0.2138 0.0112  -0.0247 -0.0024 23  LEU A CB  
29   C CG  . LEU A 6   ? 0.3104 0.2211 0.2475 0.0104  -0.0303 -0.0014 23  LEU A CG  
30   C CD1 . LEU A 6   ? 0.3166 0.2227 0.2440 0.0101  -0.0215 -0.0059 23  LEU A CD1 
31   C CD2 . LEU A 6   ? 0.3207 0.2165 0.2338 -0.0003 -0.0365 0.0009  23  LEU A CD2 
32   N N   . TYR A 7   ? 0.2325 0.1931 0.2063 0.0060  -0.0281 0.0003  24  TYR A N   
33   C CA  . TYR A 7   ? 0.2071 0.1838 0.1932 0.0057  -0.0239 -0.0003 24  TYR A CA  
34   C C   . TYR A 7   ? 0.2091 0.1881 0.1816 0.0012  -0.0146 -0.0051 24  TYR A C   
35   O O   . TYR A 7   ? 0.2519 0.2215 0.2062 -0.0052 -0.0151 -0.0067 24  TYR A O   
36   C CB  . TYR A 7   ? 0.2040 0.1780 0.1893 0.0012  -0.0343 0.0028  24  TYR A CB  
37   C CG  . TYR A 7   ? 0.2204 0.2095 0.2213 0.0012  -0.0321 0.0031  24  TYR A CG  
38   C CD1 . TYR A 7   ? 0.2151 0.2076 0.2061 -0.0028 -0.0255 -0.0005 24  TYR A CD1 
39   C CD2 . TYR A 7   ? 0.2245 0.2221 0.2495 0.0040  -0.0390 0.0074  24  TYR A CD2 
40   C CE1 . TYR A 7   ? 0.2141 0.2171 0.2169 -0.0033 -0.0247 0.0001  24  TYR A CE1 
41   C CE2 . TYR A 7   ? 0.2190 0.2283 0.2570 0.0024  -0.0377 0.0082  24  TYR A CE2 
42   C CZ  . TYR A 7   ? 0.1988 0.2094 0.2235 -0.0013 -0.0306 0.0046  24  TYR A CZ  
43   O OH  . TYR A 7   ? 0.2170 0.2363 0.2523 -0.0032 -0.0301 0.0057  24  TYR A OH  
44   N N   . PHE A 8   ? 0.1908 0.1810 0.1718 0.0042  -0.0063 -0.0073 25  PHE A N   
45   C CA  . PHE A 8   ? 0.1741 0.1668 0.1458 0.0006  -0.0003 -0.0115 25  PHE A CA  
46   C C   . PHE A 8   ? 0.1792 0.1818 0.1575 -0.0007 0.0006  -0.0117 25  PHE A C   
47   O O   . PHE A 8   ? 0.2009 0.2112 0.1923 0.0025  0.0013  -0.0093 25  PHE A O   
48   C CB  . PHE A 8   ? 0.1965 0.1890 0.1664 0.0040  0.0062  -0.0141 25  PHE A CB  
49   C CG  . PHE A 8   ? 0.1888 0.1843 0.1526 0.0005  0.0092  -0.0179 25  PHE A CG  
50   C CD1 . PHE A 8   ? 0.1947 0.1859 0.1498 -0.0052 0.0087  -0.0207 25  PHE A CD1 
51   C CD2 . PHE A 8   ? 0.2033 0.2058 0.1719 0.0023  0.0119  -0.0182 25  PHE A CD2 
52   C CE1 . PHE A 8   ? 0.2181 0.2142 0.1739 -0.0079 0.0102  -0.0243 25  PHE A CE1 
53   C CE2 . PHE A 8   ? 0.1967 0.2010 0.1616 -0.0003 0.0118  -0.0214 25  PHE A CE2 
54   C CZ  . PHE A 8   ? 0.2139 0.2163 0.1749 -0.0050 0.0105  -0.0246 25  PHE A CZ  
55   N N   . CYS A 9   ? 0.1736 0.1757 0.1437 -0.0054 0.0015  -0.0150 26  CYS A N   
56   C CA  . CYS A 9   ? 0.1676 0.1765 0.1423 -0.0063 0.0018  -0.0160 26  CYS A CA  
57   C C   . CYS A 9   ? 0.1743 0.1870 0.1482 -0.0066 0.0059  -0.0203 26  CYS A C   
58   O O   . CYS A 9   ? 0.1989 0.2091 0.1674 -0.0096 0.0079  -0.0236 26  CYS A O   
59   C CB  . CYS A 9   ? 0.1876 0.1912 0.1553 -0.0107 -0.0016 -0.0168 26  CYS A CB  
60   S SG  . CYS A 9   ? 0.2094 0.2011 0.1698 -0.0128 -0.0102 -0.0125 26  CYS A SG  
61   N N   . GLY A 10  ? 0.1586 0.1766 0.1384 -0.0043 0.0063  -0.0198 27  GLY A N   
62   C CA  . GLY A 10  ? 0.1622 0.1823 0.1421 -0.0042 0.0067  -0.0231 27  GLY A CA  
63   C C   . GLY A 10  ? 0.1504 0.1729 0.1343 -0.0025 0.0050  -0.0213 27  GLY A C   
64   O O   . GLY A 10  ? 0.1531 0.1759 0.1391 -0.0011 0.0061  -0.0172 27  GLY A O   
65   N N   . SER A 11  ? 0.1510 0.1749 0.1377 -0.0027 0.0026  -0.0244 28  SER A N   
66   C CA  . SER A 11  ? 0.1521 0.1751 0.1407 -0.0014 -0.0005 -0.0227 28  SER A CA  
67   C C   . SER A 11  ? 0.1787 0.1973 0.1609 -0.0001 0.0007  -0.0185 28  SER A C   
68   O O   . SER A 11  ? 0.1722 0.1866 0.1469 0.0007  0.0015  -0.0192 28  SER A O   
69   C CB  . SER A 11  ? 0.1539 0.1778 0.1475 -0.0004 -0.0045 -0.0271 28  SER A CB  
70   O OG  . SER A 11  ? 0.1624 0.1826 0.1564 0.0011  -0.0090 -0.0254 28  SER A OG  
71   N N   . ILE A 12  ? 0.1704 0.1883 0.1542 -0.0006 0.0010  -0.0143 29  ILE A N   
72   C CA  . ILE A 12  ? 0.1707 0.1827 0.1469 -0.0005 0.0040  -0.0103 29  ILE A CA  
73   C C   . ILE A 12  ? 0.1942 0.2009 0.1685 -0.0016 -0.0011 -0.0086 29  ILE A C   
74   O O   . ILE A 12  ? 0.1991 0.1974 0.1642 -0.0008 -0.0060 -0.0095 29  ILE A O   
75   C CB  . ILE A 12  ? 0.1674 0.1834 0.1495 -0.0009 0.0115  -0.0061 29  ILE A CB  
76   C CG1 . ILE A 12  ? 0.1860 0.2048 0.1696 0.0012  0.0150  -0.0080 29  ILE A CG1 
77   C CG2 . ILE A 12  ? 0.2191 0.2278 0.1920 -0.0017 0.0181  -0.0022 29  ILE A CG2 
78   C CD1 . ILE A 12  ? 0.2153 0.2397 0.2105 0.0023  0.0213  -0.0045 29  ILE A CD1 
79   N N   . ARG A 13  ? 0.1697 0.1791 0.1520 -0.0036 -0.0018 -0.0060 30  ARG A N   
80   C CA  . ARG A 13  ? 0.1791 0.1811 0.1585 -0.0047 -0.0075 -0.0044 30  ARG A CA  
81   C C   . ARG A 13  ? 0.1834 0.1844 0.1659 -0.0020 -0.0150 -0.0101 30  ARG A C   
82   O O   . ARG A 13  ? 0.2211 0.2136 0.2001 -0.0012 -0.0213 -0.0098 30  ARG A O   
83   C CB  . ARG A 13  ? 0.1812 0.1847 0.1682 -0.0085 -0.0068 0.0000  30  ARG A CB  
84   C CG  . ARG A 13  ? 0.1935 0.1994 0.1821 -0.0111 0.0022  0.0058  30  ARG A CG  
85   C CD  . ARG A 13  ? 0.1737 0.1822 0.1737 -0.0160 0.0022  0.0107  30  ARG A CD  
86   N NE  . ARG A 13  ? 0.2021 0.2159 0.2095 -0.0184 0.0129  0.0157  30  ARG A NE  
87   C CZ  . ARG A 13  ? 0.2195 0.2410 0.2451 -0.0228 0.0147  0.0203  30  ARG A CZ  
88   N NH1 . ARG A 13  ? 0.2050 0.2266 0.2388 -0.0261 0.0050  0.0211  30  ARG A NH1 
89   N NH2 . ARG A 13  ? 0.2252 0.2544 0.2624 -0.0239 0.0265  0.0239  30  ARG A NH2 
90   N N   . GLY A 14  ? 0.1712 0.1796 0.1601 -0.0006 -0.0139 -0.0152 31  GLY A N   
91   C CA  . GLY A 14  ? 0.1797 0.1885 0.1742 0.0023  -0.0183 -0.0213 31  GLY A CA  
92   C C   . GLY A 14  ? 0.2130 0.2193 0.2058 0.0045  -0.0228 -0.0227 31  GLY A C   
93   O O   . GLY A 14  ? 0.2228 0.2301 0.2250 0.0075  -0.0281 -0.0272 31  GLY A O   
94   N N   . GLY A 15  ? 0.2066 0.2085 0.1882 0.0033  -0.0212 -0.0191 32  GLY A N   
95   C CA  . GLY A 15  ? 0.2133 0.2092 0.1887 0.0044  -0.0270 -0.0201 32  GLY A CA  
96   C C   . GLY A 15  ? 0.2080 0.2059 0.1777 0.0031  -0.0216 -0.0208 32  GLY A C   
97   O O   . GLY A 15  ? 0.2006 0.2079 0.1780 0.0025  -0.0156 -0.0229 32  GLY A O   
98   N N   . ARG A 16  ? 0.2165 0.2025 0.1697 0.0026  -0.0240 -0.0190 33  ARG A N   
99   C CA  . ARG A 16  ? 0.2325 0.2164 0.1768 0.0018  -0.0190 -0.0198 33  ARG A CA  
100  C C   . ARG A 16  ? 0.2321 0.2131 0.1769 0.0014  -0.0279 -0.0238 33  ARG A C   
101  O O   . ARG A 16  ? 0.2702 0.2412 0.1998 0.0004  -0.0276 -0.0241 33  ARG A O   
102  C CB  . ARG A 16  ? 0.2660 0.2360 0.1884 0.0010  -0.0127 -0.0154 33  ARG A CB  
103  C CG  . ARG A 16  ? 0.2470 0.2213 0.1736 0.0003  -0.0041 -0.0109 33  ARG A CG  
104  C CD  . ARG A 16  ? 0.2940 0.2623 0.2087 -0.0003 0.0083  -0.0078 33  ARG A CD  
105  N NE  . ARG A 16  ? 0.2722 0.2483 0.1943 0.0017  0.0152  -0.0100 33  ARG A NE  
106  C CZ  . ARG A 16  ? 0.2919 0.2653 0.2093 0.0028  0.0268  -0.0088 33  ARG A CZ  
107  N NH1 . ARG A 16  ? 0.3476 0.3103 0.2511 0.0016  0.0352  -0.0055 33  ARG A NH1 
108  N NH2 . ARG A 16  ? 0.3178 0.2983 0.2448 0.0054  0.0309  -0.0108 33  ARG A NH2 
109  N N   . GLU A 17  ? 0.2305 0.2203 0.1945 0.0023  -0.0355 -0.0273 34  GLU A N   
110  C CA  . GLU A 17  ? 0.2193 0.2095 0.1910 0.0015  -0.0451 -0.0310 34  GLU A CA  
111  C C   . GLU A 17  ? 0.2204 0.2130 0.1903 -0.0014 -0.0398 -0.0332 34  GLU A C   
112  O O   . GLU A 17  ? 0.2411 0.2254 0.2045 -0.0034 -0.0477 -0.0344 34  GLU A O   
113  C CB  . GLU A 17  ? 0.2314 0.2361 0.2322 0.0033  -0.0495 -0.0353 34  GLU A CB  
114  C CG  . GLU A 17  ? 0.2596 0.2595 0.2654 0.0070  -0.0596 -0.0344 34  GLU A CG  
115  C CD  . GLU A 17  ? 0.2900 0.2914 0.2948 0.0087  -0.0525 -0.0324 34  GLU A CD  
116  O OE1 . GLU A 17  ? 0.2507 0.2539 0.2466 0.0069  -0.0413 -0.0303 34  GLU A OE1 
117  O OE2 . GLU A 17  ? 0.2672 0.2676 0.2822 0.0122  -0.0594 -0.0333 34  GLU A OE2 
118  N N   . ASP A 18  ? 0.1958 0.1976 0.1704 -0.0021 -0.0282 -0.0335 35  ASP A N   
119  C CA  . ASP A 18  ? 0.1933 0.1970 0.1676 -0.0050 -0.0234 -0.0354 35  ASP A CA  
120  C C   . ASP A 18  ? 0.2184 0.2116 0.1726 -0.0043 -0.0165 -0.0326 35  ASP A C   
121  O O   . ASP A 18  ? 0.2086 0.2024 0.1621 -0.0059 -0.0115 -0.0336 35  ASP A O   
122  C CB  . ASP A 18  ? 0.2068 0.2246 0.1983 -0.0068 -0.0162 -0.0378 35  ASP A CB  
123  C CG  . ASP A 18  ? 0.2092 0.2384 0.2239 -0.0079 -0.0198 -0.0423 35  ASP A CG  
124  O OD1 . ASP A 18  ? 0.2344 0.2624 0.2561 -0.0081 -0.0299 -0.0438 35  ASP A OD1 
125  O OD2 . ASP A 18  ? 0.2082 0.2467 0.2343 -0.0085 -0.0125 -0.0446 35  ASP A OD2 
126  N N   . ARG A 19  ? 0.2188 0.2014 0.1571 -0.0020 -0.0155 -0.0294 36  ARG A N   
127  C CA  . ARG A 19  ? 0.2222 0.1961 0.1450 -0.0004 -0.0064 -0.0272 36  ARG A CA  
128  C C   . ARG A 19  ? 0.2472 0.2104 0.1579 -0.0014 -0.0063 -0.0298 36  ARG A C   
129  O O   . ARG A 19  ? 0.2489 0.2116 0.1580 0.0002  0.0017  -0.0296 36  ARG A O   
130  C CB  . ARG A 19  ? 0.2578 0.2198 0.1639 0.0009  -0.0046 -0.0239 36  ARG A CB  
131  C CG  . ARG A 19  ? 0.3041 0.2567 0.1954 0.0030  0.0072  -0.0223 36  ARG A CG  
132  C CD  . ARG A 19  ? 0.3111 0.2525 0.1866 0.0029  0.0111  -0.0187 36  ARG A CD  
133  N NE  . ARG A 19  ? 0.3531 0.2917 0.2235 0.0050  0.0264  -0.0170 36  ARG A NE  
134  C CZ  . ARG A 19  ? 0.4011 0.3232 0.2492 0.0044  0.0343  -0.0150 36  ARG A CZ  
135  N NH1 . ARG A 19  ? 0.4222 0.3287 0.2499 0.0013  0.0269  -0.0133 36  ARG A NH1 
136  N NH2 . ARG A 19  ? 0.4394 0.3603 0.2863 0.0070  0.0504  -0.0146 36  ARG A NH2 
137  N N   . THR A 20  ? 0.2447 0.1979 0.1470 -0.0040 -0.0163 -0.0321 37  THR A N   
138  C CA  . THR A 20  ? 0.2694 0.2098 0.1583 -0.0057 -0.0174 -0.0347 37  THR A CA  
139  C C   . THR A 20  ? 0.2408 0.1926 0.1460 -0.0081 -0.0149 -0.0364 37  THR A C   
140  O O   . THR A 20  ? 0.2510 0.1947 0.1472 -0.0075 -0.0099 -0.0371 37  THR A O   
141  C CB  . THR A 20  ? 0.2730 0.1997 0.1509 -0.0091 -0.0317 -0.0367 37  THR A CB  
142  O OG1 . THR A 20  ? 0.3197 0.2313 0.1769 -0.0075 -0.0347 -0.0345 37  THR A OG1 
143  C CG2 . THR A 20  ? 0.3157 0.2257 0.1768 -0.0116 -0.0339 -0.0396 37  THR A CG2 
144  N N   . LEU A 21  ? 0.2276 0.1963 0.1556 -0.0107 -0.0175 -0.0373 38  LEU A N   
145  C CA  . LEU A 21  ? 0.2357 0.2135 0.1761 -0.0139 -0.0129 -0.0383 38  LEU A CA  
146  C C   . LEU A 21  ? 0.2441 0.2231 0.1816 -0.0106 -0.0034 -0.0356 38  LEU A C   
147  O O   . LEU A 21  ? 0.2385 0.2130 0.1724 -0.0121 -0.0003 -0.0357 38  LEU A O   
148  C CB  . LEU A 21  ? 0.2334 0.2280 0.1973 -0.0168 -0.0145 -0.0401 38  LEU A CB  
149  C CG  . LEU A 21  ? 0.2705 0.2736 0.2451 -0.0213 -0.0076 -0.0412 38  LEU A CG  
150  C CD1 . LEU A 21  ? 0.2742 0.2704 0.2457 -0.0273 -0.0091 -0.0427 38  LEU A CD1 
151  C CD2 . LEU A 21  ? 0.2759 0.2946 0.2726 -0.0228 -0.0065 -0.0438 38  LEU A CD2 
152  N N   . TYR A 22  ? 0.2180 0.2022 0.1579 -0.0066 -0.0001 -0.0330 39  TYR A N   
153  C CA  . TYR A 22  ? 0.2123 0.1982 0.1530 -0.0036 0.0067  -0.0302 39  TYR A CA  
154  C C   . TYR A 22  ? 0.2438 0.2170 0.1715 -0.0002 0.0105  -0.0299 39  TYR A C   
155  O O   . TYR A 22  ? 0.2504 0.2221 0.1798 0.0012  0.0133  -0.0288 39  TYR A O   
156  C CB  . TYR A 22  ? 0.1885 0.1816 0.1353 -0.0006 0.0090  -0.0272 39  TYR A CB  
157  C CG  . TYR A 22  ? 0.1812 0.1841 0.1391 -0.0025 0.0055  -0.0278 39  TYR A CG  
158  C CD1 . TYR A 22  ? 0.1741 0.1829 0.1405 -0.0063 0.0038  -0.0309 39  TYR A CD1 
159  C CD2 . TYR A 22  ? 0.1840 0.1897 0.1444 -0.0005 0.0054  -0.0254 39  TYR A CD2 
160  C CE1 . TYR A 22  ? 0.1941 0.2113 0.1718 -0.0069 0.0022  -0.0325 39  TYR A CE1 
161  C CE2 . TYR A 22  ? 0.1741 0.1867 0.1442 -0.0015 0.0020  -0.0264 39  TYR A CE2 
162  C CZ  . TYR A 22  ? 0.1807 0.1990 0.1596 -0.0040 0.0006  -0.0303 39  TYR A CZ  
163  O OH  . TYR A 22  ? 0.1801 0.2043 0.1692 -0.0038 -0.0013 -0.0322 39  TYR A OH  
164  N N   . GLU A 23  ? 0.2215 0.1831 0.1346 0.0014  0.0103  -0.0310 40  GLU A N   
165  C CA  . GLU A 23  ? 0.2454 0.1924 0.1442 0.0052  0.0158  -0.0319 40  GLU A CA  
166  C C   . GLU A 23  ? 0.2655 0.2040 0.1596 0.0026  0.0124  -0.0343 40  GLU A C   
167  O O   . GLU A 23  ? 0.2669 0.1978 0.1576 0.0063  0.0168  -0.0343 40  GLU A O   
168  C CB  . GLU A 23  ? 0.2813 0.2123 0.1586 0.0064  0.0166  -0.0332 40  GLU A CB  
169  C CG  . GLU A 23  ? 0.2587 0.1923 0.1352 0.0097  0.0245  -0.0302 40  GLU A CG  
170  C CD  . GLU A 23  ? 0.3171 0.2371 0.1729 0.0076  0.0207  -0.0303 40  GLU A CD  
171  O OE1 . GLU A 23  ? 0.3180 0.2270 0.1615 0.0039  0.0099  -0.0327 40  GLU A OE1 
172  O OE2 . GLU A 23  ? 0.3150 0.2321 0.1646 0.0093  0.0289  -0.0278 40  GLU A OE2 
173  N N   . ARG A 24  ? 0.2587 0.1982 0.1545 -0.0040 0.0043  -0.0362 41  ARG A N   
174  C CA  . ARG A 24  ? 0.2645 0.1966 0.1575 -0.0084 0.0013  -0.0379 41  ARG A CA  
175  C C   . ARG A 24  ? 0.2545 0.1935 0.1576 -0.0089 0.0049  -0.0356 41  ARG A C   
176  O O   . ARG A 24  ? 0.2805 0.2081 0.1764 -0.0088 0.0054  -0.0355 41  ARG A O   
177  C CB  . ARG A 24  ? 0.2600 0.1959 0.1595 -0.0163 -0.0072 -0.0402 41  ARG A CB  
178  C CG  . ARG A 24  ? 0.2887 0.2098 0.1730 -0.0175 -0.0151 -0.0426 41  ARG A CG  
179  C CD  . ARG A 24  ? 0.3311 0.2613 0.2308 -0.0246 -0.0252 -0.0443 41  ARG A CD  
180  N NE  . ARG A 24  ? 0.3062 0.2433 0.2200 -0.0319 -0.0252 -0.0452 41  ARG A NE  
181  C CZ  . ARG A 24  ? 0.3515 0.3039 0.2886 -0.0380 -0.0292 -0.0465 41  ARG A CZ  
182  N NH1 . ARG A 24  ? 0.3383 0.3013 0.2889 -0.0365 -0.0351 -0.0471 41  ARG A NH1 
183  N NH2 . ARG A 24  ? 0.3458 0.3024 0.2936 -0.0457 -0.0267 -0.0471 41  ARG A NH2 
184  N N   . ILE A 25  ? 0.2417 0.1965 0.1591 -0.0097 0.0062  -0.0337 42  ILE A N   
185  C CA  . ILE A 25  ? 0.2457 0.2032 0.1679 -0.0111 0.0081  -0.0313 42  ILE A CA  
186  C C   . ILE A 25  ? 0.2538 0.2049 0.1734 -0.0039 0.0105  -0.0287 42  ILE A C   
187  O O   . ILE A 25  ? 0.2541 0.1958 0.1693 -0.0041 0.0092  -0.0274 42  ILE A O   
188  C CB  . ILE A 25  ? 0.2245 0.1969 0.1589 -0.0131 0.0089  -0.0304 42  ILE A CB  
189  C CG1 . ILE A 25  ? 0.2163 0.1954 0.1576 -0.0200 0.0078  -0.0336 42  ILE A CG1 
190  C CG2 . ILE A 25  ? 0.2526 0.2235 0.1867 -0.0136 0.0097  -0.0274 42  ILE A CG2 
191  C CD1 . ILE A 25  ? 0.2177 0.2106 0.1715 -0.0204 0.0093  -0.0342 42  ILE A CD1 
192  N N   . VAL A 26  ? 0.2345 0.1900 0.1580 0.0025  0.0139  -0.0279 43  VAL A N   
193  C CA  . VAL A 26  ? 0.2462 0.1990 0.1741 0.0100  0.0175  -0.0258 43  VAL A CA  
194  C C   . VAL A 26  ? 0.2488 0.1843 0.1646 0.0135  0.0190  -0.0281 43  VAL A C   
195  O O   . VAL A 26  ? 0.2660 0.1956 0.1855 0.0180  0.0186  -0.0267 43  VAL A O   
196  C CB  . VAL A 26  ? 0.2169 0.1789 0.1529 0.0147  0.0232  -0.0245 43  VAL A CB  
197  C CG1 . VAL A 26  ? 0.2916 0.2516 0.2355 0.0229  0.0294  -0.0234 43  VAL A CG1 
198  C CG2 . VAL A 26  ? 0.2478 0.2246 0.1969 0.0117  0.0203  -0.0217 43  VAL A CG2 
199  N N   . SER A 27  ? 0.2667 0.1918 0.1672 0.0115  0.0191  -0.0318 44  SER A N   
200  C CA  . SER A 27  ? 0.2654 0.1704 0.1509 0.0143  0.0199  -0.0347 44  SER A CA  
201  C C   . SER A 27  ? 0.2870 0.1839 0.1707 0.0103  0.0140  -0.0338 44  SER A C   
202  O O   . SER A 27  ? 0.3032 0.1867 0.1829 0.0155  0.0146  -0.0340 44  SER A O   
203  C CB  . SER A 27  ? 0.3226 0.2155 0.1894 0.0106  0.0179  -0.0387 44  SER A CB  
204  O OG  . SER A 27  ? 0.3319 0.2236 0.1923 0.0152  0.0244  -0.0396 44  SER A OG  
205  N N   . ARG A 28  ? 0.2837 0.1874 0.1701 0.0011  0.0090  -0.0327 45  ARG A N   
206  C CA  . ARG A 28  ? 0.3154 0.2092 0.1967 -0.0046 0.0048  -0.0313 45  ARG A CA  
207  C C   . ARG A 28  ? 0.3188 0.2140 0.2074 -0.0008 0.0037  -0.0269 45  ARG A C   
208  O O   . ARG A 28  ? 0.3475 0.2271 0.2289 0.0002  0.0001  -0.0254 45  ARG A O   
209  C CB  . ARG A 28  ? 0.2966 0.1974 0.1798 -0.0161 0.0025  -0.0318 45  ARG A CB  
210  C CG  . ARG A 28  ? 0.3093 0.1986 0.1849 -0.0245 0.0001  -0.0300 45  ARG A CG  
211  C CD  . ARG A 28  ? 0.3639 0.2295 0.2242 -0.0230 -0.0032 -0.0308 45  ARG A CD  
212  N NE  . ARG A 28  ? 0.3645 0.2232 0.2180 -0.0237 -0.0048 -0.0352 45  ARG A NE  
213  C CZ  . ARG A 28  ? 0.4285 0.2781 0.2756 -0.0333 -0.0089 -0.0370 45  ARG A CZ  
214  N NH1 . ARG A 28  ? 0.4056 0.2504 0.2511 -0.0434 -0.0098 -0.0348 45  ARG A NH1 
215  N NH2 . ARG A 28  ? 0.3739 0.2166 0.2141 -0.0334 -0.0124 -0.0410 45  ARG A NH2 
216  N N   . LEU A 29  ? 0.2866 0.1985 0.1888 0.0013  0.0051  -0.0246 46  LEU A N   
217  C CA  . LEU A 29  ? 0.2799 0.1919 0.1891 0.0044  0.0013  -0.0202 46  LEU A CA  
218  C C   . LEU A 29  ? 0.3261 0.2297 0.2407 0.0149  0.0010  -0.0197 46  LEU A C   
219  O O   . LEU A 29  ? 0.3330 0.2265 0.2478 0.0169  -0.0056 -0.0164 46  LEU A O   
220  C CB  . LEU A 29  ? 0.2518 0.1821 0.1749 0.0048  0.0021  -0.0183 46  LEU A CB  
221  C CG  . LEU A 29  ? 0.2646 0.2021 0.1844 -0.0044 0.0023  -0.0188 46  LEU A CG  
222  C CD1 . LEU A 29  ? 0.2581 0.2108 0.1911 -0.0022 0.0026  -0.0172 46  LEU A CD1 
223  C CD2 . LEU A 29  ? 0.2963 0.2212 0.2030 -0.0121 -0.0015 -0.0169 46  LEU A CD2 
224  N N   . ARG A 30  ? 0.3184 0.2243 0.2367 0.0220  0.0083  -0.0229 47  ARG A N   
225  C CA  . ARG A 30  ? 0.3198 0.2180 0.2452 0.0330  0.0113  -0.0237 47  ARG A CA  
226  C C   . ARG A 30  ? 0.3680 0.2427 0.2788 0.0338  0.0066  -0.0249 47  ARG A C   
227  O O   . ARG A 30  ? 0.4134 0.2805 0.3332 0.0431  0.0055  -0.0244 47  ARG A O   
228  C CB  . ARG A 30  ? 0.3187 0.2204 0.2446 0.0388  0.0229  -0.0278 47  ARG A CB  
229  C CG  . ARG A 30  ? 0.3322 0.2552 0.2778 0.0408  0.0278  -0.0254 47  ARG A CG  
230  C CD  . ARG A 30  ? 0.4385 0.3635 0.3813 0.0446  0.0403  -0.0285 47  ARG A CD  
231  N NE  . ARG A 30  ? 0.5092 0.4542 0.4743 0.0461  0.0445  -0.0251 47  ARG A NE  
232  C CZ  . ARG A 30  ? 0.5957 0.5463 0.5608 0.0471  0.0552  -0.0259 47  ARG A CZ  
233  N NH1 . ARG A 30  ? 0.6249 0.5625 0.5648 0.0450  0.0606  -0.0297 47  ARG A NH1 
234  N NH2 . ARG A 30  ? 0.6002 0.5679 0.5897 0.0492  0.0596  -0.0225 47  ARG A NH2 
235  N N   . ARG A 31  ? 0.3630 0.2261 0.2539 0.0245  0.0035  -0.0265 48  ARG A N   
236  C CA  . ARG A 31  ? 0.3696 0.2085 0.2453 0.0233  -0.0021 -0.0268 48  ARG A CA  
237  C C   . ARG A 31  ? 0.4169 0.2495 0.2957 0.0226  -0.0115 -0.0210 48  ARG A C   
238  O O   . ARG A 31  ? 0.4406 0.2527 0.3126 0.0263  -0.0171 -0.0203 48  ARG A O   
239  C CB  . ARG A 31  ? 0.3985 0.2284 0.2555 0.0112  -0.0041 -0.0288 48  ARG A CB  
240  C CG  . ARG A 31  ? 0.4698 0.3046 0.3218 0.0096  0.0011  -0.0336 48  ARG A CG  
241  C CD  . ARG A 31  ? 0.4271 0.2380 0.2595 0.0082  -0.0008 -0.0377 48  ARG A CD  
242  N NE  . ARG A 31  ? 0.4108 0.2216 0.2341 0.0055  0.0010  -0.0422 48  ARG A NE  
243  C CZ  . ARG A 31  ? 0.3923 0.1921 0.2028 -0.0043 -0.0049 -0.0443 48  ARG A CZ  
244  N NH1 . ARG A 31  ? 0.4460 0.2343 0.2511 -0.0126 -0.0107 -0.0426 48  ARG A NH1 
245  N NH2 . ARG A 31  ? 0.3851 0.1838 0.1875 -0.0065 -0.0057 -0.0479 48  ARG A NH2 
246  N N   . PHE A 32  ? 0.3921 0.2389 0.2784 0.0176  -0.0143 -0.0170 49  PHE A N   
247  C CA  . PHE A 32  ? 0.4211 0.2577 0.3030 0.0142  -0.0246 -0.0113 49  PHE A CA  
248  C C   . PHE A 32  ? 0.4228 0.2673 0.3259 0.0237  -0.0304 -0.0077 49  PHE A C   
249  O O   . PHE A 32  ? 0.4423 0.2715 0.3421 0.0248  -0.0420 -0.0031 49  PHE A O   
250  C CB  . PHE A 32  ? 0.4134 0.2551 0.2845 0.0009  -0.0245 -0.0095 49  PHE A CB  
251  C CG  . PHE A 32  ? 0.4526 0.2895 0.3088 -0.0097 -0.0193 -0.0126 49  PHE A CG  
252  C CD1 . PHE A 32  ? 0.5595 0.3731 0.3983 -0.0140 -0.0226 -0.0125 49  PHE A CD1 
253  C CD2 . PHE A 32  ? 0.5065 0.3620 0.3684 -0.0151 -0.0122 -0.0157 49  PHE A CD2 
254  C CE1 . PHE A 32  ? 0.5898 0.4002 0.4185 -0.0249 -0.0186 -0.0151 49  PHE A CE1 
255  C CE2 . PHE A 32  ? 0.4887 0.3418 0.3427 -0.0247 -0.0088 -0.0186 49  PHE A CE2 
256  C CZ  . PHE A 32  ? 0.5354 0.3670 0.3738 -0.0300 -0.0118 -0.0183 49  PHE A CZ  
257  N N   . GLY A 33  ? 0.3870 0.2540 0.3118 0.0296  -0.0240 -0.0090 50  GLY A N   
258  C CA  . GLY A 33  ? 0.4002 0.2768 0.3496 0.0375  -0.0300 -0.0053 50  GLY A CA  
259  C C   . GLY A 33  ? 0.3871 0.2874 0.3604 0.0439  -0.0191 -0.0077 50  GLY A C   
260  O O   . GLY A 33  ? 0.4234 0.3281 0.3912 0.0441  -0.0072 -0.0125 50  GLY A O   
261  N N   . THR A 34  ? 0.3950 0.3088 0.3937 0.0481  -0.0242 -0.0040 51  THR A N   
262  C CA  . THR A 34  ? 0.3471 0.2835 0.3720 0.0537  -0.0140 -0.0052 51  THR A CA  
263  C C   . THR A 34  ? 0.2876 0.2375 0.3079 0.0445  -0.0126 -0.0041 51  THR A C   
264  O O   . THR A 34  ? 0.3149 0.2634 0.3312 0.0383  -0.0238 -0.0002 51  THR A O   
265  C CB  . THR A 34  ? 0.3269 0.2716 0.3866 0.0625  -0.0214 -0.0014 51  THR A CB  
266  O OG1 . THR A 34  ? 0.4011 0.3340 0.4683 0.0731  -0.0205 -0.0035 51  THR A OG1 
267  C CG2 . THR A 34  ? 0.3542 0.3238 0.4433 0.0657  -0.0109 -0.0015 51  THR A CG2 
268  N N   . VAL A 35  ? 0.2748 0.2348 0.2928 0.0436  0.0005  -0.0076 52  VAL A N   
269  C CA  . VAL A 35  ? 0.2755 0.2475 0.2905 0.0361  0.0019  -0.0069 52  VAL A CA  
270  C C   . VAL A 35  ? 0.3148 0.3052 0.3588 0.0397  0.0043  -0.0042 52  VAL A C   
271  O O   . VAL A 35  ? 0.3044 0.3031 0.3586 0.0441  0.0169  -0.0060 52  VAL A O   
272  C CB  . VAL A 35  ? 0.2772 0.2480 0.2734 0.0323  0.0114  -0.0114 52  VAL A CB  
273  C CG1 . VAL A 35  ? 0.3156 0.2977 0.3105 0.0255  0.0113  -0.0107 52  VAL A CG1 
274  C CG2 . VAL A 35  ? 0.2952 0.2490 0.2675 0.0278  0.0080  -0.0138 52  VAL A CG2 
275  N N   . LEU A 36  ? 0.2843 0.2558 0.2863 0.0601  0.0214  -0.0282 53  LEU A N   
276  C CA  . LEU A 36  ? 0.2874 0.2799 0.3175 0.0622  0.0264  -0.0268 53  LEU A CA  
277  C C   . LEU A 36  ? 0.2939 0.2954 0.3261 0.0561  0.0360  -0.0249 53  LEU A C   
278  O O   . LEU A 36  ? 0.3015 0.3174 0.3528 0.0588  0.0456  -0.0238 53  LEU A O   
279  C CB  . LEU A 36  ? 0.2601 0.2622 0.3075 0.0596  0.0146  -0.0248 53  LEU A CB  
280  C CG  . LEU A 36  ? 0.2624 0.2562 0.3087 0.0653  0.0029  -0.0253 53  LEU A CG  
281  C CD1 . LEU A 36  ? 0.3123 0.3131 0.3679 0.0602  -0.0093 -0.0232 53  LEU A CD1 
282  C CD2 . LEU A 36  ? 0.3106 0.3112 0.3755 0.0771  0.0064  -0.0271 53  LEU A CD2 
283  N N   . THR A 37  ? 0.2881 0.2816 0.3023 0.0481  0.0339  -0.0240 54  THR A N   
284  C CA  . THR A 37  ? 0.3346 0.3352 0.3504 0.0422  0.0409  -0.0214 54  THR A CA  
285  C C   . THR A 37  ? 0.3773 0.3727 0.3798 0.0457  0.0536  -0.0220 54  THR A C   
286  O O   . THR A 37  ? 0.4012 0.4010 0.4034 0.0418  0.0607  -0.0191 54  THR A O   
287  C CB  . THR A 37  ? 0.3001 0.2944 0.3024 0.0334  0.0333  -0.0205 54  THR A CB  
288  O OG1 . THR A 37  ? 0.2810 0.2593 0.2613 0.0336  0.0278  -0.0228 54  THR A OG1 
289  C CG2 . THR A 37  ? 0.2747 0.2772 0.2920 0.0293  0.0237  -0.0194 54  THR A CG2 
290  N N   . GLU A 38  ? 0.4457 0.4303 0.4355 0.0534  0.0564  -0.0256 55  GLU A N   
291  C CA  . GLU A 38  ? 0.5172 0.4942 0.4898 0.0576  0.0679  -0.0270 55  GLU A CA  
292  C C   . GLU A 38  ? 0.5431 0.5296 0.5308 0.0669  0.0803  -0.0276 55  GLU A C   
293  O O   . GLU A 38  ? 0.6337 0.6360 0.6496 0.0687  0.0799  -0.0262 55  GLU A O   
294  C CB  . GLU A 38  ? 0.5493 0.5051 0.4939 0.0596  0.0627  -0.0316 55  GLU A CB  
295  C CG  . GLU A 38  ? 0.5433 0.4904 0.4717 0.0505  0.0534  -0.0311 55  GLU A CG  
296  C CD  . GLU A 38  ? 0.5972 0.5425 0.5115 0.0472  0.0592  -0.0294 55  GLU A CD  
297  O OE1 . GLU A 38  ? 0.6083 0.5415 0.5017 0.0518  0.0642  -0.0324 55  GLU A OE1 
298  O OE2 . GLU A 38  ? 0.6146 0.5689 0.5372 0.0405  0.0580  -0.0252 55  GLU A OE2 
299  N N   . GLY A 54  ? 0.4793 0.6416 0.7858 -0.0215 0.1590  0.0394  71  GLY A N   
300  C CA  . GLY A 54  ? 0.4313 0.5971 0.7555 -0.0262 0.1394  0.0343  71  GLY A CA  
301  C C   . GLY A 54  ? 0.3869 0.5298 0.6816 -0.0322 0.1288  0.0345  71  GLY A C   
302  O O   . GLY A 54  ? 0.3612 0.5021 0.6638 -0.0374 0.1109  0.0303  71  GLY A O   
303  N N   . GLY A 55  ? 0.4162 0.5414 0.6759 -0.0305 0.1394  0.0390  72  GLY A N   
304  C CA  . GLY A 55  ? 0.2979 0.4015 0.5286 -0.0346 0.1307  0.0396  72  GLY A CA  
305  C C   . GLY A 55  ? 0.2826 0.3775 0.4948 -0.0302 0.1115  0.0310  72  GLY A C   
306  O O   . GLY A 55  ? 0.2803 0.3781 0.4852 -0.0217 0.1079  0.0256  72  GLY A O   
307  N N   . ASP A 56  ? 0.2679 0.3511 0.4722 -0.0362 0.0994  0.0299  73  ASP A N   
308  C CA  . ASP A 56  ? 0.2192 0.2939 0.4055 -0.0328 0.0826  0.0224  73  ASP A CA  
309  C C   . ASP A 56  ? 0.1864 0.2741 0.3966 -0.0326 0.0690  0.0159  73  ASP A C   
310  O O   . ASP A 56  ? 0.1689 0.2526 0.3646 -0.0273 0.0581  0.0100  73  ASP A O   
311  C CB  . ASP A 56  ? 0.2247 0.2829 0.3945 -0.0380 0.0751  0.0228  73  ASP A CB  
312  C CG  . ASP A 56  ? 0.2821 0.3248 0.4214 -0.0358 0.0848  0.0281  73  ASP A CG  
313  O OD1 . ASP A 56  ? 0.2949 0.3376 0.4198 -0.0293 0.0950  0.0297  73  ASP A OD1 
314  O OD2 . ASP A 56  ? 0.3162 0.3456 0.4439 -0.0395 0.0806  0.0298  73  ASP A OD2 
315  N N   . ARG A 57  ? 0.2094 0.3121 0.4558 -0.0386 0.0688  0.0171  74  ARG A N   
316  C CA  A ARG A 57  ? 0.1863 0.3022 0.4564 -0.0377 0.0548  0.0111  74  ARG A CA  
317  C CA  B ARG A 57  ? 0.1873 0.3029 0.4570 -0.0376 0.0547  0.0110  74  ARG A CA  
318  C CA  C ARG A 57  ? 0.1871 0.3028 0.4568 -0.0376 0.0547  0.0110  74  ARG A CA  
319  C C   . ARG A 57  ? 0.1638 0.2885 0.4333 -0.0271 0.0570  0.0085  74  ARG A C   
320  O O   . ARG A 57  ? 0.1581 0.2823 0.4232 -0.0224 0.0432  0.0026  74  ARG A O   
321  C CB  A ARG A 57  ? 0.1968 0.3292 0.5095 -0.0462 0.0552  0.0132  74  ARG A CB  
322  C CB  B ARG A 57  ? 0.1978 0.3290 0.5093 -0.0467 0.0541  0.0130  74  ARG A CB  
323  C CB  C ARG A 57  ? 0.1975 0.3293 0.5093 -0.0462 0.0542  0.0128  74  ARG A CB  
324  C CG  A ARG A 57  ? 0.2129 0.3595 0.5520 -0.0453 0.0389  0.0068  74  ARG A CG  
325  C CG  B ARG A 57  ? 0.2119 0.3588 0.5525 -0.0460 0.0389  0.0070  74  ARG A CG  
326  C CG  C ARG A 57  ? 0.2056 0.3274 0.5208 -0.0571 0.0489  0.0142  74  ARG A CG  
327  C CD  A ARG A 57  ? 0.2202 0.3540 0.5460 -0.0482 0.0189  0.0004  74  ARG A CD  
328  C CD  B ARG A 57  ? 0.2155 0.3501 0.5382 -0.0454 0.0183  -0.0004 74  ARG A CD  
329  C CD  C ARG A 57  ? 0.2193 0.3583 0.5797 -0.0660 0.0468  0.0153  74  ARG A CD  
330  N NE  A ARG A 57  ? 0.2345 0.3809 0.5871 -0.0491 0.0022  -0.0052 74  ARG A NE  
331  N NE  B ARG A 57  ? 0.2290 0.3700 0.5777 -0.0523 0.0021  -0.0047 74  ARG A NE  
332  N NE  C ARG A 57  ? 0.2540 0.3822 0.6198 -0.0772 0.0420  0.0166  74  ARG A NE  
333  C CZ  A ARG A 57  ? 0.2362 0.3734 0.5772 -0.0492 -0.0168 -0.0119 74  ARG A CZ  
334  C CZ  B ARG A 57  ? 0.2302 0.3831 0.5976 -0.0492 -0.0121 -0.0099 74  ARG A CZ  
335  C CZ  C ARG A 57  ? 0.2361 0.3546 0.5978 -0.0805 0.0232  0.0097  74  ARG A CZ  
336  N NH1 A ARG A 57  ? 0.2453 0.3620 0.5525 -0.0497 -0.0208 -0.0140 74  ARG A NH1 
337  N NH1 B ARG A 57  ? 0.2422 0.4092 0.6208 -0.0407 -0.0086 -0.0096 74  ARG A NH1 
338  N NH1 C ARG A 57  ? 0.2266 0.3436 0.5751 -0.0737 0.0080  0.0017  74  ARG A NH1 
339  N NH2 A ARG A 57  ? 0.2331 0.3820 0.5968 -0.0484 -0.0321 -0.0168 74  ARG A NH2 
340  N NH2 B ARG A 57  ? 0.2437 0.3939 0.6193 -0.0545 -0.0306 -0.0156 74  ARG A NH2 
341  N NH2 C ARG A 57  ? 0.2320 0.3398 0.5992 -0.0901 0.0197  0.0109  74  ARG A NH2 
342  N N   . LEU A 58  ? 0.1701 0.3014 0.4425 -0.0228 0.0747  0.0129  75  LEU A N   
343  C CA  . LEU A 58  ? 0.1797 0.3173 0.4502 -0.0118 0.0775  0.0099  75  LEU A CA  
344  C C   . LEU A 58  ? 0.1961 0.3153 0.4277 -0.0053 0.0701  0.0058  75  LEU A C   
345  O O   . LEU A 58  ? 0.1908 0.3112 0.4210 0.0013  0.0606  0.0010  75  LEU A O   
346  C CB  . LEU A 58  ? 0.1801 0.3255 0.4560 -0.0078 0.0995  0.0150  75  LEU A CB  
347  C CG  . LEU A 58  ? 0.2834 0.4313 0.5516 0.0050  0.1050  0.0117  75  LEU A CG  
348  C CD1 . LEU A 58  ? 0.3112 0.4747 0.6080 0.0096  0.0926  0.0067  75  LEU A CD1 
349  C CD2 . LEU A 58  ? 0.3672 0.5221 0.6392 0.0090  0.1285  0.0166  75  LEU A CD2 
350  N N   . ILE A 59  ? 0.1892 0.2912 0.3900 -0.0075 0.0737  0.0078  76  ILE A N   
351  C CA  . ILE A 59  ? 0.1821 0.2677 0.3488 -0.0029 0.0663  0.0040  76  ILE A CA  
352  C C   . ILE A 59  ? 0.2102 0.2939 0.3780 -0.0043 0.0477  -0.0011 76  ILE A C   
353  O O   . ILE A 59  ? 0.1731 0.2529 0.3298 0.0017  0.0405  -0.0050 76  ILE A O   
354  C CB  . ILE A 59  ? 0.2295 0.2991 0.3679 -0.0060 0.0714  0.0072  76  ILE A CB  
355  C CG1 . ILE A 59  ? 0.2465 0.3146 0.3763 -0.0028 0.0895  0.0121  76  ILE A CG1 
356  C CG2 . ILE A 59  ? 0.2273 0.2821 0.3360 -0.0033 0.0615  0.0030  76  ILE A CG2 
357  C CD1 . ILE A 59  ? 0.2587 0.3126 0.3656 -0.0066 0.0949  0.0168  76  ILE A CD1 
358  N N   . HIS A 60  ? 0.1581 0.2435 0.3385 -0.0121 0.0399  -0.0012 77  HIS A N   
359  C CA  . HIS A 60  ? 0.1592 0.2408 0.3365 -0.0133 0.0226  -0.0063 77  HIS A CA  
360  C C   . HIS A 60  ? 0.1654 0.2582 0.3605 -0.0082 0.0141  -0.0096 77  HIS A C   
361  O O   . HIS A 60  ? 0.1569 0.2427 0.3364 -0.0037 0.0042  -0.0131 77  HIS A O   
362  C CB  . HIS A 60  ? 0.1530 0.2340 0.3422 -0.0223 0.0164  -0.0064 77  HIS A CB  
363  C CG  . HIS A 60  ? 0.1518 0.2285 0.3374 -0.0234 -0.0011 -0.0122 77  HIS A CG  
364  N ND1 . HIS A 60  ? 0.1717 0.2591 0.3801 -0.0235 -0.0125 -0.0155 77  HIS A ND1 
365  C CD2 . HIS A 60  ? 0.1517 0.2144 0.3124 -0.0239 -0.0088 -0.0154 77  HIS A CD2 
366  C CE1 . HIS A 60  ? 0.1735 0.2518 0.3679 -0.0240 -0.0267 -0.0205 77  HIS A CE1 
367  N NE2 . HIS A 60  ? 0.1787 0.2425 0.3446 -0.0242 -0.0238 -0.0205 77  HIS A NE2 
368  N N   . GLU A 61  ? 0.1518 0.2620 0.3802 -0.0087 0.0181  -0.0080 78  GLU A N   
369  C CA  . GLU A 61  ? 0.1512 0.2736 0.4008 -0.0036 0.0082  -0.0112 78  GLU A CA  
370  C C   . GLU A 61  ? 0.1878 0.3074 0.4242 0.0072  0.0118  -0.0121 78  GLU A C   
371  O O   . GLU A 61  ? 0.1550 0.2723 0.3876 0.0125  -0.0008 -0.0154 78  GLU A O   
372  C CB  . GLU A 61  ? 0.1510 0.2952 0.4435 -0.0068 0.0124  -0.0092 78  GLU A CB  
373  C CG  . GLU A 61  ? 0.1506 0.2968 0.4594 -0.0184 0.0071  -0.0087 78  GLU A CG  
374  C CD  . GLU A 61  ? 0.2233 0.3642 0.5296 -0.0205 -0.0147 -0.0146 78  GLU A CD  
375  O OE1 . GLU A 61  ? 0.3088 0.4635 0.6422 -0.0194 -0.0260 -0.0174 78  GLU A OE1 
376  O OE2 . GLU A 61  ? 0.2282 0.3514 0.5052 -0.0228 -0.0205 -0.0166 78  GLU A OE2 
377  N N   . GLN A 62  ? 0.1605 0.2787 0.3885 0.0107  0.0284  -0.0092 79  GLN A N   
378  C CA  . GLN A 62  ? 0.1856 0.2986 0.3993 0.0211  0.0322  -0.0107 79  GLN A CA  
379  C C   . GLN A 62  ? 0.2224 0.3154 0.4009 0.0224  0.0227  -0.0132 79  GLN A C   
380  O O   . GLN A 62  ? 0.2108 0.2989 0.3825 0.0292  0.0151  -0.0157 79  GLN A O   
381  C CB  . GLN A 62  ? 0.2349 0.3485 0.4435 0.0240  0.0521  -0.0076 79  GLN A CB  
382  C CG  . GLN A 62  ? 0.3785 0.4849 0.5709 0.0349  0.0581  -0.0098 79  GLN A CG  
383  C CD  . GLN A 62  ? 0.4430 0.5522 0.6336 0.0382  0.0785  -0.0070 79  GLN A CD  
384  O OE1 . GLN A 62  ? 0.4352 0.5467 0.6277 0.0315  0.0884  -0.0026 79  GLN A OE1 
385  N NE2 . GLN A 62  ? 0.4705 0.5783 0.6569 0.0490  0.0852  -0.0096 79  GLN A NE2 
386  N N   . ASP A 63  ? 0.1847 0.2659 0.3420 0.0157  0.0225  -0.0124 80  ASP A N   
387  C CA  . ASP A 63  ? 0.2051 0.2692 0.3315 0.0165  0.0153  -0.0144 80  ASP A CA  
388  C C   . ASP A 63  ? 0.2113 0.2739 0.3387 0.0158  -0.0012 -0.0171 80  ASP A C   
389  O O   . ASP A 63  ? 0.2439 0.2955 0.3525 0.0194  -0.0076 -0.0186 80  ASP A O   
390  C CB  . ASP A 63  ? 0.2250 0.2791 0.3314 0.0104  0.0198  -0.0129 80  ASP A CB  
391  C CG  . ASP A 63  ? 0.2846 0.3320 0.3745 0.0138  0.0326  -0.0113 80  ASP A CG  
392  O OD1 . ASP A 63  ? 0.3451 0.3961 0.4398 0.0115  0.0434  -0.0079 80  ASP A OD1 
393  O OD2 . ASP A 63  ? 0.3688 0.4062 0.4401 0.0187  0.0317  -0.0132 80  ASP A OD2 
394  N N   . LEU A 64  ? 0.2049 0.2774 0.3536 0.0112  -0.0084 -0.0177 81  LEU A N   
395  C CA  . LEU A 64  ? 0.2116 0.2816 0.3591 0.0112  -0.0249 -0.0207 81  LEU A CA  
396  C C   . LEU A 64  ? 0.2568 0.3309 0.4132 0.0198  -0.0312 -0.0216 81  LEU A C   
397  O O   . LEU A 64  ? 0.2588 0.3237 0.4007 0.0227  -0.0430 -0.0231 81  LEU A O   
398  C CB  . LEU A 64  ? 0.2315 0.3109 0.4011 0.0043  -0.0316 -0.0218 81  LEU A CB  
399  C CG  . LEU A 64  ? 0.2637 0.3327 0.4176 -0.0020 -0.0404 -0.0244 81  LEU A CG  
400  C CD1 . LEU A 64  ? 0.3087 0.3875 0.4890 -0.0074 -0.0497 -0.0266 81  LEU A CD1 
401  C CD2 . LEU A 64  ? 0.3251 0.3801 0.4507 0.0013  -0.0500 -0.0266 81  LEU A CD2 
402  N N   . GLU A 65  ? 0.2162 0.3037 0.3959 0.0244  -0.0229 -0.0204 82  GLU A N   
403  C CA  . GLU A 65  ? 0.2140 0.3056 0.4036 0.0343  -0.0271 -0.0213 82  GLU A CA  
404  C C   . GLU A 65  ? 0.2366 0.3096 0.3948 0.0401  -0.0255 -0.0213 82  GLU A C   
405  O O   . GLU A 65  ? 0.2493 0.3142 0.3986 0.0454  -0.0366 -0.0221 82  GLU A O   
406  C CB  . GLU A 65  ? 0.2085 0.3185 0.4288 0.0379  -0.0146 -0.0200 82  GLU A CB  
407  C CG  . GLU A 65  ? 0.2398 0.3715 0.5006 0.0368  -0.0218 -0.0206 82  GLU A CG  
408  C CD  . GLU A 65  ? 0.3085 0.4593 0.5997 0.0354  -0.0051 -0.0181 82  GLU A CD  
409  O OE1 . GLU A 65  ? 0.3251 0.4732 0.6066 0.0396  0.0114  -0.0165 82  GLU A OE1 
410  O OE2 . GLU A 65  ? 0.3769 0.5456 0.7021 0.0302  -0.0085 -0.0179 82  GLU A OE2 
411  N N   . TRP A 66  ? 0.1944 0.2594 0.3350 0.0387  -0.0125 -0.0203 83  TRP A N   
412  C CA  . TRP A 66  ? 0.2196 0.2665 0.3316 0.0430  -0.0111 -0.0207 83  TRP A CA  
413  C C   . TRP A 66  ? 0.2196 0.2516 0.3068 0.0386  -0.0218 -0.0208 83  TRP A C   
414  O O   . TRP A 66  ? 0.2542 0.2724 0.3236 0.0425  -0.0265 -0.0208 83  TRP A O   
415  C CB  . TRP A 66  ? 0.2146 0.2562 0.3127 0.0419  0.0036  -0.0201 83  TRP A CB  
416  C CG  . TRP A 66  ? 0.2131 0.2654 0.3283 0.0479  0.0164  -0.0200 83  TRP A CG  
417  C CD1 . TRP A 66  ? 0.2570 0.3170 0.3901 0.0573  0.0170  -0.0212 83  TRP A CD1 
418  C CD2 . TRP A 66  ? 0.2516 0.3062 0.3641 0.0459  0.0314  -0.0185 83  TRP A CD2 
419  N NE1 . TRP A 66  ? 0.2930 0.3619 0.4369 0.0611  0.0328  -0.0208 83  TRP A NE1 
420  C CE2 . TRP A 66  ? 0.2977 0.3625 0.4274 0.0540  0.0419  -0.0189 83  TRP A CE2 
421  C CE3 . TRP A 66  ? 0.2737 0.3225 0.3706 0.0385  0.0369  -0.0167 83  TRP A CE3 
422  C CZ2 . TRP A 66  ? 0.3467 0.4154 0.4762 0.0545  0.0586  -0.0172 83  TRP A CZ2 
423  C CZ3 . TRP A 66  ? 0.3153 0.3670 0.4117 0.0391  0.0520  -0.0148 83  TRP A CZ3 
424  C CH2 . TRP A 66  ? 0.3334 0.3945 0.4449 0.0469  0.0631  -0.0149 83  TRP A CH2 
425  N N   . LEU A 67  ? 0.2403 0.2741 0.3257 0.0304  -0.0249 -0.0207 84  LEU A N   
426  C CA  . LEU A 67  ? 0.2623 0.2824 0.3231 0.0263  -0.0322 -0.0209 84  LEU A CA  
427  C C   . LEU A 67  ? 0.2570 0.2727 0.3154 0.0303  -0.0461 -0.0212 84  LEU A C   
428  O O   . LEU A 67  ? 0.3141 0.3149 0.3493 0.0310  -0.0502 -0.0203 84  LEU A O   
429  C CB  . LEU A 67  ? 0.2720 0.2959 0.3340 0.0181  -0.0322 -0.0215 84  LEU A CB  
430  C CG  . LEU A 67  ? 0.2965 0.3097 0.3363 0.0131  -0.0370 -0.0222 84  LEU A CG  
431  C CD1 . LEU A 67  ? 0.2846 0.2867 0.3030 0.0128  -0.0297 -0.0210 84  LEU A CD1 
432  C CD2 . LEU A 67  ? 0.2671 0.2855 0.3138 0.0066  -0.0364 -0.0234 84  LEU A CD2 
433  N N   . GLN A 68  ? 0.2752 0.3036 0.3581 0.0333  -0.0534 -0.0221 85  GLN A N   
434  C CA  . GLN A 68  ? 0.2932 0.3178 0.3751 0.0383  -0.0681 -0.0223 85  GLN A CA  
435  C C   . GLN A 68  ? 0.2906 0.3076 0.3681 0.0476  -0.0682 -0.0209 85  GLN A C   
436  O O   . GLN A 68  ? 0.3293 0.3351 0.3938 0.0517  -0.0794 -0.0197 85  GLN A O   
437  C CB  . GLN A 68  ? 0.3292 0.3713 0.4422 0.0388  -0.0768 -0.0242 85  GLN A CB  
438  C CG  . GLN A 68  ? 0.3532 0.3985 0.4677 0.0300  -0.0812 -0.0262 85  GLN A CG  
439  C CD  . GLN A 68  ? 0.3502 0.4146 0.5005 0.0284  -0.0868 -0.0282 85  GLN A CD  
440  O OE1 . GLN A 68  ? 0.3582 0.4251 0.5160 0.0299  -0.1025 -0.0303 85  GLN A OE1 
441  N NE2 . GLN A 68  ? 0.3562 0.4337 0.5281 0.0247  -0.0742 -0.0274 85  GLN A NE2 
442  N N   . GLN A 69  ? 0.2897 0.3110 0.3763 0.0514  -0.0561 -0.0209 86  GLN A N   
443  C CA  . GLN A 69  ? 0.2638 0.2766 0.3463 0.0609  -0.0553 -0.0205 86  GLN A CA  
444  C C   . GLN A 69  ? 0.2499 0.2405 0.2995 0.0591  -0.0524 -0.0192 86  GLN A C   
445  O O   . GLN A 69  ? 0.2941 0.2713 0.3334 0.0658  -0.0561 -0.0182 86  GLN A O   
446  C CB  . GLN A 69  ? 0.2431 0.2689 0.3470 0.0658  -0.0423 -0.0218 86  GLN A CB  
447  C CG  . GLN A 69  ? 0.2438 0.2922 0.3847 0.0694  -0.0455 -0.0226 86  GLN A CG  
448  C CD  . GLN A 69  ? 0.2348 0.2980 0.3977 0.0733  -0.0301 -0.0234 86  GLN A CD  
449  O OE1 . GLN A 69  ? 0.2352 0.2896 0.3831 0.0752  -0.0177 -0.0238 86  GLN A OE1 
450  N NE2 . GLN A 69  ? 0.2264 0.3125 0.4251 0.0736  -0.0302 -0.0237 86  GLN A NE2 
451  N N   . ALA A 70  ? 0.2700 0.2565 0.3042 0.0502  -0.0463 -0.0190 87  ALA A N   
452  C CA  . ALA A 70  ? 0.2548 0.2235 0.2628 0.0477  -0.0417 -0.0182 87  ALA A CA  
453  C C   . ALA A 70  ? 0.2912 0.2431 0.2781 0.0471  -0.0516 -0.0155 87  ALA A C   
454  O O   . ALA A 70  ? 0.3075 0.2605 0.2919 0.0446  -0.0603 -0.0145 87  ALA A O   
455  C CB  . ALA A 70  ? 0.2752 0.2462 0.2755 0.0388  -0.0338 -0.0187 87  ALA A CB  
456  N N   . ASP A 71  ? 0.2791 0.2137 0.2496 0.0492  -0.0500 -0.0145 88  ASP A N   
457  C CA  . ASP A 71  ? 0.3278 0.2437 0.2749 0.0466  -0.0563 -0.0109 88  ASP A CA  
458  C C   . ASP A 71  ? 0.3345 0.2463 0.2650 0.0360  -0.0513 -0.0100 88  ASP A C   
459  O O   . ASP A 71  ? 0.3643 0.2689 0.2801 0.0316  -0.0559 -0.0071 88  ASP A O   
460  C CB  . ASP A 71  ? 0.3564 0.2547 0.2947 0.0530  -0.0569 -0.0100 88  ASP A CB  
461  C CG  . ASP A 71  ? 0.3666 0.2688 0.3218 0.0650  -0.0629 -0.0106 88  ASP A CG  
462  O OD1 . ASP A 71  ? 0.3906 0.2979 0.3521 0.0678  -0.0731 -0.0089 88  ASP A OD1 
463  O OD2 . ASP A 71  ? 0.3803 0.2830 0.3448 0.0720  -0.0574 -0.0135 88  ASP A OD2 
464  N N   . VAL A 72  ? 0.2867 0.2034 0.2195 0.0322  -0.0419 -0.0125 89  VAL A N   
465  C CA  . VAL A 72  ? 0.2710 0.1870 0.1926 0.0228  -0.0373 -0.0123 89  VAL A CA  
466  C C   . VAL A 72  ? 0.2771 0.2083 0.2113 0.0207  -0.0304 -0.0153 89  VAL A C   
467  O O   . VAL A 72  ? 0.2734 0.2091 0.2174 0.0252  -0.0254 -0.0174 89  VAL A O   
468  C CB  . VAL A 72  ? 0.3063 0.2060 0.2118 0.0194  -0.0343 -0.0114 89  VAL A CB  
469  C CG1 . VAL A 72  ? 0.3233 0.2248 0.2208 0.0098  -0.0304 -0.0110 89  VAL A CG1 
470  C CG2 . VAL A 72  ? 0.3310 0.2128 0.2236 0.0215  -0.0407 -0.0075 89  VAL A CG2 
471  N N   . VAL A 73  ? 0.2672 0.2051 0.1998 0.0143  -0.0295 -0.0153 90  VAL A N   
472  C CA  . VAL A 73  ? 0.2601 0.2096 0.2014 0.0113  -0.0234 -0.0173 90  VAL A CA  
473  C C   . VAL A 73  ? 0.2798 0.2240 0.2085 0.0053  -0.0192 -0.0173 90  VAL A C   
474  O O   . VAL A 73  ? 0.2930 0.2332 0.2118 0.0005  -0.0211 -0.0160 90  VAL A O   
475  C CB  . VAL A 73  ? 0.2219 0.1821 0.1721 0.0092  -0.0266 -0.0177 90  VAL A CB  
476  C CG1 . VAL A 73  ? 0.2394 0.2087 0.1966 0.0057  -0.0204 -0.0191 90  VAL A CG1 
477  C CG2 . VAL A 73  ? 0.2335 0.2004 0.1993 0.0146  -0.0321 -0.0180 90  VAL A CG2 
478  N N   . VAL A 74  ? 0.2248 0.1691 0.1539 0.0057  -0.0136 -0.0189 91  VAL A N   
479  C CA  . VAL A 74  ? 0.2367 0.1767 0.1559 0.0004  -0.0111 -0.0195 91  VAL A CA  
480  C C   . VAL A 74  ? 0.2470 0.1973 0.1722 -0.0012 -0.0070 -0.0206 91  VAL A C   
481  O O   . VAL A 74  ? 0.2384 0.1931 0.1703 0.0026  -0.0031 -0.0212 91  VAL A O   
482  C CB  . VAL A 74  ? 0.2543 0.1822 0.1649 0.0024  -0.0100 -0.0210 91  VAL A CB  
483  C CG1 . VAL A 74  ? 0.2777 0.2021 0.1799 -0.0037 -0.0093 -0.0220 91  VAL A CG1 
484  C CG2 . VAL A 74  ? 0.2896 0.2049 0.1941 0.0046  -0.0146 -0.0194 91  VAL A CG2 
485  N N   . ALA A 75  ? 0.2144 0.1681 0.1372 -0.0064 -0.0073 -0.0204 92  ALA A N   
486  C CA  . ALA A 75  ? 0.2028 0.1647 0.1307 -0.0075 -0.0044 -0.0210 92  ALA A CA  
487  C C   . ALA A 75  ? 0.2218 0.1821 0.1430 -0.0115 -0.0042 -0.0217 92  ALA A C   
488  O O   . ALA A 75  ? 0.2602 0.2187 0.1774 -0.0156 -0.0061 -0.0214 92  ALA A O   
489  C CB  . ALA A 75  ? 0.2099 0.1794 0.1452 -0.0088 -0.0060 -0.0207 92  ALA A CB  
490  N N   . GLU A 76  ? 0.1962 0.1572 0.1161 -0.0103 -0.0019 -0.0224 93  GLU A N   
491  C CA  . GLU A 76  ? 0.2240 0.1856 0.1400 -0.0134 -0.0032 -0.0233 93  GLU A CA  
492  C C   . GLU A 76  ? 0.2434 0.2136 0.1665 -0.0138 -0.0023 -0.0225 93  GLU A C   
493  O O   . GLU A 76  ? 0.2179 0.1896 0.1436 -0.0110 0.0003  -0.0215 93  GLU A O   
494  C CB  . GLU A 76  ? 0.2145 0.1693 0.1217 -0.0113 -0.0028 -0.0247 93  GLU A CB  
495  C CG  . GLU A 76  ? 0.2475 0.1988 0.1490 -0.0154 -0.0073 -0.0266 93  GLU A CG  
496  C CD  . GLU A 76  ? 0.2698 0.2301 0.1772 -0.0180 -0.0093 -0.0263 93  GLU A CD  
497  O OE1 . GLU A 76  ? 0.2384 0.2050 0.1511 -0.0160 -0.0071 -0.0248 93  GLU A OE1 
498  O OE2 . GLU A 76  ? 0.2679 0.2291 0.1761 -0.0223 -0.0132 -0.0276 93  GLU A OE2 
499  N N   . VAL A 77  ? 0.2213 0.1963 0.1474 -0.0170 -0.0039 -0.0229 94  VAL A N   
500  C CA  . VAL A 77  ? 0.2138 0.1956 0.1467 -0.0167 -0.0034 -0.0229 94  VAL A CA  
501  C C   . VAL A 77  ? 0.2262 0.2123 0.1608 -0.0173 -0.0044 -0.0236 94  VAL A C   
502  O O   . VAL A 77  ? 0.2237 0.2151 0.1637 -0.0171 -0.0043 -0.0243 94  VAL A O   
503  C CB  . VAL A 77  ? 0.2311 0.2150 0.1654 -0.0182 -0.0039 -0.0233 94  VAL A CB  
504  C CG1 . VAL A 77  ? 0.2349 0.2154 0.1691 -0.0165 -0.0047 -0.0226 94  VAL A CG1 
505  C CG2 . VAL A 77  ? 0.2278 0.2118 0.1584 -0.0221 -0.0040 -0.0234 94  VAL A CG2 
506  N N   . THR A 78  ? 0.2183 0.2017 0.1483 -0.0173 -0.0061 -0.0238 95  THR A N   
507  C CA  . THR A 78  ? 0.2189 0.2068 0.1516 -0.0173 -0.0088 -0.0244 95  THR A CA  
508  C C   . THR A 78  ? 0.2219 0.2095 0.1554 -0.0133 -0.0082 -0.0230 95  THR A C   
509  O O   . THR A 78  ? 0.2344 0.2272 0.1742 -0.0123 -0.0093 -0.0233 95  THR A O   
510  C CB  . THR A 78  ? 0.2321 0.2161 0.1587 -0.0186 -0.0128 -0.0256 95  THR A CB  
511  O OG1 . THR A 78  ? 0.2455 0.2286 0.1726 -0.0232 -0.0132 -0.0265 95  THR A OG1 
512  C CG2 . THR A 78  ? 0.2353 0.2253 0.1667 -0.0183 -0.0173 -0.0264 95  THR A CG2 
513  N N   . GLN A 79  ? 0.2355 0.2168 0.1631 -0.0109 -0.0058 -0.0210 96  GLN A N   
514  C CA  . GLN A 79  ? 0.2125 0.1917 0.1401 -0.0080 -0.0042 -0.0184 96  GLN A CA  
515  C C   . GLN A 79  ? 0.2156 0.1972 0.1523 -0.0084 -0.0013 -0.0178 96  GLN A C   
516  O O   . GLN A 79  ? 0.2243 0.2057 0.1633 -0.0093 0.0012  -0.0177 96  GLN A O   
517  C CB  . GLN A 79  ? 0.2344 0.2057 0.1512 -0.0057 -0.0012 -0.0161 96  GLN A CB  
518  C CG  . GLN A 79  ? 0.2307 0.1976 0.1444 -0.0030 0.0011  -0.0121 96  GLN A CG  
519  C CD  . GLN A 79  ? 0.2850 0.2507 0.1944 -0.0011 -0.0047 -0.0118 96  GLN A CD  
520  O OE1 . GLN A 79  ? 0.2987 0.2642 0.2021 -0.0010 -0.0100 -0.0141 96  GLN A OE1 
521  N NE2 . GLN A 79  ? 0.3166 0.2808 0.2295 0.0005  -0.0046 -0.0090 96  GLN A NE2 
522  N N   . PRO A 80  ? 0.2007 0.1841 0.1432 -0.0076 -0.0025 -0.0179 97  PRO A N   
523  C CA  . PRO A 80  ? 0.1956 0.1797 0.1462 -0.0084 -0.0011 -0.0183 97  PRO A CA  
524  C C   . PRO A 80  ? 0.1984 0.1786 0.1510 -0.0086 0.0028  -0.0150 97  PRO A C   
525  O O   . PRO A 80  ? 0.2071 0.1825 0.1550 -0.0072 0.0053  -0.0113 97  PRO A O   
526  C CB  . PRO A 80  ? 0.2015 0.1856 0.1558 -0.0065 -0.0033 -0.0191 97  PRO A CB  
527  C CG  . PRO A 80  ? 0.2314 0.2198 0.1832 -0.0054 -0.0061 -0.0206 97  PRO A CG  
528  C CD  . PRO A 80  ? 0.2024 0.1877 0.1455 -0.0057 -0.0061 -0.0185 97  PRO A CD  
529  N N   . SER A 81  ? 0.1827 0.1652 0.1428 -0.0104 0.0033  -0.0161 98  SER A N   
530  C CA  . SER A 81  ? 0.1671 0.1492 0.1335 -0.0111 0.0073  -0.0132 98  SER A CA  
531  C C   . SER A 81  ? 0.1680 0.1533 0.1460 -0.0132 0.0047  -0.0155 98  SER A C   
532  O O   . SER A 81  ? 0.1810 0.1689 0.1581 -0.0134 0.0011  -0.0187 98  SER A O   
533  C CB  . SER A 81  ? 0.1887 0.1712 0.1499 -0.0098 0.0104  -0.0124 98  SER A CB  
534  O OG  . SER A 81  ? 0.1794 0.1652 0.1511 -0.0102 0.0139  -0.0110 98  SER A OG  
535  N N   . LEU A 82  ? 0.1380 0.1693 0.1386 -0.0088 0.0109  -0.0072 99  LEU A N   
536  C CA  . LEU A 82  ? 0.1519 0.1805 0.1509 -0.0115 0.0135  -0.0128 99  LEU A CA  
537  C C   . LEU A 82  ? 0.1632 0.1995 0.1544 -0.0121 0.0126  -0.0157 99  LEU A C   
538  O O   . LEU A 82  ? 0.1475 0.1829 0.1345 -0.0122 0.0124  -0.0207 99  LEU A O   
539  C CB  . LEU A 82  ? 0.1623 0.1857 0.1658 -0.0156 0.0140  -0.0102 99  LEU A CB  
540  C CG  . LEU A 82  ? 0.1577 0.1692 0.1711 -0.0141 0.0142  -0.0067 99  LEU A CG  
541  C CD1 . LEU A 82  ? 0.1926 0.1979 0.2073 -0.0196 0.0142  -0.0005 99  LEU A CD1 
542  C CD2 . LEU A 82  ? 0.1804 0.1844 0.1996 -0.0128 0.0180  -0.0161 99  LEU A CD2 
543  N N   . GLY A 83  ? 0.1416 0.1853 0.1307 -0.0125 0.0117  -0.0127 100 GLY A N   
544  C CA  . GLY A 83  ? 0.1437 0.1952 0.1307 -0.0116 0.0111  -0.0162 100 GLY A CA  
545  C C   . GLY A 83  ? 0.1494 0.1982 0.1314 -0.0074 0.0097  -0.0187 100 GLY A C   
546  O O   . GLY A 83  ? 0.1569 0.2068 0.1373 -0.0056 0.0073  -0.0213 100 GLY A O   
547  N N   . VAL A 84  ? 0.1409 0.1859 0.1212 -0.0063 0.0104  -0.0174 101 VAL A N   
548  C CA  . VAL A 84  ? 0.1502 0.1902 0.1261 -0.0043 0.0105  -0.0190 101 VAL A CA  
549  C C   . VAL A 84  ? 0.1800 0.2132 0.1511 -0.0051 0.0118  -0.0202 101 VAL A C   
550  O O   . VAL A 84  ? 0.1810 0.2095 0.1438 -0.0040 0.0104  -0.0203 101 VAL A O   
551  C CB  . VAL A 84  ? 0.1307 0.1701 0.1091 -0.0048 0.0112  -0.0184 101 VAL A CB  
552  C CG1 . VAL A 84  ? 0.1673 0.1995 0.1425 -0.0050 0.0132  -0.0197 101 VAL A CG1 
553  C CG2 . VAL A 84  ? 0.1611 0.2066 0.1385 -0.0050 0.0093  -0.0187 101 VAL A CG2 
554  N N   . GLY A 85  ? 0.1480 0.1793 0.1230 -0.0069 0.0144  -0.0212 102 GLY A N   
555  C CA  . GLY A 85  ? 0.1616 0.1865 0.1293 -0.0086 0.0174  -0.0247 102 GLY A CA  
556  C C   . GLY A 85  ? 0.1658 0.1911 0.1251 -0.0095 0.0127  -0.0264 102 GLY A C   
557  O O   . GLY A 85  ? 0.1945 0.2146 0.1399 -0.0102 0.0117  -0.0273 102 GLY A O   
558  N N   . TYR A 86  ? 0.1678 0.2000 0.1351 -0.0101 0.0092  -0.0264 103 TYR A N   
559  C CA  . TYR A 86  ? 0.1771 0.2137 0.1420 -0.0113 0.0034  -0.0291 103 TYR A CA  
560  C C   . TYR A 86  ? 0.1719 0.2112 0.1318 -0.0069 -0.0024 -0.0267 103 TYR A C   
561  O O   . TYR A 86  ? 0.1813 0.2195 0.1318 -0.0066 -0.0088 -0.0275 103 TYR A O   
562  C CB  . TYR A 86  ? 0.1844 0.2297 0.1631 -0.0141 0.0029  -0.0295 103 TYR A CB  
563  C CG  . TYR A 86  ? 0.1485 0.2030 0.1316 -0.0163 -0.0033 -0.0334 103 TYR A CG  
564  C CD1 . TYR A 86  ? 0.1818 0.2337 0.1634 -0.0219 -0.0053 -0.0391 103 TYR A CD1 
565  C CD2 . TYR A 86  ? 0.1624 0.2293 0.1537 -0.0128 -0.0075 -0.0326 103 TYR A CD2 
566  C CE1 . TYR A 86  ? 0.1993 0.2621 0.1870 -0.0248 -0.0128 -0.0435 103 TYR A CE1 
567  C CE2 . TYR A 86  ? 0.1886 0.2676 0.1892 -0.0143 -0.0145 -0.0366 103 TYR A CE2 
568  C CZ  . TYR A 86  ? 0.1856 0.2632 0.1843 -0.0208 -0.0179 -0.0418 103 TYR A CZ  
569  O OH  . TYR A 86  ? 0.2064 0.2984 0.2164 -0.0232 -0.0265 -0.0467 103 TYR A OH  
570  N N   . GLU A 87  ? 0.1676 0.2096 0.1334 -0.0031 -0.0013 -0.0239 104 GLU A N   
571  C CA  . GLU A 87  ? 0.1690 0.2099 0.1326 0.0024  -0.0060 -0.0218 104 GLU A CA  
572  C C   . GLU A 87  ? 0.1944 0.2214 0.1407 0.0025  -0.0071 -0.0185 104 GLU A C   
573  O O   . GLU A 87  ? 0.2185 0.2420 0.1576 0.0059  -0.0147 -0.0157 104 GLU A O   
574  C CB  . GLU A 87  ? 0.1501 0.1928 0.1210 0.0052  -0.0024 -0.0217 104 GLU A CB  
575  C CG  . GLU A 87  ? 0.1718 0.2290 0.1566 0.0053  -0.0011 -0.0249 104 GLU A CG  
576  C CD  . GLU A 87  ? 0.1668 0.2260 0.1540 0.0059  0.0040  -0.0264 104 GLU A CD  
577  O OE1 . GLU A 87  ? 0.1794 0.2313 0.1599 0.0040  0.0064  -0.0249 104 GLU A OE1 
578  O OE2 . GLU A 87  ? 0.1950 0.2649 0.1916 0.0077  0.0059  -0.0302 104 GLU A OE2 
579  N N   . LEU A 88  ? 0.1869 0.2061 0.1269 -0.0012 0.0004  -0.0182 105 LEU A N   
580  C CA  . LEU A 88  ? 0.2001 0.2063 0.1226 -0.0032 0.0025  -0.0151 105 LEU A CA  
581  C C   . LEU A 88  ? 0.2300 0.2332 0.1359 -0.0062 -0.0007 -0.0163 105 LEU A C   
582  O O   . LEU A 88  ? 0.2337 0.2272 0.1207 -0.0062 -0.0049 -0.0115 105 LEU A O   
583  C CB  . LEU A 88  ? 0.1999 0.2026 0.1249 -0.0072 0.0129  -0.0162 105 LEU A CB  
584  C CG  . LEU A 88  ? 0.2008 0.2038 0.1370 -0.0057 0.0144  -0.0149 105 LEU A CG  
585  C CD1 . LEU A 88  ? 0.2000 0.2061 0.1460 -0.0094 0.0219  -0.0174 105 LEU A CD1 
586  C CD2 . LEU A 88  ? 0.2132 0.2033 0.1398 -0.0046 0.0126  -0.0099 105 LEU A CD2 
587  N N   . GLY A 89  ? 0.2283 0.2383 0.1392 -0.0093 0.0003  -0.0227 106 GLY A N   
588  C CA  . GLY A 89  ? 0.2185 0.2263 0.1130 -0.0131 -0.0036 -0.0265 106 GLY A CA  
589  C C   . GLY A 89  ? 0.2366 0.2492 0.1269 -0.0099 -0.0179 -0.0236 106 GLY A C   
590  O O   . GLY A 89  ? 0.2582 0.2641 0.1258 -0.0114 -0.0243 -0.0214 106 GLY A O   
591  N N   . ARG A 90  ? 0.2293 0.2546 0.1418 -0.0055 -0.0234 -0.0237 107 ARG A N   
592  C CA  . ARG A 90  ? 0.2489 0.2821 0.1649 -0.0008 -0.0374 -0.0214 107 ARG A CA  
593  C C   . ARG A 90  ? 0.2716 0.2930 0.1751 0.0055  -0.0427 -0.0121 107 ARG A C   
594  O O   . ARG A 90  ? 0.2700 0.2896 0.1619 0.0082  -0.0556 -0.0077 107 ARG A O   
595  C CB  . ARG A 90  ? 0.2081 0.2588 0.1537 0.0024  -0.0386 -0.0245 107 ARG A CB  
596  C CG  . ARG A 90  ? 0.1999 0.2611 0.1583 -0.0049 -0.0348 -0.0322 107 ARG A CG  
597  C CD  . ARG A 90  ? 0.2402 0.3047 0.1908 -0.0107 -0.0435 -0.0379 107 ARG A CD  
598  N NE  . ARG A 90  ? 0.2475 0.3244 0.2043 -0.0065 -0.0590 -0.0372 107 ARG A NE  
599  C CZ  . ARG A 90  ? 0.2564 0.3535 0.2389 -0.0073 -0.0647 -0.0421 107 ARG A CZ  
600  N NH1 . ARG A 90  ? 0.2633 0.3687 0.2656 -0.0128 -0.0549 -0.0466 107 ARG A NH1 
601  N NH2 . ARG A 90  ? 0.2570 0.3667 0.2467 -0.0028 -0.0809 -0.0417 107 ARG A NH2 
602  N N   . ALA A 91  ? 0.2607 0.2729 0.1662 0.0074  -0.0338 -0.0084 108 ALA A N   
603  C CA  . ALA A 91  ? 0.2626 0.2601 0.1585 0.0127  -0.0378 0.0006  108 ALA A CA  
604  C C   . ALA A 91  ? 0.3046 0.2851 0.1674 0.0078  -0.0391 0.0073  108 ALA A C   
605  O O   . ALA A 91  ? 0.3118 0.2814 0.1610 0.0123  -0.0499 0.0166  108 ALA A O   
606  C CB  . ALA A 91  ? 0.2555 0.2467 0.1613 0.0134  -0.0272 0.0009  108 ALA A CB  
607  N N   . VAL A 92  ? 0.2910 0.2682 0.1400 -0.0011 -0.0279 0.0030  109 VAL A N   
608  C CA  . VAL A 92  ? 0.3329 0.2953 0.1474 -0.0075 -0.0261 0.0075  109 VAL A CA  
609  C C   . VAL A 92  ? 0.3688 0.3339 0.1660 -0.0068 -0.0422 0.0089  109 VAL A C   
610  O O   . VAL A 92  ? 0.4038 0.3548 0.1722 -0.0072 -0.0500 0.0189  109 VAL A O   
611  C CB  . VAL A 92  ? 0.3663 0.3289 0.1751 -0.0165 -0.0096 -0.0011 109 VAL A CB  
612  C CG1 . VAL A 92  ? 0.3940 0.3447 0.1646 -0.0245 -0.0069 0.0002  109 VAL A CG1 
613  C CG2 . VAL A 92  ? 0.3533 0.3125 0.1763 -0.0178 0.0042  -0.0005 109 VAL A CG2 
614  N N   . ALA A 93  ? 0.3583 0.3413 0.1722 -0.0064 -0.0483 -0.0005 110 ALA A N   
615  C CA  . ALA A 93  ? 0.3697 0.3587 0.1704 -0.0069 -0.0651 -0.0014 110 ALA A CA  
616  C C   . ALA A 93  ? 0.3745 0.3658 0.1834 0.0037  -0.0836 0.0087  110 ALA A C   
617  O O   . ALA A 93  ? 0.4201 0.4103 0.2095 0.0044  -0.1003 0.0135  110 ALA A O   
618  C CB  . ALA A 93  ? 0.3613 0.3689 0.1822 -0.0107 -0.0657 -0.0150 110 ALA A CB  
619  N N   . PHE A 94  ? 0.3607 0.3554 0.1986 0.0122  -0.0814 0.0113  111 PHE A N   
620  C CA  . PHE A 94  ? 0.3609 0.3549 0.2107 0.0242  -0.0964 0.0204  111 PHE A CA  
621  C C   . PHE A 94  ? 0.4194 0.3859 0.2436 0.0265  -0.0971 0.0351  111 PHE A C   
622  O O   . PHE A 94  ? 0.4420 0.4026 0.2759 0.0375  -0.1092 0.0440  111 PHE A O   
623  C CB  . PHE A 94  ? 0.3366 0.3441 0.2272 0.0319  -0.0913 0.0150  111 PHE A CB  
624  C CG  . PHE A 94  ? 0.3518 0.3870 0.2713 0.0315  -0.0944 0.0037  111 PHE A CG  
625  C CD1 . PHE A 94  ? 0.3552 0.4047 0.2760 0.0314  -0.1111 0.0017  111 PHE A CD1 
626  C CD2 . PHE A 94  ? 0.3449 0.3919 0.2896 0.0301  -0.0808 -0.0048 111 PHE A CD2 
627  C CE1 . PHE A 94  ? 0.3617 0.4372 0.3120 0.0292  -0.1127 -0.0092 111 PHE A CE1 
628  C CE2 . PHE A 94  ? 0.3266 0.3975 0.2969 0.0279  -0.0817 -0.0140 111 PHE A CE2 
629  C CZ  . PHE A 94  ? 0.3214 0.4068 0.2961 0.0271  -0.0970 -0.0166 111 PHE A CZ  
630  N N   . ASN A 95  ? 0.4091 0.3583 0.2037 0.0164  -0.0834 0.0376  112 ASN A N   
631  C CA  . ASN A 95  ? 0.4808 0.4020 0.2480 0.0155  -0.0817 0.0524  112 ASN A CA  
632  C C   . ASN A 95  ? 0.4480 0.3596 0.2396 0.0229  -0.0765 0.0562  112 ASN A C   
633  O O   . ASN A 95  ? 0.5043 0.3946 0.2871 0.0285  -0.0838 0.0696  112 ASN A O   
634  C CB  . ASN A 95  ? 0.5455 0.4561 0.2847 0.0193  -0.1029 0.0657  112 ASN A CB  
635  C CG  . ASN A 95  ? 0.7286 0.6071 0.4306 0.0149  -0.0994 0.0825  112 ASN A CG  
636  O OD1 . ASN A 95  ? 0.7912 0.6600 0.4728 0.0026  -0.0802 0.0811  112 ASN A OD1 
637  N ND2 . ASN A 95  ? 0.7240 0.5915 0.4278 0.0246  -0.1144 0.0967  112 ASN A ND2 
638  N N   . LYS A 96  ? 0.3802 0.3058 0.2014 0.0227  -0.0643 0.0443  113 LYS A N   
639  C CA  . LYS A 96  ? 0.3768 0.2951 0.2202 0.0280  -0.0582 0.0443  113 LYS A CA  
640  C C   . LYS A 96  ? 0.4198 0.3179 0.2480 0.0186  -0.0429 0.0484  113 LYS A C   
641  O O   . LYS A 96  ? 0.4308 0.3302 0.2439 0.0077  -0.0311 0.0452  113 LYS A O   
642  C CB  . LYS A 96  ? 0.3618 0.3039 0.2390 0.0303  -0.0521 0.0301  113 LYS A CB  
643  C CG  . LYS A 96  ? 0.3809 0.3441 0.2805 0.0393  -0.0648 0.0254  113 LYS A CG  
644  C CD  . LYS A 96  ? 0.4125 0.3653 0.3206 0.0520  -0.0781 0.0336  113 LYS A CD  
645  C CE  . LYS A 96  ? 0.4304 0.4070 0.3664 0.0619  -0.0912 0.0285  113 LYS A CE  
646  N NZ  . LYS A 96  ? 0.4016 0.3672 0.3507 0.0763  -0.1039 0.0362  113 LYS A NZ  
647  N N   . ARG A 97  ? 0.3749 0.2544 0.2103 0.0229  -0.0425 0.0542  114 ARG A N   
648  C CA  . ARG A 97  ? 0.3879 0.2523 0.2197 0.0135  -0.0271 0.0548  114 ARG A CA  
649  C C   . ARG A 97  ? 0.3556 0.2405 0.2137 0.0109  -0.0164 0.0396  114 ARG A C   
650  O O   . ARG A 97  ? 0.3335 0.2313 0.2161 0.0191  -0.0204 0.0317  114 ARG A O   
651  C CB  . ARG A 97  ? 0.4214 0.2581 0.2551 0.0183  -0.0303 0.0643  114 ARG A CB  
652  C CG  . ARG A 97  ? 0.4950 0.3146 0.3237 0.0060  -0.0144 0.0654  114 ARG A CG  
653  C CD  . ARG A 97  ? 0.5990 0.3817 0.4134 0.0058  -0.0168 0.0808  114 ARG A CD  
654  N NE  . ARG A 97  ? 0.6814 0.4536 0.5211 0.0175  -0.0237 0.0784  114 ARG A NE  
655  C CZ  . ARG A 97  ? 0.7269 0.4709 0.5705 0.0147  -0.0188 0.0824  114 ARG A CZ  
656  N NH1 . ARG A 97  ? 0.8078 0.5318 0.6325 -0.0005 -0.0068 0.0903  114 ARG A NH1 
657  N NH2 . ARG A 97  ? 0.7549 0.4901 0.6232 0.0267  -0.0250 0.0775  114 ARG A NH2 
658  N N   . ILE A 98  ? 0.3228 0.2114 0.1756 -0.0004 -0.0028 0.0356  115 ILE A N   
659  C CA  . ILE A 98  ? 0.3027 0.2126 0.1770 -0.0030 0.0049  0.0229  115 ILE A CA  
660  C C   . ILE A 98  ? 0.3251 0.2287 0.2050 -0.0123 0.0173  0.0207  115 ILE A C   
661  O O   . ILE A 98  ? 0.3351 0.2265 0.1989 -0.0213 0.0257  0.0264  115 ILE A O   
662  C CB  . ILE A 98  ? 0.2889 0.2160 0.1580 -0.0063 0.0071  0.0178  115 ILE A CB  
663  C CG1 . ILE A 98  ? 0.3046 0.2430 0.1761 0.0018  -0.0055 0.0167  115 ILE A CG1 
664  C CG2 . ILE A 98  ? 0.2836 0.2276 0.1725 -0.0100 0.0159  0.0077  115 ILE A CG2 
665  C CD1 . ILE A 98  ? 0.3264 0.2731 0.1841 -0.0027 -0.0052 0.0139  115 ILE A CD1 
666  N N   . LEU A 99  ? 0.3128 0.2258 0.2150 -0.0111 0.0186  0.0120  116 LEU A N   
667  C CA  . LEU A 99  ? 0.2802 0.1935 0.1934 -0.0200 0.0282  0.0072  116 LEU A CA  
668  C C   . LEU A 99  ? 0.2550 0.1935 0.1854 -0.0203 0.0294  -0.0028 116 LEU A C   
669  O O   . LEU A 99  ? 0.2354 0.1841 0.1761 -0.0140 0.0234  -0.0083 116 LEU A O   
670  C CB  . LEU A 99  ? 0.2992 0.1973 0.2213 -0.0192 0.0266  0.0057  116 LEU A CB  
671  C CG  . LEU A 99  ? 0.3206 0.2230 0.2582 -0.0288 0.0339  -0.0022 116 LEU A CG  
672  C CD1 . LEU A 99  ? 0.3600 0.2565 0.2917 -0.0412 0.0451  0.0025  116 LEU A CD1 
673  C CD2 . LEU A 99  ? 0.3337 0.2208 0.2801 -0.0279 0.0315  -0.0067 116 LEU A CD2 
674  N N   . CYS A 100 ? 0.2420 0.1899 0.1756 -0.0273 0.0375  -0.0049 117 CYS A N   
675  C CA  . CYS A 100 ? 0.2208 0.1901 0.1725 -0.0273 0.0378  -0.0126 117 CYS A CA  
676  C C   . CYS A 100 ? 0.2533 0.2272 0.2220 -0.0348 0.0424  -0.0174 117 CYS A C   
677  O O   . CYS A 100 ? 0.2755 0.2405 0.2431 -0.0432 0.0509  -0.0154 117 CYS A O   
678  C CB  . CYS A 100 ? 0.2256 0.2049 0.1754 -0.0279 0.0424  -0.0133 117 CYS A CB  
679  S SG  . CYS A 100 ? 0.2515 0.2310 0.1865 -0.0205 0.0351  -0.0110 117 CYS A SG  
680  N N   . LEU A 101 ? 0.2267 0.2149 0.2103 -0.0329 0.0365  -0.0236 118 LEU A N   
681  C CA  . LEU A 101 ? 0.2207 0.2165 0.2218 -0.0396 0.0368  -0.0297 118 LEU A CA  
682  C C   . LEU A 101 ? 0.2079 0.2261 0.2257 -0.0383 0.0340  -0.0330 118 LEU A C   
683  O O   . LEU A 101 ? 0.2016 0.2277 0.2172 -0.0316 0.0268  -0.0327 118 LEU A O   
684  C CB  . LEU A 101 ? 0.2497 0.2406 0.2500 -0.0382 0.0296  -0.0345 118 LEU A CB  
685  C CG  . LEU A 101 ? 0.2747 0.2422 0.2615 -0.0359 0.0305  -0.0313 118 LEU A CG  
686  C CD1 . LEU A 101 ? 0.3089 0.2738 0.2969 -0.0327 0.0245  -0.0391 118 LEU A CD1 
687  C CD2 . LEU A 101 ? 0.3510 0.3020 0.3380 -0.0453 0.0385  -0.0281 118 LEU A CD2 
688  N N   . PHE A 102 ? 0.1955 0.2236 0.2315 -0.0447 0.0399  -0.0357 119 PHE A N   
689  C CA  . PHE A 102 ? 0.1860 0.2353 0.2430 -0.0421 0.0371  -0.0383 119 PHE A CA  
690  C C   . PHE A 102 ? 0.1684 0.2327 0.2510 -0.0489 0.0342  -0.0445 119 PHE A C   
691  O O   . PHE A 102 ? 0.1901 0.2504 0.2799 -0.0584 0.0422  -0.0471 119 PHE A O   
692  C CB  . PHE A 102 ? 0.1712 0.2228 0.2319 -0.0415 0.0481  -0.0374 119 PHE A CB  
693  C CG  . PHE A 102 ? 0.1618 0.2334 0.2486 -0.0372 0.0458  -0.0406 119 PHE A CG  
694  C CD1 . PHE A 102 ? 0.1659 0.2414 0.2514 -0.0282 0.0359  -0.0379 119 PHE A CD1 
695  C CD2 . PHE A 102 ? 0.1828 0.2691 0.2977 -0.0420 0.0534  -0.0460 119 PHE A CD2 
696  C CE1 . PHE A 102 ? 0.1761 0.2668 0.2868 -0.0228 0.0324  -0.0393 119 PHE A CE1 
697  C CE2 . PHE A 102 ? 0.1733 0.2786 0.3170 -0.0361 0.0500  -0.0491 119 PHE A CE2 
698  C CZ  . PHE A 102 ? 0.1635 0.2696 0.3047 -0.0258 0.0387  -0.0451 119 PHE A CZ  
699  N N   . ARG A 103 ? 0.1589 0.2408 0.2561 -0.0446 0.0223  -0.0463 120 ARG A N   
700  C CA  . ARG A 103 ? 0.1800 0.2803 0.3037 -0.0502 0.0157  -0.0524 120 ARG A CA  
701  C C   . ARG A 103 ? 0.1688 0.2903 0.3242 -0.0470 0.0165  -0.0535 120 ARG A C   
702  O O   . ARG A 103 ? 0.1803 0.3115 0.3418 -0.0381 0.0057  -0.0502 120 ARG A O   
703  C CB  . ARG A 103 ? 0.1781 0.2834 0.2939 -0.0484 -0.0011 -0.0538 120 ARG A CB  
704  C CG  . ARG A 103 ? 0.1853 0.2711 0.2737 -0.0506 -0.0007 -0.0553 120 ARG A CG  
705  C CD  . ARG A 103 ? 0.1919 0.2830 0.2729 -0.0527 -0.0142 -0.0609 120 ARG A CD  
706  N NE  . ARG A 103 ? 0.1986 0.3057 0.2812 -0.0467 -0.0272 -0.0567 120 ARG A NE  
707  C CZ  . ARG A 103 ? 0.1559 0.2590 0.2207 -0.0386 -0.0293 -0.0493 120 ARG A CZ  
708  N NH1 . ARG A 103 ? 0.1710 0.2582 0.2181 -0.0350 -0.0198 -0.0461 120 ARG A NH1 
709  N NH2 . ARG A 103 ? 0.1938 0.3091 0.2595 -0.0346 -0.0419 -0.0442 120 ARG A NH2 
710  N N   . PRO A 104 ? 0.1543 0.2834 0.3323 -0.0540 0.0293  -0.0581 121 PRO A N   
711  C CA  . PRO A 104 ? 0.1472 0.2996 0.3621 -0.0500 0.0311  -0.0615 121 PRO A CA  
712  C C   . PRO A 104 ? 0.1796 0.3557 0.4222 -0.0469 0.0119  -0.0637 121 PRO A C   
713  O O   . PRO A 104 ? 0.1898 0.3828 0.4597 -0.0381 0.0072  -0.0634 121 PRO A O   
714  C CB  . PRO A 104 ? 0.1933 0.3499 0.4258 -0.0619 0.0501  -0.0675 121 PRO A CB  
715  C CG  . PRO A 104 ? 0.2223 0.3506 0.4176 -0.0689 0.0601  -0.0634 121 PRO A CG  
716  C CD  . PRO A 104 ? 0.1782 0.2945 0.3500 -0.0660 0.0440  -0.0602 121 PRO A CD  
717  N N   . GLN A 105 ? 0.1621 0.3400 0.3996 -0.0538 0.0000  -0.0664 122 GLN A N   
718  C CA  . GLN A 105 ? 0.1635 0.3649 0.4243 -0.0518 -0.0207 -0.0685 122 GLN A CA  
719  C C   . GLN A 105 ? 0.1961 0.3958 0.4413 -0.0389 -0.0367 -0.0592 122 GLN A C   
720  O O   . GLN A 105 ? 0.2128 0.4315 0.4764 -0.0348 -0.0555 -0.0580 122 GLN A O   
721  C CB  . GLN A 105 ? 0.2071 0.4091 0.4618 -0.0637 -0.0295 -0.0755 122 GLN A CB  
722  C CG  . GLN A 105 ? 0.2100 0.4189 0.4905 -0.0778 -0.0174 -0.0846 122 GLN A CG  
723  C CD  . GLN A 105 ? 0.2420 0.4446 0.5116 -0.0896 -0.0254 -0.0915 122 GLN A CD  
724  O OE1 . GLN A 105 ? 0.2409 0.4321 0.4818 -0.0892 -0.0355 -0.0925 122 GLN A OE1 
725  N NE2 . GLN A 105 ? 0.2541 0.4620 0.5439 -0.0995 -0.0198 -0.0963 122 GLN A NE2 
726  N N   . SER A 106 ? 0.1942 0.3718 0.4069 -0.0331 -0.0302 -0.0522 123 SER A N   
727  C CA  . SER A 106 ? 0.2116 0.3853 0.4110 -0.0221 -0.0416 -0.0425 123 SER A CA  
728  C C   . SER A 106 ? 0.2142 0.4013 0.4474 -0.0119 -0.0441 -0.0396 123 SER A C   
729  O O   . SER A 106 ? 0.2358 0.4231 0.4667 -0.0029 -0.0582 -0.0307 123 SER A O   
730  C CB  . SER A 106 ? 0.1978 0.3469 0.3622 -0.0194 -0.0311 -0.0374 123 SER A CB  
731  O OG  . SER A 106 ? 0.1905 0.3342 0.3641 -0.0177 -0.0141 -0.0391 123 SER A OG  
732  N N   . GLY A 107 ? 0.1698 0.3666 0.4338 -0.0131 -0.0297 -0.0467 124 GLY A N   
733  C CA  . GLY A 107 ? 0.2003 0.4080 0.4985 -0.0025 -0.0279 -0.0465 124 GLY A CA  
734  C C   . GLY A 107 ? 0.2209 0.4088 0.5035 0.0038  -0.0139 -0.0440 124 GLY A C   
735  O O   . GLY A 107 ? 0.2470 0.4408 0.5578 0.0129  -0.0097 -0.0458 124 GLY A O   
736  N N   . ARG A 108 ? 0.2283 0.3936 0.4694 -0.0004 -0.0069 -0.0410 125 ARG A N   
737  C CA  . ARG A 108 ? 0.2267 0.3742 0.4520 0.0038  0.0053  -0.0399 125 ARG A CA  
738  C C   . ARG A 108 ? 0.2428 0.3880 0.4699 -0.0026 0.0274  -0.0489 125 ARG A C   
739  O O   . ARG A 108 ? 0.2139 0.3653 0.4445 -0.0123 0.0347  -0.0538 125 ARG A O   
740  C CB  . ARG A 108 ? 0.2539 0.3809 0.4366 0.0025  0.0016  -0.0326 125 ARG A CB  
741  C CG  . ARG A 108 ? 0.3443 0.4719 0.5182 0.0066  -0.0176 -0.0233 125 ARG A CG  
742  C CD  . ARG A 108 ? 0.3165 0.4254 0.4547 0.0064  -0.0177 -0.0170 125 ARG A CD  
743  N NE  . ARG A 108 ? 0.2437 0.3526 0.3695 0.0084  -0.0338 -0.0077 125 ARG A NE  
744  C CZ  . ARG A 108 ? 0.2701 0.3710 0.3930 0.0146  -0.0401 0.0016  125 ARG A CZ  
745  N NH1 . ARG A 108 ? 0.2752 0.3677 0.4106 0.0202  -0.0326 0.0016  125 ARG A NH1 
746  N NH2 . ARG A 108 ? 0.3553 0.4552 0.4611 0.0143  -0.0538 0.0110  125 ARG A NH2 
747  N N   . VAL A 109 ? 0.2150 0.3498 0.4381 0.0020  0.0384  -0.0512 126 VAL A N   
748  C CA  . VAL A 109 ? 0.2144 0.3410 0.4244 -0.0047 0.0591  -0.0582 126 VAL A CA  
749  C C   . VAL A 109 ? 0.2042 0.3080 0.3703 -0.0067 0.0590  -0.0529 126 VAL A C   
750  O O   . VAL A 109 ? 0.2113 0.3055 0.3683 -0.0002 0.0526  -0.0491 126 VAL A O   
751  C CB  . VAL A 109 ? 0.1925 0.3244 0.4280 0.0011  0.0723  -0.0675 126 VAL A CB  
752  C CG1 . VAL A 109 ? 0.2553 0.3818 0.4757 -0.0083 0.0951  -0.0757 126 VAL A CG1 
753  C CG2 . VAL A 109 ? 0.2265 0.3839 0.5129 0.0066  0.0680  -0.0718 126 VAL A CG2 
754  N N   . LEU A 110 ? 0.1623 0.2574 0.3034 -0.0159 0.0656  -0.0522 127 LEU A N   
755  C CA  . LEU A 110 ? 0.1965 0.2725 0.2998 -0.0171 0.0641  -0.0472 127 LEU A CA  
756  C C   . LEU A 110 ? 0.1848 0.2515 0.2766 -0.0155 0.0741  -0.0517 127 LEU A C   
757  O O   . LEU A 110 ? 0.2053 0.2746 0.3034 -0.0189 0.0892  -0.0593 127 LEU A O   
758  C CB  . LEU A 110 ? 0.1924 0.2597 0.2746 -0.0262 0.0685  -0.0449 127 LEU A CB  
759  C CG  . LEU A 110 ? 0.2119 0.2608 0.2583 -0.0266 0.0664  -0.0398 127 LEU A CG  
760  C CD1 . LEU A 110 ? 0.2129 0.2607 0.2540 -0.0204 0.0514  -0.0349 127 LEU A CD1 
761  C CD2 . LEU A 110 ? 0.2440 0.2823 0.2735 -0.0346 0.0707  -0.0364 127 LEU A CD2 
762  N N   . SER A 111 ? 0.1892 0.2453 0.2638 -0.0114 0.0662  -0.0479 128 SER A N   
763  C CA  . SER A 111 ? 0.1996 0.2447 0.2580 -0.0113 0.0728  -0.0526 128 SER A CA  
764  C C   . SER A 111 ? 0.2207 0.2603 0.2600 -0.0190 0.0876  -0.0579 128 SER A C   
765  O O   . SER A 111 ? 0.2311 0.2653 0.2504 -0.0249 0.0878  -0.0527 128 SER A O   
766  C CB  . SER A 111 ? 0.2035 0.2384 0.2386 -0.0104 0.0620  -0.0464 128 SER A CB  
767  O OG  . SER A 111 ? 0.2153 0.2408 0.2358 -0.0114 0.0667  -0.0520 128 SER A OG  
768  N N   . ALA A 112 ? 0.2259 0.2643 0.2682 -0.0192 0.0998  -0.0680 129 ALA A N   
769  C CA  . ALA A 112 ? 0.2832 0.3146 0.2997 -0.0277 0.1146  -0.0733 129 ALA A CA  
770  C C   . ALA A 112 ? 0.2892 0.3056 0.2651 -0.0314 0.1072  -0.0673 129 ALA A C   
771  O O   . ALA A 112 ? 0.2897 0.2983 0.2375 -0.0391 0.1143  -0.0655 129 ALA A O   
772  C CB  . ALA A 112 ? 0.2643 0.2957 0.2896 -0.0267 0.1262  -0.0857 129 ALA A CB  
773  N N   . MET A 113 ? 0.2537 0.2662 0.2263 -0.0262 0.0929  -0.0638 130 MET A N   
774  C CA  . MET A 113 ? 0.2947 0.2968 0.2348 -0.0289 0.0843  -0.0590 130 MET A CA  
775  C C   . MET A 113 ? 0.3123 0.3119 0.2416 -0.0299 0.0765  -0.0473 130 MET A C   
776  O O   . MET A 113 ? 0.3335 0.3240 0.2352 -0.0324 0.0712  -0.0423 130 MET A O   
777  C CB  . MET A 113 ? 0.2905 0.2917 0.2352 -0.0243 0.0728  -0.0599 130 MET A CB  
778  C CG  . MET A 113 ? 0.3017 0.2997 0.2522 -0.0243 0.0803  -0.0725 130 MET A CG  
779  S SD  . MET A 113 ? 0.3512 0.3414 0.2713 -0.0326 0.0950  -0.0845 130 MET A SD  
780  C CE  . MET A 113 ? 0.3855 0.3679 0.2721 -0.0364 0.0802  -0.0822 130 MET A CE  
781  N N   . ILE A 114 ? 0.2319 0.2390 0.1830 -0.0277 0.0744  -0.0432 131 ILE A N   
782  C CA  . ILE A 114 ? 0.2729 0.2755 0.2159 -0.0291 0.0688  -0.0344 131 ILE A CA  
783  C C   . ILE A 114 ? 0.3144 0.3132 0.2524 -0.0370 0.0813  -0.0336 131 ILE A C   
784  O O   . ILE A 114 ? 0.3096 0.2953 0.2233 -0.0412 0.0813  -0.0267 131 ILE A O   
785  C CB  . ILE A 114 ? 0.2452 0.2567 0.2107 -0.0241 0.0593  -0.0316 131 ILE A CB  
786  C CG1 . ILE A 114 ? 0.2905 0.3051 0.2593 -0.0182 0.0491  -0.0313 131 ILE A CG1 
787  C CG2 . ILE A 114 ? 0.2476 0.2526 0.2050 -0.0255 0.0542  -0.0250 131 ILE A CG2 
788  C CD1 . ILE A 114 ? 0.2586 0.2657 0.2056 -0.0178 0.0432  -0.0293 131 ILE A CD1 
789  N N   . ARG A 115 ? 0.2740 0.2843 0.2365 -0.0390 0.0920  -0.0401 132 ARG A N   
790  C CA  . ARG A 115 ? 0.2802 0.2896 0.2420 -0.0484 0.1071  -0.0410 132 ARG A CA  
791  C C   . ARG A 115 ? 0.3231 0.3189 0.2491 -0.0555 0.1178  -0.0407 132 ARG A C   
792  O O   . ARG A 115 ? 0.3785 0.3621 0.2837 -0.0636 0.1235  -0.0336 132 ARG A O   
793  C CB  . ARG A 115 ? 0.3175 0.3459 0.3167 -0.0481 0.1171  -0.0507 132 ARG A CB  
794  C CG  . ARG A 115 ? 0.3882 0.4213 0.3961 -0.0586 0.1342  -0.0534 132 ARG A CG  
795  C CD  . ARG A 115 ? 0.3529 0.3881 0.3741 -0.0624 0.1282  -0.0477 132 ARG A CD  
796  N NE  . ARG A 115 ? 0.2962 0.3507 0.3560 -0.0561 0.1179  -0.0514 132 ARG A NE  
797  C CZ  . ARG A 115 ? 0.2653 0.3232 0.3379 -0.0593 0.1102  -0.0486 132 ARG A CZ  
798  N NH1 . ARG A 115 ? 0.3635 0.4053 0.4163 -0.0677 0.1123  -0.0425 132 ARG A NH1 
799  N NH2 . ARG A 115 ? 0.2623 0.3384 0.3666 -0.0540 0.0992  -0.0520 132 ARG A NH2 
800  N N   . GLY A 116 ? 0.3303 0.3260 0.2468 -0.0529 0.1193  -0.0478 133 GLY A N   
801  C CA  . GLY A 116 ? 0.3544 0.3387 0.2398 -0.0578 0.1230  -0.0475 133 GLY A CA  
802  C C   . GLY A 116 ? 0.3689 0.3378 0.2165 -0.0581 0.1109  -0.0380 133 GLY A C   
803  O O   . GLY A 116 ? 0.4012 0.3604 0.2204 -0.0629 0.1125  -0.0356 133 GLY A O   
804  N N   . ALA A 117 ? 0.3560 0.3235 0.2044 -0.0526 0.0974  -0.0326 134 ALA A N   
805  C CA  . ALA A 117 ? 0.3989 0.3535 0.2181 -0.0510 0.0829  -0.0225 134 ALA A CA  
806  C C   . ALA A 117 ? 0.4059 0.3456 0.2094 -0.0552 0.0830  -0.0094 134 ALA A C   
807  O O   . ALA A 117 ? 0.4459 0.3713 0.2196 -0.0552 0.0733  0.0003  134 ALA A O   
808  C CB  . ALA A 117 ? 0.3487 0.3104 0.1856 -0.0410 0.0653  -0.0212 134 ALA A CB  
809  N N   . ALA A 118 ? 0.4112 0.3533 0.2348 -0.0591 0.0929  -0.0089 135 ALA A N   
810  C CA  . ALA A 118 ? 0.4259 0.3516 0.2389 -0.0637 0.0932  0.0031  135 ALA A CA  
811  C C   . ALA A 118 ? 0.4770 0.3863 0.2533 -0.0730 0.1015  0.0102  135 ALA A C   
812  O O   . ALA A 118 ? 0.5419 0.4594 0.3211 -0.0779 0.1134  0.0027  135 ALA A O   
813  C CB  . ALA A 118 ? 0.4484 0.3825 0.2941 -0.0677 0.1023  -0.0004 135 ALA A CB  
814  N N   . ASP A 119 ? 0.5033 0.3913 0.2521 -0.0725 0.0911  0.0247  136 ASP A N   
815  C CA  . ASP A 119 ? 0.4934 0.3660 0.2139 -0.0792 0.0942  0.0344  136 ASP A CA  
816  C C   . ASP A 119 ? 0.5572 0.4112 0.2779 -0.0857 0.0996  0.0460  136 ASP A C   
817  O O   . ASP A 119 ? 0.5824 0.4207 0.2793 -0.0916 0.1021  0.0564  136 ASP A O   
818  C CB  . ASP A 119 ? 0.5598 0.4227 0.2490 -0.0730 0.0761  0.0429  136 ASP A CB  
819  C CG  . ASP A 119 ? 0.6087 0.4555 0.2937 -0.0647 0.0584  0.0559  136 ASP A CG  
820  O OD1 . ASP A 119 ? 0.7454 0.5876 0.4119 -0.0578 0.0409  0.0625  136 ASP A OD1 
821  O OD2 . ASP A 119 ? 0.5762 0.4163 0.2802 -0.0641 0.0608  0.0583  136 ASP A OD2 
822  N N   . GLY A 120 ? 0.5259 0.3808 0.2731 -0.0853 0.1015  0.0441  137 GLY A N   
823  C CA  . GLY A 120 ? 0.5639 0.4023 0.3180 -0.0926 0.1075  0.0519  137 GLY A CA  
824  C C   . GLY A 120 ? 0.5678 0.3757 0.3023 -0.0881 0.0935  0.0687  137 GLY A C   
825  O O   . GLY A 120 ? 0.6404 0.4310 0.3818 -0.0939 0.0976  0.0753  137 GLY A O   
826  N N   . SER A 121 ? 0.5628 0.3653 0.2780 -0.0768 0.0755  0.0749  138 SER A N   
827  C CA  . SER A 121 ? 0.5937 0.3711 0.2992 -0.0681 0.0586  0.0896  138 SER A CA  
828  C C   . SER A 121 ? 0.5884 0.3812 0.3159 -0.0506 0.0389  0.0832  138 SER A C   
829  O O   . SER A 121 ? 0.5526 0.3485 0.3114 -0.0436 0.0344  0.0776  138 SER A O   
830  C CB  . SER A 121 ? 0.6328 0.3946 0.3020 -0.0694 0.0523  0.1042  138 SER A CB  
831  O OG  . SER A 121 ? 0.8164 0.5594 0.4801 -0.0795 0.0628  0.1138  138 SER A OG  
832  N N   . ARG A 122 ? 0.5304 0.3335 0.2415 -0.0446 0.0278  0.0828  139 ARG A N   
833  C CA  . ARG A 122 ? 0.5649 0.3857 0.2988 -0.0296 0.0109  0.0759  139 ARG A CA  
834  C C   . ARG A 122 ? 0.4943 0.3442 0.2629 -0.0284 0.0175  0.0578  139 ARG A C   
835  O O   . ARG A 122 ? 0.4888 0.3515 0.2831 -0.0179 0.0079  0.0516  139 ARG A O   
836  C CB  . ARG A 122 ? 0.5915 0.4171 0.3004 -0.0254 -0.0032 0.0794  139 ARG A CB  
837  C CG  . ARG A 122 ? 0.6573 0.4877 0.3827 -0.0096 -0.0250 0.0818  139 ARG A CG  
838  C CD  . ARG A 122 ? 0.7186 0.5347 0.4112 -0.0055 -0.0432 0.0968  139 ARG A CD  
839  N NE  . ARG A 122 ? 0.7280 0.5520 0.4440 0.0107  -0.0642 0.0980  139 ARG A NE  
840  C CZ  . ARG A 122 ? 0.7081 0.5237 0.4516 0.0214  -0.0690 0.1007  139 ARG A CZ  
841  N NH1 . ARG A 122 ? 0.7512 0.5442 0.4966 0.0173  -0.0573 0.1056  139 ARG A NH1 
842  N NH2 . ARG A 122 ? 0.6465 0.4765 0.4171 0.0362  -0.0855 0.0976  139 ARG A NH2 
843  N N   . PHE A 123 ? 0.4389 0.2998 0.2083 -0.0385 0.0337  0.0494  140 PHE A N   
844  C CA  . PHE A 123 ? 0.3975 0.2840 0.1983 -0.0372 0.0391  0.0343  140 PHE A CA  
845  C C   . PHE A 123 ? 0.3949 0.2813 0.2084 -0.0475 0.0560  0.0308  140 PHE A C   
846  O O   . PHE A 123 ? 0.4050 0.2892 0.2039 -0.0579 0.0701  0.0307  140 PHE A O   
847  C CB  . PHE A 123 ? 0.4122 0.3149 0.2062 -0.0377 0.0403  0.0258  140 PHE A CB  
848  C CG  . PHE A 123 ? 0.3677 0.2938 0.1935 -0.0336 0.0412  0.0129  140 PHE A CG  
849  C CD1 . PHE A 123 ? 0.3402 0.2756 0.1907 -0.0371 0.0518  0.0064  140 PHE A CD1 
850  C CD2 . PHE A 123 ? 0.3658 0.3042 0.1963 -0.0271 0.0312  0.0078  140 PHE A CD2 
851  C CE1 . PHE A 123 ? 0.3384 0.2929 0.2151 -0.0330 0.0508  -0.0029 140 PHE A CE1 
852  C CE2 . PHE A 123 ? 0.3211 0.2773 0.1779 -0.0243 0.0325  -0.0018 140 PHE A CE2 
853  C CZ  . PHE A 123 ? 0.3130 0.2762 0.1914 -0.0267 0.0417  -0.0063 140 PHE A CZ  
854  N N   . GLN A 124 ? 0.3789 0.2684 0.2195 -0.0455 0.0549  0.0271  141 GLN A N   
855  C CA  . GLN A 124 ? 0.3503 0.2423 0.2080 -0.0555 0.0683  0.0229  141 GLN A CA  
856  C C   . GLN A 124 ? 0.3244 0.2426 0.2147 -0.0522 0.0677  0.0098  141 GLN A C   
857  O O   . GLN A 124 ? 0.3147 0.2416 0.2160 -0.0426 0.0562  0.0063  141 GLN A O   
858  C CB  . GLN A 124 ? 0.3618 0.2320 0.2216 -0.0581 0.0669  0.0295  141 GLN A CB  
859  C CG  . GLN A 124 ? 0.3882 0.2288 0.2150 -0.0632 0.0689  0.0450  141 GLN A CG  
860  C CD  . GLN A 124 ? 0.4986 0.3131 0.3287 -0.0650 0.0668  0.0522  141 GLN A CD  
861  O OE1 . GLN A 124 ? 0.4973 0.3158 0.3529 -0.0697 0.0715  0.0442  141 GLN A OE1 
862  N NE2 . GLN A 124 ? 0.5857 0.3724 0.3904 -0.0611 0.0587  0.0674  141 GLN A NE2 
863  N N   . VAL A 125 ? 0.3282 0.2594 0.2342 -0.0604 0.0803  0.0032  142 VAL A N   
864  C CA  . VAL A 125 ? 0.2909 0.2460 0.2292 -0.0580 0.0789  -0.0074 142 VAL A CA  
865  C C   . VAL A 125 ? 0.3082 0.2653 0.2667 -0.0679 0.0863  -0.0105 142 VAL A C   
866  O O   . VAL A 125 ? 0.3624 0.3177 0.3207 -0.0786 0.1009  -0.0100 142 VAL A O   
867  C CB  . VAL A 125 ? 0.3208 0.2937 0.2666 -0.0568 0.0853  -0.0142 142 VAL A CB  
868  C CG1 . VAL A 125 ? 0.3300 0.3255 0.3100 -0.0535 0.0818  -0.0227 142 VAL A CG1 
869  C CG2 . VAL A 125 ? 0.3230 0.2932 0.2492 -0.0488 0.0778  -0.0126 142 VAL A CG2 
870  N N   . TRP A 126 ? 0.2669 0.2280 0.2424 -0.0655 0.0770  -0.0145 143 TRP A N   
871  C CA  . TRP A 126 ? 0.2808 0.2453 0.2780 -0.0755 0.0813  -0.0194 143 TRP A CA  
872  C C   . TRP A 126 ? 0.2532 0.2461 0.2809 -0.0734 0.0757  -0.0295 143 TRP A C   
873  O O   . TRP A 126 ? 0.2670 0.2677 0.2963 -0.0642 0.0632  -0.0318 143 TRP A O   
874  C CB  . TRP A 126 ? 0.3219 0.2662 0.3141 -0.0763 0.0745  -0.0177 143 TRP A CB  
875  C CG  . TRP A 126 ? 0.3781 0.2908 0.3434 -0.0777 0.0773  -0.0061 143 TRP A CG  
876  C CD1 . TRP A 126 ? 0.4043 0.3051 0.3426 -0.0712 0.0757  0.0035  143 TRP A CD1 
877  C CD2 . TRP A 126 ? 0.4051 0.2927 0.3682 -0.0853 0.0799  -0.0026 143 TRP A CD2 
878  N NE1 . TRP A 126 ? 0.4407 0.3107 0.3595 -0.0738 0.0762  0.0144  143 TRP A NE1 
879  C CE2 . TRP A 126 ? 0.4047 0.2645 0.3385 -0.0824 0.0796  0.0112  143 TRP A CE2 
880  C CE3 . TRP A 126 ? 0.4271 0.3121 0.4105 -0.0952 0.0820  -0.0098 143 TRP A CE3 
881  C CZ2 . TRP A 126 ? 0.4297 0.2570 0.3544 -0.0877 0.0813  0.0194  143 TRP A CZ2 
882  C CZ3 . TRP A 126 ? 0.4815 0.3341 0.4564 -0.1018 0.0851  -0.0035 143 TRP A CZ3 
883  C CH2 . TRP A 126 ? 0.4896 0.3125 0.4354 -0.0976 0.0850  0.0118  143 TRP A CH2 
884  N N   . ASP A 127 ? 0.2633 0.2722 0.3155 -0.0821 0.0850  -0.0349 144 ASP A N   
885  C CA  A ASP A 127 ? 0.2418 0.2772 0.3266 -0.0812 0.0774  -0.0437 144 ASP A CA  
886  C CA  B ASP A 127 ? 0.2419 0.2774 0.3268 -0.0812 0.0774  -0.0437 144 ASP A CA  
887  C C   . ASP A 127 ? 0.2334 0.2657 0.3284 -0.0888 0.0708  -0.0484 144 ASP A C   
888  O O   . ASP A 127 ? 0.2713 0.2872 0.3628 -0.0998 0.0795  -0.0470 144 ASP A O   
889  C CB  A ASP A 127 ? 0.2322 0.2887 0.3447 -0.0867 0.0897  -0.0489 144 ASP A CB  
890  C CB  B ASP A 127 ? 0.2319 0.2890 0.3452 -0.0867 0.0894  -0.0491 144 ASP A CB  
891  C CG  A ASP A 127 ? 0.2491 0.3087 0.3532 -0.0793 0.0968  -0.0474 144 ASP A CG  
892  C CG  B ASP A 127 ? 0.2484 0.3124 0.3579 -0.0780 0.0945  -0.0485 144 ASP A CG  
893  O OD1 A ASP A 127 ? 0.2499 0.3209 0.3610 -0.0681 0.0867  -0.0488 144 ASP A OD1 
894  O OD1 B ASP A 127 ? 0.2684 0.3279 0.3623 -0.0669 0.0841  -0.0453 144 ASP A OD1 
895  O OD2 A ASP A 127 ? 0.2847 0.3330 0.3724 -0.0854 0.1126  -0.0446 144 ASP A OD2 
896  O OD2 B ASP A 127 ? 0.2721 0.3466 0.3964 -0.0830 0.1099  -0.0526 144 ASP A OD2 
897  N N   . TYR A 128 ? 0.2253 0.2717 0.3310 -0.0837 0.0555  -0.0540 145 TYR A N   
898  C CA  . TYR A 128 ? 0.2124 0.2545 0.3236 -0.0910 0.0483  -0.0606 145 TYR A CA  
899  C C   . TYR A 128 ? 0.2065 0.2744 0.3371 -0.0886 0.0327  -0.0684 145 TYR A C   
900  O O   . TYR A 128 ? 0.1843 0.2686 0.3192 -0.0790 0.0258  -0.0661 145 TYR A O   
901  C CB  . TYR A 128 ? 0.2305 0.2453 0.3125 -0.0863 0.0447  -0.0576 145 TYR A CB  
902  C CG  . TYR A 128 ? 0.2346 0.2554 0.3040 -0.0740 0.0321  -0.0580 145 TYR A CG  
903  C CD1 . TYR A 128 ? 0.2342 0.2588 0.2928 -0.0636 0.0321  -0.0510 145 TYR A CD1 
904  C CD2 . TYR A 128 ? 0.2355 0.2575 0.3026 -0.0741 0.0215  -0.0661 145 TYR A CD2 
905  C CE1 . TYR A 128 ? 0.2175 0.2474 0.2655 -0.0542 0.0223  -0.0508 145 TYR A CE1 
906  C CE2 . TYR A 128 ? 0.2321 0.2597 0.2856 -0.0645 0.0124  -0.0662 145 TYR A CE2 
907  C CZ  . TYR A 128 ? 0.2177 0.2493 0.2626 -0.0549 0.0132  -0.0579 145 TYR A CZ  
908  O OH  . TYR A 128 ? 0.2232 0.2602 0.2553 -0.0472 0.0057  -0.0574 145 TYR A OH  
909  N N   . GLU A 129 ? 0.2212 0.2909 0.3622 -0.0981 0.0264  -0.0774 146 GLU A N   
910  C CA  . GLU A 129 ? 0.2084 0.2991 0.3605 -0.0974 0.0089  -0.0852 146 GLU A CA  
911  C C   . GLU A 129 ? 0.2496 0.3243 0.3730 -0.0935 0.0004  -0.0882 146 GLU A C   
912  O O   . GLU A 129 ? 0.2429 0.2921 0.3516 -0.0969 0.0072  -0.0898 146 GLU A O   
913  C CB  . GLU A 129 ? 0.2324 0.3385 0.4159 -0.1119 0.0065  -0.0958 146 GLU A CB  
914  C CG  . GLU A 129 ? 0.2273 0.3553 0.4457 -0.1161 0.0155  -0.0952 146 GLU A CG  
915  C CD  . GLU A 129 ? 0.2620 0.4002 0.5051 -0.1276 0.0138  -0.1023 146 GLU A CD  
916  O OE1 . GLU A 129 ? 0.3404 0.4757 0.5781 -0.1324 0.0015  -0.1096 146 GLU A OE1 
917  O OE2 . GLU A 129 ? 0.2974 0.4433 0.5609 -0.1318 0.0260  -0.1005 146 GLU A OE2 
918  N N   . GLU A 130 ? 0.1819 0.3694 0.3914 -0.0304 0.0160  -0.1079 147 GLU A N   
919  C CA  . GLU A 130 ? 0.2017 0.3588 0.3692 -0.0175 0.0048  -0.0900 147 GLU A CA  
920  C C   . GLU A 130 ? 0.2182 0.3521 0.3504 -0.0306 0.0037  -0.0941 147 GLU A C   
921  O O   . GLU A 130 ? 0.2817 0.3795 0.3729 -0.0255 0.0061  -0.0820 147 GLU A O   
922  C CB  . GLU A 130 ? 0.2260 0.4061 0.4091 0.0056  -0.0179 -0.0803 147 GLU A CB  
923  C CG  . GLU A 130 ? 0.2489 0.4676 0.4585 0.0049  -0.0361 -0.0923 147 GLU A CG  
924  C CD  . GLU A 130 ? 0.2129 0.4203 0.3862 -0.0014 -0.0464 -0.0949 147 GLU A CD  
925  O OE1 . GLU A 130 ? 0.3011 0.4737 0.4289 0.0036  -0.0433 -0.0833 147 GLU A OE1 
926  O OE2 . GLU A 130 ? 0.2615 0.4973 0.4537 -0.0113 -0.0580 -0.1104 147 GLU A OE2 
927  N N   . GLY A 131 ? 0.2217 0.3757 0.3711 -0.0472 -0.0001 -0.1118 148 GLY A N   
928  C CA  . GLY A 131 ? 0.2510 0.3789 0.3670 -0.0600 -0.0034 -0.1186 148 GLY A CA  
929  C C   . GLY A 131 ? 0.2713 0.3507 0.3529 -0.0761 0.0151  -0.1164 148 GLY A C   
930  O O   . GLY A 131 ? 0.3300 0.3729 0.3744 -0.0785 0.0126  -0.1170 148 GLY A O   
931  N N   . GLU A 132 ? 0.2888 0.3654 0.3798 -0.0858 0.0331  -0.1136 149 GLU A N   
932  C CA  . GLU A 132 ? 0.2884 0.3220 0.3484 -0.1047 0.0504  -0.1100 149 GLU A CA  
933  C C   . GLU A 132 ? 0.3180 0.3138 0.3412 -0.0891 0.0545  -0.0900 149 GLU A C   
934  O O   . GLU A 132 ? 0.3401 0.2998 0.3362 -0.1022 0.0669  -0.0837 149 GLU A O   
935  C CB  . GLU A 132 ? 0.3247 0.3801 0.4115 -0.1268 0.0691  -0.1183 149 GLU A CB  
936  C CG  . GLU A 132 ? 0.3553 0.4512 0.4828 -0.1492 0.0697  -0.1387 149 GLU A CG  
937  C CD  . GLU A 132 ? 0.4819 0.5482 0.5881 -0.1733 0.0669  -0.1460 149 GLU A CD  
938  O OE1 . GLU A 132 ? 0.5589 0.6586 0.6962 -0.1868 0.0580  -0.1625 149 GLU A OE1 
939  O OE2 . GLU A 132 ? 0.4691 0.4780 0.5288 -0.1790 0.0726  -0.1357 149 GLU A OE2 
940  N N   . VAL A 133 ? 0.2672 0.2713 0.2891 -0.0628 0.0437  -0.0784 150 VAL A N   
941  C CA  . VAL A 133 ? 0.2588 0.2391 0.2573 -0.0507 0.0484  -0.0599 150 VAL A CA  
942  C C   . VAL A 133 ? 0.3075 0.2404 0.2637 -0.0510 0.0507  -0.0516 150 VAL A C   
943  O O   . VAL A 133 ? 0.3239 0.2310 0.2596 -0.0540 0.0588  -0.0400 150 VAL A O   
944  C CB  . VAL A 133 ? 0.2377 0.2386 0.2469 -0.0258 0.0368  -0.0479 150 VAL A CB  
945  C CG1 . VAL A 133 ? 0.2886 0.2836 0.2775 -0.0094 0.0250  -0.0420 150 VAL A CG1 
946  C CG2 . VAL A 133 ? 0.2723 0.2605 0.2721 -0.0204 0.0428  -0.0328 150 VAL A CG2 
947  N N   . GLU A 134 ? 0.3059 0.2258 0.2478 -0.0471 0.0427  -0.0584 151 GLU A N   
948  C CA  . GLU A 134 ? 0.3555 0.2270 0.2596 -0.0442 0.0447  -0.0531 151 GLU A CA  
949  C C   . GLU A 134 ? 0.4078 0.2442 0.2980 -0.0698 0.0562  -0.0547 151 GLU A C   
950  O O   . GLU A 134 ? 0.4023 0.2007 0.2652 -0.0679 0.0609  -0.0409 151 GLU A O   
951  C CB  . GLU A 134 ? 0.3635 0.2267 0.2547 -0.0367 0.0349  -0.0658 151 GLU A CB  
952  C CG  . GLU A 134 ? 0.3445 0.2316 0.2338 -0.0094 0.0256  -0.0596 151 GLU A CG  
953  C CD  . GLU A 134 ? 0.3177 0.2540 0.2362 -0.0081 0.0154  -0.0654 151 GLU A CD  
954  O OE1 . GLU A 134 ? 0.3100 0.2663 0.2559 -0.0262 0.0154  -0.0758 151 GLU A OE1 
955  O OE2 . GLU A 134 ? 0.3076 0.2641 0.2221 0.0114  0.0072  -0.0587 151 GLU A OE2 
956  N N   . ALA A 135 ? 0.3961 0.2463 0.3054 -0.0948 0.0602  -0.0703 152 ALA A N   
957  C CA  . ALA A 135 ? 0.4173 0.2383 0.3146 -0.1241 0.0730  -0.0710 152 ALA A CA  
958  C C   . ALA A 135 ? 0.4215 0.2433 0.3135 -0.1292 0.0856  -0.0567 152 ALA A C   
959  O O   . ALA A 135 ? 0.4998 0.2795 0.3606 -0.1417 0.0933  -0.0452 152 ALA A O   
960  C CB  . ALA A 135 ? 0.4217 0.2726 0.3500 -0.1504 0.0755  -0.0909 152 ALA A CB  
961  N N   . LEU A 136 ? 0.3823 0.2490 0.3024 -0.1200 0.0868  -0.0576 153 LEU A N   
962  C CA  . LEU A 136 ? 0.3623 0.2300 0.2748 -0.1250 0.0983  -0.0477 153 LEU A CA  
963  C C   . LEU A 136 ? 0.3845 0.2161 0.2612 -0.1089 0.0930  -0.0267 153 LEU A C   
964  O O   . LEU A 136 ? 0.4487 0.2538 0.2974 -0.1208 0.1009  -0.0153 153 LEU A O   
965  C CB  . LEU A 136 ? 0.3458 0.2643 0.2967 -0.1153 0.0988  -0.0556 153 LEU A CB  
966  C CG  . LEU A 136 ? 0.4187 0.3475 0.3691 -0.1174 0.1096  -0.0524 153 LEU A CG  
967  C CD1 . LEU A 136 ? 0.3992 0.3753 0.3951 -0.1061 0.1076  -0.0656 153 LEU A CD1 
968  C CD2 . LEU A 136 ? 0.4317 0.3358 0.3528 -0.1014 0.1024  -0.0328 153 LEU A CD2 
969  N N   . LEU A 137 ? 0.3823 0.2159 0.2598 -0.0822 0.0794  -0.0205 154 LEU A N   
970  C CA  . LEU A 137 ? 0.3931 0.1991 0.2433 -0.0654 0.0736  -0.0011 154 LEU A CA  
971  C C   . LEU A 137 ? 0.4486 0.2011 0.2640 -0.0730 0.0750  0.0057  154 LEU A C   
972  O O   . LEU A 137 ? 0.4863 0.2113 0.2756 -0.0711 0.0746  0.0229  154 LEU A O   
973  C CB  . LEU A 137 ? 0.3463 0.1700 0.2071 -0.0372 0.0616  0.0025  154 LEU A CB  
974  C CG  . LEU A 137 ? 0.3013 0.1691 0.1919 -0.0279 0.0579  0.0026  154 LEU A CG  
975  C CD1 . LEU A 137 ? 0.3558 0.2408 0.2539 -0.0045 0.0474  0.0063  154 LEU A CD1 
976  C CD2 . LEU A 137 ? 0.3457 0.2131 0.2301 -0.0283 0.0596  0.0163  154 LEU A CD2 
977  N N   . ASP A 138 ? 0.4493 0.1841 0.2632 -0.0823 0.0751  -0.0075 155 ASP A N   
978  C CA  . ASP A 138 ? 0.5379 0.2141 0.3188 -0.0929 0.0766  -0.0022 155 ASP A CA  
979  C C   . ASP A 138 ? 0.5596 0.2307 0.3284 -0.1146 0.0850  0.0072  155 ASP A C   
980  O O   . ASP A 138 ? 0.5855 0.2320 0.3322 -0.1078 0.0794  0.0221  155 ASP A O   
981  C CB  . ASP A 138 ? 0.5512 0.2140 0.3368 -0.1061 0.0754  -0.0219 155 ASP A CB  
982  C CG  . ASP A 138 ? 0.5723 0.2321 0.3575 -0.0792 0.0637  -0.0308 155 ASP A CG  
983  O OD1 . ASP A 138 ? 0.5608 0.2293 0.3432 -0.0501 0.0583  -0.0200 155 ASP A OD1 
984  O OD2 . ASP A 138 ? 0.5995 0.2491 0.3861 -0.0885 0.0604  -0.0495 155 ASP A OD2 
985  N N   . ARG A 139 ? 0.5119 0.2187 0.3011 -0.1360 0.0959  -0.0036 156 ARG A N   
986  C CA  . ARG A 139 ? 0.5298 0.2426 0.3091 -0.1521 0.1033  0.0016  156 ARG A CA  
987  C C   . ARG A 139 ? 0.5253 0.2407 0.2898 -0.1376 0.0979  0.0170  156 ARG A C   
988  O O   . ARG A 139 ? 0.6115 0.3086 0.3533 -0.1423 0.0959  0.0285  156 ARG A O   
989  C CB  . ARG A 139 ? 0.5554 0.3129 0.3638 -0.1721 0.1170  -0.0155 156 ARG A CB  
990  C CG  . ARG A 139 ? 0.5494 0.3180 0.3817 -0.1894 0.1205  -0.0328 156 ARG A CG  
991  C CD  . ARG A 139 ? 0.6008 0.3372 0.4130 -0.2080 0.1222  -0.0286 156 ARG A CD  
992  N NE  . ARG A 139 ? 0.6971 0.3813 0.4852 -0.1988 0.1101  -0.0207 156 ARG A NE  
993  C CZ  . ARG A 139 ? 0.6665 0.3391 0.4617 -0.1876 0.1003  -0.0303 156 ARG A CZ  
994  N NH1 . ARG A 139 ? 0.6305 0.3412 0.4581 -0.1880 0.0994  -0.0483 156 ARG A NH1 
995  N NH2 . ARG A 139 ? 0.7272 0.3496 0.4971 -0.1749 0.0902  -0.0235 156 ARG A NH2 
996  N N   . TYR A 140 ? 0.5328 0.2718 0.3114 -0.1210 0.0941  0.0178  157 TYR A N   
997  C CA  . TYR A 140 ? 0.5390 0.2872 0.3097 -0.1095 0.0869  0.0298  157 TYR A CA  
998  C C   . TYR A 140 ? 0.5486 0.2708 0.3025 -0.0909 0.0723  0.0474  157 TYR A C   
999  O O   . TYR A 140 ? 0.5948 0.3133 0.3353 -0.0905 0.0666  0.0588  157 TYR A O   
1000 C CB  . TYR A 140 ? 0.4894 0.2706 0.2829 -0.0981 0.0861  0.0259  157 TYR A CB  
1001 C CG  . TYR A 140 ? 0.5019 0.2951 0.2906 -0.0900 0.0781  0.0351  157 TYR A CG  
1002 C CD1 . TYR A 140 ? 0.4906 0.2819 0.2783 -0.0696 0.0629  0.0504  157 TYR A CD1 
1003 C CD2 . TYR A 140 ? 0.5085 0.3180 0.2964 -0.1035 0.0864  0.0267  157 TYR A CD2 
1004 C CE1 . TYR A 140 ? 0.4956 0.3006 0.2822 -0.0655 0.0550  0.0580  157 TYR A CE1 
1005 C CE2 . TYR A 140 ? 0.4822 0.2983 0.2619 -0.0989 0.0790  0.0334  157 TYR A CE2 
1006 C CZ  . TYR A 140 ? 0.4975 0.3115 0.2771 -0.0809 0.0626  0.0495  157 TYR A CZ  
1007 O OH  . TYR A 140 ? 0.5279 0.3501 0.3006 -0.0790 0.0547  0.0557  157 TYR A OH  
1008 N N   . PHE A 141 ? 0.5488 0.2544 0.3043 -0.0746 0.0663  0.0492  158 PHE A N   
1009 C CA  . PHE A 141 ? 0.5698 0.2598 0.3182 -0.0525 0.0531  0.0637  158 PHE A CA  
1010 C C   . PHE A 141 ? 0.7205 0.3660 0.4479 -0.0556 0.0510  0.0683  158 PHE A C   
1011 O O   . PHE A 141 ? 0.7378 0.3682 0.4620 -0.0356 0.0408  0.0786  158 PHE A O   
1012 C CB  . PHE A 141 ? 0.5452 0.2460 0.3077 -0.0280 0.0479  0.0631  158 PHE A CB  
1013 C CG  . PHE A 141 ? 0.5286 0.2733 0.3132 -0.0196 0.0444  0.0662  158 PHE A CG  
1014 C CD1 . PHE A 141 ? 0.5306 0.2959 0.3243 -0.0105 0.0337  0.0789  158 PHE A CD1 
1015 C CD2 . PHE A 141 ? 0.4730 0.2379 0.2709 -0.0234 0.0514  0.0569  158 PHE A CD2 
1016 C CE1 . PHE A 141 ? 0.4697 0.2729 0.2845 -0.0065 0.0294  0.0812  158 PHE A CE1 
1017 C CE2 . PHE A 141 ? 0.4629 0.2642 0.2811 -0.0168 0.0471  0.0604  158 PHE A CE2 
1018 C CZ  . PHE A 141 ? 0.4649 0.2841 0.2912 -0.0093 0.0358  0.0719  158 PHE A CZ  
1019 N N   . GLU A 142 ? 0.7493 0.3761 0.4655 -0.0801 0.0602  0.0612  159 GLU A N   
1020 C CA  . GLU A 142 ? 0.7990 0.3806 0.4955 -0.0851 0.0574  0.0669  159 GLU A CA  
1021 C C   . GLU A 142 ? 0.9125 0.4864 0.5921 -0.1053 0.0606  0.0770  159 GLU A C   
1022 O O   . GLU A 142 ? 0.9421 0.5425 0.6215 -0.1084 0.0613  0.0823  159 GLU A O   
1023 C CB  . GLU A 142 ? 0.8414 0.4018 0.5391 -0.0976 0.0636  0.0508  159 GLU A CB  
1024 C CG  . GLU A 142 ? 0.9846 0.5252 0.6845 -0.0736 0.0565  0.0442  159 GLU A CG  
1025 C CD  . GLU A 142 ? 0.9637 0.5056 0.6743 -0.0849 0.0619  0.0222  159 GLU A CD  
1026 O OE1 . GLU A 142 ? 1.0427 0.5787 0.7551 -0.1122 0.0679  0.0136  159 GLU A OE1 
1027 O OE2 . GLU A 142 ? 0.9770 0.5286 0.6960 -0.0662 0.0593  0.0133  159 GLU A OE2 
1028 N N   . ARG B 3   ? 0.6619 0.7009 0.7456 0.0007  -0.1454 -0.3503 20  ARG B N   
1029 C CA  . ARG B 3   ? 0.5818 0.6171 0.6694 0.0051  -0.1261 -0.3376 20  ARG B CA  
1030 C C   . ARG B 3   ? 0.5463 0.5981 0.6183 0.0132  -0.1237 -0.3222 20  ARG B C   
1031 O O   . ARG B 3   ? 0.5318 0.5815 0.5618 0.0209  -0.1260 -0.3211 20  ARG B O   
1032 C CB  . ARG B 3   ? 0.6133 0.6248 0.6739 0.0110  -0.1142 -0.3446 20  ARG B CB  
1033 C CG  . ARG B 3   ? 0.6346 0.6254 0.7189 0.0042  -0.1082 -0.3509 20  ARG B CG  
1034 C CD  . ARG B 3   ? 0.6422 0.6097 0.7014 0.0130  -0.0963 -0.3579 20  ARG B CD  
1035 N NE  . ARG B 3   ? 0.6116 0.5748 0.6873 0.0171  -0.0799 -0.3461 20  ARG B NE  
1036 C CZ  . ARG B 3   ? 0.5963 0.5655 0.6559 0.0281  -0.0668 -0.3387 20  ARG B CZ  
1037 N NH1 . ARG B 3   ? 0.6204 0.5972 0.6434 0.0356  -0.0658 -0.3417 20  ARG B NH1 
1038 N NH2 . ARG B 3   ? 0.5922 0.5582 0.6710 0.0306  -0.0541 -0.3270 20  ARG B NH2 
1039 N N   . PRO B 4   ? 0.6153 0.6800 0.7171 0.0103  -0.1183 -0.3092 21  PRO B N   
1040 C CA  . PRO B 4   ? 0.5207 0.5988 0.6069 0.0170  -0.1181 -0.2943 21  PRO B CA  
1041 C C   . PRO B 4   ? 0.4964 0.5657 0.5463 0.0244  -0.1036 -0.2847 21  PRO B C   
1042 O O   . PRO B 4   ? 0.5215 0.5783 0.5707 0.0249  -0.0904 -0.2873 21  PRO B O   
1043 C CB  . PRO B 4   ? 0.5429 0.6315 0.6738 0.0095  -0.1126 -0.2844 21  PRO B CB  
1044 C CG  . PRO B 4   ? 0.6887 0.7766 0.8532 -0.0012 -0.1195 -0.2976 21  PRO B CG  
1045 C CD  . PRO B 4   ? 0.6024 0.6670 0.7498 -0.0003 -0.1113 -0.3050 21  PRO B CD  
1046 N N   . ALA B 5   ? 0.4393 0.5147 0.4569 0.0303  -0.1064 -0.2726 22  ALA B N   
1047 C CA  . ALA B 5   ? 0.4270 0.4982 0.4141 0.0344  -0.0914 -0.2577 22  ALA B CA  
1048 C C   . ALA B 5   ? 0.3828 0.4614 0.3967 0.0314  -0.0843 -0.2438 22  ALA B C   
1049 O O   . ALA B 5   ? 0.3686 0.4574 0.3950 0.0308  -0.0939 -0.2379 22  ALA B O   
1050 C CB  . ALA B 5   ? 0.4511 0.5185 0.3860 0.0390  -0.0968 -0.2480 22  ALA B CB  
1051 N N   . LEU B 6   ? 0.3639 0.4364 0.3867 0.0298  -0.0674 -0.2388 23  LEU B N   
1052 C CA  . LEU B 6   ? 0.3268 0.3996 0.3791 0.0243  -0.0591 -0.2272 23  LEU B CA  
1053 C C   . LEU B 6   ? 0.3305 0.4021 0.3520 0.0273  -0.0458 -0.2099 23  LEU B C   
1054 O O   . LEU B 6   ? 0.3721 0.4412 0.3710 0.0314  -0.0348 -0.2094 23  LEU B O   
1055 C CB  . LEU B 6   ? 0.3266 0.3874 0.4200 0.0179  -0.0508 -0.2333 23  LEU B CB  
1056 C CG  . LEU B 6   ? 0.3814 0.4405 0.5020 0.0124  -0.0615 -0.2485 23  LEU B CG  
1057 C CD1 . LEU B 6   ? 0.3955 0.4358 0.5381 0.0086  -0.0523 -0.2524 23  LEU B CD1 
1058 C CD2 . LEU B 6   ? 0.3837 0.4543 0.5349 0.0044  -0.0699 -0.2451 23  LEU B CD2 
1059 N N   . TYR B 7   ? 0.2983 0.3721 0.3202 0.0246  -0.0454 -0.1934 24  TYR B N   
1060 C CA  . TYR B 7   ? 0.2733 0.3436 0.2661 0.0247  -0.0317 -0.1667 24  TYR B CA  
1061 C C   . TYR B 7   ? 0.2494 0.3099 0.2789 0.0165  -0.0190 -0.1472 24  TYR B C   
1062 O O   . TYR B 7   ? 0.2726 0.3315 0.3291 0.0111  -0.0231 -0.1418 24  TYR B O   
1063 C CB  . TYR B 7   ? 0.2795 0.3524 0.2327 0.0283  -0.0418 -0.1544 24  TYR B CB  
1064 C CG  . TYR B 7   ? 0.2881 0.3543 0.1990 0.0271  -0.0300 -0.1280 24  TYR B CG  
1065 C CD1 . TYR B 7   ? 0.2757 0.3334 0.1998 0.0207  -0.0189 -0.1021 24  TYR B CD1 
1066 C CD2 . TYR B 7   ? 0.3441 0.4036 0.2070 0.0277  -0.0281 -0.1197 24  TYR B CD2 
1067 C CE1 . TYR B 7   ? 0.2978 0.3478 0.1808 0.0176  -0.0092 -0.0774 24  TYR B CE1 
1068 C CE2 . TYR B 7   ? 0.3645 0.4106 0.1953 0.0212  -0.0168 -0.0916 24  TYR B CE2 
1069 C CZ  . TYR B 7   ? 0.3586 0.4030 0.1962 0.0175  -0.0087 -0.0734 24  TYR B CZ  
1070 O OH  . TYR B 7   ? 0.3552 0.3765 0.1674 0.0080  0.0007  -0.0449 24  TYR B OH  
1071 N N   . PHE B 8   ? 0.2357 0.2900 0.2659 0.0154  -0.0039 -0.1369 25  PHE B N   
1072 C CA  . PHE B 8   ? 0.2231 0.2630 0.2831 0.0074  0.0067  -0.1178 25  PHE B CA  
1073 C C   . PHE B 8   ? 0.2155 0.2514 0.2475 0.0041  0.0156  -0.0869 25  PHE B C   
1074 O O   . PHE B 8   ? 0.2409 0.2847 0.2378 0.0073  0.0208  -0.0807 25  PHE B O   
1075 C CB  . PHE B 8   ? 0.2627 0.2941 0.3470 0.0088  0.0151  -0.1257 25  PHE B CB  
1076 C CG  . PHE B 8   ? 0.2288 0.2408 0.3365 0.0007  0.0240  -0.1045 25  PHE B CG  
1077 C CD1 . PHE B 8   ? 0.2689 0.2638 0.4088 -0.0090 0.0216  -0.1044 25  PHE B CD1 
1078 C CD2 . PHE B 8   ? 0.2437 0.2542 0.3380 0.0009  0.0344  -0.0831 25  PHE B CD2 
1079 C CE1 . PHE B 8   ? 0.2491 0.2208 0.4040 -0.0179 0.0295  -0.0843 25  PHE B CE1 
1080 C CE2 . PHE B 8   ? 0.2445 0.2336 0.3559 -0.0071 0.0404  -0.0624 25  PHE B CE2 
1081 C CZ  . PHE B 8   ? 0.2452 0.2124 0.3846 -0.0163 0.0381  -0.0628 25  PHE B CZ  
1082 N N   . CYS B 9   ? 0.2014 0.2237 0.2486 -0.0039 0.0185  -0.0680 26  CYS B N   
1083 C CA  . CYS B 9   ? 0.2064 0.2182 0.2279 -0.0089 0.0265  -0.0375 26  CYS B CA  
1084 C C   . CYS B 9   ? 0.1804 0.1721 0.2278 -0.0177 0.0368  -0.0213 26  CYS B C   
1085 O O   . CYS B 9   ? 0.2171 0.1958 0.2996 -0.0235 0.0366  -0.0261 26  CYS B O   
1086 C CB  . CYS B 9   ? 0.2040 0.2121 0.2121 -0.0098 0.0207  -0.0270 26  CYS B CB  
1087 S SG  . CYS B 9   ? 0.2351 0.2619 0.2223 0.0012  0.0031  -0.0477 26  CYS B SG  
1088 N N   . GLY B 10  ? 0.1673 0.2443 0.2152 -0.0022 0.0377  -0.0679 27  GLY B N   
1089 C CA  . GLY B 10  ? 0.1613 0.2338 0.2197 -0.0039 0.0384  -0.0616 27  GLY B CA  
1090 C C   . GLY B 10  ? 0.1610 0.2342 0.2127 -0.0031 0.0441  -0.0594 27  GLY B C   
1091 O O   . GLY B 10  ? 0.1902 0.2683 0.2370 -0.0017 0.0492  -0.0644 27  GLY B O   
1092 N N   . SER B 11  ? 0.1653 0.2328 0.2157 -0.0045 0.0433  -0.0514 28  SER B N   
1093 C CA  . SER B 11  ? 0.1552 0.2211 0.1999 -0.0058 0.0449  -0.0492 28  SER B CA  
1094 C C   . SER B 11  ? 0.1722 0.2464 0.2324 -0.0057 0.0453  -0.0554 28  SER B C   
1095 O O   . SER B 11  ? 0.1725 0.2484 0.2484 -0.0028 0.0413  -0.0594 28  SER B O   
1096 C CB  . SER B 11  ? 0.1689 0.2233 0.2072 -0.0062 0.0401  -0.0421 28  SER B CB  
1097 O OG  . SER B 11  ? 0.1866 0.2367 0.2195 -0.0086 0.0374  -0.0416 28  SER B OG  
1098 N N   . ILE B 12  ? 0.1437 0.2226 0.2017 -0.0087 0.0508  -0.0550 29  ILE B N   
1099 C CA  . ILE B 12  ? 0.1599 0.2513 0.2387 -0.0097 0.0535  -0.0584 29  ILE B CA  
1100 C C   . ILE B 12  ? 0.1792 0.2677 0.2612 -0.0166 0.0486  -0.0531 29  ILE B C   
1101 O O   . ILE B 12  ? 0.1712 0.2588 0.2656 -0.0171 0.0375  -0.0523 29  ILE B O   
1102 C CB  . ILE B 12  ? 0.1524 0.2541 0.2293 -0.0082 0.0669  -0.0625 29  ILE B CB  
1103 C CG1 . ILE B 12  ? 0.1672 0.2671 0.2361 -0.0011 0.0679  -0.0704 29  ILE B CG1 
1104 C CG2 . ILE B 12  ? 0.1732 0.2922 0.2777 -0.0086 0.0732  -0.0646 29  ILE B CG2 
1105 C CD1 . ILE B 12  ? 0.1869 0.2920 0.2426 0.0022  0.0804  -0.0751 29  ILE B CD1 
1106 N N   . ARG B 13  ? 0.1789 0.2628 0.2480 -0.0220 0.0547  -0.0494 30  ARG B N   
1107 C CA  . ARG B 13  ? 0.1920 0.2679 0.2626 -0.0300 0.0479  -0.0457 30  ARG B CA  
1108 C C   . ARG B 13  ? 0.2010 0.2554 0.2488 -0.0284 0.0367  -0.0437 30  ARG B C   
1109 O O   . ARG B 13  ? 0.2204 0.2646 0.2673 -0.0337 0.0259  -0.0432 30  ARG B O   
1110 C CB  . ARG B 13  ? 0.1786 0.2510 0.2414 -0.0366 0.0581  -0.0415 30  ARG B CB  
1111 C CG  . ARG B 13  ? 0.1894 0.2831 0.2741 -0.0389 0.0716  -0.0416 30  ARG B CG  
1112 C CD  . ARG B 13  ? 0.1804 0.2689 0.2569 -0.0465 0.0832  -0.0346 30  ARG B CD  
1113 N NE  . ARG B 13  ? 0.2092 0.3193 0.3033 -0.0469 0.1004  -0.0338 30  ARG B NE  
1114 C CZ  . ARG B 13  ? 0.2548 0.3630 0.3384 -0.0512 0.1162  -0.0263 30  ARG B CZ  
1115 N NH1 . ARG B 13  ? 0.2391 0.3238 0.2981 -0.0564 0.1153  -0.0188 30  ARG B NH1 
1116 N NH2 . ARG B 13  ? 0.2407 0.3690 0.3367 -0.0491 0.1344  -0.0259 30  ARG B NH2 
1117 N N   . GLY B 14  ? 0.1740 0.2215 0.2041 -0.0213 0.0389  -0.0427 31  GLY B N   
1118 C CA  . GLY B 14  ? 0.1852 0.2151 0.1956 -0.0181 0.0315  -0.0400 31  GLY B CA  
1119 C C   . GLY B 14  ? 0.2114 0.2419 0.2316 -0.0165 0.0204  -0.0402 31  GLY B C   
1120 O O   . GLY B 14  ? 0.2622 0.2757 0.2616 -0.0139 0.0134  -0.0372 31  GLY B O   
1121 N N   . GLY B 15  ? 0.2086 0.2566 0.2574 -0.0164 0.0189  -0.0433 32  GLY B N   
1122 C CA  . GLY B 15  ? 0.2189 0.2674 0.2799 -0.0128 0.0077  -0.0427 32  GLY B CA  
1123 C C   . GLY B 15  ? 0.1816 0.2401 0.2598 -0.0076 0.0129  -0.0453 32  GLY B C   
1124 O O   . GLY B 15  ? 0.1934 0.2510 0.2631 -0.0064 0.0219  -0.0456 32  GLY B O   
1125 N N   . ARG B 16  ? 0.1914 0.2590 0.2952 -0.0040 0.0059  -0.0478 33  ARG B N   
1126 C CA  . ARG B 16  ? 0.1765 0.2500 0.2972 0.0023  0.0099  -0.0525 33  ARG B CA  
1127 C C   . ARG B 16  ? 0.1842 0.2424 0.3035 0.0074  -0.0005 -0.0476 33  ARG B C   
1128 O O   . ARG B 16  ? 0.2065 0.2660 0.3448 0.0139  -0.0023 -0.0515 33  ARG B O   
1129 C CB  . ARG B 16  ? 0.1971 0.2921 0.3498 0.0054  0.0135  -0.0595 33  ARG B CB  
1130 C CG  . ARG B 16  ? 0.2047 0.3127 0.3568 -0.0010 0.0258  -0.0613 33  ARG B CG  
1131 C CD  . ARG B 16  ? 0.2258 0.3545 0.4022 0.0035  0.0383  -0.0682 33  ARG B CD  
1132 N NE  . ARG B 16  ? 0.1898 0.3129 0.3523 0.0097  0.0477  -0.0753 33  ARG B NE  
1133 C CZ  . ARG B 16  ? 0.2247 0.3595 0.3973 0.0167  0.0604  -0.0835 33  ARG B CZ  
1134 N NH1 . ARG B 16  ? 0.2236 0.3807 0.4236 0.0179  0.0694  -0.0839 33  ARG B NH1 
1135 N NH2 . ARG B 16  ? 0.2507 0.3748 0.4057 0.0224  0.0644  -0.0916 33  ARG B NH2 
1136 N N   . GLU B 17  ? 0.2190 0.2598 0.3131 0.0055  -0.0059 -0.0386 34  GLU B N   
1137 C CA  . GLU B 17  ? 0.2234 0.2462 0.3107 0.0098  -0.0148 -0.0305 34  GLU B CA  
1138 C C   . GLU B 17  ? 0.2298 0.2474 0.3269 0.0115  -0.0090 -0.0313 34  GLU B C   
1139 O O   . GLU B 17  ? 0.2369 0.2441 0.3446 0.0168  -0.0168 -0.0287 34  GLU B O   
1140 C CB  . GLU B 17  ? 0.2640 0.2683 0.3152 0.0077  -0.0153 -0.0204 34  GLU B CB  
1141 C CG  . GLU B 17  ? 0.3008 0.2990 0.3352 0.0074  -0.0277 -0.0195 34  GLU B CG  
1142 C CD  . GLU B 17  ? 0.2936 0.3006 0.3237 0.0014  -0.0222 -0.0260 34  GLU B CD  
1143 O OE1 . GLU B 17  ? 0.2513 0.2727 0.2947 -0.0015 -0.0095 -0.0313 34  GLU B OE1 
1144 O OE2 . GLU B 17  ? 0.3898 0.3853 0.3993 -0.0002 -0.0318 -0.0257 34  GLU B OE2 
1145 N N   . ASP B 18  ? 0.1992 0.2223 0.2935 0.0070  0.0025  -0.0351 35  ASP B N   
1146 C CA  . ASP B 18  ? 0.2005 0.2168 0.3029 0.0059  0.0054  -0.0364 35  ASP B CA  
1147 C C   . ASP B 18  ? 0.1982 0.2236 0.3185 0.0093  0.0075  -0.0511 35  ASP B C   
1148 O O   . ASP B 18  ? 0.1976 0.2181 0.3211 0.0069  0.0092  -0.0560 35  ASP B O   
1149 C CB  . ASP B 18  ? 0.2054 0.2222 0.2954 -0.0008 0.0141  -0.0310 35  ASP B CB  
1150 C CG  . ASP B 18  ? 0.2340 0.2381 0.3049 -0.0023 0.0159  -0.0157 35  ASP B CG  
1151 O OD1 . ASP B 18  ? 0.2598 0.2493 0.3251 0.0009  0.0087  -0.0084 35  ASP B OD1 
1152 O OD2 . ASP B 18  ? 0.2323 0.2406 0.2923 -0.0054 0.0251  -0.0106 35  ASP B OD2 
1153 N N   . ARG B 19  ? 0.1934 0.2067 0.4460 0.0368  0.0214  -0.0223 36  ARG B N   
1154 C CA  . ARG B 19  ? 0.1960 0.2293 0.4564 0.0328  0.0328  -0.0318 36  ARG B CA  
1155 C C   . ARG B 19  ? 0.2080 0.2379 0.4785 0.0409  0.0426  -0.0437 36  ARG B C   
1156 O O   . ARG B 19  ? 0.2058 0.2402 0.4704 0.0377  0.0506  -0.0534 36  ARG B O   
1157 C CB  . ARG B 19  ? 0.2060 0.2627 0.4836 0.0298  0.0332  -0.0289 36  ARG B CB  
1158 C CG  . ARG B 19  ? 0.2615 0.3430 0.5496 0.0268  0.0465  -0.0380 36  ARG B CG  
1159 C CD  . ARG B 19  ? 0.2091 0.3186 0.5220 0.0250  0.0471  -0.0359 36  ARG B CD  
1160 N NE  . ARG B 19  ? 0.2077 0.3438 0.5238 0.0164  0.0611  -0.0417 36  ARG B NE  
1161 C CZ  . ARG B 19  ? 0.2094 0.3746 0.5422 0.0072  0.0651  -0.0394 36  ARG B CZ  
1162 N NH1 . ARG B 19  ? 0.2196 0.3916 0.5683 0.0045  0.0539  -0.0318 36  ARG B NH1 
1163 N NH2 . ARG B 19  ? 0.2472 0.4361 0.5806 -0.0001 0.0810  -0.0452 36  ARG B NH2 
1164 N N   . THR B 20  ? 0.2115 0.2295 0.4937 0.0519  0.0411  -0.0434 37  THR B N   
1165 C CA  . THR B 20  ? 0.2167 0.2245 0.5046 0.0595  0.0493  -0.0545 37  THR B CA  
1166 C C   . THR B 20  ? 0.2200 0.2105 0.4932 0.0534  0.0523  -0.0592 37  THR B C   
1167 O O   . THR B 20  ? 0.2531 0.2426 0.5267 0.0530  0.0599  -0.0714 37  THR B O   
1168 C CB  . THR B 20  ? 0.2456 0.2360 0.5420 0.0731  0.0453  -0.0516 37  THR B CB  
1169 O OG1 . THR B 20  ? 0.2617 0.2738 0.5758 0.0796  0.0409  -0.0494 37  THR B OG1 
1170 C CG2 . THR B 20  ? 0.2731 0.2480 0.5652 0.0791  0.0517  -0.0616 37  THR B CG2 
1171 N N   . LEU B 21  ? 0.2355 0.2139 0.4968 0.0491  0.0459  -0.0509 38  LEU B N   
1172 C CA  . LEU B 21  ? 0.2251 0.1935 0.4769 0.0427  0.0485  -0.0563 38  LEU B CA  
1173 C C   . LEU B 21  ? 0.2453 0.2307 0.4896 0.0352  0.0499  -0.0648 38  LEU B C   
1174 O O   . LEU B 21  ? 0.2614 0.2448 0.5046 0.0316  0.0543  -0.0764 38  LEU B O   
1175 C CB  . LEU B 21  ? 0.2477 0.2046 0.4892 0.0415  0.0418  -0.0458 38  LEU B CB  
1176 C CG  . LEU B 21  ? 0.2628 0.2166 0.4975 0.0345  0.0437  -0.0507 38  LEU B CG  
1177 C CD1 . LEU B 21  ? 0.3038 0.2417 0.5454 0.0317  0.0529  -0.0585 38  LEU B CD1 
1178 C CD2 . LEU B 21  ? 0.3040 0.2521 0.5276 0.0362  0.0365  -0.0393 38  LEU B CD2 
1179 N N   . TYR B 22  ? 0.2078 0.2077 0.4448 0.0325  0.0456  -0.0594 39  TYR B N   
1180 C CA  . TYR B 22  ? 0.2116 0.2230 0.4349 0.0266  0.0464  -0.0662 39  TYR B CA  
1181 C C   . TYR B 22  ? 0.2199 0.2388 0.4495 0.0281  0.0566  -0.0797 39  TYR B C   
1182 O O   . TYR B 22  ? 0.2305 0.2507 0.4502 0.0255  0.0581  -0.0907 39  TYR B O   
1183 C CB  . TYR B 22  ? 0.2079 0.2283 0.4195 0.0222  0.0416  -0.0565 39  TYR B CB  
1184 C CG  . TYR B 22  ? 0.2024 0.2129 0.4027 0.0213  0.0296  -0.0441 39  TYR B CG  
1185 C CD1 . TYR B 22  ? 0.1983 0.1968 0.3953 0.0247  0.0243  -0.0431 39  TYR B CD1 
1186 C CD2 . TYR B 22  ? 0.2042 0.2174 0.3975 0.0168  0.0242  -0.0336 39  TYR B CD2 
1187 C CE1 . TYR B 22  ? 0.2080 0.1971 0.3920 0.0261  0.0132  -0.0325 39  TYR B CE1 
1188 C CE2 . TYR B 22  ? 0.2034 0.2040 0.3836 0.0170  0.0118  -0.0229 39  TYR B CE2 
1189 C CZ  . TYR B 22  ? 0.1994 0.1878 0.3741 0.0230  0.0061  -0.0226 39  TYR B CZ  
1190 O OH  . TYR B 22  ? 0.2015 0.1771 0.3611 0.0251  -0.0062 -0.0129 39  TYR B OH  
1191 N N   . GLU B 23  ? 0.2222 0.2465 0.4680 0.0341  0.0627  -0.0803 40  GLU B N   
1192 C CA  . GLU B 23  ? 0.2482 0.2789 0.4996 0.0386  0.0725  -0.0939 40  GLU B CA  
1193 C C   . GLU B 23  ? 0.2966 0.3085 0.5481 0.0401  0.0741  -0.1056 40  GLU B C   
1194 O O   . GLU B 23  ? 0.2844 0.2978 0.5296 0.0397  0.0785  -0.1192 40  GLU B O   
1195 C CB  . GLU B 23  ? 0.2411 0.2820 0.5123 0.0477  0.0768  -0.0923 40  GLU B CB  
1196 C CG  . GLU B 23  ? 0.4417 0.4973 0.7197 0.0547  0.0876  -0.1054 40  GLU B CG  
1197 C CD  . GLU B 23  ? 0.5303 0.5960 0.7901 0.0482  0.0936  -0.1135 40  GLU B CD  
1198 O OE1 . GLU B 23  ? 0.4909 0.5691 0.7391 0.0389  0.0930  -0.1054 40  GLU B OE1 
1199 O OE2 . GLU B 23  ? 0.5417 0.6003 0.7959 0.0526  0.0983  -0.1280 40  GLU B OE2 
1200 N N   . ARG B 24  ? 0.2617 0.2542 0.5184 0.0406  0.0705  -0.1006 41  ARG B N   
1201 C CA  . ARG B 24  ? 0.3011 0.2740 0.5580 0.0379  0.0727  -0.1107 41  ARG B CA  
1202 C C   . ARG B 24  ? 0.2825 0.2619 0.5297 0.0283  0.0696  -0.1183 41  ARG B C   
1203 O O   . ARG B 24  ? 0.3213 0.2954 0.5678 0.0254  0.0719  -0.1330 41  ARG B O   
1204 C CB  . ARG B 24  ? 0.3063 0.2562 0.5671 0.0383  0.0711  -0.1014 41  ARG B CB  
1205 C CG  . ARG B 24  ? 0.4003 0.3334 0.6667 0.0494  0.0732  -0.0993 41  ARG B CG  
1206 C CD  . ARG B 24  ? 0.4437 0.3548 0.7026 0.0488  0.0694  -0.0854 41  ARG B CD  
1207 N NE  . ARG B 24  ? 0.3863 0.2791 0.6403 0.0378  0.0729  -0.0887 41  ARG B NE  
1208 C CZ  . ARG B 24  ? 0.3926 0.2713 0.6402 0.0332  0.0725  -0.0782 41  ARG B CZ  
1209 N NH1 . ARG B 24  ? 0.4554 0.3341 0.6968 0.0394  0.0668  -0.0636 41  ARG B NH1 
1210 N NH2 . ARG B 24  ? 0.4152 0.2802 0.6623 0.0214  0.0782  -0.0831 41  ARG B NH2 
1211 N N   . ILE B 25  ? 0.2601 0.2500 0.4990 0.0244  0.0627  -0.1096 42  ILE B N   
1212 C CA  . ILE B 25  ? 0.2480 0.2460 0.4772 0.0183  0.0573  -0.1175 42  ILE B CA  
1213 C C   . ILE B 25  ? 0.2813 0.2897 0.4983 0.0193  0.0583  -0.1292 42  ILE B C   
1214 O O   . ILE B 25  ? 0.2694 0.2786 0.4834 0.0165  0.0566  -0.1441 42  ILE B O   
1215 C CB  . ILE B 25  ? 0.2318 0.2360 0.4512 0.0175  0.0484  -0.1054 42  ILE B CB  
1216 C CG1 . ILE B 25  ? 0.2198 0.2130 0.4486 0.0168  0.0483  -0.0964 42  ILE B CG1 
1217 C CG2 . ILE B 25  ? 0.2505 0.2654 0.4570 0.0150  0.0406  -0.1147 42  ILE B CG2 
1218 C CD1 . ILE B 25  ? 0.2237 0.2190 0.4420 0.0193  0.0398  -0.0826 42  ILE B CD1 
1219 N N   . VAL B 26  ? 0.2634 0.2803 0.4725 0.0227  0.0610  -0.1231 43  VAL B N   
1220 C CA  . VAL B 26  ? 0.2744 0.3000 0.4666 0.0236  0.0635  -0.1325 43  VAL B CA  
1221 C C   . VAL B 26  ? 0.3099 0.3309 0.5088 0.0274  0.0708  -0.1488 43  VAL B C   
1222 O O   . VAL B 26  ? 0.3139 0.3356 0.4993 0.0275  0.0695  -0.1629 43  VAL B O   
1223 C CB  . VAL B 26  ? 0.2668 0.3033 0.4507 0.0239  0.0678  -0.1213 43  VAL B CB  
1224 C CG1 . VAL B 26  ? 0.3195 0.3637 0.4852 0.0252  0.0747  -0.1310 43  VAL B CG1 
1225 C CG2 . VAL B 26  ? 0.2930 0.3283 0.4625 0.0193  0.0581  -0.1075 43  VAL B CG2 
1226 N N   . SER B 27  ? 0.3040 0.3171 0.5213 0.0320  0.0769  -0.1479 44  SER B N   
1227 C CA  . SER B 27  ? 0.3125 0.3145 0.5345 0.0370  0.0824  -0.1635 44  SER B CA  
1228 C C   . SER B 27  ? 0.3439 0.3334 0.5646 0.0300  0.0769  -0.1766 44  SER B C   
1229 O O   . SER B 27  ? 0.3643 0.3498 0.5775 0.0316  0.0777  -0.1934 44  SER B O   
1230 C CB  . SER B 27  ? 0.3336 0.3230 0.5729 0.0442  0.0868  -0.1589 44  SER B CB  
1231 O OG  . SER B 27  ? 0.4011 0.4074 0.6460 0.0521  0.0920  -0.1517 44  SER B OG  
1232 N N   . ARG B 28  ? 0.3179 0.3024 0.5464 0.0221  0.0715  -0.1701 45  ARG B N   
1233 C CA  . ARG B 28  ? 0.3483 0.3260 0.5808 0.0132  0.0673  -0.1834 45  ARG B CA  
1234 C C   . ARG B 28  ? 0.3615 0.3567 0.5800 0.0113  0.0589  -0.1930 45  ARG B C   
1235 O O   . ARG B 28  ? 0.3770 0.3704 0.5942 0.0080  0.0552  -0.2108 45  ARG B O   
1236 C CB  . ARG B 28  ? 0.3320 0.3017 0.5783 0.0049  0.0665  -0.1742 45  ARG B CB  
1237 C CG  . ARG B 28  ? 0.4013 0.3712 0.6565 -0.0075 0.0631  -0.1875 45  ARG B CG  
1238 C CD  . ARG B 28  ? 0.4954 0.4428 0.7559 -0.0126 0.0670  -0.2027 45  ARG B CD  
1239 N NE  . ARG B 28  ? 0.4737 0.3948 0.7331 -0.0059 0.0745  -0.1956 45  ARG B NE  
1240 C CZ  . ARG B 28  ? 0.5513 0.4466 0.8128 -0.0129 0.0778  -0.1930 45  ARG B CZ  
1241 N NH1 . ARG B 28  ? 0.5886 0.4805 0.8588 -0.0291 0.0774  -0.1993 45  ARG B NH1 
1242 N NH2 . ARG B 28  ? 0.5215 0.3944 0.7750 -0.0033 0.0813  -0.1840 45  ARG B NH2 
1243 N N   . LEU B 29  ? 0.3045 0.3139 0.5096 0.0142  0.0545  -0.1820 46  LEU B N   
1244 C CA  . LEU B 29  ? 0.3022 0.3234 0.4880 0.0149  0.0449  -0.1904 46  LEU B CA  
1245 C C   . LEU B 29  ? 0.3285 0.3482 0.4969 0.0201  0.0469  -0.2052 46  LEU B C   
1246 O O   . LEU B 29  ? 0.3558 0.3794 0.5121 0.0204  0.0380  -0.2201 46  LEU B O   
1247 C CB  . LEU B 29  ? 0.2905 0.3191 0.4593 0.0177  0.0401  -0.1745 46  LEU B CB  
1248 C CG  . LEU B 29  ? 0.2755 0.3064 0.4551 0.0148  0.0350  -0.1621 46  LEU B CG  
1249 C CD1 . LEU B 29  ? 0.2650 0.2978 0.4231 0.0183  0.0291  -0.1472 46  LEU B CD1 
1250 C CD2 . LEU B 29  ? 0.2732 0.3125 0.4631 0.0108  0.0267  -0.1741 46  LEU B CD2 
1251 N N   . ARG B 30  ? 0.3694 0.3847 0.5359 0.0256  0.0581  -0.2026 47  ARG B N   
1252 C CA  . ARG B 30  ? 0.3598 0.3744 0.5070 0.0320  0.0617  -0.2165 47  ARG B CA  
1253 C C   . ARG B 30  ? 0.3987 0.4025 0.5511 0.0308  0.0574  -0.2382 47  ARG B C   
1254 O O   . ARG B 30  ? 0.4471 0.4500 0.5790 0.0355  0.0544  -0.2535 47  ARG B O   
1255 C CB  . ARG B 30  ? 0.4199 0.4362 0.5696 0.0390  0.0758  -0.2108 47  ARG B CB  
1256 C CG  . ARG B 30  ? 0.4173 0.4475 0.5527 0.0393  0.0807  -0.1951 47  ARG B CG  
1257 C CD  . ARG B 30  ? 0.5381 0.5777 0.6795 0.0458  0.0955  -0.1925 47  ARG B CD  
1258 N NE  . ARG B 30  ? 0.5236 0.5638 0.6942 0.0467  0.0984  -0.1820 47  ARG B NE  
1259 C CZ  . ARG B 30  ? 0.5225 0.5771 0.7021 0.0458  0.1036  -0.1670 47  ARG B CZ  
1260 N NH1 . ARG B 30  ? 0.5717 0.6399 0.7339 0.0409  0.1073  -0.1586 47  ARG B NH1 
1261 N NH2 . ARG B 30  ? 0.5022 0.5557 0.7074 0.0493  0.1045  -0.1603 47  ARG B NH2 
1262 N N   . ARG B 31  ? 0.4248 0.4179 0.6022 0.0238  0.0570  -0.2398 48  ARG B N   
1263 C CA  . ARG B 31  ? 0.4283 0.4095 0.6123 0.0182  0.0517  -0.2588 48  ARG B CA  
1264 C C   . ARG B 31  ? 0.3983 0.3929 0.5752 0.0136  0.0378  -0.2709 48  ARG B C   
1265 O O   . ARG B 31  ? 0.4427 0.4336 0.6150 0.0113  0.0306  -0.2852 48  ARG B O   
1266 C CB  . ARG B 31  ? 0.4185 0.3854 0.6276 0.0082  0.0546  -0.2523 48  ARG B CB  
1267 C CG  . ARG B 31  ? 0.4321 0.3808 0.6447 0.0147  0.0647  -0.2423 48  ARG B CG  
1268 C CD  . ARG B 31  ? 0.6296 0.5524 0.8496 0.0072  0.0646  -0.2463 48  ARG B CD  
1269 N NE  . ARG B 31  ? 0.6414 0.5455 0.8691 0.0092  0.0714  -0.2314 48  ARG B NE  
1270 C CZ  . ARG B 31  ? 0.6408 0.5214 0.8755 -0.0008 0.0722  -0.2279 48  ARG B CZ  
1271 N NH1 . ARG B 31  ? 0.6146 0.4929 0.8562 -0.0165 0.0681  -0.2373 48  ARG B NH1 
1272 N NH2 . ARG B 31  ? 0.6787 0.5383 0.9122 0.0050  0.0770  -0.2147 48  ARG B NH2 
1273 N N   . PHE B 32  ? 0.3946 0.4058 0.5683 0.0132  0.0316  -0.2619 49  PHE B N   
1274 C CA  . PHE B 32  ? 0.3811 0.4070 0.5512 0.0109  0.0165  -0.2742 49  PHE B CA  
1275 C C   . PHE B 32  ? 0.4533 0.4855 0.5874 0.0220  0.0084  -0.2764 49  PHE B C   
1276 O O   . PHE B 32  ? 0.4809 0.5219 0.6064 0.0237  -0.0061 -0.2906 49  PHE B O   
1277 C CB  . PHE B 32  ? 0.3549 0.3950 0.5455 0.0037  0.0124  -0.2640 49  PHE B CB  
1278 C CG  . PHE B 32  ? 0.3568 0.3875 0.5763 -0.0069 0.0228  -0.2557 49  PHE B CG  
1279 C CD1 . PHE B 32  ? 0.4198 0.4415 0.6595 -0.0183 0.0245  -0.2701 49  PHE B CD1 
1280 C CD2 . PHE B 32  ? 0.4309 0.4597 0.6552 -0.0061 0.0298  -0.2337 49  PHE B CD2 
1281 C CE1 . PHE B 32  ? 0.4378 0.4454 0.6983 -0.0285 0.0344  -0.2614 49  PHE B CE1 
1282 C CE2 . PHE B 32  ? 0.4162 0.4328 0.6618 -0.0145 0.0387  -0.2258 49  PHE B CE2 
1283 C CZ  . PHE B 32  ? 0.3621 0.3669 0.6243 -0.0257 0.0416  -0.2391 49  PHE B CZ  
1284 N N   . GLY B 33  ? 0.3943 0.4221 0.5061 0.0290  0.0167  -0.2614 50  GLY B N   
1285 C CA  . GLY B 33  ? 0.4336 0.4614 0.5055 0.0382  0.0105  -0.2630 50  GLY B CA  
1286 C C   . GLY B 33  ? 0.4419 0.4651 0.4933 0.0417  0.0238  -0.2450 50  GLY B C   
1287 O O   . GLY B 33  ? 0.4515 0.4744 0.5223 0.0388  0.0372  -0.2338 50  GLY B O   
1288 N N   . THR B 34  ? 0.4597 0.4790 0.4705 0.0480  0.0196  -0.2432 51  THR B N   
1289 C CA  . THR B 34  ? 0.4473 0.4629 0.4342 0.0485  0.0322  -0.2259 51  THR B CA  
1290 C C   . THR B 34  ? 0.4419 0.4602 0.4397 0.0424  0.0319  -0.2041 51  THR B C   
1291 O O   . THR B 34  ? 0.4376 0.4538 0.4258 0.0433  0.0174  -0.2008 51  THR B O   
1292 C CB  . THR B 34  ? 0.4860 0.4909 0.4208 0.0555  0.0266  -0.2292 51  THR B CB  
1293 O OG1 . THR B 34  ? 0.5154 0.5163 0.4356 0.0626  0.0279  -0.2493 51  THR B OG1 
1294 C CG2 . THR B 34  ? 0.5351 0.5353 0.4443 0.0521  0.0403  -0.2092 51  THR B CG2 
1295 N N   . VAL B 35  ? 0.4039 0.4269 0.4201 0.0377  0.0466  -0.1902 52  VAL B N   
1296 C CA  . VAL B 35  ? 0.3939 0.4179 0.4181 0.0319  0.0460  -0.1696 52  VAL B CA  
1297 C C   . VAL B 35  ? 0.4564 0.4752 0.4464 0.0290  0.0525  -0.1561 52  VAL B C   
1298 O O   . VAL B 35  ? 0.4871 0.5132 0.4789 0.0266  0.0688  -0.1525 52  VAL B O   
1299 C CB  . VAL B 35  ? 0.3765 0.4083 0.4418 0.0283  0.0554  -0.1626 52  VAL B CB  
1300 C CG1 . VAL B 35  ? 0.4053 0.4366 0.4771 0.0233  0.0517  -0.1429 52  VAL B CG1 
1301 C CG2 . VAL B 35  ? 0.4027 0.4341 0.4963 0.0292  0.0511  -0.1759 52  VAL B CG2 
1302 N N   . LEU B 36  ? 0.4410 0.4466 0.3989 0.0292  0.0400  -0.1489 53  LEU B N   
1303 C CA  . LEU B 36  ? 0.4462 0.4393 0.3627 0.0250  0.0450  -0.1364 53  LEU B CA  
1304 C C   . LEU B 36  ? 0.4378 0.4355 0.3686 0.0136  0.0553  -0.1164 53  LEU B C   
1305 O O   . LEU B 36  ? 0.5092 0.5122 0.4706 0.0113  0.0505  -0.1091 53  LEU B O   
1306 C CB  . LEU B 36  ? 0.4753 0.4467 0.3489 0.0303  0.0259  -0.1352 53  LEU B CB  
1307 C CG  . LEU B 36  ? 0.4906 0.4612 0.3558 0.0426  0.0101  -0.1561 53  LEU B CG  
1308 C CD1 . LEU B 36  ? 0.4848 0.4445 0.3330 0.0498  -0.0123 -0.1552 53  LEU B CD1 
1309 C CD2 . LEU B 36  ? 0.5501 0.5104 0.3742 0.0482  0.0139  -0.1667 53  LEU B CD2 
1310 N N   . GLY B 54  ? 1.3116 0.9349 0.7468 -0.2589 0.1058  0.1306  71  GLY B N   
1311 C CA  . GLY B 54  ? 1.2588 0.9530 0.7764 -0.2749 0.1259  0.1268  71  GLY B CA  
1312 C C   . GLY B 54  ? 1.1244 0.8472 0.7072 -0.2651 0.1068  0.1207  71  GLY B C   
1313 O O   . GLY B 54  ? 1.1776 0.8589 0.7394 -0.2583 0.0796  0.1257  71  GLY B O   
1314 N N   . GLY B 55  ? 0.8759 0.6683 0.5351 -0.2628 0.1208  0.1096  72  GLY B N   
1315 C CA  . GLY B 55  ? 0.7779 0.5995 0.4997 -0.2562 0.1056  0.1050  72  GLY B CA  
1316 C C   . GLY B 55  ? 0.7232 0.5309 0.4448 -0.2217 0.0800  0.0947  72  GLY B C   
1317 O O   . GLY B 55  ? 0.7034 0.5250 0.4267 -0.1989 0.0827  0.0817  72  GLY B O   
1318 N N   . ASP B 56  ? 0.4406 0.5839 0.3711 -0.0758 0.1835  -0.0634 73  ASP B N   
1319 C CA  . ASP B 56  ? 0.3940 0.5046 0.3232 -0.0579 0.1596  -0.0558 73  ASP B CA  
1320 C C   . ASP B 56  ? 0.4348 0.5078 0.3114 -0.0545 0.1543  -0.0437 73  ASP B C   
1321 O O   . ASP B 56  ? 0.3801 0.4383 0.2559 -0.0366 0.1366  -0.0440 73  ASP B O   
1322 C CB  . ASP B 56  ? 0.3735 0.4677 0.3170 -0.0635 0.1498  -0.0435 73  ASP B CB  
1323 C CG  . ASP B 56  ? 0.3435 0.4749 0.3429 -0.0601 0.1449  -0.0540 73  ASP B CG  
1324 O OD1 . ASP B 56  ? 0.3887 0.5546 0.4195 -0.0503 0.1476  -0.0700 73  ASP B OD1 
1325 O OD2 . ASP B 56  ? 0.3620 0.4882 0.3743 -0.0661 0.1372  -0.0468 73  ASP B OD2 
1326 N N   . ARG B 57  ? 0.4370 0.4956 0.2703 -0.0724 0.1680  -0.0313 74  ARG B N   
1327 C CA  . ARG B 57  ? 0.4750 0.5017 0.2582 -0.0689 0.1613  -0.0181 74  ARG B CA  
1328 C C   . ARG B 57  ? 0.4774 0.5253 0.2534 -0.0559 0.1599  -0.0359 74  ARG B C   
1329 O O   . ARG B 57  ? 0.4789 0.5062 0.2368 -0.0422 0.1428  -0.0319 74  ARG B O   
1330 C CB  . ARG B 57  ? 0.5533 0.5608 0.2910 -0.0927 0.1754  0.0019  74  ARG B CB  
1331 C CG  . ARG B 57  ? 0.6494 0.6367 0.3350 -0.0902 0.1696  0.0146  74  ARG B CG  
1332 C CD  . ARG B 57  ? 0.6265 0.5648 0.2919 -0.0779 0.1476  0.0349  74  ARG B CD  
1333 N NE  . ARG B 57  ? 0.7304 0.6393 0.3444 -0.0854 0.1436  0.0598  74  ARG B NE  
1334 C CZ  . ARG B 57  ? 0.7529 0.6796 0.3387 -0.0869 0.1441  0.0610  74  ARG B CZ  
1335 N NH1 . ARG B 57  ? 0.7373 0.7087 0.3317 -0.0858 0.1551  0.0368  74  ARG B NH1 
1336 N NH2 . ARG B 57  ? 0.7903 0.6901 0.3408 -0.0884 0.1327  0.0865  74  ARG B NH2 
1337 N N   . LEU B 58  ? 0.4782 0.5689 0.2706 -0.0597 0.1774  -0.0576 75  LEU B N   
1338 C CA  . LEU B 58  ? 0.4868 0.5978 0.2749 -0.0467 0.1770  -0.0804 75  LEU B CA  
1339 C C   . LEU B 58  ? 0.4471 0.5517 0.2733 -0.0228 0.1539  -0.0919 75  LEU B C   
1340 O O   . LEU B 58  ? 0.4576 0.5528 0.2670 -0.0113 0.1415  -0.0993 75  LEU B O   
1341 C CB  . LEU B 58  ? 0.4965 0.6495 0.3116 -0.0484 0.1924  -0.0991 75  LEU B CB  
1342 C CG  . LEU B 58  ? 0.5519 0.7228 0.3644 -0.0348 0.1921  -0.1244 75  LEU B CG  
1343 C CD1 . LEU B 58  ? 0.5843 0.7311 0.3375 -0.0353 0.1842  -0.1161 75  LEU B CD1 
1344 C CD2 . LEU B 58  ? 0.5400 0.7487 0.3679 -0.0404 0.2104  -0.1379 75  LEU B CD2 
1345 N N   . ILE B 59  ? 0.4046 0.5154 0.2816 -0.0169 0.1469  -0.0924 76  ILE B N   
1346 C CA  . ILE B 59  ? 0.3697 0.4728 0.2825 0.0025  0.1238  -0.0974 76  ILE B CA  
1347 C C   . ILE B 59  ? 0.3733 0.4387 0.2573 0.0075  0.1045  -0.0779 76  ILE B C   
1348 O O   . ILE B 59  ? 0.3692 0.4266 0.2538 0.0202  0.0884  -0.0840 76  ILE B O   
1349 C CB  . ILE B 59  ? 0.3292 0.4467 0.2956 0.0044  0.1191  -0.0956 76  ILE B CB  
1350 C CG1 . ILE B 59  ? 0.3274 0.4875 0.3325 0.0040  0.1347  -0.1168 76  ILE B CG1 
1351 C CG2 . ILE B 59  ? 0.3198 0.4251 0.3164 0.0205  0.0936  -0.0922 76  ILE B CG2 
1352 C CD1 . ILE B 59  ? 0.3609 0.5392 0.4061 -0.0025 0.1351  -0.1099 76  ILE B CD1 
1353 N N   . HIS B 60  ? 0.3769 0.4192 0.2386 -0.0024 0.1053  -0.0552 77  HIS B N   
1354 C CA  . HIS B 60  ? 0.3793 0.3890 0.2190 0.0046  0.0875  -0.0373 77  HIS B CA  
1355 C C   . HIS B 60  ? 0.4152 0.4150 0.2122 0.0073  0.0830  -0.0372 77  HIS B C   
1356 O O   . HIS B 60  ? 0.4089 0.3987 0.2056 0.0195  0.0639  -0.0356 77  HIS B O   
1357 C CB  . HIS B 60  ? 0.3889 0.3736 0.2117 -0.0058 0.0914  -0.0164 77  HIS B CB  
1358 C CG  . HIS B 60  ? 0.3982 0.3506 0.1989 0.0028  0.0752  0.0014  77  HIS B CG  
1359 N ND1 . HIS B 60  ? 0.4406 0.3708 0.1953 0.0008  0.0735  0.0146  77  HIS B ND1 
1360 C CD2 . HIS B 60  ? 0.3723 0.3148 0.1926 0.0142  0.0598  0.0082  77  HIS B CD2 
1361 C CE1 . HIS B 60  ? 0.4393 0.3465 0.1898 0.0123  0.0569  0.0284  77  HIS B CE1 
1362 N NE2 . HIS B 60  ? 0.3977 0.3133 0.1877 0.0205  0.0497  0.0236  77  HIS B NE2 
1363 N N   . GLU B 61  ? 0.4554 0.4614 0.2156 -0.0056 0.1001  -0.0385 78  GLU B N   
1364 C CA  . GLU B 61  ? 0.4964 0.4955 0.2092 -0.0056 0.0955  -0.0366 78  GLU B CA  
1365 C C   . GLU B 61  ? 0.4914 0.5109 0.2178 0.0062  0.0883  -0.0639 78  GLU B C   
1366 O O   . GLU B 61  ? 0.5019 0.5103 0.2112 0.0143  0.0701  -0.0628 78  GLU B O   
1367 C CB  . GLU B 61  ? 0.5448 0.5496 0.2131 -0.0254 0.1169  -0.0297 78  GLU B CB  
1368 C CG  . GLU B 61  ? 0.5923 0.5662 0.2413 -0.0382 0.1201  0.0005  78  GLU B CG  
1369 C CD  . GLU B 61  ? 0.6312 0.5663 0.2605 -0.0281 0.0974  0.0240  78  GLU B CD  
1370 O OE1 . GLU B 61  ? 0.6908 0.6179 0.2774 -0.0279 0.0892  0.0336  78  GLU B OE1 
1371 O OE2 . GLU B 61  ? 0.5770 0.4930 0.2344 -0.0197 0.0875  0.0319  78  GLU B OE2 
1372 N N   . GLN B 62  ? 0.4783 0.5277 0.2381 0.0074  0.1015  -0.0897 79  GLN B N   
1373 C CA  . GLN B 62  ? 0.4745 0.5390 0.2567 0.0205  0.0938  -0.1191 79  GLN B CA  
1374 C C   . GLN B 62  ? 0.4424 0.4881 0.2548 0.0348  0.0663  -0.1145 79  GLN B C   
1375 O O   . GLN B 62  ? 0.4563 0.4953 0.2573 0.0413  0.0506  -0.1233 79  GLN B O   
1376 C CB  . GLN B 62  ? 0.4594 0.5563 0.2872 0.0233  0.1101  -0.1446 79  GLN B CB  
1377 C CG  . GLN B 62  ? 0.5428 0.6535 0.3962 0.0377  0.1046  -0.1796 79  GLN B CG  
1378 C CD  . GLN B 62  ? 0.6545 0.7666 0.4574 0.0356  0.1053  -0.1955 79  GLN B CD  
1379 O OE1 . GLN B 62  ? 0.7081 0.8348 0.4789 0.0246  0.1238  -0.1975 79  GLN B OE1 
1380 N NE2 . GLN B 62  ? 0.6410 0.7317 0.4391 0.0439  0.0807  -0.1970 79  GLN B NE2 
1381 N N   . ASP B 63  ? 0.4014 0.4416 0.2526 0.0379  0.0601  -0.1009 80  ASP B N   
1382 C CA  . ASP B 63  ? 0.3856 0.4148 0.2693 0.0492  0.0360  -0.0963 80  ASP B CA  
1383 C C   . ASP B 63  ? 0.3807 0.3879 0.2329 0.0503  0.0197  -0.0760 80  ASP B C   
1384 O O   . ASP B 63  ? 0.3865 0.3888 0.2515 0.0579  -0.0004 -0.0780 80  ASP B O   
1385 C CB  . ASP B 63  ? 0.3831 0.4176 0.3124 0.0503  0.0344  -0.0862 80  ASP B CB  
1386 C CG  . ASP B 63  ? 0.4378 0.4938 0.4169 0.0563  0.0370  -0.1068 80  ASP B CG  
1387 O OD1 . ASP B 63  ? 0.4509 0.5044 0.4600 0.0663  0.0202  -0.1163 80  ASP B OD1 
1388 O OD2 . ASP B 63  ? 0.4589 0.5344 0.4502 0.0510  0.0548  -0.1130 80  ASP B OD2 
1389 N N   . LEU B 64  ? 0.3999 0.3940 0.2133 0.0427  0.0272  -0.0563 81  LEU B N   
1390 C CA  . LEU B 64  ? 0.4181 0.3929 0.2028 0.0461  0.0112  -0.0372 81  LEU B CA  
1391 C C   . LEU B 64  ? 0.4517 0.4292 0.2041 0.0469  0.0023  -0.0480 81  LEU B C   
1392 O O   . LEU B 64  ? 0.4525 0.4230 0.2003 0.0533  -0.0185 -0.0404 81  LEU B O   
1393 C CB  . LEU B 64  ? 0.4353 0.3913 0.1874 0.0385  0.0207  -0.0140 81  LEU B CB  
1394 C CG  . LEU B 64  ? 0.4861 0.4206 0.2270 0.0463  0.0037  0.0092  81  LEU B CG  
1395 C CD1 . LEU B 64  ? 0.4297 0.3655 0.2147 0.0543  -0.0036 0.0135  81  LEU B CD1 
1396 C CD2 . LEU B 64  ? 0.5089 0.4187 0.2083 0.0390  0.0112  0.0310  81  LEU B CD2 
1397 N N   . GLU B 65  ? 0.4802 0.4716 0.2100 0.0398  0.0178  -0.0669 82  GLU B N   
1398 C CA  . GLU B 65  ? 0.5173 0.5155 0.2160 0.0397  0.0099  -0.0832 82  GLU B CA  
1399 C C   . GLU B 65  ? 0.4978 0.5004 0.2359 0.0498  -0.0077 -0.1051 82  GLU B C   
1400 O O   . GLU B 65  ? 0.5126 0.5103 0.2378 0.0524  -0.0281 -0.1060 82  GLU B O   
1401 C CB  . GLU B 65  ? 0.5780 0.5958 0.2455 0.0293  0.0338  -0.1021 82  GLU B CB  
1402 C CG  . GLU B 65  ? 0.6733 0.6853 0.2922 0.0151  0.0486  -0.0773 82  GLU B CG  
1403 C CD  . GLU B 65  ? 0.7758 0.8130 0.3555 0.0021  0.0712  -0.0944 82  GLU B CD  
1404 O OE1 . GLU B 65  ? 0.8100 0.8597 0.3612 0.0023  0.0659  -0.1137 82  GLU B OE1 
1405 O OE2 . GLU B 65  ? 0.8312 0.8782 0.4079 -0.0097 0.0946  -0.0890 82  GLU B OE2 
1406 N N   . TRP B 66  ? 0.4685 0.4800 0.2560 0.0547  -0.0015 -0.1223 83  TRP B N   
1407 C CA  . TRP B 66  ? 0.4536 0.4633 0.2835 0.0635  -0.0202 -0.1393 83  TRP B CA  
1408 C C   . TRP B 66  ? 0.4267 0.4235 0.2739 0.0668  -0.0440 -0.1157 83  TRP B C   
1409 O O   . TRP B 66  ? 0.4319 0.4245 0.2902 0.0693  -0.0647 -0.1234 83  TRP B O   
1410 C CB  . TRP B 66  ? 0.4252 0.4441 0.3105 0.0693  -0.0124 -0.1545 83  TRP B CB  
1411 C CG  . TRP B 66  ? 0.4541 0.4920 0.3403 0.0699  0.0091  -0.1851 83  TRP B CG  
1412 C CD1 . TRP B 66  ? 0.5287 0.5766 0.3808 0.0682  0.0172  -0.2126 83  TRP B CD1 
1413 C CD2 . TRP B 66  ? 0.4777 0.5322 0.4050 0.0733  0.0248  -0.1935 83  TRP B CD2 
1414 N NE1 . TRP B 66  ? 0.5509 0.6217 0.4214 0.0710  0.0392  -0.2387 83  TRP B NE1 
1415 C CE2 . TRP B 66  ? 0.5450 0.6204 0.4634 0.0745  0.0436  -0.2265 83  TRP B CE2 
1416 C CE3 . TRP B 66  ? 0.4926 0.5497 0.4626 0.0749  0.0247  -0.1764 83  TRP B CE3 
1417 C CZ2 . TRP B 66  ? 0.5542 0.6543 0.5101 0.0787  0.0621  -0.2426 83  TRP B CZ2 
1418 C CZ3 . TRP B 66  ? 0.4511 0.5311 0.4558 0.0779  0.0409  -0.1909 83  TRP B CZ3 
1419 C CH2 . TRP B 66  ? 0.5287 0.6303 0.5286 0.0805  0.0594  -0.2234 83  TRP B CH2 
1420 N N   . LEU B 67  ? 0.4001 0.3923 0.2526 0.0662  -0.0411 -0.0886 84  LEU B N   
1421 C CA  . LEU B 67  ? 0.3734 0.3606 0.2494 0.0702  -0.0611 -0.0693 84  LEU B CA  
1422 C C   . LEU B 67  ? 0.4113 0.3936 0.2530 0.0704  -0.0770 -0.0599 84  LEU B C   
1423 O O   . LEU B 67  ? 0.4057 0.3900 0.2672 0.0727  -0.0981 -0.0567 84  LEU B O   
1424 C CB  . LEU B 67  ? 0.3648 0.3511 0.2552 0.0702  -0.0524 -0.0475 84  LEU B CB  
1425 C CG  . LEU B 67  ? 0.3808 0.3665 0.2875 0.0740  -0.0662 -0.0253 84  LEU B CG  
1426 C CD1 . LEU B 67  ? 0.3548 0.3508 0.3121 0.0747  -0.0761 -0.0287 84  LEU B CD1 
1427 C CD2 . LEU B 67  ? 0.3736 0.3545 0.2733 0.0730  -0.0521 -0.0094 84  LEU B CD2 
1428 N N   . GLN B 68  ? 0.4351 0.4133 0.2259 0.0665  -0.0682 -0.0556 85  GLN B N   
1429 C CA  . GLN B 68  ? 0.4682 0.4443 0.2223 0.0664  -0.0847 -0.0478 85  GLN B CA  
1430 C C   . GLN B 68  ? 0.4920 0.4757 0.2424 0.0641  -0.0982 -0.0740 85  GLN B C   
1431 O O   . GLN B 68  ? 0.5211 0.5072 0.2589 0.0642  -0.1196 -0.0692 85  GLN B O   
1432 C CB  . GLN B 68  ? 0.5179 0.4873 0.2163 0.0607  -0.0720 -0.0354 85  GLN B CB  
1433 C CG  . GLN B 68  ? 0.5705 0.5255 0.2609 0.0651  -0.0747 -0.0033 85  GLN B CG  
1434 C CD  . GLN B 68  ? 0.6056 0.5485 0.2456 0.0572  -0.0604 0.0110  85  GLN B CD  
1435 O OE1 . GLN B 68  ? 0.6854 0.6197 0.2899 0.0579  -0.0721 0.0305  85  GLN B OE1 
1436 N NE2 . GLN B 68  ? 0.6581 0.6015 0.2964 0.0487  -0.0360 0.0032  85  GLN B NE2 
1437 N N   . GLN B 69  ? 0.4970 0.4854 0.2594 0.0623  -0.0867 -0.1034 86  GLN B N   
1438 C CA  . GLN B 69  ? 0.5248 0.5171 0.2861 0.0608  -0.0979 -0.1345 86  GLN B CA  
1439 C C   . GLN B 69  ? 0.4978 0.4849 0.3153 0.0644  -0.1177 -0.1416 86  GLN B C   
1440 O O   . GLN B 69  ? 0.5226 0.5079 0.3448 0.0626  -0.1306 -0.1678 86  GLN B O   
1441 C CB  . GLN B 69  ? 0.5555 0.5560 0.3089 0.0595  -0.0757 -0.1669 86  GLN B CB  
1442 C CG  . GLN B 69  ? 0.6602 0.6718 0.3491 0.0515  -0.0612 -0.1740 86  GLN B CG  
1443 C CD  . GLN B 69  ? 0.7943 0.8208 0.4841 0.0505  -0.0322 -0.1996 86  GLN B CD  
1444 O OE1 . GLN B 69  ? 0.8226 0.8590 0.4758 0.0428  -0.0110 -0.1898 86  GLN B OE1 
1445 N NE2 . GLN B 69  ? 0.8240 0.8526 0.5584 0.0581  -0.0317 -0.2321 86  GLN B NE2 
1446 N N   . ALA B 70  ? 0.4998 0.4505 0.2169 0.0057  -0.0295 -0.1028 87  ALA B N   
1447 C CA  . ALA B 70  ? 0.4692 0.4269 0.2244 0.0063  -0.0342 -0.1146 87  ALA B CA  
1448 C C   . ALA B 70  ? 0.5061 0.4661 0.2767 0.0044  -0.0597 -0.1180 87  ALA B C   
1449 O O   . ALA B 70  ? 0.4877 0.4498 0.2515 0.0054  -0.0750 -0.1084 87  ALA B O   
1450 C CB  . ALA B 70  ? 0.4346 0.4073 0.2327 0.0061  -0.0234 -0.1045 87  ALA B CB  
1451 N N   . ASP B 71  ? 0.4537 0.4135 0.2475 0.0015  -0.0636 -0.1312 88  ASP B N   
1452 C CA  . ASP B 71  ? 0.4634 0.4305 0.2860 -0.0023 -0.0845 -0.1342 88  ASP B CA  
1453 C C   . ASP B 71  ? 0.4540 0.4366 0.3252 -0.0026 -0.0839 -0.1310 88  ASP B C   
1454 O O   . ASP B 71  ? 0.4625 0.4580 0.3597 -0.0042 -0.0984 -0.1258 88  ASP B O   
1455 C CB  . ASP B 71  ? 0.4786 0.4344 0.2985 -0.0078 -0.0896 -0.1494 88  ASP B CB  
1456 C CG  . ASP B 71  ? 0.5418 0.4836 0.3133 -0.0089 -0.0909 -0.1546 88  ASP B CG  
1457 O OD1 . ASP B 71  ? 0.5768 0.5223 0.3283 -0.0082 -0.1033 -0.1467 88  ASP B OD1 
1458 O OD2 . ASP B 71  ? 0.5841 0.5112 0.3385 -0.0102 -0.0798 -0.1668 88  ASP B OD2 
1459 N N   . VAL B 72  ? 0.3603 0.3430 0.2482 -0.0020 -0.0644 -0.1299 89  VAL B N   
1460 C CA  . VAL B 72  ? 0.3413 0.3360 0.2727 -0.0036 -0.0583 -0.1205 89  VAL B CA  
1461 C C   . VAL B 72  ? 0.3146 0.3123 0.2454 0.0001  -0.0385 -0.1099 89  VAL B C   
1462 O O   . VAL B 72  ? 0.3011 0.2922 0.2144 0.0028  -0.0255 -0.1151 89  VAL B O   
1463 C CB  . VAL B 72  ? 0.3532 0.3431 0.3126 -0.0081 -0.0588 -0.1309 89  VAL B CB  
1464 C CG1 . VAL B 72  ? 0.3327 0.3334 0.3317 -0.0101 -0.0526 -0.1192 89  VAL B CG1 
1465 C CG2 . VAL B 72  ? 0.3884 0.3748 0.3490 -0.0141 -0.0792 -0.1439 89  VAL B CG2 
1466 N N   . VAL B 73  ? 0.2702 0.2789 0.2216 0.0001  -0.0362 -0.0959 90  VAL B N   
1467 C CA  . VAL B 73  ? 0.2589 0.2723 0.2167 0.0017  -0.0206 -0.0859 90  VAL B CA  
1468 C C   . VAL B 73  ? 0.2284 0.2466 0.2208 0.0004  -0.0169 -0.0833 90  VAL B C   
1469 O O   . VAL B 73  ? 0.2683 0.2918 0.2812 -0.0020 -0.0240 -0.0794 90  VAL B O   
1470 C CB  . VAL B 73  ? 0.2444 0.2616 0.1932 0.0024  -0.0212 -0.0727 90  VAL B CB  
1471 C CG1 . VAL B 73  ? 0.2499 0.2719 0.2080 0.0021  -0.0072 -0.0636 90  VAL B CG1 
1472 C CG2 . VAL B 73  ? 0.2929 0.3010 0.2030 0.0037  -0.0246 -0.0732 90  VAL B CG2 
1473 N N   . VAL B 74  ? 0.2324 0.2492 0.2316 0.0025  -0.0054 -0.0847 91  VAL B N   
1474 C CA  . VAL B 74  ? 0.2105 0.2283 0.2372 0.0024  -0.0020 -0.0808 91  VAL B CA  
1475 C C   . VAL B 74  ? 0.2105 0.2365 0.2415 0.0046  0.0073  -0.0703 91  VAL B C   
1476 O O   . VAL B 74  ? 0.2214 0.2504 0.2440 0.0074  0.0157  -0.0721 91  VAL B O   
1477 C CB  . VAL B 74  ? 0.2402 0.2468 0.2736 0.0046  0.0006  -0.0919 91  VAL B CB  
1478 C CG1 . VAL B 74  ? 0.2307 0.2347 0.2896 0.0052  0.0036  -0.0853 91  VAL B CG1 
1479 C CG2 . VAL B 74  ? 0.2450 0.2415 0.2720 0.0007  -0.0103 -0.1047 91  VAL B CG2 
1480 N N   . ALA B 75  ? 0.1773 0.2076 0.2220 0.0028  0.0063  -0.0602 92  ALA B N   
1481 C CA  . ALA B 75  ? 0.1689 0.2061 0.2155 0.0036  0.0121  -0.0511 92  ALA B CA  
1482 C C   . ALA B 75  ? 0.1647 0.2006 0.2289 0.0045  0.0129  -0.0451 92  ALA B C   
1483 O O   . ALA B 75  ? 0.1900 0.2220 0.2627 0.0021  0.0100  -0.0422 92  ALA B O   
1484 C CB  . ALA B 75  ? 0.1685 0.2086 0.2049 0.0010  0.0101  -0.0439 92  ALA B CB  
1485 N N   . GLU B 76  ? 0.1536 0.1935 0.2237 0.0080  0.0169  -0.0427 93  GLU B N   
1486 C CA  . GLU B 76  ? 0.1493 0.1875 0.2305 0.0096  0.0159  -0.0345 93  GLU B CA  
1487 C C   . GLU B 76  ? 0.1603 0.2053 0.2343 0.0065  0.0153  -0.0265 93  GLU B C   
1488 O O   . GLU B 76  ? 0.1734 0.2277 0.2450 0.0061  0.0170  -0.0265 93  GLU B O   
1489 C CB  . GLU B 76  ? 0.1630 0.2019 0.2564 0.0166  0.0177  -0.0362 93  GLU B CB  
1490 C CG  . GLU B 76  ? 0.1746 0.2015 0.2780 0.0197  0.0149  -0.0298 93  GLU B CG  
1491 C CD  . GLU B 76  ? 0.1920 0.2200 0.2914 0.0178  0.0117  -0.0174 93  GLU B CD  
1492 O OE1 . GLU B 76  ? 0.1679 0.2069 0.2599 0.0151  0.0109  -0.0150 93  GLU B OE1 
1493 O OE2 . GLU B 76  ? 0.1896 0.2051 0.2908 0.0188  0.0102  -0.0102 93  GLU B OE2 
1494 N N   . VAL B 77  ? 0.1509 0.1908 0.2215 0.0038  0.0139  -0.0206 94  VAL B N   
1495 C CA  . VAL B 77  ? 0.1499 0.1918 0.2093 0.0008  0.0136  -0.0158 94  VAL B CA  
1496 C C   . VAL B 77  ? 0.1637 0.2029 0.2203 0.0011  0.0121  -0.0081 94  VAL B C   
1497 O O   . VAL B 77  ? 0.1757 0.2119 0.2207 -0.0012 0.0124  -0.0048 94  VAL B O   
1498 C CB  . VAL B 77  ? 0.1386 0.1774 0.1934 -0.0011 0.0141  -0.0164 94  VAL B CB  
1499 C CG1 . VAL B 77  ? 0.1543 0.1953 0.2055 -0.0012 0.0124  -0.0230 94  VAL B CG1 
1500 C CG2 . VAL B 77  ? 0.1542 0.1887 0.2194 -0.0016 0.0157  -0.0142 94  VAL B CG2 
1501 N N   . THR B 78  ? 0.1496 0.1884 0.2146 0.0049  0.0098  -0.0054 95  THR B N   
1502 C CA  . THR B 78  ? 0.1433 0.1778 0.2014 0.0059  0.0061  0.0029  95  THR B CA  
1503 C C   . THR B 78  ? 0.1542 0.1979 0.2066 0.0038  0.0009  0.0033  95  THR B C   
1504 O O   . THR B 78  ? 0.1607 0.1991 0.1973 0.0012  -0.0019 0.0073  95  THR B O   
1505 C CB  . THR B 78  ? 0.1485 0.1775 0.2171 0.0119  0.0034  0.0070  95  THR B CB  
1506 O OG1 . THR B 78  ? 0.1741 0.1921 0.2480 0.0110  0.0084  0.0060  95  THR B OG1 
1507 C CG2 . THR B 78  ? 0.1782 0.2001 0.2351 0.0136  -0.0021 0.0173  95  THR B CG2 
1508 N N   . GLN B 79  ? 0.1448 0.2021 0.2100 0.0043  0.0000  -0.0014 96  GLN B N   
1509 C CA  . GLN B 79  ? 0.1358 0.2044 0.2013 -0.0001 -0.0048 -0.0017 96  GLN B CA  
1510 C C   . GLN B 79  ? 0.1421 0.2080 0.1953 -0.0076 -0.0005 -0.0052 96  GLN B C   
1511 O O   . GLN B 79  ? 0.1470 0.2145 0.2024 -0.0082 0.0058  -0.0095 96  GLN B O   
1512 C CB  . GLN B 79  ? 0.1260 0.2129 0.2150 0.0033  -0.0052 -0.0048 96  GLN B CB  
1513 C CG  . GLN B 79  ? 0.1450 0.2486 0.2430 -0.0020 -0.0112 -0.0046 96  GLN B CG  
1514 C CD  . GLN B 79  ? 0.1645 0.2671 0.2588 -0.0003 -0.0246 0.0016  96  GLN B CD  
1515 O OE1 . GLN B 79  ? 0.1989 0.2956 0.2948 0.0083  -0.0293 0.0067  96  GLN B OE1 
1516 N NE2 . GLN B 79  ? 0.2227 0.3292 0.3102 -0.0090 -0.0316 0.0013  96  GLN B NE2 
1517 N N   . PRO B 80  ? 0.1345 0.1937 0.1723 -0.0129 -0.0041 -0.0037 97  PRO B N   
1518 C CA  . PRO B 80  ? 0.1346 0.1864 0.1602 -0.0189 -0.0001 -0.0065 97  PRO B CA  
1519 C C   . PRO B 80  ? 0.1301 0.1934 0.1660 -0.0245 0.0026  -0.0092 97  PRO B C   
1520 O O   . PRO B 80  ? 0.1466 0.2250 0.1974 -0.0274 -0.0010 -0.0094 97  PRO B O   
1521 C CB  . PRO B 80  ? 0.1593 0.2004 0.1671 -0.0231 -0.0055 -0.0056 97  PRO B CB  
1522 C CG  . PRO B 80  ? 0.1724 0.2102 0.1755 -0.0175 -0.0094 -0.0012 97  PRO B CG  
1523 C CD  . PRO B 80  ? 0.1533 0.2063 0.1793 -0.0128 -0.0119 0.0006  97  PRO B CD  
1524 N N   . SER B 81  ? 0.1205 0.1771 0.1485 -0.0258 0.0091  -0.0108 98  SER B N   
1525 C CA  . SER B 81  ? 0.1413 0.2064 0.1749 -0.0309 0.0150  -0.0123 98  SER B CA  
1526 C C   . SER B 81  ? 0.1370 0.1859 0.1511 -0.0338 0.0189  -0.0114 98  SER B C   
1527 O O   . SER B 81  ? 0.1567 0.1963 0.1619 -0.0276 0.0190  -0.0117 98  SER B O   
1528 C CB  . SER B 81  ? 0.1411 0.2186 0.1883 -0.0245 0.0201  -0.0153 98  SER B CB  
1529 O OG  . SER B 81  ? 0.1395 0.2198 0.1827 -0.0281 0.0288  -0.0170 98  SER B OG  
1530 N N   . LEU B 82  ? 0.1510 0.1963 0.1601 -0.0435 0.0214  -0.0098 99  LEU B N   
1531 C CA  . LEU B 82  ? 0.1751 0.2018 0.1639 -0.0458 0.0250  -0.0071 99  LEU B CA  
1532 C C   . LEU B 82  ? 0.1862 0.2154 0.1694 -0.0414 0.0309  -0.0073 99  LEU B C   
1533 O O   . LEU B 82  ? 0.1808 0.1955 0.1472 -0.0365 0.0293  -0.0057 99  LEU B O   
1534 C CB  . LEU B 82  ? 0.1734 0.1942 0.1587 -0.0590 0.0279  -0.0045 99  LEU B CB  
1535 C CG  . LEU B 82  ? 0.2055 0.2187 0.1909 -0.0659 0.0207  -0.0057 99  LEU B CG  
1536 C CD1 . LEU B 82  ? 0.2158 0.2312 0.2077 -0.0817 0.0235  -0.0044 99  LEU B CD1 
1537 C CD2 . LEU B 82  ? 0.2215 0.2069 0.1847 -0.0612 0.0174  -0.0053 99  LEU B CD2 
1538 N N   . GLY B 83  ? 0.1637 0.2114 0.1605 -0.0425 0.0374  -0.0099 100 GLY B N   
1539 C CA  . GLY B 83  ? 0.1897 0.2378 0.1761 -0.0391 0.0443  -0.0116 100 GLY B CA  
1540 C C   . GLY B 83  ? 0.1845 0.2288 0.1674 -0.0285 0.0384  -0.0157 100 GLY B C   
1541 O O   . GLY B 83  ? 0.1979 0.2316 0.1616 -0.0254 0.0375  -0.0159 100 GLY B O   
1542 N N   . VAL B 84  ? 0.1598 0.2120 0.1607 -0.0234 0.0333  -0.0186 101 VAL B N   
1543 C CA  . VAL B 84  ? 0.1593 0.2074 0.1606 -0.0156 0.0279  -0.0221 101 VAL B CA  
1544 C C   . VAL B 84  ? 0.1834 0.2178 0.1720 -0.0140 0.0216  -0.0189 101 VAL B C   
1545 O O   . VAL B 84  ? 0.1834 0.2132 0.1648 -0.0099 0.0176  -0.0213 101 VAL B O   
1546 C CB  . VAL B 84  ? 0.1441 0.1999 0.1657 -0.0118 0.0248  -0.0234 101 VAL B CB  
1547 C CG1 . VAL B 84  ? 0.1513 0.2011 0.1750 -0.0066 0.0200  -0.0259 101 VAL B CG1 
1548 C CG2 . VAL B 84  ? 0.1335 0.2030 0.1704 -0.0099 0.0302  -0.0273 101 VAL B CG2 
1549 N N   . GLY B 85  ? 0.1588 0.1866 0.1453 -0.0167 0.0199  -0.0144 102 GLY B N   
1550 C CA  . GLY B 85  ? 0.1882 0.2032 0.1652 -0.0131 0.0153  -0.0120 102 GLY B CA  
1551 C C   . GLY B 85  ? 0.1878 0.1917 0.1454 -0.0127 0.0143  -0.0095 102 GLY B C   
1552 O O   . GLY B 85  ? 0.1963 0.1957 0.1498 -0.0062 0.0082  -0.0095 102 GLY B O   
1553 N N   . TYR B 86  ? 0.1919 0.1921 0.1380 -0.0197 0.0202  -0.0067 103 TYR B N   
1554 C CA  . TYR B 86  ? 0.2152 0.2012 0.1371 -0.0202 0.0206  -0.0021 103 TYR B CA  
1555 C C   . TYR B 86  ? 0.2192 0.2097 0.1331 -0.0149 0.0178  -0.0063 103 TYR B C   
1556 O O   . TYR B 86  ? 0.2346 0.2138 0.1313 -0.0098 0.0104  -0.0037 103 TYR B O   
1557 C CB  . TYR B 86  ? 0.2037 0.1866 0.1172 -0.0313 0.0307  0.0021  103 TYR B CB  
1558 C CG  . TYR B 86  ? 0.2464 0.2119 0.1305 -0.0334 0.0336  0.0088  103 TYR B CG  
1559 C CD1 . TYR B 86  ? 0.2701 0.2109 0.1367 -0.0342 0.0301  0.0170  103 TYR B CD1 
1560 C CD2 . TYR B 86  ? 0.2708 0.2416 0.1416 -0.0344 0.0405  0.0073  103 TYR B CD2 
1561 C CE1 . TYR B 86  ? 0.3084 0.2293 0.1443 -0.0360 0.0324  0.0254  103 TYR B CE1 
1562 C CE2 . TYR B 86  ? 0.3172 0.2695 0.1549 -0.0366 0.0437  0.0148  103 TYR B CE2 
1563 C CZ  . TYR B 86  ? 0.3310 0.2580 0.1509 -0.0376 0.0392  0.0249  103 TYR B CZ  
1564 O OH  . TYR B 86  ? 0.3837 0.2884 0.1673 -0.0396 0.0419  0.0346  103 TYR B OH  
1565 N N   . GLU B 87  ? 0.2161 0.2218 0.1419 -0.0154 0.0224  -0.0132 104 GLU B N   
1566 C CA  . GLU B 87  ? 0.2179 0.2256 0.1352 -0.0108 0.0192  -0.0199 104 GLU B CA  
1567 C C   . GLU B 87  ? 0.2259 0.2328 0.1506 -0.0040 0.0060  -0.0223 104 GLU B C   
1568 O O   . GLU B 87  ? 0.2545 0.2555 0.1632 -0.0004 -0.0025 -0.0240 104 GLU B O   
1569 C CB  . GLU B 87  ? 0.2032 0.2253 0.1364 -0.0110 0.0267  -0.0281 104 GLU B CB  
1570 C CG  . GLU B 87  ? 0.2409 0.2669 0.1652 -0.0164 0.0409  -0.0275 104 GLU B CG  
1571 C CD  . GLU B 87  ? 0.2038 0.2469 0.1515 -0.0153 0.0494  -0.0344 104 GLU B CD  
1572 O OE1 . GLU B 87  ? 0.2218 0.2726 0.1944 -0.0125 0.0447  -0.0358 104 GLU B OE1 
1573 O OE2 . GLU B 87  ? 0.2588 0.3068 0.1988 -0.0167 0.0617  -0.0376 104 GLU B OE2 
1574 N N   . LEU B 88  ? 0.2065 0.2198 0.1551 -0.0026 0.0038  -0.0222 105 LEU B N   
1575 C CA  . LEU B 88  ? 0.2102 0.2265 0.1717 0.0026  -0.0061 -0.0242 105 LEU B CA  
1576 C C   . LEU B 88  ? 0.2092 0.2159 0.1593 0.0074  -0.0140 -0.0184 105 LEU B C   
1577 O O   . LEU B 88  ? 0.2269 0.2361 0.1791 0.0124  -0.0251 -0.0206 105 LEU B O   
1578 C CB  . LEU B 88  ? 0.1829 0.2071 0.1694 0.0024  -0.0030 -0.0242 105 LEU B CB  
1579 C CG  . LEU B 88  ? 0.1827 0.2147 0.1830 0.0003  0.0009  -0.0297 105 LEU B CG  
1580 C CD1 . LEU B 88  ? 0.1830 0.2186 0.2003 -0.0004 0.0047  -0.0266 105 LEU B CD1 
1581 C CD2 . LEU B 88  ? 0.2039 0.2385 0.2104 0.0016  -0.0060 -0.0375 105 LEU B CD2 
1582 N N   . GLY B 89  ? 0.2032 0.1981 0.1421 0.0062  -0.0096 -0.0111 106 GLY B N   
1583 C CA  . GLY B 89  ? 0.2389 0.2203 0.1654 0.0124  -0.0170 -0.0049 106 GLY B CA  
1584 C C   . GLY B 89  ? 0.2681 0.2400 0.1676 0.0143  -0.0243 -0.0025 106 GLY B C   
1585 O O   . GLY B 89  ? 0.2807 0.2505 0.1779 0.0225  -0.0372 -0.0010 106 GLY B O   
1586 N N   . ARG B 90  ? 0.2702 0.2376 0.1490 0.0073  -0.0162 -0.0022 107 ARG B N   
1587 C CA  . ARG B 90  ? 0.3091 0.2659 0.1556 0.0087  -0.0216 -0.0003 107 ARG B CA  
1588 C C   . ARG B 90  ? 0.3198 0.2883 0.1714 0.0131  -0.0335 -0.0099 107 ARG B C   
1589 O O   . ARG B 90  ? 0.3384 0.2995 0.1699 0.0185  -0.0471 -0.0085 107 ARG B O   
1590 C CB  . ARG B 90  ? 0.3371 0.2885 0.1615 -0.0003 -0.0065 0.0013  107 ARG B CB  
1591 C CG  . ARG B 90  ? 0.3346 0.2725 0.1516 -0.0077 0.0045  0.0114  107 ARG B CG  
1592 C CD  . ARG B 90  ? 0.3565 0.2692 0.1511 -0.0032 -0.0036 0.0230  107 ARG B CD  
1593 N NE  . ARG B 90  ? 0.3915 0.2890 0.1481 0.0003  -0.0100 0.0283  107 ARG B NE  
1594 C CZ  . ARG B 90  ? 0.4464 0.3269 0.1685 -0.0070 0.0003  0.0366  107 ARG B CZ  
1595 N NH1 . ARG B 90  ? 0.4289 0.3087 0.1544 -0.0194 0.0183  0.0397  107 ARG B NH1 
1596 N NH2 . ARG B 90  ? 0.4628 0.3265 0.1455 -0.0022 -0.0080 0.0423  107 ARG B NH2 
1597 N N   . ALA B 91  ? 0.2754 0.2605 0.1532 0.0106  -0.0299 -0.0197 108 ALA B N   
1598 C CA  . ALA B 91  ? 0.2833 0.2774 0.1683 0.0127  -0.0409 -0.0301 108 ALA B CA  
1599 C C   . ALA B 91  ? 0.2960 0.2963 0.1981 0.0193  -0.0579 -0.0292 108 ALA B C   
1600 O O   . ALA B 91  ? 0.2996 0.3011 0.1934 0.0221  -0.0734 -0.0340 108 ALA B O   
1601 C CB  . ALA B 91  ? 0.2635 0.2702 0.1755 0.0087  -0.0330 -0.0390 108 ALA B CB  
1602 N N   . VAL B 92  ? 0.2543 0.2600 0.1817 0.0221  -0.0556 -0.0240 109 VAL B N   
1603 C CA  . VAL B 92  ? 0.2708 0.2857 0.2197 0.0297  -0.0694 -0.0229 109 VAL B CA  
1604 C C   . VAL B 92  ? 0.3127 0.3151 0.2348 0.0373  -0.0839 -0.0165 109 VAL B C   
1605 O O   . VAL B 92  ? 0.3252 0.3360 0.2530 0.0423  -0.1019 -0.0197 109 VAL B O   
1606 C CB  . VAL B 92  ? 0.2748 0.2941 0.2491 0.0326  -0.0607 -0.0182 109 VAL B CB  
1607 C CG1 . VAL B 92  ? 0.3011 0.3281 0.2944 0.0432  -0.0731 -0.0156 109 VAL B CG1 
1608 C CG2 . VAL B 92  ? 0.2427 0.2762 0.2451 0.0264  -0.0508 -0.0241 109 VAL B CG2 
1609 N N   . ALA B 93  ? 0.3446 0.3260 0.2367 0.0378  -0.0771 -0.0068 110 ALA B N   
1610 C CA  . ALA B 93  ? 0.3679 0.3323 0.2310 0.0458  -0.0906 0.0021  110 ALA B CA  
1611 C C   . ALA B 93  ? 0.3889 0.3478 0.2178 0.0440  -0.1009 -0.0014 110 ALA B C   
1612 O O   . ALA B 93  ? 0.4297 0.3800 0.2383 0.0521  -0.1190 0.0037  110 ALA B O   
1613 C CB  . ALA B 93  ? 0.3484 0.2879 0.1878 0.0447  -0.0790 0.0140  110 ALA B CB  
1614 N N   . PHE B 94  ? 0.3770 0.3391 0.1968 0.0346  -0.0901 -0.0102 111 PHE B N   
1615 C CA  . PHE B 94  ? 0.4167 0.3746 0.2051 0.0328  -0.0985 -0.0176 111 PHE B CA  
1616 C C   . PHE B 94  ? 0.4168 0.3935 0.2305 0.0341  -0.1165 -0.0305 111 PHE B C   
1617 O O   . PHE B 94  ? 0.4400 0.4132 0.2300 0.0313  -0.1236 -0.0404 111 PHE B O   
1618 C CB  . PHE B 94  ? 0.4020 0.3558 0.1728 0.0235  -0.0779 -0.0235 111 PHE B CB  
1619 C CG  . PHE B 94  ? 0.4299 0.3646 0.1674 0.0198  -0.0615 -0.0117 111 PHE B CG  
1620 C CD1 . PHE B 94  ? 0.4762 0.3889 0.1729 0.0237  -0.0690 0.0004  111 PHE B CD1 
1621 C CD2 . PHE B 94  ? 0.4447 0.3837 0.1915 0.0118  -0.0388 -0.0128 111 PHE B CD2 
1622 C CE1 . PHE B 94  ? 0.5412 0.4355 0.2089 0.0180  -0.0522 0.0119  111 PHE B CE1 
1623 C CE2 . PHE B 94  ? 0.4710 0.3953 0.1918 0.0061  -0.0230 -0.0026 111 PHE B CE2 
1624 C CZ  . PHE B 94  ? 0.5260 0.4268 0.2063 0.0083  -0.0287 0.0100  111 PHE B CZ  
1625 N N   . ASN B 95  ? 0.3886 0.3841 0.2485 0.0375  -0.1230 -0.0312 112 ASN B N   
1626 C CA  . ASN B 95  ? 0.3562 0.3728 0.2497 0.0364  -0.1383 -0.0428 112 ASN B CA  
1627 C C   . ASN B 95  ? 0.3580 0.3768 0.2525 0.0264  -0.1312 -0.0572 112 ASN B C   
1628 O O   . ASN B 95  ? 0.3886 0.4101 0.2781 0.0237  -0.1466 -0.0686 112 ASN B O   
1629 C CB  . ASN B 95  ? 0.4014 0.4200 0.2852 0.0427  -0.1642 -0.0425 112 ASN B CB  
1630 C CG  . ASN B 95  ? 0.4974 0.5161 0.3902 0.0546  -0.1722 -0.0287 112 ASN B CG  
1631 O OD1 . ASN B 95  ? 0.5273 0.5249 0.3830 0.0598  -0.1730 -0.0174 112 ASN B OD1 
1632 N ND2 . ASN B 95  ? 0.5125 0.5543 0.4567 0.0588  -0.1754 -0.0294 112 ASN B ND2 
1633 N N   . LYS B 96  ? 0.3637 0.3813 0.2676 0.0212  -0.1091 -0.0572 113 LYS B N   
1634 C CA  . LYS B 96  ? 0.3408 0.3588 0.2496 0.0137  -0.1008 -0.0698 113 LYS B CA  
1635 C C   . LYS B 96  ? 0.3350 0.3698 0.2932 0.0096  -0.0995 -0.0740 113 LYS B C   
1636 O O   . LYS B 96  ? 0.3217 0.3672 0.3081 0.0119  -0.0956 -0.0656 113 LYS B O   
1637 C CB  . LYS B 96  ? 0.3374 0.3450 0.2279 0.0114  -0.0782 -0.0672 113 LYS B CB  
1638 C CG  . LYS B 96  ? 0.3689 0.3593 0.2090 0.0128  -0.0752 -0.0643 113 LYS B CG  
1639 C CD  . LYS B 96  ? 0.3844 0.3666 0.1943 0.0125  -0.0881 -0.0768 113 LYS B CD  
1640 C CE  . LYS B 96  ? 0.4649 0.4284 0.2194 0.0146  -0.0857 -0.0709 113 LYS B CE  
1641 N NZ  . LYS B 96  ? 0.4782 0.4356 0.2079 0.0120  -0.0942 -0.0794 113 LYS B NZ  
1642 N N   . ARG B 97  ? 0.2878 0.3224 0.2541 0.0034  -0.1021 -0.0872 114 ARG B N   
1643 C CA  . ARG B 97  ? 0.2421 0.2864 0.2497 -0.0026 -0.0963 -0.0907 114 ARG B CA  
1644 C C   . ARG B 97  ? 0.2625 0.3014 0.2732 -0.0031 -0.0744 -0.0856 114 ARG B C   
1645 O O   . ARG B 97  ? 0.2620 0.2889 0.2474 -0.0024 -0.0650 -0.0889 114 ARG B O   
1646 C CB  . ARG B 97  ? 0.3213 0.3610 0.3316 -0.0096 -0.1066 -0.1069 114 ARG B CB  
1647 C CG  . ARG B 97  ? 0.2944 0.3404 0.3461 -0.0176 -0.1027 -0.1107 114 ARG B CG  
1648 C CD  . ARG B 97  ? 0.3540 0.4049 0.4205 -0.0246 -0.1202 -0.1197 114 ARG B CD  
1649 N NE  . ARG B 97  ? 0.3688 0.4011 0.4004 -0.0263 -0.1258 -0.1310 114 ARG B NE  
1650 C CZ  . ARG B 97  ? 0.4926 0.5073 0.5182 -0.0307 -0.1180 -0.1410 114 ARG B CZ  
1651 N NH1 . ARG B 97  ? 0.4203 0.4319 0.4706 -0.0333 -0.1044 -0.1400 114 ARG B NH1 
1652 N NH2 . ARG B 97  ? 0.4754 0.4737 0.4684 -0.0320 -0.1237 -0.1516 114 ARG B NH2 
1653 N N   . ILE B 98  ? 0.1928 0.2413 0.2343 -0.0042 -0.0661 -0.0777 115 ILE B N   
1654 C CA  . ILE B 98  ? 0.2076 0.2522 0.2501 -0.0035 -0.0485 -0.0705 115 ILE B CA  
1655 C C   . ILE B 98  ? 0.1882 0.2354 0.2609 -0.0085 -0.0420 -0.0707 115 ILE B C   
1656 O O   . ILE B 98  ? 0.1997 0.2574 0.2994 -0.0118 -0.0460 -0.0695 115 ILE B O   
1657 C CB  . ILE B 98  ? 0.1981 0.2463 0.2372 0.0013  -0.0436 -0.0582 115 ILE B CB  
1658 C CG1 . ILE B 98  ? 0.2361 0.2756 0.2409 0.0054  -0.0467 -0.0557 115 ILE B CG1 
1659 C CG2 . ILE B 98  ? 0.2152 0.2618 0.2604 0.0006  -0.0286 -0.0515 115 ILE B CG2 
1660 C CD1 . ILE B 98  ? 0.2404 0.2802 0.2428 0.0105  -0.0472 -0.0450 115 ILE B CD1 
1661 N N   . LEU B 99  ? 0.1970 0.2349 0.2662 -0.0089 -0.0315 -0.0716 116 LEU B N   
1662 C CA  . LEU B 99  ? 0.1766 0.2119 0.2680 -0.0123 -0.0239 -0.0686 116 LEU B CA  
1663 C C   . LEU B 99  ? 0.1715 0.2051 0.2565 -0.0083 -0.0123 -0.0592 116 LEU B C   
1664 O O   . LEU B 99  ? 0.1871 0.2161 0.2569 -0.0047 -0.0081 -0.0614 116 LEU B O   
1665 C CB  . LEU B 99  ? 0.2165 0.2389 0.3112 -0.0155 -0.0257 -0.0796 116 LEU B CB  
1666 C CG  . LEU B 99  ? 0.2007 0.2136 0.3129 -0.0176 -0.0174 -0.0753 116 LEU B CG  
1667 C CD1 . LEU B 99  ? 0.2080 0.2273 0.3459 -0.0246 -0.0160 -0.0674 116 LEU B CD1 
1668 C CD2 . LEU B 99  ? 0.2362 0.2310 0.3472 -0.0184 -0.0186 -0.0872 116 LEU B CD2 
1669 N N   . CYS B 100 ? 0.1710 0.2093 0.2678 -0.0091 -0.0071 -0.0493 117 CYS B N   
1670 C CA  . CYS B 100 ? 0.1650 0.2012 0.2555 -0.0063 0.0013  -0.0408 117 CYS B CA  
1671 C C   . CYS B 100 ? 0.1653 0.1942 0.2687 -0.0082 0.0063  -0.0361 117 CYS B C   
1672 O O   . CYS B 100 ? 0.1920 0.2204 0.3114 -0.0132 0.0069  -0.0348 117 CYS B O   
1673 C CB  . CYS B 100 ? 0.1771 0.2195 0.2627 -0.0049 0.0037  -0.0331 117 CYS B CB  
1674 S SG  . CYS B 100 ? 0.1919 0.2366 0.2578 -0.0016 -0.0009 -0.0346 117 CYS B SG  
1675 N N   . LEU B 101 ? 0.1651 0.1888 0.2626 -0.0044 0.0099  -0.0327 118 LEU B N   
1676 C CA  . LEU B 101 ? 0.1859 0.1989 0.2915 -0.0042 0.0130  -0.0271 118 LEU B CA  
1677 C C   . LEU B 101 ? 0.1769 0.1914 0.2735 -0.0013 0.0158  -0.0166 118 LEU B C   
1678 O O   . LEU B 101 ? 0.1669 0.1875 0.2555 0.0026  0.0146  -0.0171 118 LEU B O   
1679 C CB  . LEU B 101 ? 0.2115 0.2152 0.3200 0.0001  0.0117  -0.0343 118 LEU B CB  
1680 C CG  . LEU B 101 ? 0.2099 0.2097 0.3207 -0.0024 0.0077  -0.0476 118 LEU B CG  
1681 C CD1 . LEU B 101 ? 0.2587 0.2485 0.3681 0.0040  0.0088  -0.0565 118 LEU B CD1 
1682 C CD2 . LEU B 101 ? 0.2509 0.2436 0.3767 -0.0108 0.0057  -0.0480 118 LEU B CD2 
1683 N N   . PHE B 102 ? 0.1758 0.1844 0.2729 -0.0039 0.0197  -0.0072 119 PHE B N   
1684 C CA  . PHE B 102 ? 0.1818 0.1896 0.2650 -0.0019 0.0212  0.0023  119 PHE B CA  
1685 C C   . PHE B 102 ? 0.1871 0.1801 0.2689 -0.0012 0.0229  0.0123  119 PHE B C   
1686 O O   . PHE B 102 ? 0.2071 0.1909 0.2972 -0.0059 0.0278  0.0154  119 PHE B O   
1687 C CB  . PHE B 102 ? 0.1625 0.1757 0.2387 -0.0051 0.0262  0.0047  119 PHE B CB  
1688 C CG  . PHE B 102 ? 0.1736 0.1826 0.2305 -0.0036 0.0278  0.0126  119 PHE B CG  
1689 C CD1 . PHE B 102 ? 0.1904 0.2037 0.2355 -0.0011 0.0220  0.0111  119 PHE B CD1 
1690 C CD2 . PHE B 102 ? 0.1952 0.1952 0.2443 -0.0057 0.0350  0.0214  119 PHE B CD2 
1691 C CE1 . PHE B 102 ? 0.2151 0.2233 0.2406 -0.0007 0.0209  0.0169  119 PHE B CE1 
1692 C CE2 . PHE B 102 ? 0.2127 0.2062 0.2382 -0.0043 0.0355  0.0278  119 PHE B CE2 
1693 C CZ  . PHE B 102 ? 0.2026 0.2000 0.2159 -0.0017 0.0272  0.0249  119 PHE B CZ  
1694 N N   . ARG B 103 ? 0.1461 0.1818 0.2730 -0.0035 0.0376  0.0079  120 ARG B N   
1695 C CA  . ARG B 103 ? 0.1636 0.1886 0.2955 -0.0019 0.0410  0.0175  120 ARG B CA  
1696 C C   . ARG B 103 ? 0.1666 0.1895 0.2851 -0.0041 0.0434  0.0289  120 ARG B C   
1697 O O   . ARG B 103 ? 0.1800 0.2096 0.2851 -0.0025 0.0384  0.0332  120 ARG B O   
1698 C CB  . ARG B 103 ? 0.1828 0.2114 0.3152 0.0063  0.0387  0.0205  120 ARG B CB  
1699 C CG  . ARG B 103 ? 0.1820 0.2127 0.3218 0.0135  0.0370  0.0089  120 ARG B CG  
1700 C CD  . ARG B 103 ? 0.2073 0.2399 0.3500 0.0248  0.0367  0.0123  120 ARG B CD  
1701 N NE  . ARG B 103 ? 0.1829 0.2313 0.3213 0.0258  0.0354  0.0240  120 ARG B NE  
1702 C CZ  . ARG B 103 ? 0.1751 0.2457 0.3124 0.0246  0.0340  0.0258  120 ARG B CZ  
1703 N NH1 . ARG B 103 ? 0.1777 0.2565 0.3124 0.0234  0.0358  0.0189  120 ARG B NH1 
1704 N NH2 . ARG B 103 ? 0.1847 0.2697 0.3252 0.0250  0.0301  0.0354  120 ARG B NH2 
1705 N N   . PRO B 104 ? 0.1902 0.2047 0.3129 -0.0064 0.0506  0.0346  121 PRO B N   
1706 C CA  . PRO B 104 ? 0.2132 0.2251 0.3172 -0.0032 0.0544  0.0465  121 PRO B CA  
1707 C C   . PRO B 104 ? 0.2306 0.2381 0.3224 0.0047  0.0519  0.0566  121 PRO B C   
1708 O O   . PRO B 104 ? 0.2179 0.2251 0.2869 0.0102  0.0495  0.0626  121 PRO B O   
1709 C CB  . PRO B 104 ? 0.2333 0.2395 0.3511 -0.0059 0.0666  0.0538  121 PRO B CB  
1710 C CG  . PRO B 104 ? 0.2507 0.2591 0.3956 -0.0134 0.0649  0.0413  121 PRO B CG  
1711 C CD  . PRO B 104 ? 0.1957 0.2043 0.3420 -0.0115 0.0553  0.0304  121 PRO B CD  
1712 N N   . GLN B 105 ? 0.1952 0.1985 0.2996 0.0078  0.0510  0.0577  122 GLN B N   
1713 C CA  . GLN B 105 ? 0.2200 0.2213 0.3134 0.0175  0.0472  0.0672  122 GLN B CA  
1714 C C   . GLN B 105 ? 0.2033 0.2203 0.2850 0.0187  0.0346  0.0630  122 GLN B C   
1715 O O   . GLN B 105 ? 0.2065 0.2248 0.2757 0.0268  0.0279  0.0698  122 GLN B O   
1716 C CB  . GLN B 105 ? 0.2074 0.2008 0.3177 0.0223  0.0482  0.0677  122 GLN B CB  
1717 C CG  . GLN B 105 ? 0.2508 0.2411 0.3526 0.0349  0.0448  0.0785  122 GLN B CG  
1718 C CD  . GLN B 105 ? 0.2857 0.2977 0.3859 0.0390  0.0328  0.0734  122 GLN B CD  
1719 O OE1 . GLN B 105 ? 0.2460 0.2721 0.3582 0.0345  0.0301  0.0629  122 GLN B OE1 
1720 N NE2 . GLN B 105 ? 0.2418 0.2577 0.3289 0.0488  0.0256  0.0820  122 GLN B NE2 
1721 N N   . SER B 106 ? 0.1752 0.2035 0.2617 0.0109  0.0302  0.0527  123 SER B N   
1722 C CA  . SER B 106 ? 0.1956 0.2369 0.2768 0.0088  0.0183  0.0504  123 SER B CA  
1723 C C   . SER B 106 ? 0.1988 0.2332 0.2559 0.0107  0.0114  0.0522  123 SER B C   
1724 O O   . SER B 106 ? 0.2142 0.2556 0.2674 0.0101  -0.0024 0.0504  123 SER B O   
1725 C CB  . SER B 106 ? 0.1638 0.2146 0.2542 0.0002  0.0178  0.0420  123 SER B CB  
1726 O OG  . SER B 106 ? 0.1717 0.2133 0.2519 -0.0041 0.0215  0.0376  123 SER B OG  
1727 N N   . GLY B 107 ? 0.2061 0.2278 0.2484 0.0139  0.0200  0.0553  124 GLY B N   
1728 C CA  . GLY B 107 ? 0.2253 0.2396 0.2393 0.0197  0.0148  0.0554  124 GLY B CA  
1729 C C   . GLY B 107 ? 0.2209 0.2345 0.2290 0.0130  0.0092  0.0452  124 GLY B C   
1730 O O   . GLY B 107 ? 0.2591 0.2636 0.2410 0.0198  0.0043  0.0429  124 GLY B O   
1731 N N   . ARG B 108 ? 0.2092 0.2304 0.2376 0.0026  0.0098  0.0392  125 ARG B N   
1732 C CA  . ARG B 108 ? 0.2184 0.2370 0.2419 -0.0034 0.0042  0.0312  125 ARG B CA  
1733 C C   . ARG B 108 ? 0.2140 0.2278 0.2322 -0.0015 0.0156  0.0289  125 ARG B C   
1734 O O   . ARG B 108 ? 0.2217 0.2381 0.2507 -0.0001 0.0282  0.0330  125 ARG B O   
1735 C CB  . ARG B 108 ? 0.2063 0.2362 0.2516 -0.0130 0.0020  0.0287  125 ARG B CB  
1736 C CG  . ARG B 108 ? 0.2343 0.2742 0.2914 -0.0165 -0.0095 0.0317  125 ARG B CG  
1737 C CD  . ARG B 108 ? 0.2167 0.2691 0.2938 -0.0251 -0.0086 0.0324  125 ARG B CD  
1738 N NE  . ARG B 108 ? 0.2549 0.3227 0.3513 -0.0293 -0.0177 0.0377  125 ARG B NE  
1739 C CZ  . ARG B 108 ? 0.2615 0.3474 0.3760 -0.0255 -0.0130 0.0428  125 ARG B CZ  
1740 N NH1 . ARG B 108 ? 0.2633 0.3501 0.3777 -0.0181 -0.0003 0.0420  125 ARG B NH1 
1741 N NH2 . ARG B 108 ? 0.3020 0.4056 0.4372 -0.0288 -0.0224 0.0480  125 ARG B NH2 
1742 N N   . VAL B 109 ? 0.2128 0.2194 0.2171 -0.0016 0.0101  0.0224  126 VAL B N   
1743 C CA  . VAL B 109 ? 0.2050 0.2112 0.2081 0.0002  0.0187  0.0187  126 VAL B CA  
1744 C C   . VAL B 109 ? 0.1718 0.1820 0.1882 -0.0079 0.0156  0.0132  126 VAL B C   
1745 O O   . VAL B 109 ? 0.1921 0.1958 0.2028 -0.0119 0.0050  0.0110  126 VAL B O   
1746 C CB  . VAL B 109 ? 0.2333 0.2271 0.2073 0.0102  0.0153  0.0152  126 VAL B CB  
1747 C CG1 . VAL B 109 ? 0.2365 0.2347 0.2135 0.0136  0.0253  0.0123  126 VAL B CG1 
1748 C CG2 . VAL B 109 ? 0.2851 0.2750 0.2389 0.0220  0.0181  0.0218  126 VAL B CG2 
1749 N N   . LEU B 110 ? 0.1776 0.1977 0.2122 -0.0099 0.0240  0.0116  127 LEU B N   
1750 C CA  . LEU B 110 ? 0.1536 0.1786 0.1962 -0.0136 0.0218  0.0071  127 LEU B CA  
1751 C C   . LEU B 110 ? 0.1848 0.2011 0.2123 -0.0114 0.0174  0.0029  127 LEU B C   
1752 O O   . LEU B 110 ? 0.2021 0.2151 0.2207 -0.0053 0.0201  0.0001  127 LEU B O   
1753 C CB  . LEU B 110 ? 0.1493 0.1842 0.2102 -0.0129 0.0285  0.0026  127 LEU B CB  
1754 C CG  . LEU B 110 ? 0.1474 0.1878 0.2105 -0.0118 0.0262  -0.0035 127 LEU B CG  
1755 C CD1 . LEU B 110 ? 0.1695 0.2138 0.2328 -0.0136 0.0243  0.0012  127 LEU B CD1 
1756 C CD2 . LEU B 110 ? 0.1482 0.1962 0.2287 -0.0094 0.0287  -0.0119 127 LEU B CD2 
1757 N N   . SER B 111 ? 0.1600 0.1730 0.1855 -0.0155 0.0116  0.0042  128 SER B N   
1758 C CA  . SER B 111 ? 0.1613 0.1630 0.1738 -0.0134 0.0072  0.0019  128 SER B CA  
1759 C C   . SER B 111 ? 0.1830 0.1873 0.1912 -0.0048 0.0116  -0.0050 128 SER B C   
1760 O O   . SER B 111 ? 0.1740 0.1926 0.1959 -0.0029 0.0169  -0.0085 128 SER B O   
1761 C CB  . SER B 111 ? 0.1613 0.1671 0.1801 -0.0173 0.0074  0.0071  128 SER B CB  
1762 O OG  . SER B 111 ? 0.1765 0.1680 0.1819 -0.0149 0.0035  0.0075  128 SER B OG  
1763 N N   . ALA B 112 ? 0.1716 0.2068 0.1765 -0.0125 0.0332  -0.0234 129 ALA B N   
1764 C CA  . ALA B 112 ? 0.1910 0.2281 0.2039 -0.0063 0.0366  -0.0195 129 ALA B CA  
1765 C C   . ALA B 112 ? 0.1852 0.2132 0.2030 -0.0035 0.0331  -0.0180 129 ALA B C   
1766 O O   . ALA B 112 ? 0.1880 0.2231 0.2169 0.0012  0.0312  -0.0138 129 ALA B O   
1767 C CB  . ALA B 112 ? 0.1867 0.2211 0.1926 -0.0010 0.0445  -0.0256 129 ALA B CB  
1768 N N   . MET B 113 ? 0.1782 0.1926 0.1884 -0.0059 0.0324  -0.0210 130 MET B N   
1769 C CA  . MET B 113 ? 0.1979 0.2031 0.2070 -0.0011 0.0305  -0.0178 130 MET B CA  
1770 C C   . MET B 113 ? 0.2107 0.2249 0.2260 -0.0017 0.0222  -0.0144 130 MET B C   
1771 O O   . MET B 113 ? 0.2303 0.2446 0.2464 0.0046  0.0176  -0.0121 130 MET B O   
1772 C CB  . MET B 113 ? 0.2232 0.2109 0.2225 -0.0043 0.0351  -0.0200 130 MET B CB  
1773 C CG  . MET B 113 ? 0.2595 0.2316 0.2544 -0.0032 0.0432  -0.0246 130 MET B CG  
1774 S SD  . MET B 113 ? 0.2650 0.2333 0.2615 0.0099  0.0463  -0.0226 130 MET B SD  
1775 C CE  . MET B 113 ? 0.3233 0.2710 0.3117 0.0185  0.0479  -0.0137 130 MET B CE  
1776 N N   . ILE B 114 ? 0.1599 0.1813 0.1791 -0.0080 0.0193  -0.0149 131 ILE B N   
1777 C CA  . ILE B 114 ? 0.1695 0.1962 0.1958 -0.0086 0.0118  -0.0139 131 ILE B CA  
1778 C C   . ILE B 114 ? 0.1708 0.2095 0.2136 -0.0091 0.0089  -0.0110 131 ILE B C   
1779 O O   . ILE B 114 ? 0.1656 0.2091 0.2180 -0.0069 0.0024  -0.0119 131 ILE B O   
1780 C CB  . ILE B 114 ? 0.1453 0.1716 0.1700 -0.0135 0.0107  -0.0153 131 ILE B CB  
1781 C CG1 . ILE B 114 ? 0.1911 0.2090 0.2050 -0.0145 0.0154  -0.0183 131 ILE B CG1 
1782 C CG2 . ILE B 114 ? 0.1797 0.2078 0.2118 -0.0131 0.0034  -0.0162 131 ILE B CG2 
1783 C CD1 . ILE B 114 ? 0.2063 0.2147 0.2108 -0.0093 0.0167  -0.0173 131 ILE B CD1 
1784 N N   . ARG B 115 ? 0.1639 0.2089 0.2102 -0.0120 0.0140  -0.0078 132 ARG B N   
1785 C CA  . ARG B 115 ? 0.1889 0.2459 0.2526 -0.0135 0.0151  -0.0028 132 ARG B CA  
1786 C C   . ARG B 115 ? 0.1864 0.2513 0.2602 -0.0080 0.0153  -0.0038 132 ARG B C   
1787 O O   . ARG B 115 ? 0.1876 0.2636 0.2820 -0.0094 0.0111  -0.0028 132 ARG B O   
1788 C CB  . ARG B 115 ? 0.1979 0.2598 0.2566 -0.0153 0.0231  0.0023  132 ARG B CB  
1789 C CG  . ARG B 115 ? 0.2421 0.3161 0.3169 -0.0174 0.0286  0.0104  132 ARG B CG  
1790 C CD  . ARG B 115 ? 0.2303 0.3016 0.3169 -0.0234 0.0252  0.0166  132 ARG B CD  
1791 N NE  . ARG B 115 ? 0.2204 0.2861 0.2918 -0.0234 0.0261  0.0213  132 ARG B NE  
1792 C CZ  . ARG B 115 ? 0.2061 0.2654 0.2846 -0.0263 0.0235  0.0276  132 ARG B CZ  
1793 N NH1 . ARG B 115 ? 0.2410 0.2967 0.3418 -0.0312 0.0201  0.0282  132 ARG B NH1 
1794 N NH2 . ARG B 115 ? 0.2215 0.2782 0.2855 -0.0236 0.0237  0.0328  132 ARG B NH2 
1795 N N   . GLY B 116 ? 0.1676 0.2266 0.2292 -0.0015 0.0196  -0.0063 133 GLY B N   
1796 C CA  . GLY B 116 ? 0.1683 0.2343 0.2386 0.0068  0.0201  -0.0065 133 GLY B CA  
1797 C C   . GLY B 116 ? 0.1839 0.2481 0.2547 0.0129  0.0102  -0.0082 133 GLY B C   
1798 O O   . GLY B 116 ? 0.2094 0.2850 0.2923 0.0208  0.0073  -0.0079 133 GLY B O   
1799 N N   . ALA B 117 ? 0.1724 0.2246 0.2294 0.0110  0.0050  -0.0100 134 ALA B N   
1800 C CA  . ALA B 117 ? 0.1863 0.2379 0.2386 0.0179  -0.0048 -0.0116 134 ALA B CA  
1801 C C   . ALA B 117 ? 0.2257 0.2937 0.2980 0.0147  -0.0162 -0.0158 134 ALA B C   
1802 O O   . ALA B 117 ? 0.2343 0.3093 0.3072 0.0220  -0.0269 -0.0192 134 ALA B O   
1803 C CB  . ALA B 117 ? 0.2006 0.2352 0.2305 0.0173  -0.0040 -0.0121 134 ALA B CB  
1804 N N   . ALA B 118 ? 0.1897 0.2632 0.2782 0.0041  -0.0144 -0.0159 135 ALA B N   
1805 C CA  . ALA B 118 ? 0.2084 0.2921 0.3182 -0.0018 -0.0243 -0.0210 135 ALA B CA  
1806 C C   . ALA B 118 ? 0.2047 0.3106 0.3405 0.0008  -0.0301 -0.0229 135 ALA B C   
1807 O O   . ALA B 118 ? 0.2118 0.3281 0.3575 0.0037  -0.0221 -0.0177 135 ALA B O   
1808 C CB  . ALA B 118 ? 0.2186 0.2996 0.3407 -0.0132 -0.0184 -0.0173 135 ALA B CB  
1809 N N   . ASP B 119 ? 0.1742 0.2894 0.3226 0.0004  -0.0446 -0.0321 136 ASP B N   
1810 C CA  . ASP B 119 ? 0.1708 0.3121 0.3512 0.0009  -0.0529 -0.0364 136 ASP B CA  
1811 C C   . ASP B 119 ? 0.1691 0.3187 0.3822 -0.0132 -0.0597 -0.0439 136 ASP B C   
1812 O O   . ASP B 119 ? 0.1629 0.3368 0.4090 -0.0157 -0.0686 -0.0502 136 ASP B O   
1813 C CB  . ASP B 119 ? 0.2112 0.3607 0.3783 0.0161  -0.0667 -0.0418 136 ASP B CB  
1814 C CG  . ASP B 119 ? 0.2421 0.3827 0.3898 0.0181  -0.0805 -0.0524 136 ASP B CG  
1815 O OD1 . ASP B 119 ? 0.2158 0.3456 0.3668 0.0071  -0.0808 -0.0579 136 ASP B OD1 
1816 O OD2 . ASP B 119 ? 0.3016 0.4442 0.4274 0.0325  -0.0898 -0.0543 136 ASP B OD2 
1817 N N   . GLY B 120 ? 0.1775 0.3075 0.3849 -0.0226 -0.0556 -0.0434 137 GLY B N   
1818 C CA  . GLY B 120 ? 0.1687 0.2992 0.4072 -0.0365 -0.0598 -0.0494 137 GLY B CA  
1819 C C   . GLY B 120 ? 0.1748 0.3021 0.4093 -0.0355 -0.0763 -0.0653 137 GLY B C   
1820 O O   . GLY B 120 ? 0.2259 0.3441 0.4750 -0.0454 -0.0771 -0.0697 137 GLY B O   
1821 N N   . SER B 121 ? 0.2321 0.3657 0.4451 -0.0225 -0.0887 -0.0737 138 SER B N   
1822 C CA  . SER B 121 ? 0.2504 0.3820 0.4532 -0.0191 -0.1037 -0.0889 138 SER B CA  
1823 C C   . SER B 121 ? 0.2420 0.3594 0.4052 -0.0078 -0.1083 -0.0940 138 SER B C   
1824 O O   . SER B 121 ? 0.2488 0.3465 0.4022 -0.0116 -0.1053 -0.0980 138 SER B O   
1825 C CB  . SER B 121 ? 0.2442 0.4007 0.4568 -0.0124 -0.1149 -0.0937 138 SER B CB  
1826 O OG  . SER B 121 ? 0.3782 0.5354 0.5939 -0.0147 -0.1277 -0.1089 138 SER B OG  
1827 N N   . ARG B 122 ? 0.2400 0.3667 0.3793 0.0075  -0.1140 -0.0926 139 ARG B N   
1828 C CA  . ARG B 122 ? 0.2541 0.3648 0.3491 0.0192  -0.1134 -0.0931 139 ARG B CA  
1829 C C   . ARG B 122 ? 0.2895 0.3793 0.3648 0.0181  -0.0932 -0.0778 139 ARG B C   
1830 O O   . ARG B 122 ? 0.3154 0.3905 0.3598 0.0241  -0.0890 -0.0778 139 ARG B O   
1831 C CB  . ARG B 122 ? 0.3010 0.4245 0.3724 0.0371  -0.1236 -0.0928 139 ARG B CB  
1832 C CG  . ARG B 122 ? 0.3769 0.5036 0.4347 0.0426  -0.1373 -0.1075 139 ARG B CG  
1833 C CD  . ARG B 122 ? 0.4101 0.5441 0.4345 0.0625  -0.1443 -0.1036 139 ARG B CD  
1834 N NE  . ARG B 122 ? 0.3649 0.4820 0.3428 0.0741  -0.1386 -0.1000 139 ARG B NE  
1835 C CZ  . ARG B 122 ? 0.3638 0.4727 0.3214 0.0762  -0.1408 -0.1112 139 ARG B CZ  
1836 N NH1 . ARG B 122 ? 0.4051 0.5173 0.3846 0.0666  -0.1492 -0.1278 139 ARG B NH1 
1837 N NH2 . ARG B 122 ? 0.4161 0.5124 0.3310 0.0882  -0.1328 -0.1047 139 ARG B NH2 
1838 N N   . PHE B 123 ? 0.2052 0.2949 0.2977 0.0109  -0.0807 -0.0657 140 PHE B N   
1839 C CA  . PHE B 123 ? 0.2335 0.3061 0.3127 0.0075  -0.0640 -0.0545 140 PHE B CA  
1840 C C   . PHE B 123 ? 0.2045 0.2776 0.3125 -0.0058 -0.0578 -0.0508 140 PHE B C   
1841 O O   . PHE B 123 ? 0.1934 0.2782 0.3210 -0.0091 -0.0531 -0.0442 140 PHE B O   
1842 C CB  . PHE B 123 ? 0.2078 0.2783 0.2708 0.0154  -0.0543 -0.0427 140 PHE B CB  
1843 C CG  . PHE B 123 ? 0.2170 0.2703 0.2625 0.0129  -0.0396 -0.0347 140 PHE B CG  
1844 C CD1 . PHE B 123 ? 0.1985 0.2480 0.2554 0.0027  -0.0321 -0.0318 140 PHE B CD1 
1845 C CD2 . PHE B 123 ? 0.2104 0.2527 0.2291 0.0209  -0.0336 -0.0297 140 PHE B CD2 
1846 C CE1 . PHE B 123 ? 0.2186 0.2570 0.2616 0.0009  -0.0213 -0.0265 140 PHE B CE1 
1847 C CE2 . PHE B 123 ? 0.2289 0.2583 0.2369 0.0169  -0.0209 -0.0243 140 PHE B CE2 
1848 C CZ  . PHE B 123 ? 0.2119 0.2411 0.2326 0.0069  -0.0160 -0.0240 140 PHE B CZ  
1849 N N   . GLN B 124 ? 0.1935 0.2538 0.3037 -0.0123 -0.0566 -0.0540 141 GLN B N   
1850 C CA  . GLN B 124 ? 0.1889 0.2461 0.3237 -0.0235 -0.0503 -0.0483 141 GLN B CA  
1851 C C   . GLN B 124 ? 0.2011 0.2454 0.3200 -0.0237 -0.0383 -0.0381 141 GLN B C   
1852 O O   . GLN B 124 ? 0.1983 0.2326 0.2963 -0.0186 -0.0379 -0.0413 141 GLN B O   
1853 C CB  . GLN B 124 ? 0.1750 0.2260 0.3298 -0.0305 -0.0596 -0.0598 141 GLN B CB  
1854 C CG  . GLN B 124 ? 0.1735 0.2417 0.3551 -0.0344 -0.0720 -0.0705 141 GLN B CG  
1855 C CD  . GLN B 124 ? 0.2036 0.2609 0.3981 -0.0402 -0.0796 -0.0830 141 GLN B CD  
1856 O OE1 . GLN B 124 ? 0.2437 0.2832 0.4466 -0.0466 -0.0728 -0.0788 141 GLN B OE1 
1857 N NE2 . GLN B 124 ? 0.2241 0.2903 0.4170 -0.0363 -0.0923 -0.0967 141 GLN B NE2 
1858 N N   . VAL B 125 ? 0.1767 0.2237 0.3059 -0.0288 -0.0285 -0.0264 142 VAL B N   
1859 C CA  . VAL B 125 ? 0.1944 0.2328 0.3108 -0.0287 -0.0193 -0.0173 142 VAL B CA  
1860 C C   . VAL B 125 ? 0.1796 0.2127 0.3156 -0.0359 -0.0156 -0.0095 142 VAL B C   
1861 O O   . VAL B 125 ? 0.2005 0.2421 0.3540 -0.0413 -0.0101 -0.0019 142 VAL B O   
1862 C CB  . VAL B 125 ? 0.1761 0.2213 0.2792 -0.0258 -0.0103 -0.0099 142 VAL B CB  
1863 C CG1 . VAL B 125 ? 0.1861 0.2258 0.2772 -0.0259 -0.0038 -0.0028 142 VAL B CG1 
1864 C CG2 . VAL B 125 ? 0.2054 0.2505 0.2898 -0.0188 -0.0122 -0.0155 142 VAL B CG2 
1865 N N   . TRP B 126 ? 0.1726 0.1914 0.3061 -0.0353 -0.0172 -0.0101 143 TRP B N   
1866 C CA  . TRP B 126 ? 0.1858 0.1940 0.3366 -0.0405 -0.0134 -0.0010 143 TRP B CA  
1867 C C   . TRP B 126 ? 0.2369 0.2410 0.3717 -0.0354 -0.0066 0.0114  143 TRP B C   
1868 O O   . TRP B 126 ? 0.2341 0.2353 0.3526 -0.0287 -0.0093 0.0069  143 TRP B O   
1869 C CB  . TRP B 126 ? 0.1823 0.1745 0.3466 -0.0422 -0.0216 -0.0120 143 TRP B CB  
1870 C CG  . TRP B 126 ? 0.1665 0.1640 0.3539 -0.0496 -0.0292 -0.0232 143 TRP B CG  
1871 C CD1 . TRP B 126 ? 0.2324 0.2391 0.4141 -0.0465 -0.0397 -0.0391 143 TRP B CD1 
1872 C CD2 . TRP B 126 ? 0.1762 0.1732 0.3973 -0.0613 -0.0269 -0.0190 143 TRP B CD2 
1873 N NE1 . TRP B 126 ? 0.1985 0.2128 0.4090 -0.0550 -0.0466 -0.0471 143 TRP B NE1 
1874 C CE2 . TRP B 126 ? 0.1898 0.1981 0.4234 -0.0642 -0.0377 -0.0349 143 TRP B CE2 
1875 C CE3 . TRP B 126 ? 0.1899 0.1782 0.4292 -0.0686 -0.0157 -0.0021 143 TRP B CE3 
1876 C CZ2 . TRP B 126 ? 0.1870 0.2002 0.4450 -0.0723 -0.0368 -0.0350 143 TRP B CZ2 
1877 C CZ3 . TRP B 126 ? 0.2417 0.2333 0.5040 -0.0769 -0.0135 -0.0017 143 TRP B CZ3 
1878 C CH2 . TRP B 126 ? 0.2205 0.2248 0.4937 -0.0794 -0.0243 -0.0190 143 TRP B CH2 
1879 N N   . ASP B 127 ? 0.1937 0.1999 0.3333 -0.0382 0.0023  0.0269  144 ASP B N   
1880 C CA  . ASP B 127 ? 0.2292 0.2294 0.3566 -0.0327 0.0069  0.0403  144 ASP B CA  
1881 C C   . ASP B 127 ? 0.2303 0.2091 0.3723 -0.0326 0.0047  0.0434  144 ASP B C   
1882 O O   . ASP B 127 ? 0.2732 0.2417 0.4399 -0.0410 0.0053  0.0431  144 ASP B O   
1883 C CB  . ASP B 127 ? 0.2067 0.2154 0.3310 -0.0341 0.0183  0.0572  144 ASP B CB  
1884 C CG  . ASP B 127 ? 0.2526 0.2801 0.3644 -0.0333 0.0215  0.0528  144 ASP B CG  
1885 O OD1 . ASP B 127 ? 0.2384 0.2721 0.3277 -0.0271 0.0194  0.0486  144 ASP B OD1 
1886 O OD2 . ASP B 127 ? 0.2947 0.3310 0.4213 -0.0389 0.0262  0.0528  144 ASP B OD2 
1887 N N   . TYR B 128 ? 0.2319 0.2042 0.3614 -0.0232 0.0021  0.0459  145 TYR B N   
1888 C CA  . TYR B 128 ? 0.2621 0.2115 0.4049 -0.0203 0.0001  0.0483  145 TYR B CA  
1889 C C   . TYR B 128 ? 0.2657 0.2128 0.3942 -0.0079 0.0007  0.0610  145 TYR B C   
1890 O O   . TYR B 128 ? 0.2467 0.2124 0.3554 -0.0014 -0.0009 0.0611  145 TYR B O   
1891 C CB  . TYR B 128 ? 0.2423 0.1837 0.3916 -0.0195 -0.0089 0.0270  145 TYR B CB  
1892 C CG  . TYR B 128 ? 0.2445 0.1952 0.3755 -0.0089 -0.0132 0.0182  145 TYR B CG  
1893 C CD1 . TYR B 128 ? 0.2467 0.2182 0.3613 -0.0090 -0.0135 0.0121  145 TYR B CD1 
1894 C CD2 . TYR B 128 ? 0.2635 0.2023 0.3963 0.0011  -0.0157 0.0164  145 TYR B CD2 
1895 C CE1 . TYR B 128 ? 0.2345 0.2154 0.3372 -0.0015 -0.0155 0.0048  145 TYR B CE1 
1896 C CE2 . TYR B 128 ? 0.2565 0.2078 0.3774 0.0102  -0.0182 0.0086  145 TYR B CE2 
1897 C CZ  . TYR B 128 ? 0.2429 0.2158 0.3497 0.0078  -0.0177 0.0030  145 TYR B CZ  
1898 O OH  . TYR B 128 ? 0.2608 0.2469 0.3603 0.0150  -0.0184 -0.0042 145 TYR B OH  
1899 N N   . GLU B 129 ? 0.2989 0.2226 0.4394 -0.0041 0.0023  0.0712  146 GLU B N   
1900 C CA  . GLU B 129 ? 0.3381 0.2575 0.4682 0.0108  0.0007  0.0825  146 GLU B CA  
1901 C C   . GLU B 129 ? 0.3390 0.2496 0.4758 0.0189  -0.0069 0.0663  146 GLU B C   
1902 O O   . GLU B 129 ? 0.3611 0.2535 0.5147 0.0136  -0.0087 0.0532  146 GLU B O   
1903 C CB  . GLU B 129 ? 0.3968 0.2935 0.5337 0.0134  0.0086  0.1071  146 GLU B CB  
1904 C CG  . GLU B 129 ? 0.4467 0.3541 0.5732 0.0084  0.0189  0.1265  146 GLU B CG  
1905 C CD  . GLU B 129 ? 0.6368 0.5178 0.7759 0.0063  0.0304  0.1510  146 GLU B CD  
1906 O OE1 . GLU B 129 ? 0.7355 0.6244 0.8616 0.0062  0.0409  0.1714  146 GLU B OE1 
1907 O OE2 . GLU B 129 ? 0.6943 0.5453 0.8556 0.0052  0.0300  0.1500  146 GLU B OE2 
1908 N N   . GLU B 130 ? 0.4366 0.2966 0.3347 0.0568  -0.0547 0.0053  147 GLU B N   
1909 C CA  . GLU B 130 ? 0.4108 0.3030 0.3444 0.0730  -0.0662 -0.0084 147 GLU B CA  
1910 C C   . GLU B 130 ? 0.4738 0.3227 0.4043 0.0897  -0.0672 -0.0066 147 GLU B C   
1911 O O   . GLU B 130 ? 0.4654 0.3301 0.4240 0.0958  -0.0658 -0.0214 147 GLU B O   
1912 C CB  . GLU B 130 ? 0.4154 0.3506 0.3502 0.0905  -0.0882 -0.0092 147 GLU B CB  
1913 C CG  . GLU B 130 ? 0.5094 0.4201 0.4087 0.1186  -0.1057 0.0065  147 GLU B CG  
1914 C CD  . GLU B 130 ? 0.5333 0.4164 0.4324 0.1522  -0.1122 0.0097  147 GLU B CD  
1915 O OE1 . GLU B 130 ? 0.5106 0.4065 0.4412 0.1581  -0.1062 -0.0042 147 GLU B OE1 
1916 O OE2 . GLU B 130 ? 0.5921 0.4338 0.4520 0.1758  -0.1239 0.0263  147 GLU B OE2 
1917 N N   . GLY B 131 ? 0.5111 0.2981 0.4008 0.0969  -0.0698 0.0115  148 GLY B N   
1918 C CA  . GLY B 131 ? 0.5649 0.2915 0.4400 0.1133  -0.0743 0.0130  148 GLY B CA  
1919 C C   . GLY B 131 ? 0.5901 0.2896 0.4786 0.0874  -0.0613 0.0039  148 GLY B C   
1920 O O   . GLY B 131 ? 0.6289 0.2802 0.5075 0.1009  -0.0676 -0.0034 148 GLY B O   
1921 N N   . GLU B 132 ? 0.5465 0.2744 0.4542 0.0529  -0.0451 0.0033  149 GLU B N   
1922 C CA  . GLU B 132 ? 0.5729 0.2827 0.4944 0.0247  -0.0352 -0.0022 149 GLU B CA  
1923 C C   . GLU B 132 ? 0.4967 0.2641 0.4600 0.0201  -0.0311 -0.0246 149 GLU B C   
1924 O O   . GLU B 132 ? 0.4886 0.2554 0.4669 -0.0041 -0.0242 -0.0300 149 GLU B O   
1925 C CB  . GLU B 132 ? 0.6011 0.3044 0.5145 -0.0100 -0.0187 0.0176  149 GLU B CB  
1926 C CG  . GLU B 132 ? 0.5624 0.3324 0.4980 -0.0202 -0.0046 0.0151  149 GLU B CG  
1927 C CD  . GLU B 132 ? 0.6581 0.4267 0.5727 -0.0387 0.0124  0.0381  149 GLU B CD  
1928 O OE1 . GLU B 132 ? 0.5209 0.3359 0.4444 -0.0411 0.0250  0.0355  149 GLU B OE1 
1929 O OE2 . GLU B 132 ? 0.7369 0.4553 0.6223 -0.0496 0.0142  0.0594  149 GLU B OE2 
1930 N N   . VAL B 133 ? 0.4511 0.2702 0.4330 0.0407  -0.0361 -0.0360 150 VAL B N   
1931 C CA  . VAL B 133 ? 0.4376 0.3102 0.4537 0.0326  -0.0299 -0.0517 150 VAL B CA  
1932 C C   . VAL B 133 ? 0.4238 0.2808 0.4464 0.0354  -0.0320 -0.0678 150 VAL B C   
1933 O O   . VAL B 133 ? 0.4249 0.3046 0.4661 0.0179  -0.0255 -0.0760 150 VAL B O   
1934 C CB  . VAL B 133 ? 0.3943 0.3239 0.4273 0.0473  -0.0351 -0.0567 150 VAL B CB  
1935 C CG1 . VAL B 133 ? 0.3536 0.2969 0.3928 0.0790  -0.0453 -0.0658 150 VAL B CG1 
1936 C CG2 . VAL B 133 ? 0.3314 0.3057 0.3898 0.0303  -0.0262 -0.0646 150 VAL B CG2 
1937 N N   . GLU B 134 ? 0.4815 0.2956 0.4835 0.0601  -0.0425 -0.0735 151 GLU B N   
1938 C CA  . GLU B 134 ? 0.4601 0.2497 0.4576 0.0653  -0.0461 -0.0930 151 GLU B CA  
1939 C C   . GLU B 134 ? 0.5253 0.2697 0.5146 0.0285  -0.0453 -0.0910 151 GLU B C   
1940 O O   . GLU B 134 ? 0.5079 0.2630 0.5074 0.0157  -0.0457 -0.1064 151 GLU B O   
1941 C CB  . GLU B 134 ? 0.5389 0.2815 0.5070 0.1062  -0.0580 -0.1012 151 GLU B CB  
1942 C CG  . GLU B 134 ? 0.5096 0.3192 0.4965 0.1455  -0.0583 -0.1091 151 GLU B CG  
1943 C CD  . GLU B 134 ? 0.5151 0.3498 0.5051 0.1612  -0.0637 -0.0913 151 GLU B CD  
1944 O OE1 . GLU B 134 ? 0.5412 0.3385 0.5136 0.1429  -0.0655 -0.0730 151 GLU B OE1 
1945 O OE2 . GLU B 134 ? 0.5264 0.4237 0.5362 0.1916  -0.0664 -0.0949 151 GLU B OE2 
1946 N N   . ALA B 135 ? 0.5133 0.2125 0.4843 0.0092  -0.0445 -0.0706 152 ALA B N   
1947 C CA  . ALA B 135 ? 0.5792 0.2473 0.5490 -0.0325 -0.0429 -0.0642 152 ALA B CA  
1948 C C   . ALA B 135 ? 0.4742 0.2171 0.4838 -0.0586 -0.0299 -0.0619 152 ALA B C   
1949 O O   . ALA B 135 ? 0.5053 0.2556 0.5297 -0.0857 -0.0319 -0.0685 152 ALA B O   
1950 C CB  . ALA B 135 ? 0.6012 0.2099 0.5412 -0.0481 -0.0419 -0.0376 152 ALA B CB  
1951 N N   . LEU B 136 ? 0.4603 0.2568 0.4846 -0.0491 -0.0188 -0.0535 153 LEU B N   
1952 C CA  . LEU B 136 ? 0.4203 0.2802 0.4754 -0.0645 -0.0067 -0.0521 153 LEU B CA  
1953 C C   . LEU B 136 ? 0.3869 0.2805 0.4622 -0.0593 -0.0115 -0.0728 153 LEU B C   
1954 O O   . LEU B 136 ? 0.3532 0.2771 0.4494 -0.0781 -0.0093 -0.0751 153 LEU B O   
1955 C CB  . LEU B 136 ? 0.3616 0.2539 0.4155 -0.0509 0.0026  -0.0431 153 LEU B CB  
1956 C CG  . LEU B 136 ? 0.3690 0.3147 0.4434 -0.0569 0.0153  -0.0418 153 LEU B CG  
1957 C CD1 . LEU B 136 ? 0.3508 0.2994 0.4057 -0.0497 0.0242  -0.0295 153 LEU B CD1 
1958 C CD2 . LEU B 136 ? 0.3573 0.3370 0.4488 -0.0457 0.0120  -0.0573 153 LEU B CD2 
1959 N N   . LEU B 137 ? 0.3592 0.2544 0.4283 -0.0323 -0.0179 -0.0865 154 LEU B N   
1960 C CA  . LEU B 137 ? 0.3586 0.2845 0.4393 -0.0256 -0.0207 -0.1042 154 LEU B CA  
1961 C C   . LEU B 137 ? 0.4035 0.2959 0.4746 -0.0388 -0.0318 -0.1181 154 LEU B C   
1962 O O   . LEU B 137 ? 0.3459 0.2690 0.4301 -0.0496 -0.0338 -0.1268 154 LEU B O   
1963 C CB  . LEU B 137 ? 0.3442 0.2855 0.4203 0.0055  -0.0225 -0.1132 154 LEU B CB  
1964 C CG  . LEU B 137 ? 0.2996 0.2826 0.3884 0.0117  -0.0158 -0.1021 154 LEU B CG  
1965 C CD1 . LEU B 137 ? 0.3002 0.3033 0.3889 0.0393  -0.0195 -0.1078 154 LEU B CD1 
1966 C CD2 . LEU B 137 ? 0.2989 0.3249 0.4049 -0.0008 -0.0078 -0.0995 154 LEU B CD2 
1967 N N   . ASP B 138 ? 0.4192 0.2430 0.4624 -0.0379 -0.0415 -0.1207 155 ASP B N   
1968 C CA  . ASP B 138 ? 0.4885 0.2637 0.5145 -0.0570 -0.0558 -0.1350 155 ASP B CA  
1969 C C   . ASP B 138 ? 0.4814 0.2849 0.5340 -0.1007 -0.0552 -0.1251 155 ASP B C   
1970 O O   . ASP B 138 ? 0.4801 0.2926 0.5295 -0.1160 -0.0646 -0.1352 155 ASP B O   
1971 C CB  . ASP B 138 ? 0.5323 0.2172 0.5172 -0.0527 -0.0646 -0.1322 155 ASP B CB  
1972 C CG  . ASP B 138 ? 0.6361 0.2969 0.5915 -0.0051 -0.0674 -0.1466 155 ASP B CG  
1973 O OD1 . ASP B 138 ? 0.6193 0.3311 0.5852 0.0194  -0.0642 -0.1612 155 ASP B OD1 
1974 O OD2 . ASP B 138 ? 0.6883 0.2851 0.6116 0.0084  -0.0717 -0.1412 155 ASP B OD2 
1975 N N   . ARG B 139 ? 0.4584 0.2855 0.5295 -0.1172 -0.0418 -0.1003 156 ARG B N   
1976 C CA  . ARG B 139 ? 0.4367 0.3079 0.5394 -0.1545 -0.0378 -0.0882 156 ARG B CA  
1977 C C   . ARG B 139 ? 0.3382 0.2883 0.4719 -0.1466 -0.0341 -0.0954 156 ARG B C   
1978 O O   . ARG B 139 ? 0.3615 0.3419 0.5072 -0.1636 -0.0439 -0.0954 156 ARG B O   
1979 C CB  . ARG B 139 ? 0.4661 0.3492 0.5760 -0.1663 -0.0201 -0.0596 156 ARG B CB  
1980 C CG  . ARG B 139 ? 0.5040 0.4404 0.6488 -0.2035 -0.0133 -0.0431 156 ARG B CG  
1981 C CD  . ARG B 139 ? 0.4612 0.4259 0.6112 -0.2052 0.0105  -0.0168 156 ARG B CD  
1982 N NE  . ARG B 139 ? 0.4429 0.4574 0.6008 -0.1703 0.0234  -0.0195 156 ARG B NE  
1983 C CZ  . ARG B 139 ? 0.4888 0.4851 0.6215 -0.1446 0.0323  -0.0142 156 ARG B CZ  
1984 N NH1 . ARG B 139 ? 0.6032 0.5394 0.7024 -0.1439 0.0301  -0.0048 156 ARG B NH1 
1985 N NH2 . ARG B 139 ? 0.3542 0.3892 0.4916 -0.1192 0.0412  -0.0183 156 ARG B NH2 
1986 N N   . TYR B 140 ? 0.3741 0.3547 0.5102 -0.1161 -0.0228 -0.0941 157 TYR B N   
1987 C CA  . TYR B 140 ? 0.3143 0.3579 0.4720 -0.1063 -0.0187 -0.0969 157 TYR B CA  
1988 C C   . TYR B 140 ? 0.3499 0.3978 0.5017 -0.1031 -0.0342 -0.1179 157 TYR B C   
1989 O O   . TYR B 140 ? 0.2866 0.3783 0.4520 -0.1072 -0.0381 -0.1160 157 TYR B O   
1990 C CB  . TYR B 140 ? 0.2378 0.2935 0.3893 -0.0788 -0.0067 -0.0919 157 TYR B CB  
1991 C CG  . TYR B 140 ? 0.2563 0.3609 0.4211 -0.0676 -0.0019 -0.0909 157 TYR B CG  
1992 C CD1 . TYR B 140 ? 0.2623 0.3772 0.4201 -0.0549 -0.0084 -0.1026 157 TYR B CD1 
1993 C CD2 . TYR B 140 ? 0.2182 0.3550 0.3969 -0.0663 0.0098  -0.0774 157 TYR B CD2 
1994 C CE1 . TYR B 140 ? 0.2150 0.3645 0.3778 -0.0444 -0.0051 -0.0985 157 TYR B CE1 
1995 C CE2 . TYR B 140 ? 0.1838 0.3532 0.3673 -0.0509 0.0124  -0.0760 157 TYR B CE2 
1996 C CZ  . TYR B 140 ? 0.2257 0.3976 0.4004 -0.0417 0.0041  -0.0853 157 TYR B CZ  
1997 O OH  . TYR B 140 ? 0.1880 0.3830 0.3608 -0.0264 0.0058  -0.0806 157 TYR B OH  
1998 N N   . PHE B 141 ? 0.3811 0.3831 0.5038 -0.0885 -0.0424 -0.1341 158 PHE B N   
1999 C CA  . PHE B 141 ? 0.3875 0.3903 0.4920 -0.0776 -0.0540 -0.1537 158 PHE B CA  
2000 C C   . PHE B 141 ? 0.4876 0.4439 0.5671 -0.0973 -0.0717 -0.1615 158 PHE B C   
2001 O O   . PHE B 141 ? 0.5662 0.5069 0.6174 -0.0864 -0.0819 -0.1795 158 PHE B O   
2002 C CB  . PHE B 141 ? 0.4139 0.4043 0.4975 -0.0438 -0.0491 -0.1652 158 PHE B CB  
2003 C CG  . PHE B 141 ? 0.3664 0.4072 0.4656 -0.0285 -0.0338 -0.1520 158 PHE B CG  
2004 C CD1 . PHE B 141 ? 0.3385 0.4232 0.4418 -0.0244 -0.0324 -0.1525 158 PHE B CD1 
2005 C CD2 . PHE B 141 ? 0.3201 0.3591 0.4258 -0.0213 -0.0232 -0.1378 158 PHE B CD2 
2006 C CE1 . PHE B 141 ? 0.3113 0.4284 0.4228 -0.0148 -0.0197 -0.1384 158 PHE B CE1 
2007 C CE2 . PHE B 141 ? 0.3228 0.3985 0.4386 -0.0138 -0.0126 -0.1265 158 PHE B CE2 
2008 C CZ  . PHE B 141 ? 0.2950 0.4054 0.4130 -0.0118 -0.0104 -0.1263 158 PHE B CZ  
2009 N N   . GLU B 142 ? 0.6175 0.5509 0.7029 -0.1282 -0.0751 -0.1474 159 GLU B N   
2010 C CA  . GLU B 142 ? 0.6478 0.5347 0.7076 -0.1587 -0.0936 -0.1514 159 GLU B CA  
2011 C C   . GLU B 142 ? 0.8158 0.6258 0.8223 -0.1424 -0.0981 -0.1746 159 GLU B C   
2012 O O   . GLU B 142 ? 0.9054 0.6590 0.8949 -0.1348 -0.0915 -0.1738 159 GLU B O   
2013 C CB  . GLU B 142 ? 0.7271 0.6652 0.8035 -0.1744 -0.1084 -0.1529 159 GLU B CB  
2014 C CG  . GLU B 142 ? 0.8070 0.8031 0.9372 -0.2010 -0.1099 -0.1283 159 GLU B CG  
2015 C CD  . GLU B 142 ? 0.7028 0.7733 0.8694 -0.1817 -0.0860 -0.1145 159 GLU B CD  
2016 O OE1 . GLU B 142 ? 0.7671 0.8709 0.9318 -0.1562 -0.0821 -0.1235 159 GLU B OE1 
2017 O OE2 . GLU B 142 ? 0.6843 0.7759 0.8778 -0.1908 -0.0714 -0.0941 159 GLU B OE2 
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