data_7I5T
# 
_entry.id   7I5T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I5T         pdb_00007i5t 10.2210/pdb7i5t/pdb 
WWPDB D_1001408352 ?            ?                   
# 
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 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I5T 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                                            15892.732 2   3.4.22.29 
? ? ? 
2 non-polymer syn '(3S)-1-[(4S)-6,7-dihydro-4H-thieno[3,2-c]thiopyran-4-carbonyl]piperidine-3-carboxamide' 310.435   2   ?         
? ? ? 
3 non-polymer syn 'ZINC ION'                                                                               65.409    2   ?         
? ? ? 
4 water       nat water                                                                                    18.015    287 ?         
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_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       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(4S)-6,7-dihydro-4H-thieno[3,2-c]thiopyran-4-carbonyl]piperidine-3-carboxamide' A1B4A 
3 'ZINC ION'                                                                               ZN    
4 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   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN 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                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B4A non-polymer         . '(3S)-1-[(4S)-6,7-dihydro-4H-thieno[3,2-c]thiopyran-4-carbonyl]piperidine-3-carboxamide' ? 
'C14 H18 N2 O2 S2' 310.435 
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 
ZN    non-polymer         . 'ZINC ION'                                                                               ? 'Zn 2' 
65.409  
# 
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   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 ?   ?   ?   A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 ?   ?   ?   C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B4A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4A 
_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 A1B4A 1   201 201 A1B4A LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 2 A1B4A 1   201 201 A1B4A LIG C . 
F 3 ZN    1   202 1   ZN    ZN  C . 
G 4 HOH   1   301 163 HOH   HOH A . 
G 4 HOH   2   302 95  HOH   HOH A . 
G 4 HOH   3   303 165 HOH   HOH A . 
G 4 HOH   4   304 245 HOH   HOH A . 
G 4 HOH   5   305 61  HOH   HOH A . 
G 4 HOH   6   306 84  HOH   HOH A . 
G 4 HOH   7   307 176 HOH   HOH A . 
G 4 HOH   8   308 103 HOH   HOH A . 
G 4 HOH   9   309 66  HOH   HOH A . 
G 4 HOH   10  310 116 HOH   HOH A . 
G 4 HOH   11  311 285 HOH   HOH A . 
G 4 HOH   12  312 272 HOH   HOH A . 
G 4 HOH   13  313 190 HOH   HOH A . 
G 4 HOH   14  314 93  HOH   HOH A . 
G 4 HOH   15  315 227 HOH   HOH A . 
G 4 HOH   16  316 5   HOH   HOH A . 
G 4 HOH   17  317 23  HOH   HOH A . 
G 4 HOH   18  318 140 HOH   HOH A . 
G 4 HOH   19  319 13  HOH   HOH A . 
G 4 HOH   20  320 48  HOH   HOH A . 
G 4 HOH   21  321 183 HOH   HOH A . 
G 4 HOH   22  322 14  HOH   HOH A . 
G 4 HOH   23  323 70  HOH   HOH A . 
G 4 HOH   24  324 59  HOH   HOH A . 
G 4 HOH   25  325 60  HOH   HOH A . 
G 4 HOH   26  326 236 HOH   HOH A . 
G 4 HOH   27  327 63  HOH   HOH A . 
G 4 HOH   28  328 72  HOH   HOH A . 
G 4 HOH   29  329 171 HOH   HOH A . 
G 4 HOH   30  330 49  HOH   HOH A . 
G 4 HOH   31  331 56  HOH   HOH A . 
G 4 HOH   32  332 7   HOH   HOH A . 
G 4 HOH   33  333 147 HOH   HOH A . 
G 4 HOH   34  334 62  HOH   HOH A . 
G 4 HOH   35  335 230 HOH   HOH A . 
G 4 HOH   36  336 33  HOH   HOH A . 
G 4 HOH   37  337 22  HOH   HOH A . 
G 4 HOH   38  338 243 HOH   HOH A . 
G 4 HOH   39  339 302 HOH   HOH A . 
G 4 HOH   40  340 281 HOH   HOH A . 
G 4 HOH   41  341 254 HOH   HOH A . 
G 4 HOH   42  342 99  HOH   HOH A . 
G 4 HOH   43  343 107 HOH   HOH A . 
G 4 HOH   44  344 85  HOH   HOH A . 
G 4 HOH   45  345 19  HOH   HOH A . 
G 4 HOH   46  346 63  HOH   HOH A . 
G 4 HOH   47  347 88  HOH   HOH A . 
G 4 HOH   48  348 234 HOH   HOH A . 
G 4 HOH   49  349 38  HOH   HOH A . 
G 4 HOH   50  350 128 HOH   HOH A . 
G 4 HOH   51  351 71  HOH   HOH A . 
G 4 HOH   52  352 154 HOH   HOH A . 
G 4 HOH   53  353 273 HOH   HOH A . 
G 4 HOH   54  354 266 HOH   HOH A . 
G 4 HOH   55  355 61  HOH   HOH A . 
G 4 HOH   56  356 66  HOH   HOH A . 
G 4 HOH   57  357 10  HOH   HOH A . 
G 4 HOH   58  358 229 HOH   HOH A . 
G 4 HOH   59  359 261 HOH   HOH A . 
G 4 HOH   60  360 278 HOH   HOH A . 
G 4 HOH   61  361 168 HOH   HOH A . 
G 4 HOH   62  362 53  HOH   HOH A . 
G 4 HOH   63  363 149 HOH   HOH A . 
G 4 HOH   64  364 115 HOH   HOH A . 
G 4 HOH   65  365 119 HOH   HOH A . 
G 4 HOH   66  366 102 HOH   HOH A . 
G 4 HOH   67  367 26  HOH   HOH A . 
G 4 HOH   68  368 244 HOH   HOH A . 
G 4 HOH   69  369 73  HOH   HOH A . 
G 4 HOH   70  370 14  HOH   HOH A . 
G 4 HOH   71  371 29  HOH   HOH A . 
G 4 HOH   72  372 19  HOH   HOH A . 
G 4 HOH   73  373 101 HOH   HOH A . 
G 4 HOH   74  374 23  HOH   HOH A . 
G 4 HOH   75  375 125 HOH   HOH A . 
G 4 HOH   76  376 250 HOH   HOH A . 
G 4 HOH   77  377 21  HOH   HOH A . 
G 4 HOH   78  378 197 HOH   HOH A . 
G 4 HOH   79  379 115 HOH   HOH A . 
G 4 HOH   80  380 150 HOH   HOH A . 
G 4 HOH   81  381 89  HOH   HOH A . 
G 4 HOH   82  382 146 HOH   HOH A . 
G 4 HOH   83  383 239 HOH   HOH A . 
G 4 HOH   84  384 259 HOH   HOH A . 
G 4 HOH   85  385 96  HOH   HOH A . 
G 4 HOH   86  386 113 HOH   HOH A . 
G 4 HOH   87  387 75  HOH   HOH A . 
G 4 HOH   88  388 277 HOH   HOH A . 
G 4 HOH   89  389 275 HOH   HOH A . 
G 4 HOH   90  390 235 HOH   HOH A . 
G 4 HOH   91  391 297 HOH   HOH A . 
G 4 HOH   92  392 256 HOH   HOH A . 
G 4 HOH   93  393 112 HOH   HOH A . 
G 4 HOH   94  394 247 HOH   HOH A . 
G 4 HOH   95  395 156 HOH   HOH A . 
G 4 HOH   96  396 111 HOH   HOH A . 
G 4 HOH   97  397 35  HOH   HOH A . 
G 4 HOH   98  398 12  HOH   HOH A . 
G 4 HOH   99  399 265 HOH   HOH A . 
G 4 HOH   100 400 202 HOH   HOH A . 
G 4 HOH   101 401 12  HOH   HOH A . 
G 4 HOH   102 402 91  HOH   HOH A . 
G 4 HOH   103 403 155 HOH   HOH A . 
G 4 HOH   104 404 47  HOH   HOH A . 
G 4 HOH   105 405 92  HOH   HOH A . 
G 4 HOH   106 406 237 HOH   HOH A . 
G 4 HOH   107 407 40  HOH   HOH A . 
G 4 HOH   108 408 102 HOH   HOH A . 
G 4 HOH   109 409 49  HOH   HOH A . 
G 4 HOH   110 410 269 HOH   HOH A . 
G 4 HOH   111 411 16  HOH   HOH A . 
G 4 HOH   112 412 52  HOH   HOH A . 
G 4 HOH   113 413 160 HOH   HOH A . 
G 4 HOH   114 414 282 HOH   HOH A . 
G 4 HOH   115 415 157 HOH   HOH A . 
G 4 HOH   116 416 143 HOH   HOH A . 
G 4 HOH   117 417 77  HOH   HOH A . 
G 4 HOH   118 418 208 HOH   HOH A . 
G 4 HOH   119 419 15  HOH   HOH A . 
G 4 HOH   120 420 100 HOH   HOH A . 
G 4 HOH   121 421 140 HOH   HOH A . 
G 4 HOH   122 422 53  HOH   HOH A . 
G 4 HOH   123 423 311 HOH   HOH A . 
G 4 HOH   124 424 154 HOH   HOH A . 
G 4 HOH   125 425 136 HOH   HOH A . 
G 4 HOH   126 426 157 HOH   HOH A . 
G 4 HOH   127 427 166 HOH   HOH A . 
G 4 HOH   128 428 126 HOH   HOH A . 
G 4 HOH   129 429 167 HOH   HOH A . 
G 4 HOH   130 430 138 HOH   HOH A . 
G 4 HOH   131 431 263 HOH   HOH A . 
G 4 HOH   132 432 24  HOH   HOH A . 
G 4 HOH   133 433 293 HOH   HOH A . 
G 4 HOH   134 434 187 HOH   HOH A . 
G 4 HOH   135 435 82  HOH   HOH A . 
G 4 HOH   136 436 289 HOH   HOH A . 
G 4 HOH   137 437 283 HOH   HOH A . 
G 4 HOH   138 438 222 HOH   HOH A . 
G 4 HOH   139 439 99  HOH   HOH A . 
H 4 HOH   1   301 148 HOH   HOH C . 
H 4 HOH   2   302 34  HOH   HOH C . 
H 4 HOH   3   303 151 HOH   HOH C . 
H 4 HOH   4   304 271 HOH   HOH C . 
H 4 HOH   5   305 64  HOH   HOH C . 
H 4 HOH   6   306 8   HOH   HOH C . 
H 4 HOH   7   307 137 HOH   HOH C . 
H 4 HOH   8   308 309 HOH   HOH C . 
H 4 HOH   9   309 286 HOH   HOH C . 
H 4 HOH   10  310 103 HOH   HOH C . 
H 4 HOH   11  311 155 HOH   HOH C . 
H 4 HOH   12  312 174 HOH   HOH C . 
H 4 HOH   13  313 298 HOH   HOH C . 
H 4 HOH   14  314 248 HOH   HOH C . 
H 4 HOH   15  315 251 HOH   HOH C . 
H 4 HOH   16  316 162 HOH   HOH C . 
H 4 HOH   17  317 228 HOH   HOH C . 
H 4 HOH   18  318 280 HOH   HOH C . 
H 4 HOH   19  319 111 HOH   HOH C . 
H 4 HOH   20  320 64  HOH   HOH C . 
H 4 HOH   21  321 290 HOH   HOH C . 
H 4 HOH   22  322 33  HOH   HOH C . 
H 4 HOH   23  323 80  HOH   HOH C . 
H 4 HOH   24  324 2   HOH   HOH C . 
H 4 HOH   25  325 83  HOH   HOH C . 
H 4 HOH   26  326 51  HOH   HOH C . 
H 4 HOH   27  327 262 HOH   HOH C . 
H 4 HOH   28  328 210 HOH   HOH C . 
H 4 HOH   29  329 28  HOH   HOH C . 
H 4 HOH   30  330 109 HOH   HOH C . 
H 4 HOH   31  331 43  HOH   HOH C . 
H 4 HOH   32  332 255 HOH   HOH C . 
H 4 HOH   33  333 124 HOH   HOH C . 
H 4 HOH   34  334 78  HOH   HOH C . 
H 4 HOH   35  335 270 HOH   HOH C . 
H 4 HOH   36  336 69  HOH   HOH C . 
H 4 HOH   37  337 50  HOH   HOH C . 
H 4 HOH   38  338 279 HOH   HOH C . 
H 4 HOH   39  339 296 HOH   HOH C . 
H 4 HOH   40  340 130 HOH   HOH C . 
H 4 HOH   41  341 39  HOH   HOH C . 
H 4 HOH   42  342 20  HOH   HOH C . 
H 4 HOH   43  343 233 HOH   HOH C . 
H 4 HOH   44  344 306 HOH   HOH C . 
H 4 HOH   45  345 153 HOH   HOH C . 
H 4 HOH   46  346 144 HOH   HOH C . 
H 4 HOH   47  347 65  HOH   HOH C . 
H 4 HOH   48  348 204 HOH   HOH C . 
H 4 HOH   49  349 67  HOH   HOH C . 
H 4 HOH   50  350 98  HOH   HOH C . 
H 4 HOH   51  351 98  HOH   HOH C . 
H 4 HOH   52  352 30  HOH   HOH C . 
H 4 HOH   53  353 301 HOH   HOH C . 
H 4 HOH   54  354 38  HOH   HOH C . 
H 4 HOH   55  355 307 HOH   HOH C . 
H 4 HOH   56  356 13  HOH   HOH C . 
H 4 HOH   57  357 122 HOH   HOH C . 
H 4 HOH   58  358 308 HOH   HOH C . 
H 4 HOH   59  359 135 HOH   HOH C . 
H 4 HOH   60  360 6   HOH   HOH C . 
H 4 HOH   61  361 241 HOH   HOH C . 
H 4 HOH   62  362 126 HOH   HOH C . 
H 4 HOH   63  363 54  HOH   HOH C . 
H 4 HOH   64  364 292 HOH   HOH C . 
H 4 HOH   65  365 303 HOH   HOH C . 
H 4 HOH   66  366 4   HOH   HOH C . 
H 4 HOH   67  367 294 HOH   HOH C . 
H 4 HOH   68  368 264 HOH   HOH C . 
H 4 HOH   69  369 249 HOH   HOH C . 
H 4 HOH   70  370 7   HOH   HOH C . 
H 4 HOH   71  371 268 HOH   HOH C . 
H 4 HOH   72  372 123 HOH   HOH C . 
H 4 HOH   73  373 232 HOH   HOH C . 
H 4 HOH   74  374 231 HOH   HOH C . 
H 4 HOH   75  375 110 HOH   HOH C . 
H 4 HOH   76  376 71  HOH   HOH C . 
H 4 HOH   77  377 62  HOH   HOH C . 
H 4 HOH   78  378 276 HOH   HOH C . 
H 4 HOH   79  379 246 HOH   HOH C . 
H 4 HOH   80  380 45  HOH   HOH C . 
H 4 HOH   81  381 85  HOH   HOH C . 
H 4 HOH   82  382 252 HOH   HOH C . 
H 4 HOH   83  383 260 HOH   HOH C . 
H 4 HOH   84  384 87  HOH   HOH C . 
H 4 HOH   85  385 310 HOH   HOH C . 
H 4 HOH   86  386 118 HOH   HOH C . 
H 4 HOH   87  387 145 HOH   HOH C . 
H 4 HOH   88  388 29  HOH   HOH C . 
H 4 HOH   89  389 37  HOH   HOH C . 
H 4 HOH   90  390 148 HOH   HOH C . 
H 4 HOH   91  391 91  HOH   HOH C . 
H 4 HOH   92  392 83  HOH   HOH C . 
H 4 HOH   93  393 253 HOH   HOH C . 
H 4 HOH   94  394 11  HOH   HOH C . 
H 4 HOH   95  395 79  HOH   HOH C . 
H 4 HOH   96  396 78  HOH   HOH C . 
H 4 HOH   97  397 288 HOH   HOH C . 
H 4 HOH   98  398 242 HOH   HOH C . 
H 4 HOH   99  399 205 HOH   HOH C . 
H 4 HOH   100 400 70  HOH   HOH C . 
H 4 HOH   101 401 31  HOH   HOH C . 
H 4 HOH   102 402 54  HOH   HOH C . 
H 4 HOH   103 403 68  HOH   HOH C . 
H 4 HOH   104 404 16  HOH   HOH C . 
H 4 HOH   105 405 146 HOH   HOH C . 
H 4 HOH   106 406 149 HOH   HOH C . 
H 4 HOH   107 407 50  HOH   HOH C . 
H 4 HOH   108 408 41  HOH   HOH C . 
H 4 HOH   109 409 258 HOH   HOH C . 
H 4 HOH   110 410 1   HOH   HOH C . 
H 4 HOH   111 411 52  HOH   HOH C . 
H 4 HOH   112 412 3   HOH   HOH C . 
H 4 HOH   113 413 284 HOH   HOH C . 
H 4 HOH   114 414 240 HOH   HOH C . 
H 4 HOH   115 415 274 HOH   HOH C . 
H 4 HOH   116 416 124 HOH   HOH C . 
H 4 HOH   117 417 47  HOH   HOH C . 
H 4 HOH   118 418 44  HOH   HOH C . 
H 4 HOH   119 419 81  HOH   HOH C . 
H 4 HOH   120 420 238 HOH   HOH C . 
H 4 HOH   121 421 267 HOH   HOH C . 
H 4 HOH   122 422 150 HOH   HOH C . 
H 4 HOH   123 423 95  HOH   HOH C . 
H 4 HOH   124 424 90  HOH   HOH C . 
H 4 HOH   125 425 164 HOH   HOH C . 
H 4 HOH   126 426 117 HOH   HOH C . 
H 4 HOH   127 427 116 HOH   HOH C . 
H 4 HOH   128 428 41  HOH   HOH C . 
H 4 HOH   129 429 158 HOH   HOH C . 
H 4 HOH   130 430 299 HOH   HOH C . 
H 4 HOH   131 431 27  HOH   HOH C . 
H 4 HOH   132 432 185 HOH   HOH C . 
H 4 HOH   133 433 304 HOH   HOH C . 
H 4 HOH   134 434 9   HOH   HOH C . 
H 4 HOH   135 435 198 HOH   HOH C . 
H 4 HOH   136 436 287 HOH   HOH C . 
H 4 HOH   137 437 93  HOH   HOH C . 
H 4 HOH   138 438 132 HOH   HOH C . 
H 4 HOH   139 439 159 HOH   HOH C . 
H 4 HOH   140 440 161 HOH   HOH C . 
H 4 HOH   141 441 123 HOH   HOH C . 
H 4 HOH   142 442 199 HOH   HOH C . 
H 4 HOH   143 443 291 HOH   HOH C . 
H 4 HOH   144 444 142 HOH   HOH C . 
H 4 HOH   145 445 218 HOH   HOH C . 
H 4 HOH   146 446 152 HOH   HOH C . 
H 4 HOH   147 447 141 HOH   HOH C . 
H 4 HOH   148 448 196 HOH   HOH C . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I5T 
_cell.length_a           72.556 
_cell.length_b           61.719 
_cell.length_c           65.280 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.83 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5T 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7I5T 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.44 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92202 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I5T 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             65.200 
_reflns.d_resolution_high            1.194 
_reflns.number_obs                   69421 
_reflns.percent_possible_obs         76.3 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_netI_over_sigmaI        13.1 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.070 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_number_measured_all     395979 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.194 
_reflns_shell.d_res_low                   1.304 
_reflns_shell.number_measured_all         8271 
_reflns_shell.number_unique_obs           3471 
_reflns_shell.Rmerge_I_obs                0.556 
_reflns_shell.pdbx_redundancy             2.4 
_reflns_shell.percent_possible_obs        16.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.4 
_reflns_shell.pdbx_Rrim_I_all             0.712 
_reflns_shell.pdbx_Rpim_I_all             0.434 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I5T 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     69421 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             65.20 
_refine.ls_d_res_high                            1.194 
_refine.ls_percent_reflns_obs                    76.2 
_refine.ls_R_factor_obs                          0.1820 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1812 
_refine.ls_R_factor_R_free                       0.1991 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.890 
_refine.ls_number_reflns_R_free                  3396 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               15.56 
_refine.aniso_B[1][1]                            -0.03660 
_refine.aniso_B[2][2]                            -0.46570 
_refine.aniso_B[3][3]                            0.50230 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.22000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.048 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.049 
_refine.pdbx_overall_SU_R_Blow_DPI               0.050 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.050 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5T 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2130 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             287 
_refine_hist.number_atoms_total               2459 
_refine_hist.d_res_high                       1.194 
_refine_hist.d_res_low                        65.20 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.013 ? 2.00  2234 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.13  ? 2.00  3044 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  752  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  400  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2234 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.07  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           13.61 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1946 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.19 
_refine_ls_shell.d_res_low                        1.26 
_refine_ls_shell.number_reflns_R_work             1316 
_refine_ls_shell.R_factor_R_work                  0.2619 
_refine_ls_shell.percent_reflns_obs               9.65 
_refine_ls_shell.R_factor_R_free                  0.2639 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.26 
_refine_ls_shell.number_reflns_R_free             73 
_refine_ls_shell.number_reflns_all                1389 
_refine_ls_shell.R_factor_all                     0.2620 
# 
_struct.entry_id                  7I5T 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0036525-001 (A71EV2A-x4877)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5T 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
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 7I5T A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I5T C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 LEU B 134 ? ASP B 138 ? LEU C 140 ASP C 144 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.2 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.0 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.7 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.6 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 112.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.5 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.9 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.8 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.7 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
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 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I5T 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 19.7138 6.7562   18.1134 -0.0134 -0.0211 -0.0027 -0.0004 0.0052  -0.0015 0.6811 0.9508 0.2806 
-0.2511 -0.2208 -0.0073 -0.0086 -0.0030 0.0791 0.0422 0.0222 0.0429  0.0321  0.0307  -0.0136 
'X-RAY DIFFRACTION' 2 ? refined 15.1846 -23.9446 14.2917 -0.0109 -0.0156 -0.0031 0.0002  -0.0030 -0.0032 0.4269 0.8395 0.3597 
0.1899  0.0111  0.0931  -0.0100 0.0153  0.0384 0.0184 0.0225 -0.0443 -0.0037 -0.0069 -0.0125 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
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 GLU 145 ? A GLU 139 
2  1 Y 1 A GLU 146 ? A GLU 140 
3  1 Y 1 A ALA 147 ? A ALA 141 
4  1 Y 1 A MET 148 ? A MET 142 
5  1 Y 1 A GLU 149 ? A GLU 143 
6  1 Y 1 A GLN 150 ? A GLN 144 
7  1 Y 1 C GLU 145 ? B GLU 139 
8  1 Y 1 C GLU 146 ? B GLU 140 
9  1 Y 1 C ALA 147 ? B ALA 141 
10 1 Y 1 C MET 148 ? B MET 142 
11 1 Y 1 C GLU 149 ? B GLU 143 
12 1 Y 1 C GLN 150 ? B GLN 144 
# 
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 
A1B4A N1   N  N N 1   
A1B4A C4   C  N N 2   
A1B4A C5   C  N N 3   
A1B4A C6   C  N S 4   
A1B4A C7   C  N N 5   
A1B4A C8   C  N N 6   
A1B4A C10  C  Y N 7   
A1B4A C13  C  N N 8   
A1B4A O1   O  N N 9   
A1B4A C3   C  N N 10  
A1B4A C2   C  N N 11  
A1B4A C1   C  N S 12  
A1B4A C    C  N N 13  
A1B4A O    O  N N 14  
A1B4A N    N  N N 15  
A1B4A C12  C  Y N 16  
A1B4A C11  C  Y N 17  
A1B4A S1   S  Y N 18  
A1B4A C9   C  Y N 19  
A1B4A S    S  N N 20  
A1B4A H9   H  N N 21  
A1B4A H8   H  N N 22  
A1B4A H1   H  N N 23  
A1B4A H10  H  N N 24  
A1B4A H11  H  N N 25  
A1B4A H13  H  N N 26  
A1B4A H12  H  N N 27  
A1B4A H14  H  N N 28  
A1B4A H17  H  N N 29  
A1B4A H16  H  N N 30  
A1B4A H7   H  N N 31  
A1B4A H6   H  N N 32  
A1B4A H5   H  N N 33  
A1B4A H4   H  N N 34  
A1B4A H    H  N N 35  
A1B4A H3   H  N N 36  
A1B4A H2   H  N N 37  
A1B4A H15  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
ZN    ZN   ZN N N 429 
# 
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 
A1B4A N   C    sing N N 1   
A1B4A O   C    doub N N 2   
A1B4A C   C1   sing N N 3   
A1B4A C1  C2   sing N N 4   
A1B4A C2  C3   sing N N 5   
A1B4A C3  C4   sing N N 6   
A1B4A C4  N1   sing N N 7   
A1B4A N1  C5   sing N N 8   
A1B4A C5  O1   doub N N 9   
A1B4A C6  C5   sing N N 10  
A1B4A C6  S    sing N N 11  
A1B4A S   C7   sing N N 12  
A1B4A C7  C8   sing N N 13  
A1B4A C8  C9   sing N N 14  
A1B4A C9  S1   sing Y N 15  
A1B4A S1  C10  sing Y N 16  
A1B4A C10 C11  doub Y N 17  
A1B4A C11 C12  sing Y N 18  
A1B4A C9  C12  doub Y N 19  
A1B4A C12 C6   sing N N 20  
A1B4A C13 N1   sing N N 21  
A1B4A C1  C13  sing N N 22  
A1B4A C4  H9   sing N N 23  
A1B4A C4  H8   sing N N 24  
A1B4A C6  H1   sing N N 25  
A1B4A C7  H10  sing N N 26  
A1B4A C7  H11  sing N N 27  
A1B4A C8  H13  sing N N 28  
A1B4A C8  H12  sing N N 29  
A1B4A C10 H14  sing N N 30  
A1B4A C13 H17  sing N N 31  
A1B4A C13 H16  sing N N 32  
A1B4A C3  H7   sing N N 33  
A1B4A C3  H6   sing N N 34  
A1B4A C2  H5   sing N N 35  
A1B4A C2  H4   sing N N 36  
A1B4A C1  H    sing N N 37  
A1B4A N   H3   sing N N 38  
A1B4A N   H2   sing N N 39  
A1B4A C11 H15  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_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   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I5T 
_atom_sites.fract_transf_matrix[1][1]   0.013782 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000681 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016202 
_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]   0.015337 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . SER   A 1 1   ? 16.422 6.463   8.102  1.00 14.13 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.184 6.625   8.885  1.00 13.39 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.010 5.472   9.850  1.00 13.47 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.611 4.413   9.652  1.00 14.81 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.984 6.708   7.925  1.00 16.80 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.807 5.483   7.233  1.00 20.78 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.189 5.655   10.883 1.00 12.57 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.843 4.578   11.804 1.00 11.55 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.463 5.093   13.179 1.00 10.84 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.822 6.226   13.535 1.00 12.76 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.731 4.302   13.961 1.00 10.04 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.296 4.742   15.280 1.00 10.67 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.245 3.544   16.205 1.00 10.38 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.195 2.376   15.740 1.00 11.99 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.874 5.347   15.178 1.00 12.51 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.223 3.808   17.533 1.00 9.23  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 11.969 2.787   18.564 1.00 10.09 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.544 3.002   19.051 1.00 10.12 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.180 4.137   19.349 1.00 10.51 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 12.928 2.948   19.759 1.00 9.83  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.397 2.903   19.285 1.00 9.79  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.674 1.874   20.817 1.00 12.35 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.367 3.471   20.356 1.00 11.57 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.761  1.925   19.153 1.00 10.77 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.396  2.032   19.672 1.00 12.22 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.290  1.277   20.968 1.00 11.98 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.345  0.063   20.936 1.00 13.20 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.393  1.480   18.654 1.00 12.77 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.335  2.309   17.407 1.00 13.80 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.531  3.436   17.342 1.00 15.28 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.137  2.016   16.315 1.00 15.99 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.497  4.233   16.207 1.00 16.35 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.105  2.792   15.168 1.00 17.32 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.279  3.896   15.115 1.00 17.08 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.308  4.728   14.022 1.00 19.74 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.240  1.946   22.120 1.00 12.13 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.192  1.293   23.430 1.00 12.93 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.040  1.869   24.221 1.00 13.78 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 6.936  3.088   24.340 1.00 13.40 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.564  1.410   24.182 1.00 15.39 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.056 2.871   24.252 1.00 16.01 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.448  0.807   25.593 1.00 17.71 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.090  1.032   24.649 1.00 15.22 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 4.939  1.512   25.401 1.00 15.36 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.159  2.527   24.580 1.00 15.04 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 3.946  2.281   23.400 1.00 16.62 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.854  3.706   25.150 1.00 15.72 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.176  4.728   24.349 1.00 15.61 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.132  5.811   23.902 1.00 13.48 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.742  6.979   23.759 1.00 15.07 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 1.949  5.307   25.077 1.00 19.51 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.836  4.309   25.196 1.00 27.47 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.201  3.934   24.204 1.00 30.43 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.609  3.829   26.398 1.00 27.86 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.387  5.421   23.599 1.00 12.55 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.396  6.377   23.142 1.00 11.75 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 6.992  5.948   21.818 1.00 10.82 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.136  4.751   21.539 1.00 11.74 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.553  6.445   24.159 1.00 13.02 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.141  6.971   25.511 1.00 14.00 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.510  8.199   25.636 1.00 14.86 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.396  6.252   26.667 1.00 15.79 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.158  8.713   26.883 1.00 15.69 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.066  6.770   27.921 1.00 16.38 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.410  7.984   28.013 1.00 16.89 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.072  8.536   29.238 1.00 19.73 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.439  6.947   21.025 1.00 10.09 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.157  6.779   19.758 1.00 10.70 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.463  7.585   19.929 1.00 10.44 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.409  8.777   20.270 1.00 10.94 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.316  7.341   18.600 1.00 11.64 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.070  7.560   17.296 1.00 14.01 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.160  7.945   16.131 1.00 15.62 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.757  8.940   15.230 1.00 15.64 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.250  8.705   14.019 1.00 17.60 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.329  7.455   13.553 1.00 17.85 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.751  9.699   13.300 1.00 18.12 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.618 6.909   19.784 1.00 10.67 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.916 7.565   19.919 1.00 9.38  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.512 7.699   18.528 1.00 9.77  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.688 6.674   17.820 1.00 9.71  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.896 6.753   20.810 1.00 10.68 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.160 7.568   21.085 1.00 11.00 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.236 6.254   22.100 1.00 11.78 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.874 8.922   18.128 1.00 8.58  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.438 9.173   16.788 1.00 9.18  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.666 10.082  16.911 1.00 8.21  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.877 10.773  17.929 1.00 9.49  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.385 9.854   15.876 1.00 11.39 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.297 8.878   15.492 1.00 14.85 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.851 11.160  16.489 1.00 12.26 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.444 10.167  15.829 1.00 7.74  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.486 11.212  15.780 1.00 7.88  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.800 12.570  15.774 1.00 8.59  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.858 12.796  14.968 1.00 8.76  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.320 11.120  14.482 1.00 8.14  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.113 9.845   14.409 1.00 8.76  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.666 8.824   13.867 1.00 9.92  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.314 9.877   14.938 1.00 8.80  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.271 13.496  16.629 1.00 7.32  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.596 14.801  16.688 1.00 7.87  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.627 15.504  15.321 1.00 9.10  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.646 16.148  14.941 1.00 9.46  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.261 15.658  17.754 1.00 9.74  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.469 16.974  18.076 1.00 7.97  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.379 17.800  18.976 1.00 10.08 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.745 19.049  19.466 1.00 10.32 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.769 20.201  18.820 1.00 10.60 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.222 20.263  17.570 1.00 10.93 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.281 21.305  19.393 1.00 11.73 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.726 15.332  14.553 1.00 8.09  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.832 16.025  13.263 1.00 8.99  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.892 15.444  12.201 1.00 10.14 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.731 16.087  11.140 1.00 12.58 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.311 16.126  12.771 1.00 10.79 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.904 14.843  12.245 1.00 9.53  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.478 13.880  13.068 1.00 9.71  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 19.036 14.436  10.963 1.00 11.14 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.939 12.909  12.258 1.00 10.14 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.698 13.221  10.977 1.00 10.48 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.305 14.258  12.448 1.00 10.37 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.347 13.624  11.516 1.00 10.63 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.901 13.651  12.038 1.00 12.18 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.997 13.088  11.413 1.00 12.75 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.788 12.197  11.188 1.00 11.22 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.198 12.073  10.547 1.00 10.88 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.574 10.616  10.332 1.00 12.41 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.284 12.836  9.238  1.00 12.63 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.663 14.301  13.187 1.00 11.38 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.307 14.342  13.753 1.00 11.05 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.338 15.025  12.788 1.00 11.02 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.674 16.005  12.148 1.00 12.38 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.330 15.085  15.078 1.00 11.93 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.126  14.500  12.749 1.00 12.00 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.080  15.039  11.851 1.00 13.39 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.258  16.129  12.542 1.00 14.39 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.351  16.312  13.767 1.00 14.67 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.154  13.883  11.414 1.00 15.54 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.410  13.450  12.559 1.00 15.17 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.905  12.736  10.756 1.00 17.02 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.323  16.773  11.774 1.00 15.60 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.415  17.737  12.391 1.00 17.55 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.569  17.030  13.482 1.00 14.71 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.368  17.565  14.580 1.00 16.19 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.436  18.316  11.333 1.00 21.71 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.084  19.089  10.226 1.00 29.33 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.954  20.139  10.480 1.00 32.41 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.943  18.952  8.885  1.00 32.19 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.339  20.583  9.291  1.00 33.67 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.735  19.911  8.299  1.00 33.99 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.133  15.780  13.200 1.00 14.55 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.367  15.038  14.192 1.00 14.30 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.136  14.704  15.447 1.00 14.27 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.593  14.739  16.550 1.00 14.76 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.767  13.784  13.605 1.00 16.31 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.460  14.071  12.979 1.00 24.18 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.636  14.877  13.506 1.00 23.59 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.296  13.478  11.805 1.00 24.94 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.444  14.372  15.307 1.00 12.38 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.278  14.147  16.502 1.00 12.42 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.292  15.393  17.403 1.00 11.30 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.154  15.293  18.629 1.00 11.88 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.719  13.819  16.096 1.00 12.17 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.911  12.422  15.572 1.00 13.84 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.276  11.490  16.121 1.00 14.06 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.663  12.263  14.558 1.00 13.54 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.512  16.565  16.795 1.00 10.52 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.568  17.824  17.555 1.00 11.71 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.206  18.192  18.172 1.00 14.77 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.166  18.686  19.305 1.00 15.88 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.132  18.950  16.682 1.00 11.94 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.638  18.934  16.606 1.00 11.56 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.419  18.506  15.569 1.00 13.10 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.534  19.455  17.595 1.00 11.55 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.752 18.718  15.868 1.00 13.25 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.850 19.236  17.131 1.00 12.82 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.351  20.009  18.858 1.00 12.63 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.983 19.682  17.855 1.00 13.08 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.468 20.385  19.588 1.00 13.41 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.763 20.218  19.095 1.00 14.16 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.116  17.820  17.514 1.00 14.31 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.763  18.114  18.057 1.00 15.61 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.411  17.177  19.221 1.00 16.28 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.481  17.438  20.003 1.00 17.79 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.735  17.938  16.963 1.00 16.58 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.093  16.021  19.323 1.00 14.59 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.872  15.075  20.397 1.00 14.73 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.161  14.919  21.238 1.00 13.87 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.443  13.865  21.776 1.00 13.25 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.454  13.735  19.797 1.00 15.77 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.093  13.807  19.151 1.00 18.45 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.075  13.764  19.848 1.00 21.64 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.039  13.877  17.828 1.00 18.29 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.898  16.008  21.406 1.00 13.14 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.192  16.033  22.094 1.00 12.86 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.130  15.620  23.570 1.00 13.50 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.313  16.148  24.363 1.00 15.89 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.786  17.428  21.971 1.00 12.52 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.138  17.606  22.670 1.00 13.47 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.201  16.789  21.939 1.00 14.26 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.557  19.090  22.617 1.00 14.72 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.030  14.706  23.985 1.00 13.22 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.178  14.318  25.386 1.00 14.41 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.493  14.920  25.915 1.00 15.50 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.535  15.558  26.975 1.00 17.32 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.199  12.777  25.513 1.00 15.48 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.569  12.346  26.935 1.00 17.08 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.830  12.203  25.129 1.00 17.07 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.581  14.769  25.134 1.00 12.84 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.907 15.228  25.578 1.00 13.25 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.812 15.331  24.347 1.00 10.97 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.691 14.498  23.431 1.00 11.73 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.498 14.187  26.579 1.00 13.78 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 12.969 14.354  26.931 1.00 14.44 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.523 15.217  27.846 1.00 16.27 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.066 13.635  26.345 1.00 13.94 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.910 15.093  27.834 1.00 16.85 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.257 14.090  26.958 1.00 14.83 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.153 12.638  25.380 1.00 14.22 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.512 13.563  26.644 1.00 15.29 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.397 12.104  25.075 1.00 15.21 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.557 12.572  25.702 1.00 14.64 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.717 16.273  24.337 1.00 11.34 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.720 16.370  23.263 1.00 11.12 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.018 16.946  23.802 1.00 11.57 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 14.994 17.750  24.740 1.00 12.05 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.214 17.115  22.026 1.00 12.79 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.641 18.514  22.303 1.00 13.30 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.638 19.626  22.599 1.00 14.89 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.289 20.514  23.419 1.00 18.28 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.744 19.643  22.019 1.00 13.19 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.153 16.597  23.178 1.00 10.70 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.444 17.099  23.613 1.00 10.64 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.338 17.235  22.383 1.00 10.68 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.787 16.221  21.808 1.00 10.20 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.018 16.192  24.712 1.00 12.37 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.317 16.661  25.299 1.00 18.45 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.057 17.372  24.603 1.00 20.72 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.609 16.305  26.452 1.00 19.12 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.596 18.471  21.955 1.00 10.45 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.423 18.747  20.797 0.50 11.37 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.441 18.706  20.779 0.50 10.92 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.852 18.221  21.007 1.00 11.13 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.494 17.742  20.041 1.00 11.90 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.423 20.252  20.537 0.50 14.63 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.468 20.180  20.385 0.50 13.01 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.241 20.603  19.439 0.50 19.41 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.113 20.971  21.362 0.50 16.16 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.346 18.307  22.260 1.00 11.18 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.722 17.835  22.498 1.00 11.76 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.831 16.319  22.328 1.00 11.69 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.945 15.854  22.199 1.00 12.63 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.247 18.214  23.880 1.00 14.85 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.648 17.481  24.936 1.00 20.26 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.731 15.570  22.367 1.00 9.92  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.760 14.111  22.191 1.00 9.41  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.224 13.670  20.814 1.00 9.54  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.266 12.477  20.483 1.00 8.75  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.903 13.422  23.266 1.00 10.21 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.475 13.613  24.687 1.00 10.13 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.658 12.966  25.799 1.00 11.25 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.650 11.501  25.650 1.00 10.06 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.435 10.648  26.652 1.00 10.51 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.224 11.099  27.893 1.00 12.95 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.429 9.336   26.427 1.00 10.92 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.676 14.600  20.015 1.00 8.75  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.972 14.263  18.777 1.00 7.94  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.805 13.312  19.018 1.00 8.50  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.530 12.464  18.157 1.00 9.16  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.917 13.716  17.674 1.00 8.99  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.243 13.508  16.320 1.00 9.17  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.444 14.395  15.897 1.00 8.76  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.526 12.454  15.663 1.00 8.87  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.094 13.466  20.152 1.00 8.08  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.930 12.602  20.402 1.00 8.38  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.642 13.401  20.592 1.00 8.09  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.643 14.501  21.171 1.00 8.93  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.119 11.777  21.676 1.00 9.50  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.139 10.657  21.589 1.00 9.60  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.178 9.932   22.946 1.00 10.90 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.797 9.632   20.493 1.00 10.44 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.536 12.803  20.146 1.00 7.68  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.196 13.313  20.423 1.00 8.68  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.294 12.130  20.688 1.00 9.06  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.380 11.090  20.017 1.00 9.30  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.681 14.200  19.269 1.00 9.00  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.288 14.843  19.449 1.00 9.17  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.233 16.184  18.753 1.00 10.35 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.161 13.905  18.950 1.00 11.14 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.414 12.289  21.686 1.00 9.57  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.420 11.247  22.051 1.00 9.97  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.021  11.891  21.962 1.00 10.13 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.784  12.981  22.525 1.00 11.34 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.641 10.732  23.486 1.00 10.78 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.569  9.682   23.867 1.00 11.80 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.028 10.106  23.583 1.00 11.18 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.132  11.233  21.235 1.00 10.49 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.740  11.681  21.088 1.00 10.66 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.807  10.587  21.626 1.00 12.36 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.186  9.430   21.803 1.00 12.06 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.442  11.986  19.621 1.00 12.12 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.599  10.872  18.750 1.00 13.20 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.539  10.976  21.878 1.00 13.45 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.559  10.015  22.391 1.00 14.86 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.790  9.340   21.257 1.00 16.47 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.586  9.912   20.198 1.00 17.50 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.611  10.696  23.372 1.00 17.42 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 1.985  11.767  22.706 1.00 20.87 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.371  8.100   21.473 1.00 16.59 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.625  7.324   20.479 1.00 19.09 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.283  6.855   21.083 1.00 21.83 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.148  6.773   22.309 1.00 22.57 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.437  6.076   20.038 1.00 20.19 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.493  5.172   21.128 1.00 21.17 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.856  6.402   19.615 1.00 20.43 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.675 6.522   20.225 1.00 23.76 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.946 5.971   20.698 1.00 26.26 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.849 4.442   20.824 1.00 27.50 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.431 3.855   21.742 1.00 29.94 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.110 6.418   19.789 1.00 29.19 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.744 6.134   18.441 1.00 31.39 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.402 7.901   19.909 1.00 30.11 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.114 3.794   19.921 1.00 26.29 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.960 2.342   19.951 1.00 25.64 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.237  1.907   20.827 1.00 25.17 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.212  2.638   20.947 1.00 24.08 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.775 1.830   18.533 1.00 26.98 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.179  0.711   21.389 1.00 24.93 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.254  0.162   22.221 1.00 25.12 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.402  -0.321  21.343 1.00 24.46 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.153  -0.971  20.330 1.00 25.93 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.695  -1.018  23.036 1.00 28.56 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.739  -1.791  23.846 1.00 36.05 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.088  -1.109  25.151 1.00 44.11 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.436  -0.143  25.596 1.00 46.64 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.133  -1.611  25.805 1.00 45.53 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.644  0.019   21.721 1.00 21.61 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.853  -0.345  20.976 1.00 21.21 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.199  -1.808  20.763 1.00 22.38 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 4.504  -2.699  21.252 1.00 25.37 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.238  -2.062  19.926 1.00 20.17 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.734  -3.408  19.629 1.00 18.78 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.098  -3.704  20.299 1.00 17.75 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.429  -4.866  20.469 1.00 16.55 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.828  -3.615  18.115 1.00 19.67 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.903  -2.430  17.254 1.00 20.04 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.833  -2.681  20.765 1.00 16.91 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.219 -2.801  21.311 1.00 15.72 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.365 -2.871  22.889 1.00 15.44 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.451  -2.371  23.584 1.00 19.62 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 10.998 -1.603  20.720 1.00 15.81 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.169 -1.688  19.194 1.00 18.30 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.655 -2.759  18.706 1.00 18.84 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.886 -0.651  18.463 1.00 15.26 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.567 -3.378  23.450 1.00 14.29 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.119 -3.572  24.845 1.00 16.65 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.464 -2.801  24.893 1.00 14.56 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.254 -2.938  23.973 1.00 14.29 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.573 -5.132  25.119 1.00 21.16 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.440 -5.920  25.385 1.00 27.43 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.575 -5.326  26.365 1.00 22.98 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.710 -1.988  25.933 1.00 11.89 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 14.960 -1.240  26.066 1.00 10.62 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 15.943 -2.001  26.953 1.00 11.13 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.577 -2.472  28.056 1.00 12.41 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.704 0.140   26.713 1.00 10.51 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.609 0.935   25.975 1.00 12.70 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.005 0.932   26.745 1.00 10.38 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.913 1.164   24.457 1.00 13.70 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.183 -2.147  26.511 1.00 10.12 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.239 -2.772  27.308 1.00 10.93 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.572 -1.905  28.531 1.00 10.91 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.635 -0.677  28.422 1.00 10.99 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.511 -2.954  26.459 1.00 10.52 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.868 -2.534  29.672 1.00 11.48 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.295 -1.793  30.881 1.00 11.60 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.564 -2.539  31.326 1.00 13.43 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.528 -3.465  32.155 1.00 13.99 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.200 -1.808  31.970 1.00 11.91 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.870 -1.258  31.515 1.00 12.78 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.904 0.228   31.149 1.00 14.05 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.559 0.680   30.780 1.00 13.68 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.298 1.840   30.184 1.00 15.10 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.278 2.677   29.875 1.00 13.86 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.057 2.158   29.862 1.00 16.46 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.682 -2.136  30.747 1.00 13.06 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 22.920 -2.885  30.851 1.00 12.84 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.123 -1.991  30.498 1.00 13.73 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 23.964 -0.830  30.086 1.00 13.88 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.832 -4.060  29.874 1.00 12.37 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.902 -3.543  28.130 1.00 12.43 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.352 -2.596  30.582 1.00 15.72 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.567 -1.907  30.183 1.00 16.00 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.248 -2.636  29.018 1.00 16.19 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.465 -2.530  28.871 1.00 16.86 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.559 -1.777  31.366 1.00 19.93 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.019 -3.088  31.963 1.00 25.98 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.582 -4.159  31.486 1.00 26.77 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 28.797 -3.053  32.947 1.00 33.26 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.477 -3.333  28.150 1.00 14.55 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.094 -3.981  26.964 1.00 13.17 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.837 -2.970  26.114 1.00 13.04 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.392 -1.828  25.950 1.00 12.29 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.017 -4.664  26.122 1.00 13.12 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.350 -6.194  26.849 1.00 13.75 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 28.950 -3.402  25.540 1.00 11.79 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.732 -2.664  24.550 1.00 11.12 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.914 -3.444  23.267 1.00 10.45 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.771 -3.111  22.434 1.00 10.77 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.096 -2.228  25.109 1.00 13.16 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.022 -1.033  26.052 1.00 18.32 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.446 -0.627  26.427 1.00 21.98 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 32.876 -0.824  27.573 1.00 22.38 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.217 -0.025  25.500 1.00 19.40 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.077 -4.507  23.076 1.00 9.70  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 28.989 -5.184  21.776 1.00 10.41 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.491 -5.382  21.460 1.00 9.15  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.644 -5.426  22.379 1.00 10.53 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.706 -6.551  21.764 1.00 11.87 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.069 -7.457  22.662 1.00 14.85 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.201 -6.446  22.103 1.00 12.94 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.184 -5.456  20.170 1.00 8.80  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.799 -5.656  19.741 1.00 8.17  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.766 -5.721  18.222 1.00 8.11  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.787 -5.966  17.570 1.00 8.73  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.561 -5.559  17.683 1.00 7.91  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.302 -5.688  16.245 1.00 7.39  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.424 -4.517  15.854 1.00 7.80  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.426 -4.205  16.528 1.00 8.46  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.553 -7.029  15.958 1.00 8.51  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.143 -7.115  14.476 1.00 9.54  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.456 -8.234  16.310 1.00 10.91 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.788 -3.843  14.736 1.00 8.24  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.936 -2.719  14.258 1.00 7.25  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.425 -2.982  12.853 1.00 7.88  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.049 -3.723  12.069 1.00 8.22  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.664 -1.319  14.338 1.00 7.84  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.679 -1.077  13.225 1.00 7.88  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.950 -1.656  13.278 1.00 8.37  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.407 -0.194  12.177 1.00 7.96  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.893 -1.421  12.280 1.00 8.62  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.365 0.064   11.186 1.00 8.70  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.597 -0.565  11.244 1.00 9.18  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.601 -0.360  10.296 1.00 10.82 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.295 -2.338  12.527 1.00 7.82  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.756 -2.420  11.158 1.00 8.42  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.290 -1.240  10.334 1.00 8.11  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.152 -0.057  10.720 1.00 8.72  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.200 -2.409  11.175 1.00 8.87  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.650 -2.514  9.780  1.00 9.48  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.821 -3.662  9.046  1.00 11.27 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.023 -1.431  9.175  1.00 11.14 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.370 -3.747  7.731  1.00 11.10 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.547 -1.508  7.873  1.00 12.10 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.706 -2.674  7.172  1.00 12.13 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.257 -2.777  5.865  1.00 16.45 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.846 -1.557  9.139  1.00 8.31  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.407 -0.581  8.211  1.00 7.59  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.500 -0.558  6.959  1.00 8.90  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.615 -1.435  6.094  1.00 9.68  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.817 -1.006  7.868  1.00 8.18  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.601 0.048   6.612  1.00 9.95  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.674 0.467   6.855  1.00 9.17  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.745 0.537   5.733  1.00 9.77  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.393 0.669   4.358  1.00 10.26 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.898 0.098   3.371  1.00 10.96 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.741 1.645   5.947  1.00 13.64 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.313 2.929   5.997  1.00 21.98 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.576 1.334   4.317  1.00 8.93  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.304 1.513   3.054  1.00 9.35  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.967 0.234   2.556  1.00 9.12  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.517 0.229   1.440  1.00 9.67  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.318 2.639   3.149  1.00 10.45 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.348 2.292   4.062  1.00 10.39 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.896 -0.848  3.333  1.00 8.91  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.346 -2.172  2.918  1.00 9.39  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.228 -3.243  3.025  1.00 10.29 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.461 -4.416  2.733  1.00 11.07 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.562 -2.592  3.761  1.00 10.45 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.818 -1.726  3.500  1.00 10.52 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.432 -2.027  2.135  1.00 11.40 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.624 -1.188  1.881  1.00 12.96 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.595 0.001   1.291  1.00 12.23 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.450 0.505   0.858  1.00 12.98 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.722 0.693   1.111  1.00 12.63 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.044 -2.845  3.527  1.00 10.95 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.958 -3.782  3.841  1.00 13.43 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.488 -4.969  4.656  1.00 12.87 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.186 -6.139  4.358  1.00 14.29 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.276 -4.287  2.558  1.00 16.25 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.414 -3.272  1.932  1.00 22.56 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.288 -3.978  1.167  1.00 26.45 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.690 -3.022  0.266  1.00 26.12 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 16.991 -2.923  -1.033 1.00 25.40 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.853 -3.781  -1.597 1.00 27.55 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.479 -1.943  -1.763 1.00 23.84 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.334 -4.680  5.652  1.00 11.56 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 21.987 -5.764  6.406  1.00 11.68 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.239 -5.356  7.842  1.00 10.38 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.396 -4.184  8.134  1.00 10.42 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.395 -6.032  5.791  1.00 15.81 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.463 -7.027  4.622  1.00 25.14 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.932 -7.342  4.353  1.00 32.14 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.123 -8.524  3.411  1.00 37.98 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 24.941 -8.145  1.985  1.00 40.67 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.356 -6.352  8.704  1.00 9.99  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.781 -6.160  10.090 1.00 8.73  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.273 -6.473  10.233 1.00 9.96  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.790 -7.421  9.599  1.00 12.33 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 21.994 -7.080  11.048 1.00 8.94  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.529 -6.817  11.049 1.00 10.53 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.909 -6.072  12.038 1.00 13.61 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.590 -7.295  10.220 1.00 11.05 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.604 -6.137  11.763 1.00 12.79 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.379 -6.825  10.680 1.00 15.71 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.983 -5.711  11.045 1.00 8.74  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.412 -5.916  11.288 1.00 8.07  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.701 -5.979  12.782 1.00 8.74  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.158 -5.180  13.568 1.00 8.72  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.242 -4.730  10.694 1.00 8.73  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.244 -4.638  9.191  1.00 10.18 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.954 -5.558  8.405  1.00 12.28 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.571 -3.616  8.548  1.00 11.65 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 27.987 -5.445  7.006  1.00 12.76 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.608 -3.479  7.165  1.00 12.42 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.305 -4.404  6.398  1.00 12.87 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.293 -4.277  5.022  1.00 16.00 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.626 -6.836  13.208 1.00 8.49  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.063 -6.833  14.620 1.00 9.19  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.067 -5.665  14.847 1.00 9.72  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.827 -5.274  13.913 1.00 12.97 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.789 -8.186  14.764 1.00 9.97  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.334 -8.422  13.349 1.00 10.88 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.330 -7.863  12.386 1.00 9.14  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.074 -5.110  16.052 1.00 8.95  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.930 -3.946  16.373 1.00 9.27  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.413 -4.022  17.793 1.00 9.05  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.735 -4.550  18.692 1.00 10.05 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.188 -2.564  16.242 1.00 11.66 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.148 -2.100  14.782 1.00 13.24 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.790 -2.616  16.836 1.00 12.20 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.618 -3.486  18.029 1.00 10.50 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.135 -3.164  19.365 1.00 10.51 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.064 -1.627  19.437 1.00 10.64 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.498 -0.957  18.492 1.00 11.13 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.600 -3.566  19.476 1.00 13.55 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.677 -4.979  19.426 1.00 21.80 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.456 -1.063  20.487 1.00 8.87  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.231 0.382   20.560 1.00 8.65  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.719 0.965   21.882 1.00 9.92  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.785 0.281   22.928 1.00 10.55 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.737 0.757   20.279 1.00 9.13  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.683 -0.013  21.080 1.00 8.66  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.225 -1.247  20.647 1.00 9.88  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.194 0.479   22.291 1.00 8.94  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.242 -1.946  21.357 1.00 10.09 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.224 -0.246  23.022 1.00 10.35 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.777 -1.461  22.547 1.00 10.40 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.089 2.260   21.824 1.00 9.72  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.544 2.936   23.042 1.00 10.50 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.420 3.244   24.003 1.00 11.09 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.251 3.214   23.611 1.00 11.68 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.296 4.212   22.687 1.00 12.74 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.421 5.101   22.001 1.00 15.29 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.722 3.472   25.279 1.00 10.91 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.705 3.854   26.260 1.00 11.78 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.134 5.228   25.895 1.00 12.81 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.811 6.042   25.253 1.00 12.95 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.331 3.871   27.663 1.00 14.22 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.671 2.468   28.126 1.00 17.14 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.245 2.573   29.570 1.00 23.09 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.712 1.244   30.089 1.00 30.12 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 32.892 1.279   31.559 1.00 34.90 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.865 5.527   26.259 1.00 11.68 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.291 6.854   25.929 1.00 12.05 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.168 8.000   26.417 1.00 13.26 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.570 8.034   27.579 1.00 13.92 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 26.940 6.857   26.657 1.00 14.50 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.640 5.399   26.969 1.00 16.99 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 27.953 4.698   27.074 1.00 12.89 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.462 8.948   25.509 1.00 11.92 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.378 10.043  25.863 1.00 13.37 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.096 11.304  25.053 1.00 11.84 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.207 11.322  24.209 1.00 11.43 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.830 9.576   25.730 1.00 19.41 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.189 9.549   24.377 1.00 27.31 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.836 12.399  25.391 1.00 10.72 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.714 13.702  24.730 1.00 12.42 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.690 13.714  23.582 1.00 13.75 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.919 13.684  23.829 1.00 15.77 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.109 14.803  25.728 1.00 15.16 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.021 15.529  26.449 1.00 21.08 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.657 16.547  27.448 1.00 23.61 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.125 16.325  25.473 1.00 20.53 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.202 13.794  22.349 1.00 12.88 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.024 13.704  21.140 1.00 14.13 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.771 14.884  20.230 1.00 13.41 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.599 15.222  19.980 1.00 12.73 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.684 12.369  20.420 1.00 15.62 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.031 11.182  21.335 1.00 18.24 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.322 12.279  19.026 1.00 17.50 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.863 9.813   20.801 1.00 21.65 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.820 15.510  19.684 1.00 12.81 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.671 16.607  18.745 1.00 13.48 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.084 16.129  17.423 1.00 13.82 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.539 15.116  16.864 1.00 15.63 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.056 17.252  18.479 1.00 15.41 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.980 18.402  17.510 1.00 18.52 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.240 18.209  16.161 1.00 20.40 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.561 19.642  17.924 1.00 20.53 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.128 19.260  15.256 1.00 21.97 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.476 20.710  17.012 1.00 22.10 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.778 20.502  15.692 1.00 21.49 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.011 16.821  16.960 1.00 12.65 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.361 16.512  15.691 1.00 12.86 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.401 17.780  14.831 1.00 13.93 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.894 18.855  15.227 1.00 13.67 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.889 16.050  15.929 1.00 11.84 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.202 15.787  14.573 1.00 13.84 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.858 14.790  16.796 1.00 11.58 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.921 17.629  13.611 1.00 14.88 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.078 18.768  12.695 1.00 16.04 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.719 19.349  12.311 1.00 15.96 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.724 18.627  12.336 1.00 14.88 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.813 18.298  11.418 1.00 20.92 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.264 19.418  10.493 1.00 30.77 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.036 18.947  9.271  1.00 41.26 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.441 19.812  8.461  1.00 43.71 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 33.246 17.720  9.127  1.00 43.93 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.688 20.623  11.875 1.00 16.64 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.439 21.238  11.435 1.00 15.72 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.807 20.477  10.284 1.00 16.09 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.488 19.922  9.425  1.00 16.62 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.701 22.681  10.989 1.00 17.43 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.475 20.470  10.268 1.00 15.13 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.707 19.867  9.184  1.00 15.01 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.584 20.878  8.871  1.00 16.36 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.515 21.947  9.495  1.00 17.41 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 25.110 18.521  9.642  1.00 15.98 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 24.156 18.714  10.678 1.00 15.67 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.654 20.477  7.985  1.00 16.46 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.513 21.383  7.759  1.00 17.87 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.548 21.412  8.954  1.00 18.26 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.722 22.329  9.069  1.00 19.59 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.785 21.027  6.468  1.00 24.12 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.228 19.635  6.450  1.00 34.75 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 20.941 19.154  5.044  1.00 47.76 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 19.824 19.414  4.535  1.00 51.21 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 21.844 18.526  4.441  1.00 51.41 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.661 20.414  9.860  1.00 16.48 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.758 20.306  10.974 1.00 15.54 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.244 20.932  12.259 1.00 14.35 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.438 21.327  13.110 1.00 15.74 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.497 18.828  11.233 1.00 15.66 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.976 18.080  10.023 1.00 16.24 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.836 17.382  9.186  1.00 17.38 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.635 18.129  9.675  1.00 16.81 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.352 16.655  8.099  1.00 18.96 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.147 17.460  8.551  1.00 18.05 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 19.006 16.711  7.774  1.00 20.19 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.502 16.076  6.649  1.00 23.29 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.566 20.993  12.437 1.00 13.29 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.115 21.520  13.682 1.00 12.87 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.399 22.269  13.418 1.00 14.95 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.167 21.862  12.538 1.00 15.02 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.531 20.367  14.648 1.00 11.66 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.422 19.446  15.137 1.00 10.94 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.514 19.864  16.101 1.00 12.45 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.280 18.172  14.625 1.00 10.87 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.530 19.012  16.594 1.00 11.20 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.295 17.298  15.115 1.00 10.23 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.411 17.733  16.085 1.00 10.48 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.421 16.924  16.567 1.00 10.67 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.712 23.261  14.259 1.00 16.80 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.054 23.878  14.197 1.00 16.75 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.086 22.876  14.731 1.00 16.44 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.734 21.874  15.401 1.00 16.83 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.909 25.072  15.159 1.00 18.80 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 24.935 24.580  16.185 1.00 20.56 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.918 23.783  15.385 1.00 18.05 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.403 23.144  14.538 1.00 16.66 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.467 22.338  15.133 1.00 17.88 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.280 22.362  16.666 1.00 16.54 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 28.974 23.419  17.241 1.00 17.84 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.822 22.925  14.762 1.00 19.04 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.289 21.171  17.293 1.00 15.85 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 28.972 21.095  18.730 1.00 14.94 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.448 19.765  19.293 1.00 14.93 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.848 18.879  18.537 1.00 16.37 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.423 21.213  18.916 1.00 14.50 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.693 19.897  18.485 1.00 15.30 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.274 20.106  18.024 1.00 13.22 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.402 18.976  18.380 1.00 13.31 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.396 17.791  17.772 1.00 11.43 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.517 16.856  18.136 1.00 12.26 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.249 17.538  16.779 1.00 12.19 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.390 19.613  20.611 1.00 13.93 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.626 18.301  21.228 1.00 14.52 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.273 17.618  21.392 1.00 13.61 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.360 18.184  21.999 1.00 14.63 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.257 18.437  22.607 1.00 15.66 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.708 18.861  22.504 1.00 17.15 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.724 17.916  22.447 1.00 17.52 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.052 20.205  22.407 1.00 19.07 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.069 18.306  22.337 1.00 20.25 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.380 20.603  22.271 1.00 21.36 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.376 19.648  22.212 1.00 21.78 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.689 20.099  22.116 1.00 25.91 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.156 16.405  20.891 1.00 11.51 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.947 15.597  21.091 1.00 11.01 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.210 14.681  22.297 1.00 9.73  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.266 14.006  22.361 1.00 11.50 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.600 14.790  19.837 1.00 10.59 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.353 13.902  20.054 1.00 10.08 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.754 13.436  18.749 1.00 9.72  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.659 14.202  17.758 1.00 11.24 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.274 12.175  18.742 1.00 9.62  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.311 14.671  23.273 1.00 9.63  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.430 13.836  24.449 1.00 9.42  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.762 12.470  24.268 1.00 11.11 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 24.940 12.292  23.361 1.00 10.76 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.855 14.565  25.670 1.00 12.06 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.464 14.786  25.484 1.00 13.47 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.157 11.508  25.129 1.00 10.24 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.559 10.169  25.161 1.00 10.23 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.725 9.458   23.808 1.00 9.85  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.899 8.606   23.455 1.00 10.03 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.065 10.195  25.585 1.00 10.76 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.851 10.796  26.960 1.00 11.83 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.685 9.992   28.072 1.00 13.62 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.788 12.089  27.347 1.00 12.58 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.544 10.828  29.117 1.00 15.02 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.587 12.091  28.724 1.00 15.09 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.857 9.713   23.120 1.00 9.56  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.100 9.126   21.810 1.00 9.23  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.153 8.031   21.953 1.00 9.60  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.142 8.182   22.694 1.00 9.93  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.653 10.254  20.892 1.00 10.70 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.923 9.868   19.422 1.00 10.90 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.627 9.412   18.683 1.00 11.19 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.487 11.126  18.642 1.00 13.50 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.935 6.940   21.208 1.00 9.07  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.823 5.762   21.219 1.00 9.29  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.335 5.534   19.845 1.00 9.74  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.531 5.458   18.905 1.00 11.20 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.023 4.521   21.642 1.00 9.86  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.432 4.692   23.049 1.00 10.69 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.330 3.375   23.615 1.00 13.08 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 24.995 3.536   22.448 1.00 16.74 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.650 5.395   19.671 1.00 9.48  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.200 5.164   18.333 1.00 10.44 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.628 3.731   18.113 1.00 9.84  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.114 3.061   19.025 1.00 9.98  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.436 6.070   18.046 1.00 12.94 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.230 7.548   18.090 1.00 16.71 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.510 8.291   17.570 1.00 18.11 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.056 7.987   17.247 1.00 17.57 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.564 3.298   16.862 1.00 9.43  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.026 1.967   16.448 1.00 9.59  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.537 2.010   15.027 1.00 9.28  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.232 2.964   14.280 1.00 10.45 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.860 0.977   16.487 1.00 11.52 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.380 1.035   14.666 1.00 8.00  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.789 0.886   13.274 1.00 8.81  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.696 0.087   12.545 1.00 10.35 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.338 -1.030  12.956 1.00 11.24 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.148 0.178   13.233 1.00 9.54  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.585 -0.053  11.779 1.00 10.57 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.178 1.022   13.988 1.00 11.33 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.172 0.677   11.486 1.00 9.96  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.092 0.059   10.712 1.00 10.28 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.644 1.038   9.662  1.00 10.34 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.913 2.235   9.748  1.00 11.50 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.027 0.525   8.603  1.00 9.83  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.530 1.367   7.531  1.00 9.27  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.296 2.188   7.936  1.00 8.65  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.349 1.669   8.550  1.00 9.34  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.150 0.542   6.282  1.00 10.33 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.662 1.415   5.159  1.00 9.91  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.497 2.297   4.527  1.00 10.74 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.401 1.568   4.652  1.00 10.22 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.749 2.946   3.639  1.00 11.24 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.463 2.535   3.699  1.00 11.65 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.267 3.439   7.541  1.00 9.37  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.087 4.288   7.653  1.00 9.70  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.172 5.425   6.649  1.00 11.44 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.274 5.847   6.280  1.00 12.58 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.888 4.798   9.067  1.00 11.00 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.893 5.728   9.430  1.00 12.41 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 26.029 5.847   6.182  1.00 9.30  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.981 6.982   5.286  1.00 11.38 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.671 7.691   5.633  1.00 16.08 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.835 7.217   6.437  1.00 18.46 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 26.221 6.555   3.775  1.00 16.57 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 25.299 5.490   3.286  1.00 20.30 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.573 5.064   1.857  1.00 13.51 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 24.972 5.709   0.970  1.00 16.48 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.232 4.021   1.651  1.00 12.56 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.563 8.987   5.229  1.00 19.15 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.304 9.658   5.454  1.00 21.30 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 22.179 8.906   4.676  1.00 18.52 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 22.230 8.418   3.476  1.00 21.44 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.544 11.132  5.138  1.00 22.68 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.971 11.217  4.640  1.00 21.77 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.477 9.792   4.413  1.00 18.67 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.220 8.700   5.518  1.00 13.52 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 19.997 7.927   5.376  1.00 13.38 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.951 6.790   6.400  1.00 11.00 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.887 6.230   6.650  1.00 12.49 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.139 6.379   6.968  1.00 10.31 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.137 5.300   7.929  1.00 9.38  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.723 5.683   9.358  1.00 8.31  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.477 4.806   10.189 1.00 9.38  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.534 4.656   8.010  1.00 9.58  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.845 3.804   6.805  1.00 10.37 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.901 3.194   6.270  1.00 10.62 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 24.059 3.776   6.367  1.00 9.77  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.543 6.988   9.620  1.00 9.04  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.108 7.409   10.959 1.00 7.76  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.767 6.768   11.292 1.00 9.03  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.890 6.692   10.432 1.00 10.36 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.045 8.936   11.048 1.00 9.10  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.678 9.733   11.114 1.00 11.72 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.635 6.346   12.531 1.00 7.76  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.372 5.712   12.958 1.00 8.31  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.490 4.201   13.034 1.00 9.19  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.630 3.544   13.647 1.00 10.12 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.521 3.603   12.399 1.00 7.92  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.724 2.158   12.508 1.00 7.72  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 18.966 1.763   13.942 1.00 7.88  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.740 2.413   14.660 1.00 8.67  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.367 0.665   14.360 1.00 8.13  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.505 0.231   15.744 1.00 8.12  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.788 -0.569  16.025 1.00 7.81  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.144 -1.461  15.232 1.00 8.31  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.236 -0.568  16.154 1.00 10.26 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.070 0.437   16.412 1.00 11.38 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.477 -1.480  17.400 1.00 11.82 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.695 -0.306  16.678 1.00 14.62 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.422 -0.282  17.166 1.00 7.46  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.508 -1.080  17.753 1.00 7.55  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.873 -1.890  18.889 1.00 8.48  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.212 -1.286  19.769 1.00 8.42  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.581 -0.140  18.330 1.00 8.00  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.711 -0.809  19.152 1.00 9.22  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.560 -1.777  18.278 1.00 10.34 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.611 0.267   19.786 1.00 10.51 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.103 -3.221  18.920 1.00 8.02  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.571 -4.102  19.963 1.00 8.73  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.682 -4.959  20.497 1.00 8.66  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.561 -5.433  19.765 1.00 9.73  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.566 -5.099  19.322 1.00 13.57 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.331 -4.501  18.764 1.00 20.55 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.525 -5.655  18.139 1.00 20.52 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 16.814 -6.237  19.258 1.00 23.77 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.638 -5.804  19.666 1.00 22.73 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 14.960 -4.946  18.930 1.00 19.11 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.139 -6.221  20.811 1.00 16.97 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.578 -5.276  21.793 1.00 9.57  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.429 -6.347  22.422 1.00 10.07 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.462 -7.457  22.836 1.00 10.72 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.247 -7.407  22.569 1.00 11.23 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.156 -5.786  23.649 1.00 10.96 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.023 -5.247  24.966 1.00 10.45 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 21.946 -8.480  23.554 1.00 11.36 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.073 -9.570  24.014 1.00 13.06 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 19.975 -9.119  24.982 1.00 13.73 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.022 -9.897  25.214 1.00 15.24 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 21.916 -10.703 24.657 1.00 14.04 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.527 -10.264 25.985 1.00 19.78 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.558 -11.225 26.506 1.00 28.22 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.787 -11.008 26.388 1.00 33.57 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.066 -12.275 27.113 1.00 26.85 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.060 -7.910  25.549 1.00 11.85 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.099 -7.420  26.540 1.00 11.94 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 17.971 -6.594  25.974 1.00 11.56 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.002 -6.320  26.669 1.00 12.95 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.794 -6.616  27.664 1.00 12.40 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 20.917 -7.389  28.322 1.00 13.60 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.242 -7.064  28.116 1.00 14.47 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.859 -8.455  29.179 1.00 16.10 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 22.960 -7.957  28.803 1.00 16.47 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.177 -8.838  29.416 1.00 17.25 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.141 -6.098  24.747 1.00 9.66  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.150 -5.234  24.118 1.00 9.71  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.765 -4.110  23.295 1.00 9.42  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 18.947 -4.183  22.923 1.00 9.93  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 16.972 -3.096  23.037 1.00 8.72  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.431 -1.957  22.226 1.00 8.84  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.412 -1.108  23.029 1.00 7.50  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.102 -0.714  24.184 1.00 9.48  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.216 -1.105  21.792 1.00 9.20  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.698 0.184   21.102 1.00 10.55 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.328 -1.936  20.842 1.00 10.46 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.548 -0.771  22.444 1.00 8.19  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.588 0.040   23.076 1.00 8.34  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.504 1.510   22.632 1.00 9.20  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.730 2.435   23.430 1.00 9.74  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 21.969 -0.563  22.740 1.00 9.12  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.122 0.340   23.214 1.00 10.87 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.128 -1.966  23.341 1.00 9.67  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.270 1.718   21.328 1.00 8.06  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.237 3.075   20.782 1.00 8.56  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.956 3.092   19.303 1.00 7.47  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.565 2.044   18.744 1.00 8.32  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.123 4.290   18.673 1.00 7.61  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.834 4.406   17.237 1.00 8.03  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.003 5.087   16.538 1.00 7.52  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.659 5.971   17.131 1.00 7.85  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.528 5.197   16.932 1.00 9.21  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.479 6.528   17.694 1.00 10.13 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.295 4.312   17.214 1.00 11.10 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.222 7.387   17.272 1.00 11.26 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.235 4.775   15.249 1.00 6.97  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.288 5.474   14.485 1.00 6.80  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.003 6.994   14.468 1.00 6.78  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.854 7.408   14.238 1.00 6.82  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.351 4.945   13.042 1.00 6.96  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.356 5.760   12.194 1.00 8.32  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.736 3.451   13.004 1.00 8.23  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.030 7.789   14.749 1.00 7.21  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.906 9.241   14.763 1.00 7.86  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.035 9.951   14.006 1.00 8.28  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.837 11.088  13.580 1.00 8.48  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.879 9.689   16.225 1.00 8.19  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.814 11.105  16.411 1.00 9.14  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.218 9.332   13.875 1.00 8.84  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.328 10.013  13.161 1.00 9.42  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.132 8.939   12.389 1.00 9.03  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.892 7.740   12.572 1.00 8.90  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.329 10.709  14.170 1.00 10.88 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.121 9.714   14.852 1.00 11.85 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.688 11.689  15.151 1.00 12.51 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.063 9.382   11.567 1.00 10.32 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.989 8.429   10.973 1.00 11.56 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.964 9.105   10.046 1.00 13.49 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 30.051 10.332  10.011 1.00 14.32 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.691 8.293   9.309  1.00 13.96 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.534 8.723   8.190  1.00 15.35 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.824 7.962   8.229  1.00 14.37 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.255 7.530   9.310  1.00 15.24 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.470 7.804   7.067  1.00 15.11 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.791 7.163   6.923  1.00 13.96 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.978 5.880   7.690  1.00 12.82 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.073 5.598   8.220  1.00 13.53 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.894 8.162   7.278  1.00 19.16 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.771 9.411   6.432  1.00 25.66 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.791 9.330   5.225  1.00 27.35 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.566 10.566  7.041  1.00 28.34 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.015 4.985   7.576  1.00 10.91 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.074 3.689   8.231  1.00 11.23 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.726 3.695   9.708  1.00 10.27 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.931 2.661   10.370 1.00 12.06 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.141 4.795   10.196 1.00 9.34  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.632 4.905   11.558 1.00 8.97  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.088 4.994   11.534 1.00 9.05  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.491 5.459   10.557 1.00 10.09 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.172 6.154   12.294 1.00 10.07 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.677 6.099   12.560 1.00 13.83 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.224 7.510   12.855 1.00 15.96 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.009 5.058   13.696 1.00 13.99 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.498 4.597   12.644 1.00 8.39  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.061 4.732   12.856 1.00 7.86  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.872 5.127   14.335 1.00 8.46  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.550 4.587   15.215 1.00 9.91  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.255 3.472   12.464 1.00 8.07  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.761 2.188   13.113 1.00 9.51  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.762 3.684   12.685 1.00 9.20  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.057 6.152   14.585 1.00 7.77  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.799 6.616   15.945 1.00 7.57  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.356 6.400   16.344 1.00 7.69  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.449 6.618   15.527 1.00 8.82  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.136 5.989   17.583 1.00 7.41  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.772 5.644   18.055 1.00 8.24  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.414 6.517   19.269 1.00 8.23  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.214 6.637   20.223 1.00 8.28  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.719 4.170   18.537 1.00 8.24  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.220 3.179   17.504 1.00 7.46  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.362 2.690   16.522 1.00 7.51  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.535 2.724   17.538 1.00 8.97  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.823 1.771   15.569 1.00 8.00  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 26.986 1.763   16.626 1.00 9.30  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.129 1.303   15.627 1.00 9.31  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.197 7.073   19.246 1.00 7.37  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.678 7.823   20.381 1.00 8.01  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.149 6.760   21.378 1.00 8.02  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.215 5.989   21.062 1.00 8.73  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.549 8.724   19.914 1.00 8.09  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.706 6.735   22.590 1.00 7.59  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.274 5.796   23.628 1.00 9.04  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.904 6.154   24.154 1.00 9.15  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.588 7.351   24.305 1.00 9.61  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.300 5.818   24.782 1.00 11.18 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.019 4.782   25.855 1.00 13.94 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.863 3.626   25.530 1.00 13.45 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 22.852 5.167   27.030 1.00 18.57 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.078 5.123   24.472 1.00 8.64  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.776 5.359   25.115 1.00 9.22  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.666 4.593   26.429 1.00 9.53  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.632 4.679   27.083 1.00 10.47 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.556 5.031   24.220 1.00 10.01 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.585 5.893   22.935 1.00 10.97 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.518 3.544   23.874 1.00 10.51 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.703 3.848   26.851 1.00 9.31  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.589 2.960   28.019 1.00 9.19  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.425 3.668   29.315 1.00 11.32 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 18.940 3.079   30.300 1.00 12.24 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.805 2.004   28.095 1.00 9.71  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.900 1.016   26.924 1.00 10.28 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.161 0.181   27.065 1.00 10.66 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.300 1.032   26.774 1.00 10.45 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.557 0.608   26.643 1.00 10.60 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.876 -0.664  26.921 1.00 11.30 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.499 1.439   26.214 1.00 12.31 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.825 4.951   29.381 1.00 10.95 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.671 5.705   30.640 1.00 12.27 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.286 6.309   30.782 1.00 12.67 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.002 6.852   31.850 1.00 13.89 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.708 6.827   30.715 1.00 13.63 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.576 7.841   29.601 1.00 15.74 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.373 7.431   28.437 1.00 16.01 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.642 9.066   29.887 1.00 18.01 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.415 6.242   29.774 1.00 11.82 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.094 6.881   29.832 1.00 11.50 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.115 5.907   30.453 1.00 11.74 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.358 5.202   29.801 1.00 11.40 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.654 7.275   28.428 1.00 11.78 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.617 8.248   27.674 1.00 12.28 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.180 8.429   26.218 1.00 13.15 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.797 9.569   28.400 1.00 13.57 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.196 5.810   31.785 1.00 11.16 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.442 4.778   32.520 1.00 12.30 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 12.935 4.950   32.409 1.00 13.52 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.189 3.957   32.465 1.00 14.61 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.852 4.743   34.000 1.00 12.65 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.353 4.643   34.266 1.00 14.15 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.590 4.401   35.779 1.00 15.80 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.045 3.521   33.437 1.00 14.58 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.502 6.214   32.261 1.00 14.15 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.088 6.547   32.154 1.00 14.63 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.434 5.976   30.885 1.00 15.50 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.188  5.939   30.818 1.00 17.34 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.882 8.068   32.276 1.00 14.53 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.697 8.881   31.297 1.00 13.88 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 12.928 9.450   31.498 1.00 13.97 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.337 9.176   29.945 1.00 14.06 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.330 10.129  30.366 1.00 14.52 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.362 9.990   29.400 1.00 14.41 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.193 8.934   29.184 1.00 14.57 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.290 10.511  28.100 1.00 14.15 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.122 9.453   27.901 1.00 14.21 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.143 10.265  27.395 1.00 14.24 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.222 5.522   29.879 1.00 14.72 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.610 4.953   28.660 1.00 15.77 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.761  3.722   28.974 1.00 18.98 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.835  3.410   28.227 1.00 20.32 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.671 4.557   27.627 1.00 15.06 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.356 5.716   26.921 1.00 14.02 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.501 5.187   26.053 1.00 15.23 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.352 6.497   26.014 1.00 14.06 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.108 3.000   30.074 1.00 22.07 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.403  1.797   30.534 1.00 25.82 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.214  2.173   31.390 1.00 29.82 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.640  1.250   31.986 1.00 32.97 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.316 0.959   31.447 1.00 29.40 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.626 0.518   30.887 1.00 36.62 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.674 0.181   29.690 1.00 39.58 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.611 0.468   31.657 1.00 41.36 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . SER   B 1 1   ? 19.562 -24.751 23.992 1.00 19.38 ? 7   SER   C N   1 
ATOM   1070 C  CA  . SER   B 1 1   ? 20.683 -24.578 23.051 1.00 19.33 ? 7   SER   C CA  1 
ATOM   1071 C  C   . SER   B 1 1   ? 20.694 -25.715 22.018 1.00 17.97 ? 7   SER   C C   1 
ATOM   1072 O  O   . SER   B 1 1   ? 20.073 -26.768 22.243 1.00 18.78 ? 7   SER   C O   1 
ATOM   1073 C  CB  . SER   B 1 1   ? 22.019 -24.550 23.807 1.00 21.78 ? 7   SER   C CB  1 
ATOM   1074 O  OG  . SER   B 1 1   ? 22.204 -25.777 24.496 1.00 26.76 ? 7   SER   C OG  1 
ATOM   1075 N  N   . GLY   B 1 2   ? 21.427 -25.538 20.925 1.00 15.69 ? 8   GLY   C N   1 
ATOM   1076 C  CA  . GLY   B 1 2   ? 21.583 -26.591 19.922 1.00 14.39 ? 8   GLY   C CA  1 
ATOM   1077 C  C   . GLY   B 1 2   ? 21.839 -26.012 18.539 1.00 13.01 ? 8   GLY   C C   1 
ATOM   1078 O  O   . GLY   B 1 2   ? 21.474 -24.860 18.261 1.00 14.90 ? 8   GLY   C O   1 
ATOM   1079 N  N   . ALA   B 1 3   ? 22.458 -26.770 17.658 1.00 11.89 ? 9   ALA   C N   1 
ATOM   1080 C  CA  . ALA   B 1 3   ? 22.782 -26.315 16.301 1.00 12.26 ? 9   ALA   C CA  1 
ATOM   1081 C  C   . ALA   B 1 3   ? 22.733 -27.479 15.332 1.00 11.67 ? 9   ALA   C C   1 
ATOM   1082 O  O   . ALA   B 1 3   ? 22.784 -28.666 15.728 1.00 13.68 ? 9   ALA   C O   1 
ATOM   1083 C  CB  . ALA   B 1 3   ? 24.214 -25.726 16.294 1.00 13.25 ? 9   ALA   C CB  1 
ATOM   1084 N  N   . ILE   B 1 4   ? 22.636 -27.169 14.029 1.00 10.51 ? 10  ILE   C N   1 
ATOM   1085 C  CA  . ILE   B 1 4   ? 22.761 -28.127 12.924 1.00 10.16 ? 10  ILE   C CA  1 
ATOM   1086 C  C   . ILE   B 1 4   ? 24.129 -27.912 12.276 1.00 11.34 ? 10  ILE   C C   1 
ATOM   1087 O  O   . ILE   B 1 4   ? 24.519 -26.771 12.028 1.00 11.33 ? 10  ILE   C O   1 
ATOM   1088 C  CB  . ILE   B 1 4   ? 21.656 -27.868 11.894 1.00 10.17 ? 10  ILE   C CB  1 
ATOM   1089 C  CG1 . ILE   B 1 4   ? 20.278 -27.954 12.541 1.00 10.74 ? 10  ILE   C CG1 1 
ATOM   1090 C  CG2 . ILE   B 1 4   ? 21.771 -28.855 10.748 1.00 11.20 ? 10  ILE   C CG2 1 
ATOM   1091 C  CD1 . ILE   B 1 4   ? 19.174 -27.291 11.668 1.00 12.31 ? 10  ILE   C CD1 1 
ATOM   1092 N  N   . TYR   B 1 5   ? 24.875 -28.983 12.019 1.00 12.25 ? 11  TYR   C N   1 
ATOM   1093 C  CA  . TYR   B 1 5   ? 26.196 -28.911 11.415 1.00 13.00 ? 11  TYR   C CA  1 
ATOM   1094 C  C   . TYR   B 1 5   ? 26.118 -29.630 10.086 1.00 12.17 ? 11  TYR   C C   1 
ATOM   1095 O  O   . TYR   B 1 5   ? 25.946 -30.862 10.070 1.00 13.18 ? 11  TYR   C O   1 
ATOM   1096 C  CB  . TYR   B 1 5   ? 27.241 -29.583 12.329 1.00 14.28 ? 11  TYR   C CB  1 
ATOM   1097 C  CG  . TYR   B 1 5   ? 27.432 -28.787 13.603 1.00 13.26 ? 11  TYR   C CG  1 
ATOM   1098 C  CD1 . TYR   B 1 5   ? 28.274 -27.680 13.638 1.00 14.96 ? 11  TYR   C CD1 1 
ATOM   1099 C  CD2 . TYR   B 1 5   ? 26.712 -29.091 14.752 1.00 14.89 ? 11  TYR   C CD2 1 
ATOM   1100 C  CE1 . TYR   B 1 5   ? 28.426 -26.926 14.802 1.00 17.61 ? 11  TYR   C CE1 1 
ATOM   1101 C  CE2 . TYR   B 1 5   ? 26.864 -28.347 15.922 1.00 16.37 ? 11  TYR   C CE2 1 
ATOM   1102 C  CZ  . TYR   B 1 5   ? 27.732 -27.273 15.947 1.00 18.42 ? 11  TYR   C CZ  1 
ATOM   1103 O  OH  . TYR   B 1 5   ? 27.810 -26.487 17.082 1.00 22.18 ? 11  TYR   C OH  1 
ATOM   1104 N  N   . VAL   B 1 6   ? 26.217 -28.921 8.959  1.00 13.26 ? 12  VAL   C N   1 
ATOM   1105 C  CA  . VAL   B 1 6   ? 26.070 -29.512 7.628  1.00 14.50 ? 12  VAL   C CA  1 
ATOM   1106 C  C   . VAL   B 1 6   ? 27.147 -28.896 6.739  1.00 14.90 ? 12  VAL   C C   1 
ATOM   1107 O  O   . VAL   B 1 6   ? 27.284 -27.679 6.682  1.00 14.74 ? 12  VAL   C O   1 
ATOM   1108 C  CB  . VAL   B 1 6   ? 24.629 -29.329 7.053  1.00 17.14 ? 12  VAL   C CB  1 
ATOM   1109 C  CG1 . VAL   B 1 6   ? 24.171 -27.878 7.113  1.00 18.61 ? 12  VAL   C CG1 1 
ATOM   1110 C  CG2 . VAL   B 1 6   ? 24.567 -29.876 5.642  1.00 18.16 ? 12  VAL   C CG2 1 
ATOM   1111 N  N   . GLY   B 1 7   ? 28.032 -29.724 6.152  1.00 16.83 ? 13  GLY   C N   1 
ATOM   1112 C  CA  . GLY   B 1 7   ? 29.123 -29.208 5.328  1.00 18.58 ? 13  GLY   C CA  1 
ATOM   1113 C  C   . GLY   B 1 7   ? 30.010 -28.275 6.133  1.00 18.79 ? 13  GLY   C C   1 
ATOM   1114 O  O   . GLY   B 1 7   ? 30.312 -28.575 7.292  1.00 19.34 ? 13  GLY   C O   1 
ATOM   1115 N  N   . ASN   B 1 8   ? 30.314 -27.079 5.611  1.00 17.86 ? 14  ASN   C N   1 
ATOM   1116 C  CA  . ASN   B 1 8   ? 31.094 -26.103 6.386  1.00 18.26 ? 14  ASN   C CA  1 
ATOM   1117 C  C   . ASN   B 1 8   ? 30.196 -25.027 6.999  1.00 16.17 ? 14  ASN   C C   1 
ATOM   1118 O  O   . ASN   B 1 8   ? 30.631 -23.879 7.171  1.00 16.42 ? 14  ASN   C O   1 
ATOM   1119 C  CB  . ASN   B 1 8   ? 32.252 -25.511 5.592  1.00 22.07 ? 14  ASN   C CB  1 
ATOM   1120 C  CG  . ASN   B 1 8   ? 33.314 -26.554 5.327  1.00 30.06 ? 14  ASN   C CG  1 
ATOM   1121 O  OD1 . ASN   B 1 8   ? 33.995 -27.041 6.251  1.00 32.64 ? 14  ASN   C OD1 1 
ATOM   1122 N  ND2 . ASN   B 1 8   ? 33.448 -26.935 4.075  1.00 31.77 ? 14  ASN   C ND2 1 
ATOM   1123 N  N   . TYR   B 1 9   ? 28.979 -25.415 7.385  1.00 14.41 ? 15  TYR   C N   1 
ATOM   1124 C  CA  . TYR   B 1 9   ? 28.037 -24.462 7.976  1.00 13.11 ? 15  TYR   C CA  1 
ATOM   1125 C  C   . TYR   B 1 9   ? 27.533 -24.933 9.329  1.00 12.10 ? 15  TYR   C C   1 
ATOM   1126 O  O   . TYR   B 1 9   ? 27.378 -26.135 9.568  1.00 13.07 ? 15  TYR   C O   1 
ATOM   1127 C  CB  . TYR   B 1 9   ? 26.788 -24.356 7.079  1.00 14.06 ? 15  TYR   C CB  1 
ATOM   1128 C  CG  . TYR   B 1 9   ? 27.057 -23.774 5.715  1.00 14.78 ? 15  TYR   C CG  1 
ATOM   1129 C  CD1 . TYR   B 1 9   ? 27.724 -22.563 5.571  1.00 15.96 ? 15  TYR   C CD1 1 
ATOM   1130 C  CD2 . TYR   B 1 9   ? 26.661 -24.445 4.565  1.00 15.40 ? 15  TYR   C CD2 1 
ATOM   1131 C  CE1 . TYR   B 1 9   ? 27.989 -22.032 4.308  1.00 17.78 ? 15  TYR   C CE1 1 
ATOM   1132 C  CE2 . TYR   B 1 9   ? 26.894 -23.911 3.294  1.00 17.07 ? 15  TYR   C CE2 1 
ATOM   1133 C  CZ  . TYR   B 1 9   ? 27.566 -22.708 3.176  1.00 18.89 ? 15  TYR   C CZ  1 
ATOM   1134 O  OH  . TYR   B 1 9   ? 27.755 -22.115 1.944  1.00 21.90 ? 15  TYR   C OH  1 
ATOM   1135 N  N   . ARG   B 1 10  ? 27.204 -23.970 10.202 1.00 10.38 ? 16  ARG   C N   1 
ATOM   1136 C  CA  . ARG   B 1 10  ? 26.581 -24.182 11.525 1.00 11.50 ? 16  ARG   C CA  1 
ATOM   1137 C  C   . ARG   B 1 10  ? 25.304 -23.335 11.522 1.00 10.42 ? 16  ARG   C C   1 
ATOM   1138 O  O   . ARG   B 1 10  ? 25.360 -22.123 11.246 1.00 10.79 ? 16  ARG   C O   1 
ATOM   1139 C  CB  . ARG   B 1 10  ? 27.541 -23.697 12.630 1.00 13.02 ? 16  ARG   C CB  1 
ATOM   1140 C  CG  . ARG   B 1 10  ? 26.926 -23.498 14.011 1.00 13.26 ? 16  ARG   C CG  1 
ATOM   1141 C  CD  . ARG   B 1 10  ? 27.963 -23.179 15.101 1.00 13.67 ? 16  ARG   C CD  1 
ATOM   1142 N  NE  . ARG   B 1 10  ? 27.507 -22.192 16.095 1.00 14.96 ? 16  ARG   C NE  1 
ATOM   1143 C  CZ  . ARG   B 1 10  ? 27.056 -22.460 17.324 1.00 19.17 ? 16  ARG   C CZ  1 
ATOM   1144 N  NH1 . ARG   B 1 10  ? 26.888 -23.722 17.721 1.00 19.45 ? 16  ARG   C NH1 1 
ATOM   1145 N  NH2 . ARG   B 1 10  ? 26.697 -21.466 18.141 1.00 18.26 ? 16  ARG   C NH2 1 
ATOM   1146 N  N   . VAL   B 1 11  ? 24.145 -23.969 11.753 1.00 10.29 ? 17  VAL   C N   1 
ATOM   1147 C  CA  . VAL   B 1 11  ? 22.852 -23.291 11.775 1.00 9.54  ? 17  VAL   C CA  1 
ATOM   1148 C  C   . VAL   B 1 11  ? 22.396 -23.197 13.237 1.00 9.09  ? 17  VAL   C C   1 
ATOM   1149 O  O   . VAL   B 1 11  ? 22.266 -24.244 13.915 1.00 10.35 ? 17  VAL   C O   1 
ATOM   1150 C  CB  . VAL   B 1 11  ? 21.767 -24.070 10.967 1.00 11.28 ? 17  VAL   C CB  1 
ATOM   1151 C  CG1 . VAL   B 1 11  ? 20.515 -23.222 10.838 1.00 11.84 ? 17  VAL   C CG1 1 
ATOM   1152 C  CG2 . VAL   B 1 11  ? 22.286 -24.483 9.594  1.00 11.63 ? 17  VAL   C CG2 1 
ATOM   1153 N  N   . VAL   B 1 12  ? 22.131 -21.976 13.713 1.00 8.67  ? 18  VAL   C N   1 
ATOM   1154 C  CA  . VAL   B 1 12  ? 21.697 -21.772 15.097 1.00 9.44  ? 18  VAL   C CA  1 
ATOM   1155 C  C   . VAL   B 1 12  ? 20.480 -20.840 15.129 1.00 8.10  ? 18  VAL   C C   1 
ATOM   1156 O  O   . VAL   B 1 12  ? 20.225 -20.080 14.166 1.00 8.84  ? 18  VAL   C O   1 
ATOM   1157 C  CB  . VAL   B 1 12  ? 22.849 -21.151 15.944 1.00 12.26 ? 18  VAL   C CB  1 
ATOM   1158 C  CG1 . VAL   B 1 12  ? 23.954 -22.168 16.159 1.00 16.86 ? 18  VAL   C CG1 1 
ATOM   1159 C  CG2 . VAL   B 1 12  ? 23.363 -19.849 15.328 1.00 11.56 ? 18  VAL   C CG2 1 
ATOM   1160 N  N   . ASN   B 1 13  ? 19.808 -20.779 16.296 1.00 8.02  ? 19  ASN   C N   1 
ATOM   1161 C  CA  . ASN   B 1 13  ? 18.808 -19.734 16.495 1.00 8.91  ? 19  ASN   C CA  1 
ATOM   1162 C  C   . ASN   B 1 13  ? 19.539 -18.378 16.457 1.00 9.30  ? 19  ASN   C C   1 
ATOM   1163 O  O   . ASN   B 1 13  ? 20.556 -18.190 17.179 1.00 9.37  ? 19  ASN   C O   1 
ATOM   1164 C  CB  . ASN   B 1 13  ? 18.140 -19.825 17.876 1.00 9.01  ? 19  ASN   C CB  1 
ATOM   1165 C  CG  . ASN   B 1 13  ? 17.289 -21.070 18.009 1.00 10.08 ? 19  ASN   C CG  1 
ATOM   1166 O  OD1 . ASN   B 1 13  ? 17.747 -22.122 18.469 1.00 10.49 ? 19  ASN   C OD1 1 
ATOM   1167 N  ND2 . ASN   B 1 13  ? 16.037 -20.997 17.607 1.00 10.10 ? 19  ASN   C ND2 1 
ATOM   1168 N  N   . ARG   B 1 14  ? 19.024 -17.420 15.657 1.00 8.64  ? 20  ARG   C N   1 
ATOM   1169 C  CA  . ARG   B 1 14  ? 19.707 -16.119 15.585 1.00 8.70  ? 20  ARG   C CA  1 
ATOM   1170 C  C   . ARG   B 1 14  ? 19.837 -15.464 16.953 1.00 9.46  ? 20  ARG   C C   1 
ATOM   1171 O  O   . ARG   B 1 14  ? 20.884 -14.867 17.243 1.00 9.83  ? 20  ARG   C O   1 
ATOM   1172 C  CB  . ARG   B 1 14  ? 18.981 -15.198 14.613 1.00 9.00  ? 20  ARG   C CB  1 
ATOM   1173 C  CG  . ARG   B 1 14  ? 19.758 -13.882 14.231 1.00 8.45  ? 20  ARG   C CG  1 
ATOM   1174 C  CD  . ARG   B 1 14  ? 18.797 -13.023 13.448 1.00 10.76 ? 20  ARG   C CD  1 
ATOM   1175 N  NE  . ARG   B 1 14  ? 19.397 -11.767 12.937 1.00 10.83 ? 20  ARG   C NE  1 
ATOM   1176 C  CZ  . ARG   B 1 14  ? 19.446 -10.633 13.616 1.00 11.86 ? 20  ARG   C CZ  1 
ATOM   1177 N  NH1 . ARG   B 1 14  ? 19.110 -10.601 14.893 1.00 13.77 ? 20  ARG   C NH1 1 
ATOM   1178 N  NH2 . ARG   B 1 14  ? 19.921 -9.518  13.035 1.00 12.59 ? 20  ARG   C NH2 1 
ATOM   1179 N  N   . HIS   B 1 15  ? 18.806 -15.593 17.820 1.00 8.32  ? 21  HIS   C N   1 
ATOM   1180 C  CA  . HIS   B 1 15  ? 18.869 -14.953 19.124 1.00 9.52  ? 21  HIS   C CA  1 
ATOM   1181 C  C   . HIS   B 1 15  ? 19.898 -15.584 20.070 1.00 10.39 ? 21  HIS   C C   1 
ATOM   1182 O  O   . HIS   B 1 15  ? 20.221 -14.945 21.088 1.00 11.47 ? 21  HIS   C O   1 
ATOM   1183 C  CB  . HIS   B 1 15  ? 17.480 -14.839 19.767 1.00 10.63 ? 21  HIS   C CB  1 
ATOM   1184 C  CG  . HIS   B 1 15  ? 16.910 -16.121 20.336 1.00 9.81  ? 21  HIS   C CG  1 
ATOM   1185 N  ND1 . HIS   B 1 15  ? 16.213 -17.035 19.558 1.00 10.01 ? 21  HIS   C ND1 1 
ATOM   1186 C  CD2 . HIS   B 1 15  ? 16.898 -16.560 21.625 1.00 10.48 ? 21  HIS   C CD2 1 
ATOM   1187 C  CE1 . HIS   B 1 15  ? 15.794 -18.006 20.392 1.00 10.32 ? 21  HIS   C CE1 1 
ATOM   1188 N  NE2 . HIS   B 1 15  ? 16.171 -17.752 21.656 1.00 11.22 ? 21  HIS   C NE2 1 
ATOM   1189 N  N   . LEU   B 1 16  ? 20.417 -16.773 19.752 1.00 9.60  ? 22  LEU   C N   1 
ATOM   1190 C  CA  . LEU   B 1 16  ? 21.440 -17.446 20.586 1.00 10.74 ? 22  LEU   C CA  1 
ATOM   1191 C  C   . LEU   B 1 16  ? 22.826 -17.423 19.937 1.00 11.49 ? 22  LEU   C C   1 
ATOM   1192 O  O   . LEU   B 1 16  ? 23.766 -18.026 20.476 1.00 12.21 ? 22  LEU   C O   1 
ATOM   1193 C  CB  . LEU   B 1 16  ? 21.002 -18.903 20.883 1.00 11.14 ? 22  LEU   C CB  1 
ATOM   1194 C  CG  . LEU   B 1 16  ? 19.661 -19.004 21.663 1.00 12.35 ? 22  LEU   C CG  1 
ATOM   1195 C  CD1 . LEU   B 1 16  ? 19.279 -20.492 21.900 1.00 13.66 ? 22  LEU   C CD1 1 
ATOM   1196 C  CD2 . LEU   B 1 16  ? 19.737 -18.249 23.043 1.00 12.91 ? 22  LEU   C CD2 1 
ATOM   1197 N  N   . ALA   B 1 17  ? 22.977 -16.733 18.778 1.00 10.72 ? 23  ALA   C N   1 
ATOM   1198 C  CA  . ALA   B 1 17  ? 24.269 -16.716 18.099 1.00 11.45 ? 23  ALA   C CA  1 
ATOM   1199 C  C   . ALA   B 1 17  ? 25.333 -16.075 18.968 1.00 11.84 ? 23  ALA   C C   1 
ATOM   1200 O  O   . ALA   B 1 17  ? 25.066 -15.110 19.684 1.00 12.53 ? 23  ALA   C O   1 
ATOM   1201 C  CB  . ALA   B 1 17  ? 24.145 -15.955 16.775 1.00 11.24 ? 23  ALA   C CB  1 
ATOM   1202 N  N   . THR   B 1 18  ? 26.546 -16.645 18.892 1.00 12.64 ? 24  THR   C N   1 
ATOM   1203 C  CA  . THR   B 1 18  ? 27.681 -16.146 19.690 1.00 12.55 ? 24  THR   C CA  1 
ATOM   1204 C  C   . THR   B 1 18  ? 28.461 -15.047 18.956 1.00 13.10 ? 24  THR   C C   1 
ATOM   1205 O  O   . THR   B 1 18  ? 28.268 -14.847 17.761 1.00 12.86 ? 24  THR   C O   1 
ATOM   1206 C  CB  . THR   B 1 18  ? 28.611 -17.343 20.010 1.00 15.05 ? 24  THR   C CB  1 
ATOM   1207 O  OG1 . THR   B 1 18  ? 29.208 -17.754 18.775 1.00 15.90 ? 24  THR   C OG1 1 
ATOM   1208 C  CG2 . THR   B 1 18  ? 27.896 -18.468 20.714 1.00 16.66 ? 24  THR   C CG2 1 
ATOM   1209 N  N   . HIS   B 1 19  ? 29.478 -14.443 19.635 1.00 14.09 ? 25  HIS   C N   1 
ATOM   1210 C  CA  . HIS   B 1 19  ? 30.352 -13.498 18.937 1.00 14.53 ? 25  HIS   C CA  1 
ATOM   1211 C  C   . HIS   B 1 19  ? 31.066 -14.204 17.757 1.00 13.20 ? 25  HIS   C C   1 
ATOM   1212 O  O   . HIS   B 1 19  ? 31.207 -13.621 16.686 1.00 14.78 ? 25  HIS   C O   1 
ATOM   1213 C  CB  . HIS   B 1 19  ? 31.455 -12.981 19.904 1.00 17.74 ? 25  HIS   C CB  1 
ATOM   1214 C  CG  . HIS   B 1 19  ? 30.947 -12.169 21.051 1.00 25.29 ? 25  HIS   C CG  1 
ATOM   1215 N  ND1 . HIS   B 1 19  ? 30.176 -11.031 20.853 1.00 29.59 ? 25  HIS   C ND1 1 
ATOM   1216 C  CD2 . HIS   B 1 19  ? 31.183 -12.311 22.379 1.00 28.88 ? 25  HIS   C CD2 1 
ATOM   1217 C  CE1 . HIS   B 1 19  ? 29.961 -10.520 22.060 1.00 30.27 ? 25  HIS   C CE1 1 
ATOM   1218 N  NE2 . HIS   B 1 19  ? 30.527 -11.269 23.013 1.00 30.62 ? 25  HIS   C NE2 1 
ATOM   1219 N  N   . ASN   B 1 20  ? 31.476 -15.479 17.972 1.00 13.26 ? 26  ASN   C N   1 
ATOM   1220 C  CA  . ASN   B 1 20  ? 32.153 -16.205 16.887 1.00 14.07 ? 26  ASN   C CA  1 
ATOM   1221 C  C   . ASN   B 1 20  ? 31.234 -16.445 15.703 1.00 13.54 ? 26  ASN   C C   1 
ATOM   1222 O  O   . ASN   B 1 20  ? 31.673 -16.350 14.550 1.00 13.59 ? 26  ASN   C O   1 
ATOM   1223 C  CB  . ASN   B 1 20  ? 32.732 -17.506 17.390 1.00 16.23 ? 26  ASN   C CB  1 
ATOM   1224 C  CG  . ASN   B 1 20  ? 33.589 -18.221 16.363 1.00 22.50 ? 26  ASN   C CG  1 
ATOM   1225 O  OD1 . ASN   B 1 20  ? 34.677 -17.739 16.000 1.00 24.51 ? 26  ASN   C OD1 1 
ATOM   1226 N  ND2 . ASN   B 1 20  ? 33.104 -19.370 15.874 1.00 24.04 ? 26  ASN   C ND2 1 
ATOM   1227 N  N   . ASP   B 1 21  ? 29.929 -16.766 15.964 1.00 12.19 ? 27  ASP   C N   1 
ATOM   1228 C  CA  . ASP   B 1 21  ? 29.002 -16.927 14.842 1.00 12.56 ? 27  ASP   C CA  1 
ATOM   1229 C  C   . ASP   B 1 21  ? 28.890 -15.632 14.014 1.00 12.14 ? 27  ASP   C C   1 
ATOM   1230 O  O   . ASP   B 1 21  ? 28.943 -15.659 12.788 1.00 14.22 ? 27  ASP   C O   1 
ATOM   1231 C  CB  . ASP   B 1 21  ? 27.602 -17.255 15.380 1.00 12.03 ? 27  ASP   C CB  1 
ATOM   1232 C  CG  . ASP   B 1 21  ? 27.463 -18.667 15.912 1.00 13.46 ? 27  ASP   C CG  1 
ATOM   1233 O  OD1 . ASP   B 1 21  ? 28.035 -19.595 15.295 1.00 14.37 ? 27  ASP   C OD1 1 
ATOM   1234 O  OD2 . ASP   B 1 21  ? 26.772 -18.840 16.963 1.00 13.62 ? 27  ASP   C OD2 1 
ATOM   1235 N  N   . TRP   B 1 22  ? 28.754 -14.479 14.692 1.00 12.61 ? 28  TRP   C N   1 
ATOM   1236 C  CA  . TRP   B 1 22  ? 28.643 -13.208 13.990 1.00 13.00 ? 28  TRP   C CA  1 
ATOM   1237 C  C   . TRP   B 1 22  ? 29.957 -12.818 13.262 1.00 14.66 ? 28  TRP   C C   1 
ATOM   1238 O  O   . TRP   B 1 22  ? 29.891 -12.210 12.200 1.00 15.53 ? 28  TRP   C O   1 
ATOM   1239 C  CB  . TRP   B 1 22  ? 28.200 -12.106 14.968 1.00 12.98 ? 28  TRP   C CB  1 
ATOM   1240 C  CG  . TRP   B 1 22  ? 26.713 -12.079 15.144 1.00 10.81 ? 28  TRP   C CG  1 
ATOM   1241 C  CD1 . TRP   B 1 22  ? 26.003 -12.538 16.202 1.00 12.43 ? 28  TRP   C CD1 1 
ATOM   1242 C  CD2 . TRP   B 1 22  ? 25.763 -11.484 14.232 1.00 11.32 ? 28  TRP   C CD2 1 
ATOM   1243 N  NE1 . TRP   B 1 22  ? 24.656 -12.292 16.000 1.00 12.79 ? 28  TRP   C NE1 1 
ATOM   1244 C  CE2 . TRP   B 1 22  ? 24.487 -11.658 14.792 1.00 11.53 ? 28  TRP   C CE2 1 
ATOM   1245 C  CE3 . TRP   B 1 22  ? 25.875 -10.827 13.005 1.00 13.03 ? 28  TRP   C CE3 1 
ATOM   1246 C  CZ2 . TRP   B 1 22  ? 23.322 -11.151 14.173 1.00 11.73 ? 28  TRP   C CZ2 1 
ATOM   1247 C  CZ3 . TRP   B 1 22  ? 24.719 -10.377 12.374 1.00 14.03 ? 28  TRP   C CZ3 1 
ATOM   1248 C  CH2 . TRP   B 1 22  ? 23.461 -10.585 12.943 1.00 13.19 ? 28  TRP   C CH2 1 
ATOM   1249 N  N   . ALA   B 1 23  ? 31.100 -13.229 13.786 1.00 14.22 ? 29  ALA   C N   1 
ATOM   1250 C  CA  . ALA   B 1 23  ? 32.384 -12.900 13.131 1.00 15.63 ? 29  ALA   C CA  1 
ATOM   1251 C  C   . ALA   B 1 23  ? 32.615 -13.787 11.882 1.00 16.66 ? 29  ALA   C C   1 
ATOM   1252 O  O   . ALA   B 1 23  ? 33.545 -13.536 11.103 1.00 17.78 ? 29  ALA   C O   1 
ATOM   1253 C  CB  . ALA   B 1 23  ? 33.519 -13.141 14.111 1.00 15.81 ? 29  ALA   C CB  1 
ATOM   1254 N  N   . ASN   B 1 24  ? 31.894 -14.927 11.796 1.00 14.69 ? 30  ASN   C N   1 
ATOM   1255 C  CA  . ASN   B 1 24  ? 32.025 -15.869 10.679 1.00 14.10 ? 30  ASN   C CA  1 
ATOM   1256 C  C   . ASN   B 1 24  ? 30.661 -16.010 9.981  1.00 13.72 ? 30  ASN   C C   1 
ATOM   1257 O  O   . ASN   B 1 24  ? 30.285 -17.083 9.529  1.00 13.34 ? 30  ASN   C O   1 
ATOM   1258 C  CB  . ASN   B 1 24  ? 32.533 -17.224 11.192 1.00 14.82 ? 30  ASN   C CB  1 
ATOM   1259 C  CG  . ASN   B 1 24  ? 33.962 -17.114 11.677 1.00 18.95 ? 30  ASN   C CG  1 
ATOM   1260 O  OD1 . ASN   B 1 24  ? 34.890 -17.064 10.860 1.00 19.10 ? 30  ASN   C OD1 1 
ATOM   1261 N  ND2 . ASN   B 1 24  ? 34.148 -17.002 12.998 1.00 17.88 ? 30  ASN   C ND2 1 
ATOM   1262 N  N   . LEU   B 1 25  ? 29.964 -14.915 9.875  1.00 14.28 ? 31  LEU   C N   1 
ATOM   1263 C  CA  . LEU   B 1 25  ? 28.616 -14.863 9.331  1.00 13.57 ? 31  LEU   C CA  1 
ATOM   1264 C  C   . LEU   B 1 25  ? 28.497 -15.245 7.854  1.00 14.18 ? 31  LEU   C C   1 
ATOM   1265 O  O   . LEU   B 1 25  ? 29.196 -14.688 7.009  1.00 16.66 ? 31  LEU   C O   1 
ATOM   1266 C  CB  . LEU   B 1 25  ? 28.066 -13.444 9.572  1.00 13.00 ? 31  LEU   C CB  1 
ATOM   1267 C  CG  . LEU   B 1 25  ? 26.641 -13.232 9.047  1.00 14.44 ? 31  LEU   C CG  1 
ATOM   1268 C  CD1 . LEU   B 1 25  ? 25.640 -14.116 9.847  1.00 14.67 ? 31  LEU   C CD1 1 
ATOM   1269 C  CD2 . LEU   B 1 25  ? 26.248 -11.770 9.163  1.00 14.73 ? 31  LEU   C CD2 1 
ATOM   1270 N  N   . VAL   B 1 26  ? 27.543 -16.137 7.514  1.00 13.21 ? 32  VAL   C N   1 
ATOM   1271 C  CA  . VAL   B 1 26  ? 27.260 -16.495 6.130  1.00 13.72 ? 32  VAL   C CA  1 
ATOM   1272 C  C   . VAL   B 1 26  ? 25.919 -15.851 5.748  1.00 14.66 ? 32  VAL   C C   1 
ATOM   1273 O  O   . VAL   B 1 26  ? 25.805 -15.209 4.698  1.00 16.58 ? 32  VAL   C O   1 
ATOM   1274 C  CB  . VAL   B 1 26  ? 27.191 -18.034 5.958  1.00 14.47 ? 32  VAL   C CB  1 
ATOM   1275 C  CG1 . VAL   B 1 26  ? 26.658 -18.416 4.559  1.00 16.35 ? 32  VAL   C CG1 1 
ATOM   1276 C  CG2 . VAL   B 1 26  ? 28.569 -18.652 6.223  1.00 15.55 ? 32  VAL   C CG2 1 
ATOM   1277 N  N   . TRP   B 1 27  ? 24.894 -16.028 6.603  1.00 12.27 ? 33  TRP   C N   1 
ATOM   1278 C  CA  . TRP   B 1 27  ? 23.550 -15.526 6.296  1.00 12.23 ? 33  TRP   C CA  1 
ATOM   1279 C  C   . TRP   B 1 27  ? 22.787 -15.429 7.613  1.00 11.61 ? 33  TRP   C C   1 
ATOM   1280 O  O   . TRP   B 1 27  ? 22.965 -16.292 8.492  1.00 12.55 ? 33  TRP   C O   1 
ATOM   1281 C  CB  . TRP   B 1 27  ? 22.845 -16.509 5.317  1.00 13.54 ? 33  TRP   C CB  1 
ATOM   1282 C  CG  . TRP   B 1 27  ? 21.351 -16.302 5.122  1.00 13.59 ? 33  TRP   C CG  1 
ATOM   1283 C  CD1 . TRP   B 1 27  ? 20.733 -15.427 4.271  1.00 16.05 ? 33  TRP   C CD1 1 
ATOM   1284 C  CD2 . TRP   B 1 27  ? 20.302 -17.039 5.769  1.00 12.28 ? 33  TRP   C CD2 1 
ATOM   1285 N  NE1 . TRP   B 1 27  ? 19.355 -15.541 4.402  1.00 16.74 ? 33  TRP   C NE1 1 
ATOM   1286 C  CE2 . TRP   B 1 27  ? 19.070 -16.547 5.289  1.00 14.38 ? 33  TRP   C CE2 1 
ATOM   1287 C  CE3 . TRP   B 1 27  ? 20.284 -18.042 6.752  1.00 12.66 ? 33  TRP   C CE3 1 
ATOM   1288 C  CZ2 . TRP   B 1 27  ? 17.832 -17.081 5.719  1.00 14.57 ? 33  TRP   C CZ2 1 
ATOM   1289 C  CZ3 . TRP   B 1 27  ? 19.069 -18.576 7.153  1.00 12.87 ? 33  TRP   C CZ3 1 
ATOM   1290 C  CH2 . TRP   B 1 27  ? 17.862 -18.091 6.646  1.00 12.69 ? 33  TRP   C CH2 1 
ATOM   1291 N  N   . GLU   B 1 28  ? 21.894 -14.452 7.748  1.00 11.72 ? 34  GLU   C N   1 
ATOM   1292 C  CA  . GLU   B 1 28  ? 21.019 -14.379 8.906  1.00 12.29 ? 34  GLU   C CA  1 
ATOM   1293 C  C   . GLU   B 1 28  ? 19.697 -13.776 8.489  1.00 11.94 ? 34  GLU   C C   1 
ATOM   1294 O  O   . GLU   B 1 28  ? 19.652 -12.956 7.551  1.00 11.94 ? 34  GLU   C O   1 
ATOM   1295 C  CB  . GLU   B 1 28  ? 21.650 -13.653 10.105 1.00 12.75 ? 34  GLU   C CB  1 
ATOM   1296 C  CG  . GLU   B 1 28  ? 22.206 -12.260 9.813  1.00 14.19 ? 34  GLU   C CG  1 
ATOM   1297 C  CD  . GLU   B 1 28  ? 21.209 -11.132 9.646  1.00 16.36 ? 34  GLU   C CD  1 
ATOM   1298 O  OE1 . GLU   B 1 28  ? 21.499 -10.190 8.863  1.00 18.01 ? 34  GLU   C OE1 1 
ATOM   1299 O  OE2 . GLU   B 1 28  ? 20.169 -11.116 10.337 1.00 13.55 ? 34  GLU   C OE2 1 
ATOM   1300 N  N   . ASP   B 1 29  ? 18.616 -14.138 9.191  1.00 11.19 ? 35  ASP   C N   1 
ATOM   1301 C  CA  . ASP   B 1 29  ? 17.295 -13.600 8.883  1.00 10.29 ? 35  ASP   C CA  1 
ATOM   1302 C  C   . ASP   B 1 29  ? 16.519 -13.452 10.185 1.00 9.89  ? 35  ASP   C C   1 
ATOM   1303 O  O   . ASP   B 1 29  ? 16.107 -14.473 10.783 1.00 10.29 ? 35  ASP   C O   1 
ATOM   1304 C  CB  . ASP   B 1 29  ? 16.609 -14.466 7.827  1.00 11.25 ? 35  ASP   C CB  1 
ATOM   1305 C  CG  . ASP   B 1 29  ? 15.265 -13.988 7.380  1.00 14.93 ? 35  ASP   C CG  1 
ATOM   1306 O  OD1 . ASP   B 1 29  ? 14.596 -13.341 8.163  1.00 18.07 ? 35  ASP   C OD1 1 
ATOM   1307 O  OD2 . ASP   B 1 29  ? 14.871 -14.326 6.248  1.00 15.68 ? 35  ASP   C OD2 1 
ATOM   1308 N  N   . SER   B 1 30  ? 16.329 -12.206 10.657 1.00 9.89  ? 36  SER   C N   1 
ATOM   1309 C  CA  A SER   B 1 30  ? 15.632 -11.952 11.890 0.50 10.21 ? 36  SER   C CA  1 
ATOM   1310 C  CA  B SER   B 1 30  ? 15.614 -11.989 11.911 0.50 9.99  ? 36  SER   C CA  1 
ATOM   1311 C  C   . SER   B 1 30  ? 14.169 -12.449 11.810 1.00 10.90 ? 36  SER   C C   1 
ATOM   1312 O  O   . SER   B 1 30  ? 13.629 -12.916 12.819 1.00 11.01 ? 36  SER   C O   1 
ATOM   1313 C  CB  A SER   B 1 30  ? 15.681 -10.452 12.169 0.50 13.25 ? 36  SER   C CB  1 
ATOM   1314 C  CB  B SER   B 1 30  ? 15.612 -10.514 12.313 0.50 12.42 ? 36  SER   C CB  1 
ATOM   1315 O  OG  A SER   B 1 30  ? 14.989 -10.112 13.348 0.50 17.42 ? 36  SER   C OG  1 
ATOM   1316 O  OG  B SER   B 1 30  ? 16.898 -10.006 12.591 0.50 16.69 ? 36  SER   C OG  1 
ATOM   1317 N  N   . SER   B 1 31  ? 13.551 -12.329 10.622 1.00 9.82  ? 37  SER   C N   1 
ATOM   1318 C  CA  . SER   B 1 31  ? 12.155 -12.764 10.507 1.00 9.64  ? 37  SER   C CA  1 
ATOM   1319 C  C   . SER   B 1 31  ? 12.026 -14.280 10.698 1.00 10.25 ? 37  SER   C C   1 
ATOM   1320 O  O   . SER   B 1 31  ? 10.919 -14.709 11.011 1.00 12.12 ? 37  SER   C O   1 
ATOM   1321 C  CB  . SER   B 1 31  ? 11.535 -12.345 9.183  1.00 13.36 ? 37  SER   C CB  1 
ATOM   1322 O  OG  . SER   B 1 31  ? 11.990 -13.125 8.096  1.00 18.51 ? 37  SER   C OG  1 
ATOM   1323 N  N   . ARG   B 1 32  ? 13.083 -15.049 10.527 1.00 8.24  ? 38  ARG   C N   1 
ATOM   1324 C  CA  . ARG   B 1 32  ? 13.038 -16.515 10.700 1.00 8.25  ? 38  ARG   C CA  1 
ATOM   1325 C  C   . ARG   B 1 32  ? 13.670 -16.988 12.010 1.00 8.24  ? 38  ARG   C C   1 
ATOM   1326 O  O   . ARG   B 1 32  ? 13.664 -18.181 12.301 1.00 8.40  ? 38  ARG   C O   1 
ATOM   1327 C  CB  . ARG   B 1 32  ? 13.796 -17.201 9.523  1.00 8.91  ? 38  ARG   C CB  1 
ATOM   1328 C  CG  . ARG   B 1 32  ? 13.080 -16.973 8.175  1.00 10.29 ? 38  ARG   C CG  1 
ATOM   1329 C  CD  . ARG   B 1 32  ? 13.780 -17.595 6.975  1.00 9.27  ? 38  ARG   C CD  1 
ATOM   1330 N  NE  . ARG   B 1 32  ? 13.759 -19.050 7.085  1.00 8.78  ? 38  ARG   C NE  1 
ATOM   1331 C  CZ  . ARG   B 1 32  ? 13.814 -19.888 6.042  1.00 9.95  ? 38  ARG   C CZ  1 
ATOM   1332 N  NH1 . ARG   B 1 32  ? 13.890 -19.421 4.804  1.00 11.29 ? 38  ARG   C NH1 1 
ATOM   1333 N  NH2 . ARG   B 1 32  ? 13.751 -21.203 6.235  1.00 9.99  ? 38  ARG   C NH2 1 
ATOM   1334 N  N   . ASP   B 1 33  ? 14.340 -16.098 12.734 1.00 8.71  ? 39  ASP   C N   1 
ATOM   1335 C  CA  . ASP   B 1 33  ? 15.158 -16.446 13.904 1.00 8.23  ? 39  ASP   C CA  1 
ATOM   1336 C  C   . ASP   B 1 33  ? 16.272 -17.434 13.530 1.00 8.07  ? 39  ASP   C C   1 
ATOM   1337 O  O   . ASP   B 1 33  ? 16.603 -18.330 14.339 1.00 8.47  ? 39  ASP   C O   1 
ATOM   1338 C  CB  . ASP   B 1 33  ? 14.322 -17.015 15.089 1.00 8.38  ? 39  ASP   C CB  1 
ATOM   1339 C  CG  . ASP   B 1 33  ? 15.121 -17.288 16.365 1.00 8.16  ? 39  ASP   C CG  1 
ATOM   1340 O  OD1 . ASP   B 1 33  ? 15.996 -16.456 16.728 1.00 10.07 ? 39  ASP   C OD1 1 
ATOM   1341 O  OD2 . ASP   B 1 33  ? 14.880 -18.349 17.032 1.00 9.71  ? 39  ASP   C OD2 1 
ATOM   1342 N  N   . LEU   B 1 34  ? 16.875 -17.274 12.327 1.00 8.00  ? 40  LEU   C N   1 
ATOM   1343 C  CA  . LEU   B 1 34  ? 17.984 -18.159 11.948 1.00 8.59  ? 40  LEU   C CA  1 
ATOM   1344 C  C   . LEU   B 1 34  ? 19.255 -17.397 11.646 1.00 9.01  ? 40  LEU   C C   1 
ATOM   1345 O  O   . LEU   B 1 34  ? 19.234 -16.288 11.104 1.00 9.30  ? 40  LEU   C O   1 
ATOM   1346 C  CB  . LEU   B 1 34  ? 17.667 -18.977 10.695 1.00 9.54  ? 40  LEU   C CB  1 
ATOM   1347 C  CG  . LEU   B 1 34  ? 16.589 -20.054 10.857 1.00 9.98  ? 40  LEU   C CG  1 
ATOM   1348 C  CD1 . LEU   B 1 34  ? 16.412 -20.758 9.485  1.00 10.58 ? 40  LEU   C CD1 1 
ATOM   1349 C  CD2 . LEU   B 1 34  ? 16.995 -21.091 11.913 1.00 10.35 ? 40  LEU   C CD2 1 
ATOM   1350 N  N   . LEU   B 1 35  ? 20.386 -18.033 11.977 1.00 8.75  ? 41  LEU   C N   1 
ATOM   1351 C  CA  . LEU   B 1 35  ? 21.711 -17.510 11.599 1.00 8.90  ? 41  LEU   C CA  1 
ATOM   1352 C  C   . LEU   B 1 35  ? 22.579 -18.713 11.210 1.00 8.66  ? 41  LEU   C C   1 
ATOM   1353 O  O   . LEU   B 1 35  ? 22.495 -19.781 11.835 1.00 9.34  ? 41  LEU   C O   1 
ATOM   1354 C  CB  . LEU   B 1 35  ? 22.332 -16.662 12.705 1.00 10.01 ? 41  LEU   C CB  1 
ATOM   1355 C  CG  . LEU   B 1 35  ? 23.724 -16.038 12.422 1.00 10.30 ? 41  LEU   C CG  1 
ATOM   1356 C  CD1 . LEU   B 1 35  ? 23.875 -14.687 13.168 1.00 11.32 ? 41  LEU   C CD1 1 
ATOM   1357 C  CD2 . LEU   B 1 35  ? 24.883 -17.014 12.822 1.00 10.97 ? 41  LEU   C CD2 1 
ATOM   1358 N  N   . VAL   B 1 36  ? 23.356 -18.546 10.143 1.00 9.33  ? 42  VAL   C N   1 
ATOM   1359 C  CA  . VAL   B 1 36  ? 24.294 -19.580 9.646  1.00 9.28  ? 42  VAL   C CA  1 
ATOM   1360 C  C   . VAL   B 1 36  ? 25.706 -18.959 9.648  1.00 10.47 ? 42  VAL   C C   1 
ATOM   1361 O  O   . VAL   B 1 36  ? 25.922 -17.861 9.092  1.00 11.53 ? 42  VAL   C O   1 
ATOM   1362 C  CB  . VAL   B 1 36  ? 23.911 -20.047 8.224  1.00 9.53  ? 42  VAL   C CB  1 
ATOM   1363 C  CG1 . VAL   B 1 36  ? 24.924 -21.076 7.689  1.00 12.13 ? 42  VAL   C CG1 1 
ATOM   1364 C  CG2 . VAL   B 1 36  ? 22.493 -20.658 8.245  1.00 10.46 ? 42  VAL   C CG2 1 
ATOM   1365 N  N   . SER   B 1 37  ? 26.629 -19.650 10.283 1.00 10.59 ? 43  SER   C N   1 
ATOM   1366 C  CA  . SER   B 1 37  ? 28.046 -19.248 10.307 1.00 11.32 ? 43  SER   C CA  1 
ATOM   1367 C  C   . SER   B 1 37  ? 28.913 -20.342 9.652  1.00 12.60 ? 43  SER   C C   1 
ATOM   1368 O  O   . SER   B 1 37  ? 28.482 -21.483 9.465  1.00 13.18 ? 43  SER   C O   1 
ATOM   1369 C  CB  . SER   B 1 37  ? 28.488 -18.994 11.736 1.00 12.64 ? 43  SER   C CB  1 
ATOM   1370 O  OG  . SER   B 1 37  ? 28.339 -20.138 12.575 1.00 13.15 ? 43  SER   C OG  1 
ATOM   1371 N  N   . SER   B 1 38  ? 30.154 -19.967 9.281  1.00 14.06 ? 44  SER   C N   1 
ATOM   1372 C  CA  . SER   B 1 38  ? 31.046 -20.922 8.647  1.00 15.09 ? 44  SER   C CA  1 
ATOM   1373 C  C   . SER   B 1 38  ? 31.918 -21.648 9.687  1.00 17.72 ? 44  SER   C C   1 
ATOM   1374 O  O   . SER   B 1 38  ? 32.241 -21.101 10.755 1.00 18.62 ? 44  SER   C O   1 
ATOM   1375 C  CB  . SER   B 1 38  ? 31.912 -20.208 7.618  1.00 17.90 ? 44  SER   C CB  1 
ATOM   1376 O  OG  . SER   B 1 38  ? 32.658 -19.205 8.271  1.00 21.11 ? 44  SER   C OG  1 
ATOM   1377 N  N   . THR   B 1 39  ? 32.249 -22.908 9.378  1.00 18.75 ? 45  THR   C N   1 
ATOM   1378 C  CA  . THR   B 1 39  ? 33.064 -23.759 10.263 1.00 21.99 ? 45  THR   C CA  1 
ATOM   1379 C  C   . THR   B 1 39  ? 34.299 -24.268 9.502  1.00 25.66 ? 45  THR   C C   1 
ATOM   1380 O  O   . THR   B 1 39  ? 34.307 -24.283 8.271  1.00 26.18 ? 45  THR   C O   1 
ATOM   1381 C  CB  . THR   B 1 39  ? 32.230 -24.997 10.711 1.00 22.81 ? 45  THR   C CB  1 
ATOM   1382 O  OG1 . THR   B 1 39  ? 32.024 -25.847 9.585  1.00 23.51 ? 45  THR   C OG1 1 
ATOM   1383 C  CG2 . THR   B 1 39  ? 30.874 -24.635 11.301 1.00 23.60 ? 45  THR   C CG2 1 
ATOM   1384 N  N   . THR   B 1 40  ? 35.323 -24.715 10.234 1.00 28.26 ? 46  THR   C N   1 
ATOM   1385 C  CA  . THR   B 1 40  ? 36.496 -25.325 9.609  1.00 30.81 ? 46  THR   C CA  1 
ATOM   1386 C  C   . THR   B 1 40  ? 36.274 -26.843 9.461  1.00 32.05 ? 46  THR   C C   1 
ATOM   1387 O  O   . THR   B 1 40  ? 36.717 -27.430 8.473  1.00 34.15 ? 46  THR   C O   1 
ATOM   1388 C  CB  . THR   B 1 40  ? 37.769 -24.996 10.398 1.00 33.72 ? 46  THR   C CB  1 
ATOM   1389 O  OG1 . THR   B 1 40  ? 37.540 -25.295 11.773 1.00 36.91 ? 46  THR   C OG1 1 
ATOM   1390 C  CG2 . THR   B 1 40  ? 38.164 -23.530 10.276 1.00 34.31 ? 46  THR   C CG2 1 
ATOM   1391 N  N   . ALA   B 1 41  ? 35.582 -27.479 10.421 1.00 30.83 ? 47  ALA   C N   1 
ATOM   1392 C  CA  . ALA   B 1 41  ? 35.325 -28.920 10.377 1.00 30.66 ? 47  ALA   C CA  1 
ATOM   1393 C  C   . ALA   B 1 41  ? 34.080 -29.265 9.559  1.00 29.96 ? 47  ALA   C C   1 
ATOM   1394 O  O   . ALA   B 1 41  ? 33.142 -28.475 9.507  1.00 30.60 ? 47  ALA   C O   1 
ATOM   1395 C  CB  . ALA   B 1 41  ? 35.173 -29.470 11.788 1.00 31.30 ? 47  ALA   C CB  1 
ATOM   1396 N  N   . GLN   B 1 42  ? 34.054 -30.455 8.966  1.00 29.04 ? 48  GLN   C N   1 
ATOM   1397 C  CA  . GLN   B 1 42  ? 32.938 -30.912 8.133  1.00 28.48 ? 48  GLN   C CA  1 
ATOM   1398 C  C   . GLN   B 1 42  ? 31.812 -31.433 9.017  1.00 26.81 ? 48  GLN   C C   1 
ATOM   1399 O  O   . GLN   B 1 42  ? 32.028 -32.257 9.896  1.00 28.29 ? 48  GLN   C O   1 
ATOM   1400 C  CB  . GLN   B 1 42  ? 33.435 -32.018 7.180  1.00 31.53 ? 48  GLN   C CB  1 
ATOM   1401 C  CG  . GLN   B 1 42  ? 32.346 -32.706 6.361  1.00 36.43 ? 48  GLN   C CG  1 
ATOM   1402 C  CD  . GLN   B 1 42  ? 31.909 -31.914 5.148  1.00 43.38 ? 48  GLN   C CD  1 
ATOM   1403 O  OE1 . GLN   B 1 42  ? 32.552 -30.939 4.737  1.00 45.77 ? 48  GLN   C OE1 1 
ATOM   1404 N  NE2 . GLN   B 1 42  ? 30.805 -32.329 4.537  1.00 44.87 ? 48  GLN   C NE2 1 
ATOM   1405 N  N   . GLY   B 1 43  ? 30.601 -30.940 8.790  1.00 22.35 ? 49  GLY   C N   1 
ATOM   1406 C  CA  . GLY   B 1 43  ? 29.432 -31.377 9.556  1.00 20.43 ? 49  GLY   C CA  1 
ATOM   1407 C  C   . GLY   B 1 43  ? 28.744 -32.498 8.806  1.00 19.51 ? 49  GLY   C C   1 
ATOM   1408 O  O   . GLY   B 1 43  ? 28.700 -32.484 7.564  1.00 20.49 ? 49  GLY   C O   1 
ATOM   1409 N  N   . CYS   B 1 44  ? 28.161 -33.404 9.537  1.00 16.95 ? 50  CYS   C N   1 
ATOM   1410 C  CA  . CYS   B 1 44  ? 27.563 -34.599 8.949  1.00 17.51 ? 50  CYS   C CA  1 
ATOM   1411 C  C   . CYS   B 1 44  ? 26.050 -34.720 9.099  1.00 16.46 ? 50  CYS   C C   1 
ATOM   1412 O  O   . CYS   B 1 44  ? 25.523 -35.837 8.903  1.00 18.00 ? 50  CYS   C O   1 
ATOM   1413 C  CB  . CYS   B 1 44  ? 28.254 -35.861 9.460  1.00 19.34 ? 50  CYS   C CB  1 
ATOM   1414 S  SG  . CYS   B 1 44  ? 30.037 -35.907 9.154  1.00 23.03 ? 50  CYS   C SG  1 
ATOM   1415 N  N   . ASP   B 1 45  ? 25.323 -33.640 9.441  1.00 13.27 ? 51  ASP   C N   1 
ATOM   1416 C  CA  . ASP   B 1 45  ? 23.857 -33.761 9.529  1.00 13.62 ? 51  ASP   C CA  1 
ATOM   1417 C  C   . ASP   B 1 45  ? 23.278 -33.786 8.126  1.00 14.75 ? 51  ASP   C C   1 
ATOM   1418 O  O   . ASP   B 1 45  ? 23.748 -33.071 7.220  1.00 17.05 ? 51  ASP   C O   1 
ATOM   1419 C  CB  . ASP   B 1 45  ? 23.248 -32.577 10.317 1.00 13.96 ? 51  ASP   C CB  1 
ATOM   1420 C  CG  . ASP   B 1 45  ? 23.621 -32.590 11.800 1.00 17.88 ? 51  ASP   C CG  1 
ATOM   1421 O  OD1 . ASP   B 1 45  ? 24.002 -33.676 12.321 1.00 20.60 ? 51  ASP   C OD1 1 
ATOM   1422 O  OD2 . ASP   B 1 45  ? 23.528 -31.521 12.459 1.00 17.91 ? 51  ASP   C OD2 1 
ATOM   1423 N  N   . THR   B 1 46  ? 22.270 -34.606 7.928  1.00 14.15 ? 52  THR   C N   1 
ATOM   1424 C  CA  . THR   B 1 46  ? 21.566 -34.656 6.643  1.00 14.89 ? 52  THR   C CA  1 
ATOM   1425 C  C   . THR   B 1 46  ? 20.322 -33.768 6.792  1.00 12.72 ? 52  THR   C C   1 
ATOM   1426 O  O   . THR   B 1 46  ? 19.564 -33.986 7.734  1.00 13.87 ? 52  THR   C O   1 
ATOM   1427 C  CB  . THR   B 1 46  ? 21.108 -36.110 6.326  1.00 18.89 ? 52  THR   C CB  1 
ATOM   1428 O  OG1 . THR   B 1 46  ? 22.275 -36.910 5.961  1.00 22.16 ? 52  THR   C OG1 1 
ATOM   1429 C  CG2 . THR   B 1 46  ? 20.089 -36.166 5.169  1.00 20.63 ? 52  THR   C CG2 1 
ATOM   1430 N  N   . ILE   B 1 47  ? 20.104 -32.842 5.867  1.00 12.29 ? 53  ILE   C N   1 
ATOM   1431 C  CA  . ILE   B 1 47  ? 18.922 -31.992 5.860  1.00 11.13 ? 53  ILE   C CA  1 
ATOM   1432 C  C   . ILE   B 1 47  ? 17.781 -32.653 5.070  1.00 10.47 ? 53  ILE   C C   1 
ATOM   1433 O  O   . ILE   B 1 47  ? 17.991 -33.087 3.921  1.00 10.88 ? 53  ILE   C O   1 
ATOM   1434 C  CB  . ILE   B 1 47  ? 19.207 -30.618 5.239  1.00 13.04 ? 53  ILE   C CB  1 
ATOM   1435 C  CG1 . ILE   B 1 47  ? 20.448 -29.935 5.872  1.00 15.19 ? 53  ILE   C CG1 1 
ATOM   1436 C  CG2 . ILE   B 1 47  ? 17.956 -29.695 5.377  1.00 12.99 ? 53  ILE   C CG2 1 
ATOM   1437 C  CD1 . ILE   B 1 47  ? 20.292 -29.706 7.379  1.00 17.68 ? 53  ILE   C CD1 1 
ATOM   1438 N  N   . ALA   B 1 48  ? 16.586 -32.730 5.648  1.00 9.33  ? 54  ALA   C N   1 
ATOM   1439 C  CA  . ALA   B 1 48  ? 15.441 -33.269 4.937  1.00 9.62  ? 54  ALA   C CA  1 
ATOM   1440 C  C   . ALA   B 1 48  ? 15.036 -32.338 3.785  1.00 8.62  ? 54  ALA   C C   1 
ATOM   1441 O  O   . ALA   B 1 48  ? 15.042 -31.113 3.928  1.00 8.74  ? 54  ALA   C O   1 
ATOM   1442 C  CB  . ALA   B 1 48  ? 14.283 -33.374 5.929  1.00 9.29  ? 54  ALA   C CB  1 
ATOM   1443 N  N   . ARG   B 1 49  ? 14.602 -32.941 2.666  1.00 7.86  ? 55  ARG   C N   1 
ATOM   1444 C  CA  . ARG   B 1 49  ? 14.109 -32.158 1.503  1.00 8.48  ? 55  ARG   C CA  1 
ATOM   1445 C  C   . ARG   B 1 49  ? 12.768 -32.813 1.165  1.00 8.82  ? 55  ARG   C C   1 
ATOM   1446 O  O   . ARG   B 1 49  ? 12.705 -33.821 0.423  1.00 9.38  ? 55  ARG   C O   1 
ATOM   1447 C  CB  . ARG   B 1 49  ? 15.090 -32.218 0.316  1.00 9.36  ? 55  ARG   C CB  1 
ATOM   1448 C  CG  . ARG   B 1 49  ? 16.495 -31.732 0.676  1.00 10.06 ? 55  ARG   C CG  1 
ATOM   1449 C  CD  . ARG   B 1 49  ? 16.535 -30.242 1.074  1.00 11.14 ? 55  ARG   C CD  1 
ATOM   1450 N  NE  . ARG   B 1 49  ? 17.942 -29.820 1.313  1.00 11.96 ? 55  ARG   C NE  1 
ATOM   1451 C  CZ  . ARG   B 1 49  ? 18.284 -28.701 1.940  1.00 13.86 ? 55  ARG   C CZ  1 
ATOM   1452 N  NH1 . ARG   B 1 49  ? 17.355 -27.868 2.374  1.00 12.10 ? 55  ARG   C NH1 1 
ATOM   1453 N  NH2 . ARG   B 1 49  ? 19.572 -28.422 2.170  1.00 14.91 ? 55  ARG   C NH2 1 
ATOM   1454 N  N   . CYS   B 1 50  ? 11.699 -32.296 1.782  1.00 8.09  ? 56  CYS   C N   1 
ATOM   1455 C  CA  . CYS   B 1 50  ? 10.404 -32.977 1.806  1.00 8.59  ? 56  CYS   C CA  1 
ATOM   1456 C  C   . CYS   B 1 50  ? 9.292  -32.031 2.311  1.00 9.70  ? 56  CYS   C C   1 
ATOM   1457 O  O   . CYS   B 1 50  ? 9.575  -30.916 2.754  1.00 9.37  ? 56  CYS   C O   1 
ATOM   1458 C  CB  . CYS   B 1 50  ? 10.516 -34.174 2.761  1.00 9.40  ? 56  CYS   C CB  1 
ATOM   1459 S  SG  . CYS   B 1 50  ? 10.670 -33.695 4.517  1.00 8.96  ? 56  CYS   C SG  1 
ATOM   1460 N  N   . ASP   B 1 51  ? 8.028  -32.554 2.326  1.00 9.99  ? 57  ASP   C N   1 
ATOM   1461 C  CA  . ASP   B 1 51  ? 6.890  -31.852 2.919  1.00 10.28 ? 57  ASP   C CA  1 
ATOM   1462 C  C   . ASP   B 1 51  ? 6.296  -32.632 4.098  1.00 10.10 ? 57  ASP   C C   1 
ATOM   1463 O  O   . ASP   B 1 51  ? 5.103  -32.524 4.388  1.00 10.55 ? 57  ASP   C O   1 
ATOM   1464 C  CB  . ASP   B 1 51  ? 5.827  -31.496 1.866  1.00 13.51 ? 57  ASP   C CB  1 
ATOM   1465 C  CG  . ASP   B 1 51  ? 5.181  -32.701 1.237  1.00 16.29 ? 57  ASP   C CG  1 
ATOM   1466 O  OD1 . ASP   B 1 51  ? 5.537  -33.860 1.596  1.00 17.11 ? 57  ASP   C OD1 1 
ATOM   1467 O  OD2 . ASP   B 1 51  ? 4.256  -32.505 0.379  1.00 22.86 ? 57  ASP   C OD2 1 
ATOM   1468 N  N   . CYS   B 1 52  ? 7.115  -33.427 4.802  1.00 8.86  ? 58  CYS   C N   1 
ATOM   1469 C  CA  . CYS   B 1 52  ? 6.617  -34.131 6.013  1.00 8.90  ? 58  CYS   C CA  1 
ATOM   1470 C  C   . CYS   B 1 52  ? 5.967  -33.177 6.993  1.00 8.14  ? 58  CYS   C C   1 
ATOM   1471 O  O   . CYS   B 1 52  ? 6.370  -32.022 7.184  1.00 7.99  ? 58  CYS   C O   1 
ATOM   1472 C  CB  . CYS   B 1 52  ? 7.760  -34.856 6.727  1.00 8.59  ? 58  CYS   C CB  1 
ATOM   1473 S  SG  . CYS   B 1 52  ? 8.327  -36.349 5.866  1.00 10.08 ? 58  CYS   C SG  1 
ATOM   1474 N  N   . GLN   B 1 53  ? 4.942  -33.742 7.668  1.00 7.92  ? 59  GLN   C N   1 
ATOM   1475 C  CA  . GLN   B 1 53  ? 4.239  -33.098 8.800  1.00 8.21  ? 59  GLN   C CA  1 
ATOM   1476 C  C   . GLN   B 1 53  ? 4.228  -34.025 10.022 1.00 8.78  ? 59  GLN   C C   1 
ATOM   1477 O  O   . GLN   B 1 53  ? 3.448  -33.787 10.979 1.00 8.75  ? 59  GLN   C O   1 
ATOM   1478 C  CB  . GLN   B 1 53  ? 2.799  -32.695 8.431  1.00 7.70  ? 59  GLN   C CB  1 
ATOM   1479 C  CG  . GLN   B 1 53  ? 2.800  -31.447 7.537  1.00 9.50  ? 59  GLN   C CG  1 
ATOM   1480 C  CD  . GLN   B 1 53  ? 1.399  -31.043 7.241  1.00 10.78 ? 59  GLN   C CD  1 
ATOM   1481 O  OE1 . GLN   B 1 53  ? 0.893  -31.229 6.118  1.00 13.26 ? 59  GLN   C OE1 1 
ATOM   1482 N  NE2 . GLN   B 1 53  ? 0.712  -30.511 8.259  1.00 10.67 ? 59  GLN   C NE2 1 
ATOM   1483 N  N   . THR   B 1 54  ? 5.127  -35.034 10.071 1.00 8.48  ? 60  THR   C N   1 
ATOM   1484 C  CA  . THR   B 1 54  ? 5.273  -35.874 11.274 1.00 9.49  ? 60  THR   C CA  1 
ATOM   1485 C  C   . THR   B 1 54  ? 6.777  -36.056 11.486 1.00 9.40  ? 60  THR   C C   1 
ATOM   1486 O  O   . THR   B 1 54  ? 7.548  -36.163 10.515 1.00 10.12 ? 60  THR   C O   1 
ATOM   1487 C  CB  . THR   B 1 54  ? 4.541  -37.195 11.212 1.00 14.08 ? 60  THR   C CB  1 
ATOM   1488 O  OG1 . THR   B 1 54  ? 5.095  -38.029 10.216 1.00 17.54 ? 60  THR   C OG1 1 
ATOM   1489 C  CG2 . THR   B 1 54  ? 3.050  -37.057 10.959 1.00 16.84 ? 60  THR   C CG2 1 
ATOM   1490 N  N   . GLY   B 1 55  ? 7.180  -36.065 12.765 1.00 8.52  ? 61  GLY   C N   1 
ATOM   1491 C  CA  . GLY   B 1 55  ? 8.607  -36.209 13.072 1.00 9.13  ? 61  GLY   C CA  1 
ATOM   1492 C  C   . GLY   B 1 55  ? 8.825  -36.329 14.564 1.00 7.59  ? 61  GLY   C C   1 
ATOM   1493 O  O   . GLY   B 1 55  ? 7.878  -36.614 15.305 1.00 9.45  ? 61  GLY   C O   1 
ATOM   1494 N  N   . VAL   B 1 56  ? 10.092 -36.179 14.977 1.00 7.18  ? 62  VAL   C N   1 
ATOM   1495 C  CA  . VAL   B 1 56  ? 10.447 -36.356 16.404 1.00 7.13  ? 62  VAL   C CA  1 
ATOM   1496 C  C   . VAL   B 1 56  ? 11.343 -35.189 16.767 1.00 8.03  ? 62  VAL   C C   1 
ATOM   1497 O  O   . VAL   B 1 56  ? 12.287 -34.912 16.021 1.00 8.33  ? 62  VAL   C O   1 
ATOM   1498 C  CB  . VAL   B 1 56  ? 11.207 -37.705 16.611 1.00 7.82  ? 62  VAL   C CB  1 
ATOM   1499 C  CG1 . VAL   B 1 56  ? 11.701 -37.854 18.063 1.00 9.53  ? 62  VAL   C CG1 1 
ATOM   1500 C  CG2 . VAL   B 1 56  ? 10.340 -38.906 16.239 1.00 8.82  ? 62  VAL   C CG2 1 
ATOM   1501 N  N   . TYR   B 1 57  ? 11.111 -34.549 17.933 1.00 7.91  ? 63  TYR   C N   1 
ATOM   1502 C  CA  . TYR   B 1 57  ? 12.015 -33.459 18.366 1.00 8.18  ? 63  TYR   C CA  1 
ATOM   1503 C  C   . TYR   B 1 57  ? 12.622 -33.749 19.730 1.00 8.35  ? 63  TYR   C C   1 
ATOM   1504 O  O   . TYR   B 1 57  ? 12.031 -34.476 20.566 1.00 8.53  ? 63  TYR   C O   1 
ATOM   1505 C  CB  . TYR   B 1 57  ? 11.339 -32.033 18.362 1.00 9.04  ? 63  TYR   C CB  1 
ATOM   1506 C  CG  . TYR   B 1 57  ? 10.423 -31.776 19.545 1.00 8.64  ? 63  TYR   C CG  1 
ATOM   1507 C  CD1 . TYR   B 1 57  ? 9.133  -32.297 19.577 1.00 10.12 ? 63  TYR   C CD1 1 
ATOM   1508 C  CD2 . TYR   B 1 57  ? 10.809 -30.926 20.577 1.00 8.84  ? 63  TYR   C CD2 1 
ATOM   1509 C  CE1 . TYR   B 1 57  ? 8.260  -32.027 20.626 1.00 11.19 ? 63  TYR   C CE1 1 
ATOM   1510 C  CE2 . TYR   B 1 57  ? 9.936  -30.645 21.644 1.00 9.70  ? 63  TYR   C CE2 1 
ATOM   1511 C  CZ  . TYR   B 1 57  ? 8.664  -31.198 21.660 1.00 10.73 ? 63  TYR   C CZ  1 
ATOM   1512 O  OH  . TYR   B 1 57  ? 7.767  -30.929 22.679 1.00 11.60 ? 63  TYR   C OH  1 
ATOM   1513 N  N   . TYR   B 1 58  ? 13.809 -33.180 19.957 1.00 8.09  ? 64  TYR   C N   1 
ATOM   1514 C  CA  . TYR   B 1 58  ? 14.451 -33.302 21.268 1.00 8.15  ? 64  TYR   C CA  1 
ATOM   1515 C  C   . TYR   B 1 58  ? 14.034 -32.139 22.168 1.00 8.49  ? 64  TYR   C C   1 
ATOM   1516 O  O   . TYR   B 1 58  ? 14.198 -30.975 21.800 1.00 8.96  ? 64  TYR   C O   1 
ATOM   1517 C  CB  . TYR   B 1 58  ? 15.985 -33.348 21.124 1.00 9.80  ? 64  TYR   C CB  1 
ATOM   1518 C  CG  . TYR   B 1 58  ? 16.650 -33.511 22.483 1.00 10.75 ? 64  TYR   C CG  1 
ATOM   1519 C  CD1 . TYR   B 1 58  ? 16.502 -34.685 23.210 1.00 11.92 ? 64  TYR   C CD1 1 
ATOM   1520 C  CD2 . TYR   B 1 58  ? 17.378 -32.474 23.058 1.00 13.60 ? 64  TYR   C CD2 1 
ATOM   1521 C  CE1 . TYR   B 1 58  ? 17.049 -34.828 24.499 1.00 13.40 ? 64  TYR   C CE1 1 
ATOM   1522 C  CE2 . TYR   B 1 58  ? 17.945 -32.619 24.330 1.00 13.98 ? 64  TYR   C CE2 1 
ATOM   1523 C  CZ  . TYR   B 1 58  ? 17.798 -33.801 25.019 1.00 15.25 ? 64  TYR   C CZ  1 
ATOM   1524 O  OH  . TYR   B 1 58  ? 18.336 -33.918 26.294 1.00 17.72 ? 64  TYR   C OH  1 
ATOM   1525 N  N   . CYS   B 1 59  ? 13.578 -32.478 23.382 1.00 8.96  ? 65  CYS   C N   1 
ATOM   1526 C  CA  . CYS   B 1 59  ? 13.142 -31.491 24.385 1.00 9.17  ? 65  CYS   C CA  1 
ATOM   1527 C  C   . CYS   B 1 59  ? 14.131 -31.548 25.591 1.00 9.52  ? 65  CYS   C C   1 
ATOM   1528 O  O   . CYS   B 1 59  ? 14.045 -32.478 26.409 1.00 11.33 ? 65  CYS   C O   1 
ATOM   1529 C  CB  . CYS   B 1 59  ? 11.723 -31.832 24.806 1.00 8.61  ? 65  CYS   C CB  1 
ATOM   1530 S  SG  . CYS   B 1 59  ? 11.095 -30.775 26.146 1.00 11.63 ? 65  CYS   C SG  1 
ATOM   1531 N  N   . SER   B 1 60  ? 15.028 -30.575 25.662 1.00 10.41 ? 66  SER   C N   1 
ATOM   1532 C  CA  . SER   B 1 60  ? 16.035 -30.611 26.720 1.00 12.40 ? 66  SER   C CA  1 
ATOM   1533 C  C   . SER   B 1 60  ? 15.463 -30.486 28.121 1.00 12.01 ? 66  SER   C C   1 
ATOM   1534 O  O   . SER   B 1 60  ? 15.963 -31.150 29.037 1.00 13.86 ? 66  SER   C O   1 
ATOM   1535 C  CB  . SER   B 1 60  ? 17.089 -29.552 26.471 1.00 18.02 ? 66  SER   C CB  1 
ATOM   1536 O  OG  . SER   B 1 60  ? 16.596 -28.237 26.518 1.00 26.10 ? 66  SER   C OG  1 
ATOM   1537 N  N   . SER   B 1 61  ? 14.346 -29.736 28.275 1.00 11.45 ? 67  SER   C N   1 
ATOM   1538 C  CA  . SER   B 1 61  ? 13.714 -29.570 29.604 1.00 11.12 ? 67  SER   C CA  1 
ATOM   1539 C  C   . SER   B 1 61  ? 13.024 -30.829 30.111 1.00 12.19 ? 67  SER   C C   1 
ATOM   1540 O  O   . SER   B 1 61  ? 12.577 -30.862 31.276 1.00 13.00 ? 67  SER   C O   1 
ATOM   1541 C  CB  . SER   B 1 61  ? 12.769 -28.384 29.570 1.00 10.84 ? 67  SER   C CB  1 
ATOM   1542 O  OG  . SER   B 1 61  ? 11.654 -28.632 28.737 1.00 11.55 ? 67  SER   C OG  1 
ATOM   1543 N  N   . ARG   B 1 62  ? 12.939 -31.880 29.281 1.00 11.10 ? 68  ARG   C N   1 
ATOM   1544 C  CA  . ARG   B 1 62  ? 12.420 -33.182 29.687 1.00 10.95 ? 68  ARG   C CA  1 
ATOM   1545 C  C   . ARG   B 1 62  ? 13.467 -34.308 29.490 1.00 11.24 ? 68  ARG   C C   1 
ATOM   1546 O  O   . ARG   B 1 62  ? 13.180 -35.483 29.781 1.00 12.83 ? 68  ARG   C O   1 
ATOM   1547 C  CB  . ARG   B 1 62  ? 11.131 -33.498 28.893 1.00 13.22 ? 68  ARG   C CB  1 
ATOM   1548 C  CG  . ARG   B 1 62  ? 9.975  -32.548 29.230 1.00 13.35 ? 68  ARG   C CG  1 
ATOM   1549 C  CD  . ARG   B 1 62  ? 9.407  -32.839 30.618 1.00 14.48 ? 68  ARG   C CD  1 
ATOM   1550 N  NE  . ARG   B 1 62  ? 8.295  -31.939 30.946 1.00 16.66 ? 68  ARG   C NE  1 
ATOM   1551 C  CZ  . ARG   B 1 62  ? 8.415  -30.797 31.595 1.00 19.57 ? 68  ARG   C CZ  1 
ATOM   1552 N  NH1 . ARG   B 1 62  ? 9.613  -30.372 32.001 1.00 19.47 ? 68  ARG   C NH1 1 
ATOM   1553 N  NH2 . ARG   B 1 62  ? 7.336  -30.071 31.873 1.00 22.82 ? 68  ARG   C NH2 1 
ATOM   1554 N  N   . ARG   B 1 63  ? 14.654 -33.951 28.927 1.00 12.18 ? 69  ARG   C N   1 
ATOM   1555 C  CA  . ARG   B 1 63  ? 15.704 -34.941 28.533 1.00 13.78 ? 69  ARG   C CA  1 
ATOM   1556 C  C   . ARG   B 1 63  ? 15.090 -36.067 27.739 1.00 14.78 ? 69  ARG   C C   1 
ATOM   1557 O  O   . ARG   B 1 63  ? 15.320 -37.256 27.999 1.00 17.06 ? 69  ARG   C O   1 
ATOM   1558 C  CB  . ARG   B 1 63  ? 16.456 -35.500 29.762 1.00 17.13 ? 69  ARG   C CB  1 
ATOM   1559 C  CG  . ARG   B 1 63  ? 17.256 -34.489 30.480 1.00 21.94 ? 69  ARG   C CG  1 
ATOM   1560 C  CD  . ARG   B 1 63  ? 18.471 -34.061 29.720 1.00 29.80 ? 69  ARG   C CD  1 
ATOM   1561 N  NE  . ARG   B 1 63  ? 19.444 -33.455 30.618 1.00 34.40 ? 69  ARG   C NE  1 
ATOM   1562 C  CZ  . ARG   B 1 63  ? 19.476 -32.163 30.927 1.00 38.19 ? 69  ARG   C CZ  1 
ATOM   1563 N  NH1 . ARG   B 1 63  ? 18.574 -31.327 30.422 1.00 37.76 ? 69  ARG   C NH1 1 
ATOM   1564 N  NH2 . ARG   B 1 63  ? 20.402 -31.699 31.748 1.00 38.90 ? 69  ARG   C NH2 1 
ATOM   1565 N  N   . LYS   B 1 64  ? 14.203 -35.707 26.784 1.00 12.59 ? 70  LYS   C N   1 
ATOM   1566 C  CA  . LYS   B 1 64  ? 13.451 -36.726 26.060 1.00 13.73 ? 70  LYS   C CA  1 
ATOM   1567 C  C   . LYS   B 1 64  ? 13.148 -36.271 24.660 1.00 11.66 ? 70  LYS   C C   1 
ATOM   1568 O  O   . LYS   B 1 64  ? 12.979 -35.077 24.415 1.00 11.48 ? 70  LYS   C O   1 
ATOM   1569 C  CB  . LYS   B 1 64  ? 12.036 -36.930 26.765 1.00 19.68 ? 70  LYS   C CB  1 
ATOM   1570 C  CG  . LYS   B 1 64  ? 11.948 -37.949 27.887 1.00 31.45 ? 70  LYS   C CG  1 
ATOM   1571 C  CD  . LYS   B 1 64  ? 10.464 -38.167 28.193 1.00 38.12 ? 70  LYS   C CD  1 
ATOM   1572 C  CE  . LYS   B 1 64  ? 10.185 -39.374 29.066 1.00 43.78 ? 70  LYS   C CE  1 
ATOM   1573 N  NZ  . LYS   B 1 64  ? 10.374 -39.076 30.511 1.00 46.13 ? 70  LYS   C NZ  1 
ATOM   1574 N  N   . HIS   B 1 65  ? 12.915 -37.242 23.800 1.00 9.96  ? 71  HIS   C N   1 
ATOM   1575 C  CA  . HIS   B 1 65  ? 12.411 -37.003 22.437 1.00 8.78  ? 71  HIS   C CA  1 
ATOM   1576 C  C   . HIS   B 1 65  ? 10.922 -37.245 22.399 1.00 11.33 ? 71  HIS   C C   1 
ATOM   1577 O  O   . HIS   B 1 65  ? 10.406 -38.191 23.061 1.00 14.59 ? 71  HIS   C O   1 
ATOM   1578 C  CB  . HIS   B 1 65  ? 13.086 -37.953 21.419 1.00 9.28  ? 71  HIS   C CB  1 
ATOM   1579 C  CG  . HIS   B 1 65  ? 14.554 -37.711 21.294 1.00 9.86  ? 71  HIS   C CG  1 
ATOM   1580 N  ND1 . HIS   B 1 65  ? 15.119 -36.976 20.247 1.00 13.51 ? 71  HIS   C ND1 1 
ATOM   1581 C  CD2 . HIS   B 1 65  ? 15.555 -38.208 22.066 1.00 10.19 ? 71  HIS   C CD2 1 
ATOM   1582 C  CE1 . HIS   B 1 65  ? 16.439 -37.050 20.436 1.00 11.80 ? 71  HIS   C CE1 1 
ATOM   1583 N  NE2 . HIS   B 1 65  ? 16.738 -37.743 21.507 1.00 14.30 ? 71  HIS   C NE2 1 
ATOM   1584 N  N   . TYR   B 1 66  ? 10.171 -36.429 21.639 1.00 9.24  ? 72  TYR   C N   1 
ATOM   1585 C  CA  . TYR   B 1 66  ? 8.727  -36.616 21.504 1.00 9.47  ? 72  TYR   C CA  1 
ATOM   1586 C  C   . TYR   B 1 66  ? 8.349  -36.692 20.022 1.00 9.13  ? 72  TYR   C C   1 
ATOM   1587 O  O   . TYR   B 1 66  ? 8.774  -35.862 19.219 1.00 9.08  ? 72  TYR   C O   1 
ATOM   1588 C  CB  . TYR   B 1 66  ? 7.977  -35.409 22.097 1.00 10.13 ? 72  TYR   C CB  1 
ATOM   1589 C  CG  . TYR   B 1 66  ? 8.063  -35.304 23.597 1.00 11.30 ? 72  TYR   C CG  1 
ATOM   1590 C  CD1 . TYR   B 1 66  ? 7.315  -36.141 24.417 1.00 13.34 ? 72  TYR   C CD1 1 
ATOM   1591 C  CD2 . TYR   B 1 66  ? 8.817  -34.300 24.203 1.00 12.27 ? 72  TYR   C CD2 1 
ATOM   1592 C  CE1 . TYR   B 1 66  ? 7.379  -36.032 25.801 1.00 13.89 ? 72  TYR   C CE1 1 
ATOM   1593 C  CE2 . TYR   B 1 66  ? 8.841  -34.152 25.587 1.00 13.38 ? 72  TYR   C CE2 1 
ATOM   1594 C  CZ  . TYR   B 1 66  ? 8.146  -35.041 26.373 1.00 14.91 ? 72  TYR   C CZ  1 
ATOM   1595 O  OH  . TYR   B 1 66  ? 8.171  -34.880 27.747 1.00 18.28 ? 72  TYR   C OH  1 
ATOM   1596 N  N   . PRO   B 1 67  ? 7.498  -37.678 19.652 1.00 8.98  ? 73  PRO   C N   1 
ATOM   1597 C  CA  . PRO   B 1 67  ? 6.953  -37.723 18.285 1.00 8.29  ? 73  PRO   C CA  1 
ATOM   1598 C  C   . PRO   B 1 67  ? 5.808  -36.702 18.193 1.00 10.17 ? 73  PRO   C C   1 
ATOM   1599 O  O   . PRO   B 1 67  ? 4.959  -36.661 19.111 1.00 11.28 ? 73  PRO   C O   1 
ATOM   1600 C  CB  . PRO   B 1 67  ? 6.449  -39.185 18.164 1.00 8.74  ? 73  PRO   C CB  1 
ATOM   1601 C  CG  . PRO   B 1 67  ? 6.064  -39.550 19.554 1.00 9.82  ? 73  PRO   C CG  1 
ATOM   1602 C  CD  . PRO   B 1 67  ? 7.000  -38.802 20.495 1.00 9.76  ? 73  PRO   C CD  1 
ATOM   1603 N  N   . VAL   B 1 68  ? 5.755  -35.947 17.105 1.00 9.04  ? 74  VAL   C N   1 
ATOM   1604 C  CA  . VAL   B 1 68  ? 4.672  -34.938 16.923 1.00 10.10 ? 74  VAL   C CA  1 
ATOM   1605 C  C   . VAL   B 1 68  ? 4.265  -34.833 15.483 1.00 9.41  ? 74  VAL   C C   1 
ATOM   1606 O  O   . VAL   B 1 68  ? 5.059  -35.043 14.566 1.00 10.69 ? 74  VAL   C O   1 
ATOM   1607 C  CB  . VAL   B 1 68  ? 5.123  -33.524 17.394 1.00 12.00 ? 74  VAL   C CB  1 
ATOM   1608 C  CG1 . VAL   B 1 68  ? 5.252  -33.471 18.941 1.00 13.03 ? 74  VAL   C CG1 1 
ATOM   1609 C  CG2 . VAL   B 1 68  ? 6.418  -33.061 16.695 1.00 12.93 ? 74  VAL   C CG2 1 
ATOM   1610 N  N   . SER   B 1 69  ? 2.997  -34.381 15.283 1.00 9.16  ? 75  SER   C N   1 
ATOM   1611 C  CA  . SER   B 1 69  ? 2.545  -33.833 14.024 1.00 9.24  ? 75  SER   C CA  1 
ATOM   1612 C  C   . SER   B 1 69  ? 2.848  -32.305 14.078 1.00 9.04  ? 75  SER   C C   1 
ATOM   1613 O  O   . SER   B 1 69  ? 2.773  -31.670 15.140 1.00 9.22  ? 75  SER   C O   1 
ATOM   1614 C  CB  . SER   B 1 69  ? 1.032  -34.008 13.862 1.00 12.30 ? 75  SER   C CB  1 
ATOM   1615 O  OG  . SER   B 1 69  ? 0.733  -35.394 13.782 1.00 17.34 ? 75  SER   C OG  1 
ATOM   1616 N  N   . PHE   B 1 70  ? 3.169  -31.704 12.935 1.00 7.74  ? 76  PHE   C N   1 
ATOM   1617 C  CA  . PHE   B 1 70  ? 3.499  -30.295 12.884 1.00 7.58  ? 76  PHE   C CA  1 
ATOM   1618 C  C   . PHE   B 1 70  ? 2.902  -29.654 11.620 1.00 7.72  ? 76  PHE   C C   1 
ATOM   1619 O  O   . PHE   B 1 70  ? 2.650  -30.344 10.613 1.00 8.59  ? 76  PHE   C O   1 
ATOM   1620 C  CB  . PHE   B 1 70  ? 5.024  -30.015 13.061 1.00 7.88  ? 76  PHE   C CB  1 
ATOM   1621 C  CG  . PHE   B 1 70  ? 5.928  -30.739 12.087 1.00 7.71  ? 76  PHE   C CG  1 
ATOM   1622 C  CD1 . PHE   B 1 70  ? 6.434  -31.990 12.379 1.00 8.52  ? 76  PHE   C CD1 1 
ATOM   1623 C  CD2 . PHE   B 1 70  ? 6.336  -30.123 10.918 1.00 8.31  ? 76  PHE   C CD2 1 
ATOM   1624 C  CE1 . PHE   B 1 70  ? 7.286  -32.638 11.479 1.00 9.60  ? 76  PHE   C CE1 1 
ATOM   1625 C  CE2 . PHE   B 1 70  ? 7.234  -30.738 10.047 1.00 8.56  ? 76  PHE   C CE2 1 
ATOM   1626 C  CZ  . PHE   B 1 70  ? 7.656  -32.020 10.301 1.00 8.91  ? 76  PHE   C CZ  1 
ATOM   1627 N  N   . SER   B 1 71  ? 2.671  -28.350 11.673 1.00 8.19  ? 77  SER   C N   1 
ATOM   1628 C  CA  . SER   B 1 71  ? 2.033  -27.613 10.567 1.00 9.13  ? 77  SER   C CA  1 
ATOM   1629 C  C   . SER   B 1 71  ? 2.975  -27.315 9.403  1.00 9.69  ? 77  SER   C C   1 
ATOM   1630 O  O   . SER   B 1 71  ? 4.152  -27.684 9.434  1.00 10.05 ? 77  SER   C O   1 
ATOM   1631 C  CB  . SER   B 1 71  ? 1.414  -26.336 11.120 1.00 10.06 ? 77  SER   C CB  1 
ATOM   1632 O  OG  . SER   B 1 71  ? 2.377  -25.400 11.593 1.00 11.14 ? 77  SER   C OG  1 
ATOM   1633 N  N   . LYS   B 1 72  ? 2.444  -26.715 8.362  1.00 9.18  ? 78  LYS   C N   1 
ATOM   1634 C  CA  . LYS   B 1 72  ? 3.277  -26.305 7.215  1.00 10.28 ? 78  LYS   C CA  1 
ATOM   1635 C  C   . LYS   B 1 72  ? 3.968  -24.977 7.562  1.00 10.22 ? 78  LYS   C C   1 
ATOM   1636 O  O   . LYS   B 1 72  ? 3.372  -24.137 8.256  1.00 12.83 ? 78  LYS   C O   1 
ATOM   1637 C  CB  . LYS   B 1 72  ? 2.403  -26.141 5.957  1.00 12.32 ? 78  LYS   C CB  1 
ATOM   1638 C  CG  . LYS   B 1 72  ? 1.688  -27.453 5.608  1.00 14.26 ? 78  LYS   C CG  1 
ATOM   1639 C  CD  . LYS   B 1 72  ? 0.727  -27.203 4.417  1.00 22.79 ? 78  LYS   C CD  1 
ATOM   1640 C  CE  . LYS   B 1 72  ? 0.160  -28.479 3.868  1.00 31.51 ? 78  LYS   C CE  1 
ATOM   1641 N  NZ  . LYS   B 1 72  ? -0.555 -28.212 2.592  1.00 36.76 ? 78  LYS   C NZ  1 
ATOM   1642 N  N   . PRO   B 1 73  ? 5.177  -24.696 7.053  1.00 9.73  ? 79  PRO   C N   1 
ATOM   1643 C  CA  . PRO   B 1 73  ? 5.868  -23.414 7.388  1.00 10.29 ? 79  PRO   C CA  1 
ATOM   1644 C  C   . PRO   B 1 73  ? 5.013  -22.198 7.015  1.00 11.57 ? 79  PRO   C C   1 
ATOM   1645 O  O   . PRO   B 1 73  ? 4.468  -22.113 5.899  1.00 13.41 ? 79  PRO   C O   1 
ATOM   1646 C  CB  . PRO   B 1 73  ? 7.161  -23.434 6.556  1.00 12.53 ? 79  PRO   C CB  1 
ATOM   1647 C  CG  . PRO   B 1 73  ? 7.335  -24.872 6.125  1.00 14.84 ? 79  PRO   C CG  1 
ATOM   1648 C  CD  . PRO   B 1 73  ? 5.967  -25.547 6.144  1.00 10.30 ? 79  PRO   C CD  1 
ATOM   1649 N  N   . SER   B 1 74  ? 4.875  -21.265 7.959  1.00 11.23 ? 80  SER   C N   1 
ATOM   1650 C  CA  . SER   B 1 74  ? 3.994  -20.123 7.732  1.00 12.53 ? 80  SER   C CA  1 
ATOM   1651 C  C   . SER   B 1 74  ? 4.380  -18.947 8.606  1.00 11.69 ? 80  SER   C C   1 
ATOM   1652 O  O   . SER   B 1 74  ? 5.332  -19.007 9.393  1.00 10.30 ? 80  SER   C O   1 
ATOM   1653 C  CB  . SER   B 1 74  ? 2.536  -20.533 7.960  1.00 16.52 ? 80  SER   C CB  1 
ATOM   1654 O  OG  . SER   B 1 74  ? 2.268  -20.673 9.350  1.00 22.07 ? 80  SER   C OG  1 
ATOM   1655 N  N   . LEU   B 1 75  ? 3.686  -17.821 8.390  1.00 11.25 ? 81  LEU   C N   1 
ATOM   1656 C  CA  . LEU   B 1 75  ? 3.859  -16.574 9.129  1.00 11.75 ? 81  LEU   C CA  1 
ATOM   1657 C  C   . LEU   B 1 75  ? 2.991  -16.642 10.372 1.00 13.25 ? 81  LEU   C C   1 
ATOM   1658 O  O   . LEU   B 1 75  ? 1.745  -16.707 10.253 1.00 14.81 ? 81  LEU   C O   1 
ATOM   1659 C  CB  . LEU   B 1 75  ? 3.375  -15.413 8.258  1.00 13.91 ? 81  LEU   C CB  1 
ATOM   1660 C  CG  . LEU   B 1 75  ? 4.425  -14.759 7.389  1.00 18.52 ? 81  LEU   C CG  1 
ATOM   1661 C  CD1 . LEU   B 1 75  ? 3.736  -13.792 6.367  1.00 22.03 ? 81  LEU   C CD1 1 
ATOM   1662 C  CD2 . LEU   B 1 75  ? 5.429  -13.997 8.230  1.00 19.30 ? 81  LEU   C CD2 1 
ATOM   1663 N  N   . ILE   B 1 76  ? 3.601  -16.618 11.557 1.00 12.03 ? 82  ILE   C N   1 
ATOM   1664 C  CA  . ILE   B 1 76  ? 2.925  -16.754 12.856 1.00 13.01 ? 82  ILE   C CA  1 
ATOM   1665 C  C   . ILE   B 1 76  ? 3.320  -15.632 13.807 1.00 14.59 ? 82  ILE   C C   1 
ATOM   1666 O  O   . ILE   B 1 76  ? 4.496  -15.324 13.929 1.00 12.93 ? 82  ILE   C O   1 
ATOM   1667 C  CB  . ILE   B 1 76  ? 3.260  -18.116 13.466 1.00 15.15 ? 82  ILE   C CB  1 
ATOM   1668 C  CG1 . ILE   B 1 76  ? 2.785  -19.250 12.499 1.00 17.61 ? 82  ILE   C CG1 1 
ATOM   1669 C  CG2 . ILE   B 1 76  ? 2.698  -18.238 14.909 1.00 17.44 ? 82  ILE   C CG2 1 
ATOM   1670 C  CD1 . ILE   B 1 76  ? 2.931  -20.632 12.938 1.00 20.75 ? 82  ILE   C CD1 1 
ATOM   1671 N  N   . PHE   B 1 77  ? 2.355  -14.980 14.478 1.00 15.69 ? 83  PHE   C N   1 
ATOM   1672 C  CA  . PHE   B 1 77  ? 2.646  -13.907 15.418 1.00 16.69 ? 83  PHE   C CA  1 
ATOM   1673 C  C   . PHE   B 1 77  ? 3.378  -14.411 16.647 1.00 16.79 ? 83  PHE   C C   1 
ATOM   1674 O  O   . PHE   B 1 77  ? 3.002  -15.422 17.224 1.00 17.83 ? 83  PHE   C O   1 
ATOM   1675 C  CB  . PHE   B 1 77  ? 1.312  -13.225 15.854 1.00 18.74 ? 83  PHE   C CB  1 
ATOM   1676 C  CG  . PHE   B 1 77  ? 1.506  -12.063 16.803 1.00 21.01 ? 83  PHE   C CG  1 
ATOM   1677 C  CD1 . PHE   B 1 77  ? 1.387  -12.242 18.165 1.00 24.09 ? 83  PHE   C CD1 1 
ATOM   1678 C  CD2 . PHE   B 1 77  ? 1.928  -10.837 16.340 1.00 23.46 ? 83  PHE   C CD2 1 
ATOM   1679 C  CE1 . PHE   B 1 77  ? 1.602  -11.189 19.041 1.00 25.37 ? 83  PHE   C CE1 1 
ATOM   1680 C  CE2 . PHE   B 1 77  ? 2.141  -9.771  17.224 1.00 25.66 ? 83  PHE   C CE2 1 
ATOM   1681 C  CZ  . PHE   B 1 77  ? 1.968  -9.962  18.563 1.00 25.51 ? 83  PHE   C CZ  1 
ATOM   1682 N  N   . VAL   B 1 78  ? 4.473  -13.713 17.000 1.00 15.59 ? 84  VAL   C N   1 
ATOM   1683 C  CA  . VAL   B 1 78  ? 5.274  -14.036 18.188 1.00 14.81 ? 84  VAL   C CA  1 
ATOM   1684 C  C   . VAL   B 1 78  ? 5.368  -12.748 19.038 1.00 15.09 ? 84  VAL   C C   1 
ATOM   1685 O  O   . VAL   B 1 78  ? 5.814  -11.686 18.597 1.00 15.56 ? 84  VAL   C O   1 
ATOM   1686 C  CB  . VAL   B 1 78  ? 6.705  -14.534 17.759 1.00 13.08 ? 84  VAL   C CB  1 
ATOM   1687 C  CG1 . VAL   B 1 78  ? 7.591  -14.844 18.987 1.00 13.80 ? 84  VAL   C CG1 1 
ATOM   1688 C  CG2 . VAL   B 1 78  ? 6.590  -15.786 16.873 1.00 12.94 ? 84  VAL   C CG2 1 
ATOM   1689 N  N   . GLU   B 1 79  ? 5.034  -12.917 20.328 1.00 18.13 ? 85  GLU   C N   1 
ATOM   1690 C  CA  . GLU   B 1 79  ? 5.129  -11.856 21.300 1.00 18.98 ? 85  GLU   C CA  1 
ATOM   1691 C  C   . GLU   B 1 79  ? 6.541  -11.253 21.435 1.00 17.32 ? 85  GLU   C C   1 
ATOM   1692 O  O   . GLU   B 1 79  ? 7.518  -11.984 21.270 1.00 16.26 ? 85  GLU   C O   1 
ATOM   1693 C  CB  . GLU   B 1 79  ? 4.708  -12.406 22.684 1.00 23.26 ? 85  GLU   C CB  1 
ATOM   1694 C  CG  . GLU   B 1 79  ? 3.381  -13.146 22.717 1.00 29.31 ? 85  GLU   C CG  1 
ATOM   1695 C  CD  . GLU   B 1 79  ? 2.178  -12.257 22.971 1.00 35.42 ? 85  GLU   C CD  1 
ATOM   1696 O  OE1 . GLU   B 1 79  ? 1.048  -12.795 22.964 1.00 33.52 ? 85  GLU   C OE1 1 
ATOM   1697 O  OE2 . GLU   B 1 79  ? 2.355  -11.030 23.151 1.00 37.75 ? 85  GLU   C OE2 1 
ATOM   1698 N  N   . ALA   B 1 80  ? 6.656  -9.962  21.832 1.00 17.41 ? 86  ALA   C N   1 
ATOM   1699 C  CA  . ALA   B 1 80  ? 7.946  -9.317  22.070 1.00 16.74 ? 86  ALA   C CA  1 
ATOM   1700 C  C   . ALA   B 1 80  ? 8.696  -10.089 23.150 1.00 15.31 ? 86  ALA   C C   1 
ATOM   1701 O  O   . ALA   B 1 80  ? 8.109  -10.641 24.093 1.00 15.20 ? 86  ALA   C O   1 
ATOM   1702 C  CB  . ALA   B 1 80  ? 7.761  -7.846  22.545 1.00 18.29 ? 86  ALA   C CB  1 
ATOM   1703 N  N   . SER   B 1 81  ? 9.994  -10.105 23.006 1.00 13.20 ? 87  SER   C N   1 
ATOM   1704 C  CA  . SER   B 1 81  ? 10.894 -10.647 24.000 1.00 12.74 ? 87  SER   C CA  1 
ATOM   1705 C  C   . SER   B 1 81  ? 12.052 -9.649  24.111 1.00 12.34 ? 87  SER   C C   1 
ATOM   1706 O  O   . SER   B 1 81  ? 12.049 -8.593  23.419 1.00 14.25 ? 87  SER   C O   1 
ATOM   1707 C  CB  . SER   B 1 81  ? 11.407 -12.032 23.552 1.00 13.40 ? 87  SER   C CB  1 
ATOM   1708 O  OG  . SER   B 1 81  ? 12.152 -11.888 22.353 1.00 13.25 ? 87  SER   C OG  1 
ATOM   1709 N  N   . GLU   B 1 82  ? 13.084 -10.004 24.884 1.00 13.17 ? 88  GLU   C N   1 
ATOM   1710 C  CA  . GLU   B 1 82  ? 14.265 -9.121  24.938 1.00 14.41 ? 88  GLU   C CA  1 
ATOM   1711 C  C   . GLU   B 1 82  ? 15.059 -9.177  23.632 1.00 15.28 ? 88  GLU   C C   1 
ATOM   1712 O  O   . GLU   B 1 82  ? 15.868 -8.274  23.362 1.00 15.22 ? 88  GLU   C O   1 
ATOM   1713 C  CB  . GLU   B 1 82  ? 15.154 -9.455  26.120 1.00 18.98 ? 88  GLU   C CB  1 
ATOM   1714 C  CG  . GLU   B 1 82  ? 15.670 -10.864 26.112 1.00 25.32 ? 88  GLU   C CG  1 
ATOM   1715 C  CD  . GLU   B 1 82  ? 14.869 -11.912 26.869 1.00 34.67 ? 88  GLU   C CD  1 
ATOM   1716 O  OE1 . GLU   B 1 82  ? 15.496 -12.631 27.681 1.00 38.09 ? 88  GLU   C OE1 1 
ATOM   1717 O  OE2 . GLU   B 1 82  ? 13.638 -12.036 26.643 1.00 31.74 ? 88  GLU   C OE2 1 
ATOM   1718 N  N   . TYR   B 1 83  ? 14.829 -10.214 22.794 1.00 15.06 ? 89  TYR   C N   1 
ATOM   1719 C  CA  . TYR   B 1 83  ? 15.571 -10.413 21.570 1.00 14.97 ? 89  TYR   C CA  1 
ATOM   1720 C  C   . TYR   B 1 83  ? 14.931 -9.788  20.354 1.00 15.47 ? 89  TYR   C C   1 
ATOM   1721 O  O   . TYR   B 1 83  ? 15.635 -9.499  19.367 1.00 18.50 ? 89  TYR   C O   1 
ATOM   1722 C  CB  . TYR   B 1 83  ? 15.683 -11.930 21.338 1.00 14.28 ? 89  TYR   C CB  1 
ATOM   1723 C  CG  . TYR   B 1 83  ? 16.310 -12.681 22.490 1.00 14.91 ? 89  TYR   C CG  1 
ATOM   1724 C  CD1 . TYR   B 1 83  ? 17.681 -12.642 22.710 1.00 16.35 ? 89  TYR   C CD1 1 
ATOM   1725 C  CD2 . TYR   B 1 83  ? 15.537 -13.416 23.363 1.00 14.69 ? 89  TYR   C CD2 1 
ATOM   1726 C  CE1 . TYR   B 1 83  ? 18.256 -13.297 23.782 1.00 18.26 ? 89  TYR   C CE1 1 
ATOM   1727 C  CE2 . TYR   B 1 83  ? 16.102 -14.096 24.429 1.00 17.75 ? 89  TYR   C CE2 1 
ATOM   1728 C  CZ  . TYR   B 1 83  ? 17.471 -14.045 24.629 1.00 19.94 ? 89  TYR   C CZ  1 
ATOM   1729 O  OH  . TYR   B 1 83  ? 18.058 -14.726 25.666 1.00 25.02 ? 89  TYR   C OH  1 
ATOM   1730 N  N   . TYR   B 1 84  ? 13.625 -9.640  20.352 1.00 13.23 ? 90  TYR   C N   1 
ATOM   1731 C  CA  . TYR   B 1 84  ? 12.903 -9.199  19.177 1.00 13.70 ? 90  TYR   C CA  1 
ATOM   1732 C  C   . TYR   B 1 84  ? 11.728 -8.378  19.571 1.00 15.91 ? 90  TYR   C C   1 
ATOM   1733 O  O   . TYR   B 1 84  ? 11.039 -8.655  20.584 1.00 15.63 ? 90  TYR   C O   1 
ATOM   1734 C  CB  . TYR   B 1 84  ? 12.296 -10.385 18.349 1.00 13.24 ? 90  TYR   C CB  1 
ATOM   1735 C  CG  . TYR   B 1 84  ? 13.286 -11.320 17.746 1.00 11.60 ? 90  TYR   C CG  1 
ATOM   1736 C  CD1 . TYR   B 1 84  ? 13.464 -12.592 18.263 1.00 11.63 ? 90  TYR   C CD1 1 
ATOM   1737 C  CD2 . TYR   B 1 84  ? 14.068 -10.936 16.660 1.00 11.03 ? 90  TYR   C CD2 1 
ATOM   1738 C  CE1 . TYR   B 1 84  ? 14.355 -13.472 17.707 1.00 11.74 ? 90  TYR   C CE1 1 
ATOM   1739 C  CE2 . TYR   B 1 84  ? 14.962 -11.816 16.086 1.00 11.13 ? 90  TYR   C CE2 1 
ATOM   1740 C  CZ  . TYR   B 1 84  ? 15.115 -13.080 16.616 1.00 10.78 ? 90  TYR   C CZ  1 
ATOM   1741 O  OH  . TYR   B 1 84  ? 16.031 -13.922 16.071 1.00 10.94 ? 90  TYR   C OH  1 
ATOM   1742 N  N   . PRO   B 1 85  ? 11.387 -7.403  18.715 1.00 18.11 ? 91  PRO   C N   1 
ATOM   1743 C  CA  . PRO   B 1 85  ? 10.122 -6.764  18.898 1.00 18.10 ? 91  PRO   C CA  1 
ATOM   1744 C  C   . PRO   B 1 85  ? 8.972  -7.751  18.634 1.00 17.66 ? 91  PRO   C C   1 
ATOM   1745 O  O   . PRO   B 1 85  ? 9.144  -8.783  17.967 1.00 15.88 ? 91  PRO   C O   1 
ATOM   1746 C  CB  . PRO   B 1 85  ? 10.142 -5.668  17.782 1.00 18.86 ? 91  PRO   C CB  1 
ATOM   1747 C  CG  . PRO   B 1 85  ? 11.003 -6.233  16.744 1.00 19.87 ? 91  PRO   C CG  1 
ATOM   1748 C  CD  . PRO   B 1 85  ? 12.062 -6.982  17.459 1.00 18.53 ? 91  PRO   C CD  1 
ATOM   1749 N  N   . ALA   B 1 86  ? 7.777  -7.425  19.042 1.00 17.70 ? 92  ALA   C N   1 
ATOM   1750 C  CA  . ALA   B 1 86  ? 6.556  -8.133  18.695 1.00 17.77 ? 92  ALA   C CA  1 
ATOM   1751 C  C   . ALA   B 1 86  ? 6.489  -8.164  17.111 1.00 17.68 ? 92  ALA   C C   1 
ATOM   1752 O  O   . ALA   B 1 86  ? 6.870  -7.138  16.483 1.00 18.56 ? 92  ALA   C O   1 
ATOM   1753 C  CB  . ALA   B 1 86  ? 5.342  -7.370  19.220 1.00 19.30 ? 92  ALA   C CB  1 
ATOM   1754 N  N   . ARG   B 1 87  ? 6.251  -9.362  16.484 1.00 17.22 ? 93  ARG   C N   1 
ATOM   1755 C  CA  . ARG   B 1 87  ? 6.353  -9.433  15.015 1.00 16.56 ? 93  ARG   C CA  1 
ATOM   1756 C  C   . ARG   B 1 87  ? 5.787  -10.763 14.508 1.00 16.34 ? 93  ARG   C C   1 
ATOM   1757 O  O   . ARG   B 1 87  ? 5.490  -11.664 15.298 1.00 16.63 ? 93  ARG   C O   1 
ATOM   1758 C  CB  . ARG   B 1 87  ? 7.845  -9.358  14.621 1.00 16.18 ? 93  ARG   C CB  1 
ATOM   1759 C  CG  . ARG   B 1 87  ? 8.617  -10.690 14.965 1.00 12.66 ? 93  ARG   C CG  1 
ATOM   1760 C  CD  . ARG   B 1 87  ? 10.088 -10.508 15.166 1.00 13.97 ? 93  ARG   C CD  1 
ATOM   1761 N  NE  . ARG   B 1 87  ? 10.912 -11.643 14.742 1.00 11.80 ? 93  ARG   C NE  1 
ATOM   1762 C  CZ  . ARG   B 1 87  ? 10.973 -12.830 15.351 1.00 11.74 ? 93  ARG   C CZ  1 
ATOM   1763 N  NH1 . ARG   B 1 87  ? 11.769 -13.779 14.880 1.00 10.49 ? 93  ARG   C NH1 1 
ATOM   1764 N  NH2 . ARG   B 1 87  ? 10.221 -13.077 16.433 1.00 11.96 ? 93  ARG   C NH2 1 
ATOM   1765 N  N   . TYR   B 1 88  ? 5.669  -10.903 13.185 1.00 16.54 ? 94  TYR   C N   1 
ATOM   1766 C  CA  . TYR   B 1 88  ? 5.328  -12.204 12.606 1.00 16.94 ? 94  TYR   C CA  1 
ATOM   1767 C  C   . TYR   B 1 88  ? 6.647  -12.889 12.235 1.00 13.96 ? 94  TYR   C C   1 
ATOM   1768 O  O   . TYR   B 1 88  ? 7.489  -12.299 11.528 1.00 14.68 ? 94  TYR   C O   1 
ATOM   1769 C  CB  . TYR   B 1 88  ? 4.553  -12.007 11.311 1.00 18.77 ? 94  TYR   C CB  1 
ATOM   1770 C  CG  . TYR   B 1 88  ? 3.128  -11.613 11.585 1.00 21.66 ? 94  TYR   C CG  1 
ATOM   1771 C  CD1 . TYR   B 1 88  ? 2.141  -12.572 11.742 1.00 23.03 ? 94  TYR   C CD1 1 
ATOM   1772 C  CD2 . TYR   B 1 88  ? 2.778  -10.283 11.758 1.00 24.71 ? 94  TYR   C CD2 1 
ATOM   1773 C  CE1 . TYR   B 1 88  ? 0.820  -12.215 11.988 1.00 26.12 ? 94  TYR   C CE1 1 
ATOM   1774 C  CE2 . TYR   B 1 88  ? 1.462  -9.917  12.039 1.00 26.21 ? 94  TYR   C CE2 1 
ATOM   1775 C  CZ  . TYR   B 1 88  ? 0.498  -10.895 12.187 1.00 27.83 ? 94  TYR   C CZ  1 
ATOM   1776 O  OH  . TYR   B 1 88  ? -0.826 -10.571 12.413 1.00 31.62 ? 94  TYR   C OH  1 
ATOM   1777 N  N   . GLN   B 1 89  ? 6.840  -14.112 12.744 1.00 10.90 ? 95  GLN   C N   1 
ATOM   1778 C  CA  . GLN   B 1 89  ? 8.006  -14.902 12.362 1.00 10.00 ? 95  GLN   C CA  1 
ATOM   1779 C  C   . GLN   B 1 89  ? 7.608  -15.779 11.185 1.00 10.20 ? 95  GLN   C C   1 
ATOM   1780 O  O   . GLN   B 1 89  ? 6.535  -16.430 11.231 1.00 11.20 ? 95  GLN   C O   1 
ATOM   1781 C  CB  . GLN   B 1 89  ? 8.469  -15.744 13.555 1.00 10.65 ? 95  GLN   C CB  1 
ATOM   1782 C  CG  . GLN   B 1 89  ? 9.651  -16.671 13.193 1.00 9.98  ? 95  GLN   C CG  1 
ATOM   1783 C  CD  . GLN   B 1 89  ? 10.399 -17.161 14.424 1.00 9.62  ? 95  GLN   C CD  1 
ATOM   1784 O  OE1 . GLN   B 1 89  ? 10.614 -16.436 15.395 1.00 10.13 ? 95  GLN   C OE1 1 
ATOM   1785 N  NE2 . GLN   B 1 89  ? 10.853 -18.421 14.366 1.00 8.78  ? 95  GLN   C NE2 1 
ATOM   1786 N  N   . SER   B 1 90  ? 8.414  -15.781 10.125 1.00 9.47  ? 96  SER   C N   1 
ATOM   1787 C  CA  . SER   B 1 90  ? 8.159  -16.554 8.933  1.00 8.98  ? 96  SER   C CA  1 
ATOM   1788 C  C   . SER   B 1 90  ? 8.792  -17.944 9.010  1.00 8.98  ? 96  SER   C C   1 
ATOM   1789 O  O   . SER   B 1 90  ? 9.690  -18.208 9.855  1.00 9.18  ? 96  SER   C O   1 
ATOM   1790 C  CB  . SER   B 1 90  ? 8.659  -15.813 7.691  1.00 10.57 ? 96  SER   C CB  1 
ATOM   1791 O  OG  . SER   B 1 90  ? 10.067 -15.647 7.788  1.00 13.10 ? 96  SER   C OG  1 
ATOM   1792 N  N   . HIS   B 1 91  ? 8.296  -18.858 8.128  1.00 9.08  ? 97  HIS   C N   1 
ATOM   1793 C  CA  . HIS   B 1 91  ? 8.832  -20.213 7.999  1.00 8.86  ? 97  HIS   C CA  1 
ATOM   1794 C  C   . HIS   B 1 91  ? 8.743  -20.987 9.333  1.00 9.60  ? 97  HIS   C C   1 
ATOM   1795 O  O   . HIS   B 1 91  ? 9.587  -21.838 9.598  1.00 9.30  ? 97  HIS   C O   1 
ATOM   1796 C  CB  . HIS   B 1 91  ? 10.287 -20.194 7.437  1.00 10.13 ? 97  HIS   C CB  1 
ATOM   1797 C  CG  . HIS   B 1 91  ? 10.393 -19.562 6.073  1.00 10.19 ? 97  HIS   C CG  1 
ATOM   1798 N  ND1 . HIS   B 1 91  ? 10.356 -20.333 4.919  1.00 12.92 ? 97  HIS   C ND1 1 
ATOM   1799 C  CD2 . HIS   B 1 91  ? 10.476 -18.252 5.721  1.00 11.52 ? 97  HIS   C CD2 1 
ATOM   1800 C  CE1 . HIS   B 1 91  ? 10.470 -19.473 3.899  1.00 13.58 ? 97  HIS   C CE1 1 
ATOM   1801 N  NE2 . HIS   B 1 91  ? 10.538 -18.208 4.335  1.00 13.53 ? 97  HIS   C NE2 1 
ATOM   1802 N  N   . LEU   B 1 92  ? 7.720  -20.715 10.136 1.00 8.87  ? 98  LEU   C N   1 
ATOM   1803 C  CA  . LEU   B 1 92  ? 7.559  -21.325 11.458 1.00 8.51  ? 98  LEU   C CA  1 
ATOM   1804 C  C   . LEU   B 1 92  ? 6.464  -22.400 11.375 1.00 9.43  ? 98  LEU   C C   1 
ATOM   1805 O  O   . LEU   B 1 92  ? 5.433  -22.226 10.706 1.00 9.67  ? 98  LEU   C O   1 
ATOM   1806 C  CB  . LEU   B 1 92  ? 7.153  -20.226 12.478 1.00 9.68  ? 98  LEU   C CB  1 
ATOM   1807 C  CG  . LEU   B 1 92  ? 7.027  -20.634 13.939 1.00 10.69 ? 98  LEU   C CG  1 
ATOM   1808 C  CD1 . LEU   B 1 92  ? 8.396  -21.053 14.513 1.00 11.20 ? 98  LEU   C CD1 1 
ATOM   1809 C  CD2 . LEU   B 1 92  ? 6.559  -19.430 14.839 1.00 14.56 ? 98  LEU   C CD2 1 
ATOM   1810 N  N   . MET   B 1 93  ? 6.702  -23.508 12.080 1.00 8.81  ? 99  MET   C N   1 
ATOM   1811 C  CA  . MET   B 1 93  ? 5.772  -24.652 12.122 1.00 8.79  ? 99  MET   C CA  1 
ATOM   1812 C  C   . MET   B 1 93  ? 5.397  -24.909 13.558 1.00 9.26  ? 99  MET   C C   1 
ATOM   1813 O  O   . MET   B 1 93  ? 6.292  -24.921 14.417 1.00 10.05 ? 99  MET   C O   1 
ATOM   1814 C  CB  . MET   B 1 93  ? 6.463  -25.912 11.570 1.00 8.51  ? 99  MET   C CB  1 
ATOM   1815 C  CG  . MET   B 1 93  ? 6.872  -25.688 10.126 1.00 9.57  ? 99  MET   C CG  1 
ATOM   1816 S  SD  . MET   B 1 93  ? 7.895  -27.004 9.477  1.00 11.60 ? 99  MET   C SD  1 
ATOM   1817 C  CE  . MET   B 1 93  ? 9.408  -26.890 10.512 1.00 12.57 ? 99  MET   C CE  1 
ATOM   1818 N  N   . LEU   B 1 94  ? 4.111  -25.184 13.852 1.00 8.11  ? 100 LEU   C N   1 
ATOM   1819 C  CA  . LEU   B 1 94  ? 3.709  -25.452 15.233 1.00 7.63  ? 100 LEU   C CA  1 
ATOM   1820 C  C   . LEU   B 1 94  ? 3.323  -26.913 15.437 1.00 8.19  ? 100 LEU   C C   1 
ATOM   1821 O  O   . LEU   B 1 94  ? 2.804  -27.590 14.532 1.00 8.14  ? 100 LEU   C O   1 
ATOM   1822 C  CB  . LEU   B 1 94  ? 2.492  -24.587 15.670 1.00 9.84  ? 100 LEU   C CB  1 
ATOM   1823 C  CG  . LEU   B 1 94  ? 2.671  -23.081 15.541 1.00 10.81 ? 100 LEU   C CG  1 
ATOM   1824 C  CD1 . LEU   B 1 94  ? 1.394  -22.316 16.016 1.00 13.77 ? 100 LEU   C CD1 1 
ATOM   1825 C  CD2 . LEU   B 1 94  ? 3.881  -22.598 16.321 1.00 12.19 ? 100 LEU   C CD2 1 
ATOM   1826 N  N   . ALA   B 1 95  ? 3.550  -27.398 16.668 1.00 8.11  ? 101 ALA   C N   1 
ATOM   1827 C  CA  . ALA   B 1 95  ? 3.084  -28.735 17.107 1.00 8.47  ? 101 ALA   C CA  1 
ATOM   1828 C  C   . ALA   B 1 95  ? 2.534  -28.585 18.523 1.00 8.18  ? 101 ALA   C C   1 
ATOM   1829 O  O   . ALA   B 1 95  ? 2.850  -27.620 19.251 1.00 9.31  ? 101 ALA   C O   1 
ATOM   1830 C  CB  . ALA   B 1 95  ? 4.245  -29.752 17.154 1.00 9.31  ? 101 ALA   C CB  1 
ATOM   1831 N  N   . VAL   B 1 96  ? 1.663  -29.516 18.919 1.00 8.82  ? 102 VAL   C N   1 
ATOM   1832 C  CA  . VAL   B 1 96  ? 1.225  -29.583 20.320 1.00 9.02  ? 102 VAL   C CA  1 
ATOM   1833 C  C   . VAL   B 1 96  ? 2.305  -30.316 21.110 1.00 10.64 ? 102 VAL   C C   1 
ATOM   1834 O  O   . VAL   B 1 96  ? 2.564  -31.498 20.841 1.00 11.96 ? 102 VAL   C O   1 
ATOM   1835 C  CB  . VAL   B 1 96  ? -0.161 -30.313 20.386 1.00 9.90  ? 102 VAL   C CB  1 
ATOM   1836 C  CG1 . VAL   B 1 96  ? -0.623 -30.428 21.848 1.00 11.35 ? 102 VAL   C CG1 1 
ATOM   1837 C  CG2 . VAL   B 1 96  ? -1.193 -29.528 19.567 1.00 12.44 ? 102 VAL   C CG2 1 
ATOM   1838 N  N   . GLY   B 1 97  ? 2.956  -29.622 22.007 1.00 10.59 ? 103 GLY   C N   1 
ATOM   1839 C  CA  . GLY   B 1 97  ? 4.035  -30.250 22.767 1.00 13.15 ? 103 GLY   C CA  1 
ATOM   1840 C  C   . GLY   B 1 97  ? 4.664  -29.292 23.723 1.00 13.69 ? 103 GLY   C C   1 
ATOM   1841 O  O   . GLY   B 1 97  ? 4.436  -28.075 23.674 1.00 14.08 ? 103 GLY   C O   1 
ATOM   1842 N  N   . HIS   B 1 98  ? 5.505  -29.824 24.607 1.00 12.89 ? 104 HIS   C N   1 
ATOM   1843 C  CA  . HIS   B 1 98  ? 6.162  -29.013 25.603 1.00 13.19 ? 104 HIS   C CA  1 
ATOM   1844 C  C   . HIS   B 1 98  ? 7.428  -28.342 25.097 1.00 12.49 ? 104 HIS   C C   1 
ATOM   1845 O  O   . HIS   B 1 98  ? 8.279  -28.951 24.434 1.00 12.10 ? 104 HIS   C O   1 
ATOM   1846 C  CB  . HIS   B 1 98  ? 6.565  -29.927 26.788 1.00 14.02 ? 104 HIS   C CB  1 
ATOM   1847 C  CG  . HIS   B 1 98  ? 7.211  -29.154 27.895 1.00 13.85 ? 104 HIS   C CG  1 
ATOM   1848 N  ND1 . HIS   B 1 98  ? 6.485  -28.221 28.648 1.00 16.96 ? 104 HIS   C ND1 1 
ATOM   1849 C  CD2 . HIS   B 1 98  ? 8.516  -29.124 28.304 1.00 13.83 ? 104 HIS   C CD2 1 
ATOM   1850 C  CE1 . HIS   B 1 98  ? 7.371  -27.673 29.479 1.00 17.02 ? 104 HIS   C CE1 1 
ATOM   1851 N  NE2 . HIS   B 1 98  ? 8.592  -28.195 29.317 1.00 16.68 ? 104 HIS   C NE2 1 
ATOM   1852 N  N   . SER   B 1 99  ? 7.606  -27.090 25.499 1.00 12.43 ? 105 SER   C N   1 
ATOM   1853 C  CA  . SER   B 1 99  ? 8.852  -26.356 25.322 1.00 13.60 ? 105 SER   C CA  1 
ATOM   1854 C  C   . SER   B 1 99  ? 8.968  -25.247 26.370 1.00 14.95 ? 105 SER   C C   1 
ATOM   1855 O  O   . SER   B 1 99  ? 7.956  -24.675 26.820 1.00 17.55 ? 105 SER   C O   1 
ATOM   1856 C  CB  . SER   B 1 99  ? 9.030  -25.823 23.916 1.00 16.16 ? 105 SER   C CB  1 
ATOM   1857 O  OG  . SER   B 1 99  ? 8.007  -24.882 23.682 1.00 18.81 ? 105 SER   C OG  1 
ATOM   1858 N  N   . GLU   B 1 100 ? 10.194 -24.980 26.751 1.00 12.69 ? 106 GLU   C N   1 
ATOM   1859 C  CA  . GLU   B 1 100 ? 10.633 -23.916 27.703 1.00 14.80 ? 106 GLU   C CA  1 
ATOM   1860 C  C   . GLU   B 1 100 ? 11.806 -23.187 27.038 1.00 15.89 ? 106 GLU   C C   1 
ATOM   1861 O  O   . GLU   B 1 100 ? 12.387 -23.705 26.102 1.00 17.02 ? 106 GLU   C O   1 
ATOM   1862 C  CB  . GLU   B 1 100 ? 11.164 -24.563 28.980 1.00 19.62 ? 106 GLU   C CB  1 
ATOM   1863 C  CG  . GLU   B 1 100 ? 10.030 -25.207 29.690 1.00 22.96 ? 106 GLU   C CG  1 
ATOM   1864 C  CD  . GLU   B 1 100 ? 10.452 -25.861 30.985 1.00 22.18 ? 106 GLU   C CD  1 
ATOM   1865 O  OE1 . GLU   B 1 100 ? 11.328 -25.310 31.683 1.00 27.50 ? 106 GLU   C OE1 1 
ATOM   1866 O  OE2 . GLU   B 1 100 ? 9.891  -26.921 31.305 1.00 22.80 ? 106 GLU   C OE2 1 
ATOM   1867 N  N   . PRO   B 1 101 ? 12.145 -21.927 27.447 1.00 17.89 ? 107 PRO   C N   1 
ATOM   1868 C  CA  . PRO   B 1 101 ? 13.122 -21.135 26.615 1.00 17.97 ? 107 PRO   C CA  1 
ATOM   1869 C  C   . PRO   B 1 101 ? 14.469 -21.825 26.243 1.00 15.91 ? 107 PRO   C C   1 
ATOM   1870 O  O   . PRO   B 1 101 ? 14.995 -21.726 25.084 1.00 17.77 ? 107 PRO   C O   1 
ATOM   1871 C  CB  . PRO   B 1 101 ? 13.326 -19.858 27.438 1.00 19.73 ? 107 PRO   C CB  1 
ATOM   1872 C  CG  . PRO   B 1 101 ? 11.983 -19.701 28.208 1.00 20.93 ? 107 PRO   C CG  1 
ATOM   1873 C  CD  . PRO   B 1 101 ? 11.474 -21.119 28.483 1.00 18.88 ? 107 PRO   C CD  1 
ATOM   1874 N  N   . GLY   B 1 102 ? 15.006 -22.553 27.245 1.00 13.78 ? 108 GLY   C N   1 
ATOM   1875 C  CA  . GLY   B 1 102 ? 16.222 -23.334 27.154 1.00 14.39 ? 108 GLY   C CA  1 
ATOM   1876 C  C   . GLY   B 1 102 ? 16.143 -24.484 26.163 1.00 12.83 ? 108 GLY   C C   1 
ATOM   1877 O  O   . GLY   B 1 102 ? 17.163 -25.085 25.842 1.00 13.34 ? 108 GLY   C O   1 
ATOM   1878 N  N   . ASP   B 1 103 ? 14.947 -24.766 25.651 1.00 12.06 ? 109 ASP   C N   1 
ATOM   1879 C  CA  . ASP   B 1 103 ? 14.757 -25.808 24.639 1.00 11.05 ? 109 ASP   C CA  1 
ATOM   1880 C  C   . ASP   B 1 103 ? 15.052 -25.346 23.219 1.00 9.59  ? 109 ASP   C C   1 
ATOM   1881 O  O   . ASP   B 1 103 ? 15.160 -26.195 22.328 1.00 10.24 ? 109 ASP   C O   1 
ATOM   1882 C  CB  . ASP   B 1 103 ? 13.309 -26.359 24.667 1.00 11.56 ? 109 ASP   C CB  1 
ATOM   1883 C  CG  . ASP   B 1 103 ? 13.053 -27.178 25.928 1.00 13.71 ? 109 ASP   C CG  1 
ATOM   1884 O  OD1 . ASP   B 1 103 ? 14.002 -27.819 26.417 1.00 13.57 ? 109 ASP   C OD1 1 
ATOM   1885 O  OD2 . ASP   B 1 103 ? 11.892 -27.173 26.411 1.00 13.30 ? 109 ASP   C OD2 1 
ATOM   1886 N  N   . CYS   B 1 104 ? 15.229 -24.010 22.985 1.00 9.52  ? 110 CYS   C N   1 
ATOM   1887 C  CA  . CYS   B 1 104 ? 15.564 -23.551 21.630 1.00 9.49  ? 110 CYS   C CA  1 
ATOM   1888 C  C   . CYS   B 1 104 ? 16.838 -24.190 21.138 1.00 10.44 ? 110 CYS   C C   1 
ATOM   1889 O  O   . CYS   B 1 104 ? 17.801 -24.365 21.909 1.00 11.46 ? 110 CYS   C O   1 
ATOM   1890 C  CB  . CYS   B 1 104 ? 15.658 -22.031 21.566 1.00 9.87  ? 110 CYS   C CB  1 
ATOM   1891 S  SG  . CYS   B 1 104 ? 14.052 -21.188 21.697 1.00 13.43 ? 110 CYS   C SG  1 
ATOM   1892 N  N   . GLY   B 1 105 ? 16.817 -24.590 19.882 1.00 9.17  ? 111 GLY   C N   1 
ATOM   1893 C  CA  . GLY   B 1 105 ? 17.976 -25.258 19.297 1.00 10.21 ? 111 GLY   C CA  1 
ATOM   1894 C  C   . GLY   B 1 105 ? 17.812 -26.766 19.206 1.00 10.68 ? 111 GLY   C C   1 
ATOM   1895 O  O   . GLY   B 1 105 ? 18.572 -27.443 18.493 1.00 11.38 ? 111 GLY   C O   1 
ATOM   1896 N  N   . GLY   B 1 106 ? 16.822 -27.329 19.948 1.00 8.66  ? 112 GLY   C N   1 
ATOM   1897 C  CA  . GLY   B 1 106 ? 16.539 -28.756 19.828 1.00 8.79  ? 112 GLY   C CA  1 
ATOM   1898 C  C   . GLY   B 1 106 ? 16.125 -29.110 18.411 1.00 8.43  ? 112 GLY   C C   1 
ATOM   1899 O  O   . GLY   B 1 106 ? 15.332 -28.386 17.792 1.00 9.20  ? 112 GLY   C O   1 
ATOM   1900 N  N   . ILE   B 1 107 ? 16.635 -30.233 17.897 1.00 8.69  ? 113 ILE   C N   1 
ATOM   1901 C  CA  . ILE   B 1 107 ? 16.359 -30.592 16.510 1.00 9.32  ? 113 ILE   C CA  1 
ATOM   1902 C  C   . ILE   B 1 107 ? 15.053 -31.357 16.335 1.00 8.55  ? 113 ILE   C C   1 
ATOM   1903 O  O   . ILE   B 1 107 ? 14.738 -32.258 17.136 1.00 9.42  ? 113 ILE   C O   1 
ATOM   1904 C  CB  . ILE   B 1 107 ? 17.586 -31.377 15.929 1.00 13.02 ? 113 ILE   C CB  1 
ATOM   1905 C  CG1 . ILE   B 1 107 ? 18.758 -30.406 15.615 1.00 17.24 ? 113 ILE   C CG1 1 
ATOM   1906 C  CG2 . ILE   B 1 107 ? 17.213 -32.185 14.630 1.00 15.02 ? 113 ILE   C CG2 1 
ATOM   1907 C  CD1 . ILE   B 1 107 ? 20.072 -31.201 15.165 1.00 20.99 ? 113 ILE   C CD1 1 
ATOM   1908 N  N   . LEU   B 1 108 ? 14.319 -31.000 15.277 1.00 7.89  ? 114 LEU   C N   1 
ATOM   1909 C  CA  . LEU   B 1 108 ? 13.139 -31.768 14.794 1.00 7.24  ? 114 LEU   C CA  1 
ATOM   1910 C  C   . LEU   B 1 108 ? 13.648 -32.553 13.570 1.00 7.73  ? 114 LEU   C C   1 
ATOM   1911 O  O   . LEU   B 1 108 ? 14.230 -31.953 12.638 1.00 8.31  ? 114 LEU   C O   1 
ATOM   1912 C  CB  . LEU   B 1 108 ? 12.038 -30.770 14.364 1.00 7.84  ? 114 LEU   C CB  1 
ATOM   1913 C  CG  . LEU   B 1 108 ? 10.821 -31.390 13.647 1.00 7.93  ? 114 LEU   C CG  1 
ATOM   1914 C  CD1 . LEU   B 1 108 ? 10.016 -32.367 14.563 1.00 9.35  ? 114 LEU   C CD1 1 
ATOM   1915 C  CD2 . LEU   B 1 108 ? 9.878  -30.260 13.104 1.00 9.77  ? 114 LEU   C CD2 1 
ATOM   1916 N  N   . ARG   B 1 109 ? 13.379 -33.867 13.548 1.00 7.65  ? 115 ARG   C N   1 
ATOM   1917 C  CA  . ARG   B 1 109 ? 13.804 -34.754 12.446 1.00 8.60  ? 115 ARG   C CA  1 
ATOM   1918 C  C   . ARG   B 1 109 ? 12.629 -35.542 11.945 1.00 9.28  ? 115 ARG   C C   1 
ATOM   1919 O  O   . ARG   B 1 109 ? 11.797 -36.007 12.742 1.00 10.79 ? 115 ARG   C O   1 
ATOM   1920 C  CB  . ARG   B 1 109 ? 14.825 -35.807 12.965 1.00 11.29 ? 115 ARG   C CB  1 
ATOM   1921 C  CG  . ARG   B 1 109 ? 16.115 -35.252 13.421 1.00 17.12 ? 115 ARG   C CG  1 
ATOM   1922 C  CD  . ARG   B 1 109 ? 16.967 -36.415 13.959 1.00 22.09 ? 115 ARG   C CD  1 
ATOM   1923 N  NE  . ARG   B 1 109 ? 17.520 -37.064 12.788 1.00 29.82 ? 115 ARG   C NE  1 
ATOM   1924 C  CZ  . ARG   B 1 109 ? 18.665 -36.694 12.218 1.00 34.45 ? 115 ARG   C CZ  1 
ATOM   1925 N  NH1 . ARG   B 1 109 ? 19.481 -35.847 12.837 1.00 36.86 ? 115 ARG   C NH1 1 
ATOM   1926 N  NH2 . ARG   B 1 109 ? 19.028 -37.210 11.066 1.00 36.43 ? 115 ARG   C NH2 1 
ATOM   1927 N  N   . CYS   B 1 110 ? 12.587 -35.789 10.644 1.00 8.55  ? 116 CYS   C N   1 
ATOM   1928 C  CA  . CYS   B 1 110 ? 11.588 -36.726 10.045 1.00 9.57  ? 116 CYS   C CA  1 
ATOM   1929 C  C   . CYS   B 1 110 ? 12.370 -37.912 9.512  1.00 11.82 ? 116 CYS   C C   1 
ATOM   1930 O  O   . CYS   B 1 110 ? 13.603 -38.003 9.661  1.00 10.69 ? 116 CYS   C O   1 
ATOM   1931 C  CB  . CYS   B 1 110 ? 10.793 -36.040 8.926  1.00 8.66  ? 116 CYS   C CB  1 
ATOM   1932 S  SG  . CYS   B 1 110 ? 11.823 -35.534 7.520  1.00 8.44  ? 116 CYS   C SG  1 
ATOM   1933 N  N   . GLN   B 1 111 ? 11.662 -38.802 8.771  1.00 12.15 ? 117 GLN   C N   1 
ATOM   1934 C  CA  . GLN   B 1 111 ? 12.334 -39.953 8.188  1.00 13.53 ? 117 GLN   C CA  1 
ATOM   1935 C  C   . GLN   B 1 111 ? 13.437 -39.560 7.176  1.00 12.80 ? 117 GLN   C C   1 
ATOM   1936 O  O   . GLN   B 1 111 ? 14.287 -40.395 6.815  1.00 16.39 ? 117 GLN   C O   1 
ATOM   1937 C  CB  . GLN   B 1 111 ? 11.298 -40.894 7.540  1.00 16.15 ? 117 GLN   C CB  1 
ATOM   1938 C  CG  . GLN   B 1 111 ? 10.631 -40.275 6.311  1.00 17.53 ? 117 GLN   C CG  1 
ATOM   1939 C  CD  . GLN   B 1 111 ? 9.622  -41.226 5.703  1.00 26.55 ? 117 GLN   C CD  1 
ATOM   1940 O  OE1 . GLN   B 1 111 ? 8.412  -40.976 5.773  1.00 28.85 ? 117 GLN   C OE1 1 
ATOM   1941 N  NE2 . GLN   B 1 111 ? 10.096 -42.298 5.067  1.00 28.88 ? 117 GLN   C NE2 1 
ATOM   1942 N  N   . HIS   B 1 112 ? 13.439 -38.293 6.666  1.00 11.23 ? 118 HIS   C N   1 
ATOM   1943 C  CA  . HIS   B 1 112 ? 14.397 -37.866 5.660  1.00 11.60 ? 118 HIS   C CA  1 
ATOM   1944 C  C   . HIS   B 1 112 ? 15.604 -37.112 6.223  1.00 12.97 ? 118 HIS   C C   1 
ATOM   1945 O  O   . HIS   B 1 112 ? 16.506 -36.815 5.448  1.00 14.84 ? 118 HIS   C O   1 
ATOM   1946 C  CB  . HIS   B 1 112 ? 13.714 -36.952 4.617  1.00 11.09 ? 118 HIS   C CB  1 
ATOM   1947 C  CG  . HIS   B 1 112 ? 12.515 -37.597 3.970  1.00 11.05 ? 118 HIS   C CG  1 
ATOM   1948 N  ND1 . HIS   B 1 112 ? 11.222 -37.183 4.278  1.00 10.08 ? 118 HIS   C ND1 1 
ATOM   1949 C  CD2 . HIS   B 1 112 ? 12.462 -38.598 3.043  1.00 13.39 ? 118 HIS   C CD2 1 
ATOM   1950 C  CE1 . HIS   B 1 112 ? 10.405 -37.972 3.577  1.00 11.60 ? 118 HIS   C CE1 1 
ATOM   1951 N  NE2 . HIS   B 1 112 ? 11.088 -38.870 2.826  1.00 13.89 ? 118 HIS   C NE2 1 
ATOM   1952 N  N   . GLY   B 1 113 ? 15.590 -36.745 7.503  1.00 11.14 ? 119 GLY   C N   1 
ATOM   1953 C  CA  . GLY   B 1 113 ? 16.691 -35.972 8.091  1.00 10.69 ? 119 GLY   C CA  1 
ATOM   1954 C  C   . GLY   B 1 113 ? 16.214 -34.804 8.938  1.00 9.68  ? 119 GLY   C C   1 
ATOM   1955 O  O   . GLY   B 1 113 ? 15.081 -34.790 9.453  1.00 9.65  ? 119 GLY   C O   1 
ATOM   1956 N  N   . VAL   B 1 114 ? 17.099 -33.824 9.075  1.00 9.50  ? 120 VAL   C N   1 
ATOM   1957 C  CA  . VAL   B 1 114 ? 16.789 -32.647 9.911  1.00 8.76  ? 120 VAL   C CA  1 
ATOM   1958 C  C   . VAL   B 1 114 ? 15.782 -31.724 9.255  1.00 8.24  ? 120 VAL   C C   1 
ATOM   1959 O  O   . VAL   B 1 114 ? 15.995 -31.313 8.083  1.00 9.37  ? 120 VAL   C O   1 
ATOM   1960 C  CB  . VAL   B 1 114 ? 18.091 -31.884 10.216 1.00 10.17 ? 120 VAL   C CB  1 
ATOM   1961 C  CG1 . VAL   B 1 114 ? 17.777 -30.576 10.970 1.00 11.47 ? 120 VAL   C CG1 1 
ATOM   1962 C  CG2 . VAL   B 1 114 ? 19.035 -32.794 11.050 1.00 12.14 ? 120 VAL   C CG2 1 
ATOM   1963 N  N   . VAL   B 1 115 ? 14.702 -31.375 9.958  1.00 8.42  ? 121 VAL   C N   1 
ATOM   1964 C  CA  . VAL   B 1 115 ? 13.631 -30.512 9.455  1.00 7.97  ? 121 VAL   C CA  1 
ATOM   1965 C  C   . VAL   B 1 115 ? 13.826 -29.064 9.897  1.00 8.54  ? 121 VAL   C C   1 
ATOM   1966 O  O   . VAL   B 1 115 ? 13.589 -28.113 9.133  1.00 8.84  ? 121 VAL   C O   1 
ATOM   1967 C  CB  . VAL   B 1 115 ? 12.248 -31.041 9.920  1.00 7.75  ? 121 VAL   C CB  1 
ATOM   1968 C  CG1 . VAL   B 1 115 ? 11.127 -30.068 9.548  1.00 8.45  ? 121 VAL   C CG1 1 
ATOM   1969 C  CG2 . VAL   B 1 115 ? 12.004 -32.394 9.285  1.00 8.88  ? 121 VAL   C CG2 1 
ATOM   1970 N  N   . GLY   B 1 116 ? 14.216 -28.886 11.164 1.00 7.90  ? 122 GLY   C N   1 
ATOM   1971 C  CA  . GLY   B 1 116 ? 14.345 -27.534 11.713 1.00 9.21  ? 122 GLY   C CA  1 
ATOM   1972 C  C   . GLY   B 1 116 ? 14.712 -27.574 13.179 1.00 8.20  ? 122 GLY   C C   1 
ATOM   1973 O  O   . GLY   B 1 116 ? 15.118 -28.651 13.686 1.00 8.47  ? 122 GLY   C O   1 
ATOM   1974 N  N   . ILE   B 1 117 ? 14.659 -26.403 13.845 1.00 8.23  ? 123 ILE   C N   1 
ATOM   1975 C  CA  . ILE   B 1 117 ? 15.065 -26.329 15.256 1.00 8.23  ? 123 ILE   C CA  1 
ATOM   1976 C  C   . ILE   B 1 117 ? 14.007 -25.613 16.081 1.00 8.47  ? 123 ILE   C C   1 
ATOM   1977 O  O   . ILE   B 1 117 ? 13.332 -24.695 15.576 1.00 8.52  ? 123 ILE   C O   1 
ATOM   1978 C  CB  . ILE   B 1 117 ? 16.426 -25.608 15.449 1.00 9.84  ? 123 ILE   C CB  1 
ATOM   1979 C  CG1 . ILE   B 1 117 ? 16.437 -24.249 14.741 1.00 10.30 ? 123 ILE   C CG1 1 
ATOM   1980 C  CG2 . ILE   B 1 117 ? 17.618 -26.518 15.041 1.00 11.10 ? 123 ILE   C CG2 1 
ATOM   1981 C  CD1 . ILE   B 1 117 ? 17.793 -23.453 15.024 1.00 11.61 ? 123 ILE   C CD1 1 
ATOM   1982 N  N   . VAL   B 1 118 ? 13.880 -25.970 17.377 1.00 7.30  ? 124 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 118 ? 12.925 -25.264 18.253 1.00 7.48  ? 124 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 118 ? 13.268 -23.761 18.303 1.00 7.64  ? 124 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 118 ? 14.469 -23.408 18.465 1.00 8.27  ? 124 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 118 ? 12.974 -25.850 19.675 1.00 7.81  ? 124 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 118 ? 12.100 -25.033 20.640 1.00 8.79  ? 124 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 118 ? 12.534 -27.308 19.680 1.00 9.44  ? 124 VAL   C CG2 1 
ATOM   1989 N  N   . SER   B 1 119 ? 12.263 -22.907 18.128 1.00 7.80  ? 125 SER   C N   1 
ATOM   1990 C  CA  . SER   B 1 119 ? 12.420 -21.462 18.147 1.00 7.02  ? 125 SER   C CA  1 
ATOM   1991 C  C   . SER   B 1 119 ? 11.434 -20.739 19.016 1.00 8.53  ? 125 SER   C C   1 
ATOM   1992 O  O   . SER   B 1 119 ? 11.755 -19.625 19.490 1.00 9.50  ? 125 SER   C O   1 
ATOM   1993 C  CB  . SER   B 1 119 ? 12.353 -20.998 16.692 1.00 8.26  ? 125 SER   C CB  1 
ATOM   1994 O  OG  . SER   B 1 119 ? 12.452 -19.577 16.540 1.00 8.90  ? 125 SER   C OG  1 
ATOM   1995 N  N   . THR   B 1 120 ? 10.238 -21.274 19.265 1.00 9.42  ? 126 THR   C N   1 
ATOM   1996 C  CA  . THR   B 1 120 ? 9.236  -20.574 20.106 1.00 10.54 ? 126 THR   C CA  1 
ATOM   1997 C  C   . THR   B 1 120 ? 8.477  -21.613 20.937 1.00 10.61 ? 126 THR   C C   1 
ATOM   1998 O  O   . THR   B 1 120 ? 8.547  -22.824 20.678 1.00 10.43 ? 126 THR   C O   1 
ATOM   1999 C  CB  . THR   B 1 120 ? 8.169  -19.828 19.211 1.00 12.45 ? 126 THR   C CB  1 
ATOM   2000 O  OG1 . THR   B 1 120 ? 7.302  -20.787 18.561 1.00 14.32 ? 126 THR   C OG1 1 
ATOM   2001 C  CG2 . THR   B 1 120 ? 8.782  -18.877 18.218 1.00 13.99 ? 126 THR   C CG2 1 
ATOM   2002 N  N   . GLY   B 1 121 ? 7.747  -21.144 21.942 1.00 11.71 ? 127 GLY   C N   1 
ATOM   2003 C  CA  . GLY   B 1 121 ? 6.882  -22.004 22.748 1.00 13.79 ? 127 GLY   C CA  1 
ATOM   2004 C  C   . GLY   B 1 121 ? 5.844  -21.191 23.484 1.00 15.09 ? 127 GLY   C C   1 
ATOM   2005 O  O   . GLY   B 1 121 ? 5.988  -20.006 23.661 1.00 15.88 ? 127 GLY   C O   1 
ATOM   2006 N  N   . GLY   B 1 122 ? 4.816  -21.850 23.985 1.00 17.81 ? 128 GLY   C N   1 
ATOM   2007 C  CA  . GLY   B 1 122 ? 3.785  -21.191 24.787 1.00 19.86 ? 128 GLY   C CA  1 
ATOM   2008 C  C   . GLY   B 1 122 ? 2.467  -21.897 24.622 1.00 19.93 ? 128 GLY   C C   1 
ATOM   2009 O  O   . GLY   B 1 122 ? 2.200  -22.436 23.560 1.00 19.66 ? 128 GLY   C O   1 
ATOM   2010 N  N   . ASN   B 1 123 ? 1.616  -21.837 25.671 1.00 19.51 ? 129 ASN   C N   1 
ATOM   2011 C  CA  . ASN   B 1 123 ? 0.278  -22.424 25.686 1.00 19.81 ? 129 ASN   C CA  1 
ATOM   2012 C  C   . ASN   B 1 123 ? 0.265  -23.896 25.244 1.00 18.47 ? 129 ASN   C C   1 
ATOM   2013 O  O   . ASN   B 1 123 ? -0.717 -24.347 24.638 1.00 19.90 ? 129 ASN   C O   1 
ATOM   2014 C  CB  . ASN   B 1 123 ? -0.646 -21.625 24.770 1.00 21.43 ? 129 ASN   C CB  1 
ATOM   2015 C  CG  . ASN   B 1 123 ? -0.938 -20.268 25.260 1.00 25.12 ? 129 ASN   C CG  1 
ATOM   2016 O  OD1 . ASN   B 1 123 ? -1.104 -20.057 26.443 1.00 24.87 ? 129 ASN   C OD1 1 
ATOM   2017 N  ND2 . ASN   B 1 123 ? -1.083 -19.356 24.325 1.00 28.27 ? 129 ASN   C ND2 1 
ATOM   2018 N  N   . GLY   B 1 124 ? 1.312  -24.667 25.548 1.00 15.47 ? 130 GLY   C N   1 
ATOM   2019 C  CA  . GLY   B 1 124 ? 1.358  -26.067 25.130 1.00 14.34 ? 130 GLY   C CA  1 
ATOM   2020 C  C   . GLY   B 1 124 ? 1.615  -26.288 23.646 1.00 12.53 ? 130 GLY   C C   1 
ATOM   2021 O  O   . GLY   B 1 124 ? 1.326  -27.369 23.121 1.00 13.25 ? 130 GLY   C O   1 
ATOM   2022 N  N   . LEU   B 1 125 ? 2.191  -25.303 22.988 1.00 11.60 ? 131 LEU   C N   1 
ATOM   2023 C  CA  . LEU   B 1 125 ? 2.575  -25.373 21.590 1.00 11.65 ? 131 LEU   C CA  1 
ATOM   2024 C  C   . LEU   B 1 125 ? 4.089  -25.195 21.508 1.00 13.53 ? 131 LEU   C C   1 
ATOM   2025 O  O   . LEU   B 1 125 ? 4.663  -24.463 22.351 1.00 18.52 ? 131 LEU   C O   1 
ATOM   2026 C  CB  . LEU   B 1 125 ? 1.832  -24.298 20.774 1.00 13.64 ? 131 LEU   C CB  1 
ATOM   2027 C  CG  . LEU   B 1 125 ? 0.283  -24.397 20.836 1.00 17.18 ? 131 LEU   C CG  1 
ATOM   2028 C  CD1 . LEU   B 1 125 ? -0.365 -23.071 20.391 1.00 20.59 ? 131 LEU   C CD1 1 
ATOM   2029 C  CD2 . LEU   B 1 125 ? -0.198 -25.496 19.920 1.00 16.86 ? 131 LEU   C CD2 1 
ATOM   2030 N  N   . VAL   B 1 126 ? 4.724  -25.860 20.576 1.00 9.65  ? 132 VAL   C N   1 
ATOM   2031 C  CA  . VAL   B 1 126 ? 6.150  -25.671 20.309 1.00 9.56  ? 132 VAL   C CA  1 
ATOM   2032 C  C   . VAL   B 1 126 ? 6.264  -25.235 18.859 1.00 9.04  ? 132 VAL   C C   1 
ATOM   2033 O  O   . VAL   B 1 126 ? 5.590  -25.805 17.965 1.00 9.05  ? 132 VAL   C O   1 
ATOM   2034 C  CB  . VAL   B 1 126 ? 6.949  -26.955 20.610 1.00 11.71 ? 132 VAL   C CB  1 
ATOM   2035 C  CG1 . VAL   B 1 126 ? 6.364  -28.216 20.009 1.00 14.24 ? 132 VAL   C CG1 1 
ATOM   2036 C  CG2 . VAL   B 1 126 ? 8.451  -26.807 20.284 1.00 11.78 ? 132 VAL   C CG2 1 
ATOM   2037 N  N   . GLY   B 1 127 ? 7.135  -24.254 18.618 1.00 7.73  ? 133 GLY   C N   1 
ATOM   2038 C  CA  . GLY   B 1 127 ? 7.332  -23.778 17.253 1.00 8.32  ? 133 GLY   C CA  1 
ATOM   2039 C  C   . GLY   B 1 127 ? 8.736  -24.080 16.771 1.00 8.16  ? 133 GLY   C C   1 
ATOM   2040 O  O   . GLY   B 1 127 ? 9.706  -23.934 17.538 1.00 9.37  ? 133 GLY   C O   1 
ATOM   2041 N  N   . PHE   B 1 128 ? 8.834  -24.516 15.500 1.00 7.39  ? 134 PHE   C N   1 
ATOM   2042 C  CA  . PHE   B 1 128 ? 10.132 -24.907 14.906 1.00 7.55  ? 134 PHE   C CA  1 
ATOM   2043 C  C   . PHE   B 1 128 ? 10.411 -24.029 13.690 1.00 7.54  ? 134 PHE   C C   1 
ATOM   2044 O  O   . PHE   B 1 128 ? 9.517  -23.840 12.836 1.00 8.12  ? 134 PHE   C O   1 
ATOM   2045 C  CB  . PHE   B 1 128 ? 10.058 -26.374 14.400 1.00 8.49  ? 134 PHE   C CB  1 
ATOM   2046 C  CG  . PHE   B 1 128 ? 9.625  -27.364 15.454 1.00 7.79  ? 134 PHE   C CG  1 
ATOM   2047 C  CD1 . PHE   B 1 128 ? 10.547 -27.916 16.334 1.00 8.11  ? 134 PHE   C CD1 1 
ATOM   2048 C  CD2 . PHE   B 1 128 ? 8.308  -27.753 15.552 1.00 9.46  ? 134 PHE   C CD2 1 
ATOM   2049 C  CE1 . PHE   B 1 128 ? 10.138 -28.842 17.299 1.00 8.58  ? 134 PHE   C CE1 1 
ATOM   2050 C  CE2 . PHE   B 1 128 ? 7.914  -28.700 16.495 1.00 9.93  ? 134 PHE   C CE2 1 
ATOM   2051 C  CZ  . PHE   B 1 128 ? 8.832  -29.235 17.360 1.00 9.33  ? 134 PHE   C CZ  1 
ATOM   2052 N  N   . ALA   B 1 129 ? 11.654 -23.526 13.632 1.00 7.41  ? 135 ALA   C N   1 
ATOM   2053 C  CA  . ALA   B 1 129 ? 12.093 -22.768 12.450 1.00 6.93  ? 135 ALA   C CA  1 
ATOM   2054 C  C   . ALA   B 1 129 ? 12.480 -23.795 11.370 1.00 7.28  ? 135 ALA   C C   1 
ATOM   2055 O  O   . ALA   B 1 129 ? 13.397 -24.614 11.586 1.00 7.72  ? 135 ALA   C O   1 
ATOM   2056 C  CB  . ALA   B 1 129 ? 13.304 -21.929 12.839 1.00 7.63  ? 135 ALA   C CB  1 
ATOM   2057 N  N   . ASP   B 1 130 ? 11.797 -23.795 10.234 1.00 7.16  ? 136 ASP   C N   1 
ATOM   2058 C  CA  . ASP   B 1 130 ? 12.100 -24.709 9.145  1.00 7.35  ? 136 ASP   C CA  1 
ATOM   2059 C  C   . ASP   B 1 130 ? 13.432 -24.405 8.489  1.00 7.94  ? 136 ASP   C C   1 
ATOM   2060 O  O   . ASP   B 1 130 ? 13.770 -23.219 8.328  1.00 8.47  ? 136 ASP   C O   1 
ATOM   2061 C  CB  . ASP   B 1 130 ? 10.959 -24.584 8.086  1.00 9.17  ? 136 ASP   C CB  1 
ATOM   2062 C  CG  . ASP   B 1 130 ? 11.083 -25.616 6.973  1.00 12.59 ? 136 ASP   C CG  1 
ATOM   2063 O  OD1 . ASP   B 1 130 ? 11.217 -26.790 7.273  1.00 12.72 ? 136 ASP   C OD1 1 
ATOM   2064 O  OD2 . ASP   B 1 130 ? 11.136 -25.215 5.788  1.00 17.12 ? 136 ASP   C OD2 1 
ATOM   2065 N  N   . VAL   B 1 131 ? 14.175 -25.444 8.060  1.00 7.98  ? 137 VAL   C N   1 
ATOM   2066 C  CA  . VAL   B 1 131 ? 15.412 -25.230 7.291  1.00 8.91  ? 137 VAL   C CA  1 
ATOM   2067 C  C   . VAL   B 1 131 ? 15.361 -26.000 5.962  1.00 9.17  ? 137 VAL   C C   1 
ATOM   2068 O  O   . VAL   B 1 131 ? 16.321 -25.939 5.175  1.00 9.58  ? 137 VAL   C O   1 
ATOM   2069 C  CB  . VAL   B 1 131 ? 16.711 -25.619 8.045  1.00 9.61  ? 137 VAL   C CB  1 
ATOM   2070 C  CG1 . VAL   B 1 131 ? 16.847 -24.778 9.331  1.00 9.44  ? 137 VAL   C CG1 1 
ATOM   2071 C  CG2 . VAL   B 1 131 ? 16.752 -27.133 8.349  1.00 9.60  ? 137 VAL   C CG2 1 
ATOM   2072 N  N   . ARG   B 1 132 ? 14.232 -26.707 5.636  1.00 8.67  ? 138 ARG   C N   1 
ATOM   2073 C  CA  . ARG   B 1 132 ? 14.192 -27.563 4.470  1.00 7.73  ? 138 ARG   C CA  1 
ATOM   2074 C  C   . ARG   B 1 132 ? 14.256 -26.813 3.149  1.00 8.88  ? 138 ARG   C C   1 
ATOM   2075 O  O   . ARG   B 1 132 ? 14.617 -27.430 2.119  1.00 10.39 ? 138 ARG   C O   1 
ATOM   2076 C  CB  . ARG   B 1 132 ? 12.949 -28.453 4.500  1.00 7.50  ? 138 ARG   C CB  1 
ATOM   2077 C  CG  . ARG   B 1 132 ? 12.934 -29.446 5.646  1.00 8.79  ? 138 ARG   C CG  1 
ATOM   2078 C  CD  . ARG   B 1 132 ? 11.612 -30.199 5.641  1.00 7.87  ? 138 ARG   C CD  1 
ATOM   2079 N  NE  . ARG   B 1 132 ? 10.537 -29.284 6.047  1.00 8.60  ? 138 ARG   C NE  1 
ATOM   2080 C  CZ  . ARG   B 1 132 ? 9.276  -29.660 6.286  1.00 8.62  ? 138 ARG   C CZ  1 
ATOM   2081 N  NH1 . ARG   B 1 132 ? 8.883  -30.904 6.031  1.00 9.19  ? 138 ARG   C NH1 1 
ATOM   2082 N  NH2 . ARG   B 1 132 ? 8.399  -28.788 6.806  1.00 9.69  ? 138 ARG   C NH2 1 
ATOM   2083 N  N   . ASP   B 1 133 ? 13.900 -25.537 3.134  1.00 9.01  ? 139 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 133 ? 13.977 -24.768 1.886  1.00 9.66  ? 139 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 133 ? 15.351 -24.186 1.656  1.00 11.14 ? 139 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 133 ? 15.581 -23.657 0.556  1.00 12.38 ? 139 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 133 ? 12.965 -23.618 1.928  1.00 11.09 ? 139 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 133 ? 13.243 -22.600 3.038  1.00 13.43 ? 139 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 133 ? 13.531 -23.025 4.171  1.00 13.31 ? 139 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 133 ? 13.197 -21.345 2.754  1.00 14.69 ? 139 ASP   C OD2 1 
ATOM   2091 N  N   . LEU   B 1 134 ? 16.310 -24.301 2.587  1.00 10.51 ? 140 LEU   C N   1 
ATOM   2092 C  CA  . LEU   B 1 134 ? 17.644 -23.700 2.404  1.00 11.14 ? 140 LEU   C CA  1 
ATOM   2093 C  C   . LEU   B 1 134 ? 18.534 -24.687 1.675  1.00 10.81 ? 140 LEU   C C   1 
ATOM   2094 O  O   . LEU   B 1 134 ? 19.397 -25.382 2.245  1.00 11.15 ? 140 LEU   C O   1 
ATOM   2095 C  CB  . LEU   B 1 134 ? 18.248 -23.329 3.781  1.00 10.94 ? 140 LEU   C CB  1 
ATOM   2096 C  CG  . LEU   B 1 134 ? 17.387 -22.391 4.636  1.00 12.17 ? 140 LEU   C CG  1 
ATOM   2097 C  CD1 . LEU   B 1 134 ? 18.012 -22.233 6.046  1.00 13.38 ? 140 LEU   C CD1 1 
ATOM   2098 C  CD2 . LEU   B 1 134 ? 17.194 -21.046 3.982  1.00 13.35 ? 140 LEU   C CD2 1 
ATOM   2099 N  N   . LEU   B 1 135 ? 18.316 -24.757 0.345  1.00 10.67 ? 141 LEU   C N   1 
ATOM   2100 C  CA  . LEU   B 1 135 ? 18.981 -25.777 -0.481 1.00 12.07 ? 141 LEU   C CA  1 
ATOM   2101 C  C   . LEU   B 1 135 ? 20.471 -25.601 -0.525 1.00 13.02 ? 141 LEU   C C   1 
ATOM   2102 O  O   . LEU   B 1 135 ? 21.202 -26.588 -0.665 1.00 14.81 ? 141 LEU   C O   1 
ATOM   2103 C  CB  . LEU   B 1 135 ? 18.392 -25.862 -1.882 1.00 12.07 ? 141 LEU   C CB  1 
ATOM   2104 C  CG  . LEU   B 1 135 ? 16.868 -25.905 -1.994 1.00 12.25 ? 141 LEU   C CG  1 
ATOM   2105 C  CD1 . LEU   B 1 135 ? 16.430 -26.118 -3.425 1.00 14.40 ? 141 LEU   C CD1 1 
ATOM   2106 C  CD2 . LEU   B 1 135 ? 16.239 -26.973 -1.102 1.00 13.54 ? 141 LEU   C CD2 1 
ATOM   2107 N  N   . TRP   B 1 136 ? 20.931 -24.322 -0.417 1.00 12.96 ? 142 TRP   C N   1 
ATOM   2108 C  CA  . TRP   B 1 136 ? 22.362 -23.997 -0.494 1.00 14.21 ? 142 TRP   C CA  1 
ATOM   2109 C  C   . TRP   B 1 136 ? 23.170 -24.593 0.683  1.00 15.40 ? 142 TRP   C C   1 
ATOM   2110 O  O   . TRP   B 1 136 ? 24.398 -24.657 0.607  1.00 16.63 ? 142 TRP   C O   1 
ATOM   2111 C  CB  . TRP   B 1 136 ? 22.533 -22.475 -0.588 1.00 14.39 ? 142 TRP   C CB  1 
ATOM   2112 C  CG  . TRP   B 1 136 ? 21.867 -21.699 0.516  1.00 13.54 ? 142 TRP   C CG  1 
ATOM   2113 C  CD1 . TRP   B 1 136 ? 20.636 -21.111 0.493  1.00 13.89 ? 142 TRP   C CD1 1 
ATOM   2114 C  CD2 . TRP   B 1 136 ? 22.415 -21.443 1.832  1.00 13.65 ? 142 TRP   C CD2 1 
ATOM   2115 N  NE1 . TRP   B 1 136 ? 20.393 -20.477 1.704  1.00 14.22 ? 142 TRP   C NE1 1 
ATOM   2116 C  CE2 . TRP   B 1 136 ? 21.491 -20.639 2.518  1.00 13.57 ? 142 TRP   C CE2 1 
ATOM   2117 C  CE3 . TRP   B 1 136 ? 23.651 -21.720 2.442  1.00 14.52 ? 142 TRP   C CE3 1 
ATOM   2118 C  CZ2 . TRP   B 1 136 ? 21.737 -20.159 3.827  1.00 14.99 ? 142 TRP   C CZ2 1 
ATOM   2119 C  CZ3 . TRP   B 1 136 ? 23.911 -21.196 3.706  1.00 15.95 ? 142 TRP   C CZ3 1 
ATOM   2120 C  CH2 . TRP   B 1 136 ? 22.965 -20.421 4.376  1.00 15.37 ? 142 TRP   C CH2 1 
ATOM   2121 N  N   . LEU   B 1 137 ? 22.499 -25.064 1.764  1.00 14.11 ? 143 LEU   C N   1 
ATOM   2122 C  CA  . LEU   B 1 137 ? 23.244 -25.683 2.886  1.00 15.83 ? 143 LEU   C CA  1 
ATOM   2123 C  C   . LEU   B 1 137 ? 24.034 -26.901 2.428  1.00 19.81 ? 143 LEU   C C   1 
ATOM   2124 O  O   . LEU   B 1 137 ? 25.057 -27.189 3.049  1.00 20.53 ? 143 LEU   C O   1 
ATOM   2125 C  CB  . LEU   B 1 137 ? 22.281 -26.112 4.020  1.00 14.52 ? 143 LEU   C CB  1 
ATOM   2126 C  CG  . LEU   B 1 137 ? 21.692 -24.979 4.848  1.00 13.65 ? 143 LEU   C CG  1 
ATOM   2127 C  CD1 . LEU   B 1 137 ? 20.620 -25.555 5.817  1.00 13.39 ? 143 LEU   C CD1 1 
ATOM   2128 C  CD2 . LEU   B 1 137 ? 22.804 -24.223 5.639  1.00 13.62 ? 143 LEU   C CD2 1 
ATOM   2129 N  N   . ASP   B 1 138 ? 23.544 -27.606 1.385  1.00 22.59 ? 144 ASP   C N   1 
ATOM   2130 C  CA  . ASP   B 1 138 ? 24.148 -28.807 0.811  1.00 26.47 ? 144 ASP   C CA  1 
ATOM   2131 C  C   . ASP   B 1 138 ? 25.221 -28.423 -0.179 1.00 28.93 ? 144 ASP   C C   1 
ATOM   2132 O  O   . ASP   B 1 138 ? 25.733 -29.338 -0.824 1.00 31.08 ? 144 ASP   C O   1 
ATOM   2133 C  CB  . ASP   B 1 138 ? 23.101 -29.625 0.032  1.00 29.87 ? 144 ASP   C CB  1 
ATOM   2134 C  CG  . ASP   B 1 138 ? 21.849 -30.070 0.756  1.00 35.18 ? 144 ASP   C CG  1 
ATOM   2135 O  OD1 . ASP   B 1 138 ? 21.939 -30.417 1.937  1.00 36.92 ? 144 ASP   C OD1 1 
ATOM   2136 O  OD2 . ASP   B 1 138 ? 20.780 -30.113 0.113  1.00 40.33 ? 144 ASP   C OD2 1 
HETATM 2137 N  N1  . A1B4A C 2 .   ? 25.376 13.940  10.629 1.00 12.88 ? 201 A1B4A A N1  1 
HETATM 2138 C  C4  . A1B4A C 2 .   ? 24.375 14.683  9.837  1.00 13.48 ? 201 A1B4A A C4  1 
HETATM 2139 C  C5  . A1B4A C 2 .   ? 26.068 12.871  10.197 1.00 14.54 ? 201 A1B4A A C5  1 
HETATM 2140 C  C6  . A1B4A C 2 .   ? 25.816 12.430  8.762  1.00 17.68 ? 201 A1B4A A C6  1 
HETATM 2141 C  C7  . A1B4A C 2 .   ? 28.378 12.383  7.706  1.00 21.86 ? 201 A1B4A A C7  1 
HETATM 2142 C  C8  . A1B4A C 2 .   ? 28.113 10.986  7.176  1.00 21.89 ? 201 A1B4A A C8  1 
HETATM 2143 C  C10 . A1B4A C 2 .   ? 25.540 8.808   9.180  1.00 22.94 ? 201 A1B4A A C10 1 
HETATM 2144 C  C13 . A1B4A C 2 .   ? 25.480 14.371  12.026 1.00 11.59 ? 201 A1B4A A C13 1 
HETATM 2145 O  O1  . A1B4A C 2 .   ? 26.895 12.320  10.897 1.00 13.33 ? 201 A1B4A A O1  1 
HETATM 2146 C  C3  . A1B4A C 2 .   ? 23.002 14.588  10.460 1.00 13.36 ? 201 A1B4A A C3  1 
HETATM 2147 C  C2  . A1B4A C 2 .   ? 23.059 15.027  11.923 1.00 11.91 ? 201 A1B4A A C2  1 
HETATM 2148 C  C1  . A1B4A C 2 .   ? 24.113 14.202  12.682 1.00 9.99  ? 201 A1B4A A C1  1 
HETATM 2149 C  C   . A1B4A C 2 .   ? 24.211 14.638  14.131 1.00 9.97  ? 201 A1B4A A C   1 
HETATM 2150 O  O   . A1B4A C 2 .   ? 24.620 15.763  14.433 1.00 10.85 ? 201 A1B4A A O   1 
HETATM 2151 N  N   . A1B4A C 2 .   ? 23.847 13.745  15.045 1.00 9.80  ? 201 A1B4A A N   1 
HETATM 2152 C  C12 . A1B4A C 2 .   ? 26.079 10.966  8.700  1.00 20.29 ? 201 A1B4A A C12 1 
HETATM 2153 C  C11 . A1B4A C 2 .   ? 25.209 10.051  9.397  1.00 21.43 ? 201 A1B4A A C11 1 
HETATM 2154 S  S1  . A1B4A C 2 .   ? 26.897 8.651   8.167  1.00 23.64 ? 201 A1B4A A S1  1 
HETATM 2155 C  C9  . A1B4A C 2 .   ? 27.039 10.326  7.998  1.00 21.62 ? 201 A1B4A A C9  1 
HETATM 2156 S  S   . A1B4A C 2 .   ? 26.890 13.406  7.652  1.00 21.64 ? 201 A1B4A A S   1 
HETATM 2157 ZN ZN  . ZN    D 3 .   ? 23.094 -5.542  26.972 1.00 12.49 2 202 ZN    A ZN  1 
HETATM 2158 N  N1  . A1B4A E 2 .   ? 10.663 -16.687 22.589 1.00 11.98 ? 201 A1B4A C N1  1 
HETATM 2159 C  C4  . A1B4A E 2 .   ? 11.729 -15.934 23.272 1.00 12.26 ? 201 A1B4A C C4  1 
HETATM 2160 C  C5  . A1B4A E 2 .   ? 9.986  -17.744 23.079 1.00 13.83 ? 201 A1B4A C C5  1 
HETATM 2161 C  C6  . A1B4A E 2 .   ? 10.391 -18.244 24.465 1.00 16.93 ? 201 A1B4A C C6  1 
HETATM 2162 C  C7  . A1B4A E 2 .   ? 8.037  -18.316 25.877 1.00 22.97 ? 201 A1B4A C C7  1 
HETATM 2163 C  C8  . A1B4A E 2 .   ? 8.345  -19.738 26.311 1.00 23.50 ? 201 A1B4A C C8  1 
HETATM 2164 C  C10 . A1B4A E 2 .   ? 10.495 -21.891 23.870 1.00 23.65 ? 201 A1B4A C C10 1 
HETATM 2165 C  C13 . A1B4A E 2 .   ? 10.448 -16.268 21.201 1.00 10.53 ? 201 A1B4A C C13 1 
HETATM 2166 O  O1  . A1B4A E 2 .   ? 9.047  -18.259 22.486 1.00 12.60 ? 201 A1B4A C O1  1 
HETATM 2167 C  C3  . A1B4A E 2 .   ? 13.039 -16.068 22.515 1.00 11.31 ? 201 A1B4A C C3  1 
HETATM 2168 C  C2  . A1B4A E 2 .   ? 12.866 -15.652 21.046 1.00 10.52 ? 201 A1B4A C C2  1 
HETATM 2169 C  C1  . A1B4A E 2 .   ? 11.736 -16.462 20.390 1.00 9.32  ? 201 A1B4A C C1  1 
HETATM 2170 C  C   . A1B4A E 2 .   ? 11.488 -16.019 18.961 1.00 8.95  ? 201 A1B4A C C   1 
HETATM 2171 O  O   . A1B4A E 2 .   ? 11.073 -14.873 18.710 1.00 8.86  ? 201 A1B4A C O   1 
HETATM 2172 N  N   . A1B4A E 2 .   ? 11.695 -16.942 18.030 1.00 9.33  ? 201 A1B4A C N   1 
HETATM 2173 C  C12 . A1B4A E 2 .   ? 10.106 -19.715 24.491 1.00 20.40 ? 201 A1B4A C C12 1 
HETATM 2174 C  C11 . A1B4A E 2 .   ? 10.828 -20.622 23.651 1.00 21.42 ? 201 A1B4A C C11 1 
HETATM 2175 S  S1  . A1B4A E 2 .   ? 9.341  -22.068 25.034 1.00 24.75 ? 201 A1B4A C S1  1 
HETATM 2176 C  C9  . A1B4A E 2 .   ? 9.246  -20.375 25.292 1.00 22.54 ? 201 A1B4A C C9  1 
HETATM 2177 S  S   . A1B4A E 2 .   ? 9.530  -17.301 25.776 1.00 22.29 ? 201 A1B4A C S   1 
HETATM 2178 ZN ZN  . ZN    F 3 .   ? 10.561 -35.729 5.600  1.00 9.25  2 202 ZN    C ZN  1 
HETATM 2179 O  O   . HOH   G 4 .   ? 35.516 10.756  9.494  1.00 38.13 ? 301 HOH   A O   1 
HETATM 2180 O  O   . HOH   G 4 .   ? 14.741 22.226  24.428 1.00 16.01 ? 302 HOH   A O   1 
HETATM 2181 O  O   . HOH   G 4 .   ? 31.734 7.271   23.091 1.00 32.32 ? 303 HOH   A O   1 
HETATM 2182 O  O   . HOH   G 4 .   ? 23.707 7.260   28.159 1.00 16.59 ? 304 HOH   A O   1 
HETATM 2183 O  O   . HOH   G 4 .   ? 11.524 -1.643  27.877 1.00 20.85 ? 305 HOH   A O   1 
HETATM 2184 O  O   . HOH   G 4 .   ? 11.110 21.344  24.562 1.00 24.11 ? 306 HOH   A O   1 
HETATM 2185 O  O   . HOH   G 4 .   ? 34.887 15.034  24.887 1.00 31.14 ? 307 HOH   A O   1 
HETATM 2186 O  O   . HOH   G 4 .   ? 22.441 6.535   1.652  1.00 26.01 ? 308 HOH   A O   1 
HETATM 2187 O  O   . HOH   G 4 .   ? 20.836 10.178  32.286 1.00 28.69 ? 309 HOH   A O   1 
HETATM 2188 O  O   . HOH   G 4 .   ? 15.994 -0.679  4.784  1.00 24.36 ? 310 HOH   A O   1 
HETATM 2189 O  O   . HOH   G 4 .   ? 5.259  -4.800  22.742 1.00 44.84 ? 311 HOH   A O   1 
HETATM 2190 O  O   . HOH   G 4 .   ? -1.837 15.595  20.295 1.00 23.54 ? 312 HOH   A O   1 
HETATM 2191 O  O   . HOH   G 4 .   ? 34.872 13.895  16.314 1.00 20.58 ? 313 HOH   A O   1 
HETATM 2192 O  O   . HOH   G 4 .   ? 17.066 20.653  22.927 1.00 17.62 ? 314 HOH   A O   1 
HETATM 2193 O  O   . HOH   G 4 .   ? 15.014 8.626   13.296 1.00 10.13 ? 315 HOH   A O   1 
HETATM 2194 O  O   . HOH   G 4 .   ? 7.052  7.391   31.579 1.00 29.67 ? 316 HOH   A O   1 
HETATM 2195 O  O   . HOH   G 4 .   ? 29.687 7.336   4.536  1.00 29.97 ? 317 HOH   A O   1 
HETATM 2196 O  O   . HOH   G 4 .   ? 23.683 16.583  27.336 1.00 37.30 ? 318 HOH   A O   1 
HETATM 2197 O  O   . HOH   G 4 .   ? 34.427 -0.840  16.603 1.00 10.25 ? 319 HOH   A O   1 
HETATM 2198 O  O   . HOH   G 4 .   ? 11.078 -0.096  15.778 1.00 18.35 ? 320 HOH   A O   1 
HETATM 2199 O  O   . HOH   G 4 .   ? 30.968 -2.019  29.789 1.00 38.27 ? 321 HOH   A O   1 
HETATM 2200 O  O   . HOH   G 4 .   ? 25.535 17.915  12.884 1.00 12.61 ? 322 HOH   A O   1 
HETATM 2201 O  O   . HOH   G 4 .   ? 27.983 3.094   -0.221 1.00 18.06 ? 323 HOH   A O   1 
HETATM 2202 O  O   . HOH   G 4 .   ? 28.439 -6.246  3.519  1.00 21.46 ? 324 HOH   A O   1 
HETATM 2203 O  O   . HOH   G 4 .   ? 28.388 17.400  8.363  1.00 29.56 ? 325 HOH   A O   1 
HETATM 2204 O  O   . HOH   G 4 .   ? 27.014 19.169  15.032 1.00 12.90 ? 326 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 4 .   ? 18.497 -11.580 27.319 1.00 27.56 ? 327 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 4 .   ? 4.104  9.984   17.907 1.00 28.26 ? 328 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 4 .   ? 16.525 18.630  26.849 1.00 31.71 ? 329 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 4 .   ? 20.239 2.133   9.326  1.00 10.59 ? 330 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 4 .   ? 32.160 2.832   4.995  1.00 23.40 ? 331 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 4 .   ? 23.867 3.866   29.246 1.00 19.13 ? 332 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 4 .   ? 12.784 -4.564  20.590 1.00 30.91 ? 333 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 4 .   ? 31.405 12.688  9.498  1.00 35.79 ? 334 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 4 .   ? 23.476 10.916  21.442 1.00 9.28  ? 335 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 4 .   ? 5.042  11.030  12.423 1.00 33.86 ? 336 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 4 .   ? 6.671  15.435  29.042 1.00 32.84 ? 337 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 4 .   ? 25.062 4.137   -1.329 1.00 13.86 ? 338 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 4 .   ? 23.001 -11.121 30.788 1.00 48.71 ? 339 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 4 .   ? 24.130 8.395   1.433  1.00 23.52 ? 340 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 4 .   ? 13.481 18.671  14.681 1.00 21.49 ? 341 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 4 .   ? 34.692 -6.446  21.576 1.00 37.22 ? 342 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 4 .   ? 28.048 16.378  10.810 1.00 20.62 ? 343 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 4 .   ? 8.952  3.983   11.880 1.00 32.90 ? 344 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 4 .   ? 20.167 11.936  8.530  1.00 15.39 ? 345 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 4 .   ? 11.278 10.806  9.949  1.00 46.51 ? 346 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 4 .   ? 24.399 14.296  30.262 1.00 56.91 ? 347 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 4 .   ? 23.596 1.777   -0.903 1.00 11.96 ? 348 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 4 .   ? 12.025 -2.752  15.917 1.00 26.55 ? 349 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 4 .   ? 29.657 25.953  16.225 1.00 39.75 ? 350 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 4 .   ? 4.969  3.043   20.889 1.00 16.74 ? 351 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 4 .   ? 6.669  -1.952  23.824 1.00 28.11 ? 352 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 4 .   ? 4.200  4.046   27.932 1.00 30.62 ? 353 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 4 .   ? 4.098  19.974  21.583 1.00 25.76 ? 354 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 4 .   ? 20.124 23.729  21.991 1.00 50.96 ? 355 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 4 .   ? 17.292 2.161   9.278  1.00 17.18 ? 356 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 4 .   ? 25.421 1.597   29.854 1.00 18.85 ? 357 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 4 .   ? 21.520 9.867   23.349 1.00 9.65  ? 358 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 4 .   ? 29.263 13.847  11.378 1.00 23.20 ? 359 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 4 .   ? 24.756 -8.671  24.736 1.00 26.03 ? 360 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 4 .   ? 20.359 20.439  24.167 1.00 29.22 ? 361 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 4 .   ? 17.204 18.458  15.572 1.00 10.60 ? 362 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 4 .   ? 34.410 3.954   26.152 1.00 23.62 ? 363 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 4 .   ? 3.341  18.068  23.558 1.00 26.66 ? 364 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 4 .   ? 16.785 4.438   5.879  1.00 20.90 ? 365 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 4 .   ? 4.218  20.353  15.253 1.00 31.16 ? 366 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 4 .   ? 32.931 -2.631  15.267 1.00 15.91 ? 367 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 4 .   ? 30.862 5.296   7.709  1.00 17.71 ? 368 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 4 .   ? 29.866 6.360   29.901 1.00 26.41 ? 369 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 4 .   ? 17.828 20.198  13.578 1.00 18.43 ? 370 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 4 .   ? 29.695 -2.324  8.295  1.00 16.02 ? 371 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 4 .   ? 32.092 8.874   4.767  1.00 33.02 ? 372 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 4 .   ? 20.095 23.502  14.983 1.00 36.83 ? 373 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 4 .   ? 30.641 -3.213  12.050 1.00 20.66 ? 374 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 4 .   ? 4.776  10.698  14.886 1.00 39.24 ? 375 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 4 .   ? 30.253 -5.843  26.406 1.00 27.54 ? 376 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 4 .   ? 22.936 20.779  20.497 1.00 19.65 ? 377 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 4 .   ? 29.160 25.726  13.448 1.00 23.20 ? 378 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 4 .   ? 16.763 9.035   6.776  1.00 19.44 ? 379 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 4 .   ? 25.420 20.366  22.151 1.00 31.37 ? 380 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 4 .   ? 34.043 0.363   8.563  1.00 12.92 ? 381 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 4 .   ? 16.231 -0.576  12.791 1.00 17.10 ? 382 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 4 .   ? 19.834 -4.782  15.291 1.00 22.89 ? 383 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 4 .   ? 17.067 0.491   2.720  1.00 33.58 ? 384 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 4 .   ? 20.027 13.735  29.173 1.00 25.11 ? 385 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 4 .   ? 17.539 16.400  28.534 1.00 41.01 ? 386 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 4 .   ? 35.478 14.477  20.399 1.00 18.72 ? 387 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 4 .   ? 19.449 -6.106  32.874 1.00 35.67 ? 388 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 4 .   ? 24.009 17.870  6.332  1.00 36.42 ? 389 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 4 .   ? 28.324 0.838   26.808 1.00 18.39 ? 390 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 4 .   ? 10.236 16.849  29.016 1.00 36.94 ? 391 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 4 .   ? 22.108 -8.339  19.400 1.00 23.04 ? 392 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 4 .   ? 6.712  16.258  8.877  1.00 28.36 ? 393 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 4 .   ? 27.861 11.908  27.526 1.00 18.91 ? 394 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 4 .   ? 19.638 9.464   7.915  1.00 21.28 ? 395 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 4 .   ? 2.690  8.558   26.055 1.00 28.29 ? 396 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 4 .   ? 3.895  14.775  10.406 1.00 22.44 ? 397 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 4 .   ? 18.068 -5.298  30.482 1.00 20.72 ? 398 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 4 .   ? 17.450 22.299  15.758 1.00 24.39 ? 399 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 4 .   ? 2.143  14.089  24.616 1.00 46.99 ? 400 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 4 .   ? 12.136 18.440  26.358 1.00 21.74 ? 401 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 4 .   ? 31.591 14.793  12.814 1.00 23.73 ? 402 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 4 .   ? 14.536 -3.995  16.092 1.00 25.56 ? 403 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 4 .   ? 15.660 12.030  30.835 1.00 31.44 ? 404 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 4 .   ? 28.636 22.021  22.327 1.00 24.78 ? 405 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 4 .   ? 13.366 8.590   11.032 1.00 14.95 ? 406 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 4 .   ? 3.433  2.402   18.864 1.00 26.53 ? 407 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 4 .   ? 11.096 2.236   12.385 1.00 23.90 ? 408 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 4 .   ? 32.078 22.537  11.532 1.00 23.81 ? 409 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 4 .   ? -1.490 11.125  19.508 1.00 42.76 ? 410 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 4 .   ? 15.196 23.209  16.962 1.00 18.57 ? 411 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 4 .   ? 30.115 -2.145  3.546  1.00 38.23 ? 412 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 4 .   ? 27.027 -5.979  1.025  1.00 30.22 ? 413 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 4 .   ? 26.297 -6.569  29.898 1.00 31.04 ? 414 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 4 .   ? 24.793 -5.120  32.654 1.00 34.89 ? 415 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 4 .   ? 31.168 10.471  14.163 1.00 43.60 ? 416 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 4 .   ? 32.681 5.455   4.668  1.00 32.52 ? 417 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 4 .   ? 19.516 -9.836  20.501 1.00 24.71 ? 418 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 4 .   ? 15.858 8.262   33.889 1.00 29.39 ? 419 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 4 .   ? 31.552 -7.174  17.920 1.00 35.64 ? 420 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 4 .   ? 20.912 13.643  6.551  1.00 40.47 ? 421 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 4 .   ? 25.054 -12.759 30.098 1.00 57.62 ? 422 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 4 .   ? 32.919 0.546   6.188  1.00 24.06 ? 423 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 4 .   ? 8.924  17.885  8.692  1.00 45.15 ? 424 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 4 .   ? 13.805 21.599  14.933 1.00 22.51 ? 425 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 4 .   ? 23.265 22.892  18.806 1.00 25.84 ? 426 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 4 .   ? 21.155 23.802  17.384 1.00 28.41 ? 427 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 4 .   ? 18.207 10.887  6.725  1.00 30.56 ? 428 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 4 .   ? 30.935 -3.018  5.745  1.00 32.69 ? 429 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 4 .   ? 33.699 -2.280  9.259  1.00 19.24 ? 430 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 4 .   ? 28.125 1.684   29.255 1.00 27.06 ? 431 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 4 .   ? 2.289  20.932  12.288 1.00 36.55 ? 432 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 4 .   ? 27.304 14.164  29.323 1.00 38.06 ? 433 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 4 .   ? 2.729  4.109   16.789 1.00 35.85 ? 434 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 4 .   ? 31.371 -3.916  9.666  1.00 21.31 ? 435 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 4 .   ? 13.097 9.943   8.407  1.00 31.17 ? 436 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 4 .   ? 28.487 4.202   30.554 1.00 31.79 ? 437 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 4 .   ? 31.782 25.453  12.448 1.00 31.40 ? 438 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 4 .   ? 23.511 14.610  6.476  1.00 35.51 ? 439 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 4 .   ? 20.286 -8.463  7.838  1.00 18.49 ? 301 HOH   C O   1 
HETATM 2319 O  O   . HOH   H 4 .   ? 13.600 -24.881 31.131 1.00 33.20 ? 302 HOH   C O   1 
HETATM 2320 O  O   . HOH   H 4 .   ? 5.410  -25.440 24.464 1.00 23.42 ? 303 HOH   C O   1 
HETATM 2321 O  O   . HOH   H 4 .   ? 2.688  -23.064 10.452 1.00 21.66 ? 304 HOH   C O   1 
HETATM 2322 O  O   . HOH   H 4 .   ? 25.080 -37.427 10.850 1.00 29.76 ? 305 HOH   C O   1 
HETATM 2323 O  O   . HOH   H 4 .   ? 10.224 -23.021 4.821  1.00 14.78 ? 306 HOH   C O   1 
HETATM 2324 O  O   . HOH   H 4 .   ? 31.065 -10.591 10.549 1.00 26.49 ? 307 HOH   C O   1 
HETATM 2325 O  O   . HOH   H 4 .   ? 11.920 -20.603 0.579  1.00 30.55 ? 308 HOH   C O   1 
HETATM 2326 O  O   . HOH   H 4 .   ? 17.990 -10.430 18.652 1.00 31.10 ? 309 HOH   C O   1 
HETATM 2327 O  O   . HOH   H 4 .   ? 10.660 -27.631 33.723 1.00 25.25 ? 310 HOH   C O   1 
HETATM 2328 O  O   . HOH   H 4 .   ? 14.340 -19.841 0.909  1.00 37.28 ? 311 HOH   C O   1 
HETATM 2329 O  O   . HOH   H 4 .   ? 35.628 -15.280 15.744 1.00 33.54 ? 312 HOH   C O   1 
HETATM 2330 O  O   . HOH   H 4 .   ? 24.738 -37.412 6.911  1.00 33.56 ? 313 HOH   C O   1 
HETATM 2331 O  O   . HOH   H 4 .   ? 23.792 -9.325  7.828  1.00 16.61 ? 314 HOH   C O   1 
HETATM 2332 O  O   . HOH   H 4 .   ? 23.919 -12.758 19.194 1.00 23.83 ? 315 HOH   C O   1 
HETATM 2333 O  O   . HOH   H 4 .   ? 0.353  -15.349 22.669 1.00 37.82 ? 316 HOH   C O   1 
HETATM 2334 O  O   . HOH   H 4 .   ? 20.478 -22.421 18.681 1.00 11.15 ? 317 HOH   C O   1 
HETATM 2335 O  O   . HOH   H 4 .   ? 4.388  -36.189 21.674 1.00 25.02 ? 318 HOH   C O   1 
HETATM 2336 O  O   . HOH   H 4 .   ? 34.481 -11.064 10.713 1.00 44.55 ? 319 HOH   C O   1 
HETATM 2337 O  O   . HOH   H 4 .   ? 26.125 -33.014 6.001  1.00 33.63 ? 320 HOH   C O   1 
HETATM 2338 O  O   . HOH   H 4 .   ? -0.597 -17.061 11.517 1.00 32.07 ? 321 HOH   C O   1 
HETATM 2339 O  O   . HOH   H 4 .   ? 17.236 -37.771 3.044  1.00 29.90 ? 322 HOH   C O   1 
HETATM 2340 O  O   . HOH   H 4 .   ? 6.840  -36.647 29.276 1.00 32.00 ? 323 HOH   C O   1 
HETATM 2341 O  O   . HOH   H 4 .   ? 23.580 -31.302 15.141 1.00 19.99 ? 324 HOH   C O   1 
HETATM 2342 O  O   . HOH   H 4 .   ? 7.761  -5.467  14.570 1.00 28.95 ? 325 HOH   C O   1 
HETATM 2343 O  O   . HOH   H 4 .   ? 26.497 -23.042 -0.257 1.00 34.98 ? 326 HOH   C O   1 
HETATM 2344 O  O   . HOH   H 4 .   ? 11.334 -35.921 -0.578 1.00 25.49 ? 327 HOH   C O   1 
HETATM 2345 O  O   . HOH   H 4 .   ? 16.547 -14.225 4.133  1.00 31.55 ? 328 HOH   C O   1 
HETATM 2346 O  O   . HOH   H 4 .   ? 12.385 -29.527 33.623 1.00 16.90 ? 329 HOH   C O   1 
HETATM 2347 O  O   . HOH   H 4 .   ? 17.703 -7.589  21.491 1.00 18.15 ? 330 HOH   C O   1 
HETATM 2348 O  O   . HOH   H 4 .   ? 10.461 -12.711 20.400 1.00 11.90 ? 331 HOH   C O   1 
HETATM 2349 O  O   . HOH   H 4 .   ? 14.505 -22.696 29.906 1.00 25.94 ? 332 HOH   C O   1 
HETATM 2350 O  O   . HOH   H 4 .   ? 3.619  -23.534 3.746  1.00 19.87 ? 333 HOH   C O   1 
HETATM 2351 O  O   . HOH   H 4 .   ? 6.790  -23.000 28.612 1.00 32.27 ? 334 HOH   C O   1 
HETATM 2352 O  O   . HOH   H 4 .   ? 2.761  -31.232 3.909  1.00 26.99 ? 335 HOH   C O   1 
HETATM 2353 O  O   . HOH   H 4 .   ? 22.935 -36.174 12.130 1.00 28.40 ? 336 HOH   C O   1 
HETATM 2354 O  O   . HOH   H 4 .   ? 9.863  -26.284 3.626  1.00 13.70 ? 337 HOH   C O   1 
HETATM 2355 O  O   . HOH   H 4 .   ? 4.948  -31.098 -1.855 1.00 28.88 ? 338 HOH   C O   1 
HETATM 2356 O  O   . HOH   H 4 .   ? 7.147  -39.044 7.229  1.00 29.78 ? 339 HOH   C O   1 
HETATM 2357 O  O   . HOH   H 4 .   ? 0.769  -16.776 18.024 1.00 21.94 ? 340 HOH   C O   1 
HETATM 2358 O  O   . HOH   H 4 .   ? 11.296 -19.648 11.531 1.00 9.53  ? 341 HOH   C O   1 
HETATM 2359 O  O   . HOH   H 4 .   ? 8.323  -28.503 3.038  1.00 13.81 ? 342 HOH   C O   1 
HETATM 2360 O  O   . HOH   H 4 .   ? 15.381 -28.913 23.160 1.00 11.68 ? 343 HOH   C O   1 
HETATM 2361 O  O   . HOH   H 4 .   ? -1.504 -31.611 4.843  1.00 31.83 ? 344 HOH   C O   1 
HETATM 2362 O  O   . HOH   H 4 .   ? 11.217 -36.326 31.500 1.00 26.95 ? 345 HOH   C O   1 
HETATM 2363 O  O   . HOH   H 4 .   ? 0.898  -31.653 17.147 1.00 9.47  ? 346 HOH   C O   1 
HETATM 2364 O  O   . HOH   H 4 .   ? 30.786 -21.323 13.077 1.00 29.76 ? 347 HOH   C O   1 
HETATM 2365 O  O   . HOH   H 4 .   ? 21.442 -36.584 9.899  1.00 20.97 ? 348 HOH   C O   1 
HETATM 2366 O  O   . HOH   H 4 .   ? 16.003 -19.010 24.101 1.00 16.01 ? 349 HOH   C O   1 
HETATM 2367 O  O   . HOH   H 4 .   ? 27.641 -14.849 2.676  1.00 36.54 ? 350 HOH   C O   1 
HETATM 2368 O  O   . HOH   H 4 .   ? 22.101 -12.395 17.197 1.00 18.64 ? 351 HOH   C O   1 
HETATM 2369 O  O   . HOH   H 4 .   ? 8.702  -11.487 18.359 1.00 12.66 ? 352 HOH   C O   1 
HETATM 2370 O  O   . HOH   H 4 .   ? 3.987  -27.195 28.012 1.00 31.33 ? 353 HOH   C O   1 
HETATM 2371 O  O   . HOH   H 4 .   ? 30.444 -20.214 19.139 1.00 23.94 ? 354 HOH   C O   1 
HETATM 2372 O  O   . HOH   H 4 .   ? 26.513 -27.459 19.337 1.00 35.02 ? 355 HOH   C O   1 
HETATM 2373 O  O   . HOH   H 4 .   ? 3.921  -8.785  22.645 1.00 28.37 ? 356 HOH   C O   1 
HETATM 2374 O  O   . HOH   H 4 .   ? 17.753 -10.060 9.434  1.00 16.96 ? 357 HOH   C O   1 
HETATM 2375 O  O   . HOH   H 4 .   ? 30.588 -20.426 16.442 1.00 28.19 ? 358 HOH   C O   1 
HETATM 2376 O  O   . HOH   H 4 .   ? 28.619 -9.881  18.829 1.00 54.94 ? 359 HOH   C O   1 
HETATM 2377 O  O   . HOH   H 4 .   ? 12.558 -6.193  22.067 1.00 17.28 ? 360 HOH   C O   1 
HETATM 2378 O  O   . HOH   H 4 .   ? 29.462 -27.986 9.918  1.00 19.61 ? 361 HOH   C O   1 
HETATM 2379 O  O   . HOH   H 4 .   ? 18.090 -11.886 5.466  1.00 27.93 ? 362 HOH   C O   1 
HETATM 2380 O  O   . HOH   H 4 .   ? 5.841  -32.673 29.773 1.00 42.43 ? 363 HOH   C O   1 
HETATM 2381 O  O   . HOH   H 4 .   ? 5.824  -9.949  25.594 1.00 32.68 ? 364 HOH   C O   1 
HETATM 2382 O  O   . HOH   H 4 .   ? 29.830 -26.416 2.897  1.00 33.33 ? 365 HOH   C O   1 
HETATM 2383 O  O   . HOH   H 4 .   ? 13.035 -20.716 9.442  1.00 8.71  ? 366 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 4 .   ? 16.395 -22.091 -1.669 1.00 37.38 ? 367 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 4 .   ? 6.753  -16.578 22.539 1.00 22.00 ? 368 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 4 .   ? 18.296 -28.849 23.026 1.00 18.50 ? 369 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 4 .   ? 3.714  -36.198 6.913  1.00 19.95 ? 370 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 4 .   ? 32.973 -16.756 6.851  1.00 41.15 ? 371 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 4 .   ? 22.095 -32.621 3.736  1.00 22.22 ? 372 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 4 .   ? 18.390 -12.448 16.949 1.00 11.71 ? 373 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 4 .   ? 5.571  -29.272 7.387  1.00 11.11 ? 374 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 4 .   ? 31.163 -10.770 16.350 1.00 21.02 ? 375 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 4 .   ? 19.957 -31.651 27.014 1.00 23.45 ? 376 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 4 .   ? 6.520  -18.388 5.912  1.00 16.93 ? 377 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 4 .   ? 21.864 -14.802 23.448 1.00 33.52 ? 378 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 4 .   ? 14.819 -35.813 17.069 1.00 17.29 ? 379 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 4 .   ? 31.331 -22.125 4.976  1.00 29.70 ? 380 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 4 .   ? -3.475 -18.797 27.546 1.00 24.74 ? 381 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 4 .   ? 26.422 -33.208 13.855 1.00 28.51 ? 382 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 4 .   ? 8.151  -14.271 22.944 1.00 22.06 ? 383 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 4 .   ? 8.721  -38.642 9.544  1.00 19.29 ? 384 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 4 .   ? 19.538 -27.328 25.349 1.00 33.92 ? 385 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 4 .   ? -0.136 -18.960 21.599 1.00 37.71 ? 386 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 4 .   ? 18.830 -31.521 19.314 1.00 17.75 ? 387 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 4 .   ? 1.295  -29.561 25.044 1.00 29.63 ? 388 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 4 .   ? -0.428 -15.712 13.992 1.00 21.53 ? 389 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 4 .   ? 8.224  -39.617 24.381 1.00 29.75 ? 390 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 4 .   ? 16.383 -38.624 10.317 1.00 38.87 ? 391 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 4 .   ? 14.206 -16.772 3.607  1.00 23.71 ? 392 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 4 .   ? 28.749 -33.270 12.399 1.00 29.34 ? 393 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 4 .   ? 5.738  -32.738 24.505 1.00 16.56 ? 394 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 4 .   ? 19.597 -22.243 25.497 1.00 25.76 ? 395 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 4 .   ? 0.903  -33.876 20.440 1.00 27.97 ? 396 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 4 .   ? 4.080  -24.232 26.454 1.00 31.55 ? 397 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 4 .   ? 15.248 -35.705 1.821  1.00 18.50 ? 398 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 4 .   ? 4.502  -30.431 31.060 1.00 41.67 ? 399 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 4 .   ? 4.829  -17.380 24.461 1.00 50.61 ? 400 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 4 .   ? 19.487 -7.447  15.137 1.00 18.09 ? 401 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 4 .   ? 5.909  -8.493  11.439 1.00 31.29 ? 402 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 4 .   ? 29.169 -14.869 22.574 1.00 27.33 ? 403 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 4 .   ? 9.605  -10.219 11.171 1.00 32.40 ? 404 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 4 .   ? 20.910 -12.039 21.212 1.00 23.71 ? 405 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 4 .   ? 14.406 -10.280 8.620  1.00 29.52 ? 406 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 4 .   ? 1.902  -17.677 5.985  1.00 29.42 ? 407 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 4 .   ? 22.422 -12.220 5.800  1.00 22.51 ? 408 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 4 .   ? 32.059 -16.659 20.683 1.00 20.16 ? 409 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 4 .   ? 8.053  -35.102 0.496  1.00 16.50 ? 410 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 4 .   ? 31.169 -28.716 11.774 1.00 29.22 ? 411 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 4 .   ? 12.079 -9.876  12.574 1.00 23.05 ? 412 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 4 .   ? 4.269  -33.569 22.283 1.00 25.75 ? 413 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 4 .   ? 1.284  -34.353 17.834 1.00 16.79 ? 414 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 4 .   ? 24.848 -23.942 20.011 1.00 31.95 ? 415 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 4 .   ? 17.974 -18.560 1.495  1.00 34.86 ? 416 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 4 .   ? 11.967 -39.093 12.973 1.00 26.29 ? 417 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 4 .   ? 24.205 -29.033 18.898 1.00 25.45 ? 418 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 4 .   ? 8.664  -13.431 25.436 1.00 34.40 ? 419 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 4 .   ? 22.371 -22.505 20.788 1.00 17.54 ? 420 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 4 .   ? 16.940 -34.482 17.704 1.00 31.75 ? 421 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 4 .   ? 6.945  -36.494 2.959  1.00 20.31 ? 422 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 4 .   ? 20.144 -8.847  17.470 1.00 29.26 ? 423 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 4 .   ? -0.502 -35.842 16.802 1.00 36.29 ? 424 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 4 .   ? 18.801 -22.379 -2.023 1.00 28.56 ? 425 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 4 .   ? 13.525 -42.367 4.278  1.00 45.87 ? 426 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 4 .   ? 4.670  -29.258 4.816  1.00 34.71 ? 427 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 4 .   ? 4.469  -16.121 21.291 1.00 26.14 ? 428 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 4 .   ? 15.882 -17.311 26.219 1.00 33.39 ? 429 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 4 .   ? 8.864  -12.230 6.636  1.00 38.68 ? 430 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 4 .   ? 9.740  -9.662  27.232 1.00 50.63 ? 431 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 4 .   ? 30.530 -31.278 13.129 1.00 39.15 ? 432 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 4 .   ? 2.298  -34.930 4.106  1.00 53.78 ? 433 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 4 .   ? 17.516 -9.760  29.375 1.00 41.97 ? 434 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 4 .   ? 2.657  -29.035 27.254 1.00 37.82 ? 435 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 4 .   ? 32.403 -19.402 20.792 1.00 31.47 ? 436 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 4 .   ? 8.547  -24.026 2.735  1.00 24.87 ? 437 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 4 .   ? 9.478  -39.566 12.248 1.00 24.52 ? 438 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 4 .   ? 32.927 -9.434  14.633 1.00 27.28 ? 439 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 4 .   ? 2.378  -17.275 22.793 1.00 36.45 ? 440 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 4 .   ? 32.140 -27.232 13.689 1.00 35.11 ? 441 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 4 .   ? 33.019 -9.184  11.989 1.00 32.18 ? 442 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 4 .   ? 37.633 -16.874 7.298  1.00 64.75 ? 443 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 4 .   ? 13.500 -16.720 26.221 1.00 33.82 ? 444 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 4 .   ? 5.348  -39.693 23.272 1.00 30.26 ? 445 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 4 .   ? 19.386 -33.941 18.728 1.00 30.29 ? 446 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 4 .   ? 29.768 -8.600  9.179  1.00 22.84 ? 447 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 4 .   ? 0.097  -19.390 18.192 1.00 47.83 ? 448 HOH   C 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   . SER   A 1   ? 0.1781 0.1773 0.1815 -0.0001 -0.0097 0.0113  7   SER   A N   
2    C CA  . SER   A 1   ? 0.1655 0.1658 0.1774 -0.0015 -0.0106 0.0107  7   SER   A CA  
3    C C   . SER   A 1   ? 0.1669 0.1654 0.1795 -0.0028 -0.0096 0.0074  7   SER   A C   
4    O O   . SER   A 1   ? 0.1866 0.1831 0.1930 -0.0027 -0.0096 0.0055  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2076 0.2097 0.2211 -0.0013 -0.0152 0.0117  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2602 0.2613 0.2679 -0.0015 -0.0183 0.0091  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1530 0.1516 0.1730 -0.0039 -0.0084 0.0070  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1405 0.1368 0.1617 -0.0049 -0.0069 0.0046  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1297 0.1254 0.1567 -0.0053 -0.0035 0.0047  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1532 0.1497 0.1819 -0.0047 -0.0019 0.0059  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1191 0.1130 0.1493 -0.0061 -0.0018 0.0034  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1262 0.1186 0.1607 -0.0060 0.0021  0.0035  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1245 0.1132 0.1567 -0.0061 0.0050  0.0022  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1458 0.1334 0.1763 -0.0066 0.0038  0.0011  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1453 0.1398 0.1903 -0.0069 0.0016  0.0047  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1108 0.0972 0.1427 -0.0053 0.0091  0.0021  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1237 0.1059 0.1538 -0.0048 0.0130  0.0017  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1210 0.1028 0.1606 -0.0056 0.0159  0.0024  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1243 0.1073 0.1678 -0.0054 0.0170  0.0030  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1240 0.1035 0.1459 -0.0028 0.0157  0.0012  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1255 0.1064 0.1402 -0.0020 0.0127  0.0005  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1586 0.1333 0.1773 -0.0017 0.0200  0.0015  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1503 0.1302 0.1590 -0.0001 0.0138  -0.0003 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1285 0.1083 0.1724 -0.0064 0.0177  0.0024  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1436 0.1229 0.1979 -0.0072 0.0213  0.0033  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1435 0.1171 0.1946 -0.0059 0.0278  0.0038  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1601 0.1312 0.2101 -0.0062 0.0287  0.0036  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1459 0.1281 0.2110 -0.0095 0.0181  0.0028  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1562 0.1437 0.2242 -0.0102 0.0118  0.0028  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1711 0.1618 0.2479 -0.0103 0.0115  0.0042  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1857 0.1748 0.2469 -0.0103 0.0066  0.0018  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1823 0.1777 0.2612 -0.0104 0.0059  0.0048  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2007 0.1942 0.2631 -0.0104 0.0013  0.0022  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1937 0.1904 0.2649 -0.0104 0.0008  0.0039  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2260 0.2266 0.2974 -0.0100 -0.0041 0.0051  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1473 0.1183 0.1954 -0.0041 0.0324  0.0045  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1613 0.1262 0.2038 -0.0021 0.0390  0.0055  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1701 0.1333 0.2200 -0.0018 0.0448  0.0066  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1643 0.1293 0.2157 -0.0015 0.0445  0.0062  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1983 0.1607 0.2256 0.0006  0.0388  0.0048  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2062 0.1711 0.2310 0.0010  0.0365  0.0035  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2324 0.1880 0.2525 0.0033  0.0457  0.0062  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1871 0.1472 0.2438 -0.0021 0.0503  0.0081  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1867 0.1450 0.2517 -0.0016 0.0568  0.0094  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1762 0.1406 0.2546 -0.0037 0.0534  0.0090  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1919 0.1612 0.2783 -0.0061 0.0475  0.0084  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1846 0.1486 0.2640 -0.0025 0.0563  0.0092  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1771 0.1469 0.2692 -0.0040 0.0529  0.0092  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1516 0.1240 0.2364 -0.0036 0.0475  0.0079  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1688 0.1436 0.2601 -0.0035 0.0472  0.0082  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2234 0.1917 0.3264 -0.0033 0.0600  0.0106  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3201 0.2877 0.4357 -0.0044 0.0645  0.0122  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3514 0.3243 0.4804 -0.0069 0.0600  0.0123  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3288 0.2897 0.4401 -0.0026 0.0733  0.0134  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1439 0.1162 0.2166 -0.0034 0.0431  0.0067  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1351 0.1098 0.2016 -0.0031 0.0382  0.0055  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1221 0.1011 0.1878 -0.0046 0.0311  0.0053  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1348 0.1131 0.1982 -0.0052 0.0300  0.0052  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1575 0.1279 0.2091 -0.0010 0.0401  0.0039  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1725 0.1380 0.2215 0.0010  0.0468  0.0035  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1808 0.1469 0.2371 0.0010  0.0488  0.0033  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2006 0.1602 0.2389 0.0032  0.0515  0.0033  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1940 0.1550 0.2470 0.0030  0.0553  0.0025  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2114 0.1659 0.2451 0.0055  0.0577  0.0027  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2151 0.1702 0.2564 0.0052  0.0598  0.0022  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2547 0.2041 0.2910 0.0076  0.0664  0.0012  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1115 0.0942 0.1778 -0.0049 0.0267  0.0053  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1189 0.1052 0.1824 -0.0057 0.0204  0.0053  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1186 0.1045 0.1734 -0.0046 0.0195  0.0043  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1241 0.1100 0.1815 -0.0042 0.0210  0.0043  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1257 0.1169 0.1998 -0.0067 0.0165  0.0068  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1559 0.1505 0.2260 -0.0069 0.0106  0.0072  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1717 0.1709 0.2511 -0.0074 0.0061  0.0090  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1719 0.1736 0.2488 -0.0065 0.0029  0.0106  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1977 0.2014 0.2694 -0.0064 -0.0020 0.0111  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2025 0.2059 0.2700 -0.0072 -0.0045 0.0094  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2045 0.2097 0.2744 -0.0053 -0.0036 0.0132  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1250 0.1102 0.1704 -0.0043 0.0175  0.0033  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1108 0.0962 0.1494 -0.0035 0.0164  0.0022  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1145 0.1035 0.1530 -0.0041 0.0118  0.0031  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1146 0.1041 0.1502 -0.0044 0.0095  0.0033  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1317 0.1139 0.1600 -0.0021 0.0175  0.0006  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1372 0.1200 0.1607 -0.0014 0.0162  -0.0010 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1479 0.1256 0.1742 -0.0010 0.0224  0.0003  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.0979 0.0889 0.1391 -0.0041 0.0108  0.0038  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1047 0.0986 0.1454 -0.0042 0.0073  0.0053  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.0931 0.0872 0.1317 -0.0038 0.0076  0.0047  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1095 0.1020 0.1490 -0.0036 0.0099  0.0031  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1291 0.1257 0.1779 -0.0046 0.0056  0.0079  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1717 0.1690 0.2234 -0.0052 0.0040  0.0081  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1378 0.1340 0.1939 -0.0044 0.0084  0.0084  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.0871 0.0832 0.1237 -0.0037 0.0055  0.0061  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.0882 0.0850 0.1261 -0.0035 0.0062  0.0061  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.0944 0.0915 0.1405 -0.0037 0.0075  0.0076  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.0948 0.0932 0.1448 -0.0035 0.0065  0.0104  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.0918 0.0904 0.1270 -0.0030 0.0046  0.0082  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1023 0.1005 0.1300 -0.0027 0.0037  0.0068  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1183 0.1163 0.1422 -0.0026 0.0021  0.0070  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1033 0.1015 0.1295 -0.0024 0.0044  0.0051  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.0778 0.0737 0.1268 -0.0039 0.0096  0.0057  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.0820 0.0775 0.1394 -0.0040 0.0114  0.0069  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.0956 0.0930 0.1570 -0.0036 0.0106  0.0111  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.0981 0.0959 0.1655 -0.0031 0.0110  0.0138  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1058 0.0993 0.1651 -0.0044 0.0135  0.0034  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.0810 0.0729 0.1490 -0.0045 0.0163  0.0037  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1079 0.0978 0.1773 -0.0051 0.0176  -0.0004 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1092 0.0966 0.1864 -0.0052 0.0207  -0.0012 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1098 0.0973 0.1957 -0.0054 0.0221  0.0012  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1126 0.1027 0.2002 -0.0053 0.0209  0.0054  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1227 0.1074 0.2157 -0.0055 0.0253  -0.0003 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.0837 0.0822 0.1414 -0.0033 0.0097  0.0121  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.0939 0.0936 0.1541 -0.0025 0.0097  0.0166  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1090 0.1102 0.1662 -0.0014 0.0069  0.0198  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1391 0.1410 0.1979 -0.0001 0.0066  0.0241  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1172 0.1174 0.1754 -0.0024 0.0106  0.0170  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1039 0.1049 0.1532 -0.0019 0.0088  0.0167  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1078 0.1086 0.1526 -0.0025 0.0080  0.0128  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1259 0.1275 0.1698 -0.0007 0.0078  0.0198  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1154 0.1167 0.1533 -0.0017 0.0068  0.0137  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1199 0.1216 0.1567 -0.0007 0.0067  0.0176  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1132 0.1147 0.1662 -0.0018 0.0047  0.0179  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1165 0.1196 0.1676 -0.0011 0.0013  0.0199  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1337 0.1373 0.1918 -0.0016 0.0008  0.0196  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1402 0.1456 0.1987 -0.0013 -0.0025 0.0206  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1271 0.1300 0.1693 -0.0013 -0.0009 0.0180  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1251 0.1276 0.1606 -0.0006 -0.0001 0.0185  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.1475 0.1494 0.1747 -0.0007 -0.0017 0.0162  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.1473 0.1506 0.1819 0.0011  -0.0006 0.0229  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1220 0.1242 0.1861 -0.0022 0.0041  0.0181  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1154 0.1177 0.1868 -0.0024 0.0047  0.0179  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1117 0.1167 0.1902 -0.0012 0.0025  0.0221  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1284 0.1337 0.2085 -0.0001 0.0027  0.0251  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1260 0.1257 0.2016 -0.0028 0.0092  0.0157  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1218 0.1287 0.2054 -0.0014 0.0006  0.0222  24  THR   A N   
135  C CA  . THR   A 18  ? 0.1358 0.1459 0.2269 -0.0001 -0.0025 0.0260  24  THR   A CA  
136  C C   . THR   A 18  ? 0.1447 0.1545 0.2476 0.0004  0.0010  0.0273  24  THR   A C   
137  O O   . THR   A 18  ? 0.1486 0.1554 0.2533 -0.0005 0.0059  0.0246  24  THR   A O   
138  C CB  . THR   A 18  ? 0.1617 0.1746 0.2541 -0.0007 -0.0071 0.0251  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.1551 0.1671 0.2541 -0.0021 -0.0040 0.0226  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.1844 0.1971 0.2652 -0.0012 -0.0104 0.0233  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1562 0.1692 0.2674 0.0020  -0.0015 0.0312  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.1767 0.1895 0.3005 0.0027  0.0019  0.0326  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1390 0.1513 0.2685 0.0012  0.0045  0.0294  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1571 0.1664 0.2915 0.0010  0.0102  0.0279  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2251 0.2423 0.3574 0.0049  -0.0023 0.0376  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3232 0.3405 0.4506 0.0071  -0.0042 0.0419  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3637 0.3774 0.4902 0.0075  0.0006  0.0430  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3597 0.3802 0.4829 0.0091  -0.0103 0.0454  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3810 0.3954 0.5030 0.0097  -0.0020 0.0475  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3846 0.4031 0.5039 0.0110  -0.0086 0.0492  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1367 0.1514 0.2649 0.0001  0.0008  0.0279  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1318 0.1457 0.2656 -0.0013 0.0038  0.0253  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1359 0.1445 0.2617 -0.0023 0.0094  0.0216  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1414 0.1475 0.2721 -0.0025 0.0148  0.0203  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.1558 0.1730 0.2909 -0.0023 -0.0012 0.0244  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.2491 0.2716 0.3982 -0.0015 -0.0050 0.0270  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.2373 0.2602 0.3986 -0.0007 -0.0014 0.0287  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.2581 0.2844 0.4051 -0.0014 -0.0125 0.0274  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1169 0.1236 0.2299 -0.0027 0.0084  0.0201  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1217 0.1236 0.2266 -0.0033 0.0130  0.0167  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1073 0.1061 0.2160 -0.0025 0.0183  0.0162  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1162 0.1113 0.2238 -0.0026 0.0231  0.0137  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1229 0.1240 0.2155 -0.0035 0.0107  0.0156  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1458 0.1480 0.2321 -0.0042 0.0072  0.0146  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1483 0.1496 0.2362 -0.0050 0.0084  0.0132  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1437 0.1473 0.2236 -0.0040 0.0034  0.0155  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.0958 0.0956 0.2082 -0.0017 0.0175  0.0186  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1104 0.1071 0.2272 -0.0011 0.0223  0.0178  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1456 0.1417 0.2738 -0.0004 0.0263  0.0185  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1610 0.1528 0.2896 -0.0002 0.0317  0.0159  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1124 0.1099 0.2313 -0.0003 0.0209  0.0207  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1114 0.1074 0.2205 -0.0010 0.0201  0.0188  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1323 0.1306 0.2350 -0.0010 0.0161  0.0204  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1136 0.1057 0.2194 -0.0016 0.0235  0.0148  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1369 0.1330 0.2336 -0.0017 0.0172  0.0180  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1320 0.1247 0.2305 -0.0022 0.0212  0.0143  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1280 0.1160 0.2358 -0.0017 0.0281  0.0113  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1373 0.1272 0.2325 -0.0030 0.0229  0.0104  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1407 0.1256 0.2433 -0.0024 0.0295  0.0071  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1516 0.1378 0.2487 -0.0031 0.0266  0.0066  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1356 0.1359 0.2723 -0.0001 0.0236  0.0213  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1476 0.1481 0.2973 0.0005  0.0275  0.0223  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1580 0.1554 0.3053 -0.0003 0.0320  0.0191  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1748 0.1705 0.3307 0.0004  0.0375  0.0191  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1543 0.1610 0.3147 0.0011  0.0224  0.0261  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1405 0.1371 0.2767 -0.0014 0.0302  0.0170  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1448 0.1378 0.2771 -0.0018 0.0347  0.0145  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1408 0.1288 0.2576 -0.0018 0.0366  0.0110  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1363 0.1221 0.2451 -0.0021 0.0376  0.0094  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1563 0.1527 0.2903 -0.0031 0.0308  0.0152  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.1831 0.1846 0.3335 -0.0031 0.0289  0.0179  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2204 0.2210 0.3808 -0.0029 0.0341  0.0183  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.1782 0.1850 0.3317 -0.0033 0.0216  0.0200  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1332 0.1193 0.2468 -0.0012 0.0372  0.0099  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1353 0.1176 0.2358 -0.0012 0.0377  0.0063  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1477 0.1243 0.2408 -0.0003 0.0433  0.0032  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1774 0.1508 0.2754 0.0007  0.0491  0.0027  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1306 0.1122 0.2331 -0.0010 0.0378  0.0057  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1475 0.1256 0.2386 -0.0011 0.0377  0.0014  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1591 0.1402 0.2426 -0.0019 0.0324  0.0018  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1621 0.1390 0.2581 -0.0011 0.0387  0.0005  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1490 0.1239 0.2295 -0.0003 0.0421  0.0011  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1694 0.1384 0.2398 0.0011  0.0468  -0.0018 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1873 0.1540 0.2476 0.0016  0.0452  -0.0057 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2133 0.1753 0.2693 0.0028  0.0490  -0.0089 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1851 0.1537 0.2492 0.0012  0.0465  -0.0009 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2119 0.1743 0.2629 0.0033  0.0507  -0.0035 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2008 0.1713 0.2765 0.0006  0.0486  0.0023  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1534 0.1236 0.2107 0.0005  0.0394  -0.0058 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1617 0.1306 0.2109 0.0007  0.0372  -0.0096 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1304 0.1043 0.1822 -0.0007 0.0317  -0.0082 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1386 0.1158 0.1915 -0.0013 0.0291  -0.0051 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1742 0.1400 0.2095 0.0022  0.0374  -0.0119 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.1854 0.1511 0.2122 0.0025  0.0335  -0.0156 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2109 0.1737 0.2334 0.0032  0.0338  -0.0203 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1791 0.1484 0.2020 0.0020  0.0285  -0.0152 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2194 0.1842 0.2366 0.0030  0.0288  -0.0228 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.1925 0.1612 0.2097 0.0025  0.0259  -0.0195 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1812 0.1539 0.2050 0.0013  0.0261  -0.0118 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.1987 0.1705 0.2119 0.0024  0.0211  -0.0201 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.1946 0.1697 0.2134 0.0014  0.0219  -0.0125 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.1891 0.1639 0.2032 0.0019  0.0196  -0.0163 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1348 0.1089 0.1873 -0.0013 0.0301  -0.0105 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1300 0.1082 0.1843 -0.0024 0.0258  -0.0093 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1371 0.1145 0.1881 -0.0027 0.0242  -0.0136 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1444 0.1183 0.1953 -0.0024 0.0263  -0.0174 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1465 0.1277 0.2118 -0.0032 0.0254  -0.0052 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1508 0.1297 0.2248 -0.0032 0.0288  -0.0057 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1707 0.1482 0.2467 -0.0038 0.0289  -0.0091 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2140 0.1877 0.2929 -0.0036 0.0323  -0.0120 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1486 0.1285 0.2239 -0.0046 0.0260  -0.0090 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1256 0.1062 0.1748 -0.0033 0.0204  -0.0133 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1252 0.1059 0.1732 -0.0037 0.0184  -0.0174 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1225 0.1075 0.1759 -0.0048 0.0160  -0.0149 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1170 0.1045 0.1661 -0.0045 0.0138  -0.0129 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1515 0.1308 0.1879 -0.0023 0.0167  -0.0210 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2287 0.2085 0.2639 -0.0025 0.0137  -0.0259 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2536 0.2362 0.2973 -0.0041 0.0124  -0.0259 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2409 0.2184 0.2670 -0.0010 0.0126  -0.0298 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1163 0.1016 0.1791 -0.0060 0.0170  -0.0148 36  SER   A N   
241  C CA  A SER   A 30  ? 0.1249 0.1135 0.1934 -0.0068 0.0159  -0.0120 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1193 0.1080 0.1875 -0.0068 0.0158  -0.0119 36  SER   A CA  
243  C C   . SER   A 30  ? 0.1223 0.1131 0.1873 -0.0070 0.0128  -0.0148 36  SER   A C   
244  O O   . SER   A 30  ? 0.1311 0.1249 0.1963 -0.0070 0.0117  -0.0118 36  SER   A O   
245  C CB  A SER   A 30  ? 0.1629 0.1504 0.2426 -0.0079 0.0183  -0.0118 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1423 0.1302 0.2219 -0.0078 0.0182  -0.0112 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2206 0.2106 0.3063 -0.0085 0.0183  -0.0087 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1817 0.1677 0.2644 -0.0088 0.0182  -0.0170 36  SER   A OG  
249  N N   . SER   A 31  ? 0.1245 0.1139 0.1862 -0.0069 0.0114  -0.0205 37  SER   A N   
250  C CA  . SER   A 31  ? 0.1318 0.1239 0.1913 -0.0069 0.0079  -0.0233 37  SER   A CA  
251  C C   . SER   A 31  ? 0.1335 0.1272 0.1836 -0.0054 0.0061  -0.0211 37  SER   A C   
252  O O   . SER   A 31  ? 0.1445 0.1411 0.1942 -0.0052 0.0035  -0.0218 37  SER   A O   
253  C CB  . SER   A 31  ? 0.1722 0.1628 0.2294 -0.0068 0.0057  -0.0302 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2456 0.2331 0.2909 -0.0049 0.0053  -0.0321 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1139 0.1056 0.1574 -0.0043 0.0075  -0.0187 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1099 0.1024 0.1452 -0.0030 0.0063  -0.0166 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1105 0.1044 0.1476 -0.0034 0.0073  -0.0114 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1021 0.0966 0.1335 -0.0025 0.0064  -0.0097 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1243 0.1131 0.1507 -0.0015 0.0073  -0.0178 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1258 0.1127 0.1465 -0.0003 0.0057  -0.0230 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1449 0.1273 0.1554 0.0018  0.0076  -0.0238 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1320 0.1146 0.1356 0.0032  0.0073  -0.0209 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1423 0.1215 0.1356 0.0056  0.0081  -0.0214 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1765 0.1519 0.1637 0.0071  0.0091  -0.0248 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1491 0.1282 0.1376 0.0068  0.0082  -0.0185 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.0978 0.0920 0.1425 -0.0044 0.0090  -0.0088 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.0870 0.0822 0.1325 -0.0043 0.0095  -0.0041 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.0963 0.0899 0.1367 -0.0037 0.0098  -0.0032 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1052 0.0999 0.1431 -0.0035 0.0088  -0.0007 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.0998 0.0977 0.1439 -0.0041 0.0082  -0.0018 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1019 0.1005 0.1459 -0.0039 0.0083  0.0027  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.0951 0.0934 0.1445 -0.0041 0.0094  0.0050  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.0997 0.0992 0.1380 -0.0033 0.0071  0.0039  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.0923 0.0831 0.1317 -0.0034 0.0114  -0.0055 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.0977 0.0868 0.1341 -0.0029 0.0126  -0.0044 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.0922 0.0799 0.1353 -0.0032 0.0153  -0.0035 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1021 0.0883 0.1489 -0.0033 0.0170  -0.0053 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1155 0.1018 0.1436 -0.0017 0.0132  -0.0071 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1187 0.1061 0.1398 -0.0009 0.0109  -0.0074 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1392 0.1232 0.1517 0.0009  0.0119  -0.0096 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1290 0.1177 0.1498 -0.0012 0.0100  -0.0044 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.0862 0.0743 0.1313 -0.0032 0.0157  -0.0009 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.0970 0.0839 0.1488 -0.0032 0.0185  0.0001  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1027 0.0886 0.1530 -0.0030 0.0195  0.0007  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1061 0.0936 0.1537 -0.0033 0.0171  0.0019  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.0971 0.0868 0.1581 -0.0036 0.0174  0.0034  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.0963 0.0856 0.1666 -0.0034 0.0201  0.0049  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1081 0.0988 0.1864 -0.0033 0.0200  0.0072  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1196 0.1107 0.1930 -0.0036 0.0189  0.0072  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1095 0.0923 0.1616 -0.0024 0.0237  -0.0001 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1149 0.0962 0.1676 -0.0022 0.0260  0.0008  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1128 0.0947 0.1772 -0.0024 0.0287  0.0026  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1276 0.1078 0.1954 -0.0019 0.0317  0.0018  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1300 0.1063 0.1735 -0.0007 0.0298  -0.0015 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1429 0.1172 0.1883 -0.0004 0.0335  0.0000  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1385 0.1147 0.1714 -0.0002 0.0268  -0.0031 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1142 0.0988 0.1854 -0.0032 0.0273  0.0049  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1116 0.0977 0.1957 -0.0034 0.0292  0.0069  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1327 0.1172 0.2198 -0.0036 0.0326  0.0071  43  SER   A C   
300  O O   . SER   A 37  ? 0.1317 0.1146 0.2119 -0.0038 0.0324  0.0064  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1257 0.1174 0.2174 -0.0041 0.0237  0.0094  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1396 0.1337 0.2284 -0.0051 0.0191  0.0098  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1424 0.1272 0.2415 -0.0035 0.0362  0.0085  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1589 0.1422 0.2635 -0.0037 0.0403  0.0091  44  SER   A CA  
305  C C   . SER   A 38  ? 0.1738 0.1625 0.2894 -0.0054 0.0355  0.0106  44  SER   A C   
306  O O   . SER   A 38  ? 0.1830 0.1767 0.3051 -0.0059 0.0302  0.0119  44  SER   A O   
307  C CB  . SER   A 38  ? 0.1898 0.1702 0.3018 -0.0025 0.0477  0.0095  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2281 0.2127 0.3523 -0.0026 0.0458  0.0111  44  SER   A OG  
309  N N   . THR   A 39  ? 0.1752 0.1626 0.2926 -0.0063 0.0373  0.0104  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2017 0.1937 0.3298 -0.0082 0.0327  0.0110  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2320 0.2233 0.3743 -0.0087 0.0384  0.0119  45  THR   A C   
312  O O   . THR   A 39  ? 0.2441 0.2299 0.3836 -0.0075 0.0465  0.0121  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2193 0.2103 0.3375 -0.0092 0.0290  0.0094  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2351 0.2205 0.3487 -0.0087 0.0355  0.0090  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2272 0.2181 0.3311 -0.0084 0.0249  0.0085  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2497 0.2464 0.4067 -0.0104 0.0343  0.0124  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2761 0.2727 0.4489 -0.0113 0.0394  0.0132  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2934 0.2871 0.4642 -0.0129 0.0406  0.0118  46  THR   A C   
319  O O   . THR   A 40  ? 0.3239 0.3136 0.5002 -0.0128 0.0485  0.0126  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3041 0.3084 0.4964 -0.0123 0.0344  0.0142  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3312 0.3403 0.5210 -0.0135 0.0242  0.0130  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3138 0.3197 0.5107 -0.0104 0.0358  0.0162  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2802 0.2754 0.4431 -0.0140 0.0334  0.0100  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2737 0.2659 0.4347 -0.0155 0.0341  0.0086  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2764 0.2614 0.4185 -0.0137 0.0388  0.0085  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2673 0.2515 0.3962 -0.0120 0.0376  0.0085  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2889 0.2858 0.4505 -0.0174 0.0242  0.0063  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2751 0.2553 0.4167 -0.0141 0.0438  0.0085  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2855 0.2589 0.4100 -0.0121 0.0480  0.0087  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2806 0.2551 0.3938 -0.0125 0.0408  0.0067  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2959 0.2734 0.4157 -0.0148 0.0354  0.0049  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3293 0.2971 0.4588 -0.0122 0.0560  0.0100  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4322 0.3928 0.5447 -0.0098 0.0602  0.0108  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5398 0.4955 0.6406 -0.0062 0.0669  0.0126  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5698 0.5263 0.6760 -0.0056 0.0702  0.0134  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5652 0.5155 0.6494 -0.0037 0.0689  0.0132  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2509 0.2229 0.3474 -0.0103 0.0406  0.0067  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.2493 0.2221 0.3344 -0.0102 0.0347  0.0051  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.2662 0.2358 0.3485 -0.0109 0.0347  0.0042  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3029 0.2690 0.3922 -0.0115 0.0397  0.0049  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2407 0.2116 0.3140 -0.0110 0.0290  0.0025  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2255 0.1932 0.2949 -0.0114 0.0285  0.0013  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2189 0.1825 0.2729 -0.0085 0.0306  0.0021  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2062 0.1656 0.2572 -0.0081 0.0328  0.0021  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2347 0.2065 0.3060 -0.0134 0.0207  -0.0015 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2413 0.2178 0.3023 -0.0123 0.0143  -0.0018 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2108 0.1754 0.2561 -0.0064 0.0304  0.0029  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2012 0.1634 0.2326 -0.0037 0.0308  0.0033  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2019 0.1587 0.2261 -0.0006 0.0373  0.0054  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2535 0.2092 0.2826 -0.0005 0.0415  0.0065  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2021 0.1692 0.2294 -0.0035 0.0256  0.0024  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.2316 0.2026 0.2613 -0.0055 0.0195  0.0007  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.2400 0.2094 0.2665 -0.0056 0.0185  -0.0002 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.1901 0.1658 0.2240 -0.0065 0.0159  0.0005  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.1923 0.1462 0.2044 0.0022  0.0377  0.0059  52  THR   A N   
356  C CA  . THR   A 46  ? 0.2275 0.1764 0.2285 0.0061  0.0420  0.0077  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2032 0.1552 0.1947 0.0078  0.0373  0.0063  52  THR   A C   
358  O O   . THR   A 46  ? 0.1989 0.1542 0.1900 0.0069  0.0326  0.0051  52  THR   A O   
359  C CB  . THR   A 46  ? 0.2881 0.2317 0.2841 0.0080  0.0448  0.0095  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3664 0.3058 0.3701 0.0072  0.0507  0.0112  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3173 0.2570 0.2989 0.0128  0.0468  0.0113  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.1721 0.1230 0.1568 0.0101  0.0385  0.0063  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.1575 0.1114 0.1347 0.0115  0.0340  0.0045  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.1689 0.1194 0.1345 0.0154  0.0345  0.0056  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.1891 0.1340 0.1485 0.0182  0.0394  0.0075  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.1562 0.1107 0.1325 0.0118  0.0344  0.0031  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.1789 0.1364 0.1672 0.0085  0.0346  0.0027  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.1551 0.1132 0.1261 0.0126  0.0292  0.0007  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.1873 0.1505 0.1826 0.0056  0.0291  0.0018  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.1562 0.1098 0.1186 0.0161  0.0297  0.0046  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.1706 0.1221 0.1227 0.0201  0.0290  0.0055  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.1735 0.1242 0.1170 0.0228  0.0284  0.0043  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.1725 0.1267 0.1186 0.0212  0.0258  0.0016  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.1635 0.1197 0.1165 0.0198  0.0238  0.0045  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.1859 0.1319 0.1185 0.0272  0.0305  0.0061  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.1912 0.1362 0.1134 0.0304  0.0291  0.0044  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2173 0.1624 0.1307 0.0345  0.0256  0.0054  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2292 0.1689 0.1335 0.0385  0.0289  0.0087  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.1996 0.1376 0.1154 0.0324  0.0360  0.0062  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2072 0.1449 0.1334 0.0286  0.0401  0.0059  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2198 0.1625 0.1517 0.0258  0.0364  0.0019  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2120 0.1541 0.1539 0.0228  0.0407  0.0023  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2256 0.1719 0.1761 0.0197  0.0386  -0.0001 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2084 0.1593 0.1588 0.0189  0.0326  -0.0032 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2399 0.1858 0.2000 0.0174  0.0425  0.0007  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2093 0.1608 0.1263 0.0335  0.0192  0.0029  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2072 0.1604 0.1201 0.0367  0.0154  0.0039  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2147 0.1754 0.1317 0.0356  0.0081  0.0001  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2133 0.1774 0.1368 0.0322  0.0065  -0.0031 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.1994 0.1519 0.1186 0.0354  0.0178  0.0068  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.1934 0.1522 0.1268 0.0297  0.0153  0.0045  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2397 0.2030 0.1546 0.0386  0.0041  0.0007  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2388 0.2095 0.1598 0.0377  -0.0024 -0.0025 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2373 0.2113 0.1666 0.0366  -0.0029 -0.0009 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2428 0.2221 0.1757 0.0376  -0.0077 -0.0021 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.2909 0.2630 0.2033 0.0423  -0.0078 -0.0041 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.3713 0.3405 0.2753 0.0476  -0.0076 -0.0001 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.3822 0.3476 0.2872 0.0477  -0.0026 0.0039  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.4657 0.4361 0.3620 0.0519  -0.0125 -0.0011 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2162 0.1872 0.1493 0.0344  0.0019  0.0015  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.1954 0.1691 0.1358 0.0333  0.0017  0.0025  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.1885 0.1691 0.1379 0.0304  -0.0020 -0.0004 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.1773 0.1596 0.1301 0.0275  -0.0025 -0.0027 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.1952 0.1647 0.1386 0.0307  0.0069  0.0042  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2084 0.1696 0.1445 0.0340  0.0123  0.0083  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.1700 0.1541 0.1238 0.0314  -0.0039 0.0000  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.1564 0.1466 0.1197 0.0289  -0.0060 -0.0019 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1465 0.1364 0.1142 0.0279  -0.0033 -0.0003 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1466 0.1410 0.1215 0.0269  -0.0044 -0.0010 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.1792 0.1753 0.1455 0.0311  -0.0113 -0.0036 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2445 0.2423 0.2093 0.0307  -0.0149 -0.0069 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.2868 0.2912 0.2570 0.0324  -0.0207 -0.0092 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.2939 0.2985 0.2578 0.0361  -0.0246 -0.0099 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2484 0.2582 0.2305 0.0299  -0.0216 -0.0104 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1403 0.1244 0.1038 0.0281  0.0006  0.0018  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1487 0.1314 0.1155 0.0266  0.0034  0.0024  60  THR   A CA  
417  C C   . THR   A 54  ? 0.1349 0.1127 0.0999 0.0239  0.0066  0.0026  60  THR   A C   
418  O O   . THR   A 54  ? 0.1550 0.1294 0.1158 0.0244  0.0078  0.0033  60  THR   A O   
419  C CB  . THR   A 54  ? 0.1684 0.1489 0.1336 0.0299  0.0048  0.0044  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2103 0.1850 0.1690 0.0321  0.0070  0.0065  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.1792 0.1650 0.1474 0.0329  0.0014  0.0045  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1295 0.1072 0.0978 0.0212  0.0079  0.0020  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1227 0.0966 0.0910 0.0186  0.0101  0.0017  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1209 0.0955 0.0920 0.0163  0.0103  0.0007  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1278 0.1041 0.0997 0.0174  0.0101  0.0006  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1183 0.0913 0.0907 0.0135  0.0108  -0.0001 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1116 0.0844 0.0850 0.0115  0.0106  -0.0014 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1149 0.0903 0.0911 0.0088  0.0089  -0.0019 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1231 0.0977 0.1009 0.0078  0.0091  -0.0016 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1279 0.0952 0.1004 0.0109  0.0126  -0.0021 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.1409 0.1079 0.1135 0.0087  0.0115  -0.0041 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1601 0.1244 0.1302 0.0139  0.0147  -0.0013 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1193 0.0976 0.0961 0.0080  0.0076  -0.0022 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1051 0.0857 0.0847 0.0058  0.0060  -0.0022 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1139 0.0935 0.0919 0.0045  0.0051  -0.0031 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1200 0.0980 0.0944 0.0054  0.0058  -0.0039 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1101 0.0952 0.0924 0.0059  0.0052  -0.0013 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1102 0.0972 0.0918 0.0066  0.0055  -0.0008 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1167 0.1040 0.0974 0.0086  0.0067  -0.0007 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1105 0.0991 0.0928 0.0056  0.0049  0.0000  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1193 0.1081 0.1001 0.0094  0.0079  -0.0001 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1198 0.1096 0.1010 0.0065  0.0061  0.0009  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1260 0.1159 0.1068 0.0084  0.0079  0.0008  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1466 0.1375 0.1270 0.0095  0.0100  0.0019  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1120 0.0926 0.0926 0.0026  0.0033  -0.0031 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1203 0.1006 0.0989 0.0016  0.0013  -0.0041 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1157 0.0992 0.0932 0.0022  0.0006  -0.0024 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1211 0.1074 0.1027 0.0018  0.0004  -0.0008 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1247 0.1047 0.1075 -0.0005 -0.0007 -0.0049 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1333 0.1133 0.1137 -0.0012 -0.0038 -0.0062 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.1586 0.1354 0.1342 -0.0010 -0.0041 -0.0087 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1526 0.1358 0.1349 -0.0018 -0.0065 -0.0049 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.1578 0.1344 0.1295 -0.0014 -0.0075 -0.0104 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.1660 0.1493 0.1446 -0.0019 -0.0100 -0.0060 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.1694 0.1493 0.1423 -0.0018 -0.0107 -0.0090 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2259 0.2056 0.1937 -0.0017 -0.0146 -0.0106 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1204 0.1029 0.0922 0.0032  0.0007  -0.0028 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1114 0.0959 0.0810 0.0041  0.0010  -0.0008 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1298 0.1135 0.0948 0.0038  -0.0020 -0.0013 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.1430 0.1237 0.1012 0.0044  -0.0023 -0.0032 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1204 0.1041 0.0865 0.0061  0.0040  -0.0006 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.1433 0.1284 0.1062 0.0076  0.0059  0.0023  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1313 0.1175 0.0998 0.0030  -0.0041 0.0004  66  SER   A N   
464  C CA  . SER   A 60  ? 0.1402 0.1262 0.1048 0.0029  -0.0078 0.0000  66  SER   A CA  
465  C C   . SER   A 60  ? 0.1500 0.1347 0.1051 0.0051  -0.0073 0.0011  66  SER   A C   
466  O O   . SER   A 60  ? 0.1619 0.1447 0.1100 0.0055  -0.0103 -0.0009 66  SER   A O   
467  C CB  . SER   A 60  ? 0.1860 0.1751 0.1572 0.0020  -0.0101 0.0021  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.2901 0.2814 0.2637 0.0029  -0.0079 0.0056  66  SER   A OG  
469  N N   . SER   A 61  ? 0.1330 0.1184 0.0877 0.0066  -0.0033 0.0038  67  SER   A N   
470  C CA  . SER   A 61  ? 0.1419 0.1257 0.0877 0.0091  -0.0013 0.0055  67  SER   A CA  
471  C C   . SER   A 61  ? 0.1430 0.1228 0.0808 0.0102  0.0004  0.0026  67  SER   A C   
472  O O   . SER   A 61  ? 0.1537 0.1313 0.0825 0.0125  0.0023  0.0035  67  SER   A O   
473  C CB  . SER   A 61  ? 0.1539 0.1396 0.1036 0.0102  0.0031  0.0095  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.1512 0.1375 0.1062 0.0099  0.0063  0.0087  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.1397 0.1183 0.0804 0.0089  0.0001  -0.0007 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1495 0.1237 0.0835 0.0097  0.0014  -0.0040 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.1618 0.1337 0.0957 0.0078  -0.0026 -0.0084 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.1745 0.1423 0.1037 0.0081  -0.0018 -0.0117 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.1614 0.1357 0.1000 0.0104  0.0059  -0.0036 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.1614 0.1376 0.1007 0.0124  0.0103  0.0000  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.1771 0.1498 0.1060 0.0149  0.0132  0.0000  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.1955 0.1701 0.1267 0.0167  0.0182  0.0039  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.1861 0.1621 0.1164 0.0175  0.0191  0.0075  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.1969 0.1730 0.1234 0.0169  0.0149  0.0079  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.1895 0.1669 0.1236 0.0190  0.0244  0.0109  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.1671 0.1415 0.1075 0.0057  -0.0064 -0.0084 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.1979 0.1708 0.1418 0.0034  -0.0096 -0.0121 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.1911 0.1608 0.1373 0.0032  -0.0063 -0.0141 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2111 0.1769 0.1551 0.0025  -0.0071 -0.0180 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2369 0.2075 0.1732 0.0035  -0.0140 -0.0156 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3158 0.2898 0.2515 0.0035  -0.0186 -0.0139 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.3663 0.3390 0.2996 0.0023  -0.0248 -0.0186 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.3625 0.3380 0.2919 0.0036  -0.0295 -0.0167 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.3586 0.3320 0.2745 0.0062  -0.0311 -0.0170 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.3909 0.3593 0.2966 0.0076  -0.0283 -0.0197 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.3391 0.3152 0.2514 0.0079  -0.0350 -0.0142 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.1725 0.1437 0.1229 0.0039  -0.0025 -0.0114 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.1745 0.1428 0.1264 0.0044  0.0008  -0.0125 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.1549 0.1256 0.1138 0.0044  0.0025  -0.0100 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.1531 0.1278 0.1149 0.0045  0.0023  -0.0074 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2295 0.1962 0.1752 0.0071  0.0043  -0.0121 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3522 0.3138 0.2894 0.0078  0.0044  -0.0157 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4426 0.4026 0.3761 0.0106  0.0093  -0.0149 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5212 0.4752 0.4466 0.0115  0.0104  -0.0188 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.5591 0.5120 0.4743 0.0125  0.0092  -0.0197 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1501 0.1182 0.1113 0.0046  0.0045  -0.0108 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1321 0.1017 0.0978 0.0054  0.0063  -0.0085 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.1484 0.1179 0.1122 0.0080  0.0091  -0.0075 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.1808 0.1470 0.1408 0.0092  0.0108  -0.0090 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1347 0.1010 0.1038 0.0045  0.0071  -0.0093 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.1535 0.1201 0.1267 0.0019  0.0049  -0.0102 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.1900 0.1588 0.1682 0.0012  0.0048  -0.0084 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.1603 0.1252 0.1341 0.0000  0.0027  -0.0129 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.1783 0.1469 0.1608 -0.0011 0.0030  -0.0098 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2167 0.1833 0.1970 -0.0020 0.0012  -0.0126 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1307 0.1039 0.0976 0.0091  0.0096  -0.0053 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1216 0.0960 0.0889 0.0116  0.0117  -0.0042 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1287 0.1042 0.0991 0.0128  0.0116  -0.0029 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1270 0.1045 0.0998 0.0118  0.0101  -0.0023 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1280 0.1068 0.0967 0.0120  0.0118  -0.0028 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1485 0.1260 0.1124 0.0119  0.0126  -0.0033 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.1776 0.1520 0.1372 0.0136  0.0152  -0.0043 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.1668 0.1460 0.1300 0.0104  0.0109  -0.0027 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.1862 0.1589 0.1397 0.0140  0.0162  -0.0048 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.1790 0.1568 0.1363 0.0109  0.0115  -0.0027 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.1876 0.1620 0.1394 0.0127  0.0142  -0.0039 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2305 0.2029 0.1747 0.0135  0.0149  -0.0042 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1260 0.1003 0.0962 0.0153  0.0133  -0.0024 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1337 0.1096 0.1059 0.0172  0.0127  -0.0010 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1370 0.1190 0.1133 0.0179  0.0112  -0.0002 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.1767 0.1611 0.1550 0.0179  0.0120  -0.0002 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1451 0.1177 0.1160 0.0201  0.0150  -0.0005 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.1571 0.1291 0.1271 0.0200  0.0168  -0.0016 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1360 0.1073 0.1039 0.0170  0.0158  -0.0031 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1260 0.1103 0.1039 0.0183  0.0092  0.0002  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1264 0.1165 0.1093 0.0185  0.0071  0.0002  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1232 0.1147 0.1061 0.0209  0.0049  0.0004  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1386 0.1266 0.1168 0.0218  0.0049  0.0008  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1553 0.1473 0.1403 0.0156  0.0058  -0.0004 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.1747 0.1674 0.1610 0.0139  0.0073  -0.0002 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.1644 0.1531 0.1459 0.0143  0.0056  -0.0007 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1380 0.1347 0.1264 0.0221  0.0030  0.0002  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1369 0.1365 0.1260 0.0240  -0.0005 -0.0004 75  SER   A CA  
544  C C   . SER   A 69  ? 0.1355 0.1390 0.1297 0.0214  -0.0026 -0.0022 75  SER   A C   
545  O O   . SER   A 69  ? 0.1386 0.1450 0.1391 0.0198  -0.0016 -0.0023 75  SER   A O   
546  C CB  . SER   A 69  ? 0.1723 0.1759 0.1665 0.0270  -0.0018 0.0001  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2796 0.2792 0.2696 0.0296  0.0004  0.0019  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1143 0.1171 0.1054 0.0211  -0.0047 -0.0034 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1092 0.1146 0.1048 0.0185  -0.0061 -0.0054 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1244 0.1324 0.1203 0.0199  -0.0104 -0.0078 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1352 0.1415 0.1243 0.0229  -0.0121 -0.0077 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1177 0.1192 0.1099 0.0160  -0.0038 -0.0051 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1164 0.1126 0.1001 0.0170  -0.0027 -0.0044 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1345 0.1267 0.1143 0.0177  -0.0001 -0.0025 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1216 0.1165 0.1016 0.0176  -0.0040 -0.0057 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1409 0.1280 0.1144 0.0185  0.0016  -0.0017 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1437 0.1333 0.1162 0.0188  -0.0019 -0.0046 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1465 0.1323 0.1164 0.0192  0.0010  -0.0024 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1179 0.1299 0.1216 0.0178  -0.0121 -0.0100 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1267 0.1412 0.1311 0.0187  -0.0167 -0.0133 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1385 0.1485 0.1343 0.0186  -0.0168 -0.0146 77  SER   A C   
562  O O   . SER   A 71  ? 0.1485 0.1544 0.1408 0.0171  -0.0131 -0.0131 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1493 0.1690 0.1660 0.0163  -0.0182 -0.0157 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1814 0.1991 0.2004 0.0130  -0.0150 -0.0153 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1374 0.1480 0.1291 0.0207  -0.0209 -0.0174 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1529 0.1589 0.1359 0.0209  -0.0206 -0.0189 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1637 0.1699 0.1532 0.0171  -0.0192 -0.0210 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1603 0.1709 0.1609 0.0148  -0.0202 -0.0224 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.1856 0.1924 0.1623 0.0243  -0.0259 -0.0220 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2259 0.2312 0.1943 0.0287  -0.0265 -0.0190 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3035 0.3095 0.2641 0.0325  -0.0324 -0.0220 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.3955 0.4005 0.3482 0.0375  -0.0337 -0.0188 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4604 0.4642 0.4016 0.0417  -0.0387 -0.0211 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1530 0.1542 0.1367 0.0163  -0.0163 -0.0210 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1553 0.1565 0.1458 0.0130  -0.0147 -0.0228 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1674 0.1722 0.1644 0.0121  -0.0189 -0.0276 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.1777 0.1824 0.1689 0.0143  -0.0227 -0.0310 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.1913 0.1866 0.1731 0.0135  -0.0117 -0.0226 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2273 0.2192 0.1993 0.0165  -0.0101 -0.0194 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.1743 0.1697 0.1459 0.0188  -0.0140 -0.0194 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1452 0.1532 0.1544 0.0090  -0.0181 -0.0280 80  SER   A N   
582  C CA  . SER   A 74  ? 0.1594 0.1710 0.1775 0.0077  -0.0218 -0.0327 80  SER   A CA  
583  C C   . SER   A 74  ? 0.1361 0.1481 0.1655 0.0041  -0.0189 -0.0327 80  SER   A C   
584  O O   . SER   A 74  ? 0.1317 0.1415 0.1613 0.0029  -0.0144 -0.0290 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2320 0.2494 0.2560 0.0089  -0.0257 -0.0332 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3280 0.3481 0.3615 0.0072  -0.0226 -0.0296 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1179 0.1327 0.1569 0.0025  -0.0216 -0.0374 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1353 0.1503 0.1864 -0.0008 -0.0189 -0.0378 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1465 0.1663 0.2096 -0.0020 -0.0177 -0.0350 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1682 0.1927 0.2383 -0.0018 -0.0215 -0.0377 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1682 0.1835 0.2243 -0.0019 -0.0225 -0.0447 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2469 0.2567 0.2975 -0.0023 -0.0209 -0.0474 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2769 0.2874 0.3327 -0.0033 -0.0254 -0.0554 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2384 0.2457 0.2958 -0.0047 -0.0149 -0.0438 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1349 0.1536 0.2008 -0.0031 -0.0127 -0.0299 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1466 0.1687 0.2215 -0.0037 -0.0104 -0.0263 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1345 0.1557 0.2193 -0.0061 -0.0059 -0.0241 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.1287 0.1459 0.2092 -0.0065 -0.0032 -0.0220 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.1691 0.1901 0.2343 -0.0017 -0.0084 -0.0214 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2050 0.2267 0.2612 0.0010  -0.0125 -0.0231 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.1899 0.2131 0.2620 -0.0020 -0.0048 -0.0171 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2513 0.2720 0.2992 0.0030  -0.0110 -0.0193 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1211 0.1457 0.2197 -0.0075 -0.0046 -0.0240 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.1268 0.1503 0.2352 -0.0094 0.0004  -0.0211 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.1338 0.1552 0.2360 -0.0083 0.0050  -0.0142 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.1577 0.1806 0.2556 -0.0066 0.0054  -0.0116 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.1441 0.1718 0.2695 -0.0109 0.0011  -0.0223 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.1805 0.2065 0.3167 -0.0126 0.0070  -0.0187 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2037 0.2298 0.3415 -0.0118 0.0124  -0.0123 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2044 0.2281 0.3477 -0.0147 0.0077  -0.0214 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2215 0.2454 0.3678 -0.0128 0.0183  -0.0082 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2215 0.2431 0.3750 -0.0160 0.0137  -0.0174 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.2133 0.2352 0.3682 -0.0149 0.0189  -0.0106 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.1207 0.1384 0.2216 -0.0089 0.0081  -0.0114 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.1261 0.1417 0.2209 -0.0077 0.0118  -0.0051 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.1365 0.1510 0.2417 -0.0088 0.0167  -0.0016 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.1319 0.1445 0.2430 -0.0102 0.0173  -0.0030 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.1182 0.1305 0.2011 -0.0069 0.0106  -0.0045 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.1460 0.1566 0.2232 -0.0057 0.0135  0.0016  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.1180 0.1308 0.1910 -0.0057 0.0066  -0.0074 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.1480 0.1630 0.2545 -0.0078 0.0206  0.0033  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.1599 0.1735 0.2758 -0.0083 0.0260  0.0076  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.1618 0.1715 0.2730 -0.0078 0.0274  0.0110  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.1524 0.1610 0.2518 -0.0066 0.0248  0.0115  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2220 0.2362 0.3365 -0.0065 0.0303  0.0128  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3437 0.3565 0.4689 -0.0066 0.0369  0.0176  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.4772 0.4902 0.6004 -0.0046 0.0418  0.0227  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5062 0.5175 0.6372 -0.0042 0.0481  0.0274  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5137 0.5279 0.6275 -0.0031 0.0400  0.0220  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.1677 0.1756 0.2889 -0.0085 0.0316  0.0138  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.1583 0.1628 0.2764 -0.0076 0.0331  0.0178  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.1677 0.1711 0.2726 -0.0048 0.0335  0.0234  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.1754 0.1795 0.2765 -0.0034 0.0356  0.0263  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.1761 0.1785 0.3076 -0.0083 0.0386  0.0209  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.1582 0.1599 0.2565 -0.0040 0.0316  0.0247  87  SER   A N   
636  C CA  . SER   A 81  ? 0.1610 0.1618 0.2476 -0.0015 0.0311  0.0296  87  SER   A CA  
637  C C   . SER   A 81  ? 0.1780 0.1764 0.2673 -0.0006 0.0322  0.0335  87  SER   A C   
638  O O   . SER   A 81  ? 0.1880 0.1853 0.2881 -0.0021 0.0339  0.0321  87  SER   A O   
639  C CB  . SER   A 81  ? 0.1767 0.1786 0.2521 -0.0013 0.0259  0.0262  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.1723 0.1738 0.2493 -0.0025 0.0232  0.0229  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.1828 0.1805 0.2623 0.0017  0.0306  0.0376  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.2000 0.1962 0.2827 0.0028  0.0309  0.0412  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.2039 0.2004 0.2897 0.0011  0.0278  0.0366  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.2191 0.2142 0.3111 0.0014  0.0287  0.0385  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.2829 0.2786 0.3549 0.0060  0.0295  0.0469  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.4209 0.4183 0.4812 0.0063  0.0242  0.0443  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.5898 0.5866 0.6382 0.0094  0.0235  0.0490  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.6346 0.6308 0.6802 0.0116  0.0218  0.0533  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.6384 0.6350 0.6800 0.0098  0.0245  0.0484  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.1822 0.1803 0.2638 -0.0005 0.0245  0.0308  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.1699 0.1679 0.2527 -0.0017 0.0221  0.0267  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.1524 0.1496 0.2434 -0.0039 0.0233  0.0214  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.1693 0.1652 0.2635 -0.0045 0.0230  0.0189  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.1744 0.1738 0.2469 -0.0017 0.0182  0.0239  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.1844 0.1845 0.2480 0.0003  0.0161  0.0279  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.2011 0.2016 0.2577 0.0013  0.0163  0.0293  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.1919 0.1921 0.2547 0.0013  0.0141  0.0303  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.2242 0.2249 0.2715 0.0031  0.0141  0.0321  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.2100 0.2110 0.2647 0.0032  0.0113  0.0334  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.2399 0.2410 0.2861 0.0040  0.0112  0.0340  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.2821 0.2835 0.3193 0.0060  0.0083  0.0365  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.1376 0.1355 0.2319 -0.0050 0.0245  0.0191  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.1300 0.1275 0.2316 -0.0071 0.0246  0.0131  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.1529 0.1508 0.2644 -0.0081 0.0275  0.0133  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.1538 0.1532 0.2636 -0.0073 0.0287  0.0164  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.1165 0.1157 0.2109 -0.0077 0.0207  0.0076  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.1108 0.1094 0.1956 -0.0069 0.0180  0.0065  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.1301 0.1266 0.2164 -0.0074 0.0181  0.0037  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1126 0.1126 0.1878 -0.0058 0.0160  0.0082  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1170 0.1129 0.1957 -0.0067 0.0164  0.0028  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1071 0.1065 0.1751 -0.0053 0.0139  0.0070  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1102 0.1076 0.1803 -0.0058 0.0143  0.0046  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1148 0.1114 0.1792 -0.0053 0.0132  0.0038  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.1732 0.1699 0.2952 -0.0101 0.0286  0.0091  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.1685 0.1662 0.3018 -0.0116 0.0309  0.0077  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.1646 0.1658 0.2943 -0.0122 0.0272  0.0031  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.1727 0.1748 0.2919 -0.0117 0.0231  0.0001  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.1918 0.1869 0.3356 -0.0137 0.0317  0.0028  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2174 0.2115 0.3521 -0.0134 0.0281  -0.0013 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.1892 0.1836 0.3132 -0.0110 0.0277  0.0045  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.1634 0.1667 0.3028 -0.0134 0.0288  0.0023  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.1777 0.1849 0.3167 -0.0140 0.0251  -0.0024 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.1612 0.1683 0.2988 -0.0152 0.0202  -0.0103 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.1762 0.1807 0.3211 -0.0167 0.0209  -0.0135 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.1868 0.1961 0.3406 -0.0154 0.0280  -0.0023 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.1557 0.1645 0.2820 -0.0141 0.0156  -0.0131 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.1461 0.1540 0.2677 -0.0145 0.0113  -0.0199 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.1483 0.1590 0.2601 -0.0130 0.0066  -0.0222 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.1670 0.1799 0.2753 -0.0118 0.0071  -0.0184 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.1447 0.1482 0.2582 -0.0136 0.0125  -0.0184 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.1593 0.1630 0.2591 -0.0115 0.0118  -0.0143 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.1351 0.1357 0.2314 -0.0107 0.0142  -0.0101 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.1406 0.1405 0.2246 -0.0093 0.0123  -0.0100 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.1189 0.1203 0.1950 -0.0080 0.0113  -0.0070 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.1331 0.1332 0.1997 -0.0069 0.0100  -0.0070 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.1272 0.1309 0.2051 -0.0077 0.0120  -0.0040 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1374 0.1475 0.2442 -0.0129 0.0024  -0.0283 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.1482 0.1600 0.2435 -0.0109 -0.0018 -0.0298 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1424 0.1505 0.2242 -0.0092 -0.0008 -0.0275 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1574 0.1617 0.2369 -0.0095 0.0000  -0.0294 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.1623 0.1751 0.2575 -0.0109 -0.0070 -0.0374 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.1749 0.1926 0.2841 -0.0124 -0.0091 -0.0401 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.1781 0.2005 0.2870 -0.0111 -0.0121 -0.0399 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.1943 0.2119 0.3183 -0.0151 -0.0075 -0.0426 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2061 0.2336 0.3298 -0.0125 -0.0139 -0.0423 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2168 0.2391 0.3558 -0.0168 -0.0089 -0.0450 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2204 0.2478 0.3595 -0.0154 -0.0121 -0.0447 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2653 0.2978 0.4213 -0.0172 -0.0135 -0.0474 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1183 0.1272 0.1918 -0.0075 -0.0009 -0.0237 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1170 0.1227 0.1785 -0.0061 -0.0003 -0.0218 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1041 0.1096 0.1559 -0.0042 -0.0040 -0.0255 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1256 0.1344 0.1771 -0.0032 -0.0068 -0.0262 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1127 0.1188 0.1708 -0.0053 0.0018  -0.0159 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1108 0.1139 0.1584 -0.0041 0.0022  -0.0144 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1068 0.1098 0.1527 -0.0039 0.0042  -0.0092 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1238 0.1273 0.1759 -0.0047 0.0063  -0.0062 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1087 0.1107 0.1459 -0.0027 0.0036  -0.0080 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1067 0.1084 0.1509 -0.0034 -0.0040 -0.0276 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1080 0.1085 0.1413 -0.0011 -0.0069 -0.0304 96  SER   A CA  
720  C C   . SER   A 90  ? 0.1333 0.1321 0.1567 0.0008  -0.0055 -0.0264 96  SER   A C   
721  O O   . SER   A 90  ? 0.1288 0.1267 0.1534 0.0000  -0.0024 -0.0223 96  SER   A O   
722  C CB  . SER   A 90  ? 0.1440 0.1406 0.1735 -0.0008 -0.0070 -0.0351 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1637 0.1564 0.1918 -0.0012 -0.0025 -0.0325 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1254 0.1239 0.1396 0.0033  -0.0081 -0.0278 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1294 0.1254 0.1341 0.0053  -0.0066 -0.0244 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1226 0.1209 0.1308 0.0046  -0.0054 -0.0200 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1272 0.1232 0.1308 0.0051  -0.0030 -0.0169 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1395 0.1304 0.1389 0.0054  -0.0027 -0.0234 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.1560 0.1435 0.1498 0.0066  -0.0032 -0.0278 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.1839 0.1680 0.1655 0.0097  -0.0033 -0.0284 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.1643 0.1511 0.1626 0.0053  -0.0032 -0.0315 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2039 0.1852 0.1818 0.0103  -0.0036 -0.0328 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2008 0.1836 0.1889 0.0076  -0.0036 -0.0350 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1149 0.1176 0.1308 0.0038  -0.0070 -0.0201 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1092 0.1137 0.1277 0.0034  -0.0055 -0.0163 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1142 0.1208 0.1297 0.0056  -0.0077 -0.0162 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1169 0.1261 0.1342 0.0065  -0.0111 -0.0191 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1231 0.1306 0.1530 0.0012  -0.0046 -0.0159 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1241 0.1331 0.1567 0.0009  -0.0024 -0.0118 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1306 0.1365 0.1578 0.0007  -0.0001 -0.0084 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1525 0.1639 0.1966 -0.0009 -0.0008 -0.0111 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1091 0.1146 0.1207 0.0063  -0.0060 -0.0129 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1126 0.1193 0.1212 0.0086  -0.0072 -0.0121 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1160 0.1247 0.1293 0.0079  -0.0052 -0.0096 99  MET   A C   
745  O O   . MET   A 93  ? 0.1356 0.1422 0.1476 0.0068  -0.0026 -0.0074 99  MET   A O   
746  C CB  . MET   A 93  ? 0.1246 0.1269 0.1232 0.0104  -0.0060 -0.0106 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1382 0.1376 0.1304 0.0116  -0.0069 -0.0126 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.1741 0.1674 0.1556 0.0135  -0.0042 -0.0103 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2198 0.2113 0.2050 0.0104  -0.0006 -0.0082 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1097 0.1222 0.1283 0.0089  -0.0064 -0.0100 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1200 0.1339 0.1427 0.0086  -0.0037 -0.0074 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1143 0.1274 0.1321 0.0110  -0.0031 -0.0060 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1167 0.1303 0.1321 0.0132  -0.0056 -0.0070 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1461 0.1650 0.1807 0.0078  -0.0040 -0.0083 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.1909 0.2109 0.2329 0.0054  -0.0039 -0.0096 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2028 0.2273 0.2581 0.0045  -0.0029 -0.0097 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2040 0.2205 0.2431 0.0038  -0.0007 -0.0071 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1100 0.1216 0.1267 0.0108  0.0001  -0.0036 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1137 0.1241 0.1266 0.0130  0.0015  -0.0024 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1086 0.1195 0.1244 0.0127  0.0050  -0.0005 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1225 0.1336 0.1409 0.0109  0.0066  0.0004  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1431 0.1482 0.1465 0.0132  0.0022  -0.0018 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.0924 0.1035 0.1081 0.0149  0.0066  0.0003  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1029 0.1130 0.1188 0.0152  0.0108  0.0021  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1278 0.1323 0.1332 0.0149  0.0122  0.0025  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1420 0.1434 0.1417 0.0160  0.0114  0.0018  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1097 0.1222 0.1306 0.0177  0.0121  0.0025  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1235 0.1344 0.1436 0.0184  0.0174  0.0043  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1263 0.1452 0.1592 0.0176  0.0098  0.0015  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1240 0.1271 0.1272 0.0136  0.0140  0.0036  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.1329 0.1311 0.1266 0.0132  0.0145  0.0036  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.1340 0.1321 0.1267 0.0120  0.0157  0.0052  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.1455 0.1466 0.1448 0.0112  0.0160  0.0063  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.1317 0.1259 0.1160 0.0123  0.0166  0.0053  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.1258 0.1194 0.1071 0.0118  0.0174  0.0072  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.1172 0.1115 0.0999 0.0098  0.0141  0.0073  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.1270 0.1201 0.1079 0.0087  0.0112  0.0055  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.1443 0.1334 0.1148 0.0129  0.0183  0.0067  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.1408 0.1291 0.1068 0.0131  0.0187  0.0090  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.1501 0.1396 0.1185 0.0143  0.0227  0.0122  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.1470 0.1338 0.1074 0.0123  0.0155  0.0088  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.1587 0.1468 0.1215 0.0145  0.0221  0.0141  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.1659 0.1527 0.1239 0.0133  0.0173  0.0121  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.1246 0.1206 0.1108 0.0093  0.0150  0.0097  105 SER   A N   
785  C CA  . SER   A 99  ? 0.1283 0.1246 0.1156 0.0078  0.0125  0.0104  105 SER   A CA  
786  C C   . SER   A 99  ? 0.1500 0.1467 0.1379 0.0084  0.0147  0.0140  105 SER   A C   
787  O O   . SER   A 99  ? 0.1630 0.1607 0.1543 0.0094  0.0185  0.0158  105 SER   A O   
788  C CB  . SER   A 99  ? 0.1414 0.1401 0.1365 0.0063  0.0107  0.0090  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.1554 0.1570 0.1589 0.0061  0.0125  0.0098  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.1242 0.1200 0.1089 0.0081  0.0126  0.0151  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.1506 0.1464 0.1355 0.0090  0.0145  0.0191  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2088 0.2054 0.1969 0.0076  0.0111  0.0195  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2384 0.2354 0.2276 0.0062  0.0078  0.0168  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2210 0.2138 0.1948 0.0115  0.0164  0.0210  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2725 0.2628 0.2361 0.0118  0.0125  0.0186  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.1917 0.1786 0.1430 0.0145  0.0142  0.0197  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.2313 0.2174 0.1773 0.0159  0.0132  0.0226  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.1820 0.1668 0.1284 0.0154  0.0160  0.0175  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2461 0.2433 0.2382 0.0081  0.0128  0.0233  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2721 0.2700 0.2673 0.0072  0.0098  0.0241  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2403 0.2370 0.2263 0.0080  0.0056  0.0236  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2814 0.2761 0.2570 0.0100  0.0052  0.0247  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2873 0.2856 0.2888 0.0079  0.0130  0.0284  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2760 0.2738 0.2775 0.0091  0.0180  0.0300  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2398 0.2366 0.2330 0.0097  0.0176  0.0273  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.1752 0.1729 0.1654 0.0062  0.0024  0.0212  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.1747 0.1722 0.1616 0.0057  -0.0022 0.0192  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.1443 0.1413 0.1323 0.0040  -0.0029 0.0149  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.1629 0.1598 0.1518 0.0029  -0.0060 0.0129  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1358 0.1323 0.1238 0.0039  0.0000  0.0134  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1242 0.1197 0.1125 0.0029  -0.0004 0.0100  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1078 0.1044 0.1037 0.0014  -0.0003 0.0089  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1217 0.1171 0.1175 0.0008  -0.0007 0.0065  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1279 0.1227 0.1133 0.0039  0.0023  0.0090  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.1418 0.1342 0.1182 0.0053  0.0025  0.0088  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.1469 0.1379 0.1188 0.0050  -0.0005 0.0075  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.1349 0.1270 0.1092 0.0068  0.0057  0.0098  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1144 0.1126 0.1165 0.0011  0.0004  0.0107  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.0959 0.0946 0.1044 -0.0001 0.0008  0.0093  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1121 0.1098 0.1210 -0.0010 -0.0011 0.0081  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1291 0.1271 0.1374 -0.0010 -0.0033 0.0091  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1102 0.1102 0.1255 -0.0003 0.0020  0.0113  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1418 0.1429 0.1604 0.0001  0.0049  0.0118  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.0960 0.0926 0.1063 -0.0016 -0.0002 0.0060  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1028 0.0982 0.1149 -0.0024 -0.0009 0.0050  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1163 0.1095 0.1234 -0.0024 -0.0010 0.0032  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1279 0.1195 0.1370 -0.0031 -0.0006 0.0021  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1024 0.0951 0.1037 -0.0015 -0.0012 0.0028  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1022 0.0922 0.0991 -0.0012 -0.0009 0.0011  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1046 0.0930 0.1018 -0.0007 0.0013  0.0002  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1142 0.1037 0.1118 0.0000  0.0023  0.0004  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1089 0.0944 0.1056 -0.0010 0.0021  -0.0008 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1098 0.0931 0.1056 -0.0001 0.0046  -0.0010 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1081 0.0901 0.0984 0.0018  0.0054  -0.0014 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1157 0.0965 0.1033 0.0021  0.0051  -0.0019 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1369 0.1173 0.1357 -0.0011 0.0060  -0.0014 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1484 0.1303 0.1538 -0.0024 0.0061  -0.0007 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1590 0.1354 0.1545 0.0005  0.0092  -0.0012 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.1883 0.1679 0.1994 -0.0037 0.0076  -0.0010 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1041 0.0862 0.0930 0.0033  0.0064  -0.0012 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1073 0.0881 0.0916 0.0057  0.0070  -0.0012 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1212 0.0978 0.1032 0.0067  0.0095  -0.0008 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1203 0.0963 0.1032 0.0066  0.0105  -0.0007 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1119 0.0959 0.0963 0.0069  0.0058  -0.0016 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1287 0.1124 0.1092 0.0097  0.0057  -0.0016 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1433 0.1269 0.1228 0.0106  0.0059  -0.0012 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1433 0.1306 0.1254 0.0104  0.0036  -0.0027 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1174 0.0908 0.0966 0.0080  0.0109  -0.0004 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1288 0.0974 0.1056 0.0093  0.0140  0.0007  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1302 0.0971 0.1018 0.0126  0.0146  0.0016  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1435 0.1115 0.1147 0.0132  0.0135  0.0013  115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.1902 0.1553 0.1703 0.0075  0.0158  0.0005  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2760 0.2425 0.2624 0.0044  0.0150  -0.0004 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.2754 0.2387 0.2655 0.0028  0.0161  -0.0012 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3176 0.2765 0.3090 0.0035  0.0204  0.0003  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3026 0.2613 0.2996 0.0021  0.0221  0.0007  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.2536 0.2162 0.2564 -0.0004 0.0192  -0.0004 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.2312 0.1856 0.2281 0.0034  0.0269  0.0026  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1442 0.1080 0.1115 0.0150  0.0167  0.0031  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.1533 0.1142 0.1152 0.0187  0.0178  0.0048  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.1638 0.1181 0.1253 0.0191  0.0226  0.0067  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.1692 0.1220 0.1355 0.0163  0.0245  0.0062  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.1660 0.1283 0.1221 0.0219  0.0162  0.0053  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.1620 0.1208 0.1142 0.0225  0.0190  0.0060  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.1749 0.1253 0.1315 0.0227  0.0248  0.0090  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.1987 0.1421 0.1553 0.0233  0.0302  0.0113  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2085 0.1492 0.1640 0.0233  0.0335  0.0125  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2285 0.1638 0.1868 0.0228  0.0387  0.0142  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.2144 0.1539 0.1652 0.0280  0.0321  0.0142  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.2900 0.2299 0.2318 0.0324  0.0310  0.0162  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.3994 0.3371 0.3356 0.0373  0.0312  0.0190  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.4661 0.4085 0.4010 0.0392  0.0266  0.0183  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.3854 0.3158 0.3189 0.0397  0.0367  0.0226  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.1847 0.1287 0.1370 0.0237  0.0313  0.0116  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.1875 0.1286 0.1376 0.0242  0.0348  0.0126  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.1791 0.1224 0.1378 0.0199  0.0351  0.0107  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.1975 0.1379 0.1566 0.0199  0.0391  0.0117  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.1961 0.1384 0.1365 0.0276  0.0327  0.0125  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2149 0.1554 0.1465 0.0325  0.0317  0.0146  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.2246 0.1705 0.1546 0.0337  0.0258  0.0130  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.2509 0.1850 0.1758 0.0365  0.0361  0.0185  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.2533 0.1964 0.1760 0.0384  0.0262  0.0157  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.2668 0.2026 0.1860 0.0403  0.0323  0.0193  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.1511 0.0997 0.1161 0.0166  0.0308  0.0082  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.1481 0.0995 0.1212 0.0129  0.0301  0.0065  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1416 0.0995 0.1166 0.0112  0.0247  0.0042  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1483 0.1086 0.1202 0.0123  0.0215  0.0036  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1301 0.0905 0.1108 0.0089  0.0241  0.0033  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1288 0.0948 0.1121 0.0073  0.0197  0.0016  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1132 0.0808 0.0909 0.0094  0.0181  0.0008  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1403 0.1055 0.1144 0.0109  0.0203  0.0009  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1301 0.0979 0.1216 0.0045  0.0199  0.0012  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1447 0.1176 0.1384 0.0034  0.0160  0.0001  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1441 0.1113 0.1421 0.0023  0.0200  0.0013  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1209 0.0923 0.0981 0.0094  0.0144  -0.0002 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1231 0.0969 0.0969 0.0110  0.0120  -0.0015 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1307 0.1084 0.1103 0.0088  0.0102  -0.0030 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1378 0.1161 0.1162 0.0095  0.0095  -0.0045 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1331 0.1089 0.1046 0.0126  0.0096  -0.0015 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1542 0.1338 0.1250 0.0138  0.0062  -0.0033 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1435 0.1151 0.1090 0.0154  0.0116  0.0002  121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1135 0.0937 0.0989 0.0065  0.0092  -0.0026 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1169 0.1005 0.1079 0.0047  0.0077  -0.0032 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1009 0.0866 0.0964 0.0029  0.0067  -0.0021 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1126 0.0967 0.1070 0.0026  0.0071  -0.0014 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1001 0.0888 0.1003 0.0017  0.0055  -0.0020 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1039 0.0943 0.1070 0.0004  0.0045  -0.0006 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.0960 0.0894 0.1004 0.0006  0.0035  -0.0002 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.0989 0.0937 0.1057 0.0008  0.0035  -0.0012 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1168 0.1077 0.1255 -0.0010 0.0046  0.0004  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1269 0.1184 0.1396 -0.0012 0.0056  -0.0002 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1414 0.1298 0.1506 -0.0015 0.0057  0.0004  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1387 0.1309 0.1582 -0.0023 0.0059  0.0013  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.0891 0.0833 0.0923 0.0005  0.0028  0.0010  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.0856 0.0823 0.0906 0.0008  0.0029  0.0020  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.0827 0.0809 0.0939 -0.0001 0.0033  0.0029  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.0827 0.0805 0.0961 -0.0009 0.0030  0.0040  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.0889 0.0852 0.0902 0.0011  0.0027  0.0035  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1048 0.1032 0.1081 0.0017  0.0039  0.0052  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1076 0.1019 0.1032 0.0021  0.0028  0.0023  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.0862 0.0862 0.1014 0.0000  0.0039  0.0024  125 SER   A N   
922  C CA  . SER   A 119 ? 0.0918 0.0929 0.1140 -0.0009 0.0047  0.0031  125 SER   A CA  
923  C C   . SER   A 119 ? 0.0950 0.0981 0.1215 -0.0008 0.0060  0.0045  125 SER   A C   
924  O O   . SER   A 119 ? 0.0956 0.0991 0.1276 -0.0014 0.0073  0.0063  125 SER   A O   
925  C CB  . SER   A 119 ? 0.0954 0.0960 0.1199 -0.0013 0.0044  0.0000  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1048 0.1059 0.1365 -0.0023 0.0053  -0.0002 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1021 0.1064 0.1274 0.0000  0.0062  0.0040  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1069 0.1132 0.1378 0.0001  0.0083  0.0056  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1036 0.1100 0.1296 0.0016  0.0092  0.0066  126 THR   A C   
930  O O   . THR   A 120 ? 0.1047 0.1098 0.1238 0.0024  0.0078  0.0055  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1218 0.1304 0.1611 -0.0006 0.0078  0.0027  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.1346 0.1444 0.1712 0.0004  0.0060  0.0002  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1413 0.1493 0.1849 -0.0019 0.0069  0.0004  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1181 0.1258 0.1481 0.0021  0.0119  0.0087  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.1348 0.1428 0.1615 0.0036  0.0134  0.0092  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.1571 0.1661 0.1894 0.0042  0.0175  0.0120  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.1646 0.1745 0.2048 0.0031  0.0191  0.0133  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.1644 0.1730 0.1929 0.0058  0.0198  0.0131  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.1811 0.1897 0.2124 0.0070  0.0249  0.0165  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.1671 0.1775 0.2015 0.0082  0.0267  0.0156  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.1758 0.1887 0.2145 0.0078  0.0238  0.0124  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.1776 0.1866 0.2099 0.0101  0.0318  0.0186  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.1611 0.1717 0.1978 0.0116  0.0350  0.0185  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.1474 0.1588 0.1811 0.0122  0.0315  0.0151  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.1522 0.1671 0.1947 0.0128  0.0318  0.0139  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2198 0.2349 0.2733 0.0106  0.0373  0.0190  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3016 0.3151 0.3583 0.0102  0.0420  0.0230  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3266 0.3367 0.3761 0.0122  0.0469  0.0267  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3316 0.3470 0.3981 0.0080  0.0405  0.0224  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.1285 0.1362 0.1498 0.0127  0.0291  0.0141  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.1340 0.1413 0.1515 0.0135  0.0265  0.0114  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1199 0.1295 0.1410 0.0122  0.0212  0.0086  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.1432 0.1527 0.1622 0.0133  0.0193  0.0068  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1063 0.1172 0.1314 0.0102  0.0191  0.0083  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1008 0.1128 0.1272 0.0090  0.0145  0.0056  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1055 0.1142 0.1242 0.0078  0.0128  0.0056  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1203 0.1271 0.1360 0.0074  0.0145  0.0077  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1095 0.1256 0.1477 0.0076  0.0133  0.0044  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1523 0.1728 0.2006 0.0085  0.0138  0.0037  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.1736 0.1978 0.2352 0.0067  0.0138  0.0029  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1545 0.1764 0.2006 0.0101  0.0097  0.0011  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.0982 0.1062 0.1143 0.0075  0.0095  0.0034  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.0940 0.0994 0.1054 0.0063  0.0079  0.0031  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1002 0.1067 0.1145 0.0056  0.0052  0.0007  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1181 0.1257 0.1327 0.0069  0.0037  -0.0010 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1010 0.1026 0.1032 0.0068  0.0077  0.0031  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1204 0.1211 0.1197 0.0085  0.0072  0.0017  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1168 0.1164 0.1166 0.0054  0.0062  0.0028  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.0907 0.0970 0.1075 0.0040  0.0047  0.0005  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.0875 0.0941 0.1061 0.0036  0.0027  -0.0020 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.0918 0.0952 0.1053 0.0030  0.0023  -0.0021 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1067 0.1088 0.1195 0.0021  0.0033  -0.0003 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.0899 0.0919 0.0999 0.0038  0.0010  -0.0041 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1030 0.1016 0.1086 0.0035  0.0015  -0.0040 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1026 0.1006 0.1095 0.0032  0.0010  -0.0062 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1032 0.1021 0.1094 0.0043  -0.0006 -0.0085 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1061 0.1022 0.1047 0.0052  0.0015  -0.0040 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.0970 0.0930 0.0936 0.0059  0.0021  -0.0027 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.0988 0.0929 0.0937 0.0050  0.0030  -0.0014 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1154 0.1133 0.1122 0.0075  0.0015  -0.0029 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1061 0.0995 0.0982 0.0057  0.0036  -0.0007 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1204 0.1177 0.1152 0.0084  0.0026  -0.0018 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1223 0.1171 0.1142 0.0074  0.0038  -0.0009 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.0918 0.0881 0.1001 0.0020  0.0023  -0.0056 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1003 0.0950 0.1090 0.0019  0.0027  -0.0077 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1043 0.0954 0.1052 0.0036  0.0035  -0.0081 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1145 0.1035 0.1136 0.0034  0.0052  -0.0062 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.0997 0.0938 0.1137 0.0003  0.0044  -0.0064 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1006 0.0908 0.0969 0.0052  0.0025  -0.0105 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1231 0.1094 0.1109 0.0074  0.0037  -0.0104 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1259 0.1086 0.1133 0.0070  0.0070  -0.0102 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1301 0.1131 0.1219 0.0058  0.0074  -0.0118 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1520 0.1385 0.1343 0.0098  0.0011  -0.0131 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.1918 0.1740 0.1638 0.0128  0.0024  -0.0124 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.1869 0.1677 0.1565 0.0136  0.0038  -0.0098 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.2533 0.2329 0.2194 0.0144  0.0026  -0.0145 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1220 0.1010 0.1051 0.0080  0.0098  -0.0084 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1308 0.1060 0.1136 0.0079  0.0138  -0.0080 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1397 0.1100 0.1125 0.0110  0.0162  -0.0079 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1532 0.1197 0.1250 0.0115  0.0204  -0.0074 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1386 0.1136 0.1283 0.0059  0.0160  -0.0055 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1463 0.1258 0.1447 0.0034  0.0136  -0.0052 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1461 0.1198 0.1333 0.0064  0.0166  -0.0035 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1394 0.1095 0.1049 0.0134  0.0140  -0.0081 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1430 0.1080 0.0981 0.0169  0.0166  -0.0070 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.1735 0.1353 0.1213 0.0190  0.0177  -0.0092 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.1899 0.1463 0.1290 0.0219  0.0216  -0.0078 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1511 0.1172 0.1006 0.0194  0.0134  -0.0063 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.1560 0.1237 0.1108 0.0180  0.0135  -0.0039 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.1621 0.1309 0.1120 0.0208  0.0106  -0.0034 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.1564 0.1308 0.1098 0.0201  0.0056  -0.0060 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.1574 0.1350 0.1104 0.0218  0.0021  -0.0062 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.1689 0.1440 0.1164 0.0247  0.0030  -0.0037 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.1752 0.1582 0.1342 0.0205  -0.0018 -0.0085 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.1669 0.1315 0.1175 0.0178  0.0148  -0.0128 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.1874 0.1483 0.1304 0.0198  0.0157  -0.0159 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.1925 0.1500 0.1391 0.0185  0.0214  -0.0155 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2116 0.1649 0.1511 0.0204  0.0234  -0.0178 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2026 0.1675 0.1478 0.0190  0.0102  -0.0206 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2234 0.1925 0.1823 0.0149  0.0095  -0.0213 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2233 0.1951 0.1898 0.0128  0.0100  -0.0181 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.2510 0.2204 0.2129 0.0138  0.0086  -0.0250 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.1777 0.1366 0.1350 0.0157  0.0238  -0.0129 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.1723 0.1290 0.1356 0.0144  0.0288  -0.0124 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.1787 0.1299 0.1376 0.0163  0.0350  -0.0093 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.1720 0.1235 0.1378 0.0149  0.0374  -0.0061 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.1697 0.1311 0.1469 0.0107  0.0277  -0.0109 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.1724 0.1390 0.1552 0.0087  0.0224  -0.0132 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.1781 0.1489 0.1726 0.0058  0.0214  -0.0107 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.1893 0.1548 0.1715 0.0089  0.0223  -0.0171 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.1773 0.1231 0.1235 0.0199  0.0376  -0.0103 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.1960 0.1356 0.1358 0.0226  0.0441  -0.0069 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2090 0.1464 0.1582 0.0210  0.0509  -0.0048 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2233 0.1576 0.1743 0.0216  0.0560  -0.0011 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2080 0.1418 0.1306 0.0273  0.0455  -0.0083 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.2294 0.1656 0.1426 0.0293  0.0382  -0.0108 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.2587 0.1884 0.1533 0.0348  0.0400  -0.0114 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.2324 0.1725 0.1489 0.0288  0.0346  -0.0079 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2142 0.1531 0.1705 0.0192  0.0512  -0.0072 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2171 0.1546 0.1840 0.0179  0.0573  -0.0055 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2217 0.1637 0.2033 0.0145  0.0566  -0.0024 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2422 0.1831 0.2335 0.0136  0.0619  -0.0003 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2144 0.1525 0.1854 0.0170  0.0573  -0.0089 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2018 0.1463 0.1793 0.0142  0.0499  -0.0112 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2047 0.1506 0.1756 0.0146  0.0445  -0.0150 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.1971 0.1475 0.1896 0.0108  0.0474  -0.0095 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2060 0.1580 0.1875 0.0116  0.0396  -0.0156 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.1998 0.1543 0.1936 0.0094  0.0413  -0.0121 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.1988 0.1511 0.2039 0.0089  0.0497  -0.0063 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.1906 0.1506 0.1966 0.0065  0.0381  -0.0109 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.1882 0.1465 0.2050 0.0061  0.0455  -0.0055 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.1877 0.1493 0.2042 0.0051  0.0402  -0.0076 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2094 0.1564 0.1933 0.0128  0.0503  -0.0022 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2172 0.1681 0.2138 0.0098  0.0491  0.0001  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.2587 0.2057 0.2569 0.0104  0.0547  0.0032  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.2707 0.2198 0.2815 0.0080  0.0556  0.0048  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2068 0.1625 0.2029 0.0084  0.0421  -0.0003 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.1909 0.1516 0.1901 0.0069  0.0366  -0.0025 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2058 0.1702 0.2028 0.0062  0.0309  -0.0027 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.1856 0.1498 0.1987 0.0042  0.0365  -0.0016 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3039 0.2450 0.2894 0.0139  0.0584  0.0041  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.3532 0.2892 0.3385 0.0151  0.0649  0.0075  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4043 0.3357 0.3929 0.0162  0.0733  0.0087  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.4466 0.3726 0.4338 0.0179  0.0801  0.0118  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4058 0.3368 0.3746 0.0192  0.0657  0.0083  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.4977 0.4321 0.4615 0.0192  0.0586  0.0075  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5304 0.4695 0.5039 0.0160  0.0547  0.0074  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.5632 0.4954 0.5131 0.0226  0.0570  0.0069  144 ASP   A OD2 
1069 N N   . SER   B 1   ? 0.2585 0.2310 0.2467 0.0014  -0.0234 -0.0097 7   SER   C N   
1070 C CA  . SER   B 1   ? 0.2532 0.2300 0.2513 0.0020  -0.0243 -0.0099 7   SER   C CA  
1071 C C   . SER   B 1   ? 0.2337 0.2133 0.2358 0.0027  -0.0228 -0.0088 7   SER   C C   
1072 O O   . SER   B 1   ? 0.2462 0.2237 0.2435 0.0029  -0.0225 -0.0078 7   SER   C O   
1073 C CB  . SER   B 1   ? 0.2839 0.2594 0.2844 0.0021  -0.0297 -0.0107 7   SER   C CB  
1074 O OG  . SER   B 1   ? 0.3493 0.3216 0.3456 0.0026  -0.0330 -0.0097 7   SER   C OG  
1075 N N   . GLY   B 2   ? 0.2006 0.1844 0.2111 0.0030  -0.0217 -0.0092 8   GLY   C N   
1076 C CA  . GLY   B 2   ? 0.1821 0.1682 0.1966 0.0036  -0.0201 -0.0088 8   GLY   C CA  
1077 C C   . GLY   B 2   ? 0.1611 0.1515 0.1818 0.0031  -0.0166 -0.0092 8   GLY   C C   
1078 O O   . GLY   B 2   ? 0.1848 0.1760 0.2052 0.0023  -0.0149 -0.0092 8   GLY   C O   
1079 N N   . ALA   B 3   ? 0.1443 0.1371 0.1704 0.0035  -0.0155 -0.0096 9   ALA   C N   
1080 C CA  . ALA   B 3   ? 0.1462 0.1424 0.1772 0.0027  -0.0118 -0.0100 9   ALA   C CA  
1081 C C   . ALA   B 3   ? 0.1381 0.1354 0.1701 0.0029  -0.0094 -0.0102 9   ALA   C C   
1082 O O   . ALA   B 3   ? 0.1643 0.1599 0.1956 0.0040  -0.0110 -0.0103 9   ALA   C O   
1083 C CB  . ALA   B 3   ? 0.1549 0.1537 0.1948 0.0025  -0.0128 -0.0114 9   ALA   C CB  
1084 N N   . ILE   B 4   ? 0.1224 0.1217 0.1552 0.0017  -0.0055 -0.0103 10  ILE   C N   
1085 C CA  . ILE   B 4   ? 0.1174 0.1176 0.1512 0.0015  -0.0025 -0.0111 10  ILE   C CA  
1086 C C   . ILE   B 4   ? 0.1284 0.1316 0.1708 0.0011  -0.0005 -0.0128 10  ILE   C C   
1087 O O   . ILE   B 4   ? 0.1270 0.1316 0.1718 -0.0001 0.0006  -0.0127 10  ILE   C O   
1088 C CB  . ILE   B 4   ? 0.1196 0.1195 0.1472 -0.0001 0.0004  -0.0100 10  ILE   C CB  
1089 C CG1 . ILE   B 4   ? 0.1298 0.1276 0.1506 0.0002  -0.0014 -0.0084 10  ILE   C CG1 
1090 C CG2 . ILE   B 4   ? 0.1327 0.1329 0.1601 -0.0007 0.0034  -0.0111 10  ILE   C CG2 
1091 C CD1 . ILE   B 4   ? 0.1511 0.1492 0.1673 -0.0012 0.0004  -0.0070 10  ILE   C CD1 
1092 N N   . TYR   B 5   ? 0.1379 0.1419 0.1856 0.0021  0.0003  -0.0145 11  TYR   C N   
1093 C CA  . TYR   B 5   ? 0.1431 0.1504 0.2003 0.0019  0.0028  -0.0166 11  TYR   C CA  
1094 C C   . TYR   B 5   ? 0.1330 0.1404 0.1888 0.0009  0.0078  -0.0179 11  TYR   C C   
1095 O O   . TYR   B 5   ? 0.1467 0.1525 0.2018 0.0022  0.0076  -0.0187 11  TYR   C O   
1096 C CB  . TYR   B 5   ? 0.1560 0.1642 0.2222 0.0042  -0.0009 -0.0179 11  TYR   C CB  
1097 C CG  . TYR   B 5   ? 0.1430 0.1508 0.2101 0.0046  -0.0060 -0.0169 11  TYR   C CG  
1098 C CD1 . TYR   B 5   ? 0.1613 0.1721 0.2350 0.0036  -0.0059 -0.0176 11  TYR   C CD1 
1099 C CD2 . TYR   B 5   ? 0.1670 0.1712 0.2273 0.0057  -0.0105 -0.0153 11  TYR   C CD2 
1100 C CE1 . TYR   B 5   ? 0.1951 0.2051 0.2688 0.0037  -0.0107 -0.0169 11  TYR   C CE1 
1101 C CE2 . TYR   B 5   ? 0.1864 0.1896 0.2461 0.0058  -0.0150 -0.0146 11  TYR   C CE2 
1102 C CZ  . TYR   B 5   ? 0.2091 0.2152 0.2755 0.0049  -0.0153 -0.0155 11  TYR   C CZ  
1103 O OH  . TYR   B 5   ? 0.2578 0.2623 0.3225 0.0047  -0.0197 -0.0151 11  TYR   C OH  
1104 N N   . VAL   B 6   ? 0.1470 0.1555 0.2015 -0.0014 0.0123  -0.0182 12  VAL   C N   
1105 C CA  . VAL   B 6   ? 0.1641 0.1720 0.2150 -0.0029 0.0173  -0.0194 12  VAL   C CA  
1106 C C   . VAL   B 6   ? 0.1663 0.1768 0.2229 -0.0047 0.0223  -0.0211 12  VAL   C C   
1107 O O   . VAL   B 6   ? 0.1640 0.1753 0.2206 -0.0063 0.0227  -0.0198 12  VAL   C O   
1108 C CB  . VAL   B 6   ? 0.2026 0.2075 0.2411 -0.0045 0.0175  -0.0173 12  VAL   C CB  
1109 C CG1 . VAL   B 6   ? 0.2224 0.2272 0.2574 -0.0058 0.0166  -0.0147 12  VAL   C CG1 
1110 C CG2 . VAL   B 6   ? 0.2174 0.2212 0.2515 -0.0064 0.0225  -0.0188 12  VAL   C CG2 
1111 N N   . GLY   B 7   ? 0.1881 0.2001 0.2512 -0.0045 0.0262  -0.0242 13  GLY   C N   
1112 C CA  . GLY   B 7   ? 0.2072 0.2220 0.2768 -0.0065 0.0318  -0.0262 13  GLY   C CA  
1113 C C   . GLY   B 7   ? 0.2053 0.2237 0.2850 -0.0061 0.0295  -0.0260 13  GLY   C C   
1114 O O   . GLY   B 7   ? 0.2096 0.2293 0.2961 -0.0034 0.0243  -0.0260 13  GLY   C O   
1115 N N   . ASN   B 8   ? 0.1933 0.2125 0.2727 -0.0089 0.0325  -0.0252 14  ASN   C N   
1116 C CA  . ASN   B 8   ? 0.1943 0.2166 0.2830 -0.0090 0.0301  -0.0250 14  ASN   C CA  
1117 C C   . ASN   B 8   ? 0.1714 0.1909 0.2521 -0.0095 0.0258  -0.0216 14  ASN   C C   
1118 O O   . ASN   B 8   ? 0.1731 0.1936 0.2573 -0.0110 0.0257  -0.0209 14  ASN   C O   
1119 C CB  . ASN   B 8   ? 0.2387 0.2642 0.3356 -0.0117 0.0362  -0.0269 14  ASN   C CB  
1120 C CG  . ASN   B 8   ? 0.3346 0.3641 0.4435 -0.0104 0.0396  -0.0309 14  ASN   C CG  
1121 O OD1 . ASN   B 8   ? 0.3624 0.3950 0.4829 -0.0076 0.0355  -0.0323 14  ASN   C OD1 
1122 N ND2 . ASN   B 8   ? 0.3576 0.3863 0.4634 -0.0124 0.0469  -0.0327 14  ASN   C ND2 
1123 N N   . TYR   B 9   ? 0.1534 0.1695 0.2246 -0.0080 0.0222  -0.0197 15  TYR   C N   
1124 C CA  . TYR   B 9   ? 0.1401 0.1536 0.2042 -0.0082 0.0185  -0.0168 15  TYR   C CA  
1125 C C   . TYR   B 9   ? 0.1280 0.1405 0.1912 -0.0054 0.0124  -0.0162 15  TYR   C C   
1126 O O   . TYR   B 9   ? 0.1405 0.1527 0.2036 -0.0035 0.0112  -0.0170 15  TYR   C O   
1127 C CB  . TYR   B 9   ? 0.1575 0.1675 0.2092 -0.0096 0.0203  -0.0146 15  TYR   C CB  
1128 C CG  . TYR   B 9   ? 0.1678 0.1772 0.2166 -0.0128 0.0259  -0.0143 15  TYR   C CG  
1129 C CD1 . TYR   B 9   ? 0.1814 0.1913 0.2339 -0.0149 0.0275  -0.0138 15  TYR   C CD1 
1130 C CD2 . TYR   B 9   ? 0.1787 0.1863 0.2203 -0.0142 0.0295  -0.0147 15  TYR   C CD2 
1131 C CE1 . TYR   B 9   ? 0.2061 0.2146 0.2550 -0.0182 0.0330  -0.0133 15  TYR   C CE1 
1132 C CE2 . TYR   B 9   ? 0.2018 0.2079 0.2389 -0.0175 0.0347  -0.0143 15  TYR   C CE2 
1133 C CZ  . TYR   B 9   ? 0.2235 0.2300 0.2641 -0.0196 0.0365  -0.0134 15  TYR   C CZ  
1134 O OH  . TYR   B 9   ? 0.2644 0.2685 0.2993 -0.0233 0.0416  -0.0126 15  TYR   C OH  
1135 N N   . ARG   B 10  ? 0.1071 0.1185 0.1688 -0.0053 0.0089  -0.0147 16  ARG   C N   
1136 C CA  . ARG   B 10  ? 0.1230 0.1324 0.1815 -0.0032 0.0035  -0.0140 16  ARG   C CA  
1137 C C   . ARG   B 10  ? 0.1134 0.1198 0.1628 -0.0039 0.0032  -0.0116 16  ARG   C C   
1138 O O   . ARG   B 10  ? 0.1182 0.1242 0.1676 -0.0055 0.0043  -0.0108 16  ARG   C O   
1139 C CB  . ARG   B 10  ? 0.1392 0.1500 0.2054 -0.0026 -0.0003 -0.0150 16  ARG   C CB  
1140 C CG  . ARG   B 10  ? 0.1449 0.1528 0.2062 -0.0014 -0.0055 -0.0141 16  ARG   C CG  
1141 C CD  . ARG   B 10  ? 0.1474 0.1563 0.2158 -0.0009 -0.0100 -0.0154 16  ARG   C CD  
1142 N NE  . ARG   B 10  ? 0.1663 0.1723 0.2299 -0.0013 -0.0132 -0.0148 16  ARG   C NE  
1143 C CZ  . ARG   B 10  ? 0.2225 0.2253 0.2805 -0.0001 -0.0175 -0.0145 16  ARG   C CZ  
1144 N NH1 . ARG   B 10  ? 0.2272 0.2289 0.2829 0.0015  -0.0195 -0.0142 16  ARG   C NH1 
1145 N NH2 . ARG   B 10  ? 0.2134 0.2133 0.2670 -0.0008 -0.0195 -0.0145 16  ARG   C NH2 
1146 N N   . VAL   B 11  ? 0.1149 0.1192 0.1570 -0.0029 0.0019  -0.0106 17  VAL   C N   
1147 C CA  . VAL   B 11  ? 0.1086 0.1106 0.1434 -0.0032 0.0015  -0.0086 17  VAL   C CA  
1148 C C   . VAL   B 11  ? 0.1041 0.1044 0.1370 -0.0017 -0.0024 -0.0085 17  VAL   C C   
1149 O O   . VAL   B 11  ? 0.1207 0.1203 0.1523 -0.0004 -0.0044 -0.0089 17  VAL   C O   
1150 C CB  . VAL   B 11  ? 0.1330 0.1342 0.1613 -0.0033 0.0031  -0.0076 17  VAL   C CB  
1151 C CG1 . VAL   B 11  ? 0.1426 0.1421 0.1653 -0.0037 0.0027  -0.0055 17  VAL   C CG1 
1152 C CG2 . VAL   B 11  ? 0.1369 0.1392 0.1659 -0.0048 0.0069  -0.0082 17  VAL   C CG2 
1153 N N   . VAL   B 12  ? 0.0995 0.0984 0.1315 -0.0020 -0.0033 -0.0079 18  VAL   C N   
1154 C CA  . VAL   B 12  ? 0.1109 0.1076 0.1401 -0.0010 -0.0065 -0.0082 18  VAL   C CA  
1155 C C   . VAL   B 12  ? 0.0962 0.0909 0.1208 -0.0010 -0.0058 -0.0070 18  VAL   C C   
1156 O O   . VAL   B 12  ? 0.1054 0.1003 0.1302 -0.0019 -0.0037 -0.0058 18  VAL   C O   
1157 C CB  . VAL   B 12  ? 0.1450 0.1416 0.1792 -0.0012 -0.0090 -0.0097 18  VAL   C CB  
1158 C CG1 . VAL   B 12  ? 0.2008 0.1994 0.2404 -0.0006 -0.0107 -0.0109 18  VAL   C CG1 
1159 C CG2 . VAL   B 12  ? 0.1346 0.1318 0.1729 -0.0028 -0.0073 -0.0096 18  VAL   C CG2 
1160 N N   . ASN   B 13  ? 0.0971 0.0896 0.1179 -0.0002 -0.0075 -0.0074 19  ASN   C N   
1161 C CA  . ASN   B 13  ? 0.1099 0.1006 0.1282 0.0000  -0.0068 -0.0068 19  ASN   C CA  
1162 C C   . ASN   B 13  ? 0.1138 0.1036 0.1359 -0.0008 -0.0070 -0.0073 19  ASN   C C   
1163 O O   . ASN   B 13  ? 0.1141 0.1033 0.1386 -0.0012 -0.0089 -0.0088 19  ASN   C O   
1164 C CB  . ASN   B 13  ? 0.1134 0.1016 0.1272 0.0008  -0.0081 -0.0078 19  ASN   C CB  
1165 C CG  . ASN   B 13  ? 0.1283 0.1168 0.1381 0.0013  -0.0077 -0.0072 19  ASN   C CG  
1166 O OD1 . ASN   B 13  ? 0.1340 0.1221 0.1425 0.0014  -0.0091 -0.0076 19  ASN   C OD1 
1167 N ND2 . ASN   B 13  ? 0.1287 0.1178 0.1371 0.0015  -0.0058 -0.0063 19  ASN   C ND2 
1168 N N   . ARG   B 14  ? 0.1055 0.0947 0.1281 -0.0012 -0.0053 -0.0059 20  ARG   C N   
1169 C CA  . ARG   B 14  ? 0.1057 0.0933 0.1316 -0.0022 -0.0052 -0.0062 20  ARG   C CA  
1170 C C   . ARG   B 14  ? 0.1164 0.1012 0.1418 -0.0019 -0.0072 -0.0082 20  ARG   C C   
1171 O O   . ARG   B 14  ? 0.1201 0.1042 0.1490 -0.0031 -0.0083 -0.0095 20  ARG   C O   
1172 C CB  . ARG   B 14  ? 0.1100 0.0962 0.1356 -0.0025 -0.0035 -0.0040 20  ARG   C CB  
1173 C CG  . ARG   B 14  ? 0.1026 0.0868 0.1317 -0.0040 -0.0030 -0.0036 20  ARG   C CG  
1174 C CD  . ARG   B 14  ? 0.1331 0.1149 0.1607 -0.0037 -0.0021 -0.0011 20  ARG   C CD  
1175 N NE  . ARG   B 14  ? 0.1341 0.1130 0.1642 -0.0054 -0.0013 -0.0001 20  ARG   C NE  
1176 C CZ  . ARG   B 14  ? 0.1478 0.1232 0.1798 -0.0053 -0.0020 -0.0011 20  ARG   C CZ  
1177 N NH1 . ARG   B 14  ? 0.1724 0.1469 0.2039 -0.0038 -0.0034 -0.0036 20  ARG   C NH1 
1178 N NH2 . ARG   B 14  ? 0.1574 0.1297 0.1914 -0.0069 -0.0012 0.0002  20  ARG   C NH2 
1179 N N   . HIS   B 15  ? 0.1040 0.0871 0.1250 -0.0006 -0.0075 -0.0089 21  HIS   C N   
1180 C CA  . HIS   B 15  ? 0.1210 0.1006 0.1400 -0.0006 -0.0089 -0.0112 21  HIS   C CA  
1181 C C   . HIS   B 15  ? 0.1323 0.1118 0.1506 -0.0012 -0.0119 -0.0129 21  HIS   C C   
1182 O O   . HIS   B 15  ? 0.1477 0.1240 0.1643 -0.0017 -0.0137 -0.0150 21  HIS   C O   
1183 C CB  . HIS   B 15  ? 0.1373 0.1149 0.1519 0.0007  -0.0076 -0.0117 21  HIS   C CB  
1184 C CG  . HIS   B 15  ? 0.1281 0.1066 0.1380 0.0013  -0.0076 -0.0118 21  HIS   C CG  
1185 N ND1 . HIS   B 15  ? 0.1297 0.1111 0.1394 0.0018  -0.0063 -0.0099 21  HIS   C ND1 
1186 C CD2 . HIS   B 15  ? 0.1393 0.1152 0.1437 0.0011  -0.0088 -0.0135 21  HIS   C CD2 
1187 C CE1 . HIS   B 15  ? 0.1354 0.1162 0.1404 0.0020  -0.0065 -0.0106 21  HIS   C CE1 
1188 N NE2 . HIS   B 15  ? 0.1493 0.1266 0.1504 0.0016  -0.0079 -0.0126 21  HIS   C NE2 
1189 N N   . LEU   B 16  ? 0.1209 0.1033 0.1403 -0.0011 -0.0127 -0.0122 22  LEU   C N   
1190 C CA  . LEU   B 16  ? 0.1353 0.1177 0.1550 -0.0014 -0.0163 -0.0135 22  LEU   C CA  
1191 C C   . LEU   B 16  ? 0.1411 0.1266 0.1689 -0.0023 -0.0172 -0.0137 22  LEU   C C   
1192 O O   . LEU   B 16  ? 0.1492 0.1355 0.1794 -0.0023 -0.0204 -0.0146 22  LEU   C O   
1193 C CB  . LEU   B 16  ? 0.1419 0.1245 0.1571 -0.0004 -0.0169 -0.0128 22  LEU   C CB  
1194 C CG  . LEU   B 16  ? 0.1609 0.1404 0.1681 0.0001  -0.0157 -0.0129 22  LEU   C CG  
1195 C CD1 . LEU   B 16  ? 0.1789 0.1584 0.1819 0.0007  -0.0161 -0.0119 22  LEU   C CD1 
1196 C CD2 . LEU   B 16  ? 0.1711 0.1459 0.1734 -0.0005 -0.0177 -0.0150 22  LEU   C CD2 
1197 N N   . ALA   B 17  ? 0.1292 0.1165 0.1617 -0.0032 -0.0143 -0.0127 23  ALA   C N   
1198 C CA  . ALA   B 17  ? 0.1347 0.1253 0.1753 -0.0044 -0.0141 -0.0131 23  ALA   C CA  
1199 C C   . ALA   B 17  ? 0.1384 0.1283 0.1833 -0.0055 -0.0175 -0.0151 23  ALA   C C   
1200 O O   . ALA   B 17  ? 0.1493 0.1356 0.1913 -0.0059 -0.0186 -0.0161 23  ALA   C O   
1201 C CB  . ALA   B 17  ? 0.1310 0.1223 0.1738 -0.0056 -0.0102 -0.0115 23  ALA   C CB  
1202 N N   . THR   B 18  ? 0.1448 0.1383 0.1971 -0.0058 -0.0191 -0.0160 24  THR   C N   
1203 C CA  . THR   B 18  ? 0.1417 0.1354 0.1996 -0.0070 -0.0231 -0.0180 24  THR   C CA  
1204 C C   . THR   B 18  ? 0.1455 0.1409 0.2115 -0.0093 -0.0208 -0.0185 24  THR   C C   
1205 O O   . THR   B 18  ? 0.1416 0.1382 0.2089 -0.0100 -0.0162 -0.0170 24  THR   C O   
1206 C CB  . THR   B 18  ? 0.1704 0.1675 0.2338 -0.0060 -0.0265 -0.0187 24  THR   C CB  
1207 O OG1 . THR   B 18  ? 0.1769 0.1787 0.2484 -0.0063 -0.0228 -0.0184 24  THR   C OG1 
1208 C CG2 . THR   B 18  ? 0.1943 0.1890 0.2496 -0.0039 -0.0288 -0.0180 24  THR   C CG2 
1209 N N   . HIS   B 19  ? 0.1559 0.1515 0.2278 -0.0108 -0.0243 -0.0205 25  HIS   C N   
1210 C CA  . HIS   B 19  ? 0.1578 0.1555 0.2387 -0.0134 -0.0221 -0.0210 25  HIS   C CA  
1211 C C   . HIS   B 19  ? 0.1363 0.1398 0.2256 -0.0137 -0.0184 -0.0204 25  HIS   C C   
1212 O O   . HIS   B 19  ? 0.1551 0.1593 0.2472 -0.0156 -0.0136 -0.0195 25  HIS   C O   
1213 C CB  . HIS   B 19  ? 0.1961 0.1942 0.2836 -0.0150 -0.0272 -0.0236 25  HIS   C CB  
1214 C CG  . HIS   B 19  ? 0.2964 0.2885 0.3762 -0.0153 -0.0306 -0.0248 25  HIS   C CG  
1215 N ND1 . HIS   B 19  ? 0.3540 0.3414 0.4287 -0.0162 -0.0276 -0.0243 25  HIS   C ND1 
1216 C CD2 . HIS   B 19  ? 0.3435 0.3335 0.4203 -0.0151 -0.0367 -0.0266 25  HIS   C CD2 
1217 C CE1 . HIS   B 19  ? 0.3661 0.3488 0.4351 -0.0164 -0.0315 -0.0263 25  HIS   C CE1 
1218 N NE2 . HIS   B 19  ? 0.3702 0.3540 0.4393 -0.0159 -0.0370 -0.0277 25  HIS   C NE2 
1219 N N   . ASN   B 20  ? 0.1348 0.1417 0.2274 -0.0119 -0.0205 -0.0210 26  ASN   C N   
1220 C CA  . ASN   B 20  ? 0.1405 0.1527 0.2413 -0.0120 -0.0167 -0.0210 26  ASN   C CA  
1221 C C   . ASN   B 20  ? 0.1364 0.1475 0.2304 -0.0118 -0.0109 -0.0189 26  ASN   C C   
1222 O O   . ASN   B 20  ? 0.1347 0.1483 0.2333 -0.0135 -0.0058 -0.0187 26  ASN   C O   
1223 C CB  . ASN   B 20  ? 0.1651 0.1805 0.2711 -0.0098 -0.0204 -0.0221 26  ASN   C CB  
1224 C CG  . ASN   B 20  ? 0.2391 0.2602 0.3556 -0.0098 -0.0164 -0.0229 26  ASN   C CG  
1225 O OD1 . ASN   B 20  ? 0.2593 0.2845 0.3874 -0.0118 -0.0149 -0.0244 26  ASN   C OD1 
1226 N ND2 . ASN   B 20  ? 0.2597 0.2811 0.3725 -0.0078 -0.0143 -0.0221 26  ASN   C ND2 
1227 N N   . ASP   B 21  ? 0.1245 0.1317 0.2070 -0.0100 -0.0115 -0.0173 27  ASP   C N   
1228 C CA  . ASP   B 21  ? 0.1317 0.1378 0.2077 -0.0100 -0.0067 -0.0153 27  ASP   C CA  
1229 C C   . ASP   B 21  ? 0.1272 0.1314 0.2025 -0.0125 -0.0030 -0.0140 27  ASP   C C   
1230 O O   . ASP   B 21  ? 0.1533 0.1583 0.2287 -0.0138 0.0017  -0.0129 27  ASP   C O   
1231 C CB  . ASP   B 21  ? 0.1298 0.1322 0.1950 -0.0080 -0.0084 -0.0140 27  ASP   C CB  
1232 C CG  . ASP   B 21  ? 0.1482 0.1515 0.2117 -0.0057 -0.0108 -0.0144 27  ASP   C CG  
1233 O OD1 . ASP   B 21  ? 0.1570 0.1635 0.2254 -0.0054 -0.0092 -0.0149 27  ASP   C OD1 
1234 O OD2 . ASP   B 21  ? 0.1533 0.1536 0.2105 -0.0044 -0.0141 -0.0143 27  ASP   C OD2 
1235 N N   . TRP   B 22  ? 0.1347 0.1356 0.2089 -0.0133 -0.0051 -0.0142 28  TRP   C N   
1236 C CA  . TRP   B 22  ? 0.1408 0.1389 0.2143 -0.0156 -0.0020 -0.0128 28  TRP   C CA  
1237 C C   . TRP   B 22  ? 0.1576 0.1588 0.2407 -0.0186 0.0010  -0.0136 28  TRP   C C   
1238 O O   . TRP   B 22  ? 0.1696 0.1692 0.2513 -0.0207 0.0053  -0.0118 28  TRP   C O   
1239 C CB  . TRP   B 22  ? 0.1431 0.1365 0.2136 -0.0155 -0.0051 -0.0132 28  TRP   C CB  
1240 C CG  . TRP   B 22  ? 0.1201 0.1096 0.1809 -0.0134 -0.0053 -0.0117 28  TRP   C CG  
1241 C CD1 . TRP   B 22  ? 0.1427 0.1309 0.1984 -0.0112 -0.0084 -0.0126 28  TRP   C CD1 
1242 C CD2 . TRP   B 22  ? 0.1294 0.1158 0.1851 -0.0135 -0.0025 -0.0090 28  TRP   C CD2 
1243 N NE1 . TRP   B 22  ? 0.1507 0.1358 0.1994 -0.0098 -0.0072 -0.0108 28  TRP   C NE1 
1244 C CE2 . TRP   B 22  ? 0.1350 0.1192 0.1840 -0.0111 -0.0039 -0.0085 28  TRP   C CE2 
1245 C CE3 . TRP   B 22  ? 0.1513 0.1364 0.2074 -0.0156 0.0011  -0.0067 28  TRP   C CE3 
1246 C CZ2 . TRP   B 22  ? 0.1402 0.1212 0.1842 -0.0103 -0.0024 -0.0060 28  TRP   C CZ2 
1247 C CZ3 . TRP   B 22  ? 0.1673 0.1488 0.2171 -0.0149 0.0023  -0.0039 28  TRP   C CZ3 
1248 C CH2 . TRP   B 22  ? 0.1590 0.1389 0.2035 -0.0121 0.0003  -0.0036 28  TRP   C CH2 
1249 N N   . ALA   B 23  ? 0.1474 0.1530 0.2401 -0.0188 -0.0010 -0.0161 29  ALA   C N   
1250 C CA  . ALA   B 23  ? 0.1603 0.1697 0.2639 -0.0218 0.0022  -0.0172 29  ALA   C CA  
1251 C C   . ALA   B 23  ? 0.1717 0.1845 0.2767 -0.0221 0.0077  -0.0168 29  ALA   C C   
1252 O O   . ALA   B 23  ? 0.1825 0.1981 0.2951 -0.0249 0.0121  -0.0175 29  ALA   C O   
1253 C CB  . ALA   B 23  ? 0.1575 0.1711 0.2721 -0.0216 -0.0023 -0.0202 29  ALA   C CB  
1254 N N   . ASN   B 24  ? 0.1487 0.1617 0.2476 -0.0194 0.0073  -0.0162 30  ASN   C N   
1255 C CA  . ASN   B 24  ? 0.1404 0.1559 0.2394 -0.0195 0.0123  -0.0162 30  ASN   C CA  
1256 C C   . ASN   B 24  ? 0.1415 0.1527 0.2272 -0.0189 0.0141  -0.0134 30  ASN   C C   
1257 O O   . ASN   B 24  ? 0.1375 0.1495 0.2196 -0.0175 0.0154  -0.0134 30  ASN   C O   
1258 C CB  . ASN   B 24  ? 0.1458 0.1658 0.2513 -0.0168 0.0098  -0.0185 30  ASN   C CB  
1259 C CG  . ASN   B 24  ? 0.1916 0.2166 0.3119 -0.0176 0.0083  -0.0212 30  ASN   C CG  
1260 O OD1 . ASN   B 24  ? 0.1893 0.2180 0.3183 -0.0198 0.0133  -0.0225 30  ASN   C OD1 
1261 N ND2 . ASN   B 24  ? 0.1770 0.2020 0.3002 -0.0162 0.0016  -0.0221 30  ASN   C ND2 
1262 N N   . LEU   B 25  ? 0.1523 0.1588 0.2315 -0.0200 0.0140  -0.0112 31  LEU   C N   
1263 C CA  . LEU   B 25  ? 0.1486 0.1509 0.2162 -0.0193 0.0145  -0.0083 31  LEU   C CA  
1264 C C   . LEU   B 25  ? 0.1581 0.1600 0.2208 -0.0210 0.0198  -0.0070 31  LEU   C C   
1265 O O   . LEU   B 25  ? 0.1888 0.1904 0.2537 -0.0242 0.0241  -0.0067 31  LEU   C O   
1266 C CB  . LEU   B 25  ? 0.1442 0.1416 0.2082 -0.0201 0.0131  -0.0064 31  LEU   C CB  
1267 C CG  . LEU   B 25  ? 0.1674 0.1603 0.2207 -0.0192 0.0131  -0.0033 31  LEU   C CG  
1268 C CD1 . LEU   B 25  ? 0.1715 0.1650 0.2207 -0.0157 0.0095  -0.0037 31  LEU   C CD1 
1269 C CD2 . LEU   B 25  ? 0.1735 0.1614 0.2249 -0.0201 0.0122  -0.0014 31  LEU   C CD2 
1270 N N   . VAL   B 26  ? 0.1485 0.1497 0.2036 -0.0193 0.0195  -0.0061 32  VAL   C N   
1271 C CA  . VAL   B 26  ? 0.1578 0.1576 0.2060 -0.0211 0.0238  -0.0047 32  VAL   C CA  
1272 C C   . VAL   B 26  ? 0.1749 0.1696 0.2127 -0.0210 0.0222  -0.0012 32  VAL   C C   
1273 O O   . VAL   B 26  ? 0.2021 0.1934 0.2344 -0.0236 0.0250  0.0012  32  VAL   C O   
1274 C CB  . VAL   B 26  ? 0.1666 0.1692 0.2142 -0.0194 0.0245  -0.0066 32  VAL   C CB  
1275 C CG1 . VAL   B 26  ? 0.1943 0.1944 0.2324 -0.0212 0.0282  -0.0052 32  VAL   C CG1 
1276 C CG2 . VAL   B 26  ? 0.1748 0.1823 0.2339 -0.0194 0.0263  -0.0101 32  VAL   C CG2 
1277 N N   . TRP   B 27  ? 0.1456 0.1397 0.1808 -0.0180 0.0177  -0.0007 33  TRP   C N   
1278 C CA  . TRP   B 27  ? 0.1491 0.1392 0.1762 -0.0174 0.0158  0.0024  33  TRP   C CA  
1279 C C   . TRP   B 27  ? 0.1409 0.1311 0.1692 -0.0144 0.0114  0.0020  33  TRP   C C   
1280 O O   . TRP   B 27  ? 0.1508 0.1439 0.1823 -0.0126 0.0098  -0.0004 33  TRP   C O   
1281 C CB  . TRP   B 27  ? 0.1683 0.1583 0.1879 -0.0176 0.0170  0.0034  33  TRP   C CB  
1282 C CG  . TRP   B 27  ? 0.1723 0.1595 0.1847 -0.0164 0.0140  0.0062  33  TRP   C CG  
1283 C CD1 . TRP   B 27  ? 0.2068 0.1897 0.2132 -0.0177 0.0137  0.0096  33  TRP   C CD1 
1284 C CD2 . TRP   B 27  ? 0.1555 0.1442 0.1667 -0.0137 0.0109  0.0057  33  TRP   C CD2 
1285 N NE1 . TRP   B 27  ? 0.2170 0.1993 0.2199 -0.0157 0.0102  0.0112  33  TRP   C NE1 
1286 C CE2 . TRP   B 27  ? 0.1849 0.1709 0.1906 -0.0134 0.0088  0.0087  33  TRP   C CE2 
1287 C CE3 . TRP   B 27  ? 0.1582 0.1500 0.1727 -0.0116 0.0095  0.0032  33  TRP   C CE3 
1288 C CZ2 . TRP   B 27  ? 0.1874 0.1745 0.1916 -0.0111 0.0058  0.0090  33  TRP   C CZ2 
1289 C CZ3 . TRP   B 27  ? 0.1617 0.1539 0.1734 -0.0096 0.0069  0.0037  33  TRP   C CZ3 
1290 C CH2 . TRP   B 27  ? 0.1616 0.1518 0.1688 -0.0095 0.0053  0.0063  33  TRP   C CH2 
1291 N N   . GLU   B 28  ? 0.1445 0.1311 0.1698 -0.0138 0.0095  0.0041  34  GLU   C N   
1292 C CA  . GLU   B 28  ? 0.1517 0.1380 0.1773 -0.0110 0.0060  0.0035  34  GLU   C CA  
1293 C C   . GLU   B 28  ? 0.1499 0.1331 0.1707 -0.0101 0.0047  0.0064  34  GLU   C C   
1294 O O   . GLU   B 28  ? 0.1517 0.1317 0.1701 -0.0117 0.0057  0.0090  34  GLU   C O   
1295 C CB  . GLU   B 28  ? 0.1559 0.1417 0.1870 -0.0106 0.0046  0.0015  34  GLU   C CB  
1296 C CG  . GLU   B 28  ? 0.1744 0.1569 0.2078 -0.0127 0.0056  0.0025  34  GLU   C CG  
1297 C CD  . GLU   B 28  ? 0.2045 0.1822 0.2348 -0.0120 0.0046  0.0050  34  GLU   C CD  
1298 O OE1 . GLU   B 28  ? 0.2267 0.2011 0.2567 -0.0141 0.0061  0.0071  34  GLU   C OE1 
1299 O OE2 . GLU   B 28  ? 0.1696 0.1467 0.1986 -0.0095 0.0024  0.0048  34  GLU   C OE2 
1300 N N   . ASP   B 29  ? 0.1405 0.1245 0.1603 -0.0076 0.0025  0.0060  35  ASP   C N   
1301 C CA  . ASP   B 29  ? 0.1307 0.1125 0.1478 -0.0064 0.0009  0.0085  35  ASP   C CA  
1302 C C   . ASP   B 29  ? 0.1248 0.1068 0.1443 -0.0038 -0.0009 0.0068  35  ASP   C C   
1303 O O   . ASP   B 29  ? 0.1291 0.1140 0.1480 -0.0026 -0.0013 0.0053  35  ASP   C O   
1304 C CB  . ASP   B 29  ? 0.1440 0.1271 0.1562 -0.0068 0.0009  0.0102  35  ASP   C CB  
1305 C CG  . ASP   B 29  ? 0.1919 0.1732 0.2021 -0.0057 -0.0014 0.0130  35  ASP   C CG  
1306 O OD1 . ASP   B 29  ? 0.2308 0.2114 0.2442 -0.0036 -0.0028 0.0127  35  ASP   C OD1 
1307 O OD2 . ASP   B 29  ? 0.2032 0.1841 0.2086 -0.0068 -0.0018 0.0151  35  ASP   C OD2 
1308 N N   . SER   B 30  ? 0.1250 0.1038 0.1469 -0.0031 -0.0015 0.0070  36  SER   C N   
1309 C CA  A SER   B 30  ? 0.1285 0.1069 0.1523 -0.0008 -0.0025 0.0050  36  SER   C CA  
1310 C CA  B SER   B 30  ? 0.1258 0.1043 0.1496 -0.0008 -0.0025 0.0050  36  SER   C CA  
1311 C C   . SER   B 30  ? 0.1371 0.1173 0.1599 0.0011  -0.0033 0.0059  36  SER   C C   
1312 O O   . SER   B 30  ? 0.1378 0.1195 0.1611 0.0025  -0.0033 0.0038  36  SER   C O   
1313 C CB  A SER   B 30  ? 0.1678 0.1416 0.1942 -0.0006 -0.0027 0.0052  36  SER   C CB  
1314 C CB  B SER   B 30  ? 0.1571 0.1312 0.1836 -0.0003 -0.0028 0.0049  36  SER   C CB  
1315 O OG  A SER   B 30  ? 0.2204 0.1932 0.2484 0.0015  -0.0031 0.0030  36  SER   C OG  
1316 O OG  B SER   B 30  ? 0.2111 0.1836 0.2394 -0.0022 -0.0022 0.0035  36  SER   C OG  
1317 N N   . SER   B 31  ? 0.1240 0.1039 0.1454 0.0009  -0.0041 0.0091  37  SER   C N   
1318 C CA  . SER   B 31  ? 0.1208 0.1029 0.1426 0.0026  -0.0054 0.0100  37  SER   C CA  
1319 C C   . SER   B 31  ? 0.1279 0.1141 0.1475 0.0023  -0.0049 0.0085  37  SER   C C   
1320 O O   . SER   B 31  ? 0.1504 0.1389 0.1714 0.0037  -0.0054 0.0082  37  SER   C O   
1321 C CB  . SER   B 31  ? 0.1688 0.1494 0.1893 0.0023  -0.0072 0.0138  37  SER   C CB  
1322 O OG  . SER   B 31  ? 0.2355 0.2170 0.2508 0.0001  -0.0070 0.0152  37  SER   C OG  
1323 N N   . ARG   B 32  ? 0.1029 0.0901 0.1200 0.0006  -0.0038 0.0076  38  ARG   C N   
1324 C CA  . ARG   B 32  ? 0.1027 0.0930 0.1178 0.0003  -0.0034 0.0062  38  ARG   C CA  
1325 C C   . ARG   B 32  ? 0.1022 0.0930 0.1181 0.0007  -0.0027 0.0033  38  ARG   C C   
1326 O O   . ARG   B 32  ? 0.1041 0.0968 0.1184 0.0006  -0.0025 0.0022  38  ARG   C O   
1327 C CB  . ARG   B 32  ? 0.1120 0.1028 0.1237 -0.0019 -0.0025 0.0071  38  ARG   C CB  
1328 C CG  . ARG   B 32  ? 0.1307 0.1208 0.1394 -0.0027 -0.0036 0.0102  38  ARG   C CG  
1329 C CD  . ARG   B 32  ? 0.1194 0.1092 0.1234 -0.0051 -0.0023 0.0108  38  ARG   C CD  
1330 N NE  . ARG   B 32  ? 0.1128 0.1053 0.1155 -0.0053 -0.0017 0.0089  38  ARG   C NE  
1331 C CZ  . ARG   B 32  ? 0.1291 0.1218 0.1271 -0.0071 -0.0010 0.0092  38  ARG   C CZ  
1332 N NH1 . ARG   B 32  ? 0.1485 0.1388 0.1419 -0.0090 -0.0009 0.0114  38  ARG   C NH1 
1333 N NH2 . ARG   B 32  ? 0.1291 0.1238 0.1265 -0.0071 -0.0006 0.0073  38  ARG   C NH2 
1334 N N   . ASP   B 33  ? 0.1081 0.0968 0.1260 0.0009  -0.0026 0.0021  39  ASP   C N   
1335 C CA  . ASP   B 33  ? 0.1021 0.0905 0.1201 0.0008  -0.0027 -0.0005 39  ASP   C CA  
1336 C C   . ASP   B 33  ? 0.0995 0.0898 0.1173 -0.0004 -0.0025 -0.0010 39  ASP   C C   
1337 O O   . ASP   B 33  ? 0.1047 0.0957 0.1217 -0.0001 -0.0031 -0.0026 39  ASP   C O   
1338 C CB  . ASP   B 33  ? 0.1045 0.0932 0.1208 0.0021  -0.0029 -0.0021 39  ASP   C CB  
1339 C CG  . ASP   B 33  ? 0.1025 0.0899 0.1175 0.0020  -0.0036 -0.0046 39  ASP   C CG  
1340 O OD1 . ASP   B 33  ? 0.1269 0.1124 0.1435 0.0015  -0.0043 -0.0056 39  ASP   C OD1 
1341 O OD2 . ASP   B 33  ? 0.1229 0.1109 0.1351 0.0022  -0.0038 -0.0054 39  ASP   C OD2 
1342 N N   . LEU   B 34  ? 0.0983 0.0889 0.1167 -0.0019 -0.0015 0.0003  40  LEU   C N   
1343 C CA  . LEU   B 34  ? 0.1049 0.0974 0.1242 -0.0030 -0.0006 -0.0006 40  LEU   C CA  
1344 C C   . LEU   B 34  ? 0.1092 0.1011 0.1321 -0.0045 0.0004  -0.0009 40  LEU   C C   
1345 O O   . LEU   B 34  ? 0.1135 0.1034 0.1366 -0.0054 0.0011  0.0006  40  LEU   C O   
1346 C CB  . LEU   B 34  ? 0.1175 0.1112 0.1338 -0.0039 0.0007  0.0007  40  LEU   C CB  
1347 C CG  . LEU   B 34  ? 0.1237 0.1186 0.1370 -0.0029 -0.0001 0.0007  40  LEU   C CG  
1348 C CD1 . LEU   B 34  ? 0.1322 0.1278 0.1422 -0.0042 0.0012  0.0018  40  LEU   C CD1 
1349 C CD2 . LEU   B 34  ? 0.1279 0.1236 0.1420 -0.0020 -0.0008 -0.0014 40  LEU   C CD2 
1350 N N   . LEU   B 35  ? 0.1041 0.0979 0.1305 -0.0049 0.0004  -0.0028 41  LEU   C N   
1351 C CA  . LEU   B 35  ? 0.1041 0.0986 0.1356 -0.0066 0.0018  -0.0035 41  LEU   C CA  
1352 C C   . LEU   B 35  ? 0.0990 0.0966 0.1333 -0.0069 0.0032  -0.0049 41  LEU   C C   
1353 O O   . LEU   B 35  ? 0.1073 0.1060 0.1414 -0.0054 0.0016  -0.0060 41  LEU   C O   
1354 C CB  . LEU   B 35  ? 0.1171 0.1105 0.1526 -0.0065 -0.0002 -0.0050 41  LEU   C CB  
1355 C CG  . LEU   B 35  ? 0.1183 0.1127 0.1605 -0.0086 0.0010  -0.0059 41  LEU   C CG  
1356 C CD1 . LEU   B 35  ? 0.1315 0.1230 0.1754 -0.0091 -0.0006 -0.0064 41  LEU   C CD1 
1357 C CD2 . LEU   B 35  ? 0.1235 0.1217 0.1718 -0.0084 0.0001  -0.0082 41  LEU   C CD2 
1358 N N   . VAL   B 36  ? 0.1065 0.1049 0.1430 -0.0089 0.0064  -0.0048 42  VAL   C N   
1359 C CA  . VAL   B 36  ? 0.1035 0.1050 0.1440 -0.0094 0.0086  -0.0065 42  VAL   C CA  
1360 C C   . VAL   B 36  ? 0.1152 0.1185 0.1642 -0.0110 0.0100  -0.0080 42  VAL   C C   
1361 O O   . VAL   B 36  ? 0.1291 0.1310 0.1782 -0.0132 0.0120  -0.0068 42  VAL   C O   
1362 C CB  . VAL   B 36  ? 0.1088 0.1097 0.1438 -0.0108 0.0122  -0.0054 42  VAL   C CB  
1363 C CG1 . VAL   B 36  ? 0.1392 0.1429 0.1787 -0.0113 0.0152  -0.0078 42  VAL   C CG1 
1364 C CG2 . VAL   B 36  ? 0.1235 0.1229 0.1510 -0.0094 0.0103  -0.0041 42  VAL   C CG2 
1365 N N   . SER   B 37  ? 0.1132 0.1196 0.1696 -0.0100 0.0087  -0.0103 43  SER   C N   
1366 C CA  . SER   B 37  ? 0.1180 0.1273 0.1846 -0.0114 0.0098  -0.0121 43  SER   C CA  
1367 C C   . SER   B 37  ? 0.1310 0.1440 0.2036 -0.0115 0.0130  -0.0142 43  SER   C C   
1368 O O   . SER   B 37  ? 0.1395 0.1526 0.2089 -0.0099 0.0132  -0.0145 43  SER   C O   
1369 C CB  . SER   B 37  ? 0.1329 0.1428 0.2046 -0.0102 0.0047  -0.0134 43  SER   C CB  
1370 O OG  . SER   B 37  ? 0.1393 0.1497 0.2107 -0.0075 0.0011  -0.0143 43  SER   C OG  
1371 N N   . SER   B 38  ? 0.1453 0.1615 0.2275 -0.0134 0.0159  -0.0158 44  SER   C N   
1372 C CA  . SER   B 38  ? 0.1547 0.1746 0.2441 -0.0134 0.0197  -0.0182 44  SER   C CA  
1373 C C   . SER   B 38  ? 0.1829 0.2067 0.2835 -0.0109 0.0155  -0.0206 44  SER   C C   
1374 O O   . SER   B 38  ? 0.1926 0.2169 0.2977 -0.0104 0.0106  -0.0208 44  SER   C O   
1375 C CB  . SER   B 38  ? 0.1881 0.2096 0.2823 -0.0169 0.0258  -0.0189 44  SER   C CB  
1376 O OG  . SER   B 38  ? 0.2255 0.2486 0.3280 -0.0181 0.0238  -0.0193 44  SER   C OG  
1377 N N   . THR   B 39  ? 0.1940 0.2199 0.2985 -0.0093 0.0170  -0.0224 45  THR   C N   
1378 C CA  . THR   B 39  ? 0.2303 0.2595 0.3457 -0.0066 0.0129  -0.0245 45  THR   C CA  
1379 C C   . THR   B 39  ? 0.2707 0.3050 0.3991 -0.0071 0.0179  -0.0276 45  THR   C C   
1380 O O   . THR   B 39  ? 0.2782 0.3125 0.4041 -0.0092 0.0249  -0.0282 45  THR   C O   
1381 C CB  . THR   B 39  ? 0.2439 0.2702 0.3524 -0.0036 0.0096  -0.0238 45  THR   C CB  
1382 O OG1 . THR   B 39  ? 0.2538 0.2798 0.3595 -0.0038 0.0150  -0.0247 45  THR   C OG1 
1383 C CG2 . THR   B 39  ? 0.2600 0.2814 0.3552 -0.0033 0.0061  -0.0209 45  THR   C CG2 
1384 N N   . THR   B 40  ? 0.2977 0.3361 0.4398 -0.0051 0.0143  -0.0297 46  THR   C N   
1385 C CA  . THR   B 40  ? 0.3235 0.3672 0.4799 -0.0049 0.0189  -0.0330 46  THR   C CA  
1386 C C   . THR   B 40  ? 0.3398 0.3825 0.4956 -0.0018 0.0190  -0.0342 46  THR   C C   
1387 O O   . THR   B 40  ? 0.3641 0.4087 0.5247 -0.0022 0.0256  -0.0367 46  THR   C O   
1388 C CB  . THR   B 40  ? 0.3528 0.4022 0.5264 -0.0044 0.0149  -0.0348 46  THR   C CB  
1389 O OG1 . THR   B 40  ? 0.3942 0.4417 0.5666 -0.0016 0.0056  -0.0335 46  THR   C OG1 
1390 C CG2 . THR   B 40  ? 0.3589 0.4097 0.5350 -0.0082 0.0168  -0.0345 46  THR   C CG2 
1391 N N   . ALA   B 41  ? 0.3276 0.3667 0.4771 0.0010  0.0123  -0.0324 47  ALA   C N   
1392 C CA  . ALA   B 41  ? 0.3264 0.3636 0.4749 0.0040  0.0118  -0.0331 47  ALA   C CA  
1393 C C   . ALA   B 41  ? 0.3244 0.3567 0.4573 0.0029  0.0158  -0.0319 47  ALA   C C   
1394 O O   . ALA   B 41  ? 0.3376 0.3668 0.4584 0.0010  0.0156  -0.0294 47  ALA   C O   
1395 C CB  . ALA   B 41  ? 0.3353 0.3702 0.4837 0.0071  0.0027  -0.0316 47  ALA   C CB  
1396 N N   . GLN   B 42  ? 0.3130 0.3443 0.4463 0.0042  0.0189  -0.0337 48  GLN   C N   
1397 C CA  . GLN   B 42  ? 0.3120 0.3388 0.4313 0.0031  0.0226  -0.0330 48  GLN   C CA  
1398 C C   . GLN   B 42  ? 0.2958 0.3178 0.4050 0.0049  0.0165  -0.0303 48  GLN   C C   
1399 O O   . GLN   B 42  ? 0.3132 0.3344 0.4271 0.0078  0.0116  -0.0303 48  GLN   C O   
1400 C CB  . GLN   B 42  ? 0.3486 0.3761 0.4732 0.0037  0.0285  -0.0366 48  GLN   C CB  
1401 C CG  . GLN   B 42  ? 0.4170 0.4394 0.5278 0.0026  0.0317  -0.0365 48  GLN   C CG  
1402 C CD  . GLN   B 42  ? 0.5086 0.5301 0.6094 -0.0015 0.0378  -0.0361 48  GLN   C CD  
1403 O OE1 . GLN   B 42  ? 0.5366 0.5611 0.6415 -0.0037 0.0413  -0.0365 48  GLN   C OE1 
1404 N NE2 . GLN   B 42  ? 0.5335 0.5504 0.6208 -0.0027 0.0391  -0.0353 48  GLN   C NE2 
1405 N N   . GLY   B 43  ? 0.2450 0.2637 0.3404 0.0030  0.0167  -0.0278 49  GLY   C N   
1406 C CA  . GLY   B 43  ? 0.2256 0.2398 0.3110 0.0042  0.0119  -0.0253 49  GLY   C CA  
1407 C C   . GLY   B 43  ? 0.2171 0.2282 0.2959 0.0042  0.0147  -0.0261 49  GLY   C C   
1408 O O   . GLY   B 43  ? 0.2305 0.2418 0.3064 0.0021  0.0206  -0.0275 49  GLY   C O   
1409 N N   . CYS   B 44  ? 0.1870 0.1948 0.2623 0.0060  0.0107  -0.0251 50  CYS   C N   
1410 C CA  . CYS   B 44  ? 0.1969 0.2014 0.2671 0.0062  0.0128  -0.0260 50  CYS   C CA  
1411 C C   . CYS   B 44  ? 0.1892 0.1898 0.2465 0.0051  0.0110  -0.0235 50  CYS   C C   
1412 O O   . CYS   B 44  ? 0.2110 0.2083 0.2645 0.0054  0.0113  -0.0241 50  CYS   C O   
1413 C CB  . CYS   B 44  ? 0.2177 0.2210 0.2962 0.0093  0.0106  -0.0276 50  CYS   C CB  
1414 S SG  . CYS   B 44  ? 0.2568 0.2653 0.3530 0.0108  0.0132  -0.0313 50  CYS   C SG  
1415 N N   . ASP   B 45  ? 0.1507 0.1516 0.2018 0.0038  0.0093  -0.0209 51  ASP   C N   
1416 C CA  . ASP   B 45  ? 0.1597 0.1576 0.2000 0.0027  0.0080  -0.0188 51  ASP   C CA  
1417 C C   . ASP   B 45  ? 0.1763 0.1738 0.2103 0.0003  0.0124  -0.0195 51  ASP   C C   
1418 O O   . ASP   B 45  ? 0.2044 0.2039 0.2393 -0.0013 0.0161  -0.0204 51  ASP   C O   
1419 C CB  . ASP   B 45  ? 0.1652 0.1635 0.2016 0.0023  0.0051  -0.0161 51  ASP   C CB  
1420 C CG  . ASP   B 45  ? 0.2140 0.2115 0.2537 0.0043  0.0001  -0.0153 51  ASP   C CG  
1421 O OD1 . ASP   B 45  ? 0.2481 0.2438 0.2909 0.0060  -0.0019 -0.0158 51  ASP   C OD1 
1422 O OD2 . ASP   B 45  ? 0.2144 0.2127 0.2534 0.0040  -0.0019 -0.0139 51  ASP   C OD2 
1423 N N   . THR   B 46  ? 0.1720 0.1666 0.1993 -0.0003 0.0121  -0.0192 52  THR   C N   
1424 C CA  . THR   B 46  ? 0.1841 0.1778 0.2040 -0.0029 0.0153  -0.0197 52  THR   C CA  
1425 C C   . THR   B 46  ? 0.1588 0.1527 0.1718 -0.0042 0.0131  -0.0166 52  THR   C C   
1426 O O   . THR   B 46  ? 0.1743 0.1671 0.1857 -0.0033 0.0098  -0.0151 52  THR   C O   
1427 C CB  . THR   B 46  ? 0.2368 0.2271 0.2538 -0.0030 0.0159  -0.0213 52  THR   C CB  
1428 O OG1 . THR   B 46  ? 0.2762 0.2661 0.2999 -0.0018 0.0188  -0.0246 52  THR   C OG1 
1429 C CG2 . THR   B 46  ? 0.2624 0.2513 0.2700 -0.0059 0.0176  -0.0213 52  THR   C CG2 
1430 N N   . ILE   B 47  ? 0.1544 0.1492 0.1634 -0.0062 0.0150  -0.0159 53  ILE   C N   
1431 C CA  . ILE   B 47  ? 0.1416 0.1365 0.1449 -0.0073 0.0129  -0.0131 53  ILE   C CA  
1432 C C   . ILE   B 47  ? 0.1363 0.1294 0.1322 -0.0091 0.0128  -0.0130 53  ILE   C C   
1433 O O   . ILE   B 47  ? 0.1432 0.1349 0.1354 -0.0109 0.0156  -0.0147 53  ILE   C O   
1434 C CB  . ILE   B 47  ? 0.1656 0.1617 0.1680 -0.0087 0.0143  -0.0119 53  ILE   C CB  
1435 C CG1 . ILE   B 47  ? 0.1896 0.1876 0.1998 -0.0074 0.0148  -0.0124 53  ILE   C CG1 
1436 C CG2 . ILE   B 47  ? 0.1665 0.1627 0.1644 -0.0091 0.0115  -0.0088 53  ILE   C CG2 
1437 C CD1 . ILE   B 47  ? 0.2197 0.2183 0.2336 -0.0052 0.0109  -0.0113 53  ILE   C CD1 
1438 N N   . ALA   B 48  ? 0.1226 0.1156 0.1162 -0.0090 0.0097  -0.0113 54  ALA   C N   
1439 C CA  . ALA   B 48  ? 0.1287 0.1206 0.1162 -0.0109 0.0090  -0.0111 54  ALA   C CA  
1440 C C   . ALA   B 48  ? 0.1177 0.1099 0.0999 -0.0130 0.0093  -0.0097 54  ALA   C C   
1441 O O   . ALA   B 48  ? 0.1185 0.1120 0.1017 -0.0126 0.0085  -0.0076 54  ALA   C O   
1442 C CB  . ALA   B 48  ? 0.1242 0.1167 0.1121 -0.0102 0.0059  -0.0094 54  ALA   C CB  
1443 N N   . ARG   B 49  ? 0.1108 0.1011 0.0867 -0.0153 0.0100  -0.0106 55  ARG   C N   
1444 C CA  . ARG   B 49  ? 0.1211 0.1108 0.0902 -0.0177 0.0095  -0.0090 55  ARG   C CA  
1445 C C   . ARG   B 49  ? 0.1271 0.1163 0.0919 -0.0192 0.0065  -0.0087 55  ARG   C C   
1446 O O   . ARG   B 49  ? 0.1364 0.1232 0.0966 -0.0211 0.0076  -0.0109 55  ARG   C O   
1447 C CB  . ARG   B 49  ? 0.1345 0.1219 0.0990 -0.0197 0.0136  -0.0109 55  ARG   C CB  
1448 C CG  . ARG   B 49  ? 0.1411 0.1295 0.1117 -0.0183 0.0170  -0.0118 55  ARG   C CG  
1449 C CD  . ARG   B 49  ? 0.1534 0.1435 0.1265 -0.0176 0.0155  -0.0088 55  ARG   C CD  
1450 N NE  . ARG   B 49  ? 0.1614 0.1525 0.1404 -0.0168 0.0189  -0.0100 55  ARG   C NE  
1451 C CZ  . ARG   B 49  ? 0.1834 0.1761 0.1670 -0.0157 0.0181  -0.0082 55  ARG   C CZ  
1452 N NH1 . ARG   B 49  ? 0.1613 0.1544 0.1442 -0.0151 0.0144  -0.0053 55  ARG   C NH1 
1453 N NH2 . ARG   B 49  ? 0.1941 0.1881 0.1842 -0.0152 0.0209  -0.0097 55  ARG   C NH2 
1454 N N   . CYS   B 50  ? 0.1162 0.1077 0.0835 -0.0184 0.0029  -0.0062 56  CYS   C N   
1455 C CA  . CYS   B 50  ? 0.1225 0.1148 0.0890 -0.0194 0.0000  -0.0060 56  CYS   C CA  
1456 C C   . CYS   B 50  ? 0.1343 0.1298 0.1044 -0.0184 -0.0035 -0.0031 56  CYS   C C   
1457 O O   . CYS   B 50  ? 0.1287 0.1254 0.1018 -0.0167 -0.0035 -0.0014 56  CYS   C O   
1458 C CB  . CYS   B 50  ? 0.1316 0.1235 0.1021 -0.0183 0.0010  -0.0080 56  CYS   C CB  
1459 S SG  . CYS   B 50  ? 0.1227 0.1168 0.1010 -0.0150 0.0007  -0.0067 56  CYS   C SG  
1460 N N   . ASP   B 51  ? 0.1373 0.1342 0.1079 -0.0195 -0.0063 -0.0028 57  ASP   C N   
1461 C CA  . ASP   B 51  ? 0.1380 0.1386 0.1140 -0.0184 -0.0092 -0.0006 57  ASP   C CA  
1462 C C   . ASP   B 51  ? 0.1333 0.1356 0.1146 -0.0177 -0.0088 -0.0015 57  ASP   C C   
1463 O O   . ASP   B 51  ? 0.1367 0.1421 0.1221 -0.0179 -0.0109 -0.0005 57  ASP   C O   
1464 C CB  . ASP   B 51  ? 0.1795 0.1811 0.1528 -0.0202 -0.0132 0.0011  57  ASP   C CB  
1465 C CG  . ASP   B 51  ? 0.2160 0.2169 0.1860 -0.0230 -0.0146 -0.0005 57  ASP   C CG  
1466 O OD1 . ASP   B 51  ? 0.2270 0.2264 0.1967 -0.0235 -0.0122 -0.0030 57  ASP   C OD1 
1467 O OD2 . ASP   B 51  ? 0.2996 0.3014 0.2675 -0.0248 -0.0187 0.0008  57  ASP   C OD2 
1468 N N   . CYS   B 52  ? 0.1183 0.1185 0.1000 -0.0170 -0.0060 -0.0033 58  CYS   C N   
1469 C CA  . CYS   B 52  ? 0.1173 0.1181 0.1028 -0.0164 -0.0054 -0.0038 58  CYS   C CA  
1470 C C   . CYS   B 52  ? 0.1048 0.1088 0.0957 -0.0148 -0.0060 -0.0021 58  CYS   C C   
1471 O O   . CYS   B 52  ? 0.1022 0.1069 0.0944 -0.0130 -0.0059 -0.0010 58  CYS   C O   
1472 C CB  . CYS   B 52  ? 0.1146 0.1121 0.0998 -0.0153 -0.0029 -0.0053 58  CYS   C CB  
1473 S SG  . CYS   B 52  ? 0.1363 0.1297 0.1170 -0.0171 -0.0017 -0.0080 58  CYS   C SG  
1474 N N   . GLN   B 53  ? 0.1005 0.1060 0.0945 -0.0155 -0.0061 -0.0023 59  GLN   C N   
1475 C CA  . GLN   B 53  ? 0.1016 0.1098 0.1008 -0.0142 -0.0055 -0.0014 59  GLN   C CA  
1476 C C   . GLN   B 53  ? 0.1094 0.1156 0.1086 -0.0144 -0.0033 -0.0022 59  GLN   C C   
1477 O O   . GLN   B 53  ? 0.1073 0.1153 0.1100 -0.0142 -0.0022 -0.0019 59  GLN   C O   
1478 C CB  . GLN   B 53  ? 0.0918 0.1046 0.0960 -0.0150 -0.0077 -0.0005 59  GLN   C CB  
1479 C CG  . GLN   B 53  ? 0.1139 0.1284 0.1186 -0.0140 -0.0101 0.0011  59  GLN   C CG  
1480 C CD  . GLN   B 53  ? 0.1266 0.1457 0.1374 -0.0145 -0.0128 0.0021  59  GLN   C CD  
1481 O OE1 . GLN   B 53  ? 0.1580 0.1781 0.1677 -0.0162 -0.0161 0.0027  59  GLN   C OE1 
1482 N NE2 . GLN   B 53  ? 0.1219 0.1439 0.1396 -0.0130 -0.0115 0.0022  59  GLN   C NE2 
1483 N N   . THR   B 54  ? 0.1084 0.1103 0.1035 -0.0148 -0.0024 -0.0033 60  THR   C N   
1484 C CA  . THR   B 54  ? 0.1227 0.1213 0.1167 -0.0149 -0.0007 -0.0036 60  THR   C CA  
1485 C C   . THR   B 54  ? 0.1238 0.1185 0.1149 -0.0132 -0.0003 -0.0041 60  THR   C C   
1486 O O   . THR   B 54  ? 0.1336 0.1275 0.1234 -0.0130 -0.0007 -0.0049 60  THR   C O   
1487 C CB  . THR   B 54  ? 0.1815 0.1788 0.1749 -0.0174 -0.0004 -0.0043 60  THR   C CB  
1488 O OG1 . THR   B 54  ? 0.2272 0.2218 0.2176 -0.0184 -0.0011 -0.0055 60  THR   C OG1 
1489 C CG2 . THR   B 54  ? 0.2134 0.2154 0.2111 -0.0193 -0.0010 -0.0040 60  THR   C CG2 
1490 N N   . GLY   B 55  ? 0.1137 0.1060 0.1041 -0.0120 0.0004  -0.0037 61  GLY   C N   
1491 C CA  . GLY   B 55  ? 0.1231 0.1119 0.1120 -0.0102 0.0001  -0.0041 61  GLY   C CA  
1492 C C   . GLY   B 55  ? 0.1053 0.0909 0.0922 -0.0095 0.0003  -0.0033 61  GLY   C C   
1493 O O   . GLY   B 55  ? 0.1294 0.1144 0.1152 -0.0108 0.0012  -0.0027 61  GLY   C O   
1494 N N   . VAL   B 56  ? 0.1010 0.0843 0.0875 -0.0076 -0.0008 -0.0034 62  VAL   C N   
1495 C CA  . VAL   B 56  ? 0.1027 0.0819 0.0862 -0.0069 -0.0015 -0.0026 62  VAL   C CA  
1496 C C   . VAL   B 56  ? 0.1133 0.0936 0.0982 -0.0050 -0.0026 -0.0027 62  VAL   C C   
1497 O O   . VAL   B 56  ? 0.1156 0.0974 0.1036 -0.0039 -0.0032 -0.0035 62  VAL   C O   
1498 C CB  . VAL   B 56  ? 0.1138 0.0877 0.0957 -0.0066 -0.0027 -0.0026 62  VAL   C CB  
1499 C CG1 . VAL   B 56  ? 0.1383 0.1073 0.1163 -0.0058 -0.0044 -0.0014 62  VAL   C CG1 
1500 C CG2 . VAL   B 56  ? 0.1275 0.0996 0.1080 -0.0088 -0.0016 -0.0027 62  VAL   C CG2 
1501 N N   . TYR   B 57  ? 0.1131 0.0922 0.0954 -0.0048 -0.0026 -0.0021 63  TYR   C N   
1502 C CA  . TYR   B 57  ? 0.1160 0.0955 0.0992 -0.0032 -0.0039 -0.0024 63  TYR   C CA  
1503 C C   . TYR   B 57  ? 0.1214 0.0958 0.1000 -0.0028 -0.0059 -0.0019 63  TYR   C C   
1504 O O   . TYR   B 57  ? 0.1268 0.0973 0.1001 -0.0040 -0.0055 -0.0010 63  TYR   C O   
1505 C CB  . TYR   B 57  ? 0.1252 0.1083 0.1101 -0.0032 -0.0025 -0.0027 63  TYR   C CB  
1506 C CG  . TYR   B 57  ? 0.1220 0.1034 0.1029 -0.0040 -0.0010 -0.0025 63  TYR   C CG  
1507 C CD1 . TYR   B 57  ? 0.1407 0.1229 0.1209 -0.0057 0.0013  -0.0022 63  TYR   C CD1 
1508 C CD2 . TYR   B 57  ? 0.1261 0.1055 0.1044 -0.0034 -0.0016 -0.0029 63  TYR   C CD2 
1509 C CE1 . TYR   B 57  ? 0.1557 0.1367 0.1329 -0.0066 0.0036  -0.0024 63  TYR   C CE1 
1510 C CE2 . TYR   B 57  ? 0.1389 0.1165 0.1131 -0.0044 0.0006  -0.0032 63  TYR   C CE2 
1511 C CZ  . TYR   B 57  ? 0.1518 0.1303 0.1255 -0.0060 0.0034  -0.0029 63  TYR   C CZ  
1512 O OH  . TYR   B 57  ? 0.1645 0.1416 0.1347 -0.0072 0.0064  -0.0035 63  TYR   C OH  
1513 N N   . TYR   B 58  ? 0.1176 0.0917 0.0980 -0.0013 -0.0083 -0.0023 64  TYR   C N   
1514 C CA  . TYR   B 58  ? 0.1216 0.0908 0.0974 -0.0009 -0.0111 -0.0017 64  TYR   C CA  
1515 C C   . TYR   B 58  ? 0.1272 0.0960 0.0993 -0.0014 -0.0105 -0.0021 64  TYR   C C   
1516 O O   . TYR   B 58  ? 0.1307 0.1031 0.1067 -0.0008 -0.0099 -0.0031 64  TYR   C O   
1517 C CB  . TYR   B 58  ? 0.1409 0.1100 0.1214 0.0009  -0.0146 -0.0021 64  TYR   C CB  
1518 C CG  . TYR   B 58  ? 0.1564 0.1202 0.1320 0.0013  -0.0185 -0.0013 64  TYR   C CG  
1519 C CD1 . TYR   B 58  ? 0.1751 0.1331 0.1449 0.0008  -0.0201 0.0002  64  TYR   C CD1 
1520 C CD2 . TYR   B 58  ? 0.1921 0.1562 0.1683 0.0019  -0.0209 -0.0020 64  TYR   C CD2 
1521 C CE1 . TYR   B 58  ? 0.1978 0.1500 0.1615 0.0009  -0.0242 0.0013  64  TYR   C CE1 
1522 C CE2 . TYR   B 58  ? 0.2006 0.1594 0.1713 0.0019  -0.0251 -0.0013 64  TYR   C CE2 
1523 C CZ  . TYR   B 58  ? 0.2208 0.1737 0.1851 0.0015  -0.0269 0.0005  64  TYR   C CZ  
1524 O OH  . TYR   B 58  ? 0.2564 0.2032 0.2139 0.0013  -0.0316 0.0016  64  TYR   C OH  
1525 N N   . CYS   B 59  ? 0.1375 0.1013 0.1017 -0.0026 -0.0105 -0.0014 65  CYS   C N   
1526 C CA  . CYS   B 59  ? 0.1424 0.1046 0.1015 -0.0033 -0.0094 -0.0021 65  CYS   C CA  
1527 C C   . CYS   B 59  ? 0.1508 0.1071 0.1036 -0.0032 -0.0136 -0.0017 65  CYS   C C   
1528 O O   . CYS   B 59  ? 0.1783 0.1287 0.1235 -0.0042 -0.0148 -0.0002 65  CYS   C O   
1529 C CB  . CYS   B 59  ? 0.1372 0.0982 0.0916 -0.0053 -0.0053 -0.0018 65  CYS   C CB  
1530 S SG  . CYS   B 59  ? 0.1789 0.1370 0.1260 -0.0065 -0.0028 -0.0031 65  CYS   C SG  
1531 N N   . SER   B 60  ? 0.1608 0.1184 0.1165 -0.0021 -0.0161 -0.0028 66  SER   C N   
1532 C CA  . SER   B 60  ? 0.1894 0.1418 0.1400 -0.0020 -0.0210 -0.0025 66  SER   C CA  
1533 C C   . SER   B 60  ? 0.1905 0.1366 0.1291 -0.0039 -0.0205 -0.0024 66  SER   C C   
1534 O O   . SER   B 60  ? 0.2185 0.1583 0.1496 -0.0044 -0.0244 -0.0010 66  SER   C O   
1535 C CB  . SER   B 60  ? 0.2573 0.2129 0.2144 -0.0007 -0.0236 -0.0039 66  SER   C CB  
1536 O OG  . SER   B 60  ? 0.3589 0.3164 0.3162 -0.0012 -0.0208 -0.0056 66  SER   C OG  
1537 N N   . SER   B 61  ? 0.1839 0.1311 0.1202 -0.0050 -0.0155 -0.0037 67  SER   C N   
1538 C CA  . SER   B 61  ? 0.1857 0.1267 0.1100 -0.0071 -0.0137 -0.0042 67  SER   C CA  
1539 C C   . SER   B 61  ? 0.2036 0.1397 0.1198 -0.0090 -0.0121 -0.0022 67  SER   C C   
1540 O O   . SER   B 61  ? 0.2198 0.1496 0.1245 -0.0112 -0.0107 -0.0022 67  SER   C O   
1541 C CB  . SER   B 61  ? 0.1806 0.1247 0.1066 -0.0075 -0.0085 -0.0066 67  SER   C CB  
1542 O OG  . SER   B 61  ? 0.1859 0.1350 0.1178 -0.0076 -0.0037 -0.0064 67  SER   C OG  
1543 N N   . ARG   B 62  ? 0.1874 0.1256 0.1089 -0.0085 -0.0122 -0.0005 68  ARG   C N   
1544 C CA  . ARG   B 62  ? 0.1895 0.1225 0.1040 -0.0102 -0.0113 0.0016  68  ARG   C CA  
1545 C C   . ARG   B 62  ? 0.1937 0.1237 0.1095 -0.0090 -0.0170 0.0039  68  ARG   C C   
1546 O O   . ARG   B 62  ? 0.2174 0.1423 0.1278 -0.0102 -0.0171 0.0060  68  ARG   C O   
1547 C CB  . ARG   B 62  ? 0.2149 0.1528 0.1347 -0.0112 -0.0056 0.0013  68  ARG   C CB  
1548 C CG  . ARG   B 62  ? 0.2161 0.1564 0.1348 -0.0125 0.0002  -0.0007 68  ARG   C CG  
1549 C CD  . ARG   B 62  ? 0.2373 0.1699 0.1428 -0.0155 0.0027  -0.0003 68  ARG   C CD  
1550 N NE  . ARG   B 62  ? 0.2642 0.1993 0.1696 -0.0167 0.0090  -0.0028 68  ARG   C NE  
1551 C CZ  . ARG   B 62  ? 0.3026 0.2365 0.2046 -0.0166 0.0097  -0.0050 68  ARG   C CZ  
1552 N NH1 . ARG   B 62  ? 0.3038 0.2342 0.2018 -0.0155 0.0043  -0.0050 68  ARG   C NH1 
1553 N NH2 . ARG   B 62  ? 0.3428 0.2788 0.2456 -0.0175 0.0159  -0.0074 68  ARG   C NH2 
1554 N N   . ARG   B 63  ? 0.2019 0.1353 0.1258 -0.0064 -0.0213 0.0033  69  ARG   C N   
1555 C CA  . ARG   B 63  ? 0.2208 0.1531 0.1495 -0.0045 -0.0262 0.0048  69  ARG   C CA  
1556 C C   . ARG   B 63  ? 0.2322 0.1653 0.1640 -0.0048 -0.0235 0.0058  69  ARG   C C   
1557 O O   . ARG   B 63  ? 0.2641 0.1916 0.1926 -0.0049 -0.0259 0.0078  69  ARG   C O   
1558 C CB  . ARG   B 63  ? 0.2693 0.1929 0.1888 -0.0048 -0.0322 0.0069  69  ARG   C CB  
1559 C CG  . ARG   B 63  ? 0.3312 0.2539 0.2483 -0.0045 -0.0361 0.0058  69  ARG   C CG  
1560 C CD  . ARG   B 63  ? 0.4251 0.3529 0.3541 -0.0017 -0.0405 0.0048  69  ARG   C CD  
1561 N NE  . ARG   B 63  ? 0.4853 0.4111 0.4108 -0.0019 -0.0450 0.0039  69  ARG   C NE  
1562 C CZ  . ARG   B 63  ? 0.5315 0.4609 0.4585 -0.0023 -0.0430 0.0015  69  ARG   C CZ  
1563 N NH1 . ARG   B 63  ? 0.5222 0.4577 0.4550 -0.0023 -0.0369 -0.0002 69  ARG   C NH1 
1564 N NH2 . ARG   B 63  ? 0.5427 0.4694 0.4660 -0.0027 -0.0476 0.0006  69  ARG   C NH2 
1565 N N   . LYS   B 64  ? 0.2005 0.1400 0.1380 -0.0052 -0.0184 0.0043  70  LYS   C N   
1566 C CA  . LYS   B 64  ? 0.2139 0.1541 0.1536 -0.0061 -0.0155 0.0050  70  LYS   C CA  
1567 C C   . LYS   B 64  ? 0.1816 0.1301 0.1312 -0.0053 -0.0127 0.0032  70  LYS   C C   
1568 O O   . LYS   B 64  ? 0.1767 0.1300 0.1295 -0.0049 -0.0111 0.0017  70  LYS   C O   
1569 C CB  . LYS   B 64  ? 0.2930 0.2302 0.2244 -0.0093 -0.0110 0.0056  70  LYS   C CB  
1570 C CG  . LYS   B 64  ? 0.4489 0.3767 0.3694 -0.0111 -0.0123 0.0080  70  LYS   C CG  
1571 C CD  . LYS   B 64  ? 0.5352 0.4623 0.4510 -0.0144 -0.0064 0.0082  70  LYS   C CD  
1572 C CE  . LYS   B 64  ? 0.6135 0.5311 0.5188 -0.0169 -0.0067 0.0109  70  LYS   C CE  
1573 N NZ  . LYS   B 64  ? 0.6499 0.5604 0.5424 -0.0185 -0.0074 0.0118  70  LYS   C NZ  
1574 N N   . HIS   B 65  ? 0.1587 0.1080 0.1120 -0.0055 -0.0118 0.0034  71  HIS   C N   
1575 C CA  . HIS   B 65  ? 0.1390 0.0950 0.0997 -0.0054 -0.0089 0.0020  71  HIS   C CA  
1576 C C   . HIS   B 65  ? 0.1716 0.1287 0.1303 -0.0079 -0.0049 0.0021  71  HIS   C C   
1577 O O   . HIS   B 65  ? 0.2166 0.1684 0.1695 -0.0098 -0.0041 0.0035  71  HIS   C O   
1578 C CB  . HIS   B 65  ? 0.1434 0.0997 0.1095 -0.0043 -0.0102 0.0017  71  HIS   C CB  
1579 C CG  . HIS   B 65  ? 0.1490 0.1058 0.1197 -0.0017 -0.0137 0.0011  71  HIS   C CG  
1580 N ND1 . HIS   B 65  ? 0.1909 0.1535 0.1689 -0.0004 -0.0131 -0.0005 71  HIS   C ND1 
1581 C CD2 . HIS   B 65  ? 0.1554 0.1072 0.1246 -0.0004 -0.0177 0.0021  71  HIS   C CD2 
1582 C CE1 . HIS   B 65  ? 0.1685 0.1300 0.1500 0.0015  -0.0164 -0.0007 71  HIS   C CE1 
1583 N NE2 . HIS   B 65  ? 0.2037 0.1591 0.1806 0.0018  -0.0196 0.0008  71  HIS   C NE2 
1584 N N   . TYR   B 66  ? 0.1413 0.1048 0.1049 -0.0082 -0.0023 0.0009  72  TYR   C N   
1585 C CA  . TYR   B 66  ? 0.1435 0.1091 0.1073 -0.0105 0.0013  0.0008  72  TYR   C CA  
1586 C C   . TYR   B 66  ? 0.1350 0.1062 0.1057 -0.0105 0.0019  0.0000  72  TYR   C C   
1587 O O   . TYR   B 66  ? 0.1315 0.1069 0.1068 -0.0089 0.0011  -0.0008 72  TYR   C O   
1588 C CB  . TYR   B 66  ? 0.1510 0.1194 0.1145 -0.0108 0.0039  0.0001  72  TYR   C CB  
1589 C CG  . TYR   B 66  ? 0.1706 0.1331 0.1257 -0.0116 0.0043  0.0006  72  TYR   C CG  
1590 C CD1 . TYR   B 66  ? 0.1999 0.1580 0.1488 -0.0142 0.0066  0.0016  72  TYR   C CD1 
1591 C CD2 . TYR   B 66  ? 0.1839 0.1454 0.1369 -0.0101 0.0026  0.0001  72  TYR   C CD2 
1592 C CE1 . TYR   B 66  ? 0.2120 0.1640 0.1516 -0.0153 0.0072  0.0021  72  TYR   C CE1 
1593 C CE2 . TYR   B 66  ? 0.2028 0.1586 0.1469 -0.0112 0.0030  0.0003  72  TYR   C CE2 
1594 C CZ  . TYR   B 66  ? 0.2262 0.1771 0.1632 -0.0137 0.0052  0.0014  72  TYR   C CZ  
1595 O OH  . TYR   B 66  ? 0.2745 0.2190 0.2011 -0.0151 0.0057  0.0017  72  TYR   C OH  
1596 N N   . PRO   B 67  ? 0.1330 0.1040 0.1041 -0.0126 0.0033  0.0001  73  PRO   C N   
1597 C CA  . PRO   B 67  ? 0.1207 0.0968 0.0974 -0.0132 0.0037  -0.0008 73  PRO   C CA  
1598 C C   . PRO   B 67  ? 0.1412 0.1232 0.1218 -0.0138 0.0057  -0.0012 73  PRO   C C   
1599 O O   . PRO   B 67  ? 0.1561 0.1375 0.1351 -0.0152 0.0082  -0.0010 73  PRO   C O   
1600 C CB  . PRO   B 67  ? 0.1281 0.1009 0.1031 -0.0155 0.0044  -0.0005 73  PRO   C CB  
1601 C CG  . PRO   B 67  ? 0.1452 0.1132 0.1147 -0.0170 0.0059  0.0007  73  PRO   C CG  
1602 C CD  . PRO   B 67  ? 0.1466 0.1120 0.1123 -0.0149 0.0045  0.0013  73  PRO   C CD  
1603 N N   . VAL   B 68  ? 0.1236 0.1107 0.1091 -0.0128 0.0049  -0.0018 74  VAL   C N   
1604 C CA  . VAL   B 68  ? 0.1335 0.1263 0.1240 -0.0129 0.0061  -0.0020 74  VAL   C CA  
1605 C C   . VAL   B 68  ? 0.1218 0.1190 0.1168 -0.0133 0.0047  -0.0023 74  VAL   C C   
1606 O O   . VAL   B 68  ? 0.1386 0.1351 0.1327 -0.0128 0.0029  -0.0024 74  VAL   C O   
1607 C CB  . VAL   B 68  ? 0.1571 0.1508 0.1482 -0.0107 0.0061  -0.0022 74  VAL   C CB  
1608 C CG1 . VAL   B 68  ? 0.1731 0.1626 0.1591 -0.0108 0.0078  -0.0022 74  VAL   C CG1 
1609 C CG2 . VAL   B 68  ? 0.1690 0.1623 0.1600 -0.0088 0.0037  -0.0022 74  VAL   C CG2 
1610 N N   . SER   B 69  ? 0.1152 0.1173 0.1155 -0.0141 0.0054  -0.0023 75  SER   C N   
1611 C CA  . SER   B 69  ? 0.1131 0.1200 0.1180 -0.0140 0.0033  -0.0022 75  SER   C CA  
1612 C C   . SER   B 69  ? 0.1092 0.1179 0.1164 -0.0114 0.0029  -0.0018 75  SER   C C   
1613 O O   . SER   B 69  ? 0.1115 0.1197 0.1191 -0.0104 0.0048  -0.0020 75  SER   C O   
1614 C CB  . SER   B 69  ? 0.1483 0.1599 0.1593 -0.0158 0.0038  -0.0023 75  SER   C CB  
1615 O OG  . SER   B 69  ? 0.2134 0.2231 0.2225 -0.0185 0.0042  -0.0028 75  SER   C OG  
1616 N N   . PHE   B 70  ? 0.0919 0.1022 0.1000 -0.0106 0.0004  -0.0012 76  PHE   C N   
1617 C CA  . PHE   B 70  ? 0.0889 0.1002 0.0990 -0.0084 -0.0002 -0.0006 76  PHE   C CA  
1618 C C   . PHE   B 70  ? 0.0882 0.1031 0.1019 -0.0084 -0.0029 0.0005  76  PHE   C C   
1619 O O   . PHE   B 70  ? 0.0994 0.1149 0.1120 -0.0101 -0.0047 0.0006  76  PHE   C O   
1620 C CB  . PHE   B 70  ? 0.0954 0.1029 0.1010 -0.0071 -0.0002 -0.0007 76  PHE   C CB  
1621 C CG  . PHE   B 70  ? 0.0952 0.1006 0.0970 -0.0079 -0.0013 -0.0009 76  PHE   C CG  
1622 C CD1 . PHE   B 70  ? 0.1077 0.1100 0.1061 -0.0087 -0.0007 -0.0017 76  PHE   C CD1 
1623 C CD2 . PHE   B 70  ? 0.1027 0.1089 0.1042 -0.0077 -0.0028 -0.0002 76  PHE   C CD2 
1624 C CE1 . PHE   B 70  ? 0.1229 0.1233 0.1186 -0.0092 -0.0012 -0.0022 76  PHE   C CE1 
1625 C CE2 . PHE   B 70  ? 0.1077 0.1118 0.1056 -0.0085 -0.0030 -0.0007 76  PHE   C CE2 
1626 C CZ  . PHE   B 70  ? 0.1139 0.1154 0.1093 -0.0092 -0.0022 -0.0019 76  PHE   C CZ  
1627 N N   . SER   B 71  ? 0.0922 0.1088 0.1100 -0.0065 -0.0034 0.0012  77  SER   C N   
1628 C CA  . SER   B 71  ? 0.1019 0.1214 0.1235 -0.0062 -0.0065 0.0027  77  SER   C CA  
1629 C C   . SER   B 71  ? 0.1116 0.1286 0.1279 -0.0064 -0.0086 0.0039  77  SER   C C   
1630 O O   . SER   B 71  ? 0.1191 0.1328 0.1301 -0.0066 -0.0074 0.0032  77  SER   C O   
1631 C CB  . SER   B 71  ? 0.1108 0.1325 0.1391 -0.0040 -0.0060 0.0030  77  SER   C CB  
1632 O OG  . SER   B 71  ? 0.1262 0.1448 0.1523 -0.0022 -0.0050 0.0030  77  SER   C OG  
1633 N N   . LYS   B 72  ? 0.1041 0.1227 0.1221 -0.0064 -0.0118 0.0056  78  LYS   C N   
1634 C CA  . LYS   B 72  ? 0.1208 0.1366 0.1331 -0.0069 -0.0136 0.0070  78  LYS   C CA  
1635 C C   . LYS   B 72  ? 0.1205 0.1344 0.1336 -0.0048 -0.0128 0.0078  78  LYS   C C   
1636 O O   . LYS   B 72  ? 0.1508 0.1664 0.1701 -0.0029 -0.0127 0.0080  78  LYS   C O   
1637 C CB  . LYS   B 72  ? 0.1460 0.1634 0.1586 -0.0080 -0.0180 0.0089  78  LYS   C CB  
1638 C CG  . LYS   B 72  ? 0.1701 0.1894 0.1821 -0.0104 -0.0190 0.0078  78  LYS   C CG  
1639 C CD  . LYS   B 72  ? 0.2773 0.2984 0.2902 -0.0115 -0.0242 0.0097  78  LYS   C CD  
1640 C CE  . LYS   B 72  ? 0.3881 0.4103 0.3990 -0.0145 -0.0258 0.0085  78  LYS   C CE  
1641 N NZ  . LYS   B 72  ? 0.4547 0.4777 0.4645 -0.0158 -0.0315 0.0106  78  LYS   C NZ  
1642 N N   . PRO   B 73  ? 0.1172 0.1276 0.1248 -0.0052 -0.0122 0.0082  79  PRO   C N   
1643 C CA  . PRO   B 73  ? 0.1245 0.1330 0.1333 -0.0035 -0.0114 0.0090  79  PRO   C CA  
1644 C C   . PRO   B 73  ? 0.1391 0.1483 0.1522 -0.0022 -0.0142 0.0113  79  PRO   C C   
1645 O O   . PRO   B 73  ? 0.1629 0.1723 0.1745 -0.0031 -0.0174 0.0133  79  PRO   C O   
1646 C CB  . PRO   B 73  ? 0.1562 0.1613 0.1585 -0.0049 -0.0106 0.0093  79  PRO   C CB  
1647 C CG  . PRO   B 73  ? 0.1869 0.1920 0.1849 -0.0069 -0.0100 0.0078  79  PRO   C CG  
1648 C CD  . PRO   B 73  ? 0.1275 0.1357 0.1281 -0.0073 -0.0119 0.0078  79  PRO   C CD  
1649 N N   . SER   B 74  ? 0.1330 0.1423 0.1514 0.0001  -0.0132 0.0109  80  SER   C N   
1650 C CA  . SER   B 74  ? 0.1473 0.1573 0.1715 0.0018  -0.0157 0.0129  80  SER   C CA  
1651 C C   . SER   B 74  ? 0.1362 0.1442 0.1637 0.0039  -0.0139 0.0123  80  SER   C C   
1652 O O   . SER   B 74  ? 0.1200 0.1261 0.1451 0.0038  -0.0110 0.0104  80  SER   C O   
1653 C CB  . SER   B 74  ? 0.1939 0.2087 0.2250 0.0024  -0.0169 0.0124  80  SER   C CB  
1654 O OG  . SER   B 74  ? 0.2621 0.2786 0.2976 0.0036  -0.0134 0.0098  80  SER   C OG  
1655 N N   . LEU   B 75  ? 0.1290 0.1367 0.1619 0.0058  -0.0160 0.0141  81  LEU   C N   
1656 C CA  . LEU   B 75  ? 0.1347 0.1401 0.1718 0.0080  -0.0148 0.0136  81  LEU   C CA  
1657 C C   . LEU   B 75  ? 0.1503 0.1587 0.1944 0.0097  -0.0123 0.0108  81  LEU   C C   
1658 O O   . LEU   B 75  ? 0.1665 0.1788 0.2175 0.0108  -0.0138 0.0111  81  LEU   C O   
1659 C CB  . LEU   B 75  ? 0.1616 0.1650 0.2018 0.0093  -0.0185 0.0169  81  LEU   C CB  
1660 C CG  . LEU   B 75  ? 0.2240 0.2222 0.2576 0.0080  -0.0196 0.0194  81  LEU   C CG  
1661 C CD1 . LEU   B 75  ? 0.2684 0.2644 0.3043 0.0090  -0.0243 0.0234  81  LEU   C CD1 
1662 C CD2 . LEU   B 75  ? 0.2351 0.2297 0.2685 0.0085  -0.0164 0.0177  81  LEU   C CD2 
1663 N N   . ILE   B 76  ? 0.1358 0.1427 0.1784 0.0099  -0.0087 0.0080  82  ILE   C N   
1664 C CA  . ILE   B 76  ? 0.1461 0.1550 0.1931 0.0110  -0.0054 0.0050  82  ILE   C CA  
1665 C C   . ILE   B 76  ? 0.1669 0.1721 0.2152 0.0126  -0.0032 0.0031  82  ILE   C C   
1666 O O   . ILE   B 76  ? 0.1489 0.1503 0.1920 0.0119  -0.0030 0.0030  82  ILE   C O   
1667 C CB  . ILE   B 76  ? 0.1748 0.1846 0.2163 0.0090  -0.0032 0.0031  82  ILE   C CB  
1668 C CG1 . ILE   B 76  ? 0.2051 0.2183 0.2457 0.0073  -0.0053 0.0047  82  ILE   C CG1 
1669 C CG2 . ILE   B 76  ? 0.2027 0.2133 0.2466 0.0096  0.0008  0.0000  82  ILE   C CG2 
1670 C CD1 . ILE   B 76  ? 0.2461 0.2601 0.2823 0.0054  -0.0036 0.0032  82  ILE   C CD1 
1671 N N   . PHE   B 77  ? 0.1779 0.1843 0.2337 0.0147  -0.0015 0.0015  83  PHE   C N   
1672 C CA  . PHE   B 77  ? 0.1915 0.1940 0.2485 0.0162  0.0009  -0.0008 83  PHE   C CA  
1673 C C   . PHE   B 77  ? 0.1960 0.1962 0.2459 0.0147  0.0043  -0.0039 83  PHE   C C   
1674 O O   . PHE   B 77  ? 0.2090 0.2116 0.2570 0.0136  0.0064  -0.0053 83  PHE   C O   
1675 C CB  . PHE   B 77  ? 0.2133 0.2181 0.2807 0.0188  0.0026  -0.0023 83  PHE   C CB  
1676 C CG  . PHE   B 77  ? 0.2429 0.2432 0.3119 0.0205  0.0054  -0.0051 83  PHE   C CG  
1677 C CD1 . PHE   B 77  ? 0.2829 0.2824 0.3499 0.0201  0.0102  -0.0092 83  PHE   C CD1 
1678 C CD2 . PHE   B 77  ? 0.2748 0.2708 0.3456 0.0219  0.0032  -0.0036 83  PHE   C CD2 
1679 C CE1 . PHE   B 77  ? 0.3006 0.2954 0.3680 0.0213  0.0128  -0.0121 83  PHE   C CE1 
1680 C CE2 . PHE   B 77  ? 0.3039 0.2952 0.3759 0.0232  0.0058  -0.0065 83  PHE   C CE2 
1681 C CZ  . PHE   B 77  ? 0.3027 0.2936 0.3730 0.0229  0.0106  -0.0109 83  PHE   C CZ  
1682 N N   . VAL   B 78  ? 0.1838 0.1791 0.2295 0.0145  0.0043  -0.0046 84  VAL   C N   
1683 C CA  . VAL   B 78  ? 0.1772 0.1696 0.2159 0.0131  0.0066  -0.0075 84  VAL   C CA  
1684 C C   . VAL   B 78  ? 0.1817 0.1697 0.2220 0.0144  0.0084  -0.0101 84  VAL   C C   
1685 O O   . VAL   B 78  ? 0.1879 0.1729 0.2303 0.0152  0.0068  -0.0092 84  VAL   C O   
1686 C CB  . VAL   B 78  ? 0.1581 0.1489 0.1901 0.0111  0.0043  -0.0061 84  VAL   C CB  
1687 C CG1 . VAL   B 78  ? 0.1705 0.1581 0.1958 0.0098  0.0055  -0.0088 84  VAL   C CG1 
1688 C CG2 . VAL   B 78  ? 0.1555 0.1501 0.1860 0.0099  0.0028  -0.0038 84  VAL   C CG2 
1689 N N   . GLU   B 79  ? 0.2214 0.2082 0.2592 0.0142  0.0120  -0.0136 85  GLU   C N   
1690 C CA  . GLU   B 79  ? 0.2338 0.2159 0.2713 0.0150  0.0143  -0.0169 85  GLU   C CA  
1691 C C   . GLU   B 79  ? 0.2163 0.1933 0.2486 0.0139  0.0122  -0.0172 85  GLU   C C   
1692 O O   . GLU   B 79  ? 0.2046 0.1817 0.2313 0.0120  0.0100  -0.0159 85  GLU   C O   
1693 C CB  . GLU   B 79  ? 0.2901 0.2713 0.3225 0.0140  0.0186  -0.0205 85  GLU   C CB  
1694 C CG  . GLU   B 79  ? 0.3635 0.3497 0.4003 0.0143  0.0214  -0.0207 85  GLU   C CG  
1695 C CD  . GLU   B 79  ? 0.4373 0.4247 0.4836 0.0167  0.0249  -0.0230 85  GLU   C CD  
1696 O OE1 . GLU   B 79  ? 0.4098 0.4021 0.4618 0.0171  0.0274  -0.0233 85  GLU   C OE1 
1697 O OE2 . GLU   B 79  ? 0.4673 0.4508 0.5162 0.0183  0.0253  -0.0246 85  GLU   C OE2 
1698 N N   . ALA   B 80  ? 0.2181 0.1907 0.2527 0.0150  0.0130  -0.0192 86  ALA   C N   
1699 C CA  . ALA   B 80  ? 0.2127 0.1803 0.2430 0.0137  0.0112  -0.0200 86  ALA   C CA  
1700 C C   . ALA   B 80  ? 0.1983 0.1641 0.2192 0.0114  0.0114  -0.0222 86  ALA   C C   
1701 O O   . ALA   B 80  ? 0.1984 0.1641 0.2152 0.0110  0.0143  -0.0246 86  ALA   C O   
1702 C CB  . ALA   B 80  ? 0.2330 0.1953 0.2668 0.0151  0.0128  -0.0227 86  ALA   C CB  
1703 N N   . SER   B 81  ? 0.1733 0.1374 0.1907 0.0097  0.0084  -0.0215 87  SER   C N   
1704 C CA  . SER   B 81  ? 0.1711 0.1328 0.1803 0.0076  0.0074  -0.0234 87  SER   C CA  
1705 C C   . SER   B 81  ? 0.1674 0.1249 0.1765 0.0066  0.0051  -0.0245 87  SER   C C   
1706 O O   . SER   B 81  ? 0.1899 0.1462 0.2051 0.0075  0.0049  -0.0236 87  SER   C O   
1707 C CB  . SER   B 81  ? 0.1790 0.1446 0.1855 0.0064  0.0051  -0.0208 87  SER   C CB  
1708 O OG  . SER   B 81  ? 0.1750 0.1426 0.1860 0.0063  0.0026  -0.0180 87  SER   C OG  
1709 N N   . GLU   B 82  ? 0.1809 0.1361 0.1837 0.0046  0.0028  -0.0260 88  GLU   C N   
1710 C CA  . GLU   B 82  ? 0.1973 0.1492 0.2010 0.0032  0.0002  -0.0270 88  GLU   C CA  
1711 C C   . GLU   B 82  ? 0.2051 0.1606 0.2148 0.0028  -0.0020 -0.0234 88  GLU   C C   
1712 O O   . GLU   B 82  ? 0.2040 0.1573 0.2169 0.0019  -0.0034 -0.0236 88  GLU   C O   
1713 C CB  . GLU   B 82  ? 0.2588 0.2075 0.2547 0.0011  -0.0022 -0.0295 88  GLU   C CB  
1714 C CG  . GLU   B 82  ? 0.3393 0.2913 0.3317 0.0003  -0.0046 -0.0277 88  GLU   C CG  
1715 C CD  . GLU   B 82  ? 0.4600 0.4120 0.4453 0.0004  -0.0028 -0.0281 88  GLU   C CD  
1716 O OE1 . GLU   B 82  ? 0.5062 0.4565 0.4846 -0.0010 -0.0055 -0.0287 88  GLU   C OE1 
1717 O OE2 . GLU   B 82  ? 0.4218 0.3755 0.4086 0.0019  0.0010  -0.0277 88  GLU   C OE2 
1718 N N   . TYR   B 83  ? 0.2003 0.1608 0.2112 0.0033  -0.0021 -0.0204 89  TYR   C N   
1719 C CA  . TYR   B 83  ? 0.1966 0.1604 0.2119 0.0027  -0.0036 -0.0173 89  TYR   C CA  
1720 C C   . TYR   B 83  ? 0.2008 0.1656 0.2214 0.0038  -0.0024 -0.0146 89  TYR   C C   
1721 O O   . TYR   B 83  ? 0.2379 0.2033 0.2617 0.0029  -0.0033 -0.0124 89  TYR   C O   
1722 C CB  . TYR   B 83  ? 0.1871 0.1552 0.2001 0.0024  -0.0044 -0.0158 89  TYR   C CB  
1723 C CG  . TYR   B 83  ? 0.1974 0.1643 0.2048 0.0014  -0.0063 -0.0178 89  TYR   C CG  
1724 C CD1 . TYR   B 83  ? 0.2156 0.1820 0.2237 -0.0002 -0.0093 -0.0186 89  TYR   C CD1 
1725 C CD2 . TYR   B 83  ? 0.1968 0.1630 0.1983 0.0018  -0.0052 -0.0189 89  TYR   C CD2 
1726 C CE1 . TYR   B 83  ? 0.2420 0.2069 0.2450 -0.0010 -0.0119 -0.0202 89  TYR   C CE1 
1727 C CE2 . TYR   B 83  ? 0.2384 0.2025 0.2336 0.0007  -0.0074 -0.0204 89  TYR   C CE2 
1728 C CZ  . TYR   B 83  ? 0.2661 0.2295 0.2619 -0.0006 -0.0111 -0.0209 89  TYR   C CZ  
1729 O OH  . TYR   B 83  ? 0.3332 0.2944 0.3230 -0.0016 -0.0141 -0.0220 89  TYR   C OH  
1730 N N   . TYR   B 84  ? 0.1720 0.1370 0.1937 0.0058  -0.0005 -0.0144 90  TYR   C N   
1731 C CA  . TYR   B 84  ? 0.1760 0.1421 0.2026 0.0071  -0.0001 -0.0114 90  TYR   C CA  
1732 C C   . TYR   B 84  ? 0.2036 0.1676 0.2333 0.0093  0.0018  -0.0127 90  TYR   C C   
1733 O O   . TYR   B 84  ? 0.2008 0.1647 0.2285 0.0101  0.0038  -0.0155 90  TYR   C O   
1734 C CB  . TYR   B 84  ? 0.1684 0.1398 0.1949 0.0075  -0.0002 -0.0087 90  TYR   C CB  
1735 C CG  . TYR   B 84  ? 0.1474 0.1215 0.1717 0.0057  -0.0015 -0.0072 90  TYR   C CG  
1736 C CD1 . TYR   B 84  ? 0.1483 0.1247 0.1688 0.0051  -0.0017 -0.0082 90  TYR   C CD1 
1737 C CD2 . TYR   B 84  ? 0.1398 0.1136 0.1658 0.0044  -0.0024 -0.0049 90  TYR   C CD2 
1738 C CE1 . TYR   B 84  ? 0.1492 0.1280 0.1687 0.0037  -0.0027 -0.0070 90  TYR   C CE1 
1739 C CE2 . TYR   B 84  ? 0.1406 0.1170 0.1653 0.0028  -0.0030 -0.0039 90  TYR   C CE2 
1740 C CZ  . TYR   B 84  ? 0.1362 0.1152 0.1581 0.0026  -0.0032 -0.0051 90  TYR   C CZ  
1741 O OH  . TYR   B 84  ? 0.1376 0.1190 0.1591 0.0013  -0.0037 -0.0044 90  TYR   C OH  
1742 N N   . PRO   B 85  ? 0.2304 0.1927 0.2652 0.0104  0.0013  -0.0105 91  PRO   C N   
1743 C CA  . PRO   B 85  ? 0.2290 0.1903 0.2685 0.0131  0.0029  -0.0113 91  PRO   C CA  
1744 C C   . PRO   B 85  ? 0.2211 0.1880 0.2621 0.0144  0.0036  -0.0101 91  PRO   C C   
1745 O O   . PRO   B 85  ? 0.1979 0.1688 0.2366 0.0133  0.0023  -0.0078 91  PRO   C O   
1746 C CB  . PRO   B 85  ? 0.2380 0.1964 0.2823 0.0138  0.0012  -0.0080 91  PRO   C CB  
1747 C CG  . PRO   B 85  ? 0.2509 0.2114 0.2925 0.0116  -0.0008 -0.0046 91  PRO   C CG  
1748 C CD  . PRO   B 85  ? 0.2353 0.1969 0.2717 0.0093  -0.0005 -0.0069 91  PRO   C CD  
1749 N N   . ALA   B 86  ? 0.2198 0.1871 0.2655 0.0167  0.0056  -0.0117 92  ALA   C N   
1750 C CA  . ALA   B 86  ? 0.2175 0.1903 0.2672 0.0181  0.0061  -0.0105 92  ALA   C CA  
1751 C C   . ALA   B 86  ? 0.2148 0.1896 0.2673 0.0182  0.0024  -0.0054 92  ALA   C C   
1752 O O   . ALA   B 86  ? 0.2266 0.1975 0.2810 0.0186  0.0006  -0.0034 92  ALA   C O   
1753 C CB  . ALA   B 86  ? 0.2347 0.2069 0.2918 0.0209  0.0086  -0.0128 92  ALA   C CB  
1754 N N   . ARG   B 87  ? 0.2079 0.1877 0.2586 0.0173  0.0013  -0.0033 93  ARG   C N   
1755 C CA  . ARG   B 87  ? 0.1992 0.1800 0.2500 0.0167  -0.0022 0.0012  93  ARG   C CA  
1756 C C   . ARG   B 87  ? 0.1949 0.1814 0.2446 0.0160  -0.0030 0.0025  93  ARG   C C   
1757 O O   . ARG   B 87  ? 0.1981 0.1874 0.2464 0.0156  -0.0008 0.0001  93  ARG   C O   
1758 C CB  . ARG   B 87  ? 0.1974 0.1751 0.2421 0.0142  -0.0031 0.0023  93  ARG   C CB  
1759 C CG  . ARG   B 87  ? 0.1541 0.1345 0.1924 0.0120  -0.0022 0.0010  93  ARG   C CG  
1760 C CD  . ARG   B 87  ? 0.1730 0.1504 0.2073 0.0100  -0.0022 0.0002  93  ARG   C CD  
1761 N NE  . ARG   B 87  ? 0.1461 0.1261 0.1760 0.0079  -0.0026 0.0009  93  ARG   C NE  
1762 C CZ  . ARG   B 87  ? 0.1455 0.1281 0.1723 0.0073  -0.0019 -0.0008 93  ARG   C CZ  
1763 N NH1 . ARG   B 87  ? 0.1301 0.1145 0.1539 0.0057  -0.0024 -0.0001 93  ARG   C NH1 
1764 N NH2 . ARG   B 87  ? 0.1482 0.1313 0.1751 0.0084  -0.0005 -0.0032 93  ARG   C NH2 
1765 N N   . TYR   B 88  ? 0.1972 0.1847 0.2466 0.0155  -0.0061 0.0063  94  TYR   C N   
1766 C CA  . TYR   B 88  ? 0.2016 0.1937 0.2486 0.0142  -0.0072 0.0075  94  TYR   C CA  
1767 C C   . TYR   B 88  ? 0.1668 0.1578 0.2057 0.0114  -0.0071 0.0079  94  TYR   C C   
1768 O O   . TYR   B 88  ? 0.1780 0.1656 0.2142 0.0104  -0.0082 0.0099  94  TYR   C O   
1769 C CB  . TYR   B 88  ? 0.2233 0.2166 0.2732 0.0148  -0.0110 0.0113  94  TYR   C CB  
1770 C CG  . TYR   B 88  ? 0.2558 0.2518 0.3153 0.0176  -0.0115 0.0109  94  TYR   C CG  
1771 C CD1 . TYR   B 88  ? 0.2701 0.2718 0.3331 0.0177  -0.0112 0.0099  94  TYR   C CD1 
1772 C CD2 . TYR   B 88  ? 0.2934 0.2863 0.3593 0.0201  -0.0119 0.0111  94  TYR   C CD2 
1773 C CE1 . TYR   B 88  ? 0.3047 0.3098 0.3781 0.0202  -0.0114 0.0093  94  TYR   C CE1 
1774 C CE2 . TYR   B 88  ? 0.3079 0.3038 0.3843 0.0230  -0.0121 0.0103  94  TYR   C CE2 
1775 C CZ  . TYR   B 88  ? 0.3249 0.3272 0.4052 0.0230  -0.0116 0.0093  94  TYR   C CZ  
1776 O OH  . TYR   B 88  ? 0.3677 0.3738 0.4598 0.0258  -0.0116 0.0084  94  TYR   C OH  
1777 N N   . GLN   B 89  ? 0.1283 0.1219 0.1638 0.0102  -0.0055 0.0060  95  GLN   C N   
1778 C CA  . GLN   B 89  ? 0.1191 0.1124 0.1484 0.0078  -0.0055 0.0063  95  GLN   C CA  
1779 C C   . GLN   B 89  ? 0.1214 0.1174 0.1487 0.0067  -0.0073 0.0085  95  GLN   C C   
1780 O O   . GLN   B 89  ? 0.1322 0.1316 0.1618 0.0071  -0.0077 0.0083  95  GLN   C O   
1781 C CB  . GLN   B 89  ? 0.1281 0.1219 0.1546 0.0073  -0.0033 0.0032  95  GLN   C CB  
1782 C CG  . GLN   B 89  ? 0.1212 0.1152 0.1428 0.0053  -0.0034 0.0033  95  GLN   C CG  
1783 C CD  . GLN   B 89  ? 0.1178 0.1108 0.1369 0.0049  -0.0021 0.0005  95  GLN   C CD  
1784 O OE1 . GLN   B 89  ? 0.1249 0.1155 0.1446 0.0056  -0.0015 -0.0012 95  GLN   C OE1 
1785 N NE2 . GLN   B 89  ? 0.1078 0.1021 0.1237 0.0038  -0.0021 0.0002  95  GLN   C NE2 
1786 N N   . SER   B 90  ? 0.1142 0.1084 0.1372 0.0050  -0.0082 0.0105  96  SER   C N   
1787 C CA  . SER   B 90  ? 0.1087 0.1043 0.1281 0.0034  -0.0099 0.0124  96  SER   C CA  
1788 C C   . SER   B 90  ? 0.1095 0.1068 0.1247 0.0017  -0.0083 0.0106  96  SER   C C   
1789 O O   . SER   B 90  ? 0.1124 0.1092 0.1270 0.0016  -0.0063 0.0084  96  SER   C O   
1790 C CB  . SER   B 90  ? 0.1312 0.1234 0.1472 0.0021  -0.0113 0.0155  96  SER   C CB  
1791 O OG  . SER   B 90  ? 0.1649 0.1547 0.1781 0.0008  -0.0090 0.0146  96  SER   C OG  
1792 N N   . HIS   B 91  ? 0.1111 0.1102 0.1236 0.0005  -0.0096 0.0116  97  HIS   C N   
1793 C CA  . HIS   B 91  ? 0.1094 0.1095 0.1178 -0.0012 -0.0082 0.0100  97  HIS   C CA  
1794 C C   . HIS   B 91  ? 0.1176 0.1193 0.1280 -0.0004 -0.0066 0.0074  97  HIS   C C   
1795 O O   . HIS   B 91  ? 0.1147 0.1160 0.1226 -0.0012 -0.0051 0.0058  97  HIS   C O   
1796 C CB  . HIS   B 91  ? 0.1277 0.1253 0.1319 -0.0028 -0.0066 0.0099  97  HIS   C CB  
1797 C CG  . HIS   B 91  ? 0.1306 0.1257 0.1309 -0.0043 -0.0077 0.0127  97  HIS   C CG  
1798 N ND1 . HIS   B 91  ? 0.1671 0.1620 0.1617 -0.0064 -0.0081 0.0133  97  HIS   C ND1 
1799 C CD2 . HIS   B 91  ? 0.1482 0.1405 0.1489 -0.0040 -0.0086 0.0149  97  HIS   C CD2 
1800 C CE1 . HIS   B 91  ? 0.1778 0.1696 0.1686 -0.0076 -0.0091 0.0160  97  HIS   C CE1 
1801 N NE2 . HIS   B 91  ? 0.1764 0.1665 0.1710 -0.0062 -0.0096 0.0173  97  HIS   C NE2 
1802 N N   . LEU   B 92  ? 0.1063 0.1097 0.1212 0.0011  -0.0067 0.0069  98  LEU   C N   
1803 C CA  . LEU   B 92  ? 0.1011 0.1053 0.1169 0.0017  -0.0048 0.0046  98  LEU   C CA  
1804 C C   . LEU   B 92  ? 0.1114 0.1186 0.1281 0.0009  -0.0050 0.0044  98  LEU   C C   
1805 O O   . LEU   B 92  ? 0.1127 0.1222 0.1324 0.0010  -0.0068 0.0057  98  LEU   C O   
1806 C CB  . LEU   B 92  ? 0.1147 0.1182 0.1347 0.0036  -0.0039 0.0037  98  LEU   C CB  
1807 C CG  . LEU   B 92  ? 0.1278 0.1311 0.1475 0.0039  -0.0016 0.0013  98  LEU   C CG  
1808 C CD1 . LEU   B 92  ? 0.1367 0.1372 0.1516 0.0032  -0.0010 0.0000  98  LEU   C CD1 
1809 C CD2 . LEU   B 92  ? 0.1758 0.1780 0.1994 0.0057  -0.0003 0.0001  98  LEU   C CD2 
1810 N N   . MET   B 93  ? 0.1046 0.1115 0.1187 0.0002  -0.0035 0.0028  99  MET   C N   
1811 C CA  . MET   B 93  ? 0.1034 0.1126 0.1179 -0.0010 -0.0033 0.0023  99  MET   C CA  
1812 C C   . MET   B 93  ? 0.1092 0.1182 0.1244 -0.0006 -0.0009 0.0007  99  MET   C C   
1813 O O   . MET   B 93  ? 0.1213 0.1273 0.1333 -0.0003 0.0002  -0.0004 99  MET   C O   
1814 C CB  . MET   B 93  ? 0.1019 0.1099 0.1115 -0.0027 -0.0035 0.0020  99  MET   C CB  
1815 C CG  . MET   B 93  ? 0.1161 0.1238 0.1236 -0.0035 -0.0052 0.0034  99  MET   C CG  
1816 S SD  . MET   B 93  ? 0.1444 0.1500 0.1464 -0.0052 -0.0046 0.0024  99  MET   C SD  
1817 C CE  . MET   B 93  ? 0.1577 0.1607 0.1592 -0.0040 -0.0028 0.0010  99  MET   C CE  
1818 N N   . LEU   B 94  ? 0.0924 0.1043 0.1116 -0.0009 0.0000  0.0003  100 LEU   C N   
1819 C CA  . LEU   B 94  ? 0.0866 0.0978 0.1056 -0.0010 0.0030  -0.0013 100 LEU   C CA  
1820 C C   . LEU   B 94  ? 0.0943 0.1057 0.1110 -0.0031 0.0040  -0.0017 100 LEU   C C   
1821 O O   . LEU   B 94  ? 0.0925 0.1063 0.1107 -0.0044 0.0026  -0.0010 100 LEU   C O   
1822 C CB  . LEU   B 94  ? 0.1112 0.1254 0.1374 0.0002  0.0046  -0.0020 100 LEU   C CB  
1823 C CG  . LEU   B 94  ? 0.1224 0.1362 0.1520 0.0024  0.0038  -0.0017 100 LEU   C CG  
1824 C CD1 . LEU   B 94  ? 0.1561 0.1730 0.1941 0.0038  0.0058  -0.0027 100 LEU   C CD1 
1825 C CD2 . LEU   B 94  ? 0.1433 0.1524 0.1675 0.0030  0.0047  -0.0026 100 LEU   C CD2 
1826 N N   . ALA   B 95  ? 0.0958 0.1041 0.1082 -0.0037 0.0064  -0.0028 101 ALA   C N   
1827 C CA  . ALA   B 95  ? 0.1015 0.1091 0.1114 -0.0059 0.0080  -0.0031 101 ALA   C CA  
1828 C C   . ALA   B 95  ? 0.0987 0.1048 0.1074 -0.0062 0.0117  -0.0044 101 ALA   C C   
1829 O O   . ALA   B 95  ? 0.1139 0.1183 0.1216 -0.0049 0.0128  -0.0053 101 ALA   C O   
1830 C CB  . ALA   B 95  ? 0.1159 0.1189 0.1188 -0.0066 0.0068  -0.0028 101 ALA   C CB  
1831 N N   . VAL   B 96  ? 0.1064 0.1132 0.1153 -0.0084 0.0141  -0.0047 102 VAL   C N   
1832 C CA  . VAL   B 96  ? 0.1109 0.1152 0.1165 -0.0094 0.0182  -0.0059 102 VAL   C CA  
1833 C C   . VAL   B 96  ? 0.1372 0.1345 0.1324 -0.0102 0.0177  -0.0054 102 VAL   C C   
1834 O O   . VAL   B 96  ? 0.1557 0.1509 0.1477 -0.0117 0.0164  -0.0044 102 VAL   C O   
1835 C CB  . VAL   B 96  ? 0.1193 0.1271 0.1297 -0.0118 0.0212  -0.0063 102 VAL   C CB  
1836 C CG1 . VAL   B 96  ? 0.1401 0.1449 0.1463 -0.0134 0.0264  -0.0076 102 VAL   C CG1 
1837 C CG2 . VAL   B 96  ? 0.1451 0.1603 0.1673 -0.0106 0.0208  -0.0067 102 VAL   C CG2 
1838 N N   . GLY   B 97  ? 0.1395 0.1330 0.1297 -0.0092 0.0182  -0.0062 103 GLY   C N   
1839 C CA  . GLY   B 97  ? 0.1775 0.1642 0.1580 -0.0098 0.0167  -0.0055 103 GLY   C CA  
1840 C C   . GLY   B 97  ? 0.1871 0.1702 0.1628 -0.0088 0.0168  -0.0066 103 GLY   C C   
1841 O O   . GLY   B 97  ? 0.1897 0.1754 0.1699 -0.0073 0.0177  -0.0079 103 GLY   C O   
1842 N N   . HIS   B 98  ? 0.1822 0.1588 0.1487 -0.0095 0.0154  -0.0061 104 HIS   C N   
1843 C CA  . HIS   B 98  ? 0.1894 0.1618 0.1500 -0.0090 0.0149  -0.0072 104 HIS   C CA  
1844 C C   . HIS   B 98  ? 0.1797 0.1525 0.1425 -0.0068 0.0105  -0.0071 104 HIS   C C   
1845 O O   . HIS   B 98  ? 0.1743 0.1472 0.1384 -0.0061 0.0070  -0.0058 104 HIS   C O   
1846 C CB  . HIS   B 98  ? 0.2064 0.1710 0.1552 -0.0109 0.0144  -0.0063 104 HIS   C CB  
1847 C CG  . HIS   B 98  ? 0.2086 0.1680 0.1497 -0.0108 0.0135  -0.0075 104 HIS   C CG  
1848 N ND1 . HIS   B 98  ? 0.2488 0.2077 0.1880 -0.0114 0.0179  -0.0099 104 HIS   C ND1 
1849 C CD2 . HIS   B 98  ? 0.2116 0.1665 0.1474 -0.0101 0.0087  -0.0070 104 HIS   C CD2 
1850 C CE1 . HIS   B 98  ? 0.2537 0.2073 0.1855 -0.0113 0.0155  -0.0107 104 HIS   C CE1 
1851 N NE2 . HIS   B 98  ? 0.2510 0.2023 0.1807 -0.0106 0.0097  -0.0089 104 HIS   C NE2 
1852 N N   . SER   B 99  ? 0.1790 0.1514 0.1420 -0.0058 0.0109  -0.0088 105 SER   C N   
1853 C CA  . SER   B 99  ? 0.1937 0.1654 0.1577 -0.0043 0.0071  -0.0090 105 SER   C CA  
1854 C C   . SER   B 99  ? 0.2134 0.1815 0.1730 -0.0043 0.0081  -0.0112 105 SER   C C   
1855 O O   . SER   B 99  ? 0.2461 0.2146 0.2059 -0.0046 0.0124  -0.0129 105 SER   C O   
1856 C CB  . SER   B 99  ? 0.2210 0.1983 0.1945 -0.0026 0.0059  -0.0085 105 SER   C CB  
1857 O OG  . SER   B 99  ? 0.2517 0.2323 0.2306 -0.0019 0.0089  -0.0095 105 SER   C OG  
1858 N N   . GLU   B 100 ? 0.1871 0.1519 0.1433 -0.0039 0.0042  -0.0114 106 GLU   C N   
1859 C CA  . GLU   B 100 ? 0.2167 0.1775 0.1683 -0.0041 0.0037  -0.0136 106 GLU   C CA  
1860 C C   . GLU   B 100 ? 0.2279 0.1906 0.1854 -0.0026 -0.0002 -0.0135 106 GLU   C C   
1861 O O   . GLU   B 100 ? 0.2393 0.2051 0.2021 -0.0019 -0.0026 -0.0118 106 GLU   C O   
1862 C CB  . GLU   B 100 ? 0.2841 0.2377 0.2237 -0.0058 0.0015  -0.0134 106 GLU   C CB  
1863 C CG  . GLU   B 100 ? 0.3296 0.2806 0.2623 -0.0077 0.0060  -0.0135 106 GLU   C CG  
1864 C CD  . GLU   B 100 ? 0.3269 0.2698 0.2460 -0.0098 0.0041  -0.0130 106 GLU   C CD  
1865 O OE1 . GLU   B 100 ? 0.3976 0.3361 0.3111 -0.0100 0.0006  -0.0140 106 GLU   C OE1 
1866 O OE2 . GLU   B 100 ? 0.3373 0.2778 0.2510 -0.0114 0.0059  -0.0115 106 GLU   C OE2 
1867 N N   . PRO   B 101 ? 0.2538 0.2147 0.2112 -0.0023 -0.0005 -0.0157 107 PRO   C N   
1868 C CA  . PRO   B 101 ? 0.2513 0.2150 0.2165 -0.0011 -0.0034 -0.0155 107 PRO   C CA  
1869 C C   . PRO   B 101 ? 0.2244 0.1887 0.1913 -0.0010 -0.0083 -0.0140 107 PRO   C C   
1870 O O   . PRO   B 101 ? 0.2438 0.2124 0.2188 -0.0001 -0.0093 -0.0129 107 PRO   C O   
1871 C CB  . PRO   B 101 ? 0.2758 0.2356 0.2381 -0.0015 -0.0033 -0.0183 107 PRO   C CB  
1872 C CG  . PRO   B 101 ? 0.2934 0.2510 0.2508 -0.0020 0.0018  -0.0200 107 PRO   C CG  
1873 C CD  . PRO   B 101 ? 0.2694 0.2266 0.2214 -0.0031 0.0028  -0.0184 107 PRO   C CD  
1874 N N   . GLY   B 102 ? 0.2015 0.1613 0.1606 -0.0020 -0.0113 -0.0139 108 GLY   C N   
1875 C CA  . GLY   B 102 ? 0.2090 0.1685 0.1692 -0.0018 -0.0162 -0.0126 108 GLY   C CA  
1876 C C   . GLY   B 102 ? 0.1865 0.1497 0.1514 -0.0010 -0.0158 -0.0104 108 GLY   C C   
1877 O O   . GLY   B 102 ? 0.1914 0.1555 0.1599 -0.0004 -0.0193 -0.0095 108 GLY   C O   
1878 N N   . ASP   B 103 ? 0.1758 0.1411 0.1414 -0.0011 -0.0116 -0.0098 109 ASP   C N   
1879 C CA  . ASP   B 103 ? 0.1605 0.1292 0.1303 -0.0006 -0.0109 -0.0081 109 ASP   C CA  
1880 C C   . ASP   B 103 ? 0.1371 0.1112 0.1162 0.0003  -0.0103 -0.0079 109 ASP   C C   
1881 O O   . ASP   B 103 ? 0.1434 0.1199 0.1258 0.0006  -0.0103 -0.0068 109 ASP   C O   
1882 C CB  . ASP   B 103 ? 0.1678 0.1366 0.1346 -0.0015 -0.0069 -0.0076 109 ASP   C CB  
1883 C CG  . ASP   B 103 ? 0.2003 0.1633 0.1573 -0.0029 -0.0071 -0.0072 109 ASP   C CG  
1884 O OD1 . ASP   B 103 ? 0.2010 0.1603 0.1544 -0.0029 -0.0111 -0.0064 109 ASP   C OD1 
1885 O OD2 . ASP   B 103 ? 0.1968 0.1587 0.1498 -0.0041 -0.0033 -0.0076 109 ASP   C OD2 
1886 N N   . CYS   B 104 ? 0.1344 0.1100 0.1173 0.0007  -0.0099 -0.0090 110 CYS   C N   
1887 C CA  . CYS   B 104 ? 0.1301 0.1100 0.1206 0.0013  -0.0093 -0.0084 110 CYS   C CA  
1888 C C   . CYS   B 104 ? 0.1404 0.1215 0.1347 0.0015  -0.0118 -0.0081 110 CYS   C C   
1889 O O   . CYS   B 104 ? 0.1544 0.1333 0.1477 0.0016  -0.0151 -0.0086 110 CYS   C O   
1890 C CB  . CYS   B 104 ? 0.1338 0.1140 0.1272 0.0015  -0.0088 -0.0095 110 CYS   C CB  
1891 S SG  . CYS   B 104 ? 0.1792 0.1594 0.1718 0.0018  -0.0050 -0.0099 110 CYS   C SG  
1892 N N   . GLY   B 105 ? 0.1218 0.1063 0.1204 0.0017  -0.0104 -0.0072 111 GLY   C N   
1893 C CA  . GLY   B 105 ? 0.1330 0.1190 0.1360 0.0020  -0.0119 -0.0072 111 GLY   C CA  
1894 C C   . GLY   B 105 ? 0.1398 0.1251 0.1409 0.0022  -0.0121 -0.0065 111 GLY   C C   
1895 O O   . GLY   B 105 ? 0.1467 0.1336 0.1521 0.0025  -0.0123 -0.0066 111 GLY   C O   
1896 N N   . GLY   B 106 ? 0.1172 0.0998 0.1121 0.0018  -0.0117 -0.0059 112 GLY   C N   
1897 C CA  . GLY   B 106 ? 0.1200 0.1014 0.1128 0.0017  -0.0116 -0.0052 112 GLY   C CA  
1898 C C   . GLY   B 106 ? 0.1132 0.0979 0.1093 0.0014  -0.0092 -0.0049 112 GLY   C C   
1899 O O   . GLY   B 106 ? 0.1219 0.1091 0.1187 0.0009  -0.0071 -0.0048 112 GLY   C O   
1900 N N   . ILE   B 107 ? 0.1160 0.1005 0.1139 0.0017  -0.0096 -0.0050 113 ILE   C N   
1901 C CA  . ILE   B 107 ? 0.1222 0.1094 0.1224 0.0011  -0.0073 -0.0052 113 ILE   C CA  
1902 C C   . ILE   B 107 ? 0.1140 0.1006 0.1104 0.0000  -0.0058 -0.0045 113 ILE   C C   
1903 O O   . ILE   B 107 ? 0.1273 0.1106 0.1201 -0.0002 -0.0066 -0.0040 113 ILE   C O   
1904 C CB  . ILE   B 107 ? 0.1676 0.1549 0.1723 0.0019  -0.0078 -0.0061 113 ILE   C CB  
1905 C CG1 . ILE   B 107 ? 0.2182 0.2080 0.2287 0.0024  -0.0079 -0.0070 113 ILE   C CG1 
1906 C CG2 . ILE   B 107 ? 0.1925 0.1808 0.1974 0.0011  -0.0053 -0.0066 113 ILE   C CG2 
1907 C CD1 . ILE   B 107 ? 0.2635 0.2539 0.2802 0.0034  -0.0082 -0.0084 113 ILE   C CD1 
1908 N N   . LEU   B 108 ? 0.1044 0.0939 0.1016 -0.0008 -0.0040 -0.0043 114 LEU   C N   
1909 C CA  . LEU   B 108 ? 0.0968 0.0866 0.0918 -0.0022 -0.0028 -0.0040 114 LEU   C CA  
1910 C C   . LEU   B 108 ? 0.1024 0.0925 0.0987 -0.0026 -0.0021 -0.0048 114 LEU   C C   
1911 O O   . LEU   B 108 ? 0.1084 0.1005 0.1068 -0.0026 -0.0014 -0.0053 114 LEU   C O   
1912 C CB  . LEU   B 108 ? 0.1031 0.0959 0.0987 -0.0028 -0.0019 -0.0033 114 LEU   C CB  
1913 C CG  . LEU   B 108 ? 0.1041 0.0984 0.0989 -0.0043 -0.0011 -0.0030 114 LEU   C CG  
1914 C CD1 . LEU   B 108 ? 0.1235 0.1158 0.1160 -0.0052 -0.0007 -0.0028 114 LEU   C CD1 
1915 C CD2 . LEU   B 108 ? 0.1255 0.1233 0.1224 -0.0045 -0.0010 -0.0021 114 LEU   C CD2 
1916 N N   . ARG   B 109 ? 0.1028 0.0906 0.0973 -0.0033 -0.0020 -0.0051 115 ARG   C N   
1917 C CA  . ARG   B 109 ? 0.1148 0.1021 0.1100 -0.0038 -0.0011 -0.0064 115 ARG   C CA  
1918 C C   . ARG   B 109 ? 0.1243 0.1113 0.1168 -0.0057 -0.0004 -0.0064 115 ARG   C C   
1919 O O   . ARG   B 109 ? 0.1447 0.1302 0.1352 -0.0064 -0.0008 -0.0056 115 ARG   C O   
1920 C CB  . ARG   B 109 ? 0.1495 0.1333 0.1461 -0.0025 -0.0019 -0.0072 115 ARG   C CB  
1921 C CG  . ARG   B 109 ? 0.2220 0.2061 0.2225 -0.0006 -0.0031 -0.0076 115 ARG   C CG  
1922 C CD  . ARG   B 109 ? 0.2855 0.2659 0.2879 0.0008  -0.0046 -0.0081 115 ARG   C CD  
1923 N NE  . ARG   B 109 ? 0.3823 0.3631 0.3877 0.0008  -0.0026 -0.0101 115 ARG   C NE  
1924 C CZ  . ARG   B 109 ? 0.4383 0.4213 0.4493 0.0017  -0.0015 -0.0117 115 ARG   C CZ  
1925 N NH1 . ARG   B 109 ? 0.4670 0.4518 0.4819 0.0030  -0.0031 -0.0113 115 ARG   C NH1 
1926 N NH2 . ARG   B 109 ? 0.4627 0.4461 0.4754 0.0012  0.0013  -0.0138 115 ARG   C NH2 
1927 N N   . CYS   B 110 ? 0.1151 0.1029 0.1069 -0.0069 0.0006  -0.0075 116 CYS   C N   
1928 C CA  . CYS   B 110 ? 0.1292 0.1162 0.1184 -0.0090 0.0009  -0.0079 116 CYS   C CA  
1929 C C   . CYS   B 110 ? 0.1588 0.1426 0.1478 -0.0091 0.0019  -0.0100 116 CYS   C C   
1930 O O   . CYS   B 110 ? 0.1440 0.1265 0.1356 -0.0073 0.0023  -0.0109 116 CYS   C O   
1931 C CB  . CYS   B 110 ? 0.1169 0.1072 0.1048 -0.0107 0.0008  -0.0076 116 CYS   C CB  
1932 S SG  . CYS   B 110 ? 0.1144 0.1050 0.1011 -0.0109 0.0022  -0.0088 116 CYS   C SG  
1933 N N   . GLN   B 111 ? 0.1643 0.1467 0.1506 -0.0112 0.0023  -0.0110 117 GLN   C N   
1934 C CA  . GLN   B 111 ? 0.1832 0.1620 0.1691 -0.0114 0.0036  -0.0134 117 GLN   C CA  
1935 C C   . GLN   B 111 ? 0.1733 0.1529 0.1600 -0.0108 0.0056  -0.0152 117 GLN   C C   
1936 O O   . GLN   B 111 ? 0.2193 0.1961 0.2073 -0.0102 0.0073  -0.0176 117 GLN   C O   
1937 C CB  . GLN   B 111 ? 0.2180 0.1951 0.2005 -0.0142 0.0035  -0.0144 117 GLN   C CB  
1938 C CG  . GLN   B 111 ? 0.2356 0.2157 0.2149 -0.0164 0.0034  -0.0146 117 GLN   C CG  
1939 C CD  . GLN   B 111 ? 0.3514 0.3298 0.3276 -0.0194 0.0028  -0.0157 117 GLN   C CD  
1940 O OE1 . GLN   B 111 ? 0.3796 0.3607 0.3557 -0.0210 0.0009  -0.0143 117 GLN   C OE1 
1941 N NE2 . GLN   B 111 ? 0.3829 0.3572 0.3571 -0.0202 0.0043  -0.0185 117 GLN   C NE2 
1942 N N   . HIS   B 112 ? 0.1525 0.1357 0.1386 -0.0111 0.0058  -0.0143 118 HIS   C N   
1943 C CA  . HIS   B 112 ? 0.1570 0.1407 0.1429 -0.0113 0.0082  -0.0158 118 HIS   C CA  
1944 C C   . HIS   B 112 ? 0.1721 0.1573 0.1633 -0.0089 0.0088  -0.0156 118 HIS   C C   
1945 O O   . HIS   B 112 ? 0.1953 0.1811 0.1875 -0.0091 0.0114  -0.0171 118 HIS   C O   
1946 C CB  . HIS   B 112 ? 0.1516 0.1373 0.1326 -0.0135 0.0080  -0.0148 118 HIS   C CB  
1947 C CG  . HIS   B 112 ? 0.1531 0.1377 0.1290 -0.0161 0.0068  -0.0151 118 HIS   C CG  
1948 N ND1 . HIS   B 112 ? 0.1402 0.1271 0.1157 -0.0168 0.0039  -0.0128 118 HIS   C ND1 
1949 C CD2 . HIS   B 112 ? 0.1852 0.1668 0.1569 -0.0181 0.0080  -0.0176 118 HIS   C CD2 
1950 C CE1 . HIS   B 112 ? 0.1613 0.1468 0.1328 -0.0193 0.0030  -0.0138 118 HIS   C CE1 
1951 N NE2 . HIS   B 112 ? 0.1924 0.1744 0.1610 -0.0203 0.0054  -0.0168 118 HIS   C NE2 
1952 N N   . GLY   B 113 ? 0.1475 0.1336 0.1419 -0.0071 0.0066  -0.0138 119 GLY   C N   
1953 C CA  . GLY   B 113 ? 0.1397 0.1273 0.1392 -0.0052 0.0065  -0.0135 119 GLY   C CA  
1954 C C   . GLY   B 113 ? 0.1262 0.1159 0.1258 -0.0046 0.0044  -0.0111 119 GLY   C C   
1955 O O   . GLY   B 113 ? 0.1267 0.1163 0.1236 -0.0052 0.0028  -0.0096 119 GLY   C O   
1956 N N   . VAL   B 114 ? 0.1221 0.1136 0.1253 -0.0037 0.0047  -0.0109 120 VAL   C N   
1957 C CA  . VAL   B 114 ? 0.1121 0.1051 0.1157 -0.0031 0.0028  -0.0090 120 VAL   C CA  
1958 C C   . VAL   B 114 ? 0.1062 0.1007 0.1063 -0.0046 0.0031  -0.0075 120 VAL   C C   
1959 O O   . VAL   B 114 ? 0.1207 0.1160 0.1195 -0.0059 0.0048  -0.0078 120 VAL   C O   
1960 C CB  . VAL   B 114 ? 0.1277 0.1220 0.1367 -0.0020 0.0029  -0.0096 120 VAL   C CB  
1961 C CG1 . VAL   B 114 ? 0.1439 0.1392 0.1528 -0.0016 0.0013  -0.0079 120 VAL   C CG1 
1962 C CG2 . VAL   B 114 ? 0.1517 0.1445 0.1651 -0.0001 0.0015  -0.0107 120 VAL   C CG2 
1963 N N   . VAL   B 115 ? 0.1089 0.1038 0.1075 -0.0045 0.0014  -0.0060 121 VAL   C N   
1964 C CA  . VAL   B 115 ? 0.1033 0.0998 0.0999 -0.0054 0.0010  -0.0045 121 VAL   C CA  
1965 C C   . VAL   B 115 ? 0.1093 0.1069 0.1082 -0.0045 0.0005  -0.0034 121 VAL   C C   
1966 O O   . VAL   B 115 ? 0.1131 0.1116 0.1113 -0.0051 0.0006  -0.0022 121 VAL   C O   
1967 C CB  . VAL   B 115 ? 0.1009 0.0977 0.0960 -0.0059 -0.0001 -0.0038 121 VAL   C CB  
1968 C CG1 . VAL   B 115 ? 0.1090 0.1081 0.1041 -0.0064 -0.0010 -0.0022 121 VAL   C CG1 
1969 C CG2 . VAL   B 115 ? 0.1163 0.1118 0.1091 -0.0073 0.0004  -0.0049 121 VAL   C CG2 
1970 N N   . GLY   B 116 ? 0.1007 0.0977 0.1016 -0.0031 -0.0003 -0.0037 122 GLY   C N   
1971 C CA  . GLY   B 116 ? 0.1166 0.1139 0.1193 -0.0023 -0.0009 -0.0030 122 GLY   C CA  
1972 C C   . GLY   B 116 ? 0.1041 0.1000 0.1075 -0.0011 -0.0020 -0.0036 122 GLY   C C   
1973 O O   . GLY   B 116 ? 0.1082 0.1026 0.1111 -0.0008 -0.0026 -0.0044 122 GLY   C O   
1974 N N   . ILE   B 117 ? 0.1043 0.1000 0.1086 -0.0005 -0.0026 -0.0034 123 ILE   C N   
1975 C CA  . ILE   B 117 ? 0.1051 0.0988 0.1089 0.0003  -0.0039 -0.0041 123 ILE   C CA  
1976 C C   . ILE   B 117 ? 0.1089 0.1020 0.1109 0.0006  -0.0037 -0.0039 123 ILE   C C   
1977 O O   . ILE   B 117 ? 0.1086 0.1030 0.1120 0.0006  -0.0028 -0.0032 123 ILE   C O   
1978 C CB  . ILE   B 117 ? 0.1244 0.1178 0.1316 0.0007  -0.0049 -0.0049 123 ILE   C CB  
1979 C CG1 . ILE   B 117 ? 0.1290 0.1237 0.1385 0.0003  -0.0039 -0.0043 123 ILE   C CG1 
1980 C CG2 . ILE   B 117 ? 0.1392 0.1332 0.1493 0.0008  -0.0052 -0.0057 123 ILE   C CG2 
1981 C CD1 . ILE   B 117 ? 0.1444 0.1389 0.1579 0.0003  -0.0048 -0.0053 123 ILE   C CD1 
1982 N N   . VAL   B 118 ? 0.0960 0.0865 0.0948 0.0008  -0.0043 -0.0045 124 VAL   C N   
1983 C CA  . VAL   B 118 ? 0.0993 0.0888 0.0961 0.0009  -0.0033 -0.0048 124 VAL   C CA  
1984 C C   . VAL   B 118 ? 0.1005 0.0900 0.0999 0.0015  -0.0035 -0.0053 124 VAL   C C   
1985 O O   . VAL   B 118 ? 0.1084 0.0969 0.1089 0.0016  -0.0051 -0.0059 124 VAL   C O   
1986 C CB  . VAL   B 118 ? 0.1065 0.0922 0.0979 0.0006  -0.0040 -0.0054 124 VAL   C CB  
1987 C CG1 . VAL   B 118 ? 0.1202 0.1046 0.1092 0.0005  -0.0023 -0.0063 124 VAL   C CG1 
1988 C CG2 . VAL   B 118 ? 0.1284 0.1134 0.1171 -0.0001 -0.0036 -0.0047 124 VAL   C CG2 
1989 N N   . SER   B 119 ? 0.1015 0.0922 0.1026 0.0018  -0.0020 -0.0051 125 SER   C N   
1990 C CA  . SER   B 119 ? 0.0910 0.0811 0.0947 0.0024  -0.0019 -0.0055 125 SER   C CA  
1991 C C   . SER   B 119 ? 0.1107 0.0995 0.1138 0.0030  -0.0003 -0.0066 125 SER   C C   
1992 O O   . SER   B 119 ? 0.1234 0.1102 0.1273 0.0035  -0.0004 -0.0078 125 SER   C O   
1993 C CB  . SER   B 119 ? 0.1045 0.0970 0.1121 0.0025  -0.0019 -0.0038 125 SER   C CB  
1994 O OG  . SER   B 119 ? 0.1121 0.1036 0.1224 0.0030  -0.0019 -0.0037 125 SER   C OG  
1995 N N   . THR   B 120 ? 0.1217 0.1118 0.1243 0.0030  0.0015  -0.0067 126 THR   C N   
1996 C CA  . THR   B 120 ? 0.1361 0.1254 0.1391 0.0036  0.0039  -0.0082 126 THR   C CA  
1997 C C   . THR   B 120 ? 0.1385 0.1273 0.1375 0.0026  0.0059  -0.0088 126 THR   C C   
1998 O O   . THR   B 120 ? 0.1366 0.1262 0.1335 0.0016  0.0053  -0.0078 126 THR   C O   
1999 C CB  . THR   B 120 ? 0.1568 0.1494 0.1668 0.0047  0.0047  -0.0072 126 THR   C CB  
2000 O OG1 . THR   B 120 ? 0.1787 0.1749 0.1904 0.0042  0.0050  -0.0059 126 THR   C OG1 
2001 C CG2 . THR   B 120 ? 0.1752 0.1679 0.1886 0.0054  0.0028  -0.0059 126 THR   C CG2 
2002 N N   . GLY   B 121 ? 0.1533 0.1406 0.1511 0.0027  0.0088  -0.0107 127 GLY   C N   
2003 C CA  . GLY   B 121 ? 0.1811 0.1678 0.1752 0.0014  0.0116  -0.0115 127 GLY   C CA  
2004 C C   . GLY   B 121 ? 0.1969 0.1834 0.1929 0.0019  0.0157  -0.0137 127 GLY   C C   
2005 O O   . GLY   B 121 ? 0.2067 0.1919 0.2048 0.0031  0.0160  -0.0151 127 GLY   C O   
2006 N N   . GLY   B 122 ? 0.2313 0.2188 0.2266 0.0007  0.0192  -0.0144 128 GLY   C N   
2007 C CA  . GLY   B 122 ? 0.2566 0.2440 0.2538 0.0009  0.0240  -0.0170 128 GLY   C CA  
2008 C C   . GLY   B 122 ? 0.2544 0.2463 0.2567 0.0001  0.0272  -0.0168 128 GLY   C C   
2009 O O   . GLY   B 122 ? 0.2476 0.2440 0.2555 0.0002  0.0251  -0.0147 128 GLY   C O   
2010 N N   . ASN   B 123 ? 0.2499 0.2406 0.2506 -0.0009 0.0327  -0.0193 129 ASN   C N   
2011 C CA  . ASN   B 123 ? 0.2504 0.2456 0.2569 -0.0020 0.0368  -0.0198 129 ASN   C CA  
2012 C C   . ASN   B 123 ? 0.2337 0.2302 0.2378 -0.0042 0.0351  -0.0172 129 ASN   C C   
2013 O O   . ASN   B 123 ? 0.2472 0.2493 0.2595 -0.0046 0.0361  -0.0166 129 ASN   C O   
2014 C CB  . ASN   B 123 ? 0.2637 0.2658 0.2848 0.0004  0.0368  -0.0199 129 ASN   C CB  
2015 C CG  . ASN   B 123 ? 0.3093 0.3104 0.3346 0.0025  0.0397  -0.0228 129 ASN   C CG  
2016 O OD1 . ASN   B 123 ? 0.3093 0.3066 0.3292 0.0015  0.0445  -0.0257 129 ASN   C OD1 
2017 N ND2 . ASN   B 123 ? 0.3448 0.3493 0.3800 0.0053  0.0369  -0.0219 129 ASN   C ND2 
2018 N N   . GLY   B 124 ? 0.2011 0.1923 0.1945 -0.0055 0.0324  -0.0159 130 GLY   C N   
2019 C CA  . GLY   B 124 ? 0.1873 0.1789 0.1784 -0.0074 0.0308  -0.0136 130 GLY   C CA  
2020 C C   . GLY   B 124 ? 0.1607 0.1568 0.1585 -0.0062 0.0261  -0.0114 130 GLY   C C   
2021 O O   . GLY   B 124 ? 0.1689 0.1667 0.1677 -0.0076 0.0253  -0.0100 130 GLY   C O   
2022 N N   . LEU   B 125 ? 0.1473 0.1446 0.1489 -0.0038 0.0231  -0.0112 131 LEU   C N   
2023 C CA  . LEU   B 125 ? 0.1453 0.1458 0.1515 -0.0028 0.0188  -0.0092 131 LEU   C CA  
2024 C C   . LEU   B 125 ? 0.1723 0.1688 0.1729 -0.0020 0.0153  -0.0085 131 LEU   C C   
2025 O O   . LEU   B 125 ? 0.2381 0.2309 0.2347 -0.0014 0.0157  -0.0098 131 LEU   C O   
2026 C CB  . LEU   B 125 ? 0.1652 0.1709 0.1820 -0.0008 0.0184  -0.0092 131 LEU   C CB  
2027 C CG  . LEU   B 125 ? 0.2057 0.2164 0.2305 -0.0012 0.0217  -0.0101 131 LEU   C CG  
2028 C CD1 . LEU   B 125 ? 0.2443 0.2588 0.2794 0.0014  0.0215  -0.0106 131 LEU   C CD1 
2029 C CD2 . LEU   B 125 ? 0.1995 0.2139 0.2272 -0.0028 0.0198  -0.0085 131 LEU   C CD2 
2030 N N   . VAL   B 126 ? 0.1231 0.1202 0.1233 -0.0022 0.0121  -0.0068 132 VAL   C N   
2031 C CA  . VAL   B 126 ? 0.1238 0.1183 0.1209 -0.0014 0.0089  -0.0062 132 VAL   C CA  
2032 C C   . VAL   B 126 ? 0.1142 0.1123 0.1171 -0.0005 0.0067  -0.0050 132 VAL   C C   
2033 O O   . VAL   B 126 ? 0.1121 0.1135 0.1181 -0.0011 0.0063  -0.0040 132 VAL   C O   
2034 C CB  . VAL   B 126 ? 0.1545 0.1454 0.1452 -0.0027 0.0075  -0.0056 132 VAL   C CB  
2035 C CG1 . VAL   B 126 ? 0.1857 0.1783 0.1771 -0.0041 0.0077  -0.0046 132 VAL   C CG1 
2036 C CG2 . VAL   B 126 ? 0.1563 0.1455 0.1458 -0.0017 0.0042  -0.0052 132 VAL   C CG2 
2037 N N   . GLY   B 127 ? 0.0977 0.0948 0.1013 0.0007  0.0051  -0.0049 133 GLY   C N   
2038 C CA  . GLY   B 127 ? 0.1030 0.1025 0.1106 0.0013  0.0032  -0.0035 133 GLY   C CA  
2039 C C   . GLY   B 127 ? 0.1024 0.1002 0.1074 0.0011  0.0012  -0.0030 133 GLY   C C   
2040 O O   . GLY   B 127 ? 0.1196 0.1146 0.1219 0.0012  0.0008  -0.0039 133 GLY   C O   
2041 N N   . PHE   B 128 ? 0.0917 0.0914 0.0977 0.0005  0.0001  -0.0018 134 PHE   C N   
2042 C CA  . PHE   B 128 ? 0.0947 0.0932 0.0989 0.0001  -0.0010 -0.0016 134 PHE   C CA  
2043 C C   . PHE   B 128 ? 0.0935 0.0932 0.0999 0.0001  -0.0017 -0.0004 134 PHE   C C   
2044 O O   . PHE   B 128 ? 0.0997 0.1013 0.1075 -0.0001 -0.0022 0.0009  134 PHE   C O   
2045 C CB  . PHE   B 128 ? 0.1071 0.1061 0.1093 -0.0011 -0.0011 -0.0015 134 PHE   C CB  
2046 C CG  . PHE   B 128 ? 0.0996 0.0971 0.0992 -0.0016 -0.0003 -0.0021 134 PHE   C CG  
2047 C CD1 . PHE   B 128 ? 0.1058 0.1000 0.1024 -0.0014 -0.0008 -0.0028 134 PHE   C CD1 
2048 C CD2 . PHE   B 128 ? 0.1199 0.1191 0.1203 -0.0024 0.0007  -0.0020 134 PHE   C CD2 
2049 C CE1 . PHE   B 128 ? 0.1137 0.1056 0.1068 -0.0021 -0.0003 -0.0030 134 PHE   C CE1 
2050 C CE2 . PHE   B 128 ? 0.1275 0.1248 0.1250 -0.0033 0.0018  -0.0024 134 PHE   C CE2 
2051 C CZ  . PHE   B 128 ? 0.1227 0.1160 0.1159 -0.0032 0.0013  -0.0028 134 PHE   C CZ  
2052 N N   . ALA   B 129 ? 0.0924 0.0905 0.0988 0.0003  -0.0020 -0.0007 135 ALA   C N   
2053 C CA  . ALA   B 129 ? 0.0858 0.0842 0.0933 -0.0002 -0.0022 0.0006  135 ALA   C CA  
2054 C C   . ALA   B 129 ? 0.0908 0.0898 0.0961 -0.0015 -0.0019 0.0008  135 ALA   C C   
2055 O O   . ALA   B 129 ? 0.0966 0.0951 0.1015 -0.0018 -0.0015 -0.0005 135 ALA   C O   
2056 C CB  . ALA   B 129 ? 0.0947 0.0915 0.1037 0.0001  -0.0022 -0.0001 135 ALA   C CB  
2057 N N   . ASP   B 130 ? 0.0893 0.0893 0.0934 -0.0024 -0.0023 0.0022  136 ASP   C N   
2058 C CA  . ASP   B 130 ? 0.0927 0.0927 0.0937 -0.0040 -0.0018 0.0021  136 ASP   C CA  
2059 C C   . ASP   B 130 ? 0.1008 0.0995 0.1012 -0.0048 -0.0004 0.0018  136 ASP   C C   
2060 O O   . ASP   B 130 ? 0.1074 0.1053 0.1090 -0.0048 -0.0003 0.0029  136 ASP   C O   
2061 C CB  . ASP   B 130 ? 0.1161 0.1170 0.1152 -0.0049 -0.0033 0.0039  136 ASP   C CB  
2062 C CG  . ASP   B 130 ? 0.1611 0.1616 0.1558 -0.0069 -0.0029 0.0035  136 ASP   C CG  
2063 O OD1 . ASP   B 130 ? 0.1629 0.1633 0.1570 -0.0071 -0.0021 0.0018  136 ASP   C OD1 
2064 O OD2 . ASP   B 130 ? 0.2200 0.2194 0.2112 -0.0083 -0.0032 0.0048  136 ASP   C OD2 
2065 N N   . VAL   B 131 ? 0.1018 0.1004 0.1010 -0.0057 0.0010  0.0003  137 VAL   C N   
2066 C CA  . VAL   B 131 ? 0.1138 0.1117 0.1129 -0.0068 0.0032  -0.0002 137 VAL   C CA  
2067 C C   . VAL   B 131 ? 0.1191 0.1162 0.1133 -0.0088 0.0046  -0.0006 137 VAL   C C   
2068 O O   . VAL   B 131 ? 0.1248 0.1211 0.1182 -0.0101 0.0072  -0.0013 137 VAL   C O   
2069 C CB  . VAL   B 131 ? 0.1210 0.1192 0.1247 -0.0059 0.0042  -0.0024 137 VAL   C CB  
2070 C CG1 . VAL   B 131 ? 0.1177 0.1159 0.1250 -0.0044 0.0026  -0.0022 137 VAL   C CG1 
2071 C CG2 . VAL   B 131 ? 0.1210 0.1192 0.1247 -0.0054 0.0043  -0.0041 137 VAL   C CG2 
2072 N N   . ARG   B 132 ? 0.1139 0.1111 0.1046 -0.0093 0.0032  -0.0002 138 ARG   C N   
2073 C CA  . ARG   B 132 ? 0.1041 0.1001 0.0897 -0.0114 0.0044  -0.0010 138 ARG   C CA  
2074 C C   . ARG   B 132 ? 0.1210 0.1153 0.1011 -0.0135 0.0050  0.0005  138 ARG   C C   
2075 O O   . ARG   B 132 ? 0.1423 0.1350 0.1174 -0.0156 0.0072  -0.0007 138 ARG   C O   
2076 C CB  . ARG   B 132 ? 0.1016 0.0981 0.0852 -0.0117 0.0023  -0.0010 138 ARG   C CB  
2077 C CG  . ARG   B 132 ? 0.1166 0.1137 0.1038 -0.0102 0.0022  -0.0026 138 ARG   C CG  
2078 C CD  . ARG   B 132 ? 0.1052 0.1029 0.0908 -0.0110 0.0003  -0.0024 138 ARG   C CD  
2079 N NE  . ARG   B 132 ? 0.1131 0.1128 0.1008 -0.0103 -0.0020 -0.0003 138 ARG   C NE  
2080 C CZ  . ARG   B 132 ? 0.1125 0.1139 0.1013 -0.0106 -0.0038 0.0002  138 ARG   C CZ  
2081 N NH1 . ARG   B 132 ? 0.1205 0.1213 0.1073 -0.0120 -0.0038 -0.0011 138 ARG   C NH1 
2082 N NH2 . ARG   B 132 ? 0.1241 0.1276 0.1165 -0.0095 -0.0053 0.0017  138 ARG   C NH2 
2083 N N   . ASP   B 133 ? 0.1226 0.1167 0.1030 -0.0132 0.0034  0.0031  139 ASP   C N   
2084 C CA  . ASP   B 133 ? 0.1338 0.1253 0.1081 -0.0155 0.0037  0.0051  139 ASP   C CA  
2085 C C   . ASP   B 133 ? 0.1526 0.1429 0.1278 -0.0163 0.0074  0.0046  139 ASP   C C   
2086 O O   . ASP   B 133 ? 0.1713 0.1588 0.1404 -0.0187 0.0087  0.0060  139 ASP   C O   
2087 C CB  . ASP   B 133 ? 0.1518 0.1430 0.1265 -0.0147 0.0000  0.0085  139 ASP   C CB  
2088 C CG  . ASP   B 133 ? 0.1788 0.1709 0.1605 -0.0124 -0.0002 0.0090  139 ASP   C CG  
2089 O OD1 . ASP   B 133 ? 0.1749 0.1691 0.1619 -0.0107 0.0005  0.0069  139 ASP   C OD1 
2090 O OD2 . ASP   B 133 ? 0.1956 0.1857 0.1768 -0.0125 -0.0011 0.0115  139 ASP   C OD2 
2091 N N   . LEU   B 134 ? 0.1417 0.1337 0.1238 -0.0148 0.0093  0.0025  140 LEU   C N   
2092 C CA  . LEU   B 134 ? 0.1491 0.1406 0.1337 -0.0158 0.0127  0.0019  140 LEU   C CA  
2093 C C   . LEU   B 134 ? 0.1454 0.1368 0.1285 -0.0174 0.0169  -0.0010 140 LEU   C C   
2094 O O   . LEU   B 134 ? 0.1469 0.1404 0.1363 -0.0162 0.0187  -0.0038 140 LEU   C O   
2095 C CB  . LEU   B 134 ? 0.1428 0.1366 0.1363 -0.0135 0.0121  0.0009  140 LEU   C CB  
2096 C CG  . LEU   B 134 ? 0.1577 0.1515 0.1532 -0.0117 0.0085  0.0029  140 LEU   C CG  
2097 C CD1 . LEU   B 134 ? 0.1700 0.1654 0.1728 -0.0097 0.0078  0.0013  140 LEU   C CD1 
2098 C CD2 . LEU   B 134 ? 0.1745 0.1657 0.1672 -0.0129 0.0082  0.0059  140 LEU   C CD2 
2099 N N   . LEU   B 135 ? 0.1475 0.1361 0.1218 -0.0202 0.0185  -0.0003 141 LEU   C N   
2100 C CA  . LEU   B 135 ? 0.1665 0.1542 0.1377 -0.0221 0.0228  -0.0033 141 LEU   C CA  
2101 C C   . LEU   B 135 ? 0.1763 0.1651 0.1532 -0.0227 0.0279  -0.0055 141 LEU   C C   
2102 O O   . LEU   B 135 ? 0.1978 0.1875 0.1775 -0.0227 0.0314  -0.0090 141 LEU   C O   
2103 C CB  . LEU   B 135 ? 0.1720 0.1557 0.1310 -0.0253 0.0233  -0.0022 141 LEU   C CB  
2104 C CG  . LEU   B 135 ? 0.1764 0.1592 0.1300 -0.0251 0.0177  0.0003  141 LEU   C CG  
2105 C CD1 . LEU   B 135 ? 0.2091 0.1878 0.1503 -0.0286 0.0180  0.0010  141 LEU   C CD1 
2106 C CD2 . LEU   B 135 ? 0.1901 0.1757 0.1486 -0.0227 0.0152  -0.0014 141 LEU   C CD2 
2107 N N   . TRP   B 136 ? 0.1749 0.1635 0.1542 -0.0233 0.0284  -0.0035 142 TRP   C N   
2108 C CA  . TRP   B 136 ? 0.1881 0.1780 0.1737 -0.0243 0.0333  -0.0054 142 TRP   C CA  
2109 C C   . TRP   B 136 ? 0.1975 0.1919 0.1956 -0.0214 0.0331  -0.0084 142 TRP   C C   
2110 O O   . TRP   B 136 ? 0.2102 0.2066 0.2152 -0.0219 0.0372  -0.0108 142 TRP   C O   
2111 C CB  . TRP   B 136 ? 0.1911 0.1793 0.1763 -0.0257 0.0332  -0.0023 142 TRP   C CB  
2112 C CG  . TRP   B 136 ? 0.1788 0.1677 0.1679 -0.0232 0.0278  0.0000  142 TRP   C CG  
2113 C CD1 . TRP   B 136 ? 0.1858 0.1724 0.1694 -0.0227 0.0234  0.0034  142 TRP   C CD1 
2114 C CD2 . TRP   B 136 ? 0.1754 0.1677 0.1753 -0.0207 0.0262  -0.0012 142 TRP   C CD2 
2115 N NE1 . TRP   B 136 ? 0.1873 0.1754 0.1775 -0.0201 0.0199  0.0042  142 TRP   C NE1 
2116 C CE2 . TRP   B 136 ? 0.1750 0.1662 0.1744 -0.0191 0.0215  0.0014  142 TRP   C CE2 
2117 C CE3 . TRP   B 136 ? 0.1819 0.1777 0.1919 -0.0200 0.0282  -0.0042 142 TRP   C CE3 
2118 C CZ2 . TRP   B 136 ? 0.1897 0.1828 0.1970 -0.0169 0.0191  0.0009  142 TRP   C CZ2 
2119 C CZ3 . TRP   B 136 ? 0.1968 0.1945 0.2147 -0.0179 0.0251  -0.0043 142 TRP   C CZ3 
2120 C CH2 . TRP   B 136 ? 0.1907 0.1868 0.2065 -0.0165 0.0208  -0.0019 142 TRP   C CH2 
2121 N N   . LEU   B 137 ? 0.1797 0.1755 0.1808 -0.0183 0.0283  -0.0082 143 LEU   C N   
2122 C CA  . LEU   B 137 ? 0.1968 0.1960 0.2084 -0.0156 0.0274  -0.0107 143 LEU   C CA  
2123 C C   . LEU   B 137 ? 0.2459 0.2461 0.2607 -0.0156 0.0313  -0.0144 143 LEU   C C   
2124 O O   . LEU   B 137 ? 0.2507 0.2537 0.2756 -0.0141 0.0320  -0.0166 143 LEU   C O   
2125 C CB  . LEU   B 137 ? 0.1802 0.1796 0.1919 -0.0128 0.0221  -0.0098 143 LEU   C CB  
2126 C CG  . LEU   B 137 ? 0.1691 0.1684 0.1811 -0.0119 0.0183  -0.0072 143 LEU   C CG  
2127 C CD1 . LEU   B 137 ? 0.1663 0.1655 0.1770 -0.0097 0.0141  -0.0066 143 LEU   C CD1 
2128 C CD2 . LEU   B 137 ? 0.1651 0.1663 0.1860 -0.0112 0.0182  -0.0079 143 LEU   C CD2 
2129 N N   . ASP   B 138 ? 0.2848 0.2824 0.2911 -0.0173 0.0335  -0.0151 144 ASP   C N   
2130 C CA  . ASP   B 138 ? 0.3336 0.3310 0.3410 -0.0176 0.0376  -0.0188 144 ASP   C CA  
2131 C C   . ASP   B 138 ? 0.3643 0.3619 0.3730 -0.0202 0.0443  -0.0207 144 ASP   C C   
2132 O O   . ASP   B 138 ? 0.3916 0.3887 0.4005 -0.0209 0.0487  -0.0242 144 ASP   C O   
2133 C CB  . ASP   B 138 ? 0.3816 0.3755 0.3778 -0.0190 0.0373  -0.0188 144 ASP   C CB  
2134 C CG  . ASP   B 138 ? 0.4499 0.4433 0.4436 -0.0171 0.0316  -0.0172 144 ASP   C CG  
2135 O OD1 . ASP   B 138 ? 0.4688 0.4641 0.4700 -0.0142 0.0287  -0.0174 144 ASP   C OD1 
2136 O OD2 . ASP   B 138 ? 0.5192 0.5100 0.5032 -0.0188 0.0301  -0.0158 144 ASP   C OD2 
2137 N N1  . A1B4A C .   ? 0.1459 0.1507 0.1927 -0.0005 0.0158  0.0167  201 A1B4A A N1  
2138 C C4  . A1B4A C .   ? 0.1540 0.1574 0.2007 0.0001  0.0166  0.0208  201 A1B4A A C4  
2139 C C5  . A1B4A C .   ? 0.1687 0.1741 0.2095 0.0005  0.0158  0.0166  201 A1B4A A C5  
2140 C C6  . A1B4A C .   ? 0.2119 0.2157 0.2441 0.0024  0.0169  0.0205  201 A1B4A A C6  
2141 C C7  . A1B4A C .   ? 0.2629 0.2679 0.2997 0.0041  0.0241  0.0232  201 A1B4A A C7  
2142 C C8  . A1B4A C .   ? 0.2680 0.2715 0.2922 0.0056  0.0225  0.0226  201 A1B4A A C8  
2143 C C10 . A1B4A C .   ? 0.2858 0.2879 0.2979 0.0034  0.0111  0.0142  201 A1B4A A C10 
2144 C C13 . A1B4A C .   ? 0.1271 0.1328 0.1806 -0.0022 0.0146  0.0124  201 A1B4A A C13 
2145 O O1  . A1B4A C .   ? 0.1526 0.1594 0.1946 0.0002  0.0151  0.0135  201 A1B4A A O1  
2146 C C3  . A1B4A C .   ? 0.1532 0.1559 0.1984 -0.0005 0.0137  0.0193  201 A1B4A A C3  
2147 C C2  . A1B4A C .   ? 0.1326 0.1356 0.1844 -0.0022 0.0133  0.0149  201 A1B4A A C2  
2148 C C1  . A1B4A C .   ? 0.1084 0.1126 0.1584 -0.0026 0.0122  0.0110  201 A1B4A A C1  
2149 C C   . A1B4A C .   ? 0.1066 0.1108 0.1614 -0.0039 0.0113  0.0064  201 A1B4A A C   
2150 O O   . A1B4A C .   ? 0.1148 0.1192 0.1783 -0.0049 0.0127  0.0054  201 A1B4A A O   
2151 N N   . A1B4A C .   ? 0.1066 0.1102 0.1554 -0.0037 0.0090  0.0034  201 A1B4A A N   
2152 C C12 . A1B4A C .   ? 0.2479 0.2513 0.2717 0.0032  0.0153  0.0184  201 A1B4A A C12 
2153 C C11 . A1B4A C .   ? 0.2642 0.2670 0.2832 0.0026  0.0117  0.0155  201 A1B4A A C11 
2154 S S1  . A1B4A C .   ? 0.2951 0.2972 0.3059 0.0051  0.0150  0.0163  201 A1B4A A S1  
2155 C C9  . A1B4A C .   ? 0.2661 0.2693 0.2861 0.0046  0.0175  0.0193  201 A1B4A A C9  
2156 S S   . A1B4A C .   ? 0.2605 0.2640 0.2978 0.0036  0.0226  0.0252  201 A1B4A A S   
2158 N N1  . A1B4A E .   ? 0.1592 0.1364 0.1594 0.0048  0.0043  -0.0147 201 A1B4A C N1  
2159 C C4  . A1B4A E .   ? 0.1651 0.1381 0.1625 0.0042  0.0026  -0.0165 201 A1B4A C C4  
2160 C C5  . A1B4A E .   ? 0.1838 0.1617 0.1802 0.0042  0.0059  -0.0149 201 A1B4A C C5  
2161 C C6  . A1B4A E .   ? 0.2275 0.2009 0.2148 0.0027  0.0059  -0.0167 201 A1B4A C C6  
2162 C C7  . A1B4A E .   ? 0.3056 0.2778 0.2894 0.0024  0.0143  -0.0199 201 A1B4A C C7  
2163 C C8  . A1B4A E .   ? 0.3153 0.2860 0.2914 0.0005  0.0131  -0.0187 201 A1B4A C C8  
2164 C C10 . A1B4A E .   ? 0.3134 0.2902 0.2948 0.0007  0.0035  -0.0120 201 A1B4A C C10 
2165 C C13 . A1B4A E .   ? 0.1375 0.1181 0.1447 0.0058  0.0037  -0.0124 201 A1B4A C C13 
2166 O O1  . A1B4A E .   ? 0.1658 0.1473 0.1655 0.0046  0.0073  -0.0136 201 A1B4A C O1  
2167 C C3  . A1B4A E .   ? 0.1521 0.1262 0.1516 0.0036  -0.0008 -0.0149 201 A1B4A C C3  
2168 C C2  . A1B4A E .   ? 0.1386 0.1160 0.1450 0.0043  -0.0007 -0.0125 201 A1B4A C C2  
2169 C C1  . A1B4A E .   ? 0.1217 0.1030 0.1295 0.0050  0.0008  -0.0107 201 A1B4A C C1  
2170 C C   . A1B4A E .   ? 0.1144 0.0982 0.1277 0.0056  0.0004  -0.0082 201 A1B4A C C   
2171 O O   . A1B4A E .   ? 0.1123 0.0950 0.1295 0.0066  0.0009  -0.0081 201 A1B4A C O   
2172 N N   . A1B4A E .   ? 0.1182 0.1049 0.1315 0.0049  -0.0005 -0.0063 201 A1B4A C N   
2173 C C12 . A1B4A E .   ? 0.2723 0.2469 0.2561 0.0018  0.0060  -0.0152 201 A1B4A C C12 
2174 C C11 . A1B4A E .   ? 0.2840 0.2608 0.2691 0.0016  0.0031  -0.0129 201 A1B4A C C11 
2175 S S1  . A1B4A E .   ? 0.3301 0.3044 0.3059 -0.0003 0.0075  -0.0136 201 A1B4A C S1  
2176 C C9  . A1B4A E .   ? 0.3014 0.2747 0.2803 0.0008  0.0089  -0.0159 201 A1B4A C C9  
2177 S S   . A1B4A E .   ? 0.2980 0.2672 0.2818 0.0027  0.0100  -0.0204 201 A1B4A C S   
# 
