data_7HY2
# 
_entry.id   7HY2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HY2         pdb_00007hy2 10.2210/pdb7hy2/pdb 
WWPDB D_1001408074 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7HY2 
_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   2025-01-10 
_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-[(2-ethylphenyl)acetyl]piperidine-3-carboxamide' 274.358   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                               65.409    2   ?         ? ? ? 
4 water       nat water                                                    18.015    337 ?         ? ? ? 
# 
_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-[(2-ethylphenyl)acetyl]piperidine-3-carboxamide' A1BSF 
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 
A1BSF non-polymer         . '(3S)-1-[(2-ethylphenyl)acetyl]piperidine-3-carboxamide' ? 'C16 H22 N2 O2'  274.358 
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 139 145 145 GLU GLU 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 139 145 145 GLU GLU 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        A1BSF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BSF 
_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 A1BSF 1   201 201 A1BSF LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 2 A1BSF 1   201 201 A1BSF LIG C . 
F 3 ZN    1   202 1   ZN    ZN  C . 
G 4 HOH   1   301 5   HOH   HOH A . 
G 4 HOH   2   302 36  HOH   HOH A . 
G 4 HOH   3   303 61  HOH   HOH A . 
G 4 HOH   4   304 4   HOH   HOH A . 
G 4 HOH   5   305 65  HOH   HOH A . 
G 4 HOH   6   306 114 HOH   HOH A . 
G 4 HOH   7   307 237 HOH   HOH A . 
G 4 HOH   8   308 95  HOH   HOH A . 
G 4 HOH   9   309 252 HOH   HOH A . 
G 4 HOH   10  310 164 HOH   HOH A . 
G 4 HOH   11  311 24  HOH   HOH A . 
G 4 HOH   12  312 84  HOH   HOH A . 
G 4 HOH   13  313 30  HOH   HOH A . 
G 4 HOH   14  314 70  HOH   HOH A . 
G 4 HOH   15  315 22  HOH   HOH A . 
G 4 HOH   16  316 84  HOH   HOH A . 
G 4 HOH   17  317 109 HOH   HOH A . 
G 4 HOH   18  318 160 HOH   HOH A . 
G 4 HOH   19  319 22  HOH   HOH A . 
G 4 HOH   20  320 126 HOH   HOH A . 
G 4 HOH   21  321 183 HOH   HOH A . 
G 4 HOH   22  322 62  HOH   HOH A . 
G 4 HOH   23  323 190 HOH   HOH A . 
G 4 HOH   24  324 63  HOH   HOH A . 
G 4 HOH   25  325 140 HOH   HOH A . 
G 4 HOH   26  326 66  HOH   HOH A . 
G 4 HOH   27  327 14  HOH   HOH A . 
G 4 HOH   28  328 59  HOH   HOH A . 
G 4 HOH   29  329 106 HOH   HOH A . 
G 4 HOH   30  330 116 HOH   HOH A . 
G 4 HOH   31  331 71  HOH   HOH A . 
G 4 HOH   32  332 102 HOH   HOH A . 
G 4 HOH   33  333 34  HOH   HOH A . 
G 4 HOH   34  334 93  HOH   HOH A . 
G 4 HOH   35  335 66  HOH   HOH A . 
G 4 HOH   36  336 60  HOH   HOH A . 
G 4 HOH   37  337 10  HOH   HOH A . 
G 4 HOH   38  338 79  HOH   HOH A . 
G 4 HOH   39  339 7   HOH   HOH A . 
G 4 HOH   40  340 74  HOH   HOH A . 
G 4 HOH   41  341 103 HOH   HOH A . 
G 4 HOH   42  342 115 HOH   HOH A . 
G 4 HOH   43  343 13  HOH   HOH A . 
G 4 HOH   44  344 171 HOH   HOH A . 
G 4 HOH   45  345 23  HOH   HOH A . 
G 4 HOH   46  346 56  HOH   HOH A . 
G 4 HOH   47  347 10  HOH   HOH A . 
G 4 HOH   48  348 245 HOH   HOH A . 
G 4 HOH   49  349 18  HOH   HOH A . 
G 4 HOH   50  350 48  HOH   HOH A . 
G 4 HOH   51  351 113 HOH   HOH A . 
G 4 HOH   52  352 76  HOH   HOH A . 
G 4 HOH   53  353 49  HOH   HOH A . 
G 4 HOH   54  354 125 HOH   HOH A . 
G 4 HOH   55  355 19  HOH   HOH A . 
G 4 HOH   56  356 119 HOH   HOH A . 
G 4 HOH   57  357 133 HOH   HOH A . 
G 4 HOH   58  358 53  HOH   HOH A . 
G 4 HOH   59  359 56  HOH   HOH A . 
G 4 HOH   60  360 231 HOH   HOH A . 
G 4 HOH   61  361 29  HOH   HOH A . 
G 4 HOH   62  362 119 HOH   HOH A . 
G 4 HOH   63  363 42  HOH   HOH A . 
G 4 HOH   64  364 11  HOH   HOH A . 
G 4 HOH   65  365 17  HOH   HOH A . 
G 4 HOH   66  366 232 HOH   HOH A . 
G 4 HOH   67  367 26  HOH   HOH A . 
G 4 HOH   68  368 3   HOH   HOH A . 
G 4 HOH   69  369 99  HOH   HOH A . 
G 4 HOH   70  370 52  HOH   HOH A . 
G 4 HOH   71  371 101 HOH   HOH A . 
G 4 HOH   72  372 72  HOH   HOH A . 
G 4 HOH   73  373 115 HOH   HOH A . 
G 4 HOH   74  374 45  HOH   HOH A . 
G 4 HOH   75  375 92  HOH   HOH A . 
G 4 HOH   76  376 35  HOH   HOH A . 
G 4 HOH   77  377 33  HOH   HOH A . 
G 4 HOH   78  378 86  HOH   HOH A . 
G 4 HOH   79  379 128 HOH   HOH A . 
G 4 HOH   80  380 85  HOH   HOH A . 
G 4 HOH   81  381 197 HOH   HOH A . 
G 4 HOH   82  382 73  HOH   HOH A . 
G 4 HOH   83  383 89  HOH   HOH A . 
G 4 HOH   84  384 75  HOH   HOH A . 
G 4 HOH   85  385 26  HOH   HOH A . 
G 4 HOH   86  386 204 HOH   HOH A . 
G 4 HOH   87  387 153 HOH   HOH A . 
G 4 HOH   88  388 23  HOH   HOH A . 
G 4 HOH   89  389 107 HOH   HOH A . 
G 4 HOH   90  390 159 HOH   HOH A . 
G 4 HOH   91  391 35  HOH   HOH A . 
G 4 HOH   92  392 28  HOH   HOH A . 
G 4 HOH   93  393 101 HOH   HOH A . 
G 4 HOH   94  394 157 HOH   HOH A . 
G 4 HOH   95  395 228 HOH   HOH A . 
G 4 HOH   96  396 47  HOH   HOH A . 
G 4 HOH   97  397 16  HOH   HOH A . 
G 4 HOH   98  398 14  HOH   HOH A . 
G 4 HOH   99  399 12  HOH   HOH A . 
G 4 HOH   100 400 122 HOH   HOH A . 
G 4 HOH   101 401 21  HOH   HOH A . 
G 4 HOH   102 402 149 HOH   HOH A . 
G 4 HOH   103 403 234 HOH   HOH A . 
G 4 HOH   104 404 202 HOH   HOH A . 
G 4 HOH   105 405 151 HOH   HOH A . 
G 4 HOH   106 406 112 HOH   HOH A . 
G 4 HOH   107 407 91  HOH   HOH A . 
G 4 HOH   108 408 12  HOH   HOH A . 
G 4 HOH   109 409 143 HOH   HOH A . 
G 4 HOH   110 410 230 HOH   HOH A . 
G 4 HOH   111 411 111 HOH   HOH A . 
G 4 HOH   112 412 49  HOH   HOH A . 
G 4 HOH   113 413 102 HOH   HOH A . 
G 4 HOH   114 414 53  HOH   HOH A . 
G 4 HOH   115 415 96  HOH   HOH A . 
G 4 HOH   116 416 19  HOH   HOH A . 
G 4 HOH   117 417 160 HOH   HOH A . 
G 4 HOH   118 418 85  HOH   HOH A . 
G 4 HOH   119 419 21  HOH   HOH A . 
G 4 HOH   120 420 36  HOH   HOH A . 
G 4 HOH   121 421 209 HOH   HOH A . 
G 4 HOH   122 422 205 HOH   HOH A . 
G 4 HOH   123 423 15  HOH   HOH A . 
G 4 HOH   124 424 208 HOH   HOH A . 
G 4 HOH   125 425 6   HOH   HOH A . 
G 4 HOH   126 426 55  HOH   HOH A . 
G 4 HOH   127 427 77  HOH   HOH A . 
G 4 HOH   128 428 246 HOH   HOH A . 
G 4 HOH   129 429 233 HOH   HOH A . 
G 4 HOH   130 430 148 HOH   HOH A . 
G 4 HOH   131 431 90  HOH   HOH A . 
G 4 HOH   132 432 100 HOH   HOH A . 
G 4 HOH   133 433 40  HOH   HOH A . 
G 4 HOH   134 434 253 HOH   HOH A . 
G 4 HOH   135 435 172 HOH   HOH A . 
G 4 HOH   136 436 38  HOH   HOH A . 
G 4 HOH   137 437 226 HOH   HOH A . 
G 4 HOH   138 438 177 HOH   HOH A . 
G 4 HOH   139 439 249 HOH   HOH A . 
G 4 HOH   140 440 76  HOH   HOH A . 
G 4 HOH   141 441 132 HOH   HOH A . 
G 4 HOH   142 442 178 HOH   HOH A . 
G 4 HOH   143 443 201 HOH   HOH A . 
G 4 HOH   144 444 161 HOH   HOH A . 
G 4 HOH   145 445 129 HOH   HOH A . 
G 4 HOH   146 446 136 HOH   HOH A . 
G 4 HOH   147 447 147 HOH   HOH A . 
G 4 HOH   148 448 132 HOH   HOH A . 
G 4 HOH   149 449 170 HOH   HOH A . 
G 4 HOH   150 450 152 HOH   HOH A . 
G 4 HOH   151 451 154 HOH   HOH A . 
G 4 HOH   152 452 82  HOH   HOH A . 
G 4 HOH   153 453 57  HOH   HOH A . 
G 4 HOH   154 454 72  HOH   HOH A . 
G 4 HOH   155 455 138 HOH   HOH A . 
G 4 HOH   156 456 187 HOH   HOH A . 
G 4 HOH   157 457 25  HOH   HOH A . 
G 4 HOH   158 458 24  HOH   HOH A . 
G 4 HOH   159 459 221 HOH   HOH A . 
G 4 HOH   160 460 63  HOH   HOH A . 
G 4 HOH   161 461 99  HOH   HOH A . 
G 4 HOH   162 462 32  HOH   HOH A . 
G 4 HOH   163 463 82  HOH   HOH A . 
G 4 HOH   164 464 59  HOH   HOH A . 
G 4 HOH   165 465 141 HOH   HOH A . 
G 4 HOH   166 466 222 HOH   HOH A . 
G 4 HOH   167 467 163 HOH   HOH A . 
G 4 HOH   168 468 193 HOH   HOH A . 
G 4 HOH   169 469 224 HOH   HOH A . 
H 4 HOH   1   301 113 HOH   HOH C . 
H 4 HOH   2   302 192 HOH   HOH C . 
H 4 HOH   3   303 128 HOH   HOH C . 
H 4 HOH   4   304 123 HOH   HOH C . 
H 4 HOH   5   305 174 HOH   HOH C . 
H 4 HOH   6   306 64  HOH   HOH C . 
H 4 HOH   7   307 69  HOH   HOH C . 
H 4 HOH   8   308 137 HOH   HOH C . 
H 4 HOH   9   309 120 HOH   HOH C . 
H 4 HOH   10  310 8   HOH   HOH C . 
H 4 HOH   11  311 78  HOH   HOH C . 
H 4 HOH   12  312 33  HOH   HOH C . 
H 4 HOH   13  313 89  HOH   HOH C . 
H 4 HOH   14  314 32  HOH   HOH C . 
H 4 HOH   15  315 133 HOH   HOH C . 
H 4 HOH   16  316 110 HOH   HOH C . 
H 4 HOH   17  317 121 HOH   HOH C . 
H 4 HOH   18  318 2   HOH   HOH C . 
H 4 HOH   19  319 124 HOH   HOH C . 
H 4 HOH   20  320 248 HOH   HOH C . 
H 4 HOH   21  321 239 HOH   HOH C . 
H 4 HOH   22  322 64  HOH   HOH C . 
H 4 HOH   23  323 91  HOH   HOH C . 
H 4 HOH   24  324 43  HOH   HOH C . 
H 4 HOH   25  325 110 HOH   HOH C . 
H 4 HOH   26  326 156 HOH   HOH C . 
H 4 HOH   27  327 80  HOH   HOH C . 
H 4 HOH   28  328 122 HOH   HOH C . 
H 4 HOH   29  329 97  HOH   HOH C . 
H 4 HOH   30  330 1   HOH   HOH C . 
H 4 HOH   31  331 65  HOH   HOH C . 
H 4 HOH   32  332 42  HOH   HOH C . 
H 4 HOH   33  333 28  HOH   HOH C . 
H 4 HOH   34  334 51  HOH   HOH C . 
H 4 HOH   35  335 212 HOH   HOH C . 
H 4 HOH   36  336 20  HOH   HOH C . 
H 4 HOH   37  337 126 HOH   HOH C . 
H 4 HOH   38  338 250 HOH   HOH C . 
H 4 HOH   39  339 236 HOH   HOH C . 
H 4 HOH   40  340 15  HOH   HOH C . 
H 4 HOH   41  341 169 HOH   HOH C . 
H 4 HOH   42  342 30  HOH   HOH C . 
H 4 HOH   43  343 13  HOH   HOH C . 
H 4 HOH   44  344 251 HOH   HOH C . 
H 4 HOH   45  345 240 HOH   HOH C . 
H 4 HOH   46  346 111 HOH   HOH C . 
H 4 HOH   47  347 29  HOH   HOH C . 
H 4 HOH   48  348 74  HOH   HOH C . 
H 4 HOH   49  349 73  HOH   HOH C . 
H 4 HOH   50  350 46  HOH   HOH C . 
H 4 HOH   51  351 51  HOH   HOH C . 
H 4 HOH   52  352 78  HOH   HOH C . 
H 4 HOH   53  353 130 HOH   HOH C . 
H 4 HOH   54  354 98  HOH   HOH C . 
H 4 HOH   55  355 241 HOH   HOH C . 
H 4 HOH   56  356 50  HOH   HOH C . 
H 4 HOH   57  357 57  HOH   HOH C . 
H 4 HOH   58  358 138 HOH   HOH C . 
H 4 HOH   59  359 210 HOH   HOH C . 
H 4 HOH   60  360 38  HOH   HOH C . 
H 4 HOH   61  361 31  HOH   HOH C . 
H 4 HOH   62  362 6   HOH   HOH C . 
H 4 HOH   63  363 4   HOH   HOH C . 
H 4 HOH   64  364 71  HOH   HOH C . 
H 4 HOH   65  365 39  HOH   HOH C . 
H 4 HOH   66  366 37  HOH   HOH C . 
H 4 HOH   67  367 67  HOH   HOH C . 
H 4 HOH   68  368 144 HOH   HOH C . 
H 4 HOH   69  369 109 HOH   HOH C . 
H 4 HOH   70  370 151 HOH   HOH C . 
H 4 HOH   71  371 98  HOH   HOH C . 
H 4 HOH   72  372 79  HOH   HOH C . 
H 4 HOH   73  373 244 HOH   HOH C . 
H 4 HOH   74  374 86  HOH   HOH C . 
H 4 HOH   75  375 7   HOH   HOH C . 
H 4 HOH   76  376 81  HOH   HOH C . 
H 4 HOH   77  377 11  HOH   HOH C . 
H 4 HOH   78  378 62  HOH   HOH C . 
H 4 HOH   79  379 117 HOH   HOH C . 
H 4 HOH   80  380 87  HOH   HOH C . 
H 4 HOH   81  381 140 HOH   HOH C . 
H 4 HOH   82  382 103 HOH   HOH C . 
H 4 HOH   83  383 37  HOH   HOH C . 
H 4 HOH   84  384 70  HOH   HOH C . 
H 4 HOH   85  385 69  HOH   HOH C . 
H 4 HOH   86  386 44  HOH   HOH C . 
H 4 HOH   87  387 9   HOH   HOH C . 
H 4 HOH   88  388 235 HOH   HOH C . 
H 4 HOH   89  389 142 HOH   HOH C . 
H 4 HOH   90  390 107 HOH   HOH C . 
H 4 HOH   91  391 247 HOH   HOH C . 
H 4 HOH   92  392 136 HOH   HOH C . 
H 4 HOH   93  393 54  HOH   HOH C . 
H 4 HOH   94  394 16  HOH   HOH C . 
H 4 HOH   95  395 108 HOH   HOH C . 
H 4 HOH   96  396 1   HOH   HOH C . 
H 4 HOH   97  397 83  HOH   HOH C . 
H 4 HOH   98  398 97  HOH   HOH C . 
H 4 HOH   99  399 54  HOH   HOH C . 
H 4 HOH   100 400 41  HOH   HOH C . 
H 4 HOH   101 401 146 HOH   HOH C . 
H 4 HOH   102 402 148 HOH   HOH C . 
H 4 HOH   103 403 167 HOH   HOH C . 
H 4 HOH   104 404 242 HOH   HOH C . 
H 4 HOH   105 405 127 HOH   HOH C . 
H 4 HOH   106 406 229 HOH   HOH C . 
H 4 HOH   107 407 31  HOH   HOH C . 
H 4 HOH   108 408 45  HOH   HOH C . 
H 4 HOH   109 409 105 HOH   HOH C . 
H 4 HOH   110 410 200 HOH   HOH C . 
H 4 HOH   111 411 41  HOH   HOH C . 
H 4 HOH   112 412 68  HOH   HOH C . 
H 4 HOH   113 413 50  HOH   HOH C . 
H 4 HOH   114 414 145 HOH   HOH C . 
H 4 HOH   115 415 20  HOH   HOH C . 
H 4 HOH   116 416 3   HOH   HOH C . 
H 4 HOH   117 417 44  HOH   HOH C . 
H 4 HOH   118 418 52  HOH   HOH C . 
H 4 HOH   119 419 47  HOH   HOH C . 
H 4 HOH   120 420 155 HOH   HOH C . 
H 4 HOH   121 421 18  HOH   HOH C . 
H 4 HOH   122 422 149 HOH   HOH C . 
H 4 HOH   123 423 137 HOH   HOH C . 
H 4 HOH   124 424 150 HOH   HOH C . 
H 4 HOH   125 425 135 HOH   HOH C . 
H 4 HOH   126 426 95  HOH   HOH C . 
H 4 HOH   127 427 124 HOH   HOH C . 
H 4 HOH   128 428 40  HOH   HOH C . 
H 4 HOH   129 429 43  HOH   HOH C . 
H 4 HOH   130 430 182 HOH   HOH C . 
H 4 HOH   131 431 238 HOH   HOH C . 
H 4 HOH   132 432 144 HOH   HOH C . 
H 4 HOH   133 433 90  HOH   HOH C . 
H 4 HOH   134 434 165 HOH   HOH C . 
H 4 HOH   135 435 243 HOH   HOH C . 
H 4 HOH   136 436 118 HOH   HOH C . 
H 4 HOH   137 437 139 HOH   HOH C . 
H 4 HOH   138 438 105 HOH   HOH C . 
H 4 HOH   139 439 104 HOH   HOH C . 
H 4 HOH   140 440 27  HOH   HOH C . 
H 4 HOH   141 441 185 HOH   HOH C . 
H 4 HOH   142 442 156 HOH   HOH C . 
H 4 HOH   143 443 198 HOH   HOH C . 
H 4 HOH   144 444 106 HOH   HOH C . 
H 4 HOH   145 445 155 HOH   HOH C . 
H 4 HOH   146 446 157 HOH   HOH C . 
H 4 HOH   147 447 164 HOH   HOH C . 
H 4 HOH   148 448 216 HOH   HOH C . 
H 4 HOH   149 449 166 HOH   HOH C . 
H 4 HOH   150 450 199 HOH   HOH C . 
H 4 HOH   151 451 146 HOH   HOH C . 
H 4 HOH   152 452 123 HOH   HOH C . 
H 4 HOH   153 453 93  HOH   HOH C . 
H 4 HOH   154 454 17  HOH   HOH C . 
H 4 HOH   155 455 162 HOH   HOH C . 
H 4 HOH   156 456 145 HOH   HOH C . 
H 4 HOH   157 457 141 HOH   HOH C . 
H 4 HOH   158 458 158 HOH   HOH C . 
H 4 HOH   159 459 129 HOH   HOH C . 
H 4 HOH   160 460 116 HOH   HOH C . 
H 4 HOH   161 461 207 HOH   HOH C . 
H 4 HOH   162 462 218 HOH   HOH C . 
H 4 HOH   163 463 211 HOH   HOH C . 
H 4 HOH   164 464 215 HOH   HOH C . 
H 4 HOH   165 465 203 HOH   HOH C . 
H 4 HOH   166 466 147 HOH   HOH C . 
H 4 HOH   167 467 163 HOH   HOH C . 
H 4 HOH   168 468 220 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           7HY2 
_cell.length_a           72.744 
_cell.length_b           61.688 
_cell.length_c           65.511 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.13 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HY2 
_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          7HY2 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.72 
_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   2024-12-02 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HY2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.02 
_reflns.d_resolution_high            1.68 
_reflns.number_obs                   32453 
_reflns.percent_possible_obs         98.2 
_reflns.pdbx_Rmerge_I_obs            0.215 
_reflns.pdbx_netI_over_sigmaI        5.3 
_reflns.pdbx_redundancy              4.9 
_reflns.pdbx_Rrim_I_all              0.241 
_reflns.pdbx_Rpim_I_all              0.108 
_reflns.pdbx_CC_half                 0.988 
_reflns.pdbx_number_measured_all     158270 
_reflns.pdbx_chi_squared             0.93 
_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                  1.68 
_reflns_shell.d_res_low                   1.77 
_reflns_shell.number_measured_all         23037 
_reflns_shell.number_unique_obs           4689 
_reflns_shell.Rmerge_I_obs                1.623 
_reflns_shell.pdbx_chi_squared            0.88 
_reflns_shell.pdbx_redundancy             4.9 
_reflns_shell.percent_possible_obs        97.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.820 
_reflns_shell.pdbx_Rpim_I_all             0.812 
_reflns_shell.pdbx_CC_half                0.370 
_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                                 7HY2 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     32420 
_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                             47.02 
_refine.ls_d_res_high                            1.680 
_refine.ls_percent_reflns_obs                    97.9 
_refine.ls_R_factor_obs                          0.2040 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2022 
_refine.ls_R_factor_R_free                       0.2401 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.910 
_refine.ls_number_reflns_R_free                  1591 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.B_iso_mean                               19.38 
_refine.aniso_B[1][1]                            -1.09930 
_refine.aniso_B[2][2]                            0.55240 
_refine.aniso_B[3][3]                            0.54690 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.79170 
_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             0.115 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.113 
_refine.pdbx_overall_SU_R_Blow_DPI               0.124 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.118 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HY2 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             337 
_refine_hist.number_atoms_total               2527 
_refine_hist.d_res_high                       1.680 
_refine_hist.d_res_low                        47.02 
# 
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                  0.009 ? 2.00  2250 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.90  ? 2.00  3062 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  754  '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  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2250 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.89  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.73 ? ?     ?    '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  2078 '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                       1.68 
_refine_ls_shell.d_res_low                        1.69 
_refine_ls_shell.number_reflns_R_work             620 
_refine_ls_shell.R_factor_R_work                  0.2926 
_refine_ls_shell.percent_reflns_obs               95.55 
_refine_ls_shell.R_factor_R_free                  0.3704 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.47 
_refine_ls_shell.number_reflns_R_free             29 
_refine_ls_shell.number_reflns_all                649 
_refine_ls_shell.R_factor_all                     0.2958 
# 
_struct.entry_id                  7HY2 
_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-0035378-001 (A71EV2A-x4331)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HY2 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
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 7HY2 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HY2 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 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
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 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_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 ? ? ? ? ? ? ? 2.323 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.376 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
# 
_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_555 109.7 ? 
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_555 105.0 ? 
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_555 116.7 ? 
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_555 110.0 ? 
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_555 101.3 ? 
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_555 114.2 ? 
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_555 111.9 ? 
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_555 107.8 ? 
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_555 116.2 ? 
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_555 109.1 ? 
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 98.1  ? 
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_555 113.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
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 
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 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
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 GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
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 GLN B 89  ? O GLN C 95  N ILE B 76  ? N ILE C 82  
# 
_pdbx_entry_details.entry_id                   7HY2 
_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_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   C HOH 302 ? ? O C HOH 387 ? ? 1.29 
2 1 O   A HOH 365 ? ? O A HOH 368 ? ? 1.50 
3 1 O   A HOH 337 ? ? O A HOH 368 ? ? 1.70 
4 1 O   A HOH 352 ? ? O A HOH 400 ? ? 1.76 
5 1 O   C HOH 325 ? ? O C HOH 423 ? ? 1.81 
6 1 O   C HOH 330 ? ? O C HOH 334 ? ? 2.00 
7 1 O   C HOH 325 ? ? O C HOH 350 ? ? 2.18 
8 1 NE2 C GLN 59  ? ? O C HOH 301 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 315 ? ? 1_555 O C HOH 341 ? ? 4_555 2.01 
2 1 O A HOH 348 ? ? 1_555 O C HOH 330 ? ? 4_556 2.14 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -132.58 
_pdbx_validate_torsion.psi             -30.39 
# 
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 19.6193 6.7356   18.2676 -0.0226 -0.0233 -0.0182 -0.0029 0.0122 0.0048  0.8319 1.0260 0.5160 
-0.5204 -0.1429 0.0534  -0.0146 -0.0313 0.0270 0.0184 0.0146 0.0717  0.0290 0.0332  -0.0000 
'X-RAY DIFFRACTION' 2 ? refined 15.2053 -23.9536 14.1852 -0.0235 -0.0109 -0.0218 0.0032  0.0058 -0.0087 0.6668 1.0355 0.5843 
0.3832  0.1513  -0.0455 -0.0539 0.0185  0.0276 0.0404 0.0504 -0.0565 0.0028 -0.0227 0.0035  
# 
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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       468 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 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 
A1BSF N1   N  N N 1   
A1BSF C4   C  Y N 2   
A1BSF C5   C  Y N 3   
A1BSF C6   C  Y N 4   
A1BSF C7   C  Y N 5   
A1BSF C8   C  N N 6   
A1BSF C10  C  N N 7   
A1BSF C13  C  N S 8   
A1BSF C15  C  N N 9   
A1BSF O1   O  N N 10  
A1BSF C14  C  N N 11  
A1BSF C12  C  N N 12  
A1BSF C11  C  N N 13  
A1BSF N    N  N N 14  
A1BSF C9   C  N N 15  
A1BSF O    O  N N 16  
A1BSF C2   C  Y N 17  
A1BSF C1   C  N N 18  
A1BSF C    C  N N 19  
A1BSF C3   C  Y N 20  
A1BSF H18  H  N N 21  
A1BSF H19  H  N N 22  
A1BSF H7   H  N N 23  
A1BSF H8   H  N N 24  
A1BSF H9   H  N N 25  
A1BSF H10  H  N N 26  
A1BSF H11  H  N N 27  
A1BSF H12  H  N N 28  
A1BSF H13  H  N N 29  
A1BSF H    H  N N 30  
A1BSF H20  H  N N 31  
A1BSF H21  H  N N 32  
A1BSF H16  H  N N 33  
A1BSF H17  H  N N 34  
A1BSF H14  H  N N 35  
A1BSF H15  H  N N 36  
A1BSF H5   H  N N 37  
A1BSF H4   H  N N 38  
A1BSF H3   H  N N 39  
A1BSF H2   H  N N 40  
A1BSF H1   H  N N 41  
A1BSF H6   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TRP   N    N  N N 363 
TRP   CA   C  N S 364 
TRP   C    C  N N 365 
TRP   O    O  N N 366 
TRP   CB   C  N N 367 
TRP   CG   C  Y N 368 
TRP   CD1  C  Y N 369 
TRP   CD2  C  Y N 370 
TRP   NE1  N  Y N 371 
TRP   CE2  C  Y N 372 
TRP   CE3  C  Y N 373 
TRP   CZ2  C  Y N 374 
TRP   CZ3  C  Y N 375 
TRP   CH2  C  Y N 376 
TRP   OXT  O  N N 377 
TRP   H    H  N N 378 
TRP   H2   H  N N 379 
TRP   HA   H  N N 380 
TRP   HB2  H  N N 381 
TRP   HB3  H  N N 382 
TRP   HD1  H  N N 383 
TRP   HE1  H  N N 384 
TRP   HE3  H  N N 385 
TRP   HZ2  H  N N 386 
TRP   HZ3  H  N N 387 
TRP   HH2  H  N N 388 
TRP   HXT  H  N N 389 
TYR   N    N  N N 390 
TYR   CA   C  N S 391 
TYR   C    C  N N 392 
TYR   O    O  N N 393 
TYR   CB   C  N N 394 
TYR   CG   C  Y N 395 
TYR   CD1  C  Y N 396 
TYR   CD2  C  Y N 397 
TYR   CE1  C  Y N 398 
TYR   CE2  C  Y N 399 
TYR   CZ   C  Y N 400 
TYR   OH   O  N N 401 
TYR   OXT  O  N N 402 
TYR   H    H  N N 403 
TYR   H2   H  N N 404 
TYR   HA   H  N N 405 
TYR   HB2  H  N N 406 
TYR   HB3  H  N N 407 
TYR   HD1  H  N N 408 
TYR   HD2  H  N N 409 
TYR   HE1  H  N N 410 
TYR   HE2  H  N N 411 
TYR   HH   H  N N 412 
TYR   HXT  H  N N 413 
VAL   N    N  N N 414 
VAL   CA   C  N S 415 
VAL   C    C  N N 416 
VAL   O    O  N N 417 
VAL   CB   C  N N 418 
VAL   CG1  C  N N 419 
VAL   CG2  C  N N 420 
VAL   OXT  O  N N 421 
VAL   H    H  N N 422 
VAL   H2   H  N N 423 
VAL   HA   H  N N 424 
VAL   HB   H  N N 425 
VAL   HG11 H  N N 426 
VAL   HG12 H  N N 427 
VAL   HG13 H  N N 428 
VAL   HG21 H  N N 429 
VAL   HG22 H  N N 430 
VAL   HG23 H  N N 431 
VAL   HXT  H  N N 432 
ZN    ZN   ZN N N 433 
# 
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 
A1BSF C   C1   sing N N 1   
A1BSF C1  C2   sing N N 2   
A1BSF C2  C3   doub Y N 3   
A1BSF C3  C4   sing Y N 4   
A1BSF C4  C5   doub Y N 5   
A1BSF C5  C6   sing Y N 6   
A1BSF C6  C7   doub Y N 7   
A1BSF C2  C7   sing Y N 8   
A1BSF C7  C8   sing N N 9   
A1BSF C8  C9   sing N N 10  
A1BSF O   C9   doub N N 11  
A1BSF C9  N    sing N N 12  
A1BSF N   C10  sing N N 13  
A1BSF C10 C11  sing N N 14  
A1BSF C11 C12  sing N N 15  
A1BSF C12 C13  sing N N 16  
A1BSF C13 C14  sing N N 17  
A1BSF N1  C14  sing N N 18  
A1BSF C14 O1   doub N N 19  
A1BSF C15 C13  sing N N 20  
A1BSF N   C15  sing N N 21  
A1BSF N1  H18  sing N N 22  
A1BSF N1  H19  sing N N 23  
A1BSF C4  H7   sing N N 24  
A1BSF C5  H8   sing N N 25  
A1BSF C6  H9   sing N N 26  
A1BSF C8  H10  sing N N 27  
A1BSF C8  H11  sing N N 28  
A1BSF C10 H12  sing N N 29  
A1BSF C10 H13  sing N N 30  
A1BSF C13 H    sing N N 31  
A1BSF C15 H20  sing N N 32  
A1BSF C15 H21  sing N N 33  
A1BSF C12 H16  sing N N 34  
A1BSF C12 H17  sing N N 35  
A1BSF C11 H14  sing N N 36  
A1BSF C11 H15  sing N N 37  
A1BSF C1  H5   sing N N 38  
A1BSF C1  H4   sing N N 39  
A1BSF C   H3   sing N N 40  
A1BSF C   H2   sing N N 41  
A1BSF C   H1   sing N N 42  
A1BSF C3  H6   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
_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_1002329 
_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                    7HY2 
_atom_sites.fract_transf_matrix[1][1]   0.013747 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000752 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016211 
_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]   0.015287 
_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   ? 16.509 6.463   8.083  1.00 15.80  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.262 6.592   8.849  1.00 15.87  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.078 5.417   9.806  1.00 16.24  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.696 4.370   9.612  1.00 16.83  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 14.073 6.701   7.893  1.00 17.36  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.864 5.478   7.202  1.00 19.02  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.255 5.607   10.844 1.00 15.20  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.967 4.557   11.814 1.00 14.55  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.570 5.097   13.174 1.00 14.98  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.920 6.228   13.516 1.00 15.10  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.833 4.297   13.967 1.00 14.06  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.411 4.721   15.299 1.00 14.06  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.341 3.521   16.281 1.00 13.98  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.341 2.364   15.837 1.00 13.96  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 11.036 5.382   15.194 1.00 14.53  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.229 3.798   17.605 1.00 13.21  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.019 2.768   18.610 1.00 12.76  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.588 2.973   19.113 1.00 13.04  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.197 4.112   19.423 1.00 12.95  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.016 2.905   19.798 1.00 12.77  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.480 2.889   19.326 1.00 12.21  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.771 1.825   20.871 1.00 13.56  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.433 3.499   20.361 1.00 12.20  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.814  1.887   19.221 1.00 13.04  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.439  1.978   19.726 1.00 13.68  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.334  1.211   21.032 1.00 14.35  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.356  -0.022  21.019 1.00 15.51  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.440  1.431   18.683 1.00 13.72  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.424  2.277   17.429 1.00 15.09  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.665  3.437   17.361 1.00 17.00  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.220  1.951   16.336 1.00 16.60  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.666  4.233   16.224 1.00 18.32  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.249  2.753   15.202 1.00 17.84  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.463  3.889   15.148 1.00 19.47  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.505  4.692   14.036 1.00 22.11  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.252  1.925   22.166 1.00 13.77  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.180  1.261   23.473 1.00 14.82  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.047  1.862   24.292 1.00 16.18  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 6.993  3.079   24.441 1.00 16.44  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.542  1.320   24.235 1.00 15.76  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.089 2.757   24.323 1.00 16.17  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.411  0.698   25.626 1.00 16.99  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.101  1.026   24.758 1.00 16.48  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 4.955  1.498   25.526 1.00 17.40  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.153  2.502   24.716 1.00 18.04  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 3.922  2.266   23.530 1.00 18.31  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.889  3.687   25.276 1.00 18.26  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.207  4.714   24.484 1.00 18.93  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.190  5.775   23.991 1.00 17.08  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.818  6.933   23.866 1.00 16.30  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.022  5.311   25.235 1.00 22.45  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.888  4.333   25.318 1.00 27.13  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.157  4.112   24.342 1.00 29.17  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.747  3.709   26.480 1.00 27.67  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.426  5.372   23.676 1.00 15.90  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.453  6.305   23.208 1.00 15.67  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.034  5.899   21.859 1.00 14.50  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.149  4.712   21.557 1.00 15.10  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.618  6.401   24.223 1.00 15.61  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.203  6.930   25.575 1.00 16.18  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.621  8.181   25.706 1.00 16.73  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.405  6.186   26.727 1.00 17.37  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.248  8.680   26.948 1.00 17.75  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.027  6.672   27.976 1.00 18.13  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.437  7.916   28.079 1.00 18.99  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.077  8.425   29.300 1.00 19.79  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.441  6.902   21.075 1.00 13.06  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.154  6.751   19.820 1.00 12.78  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.465  7.567   19.977 1.00 12.61  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.422  8.761   20.278 1.00 13.08  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.312  7.247   18.619 1.00 13.72  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.103  7.505   17.332 1.00 14.55  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.207  7.865   16.146 1.00 15.35  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.770  8.922   15.288 1.00 17.63  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.359  8.708   14.114 1.00 18.80  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.532  7.471   13.668 1.00 17.17  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.816  9.732   13.391 1.00 18.15  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.611 6.903   19.841 1.00 11.56  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.932 7.542   19.971 1.00 11.68  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.516 7.712   18.566 1.00 11.62  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.706 6.726   17.852 1.00 12.07  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.895 6.694   20.852 1.00 11.55  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.225 7.433   21.086 1.00 10.82  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.242 6.298   22.180 1.00 11.44  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.845 8.932   18.181 1.00 11.55  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.421 9.186   16.852 1.00 11.40  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.646 10.112  16.965 1.00 11.34  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.820 10.808  17.981 1.00 11.46  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.363 9.812   15.892 1.00 12.31  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.350 8.783   15.429 1.00 14.30  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.673 10.991  16.537 1.00 12.86  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.438 10.229  15.878 1.00 10.64  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.520 11.222  15.838 1.00 10.73  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.821 12.586  15.796 1.00 11.61  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.863 12.767  15.009 1.00 11.71  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.376 11.080  14.554 1.00 11.35  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.192 9.819   14.458 1.00 13.01  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.758 8.833   13.866 1.00 13.88  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.407 9.828   14.996 1.00 13.15  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.200 13.500  16.695 1.00 10.96  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.596 14.832  16.768 1.00 10.81  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.581 15.548  15.399 1.00 10.69  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.563 16.166  15.039 1.00 11.64  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.288 15.677  17.848 1.00 12.84  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.536 16.967  18.219 1.00 13.08  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.456 17.872  19.028 1.00 13.07  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.786 19.076  19.539 1.00 15.44  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.711 20.228  18.879 1.00 15.89  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.198 20.329  17.642 1.00 14.02  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.147 21.285  19.444 1.00 15.26  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.675 15.425  14.614 1.00 9.93   ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.737 16.105  13.306 1.00 10.75  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.807 15.506  12.239 1.00 11.87  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.578 16.146  11.216 1.00 13.97  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.176 16.232  12.759 1.00 10.36  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.760 14.949  12.261 1.00 10.59  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.311 14.026  13.126 1.00 11.25  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.937 14.516  10.986 1.00 12.05  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.784 13.053  12.361 1.00 11.91  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.556 13.288  11.069 1.00 11.60  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.236 14.321  12.489 1.00 11.21  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.274 13.683  11.586 1.00 11.20  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.818 13.680  12.140 1.00 12.39  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.910 13.090  11.527 1.00 11.92  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.713 12.256  11.254 1.00 11.24  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.100 12.110  10.587 1.00 11.96  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.395 10.660  10.258 1.00 11.68  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.212 12.929  9.337  1.00 13.57  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.592 14.342  13.293 1.00 12.17  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.258 14.405  13.871 1.00 12.49  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.256 15.094  12.902 1.00 13.35  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.593 16.061  12.203 1.00 13.08  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.308 15.161  15.187 1.00 12.85  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.034  14.563  12.841 1.00 13.79  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 7.990  15.112  11.965 1.00 15.19  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.162  16.211  12.677 1.00 16.43  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.311  16.409  13.898 1.00 15.77  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.080  13.939  11.524 1.00 16.56  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.354  13.471  12.674 1.00 18.31  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.856  12.802  10.871 1.00 16.82  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.212  16.878  11.933 1.00 17.12  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.281  17.834  12.542 1.00 18.17  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.464  17.118  13.637 1.00 15.97  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.252  17.692  14.713 1.00 15.75  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.307  18.426  11.489 1.00 21.93  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 4.970  19.156  10.362 1.00 30.35  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.817  20.231  10.591 1.00 34.03  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.852  18.971  9.022  1.00 33.09  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.210  20.641  9.393  1.00 35.24  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.658  19.908  8.416  1.00 35.17  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.050  15.848  13.374 1.00 15.39  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.284  15.040  14.332 1.00 15.96  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.076  14.733  15.603 1.00 15.22  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.519  14.804  16.701 1.00 15.59  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.761  13.743  13.712 1.00 18.55  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.479  13.901  12.914 1.00 22.92  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 1.276  13.226  11.878 1.00 25.35  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 0.582  14.787  13.376 1.00 23.16  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.377  14.421  15.471 1.00 14.15  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.239  14.171  16.644 1.00 14.09  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.276  15.423  17.544 1.00 13.67  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.094  15.320  18.760 1.00 13.62  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.667  13.812  16.198 1.00 13.38  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.816  12.425  15.648 1.00 15.80  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.191  11.493  16.212 1.00 14.92  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.570  12.260  14.651 1.00 15.73  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.474  16.605  16.935 1.00 13.79  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.520  17.848  17.697 1.00 14.54  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.161  18.213  18.326 1.00 16.16  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.128  18.782  19.412 1.00 16.60  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.082  18.997  16.857 1.00 14.11  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.580  18.985  16.768 1.00 13.97  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.337  18.575  15.706 1.00 14.30  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.498  19.493  17.742 1.00 13.31  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.674 18.744  15.984 1.00 14.69  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.799 19.345  17.211 1.00 14.49  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.348  20.079  19.002 1.00 14.07  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.943 19.735  17.916 1.00 14.75  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.482 20.486  19.688 1.00 14.70  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.759 20.268  19.170 1.00 14.41  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.040  17.831  17.676 1.00 16.53  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.693  18.081  18.212 1.00 16.73  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.322  17.124  19.374 1.00 16.52  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.378  17.389  20.124 1.00 17.39  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.667  17.969  17.096 1.00 17.14  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.040  16.008  19.504 1.00 15.68  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.838  15.038  20.583 1.00 15.72  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.153  14.889  21.405 1.00 14.78  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.465  13.814  21.903 1.00 14.20  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.402  13.703  19.984 1.00 16.40  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.037  13.780  19.333 1.00 20.31  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.009  13.783  20.025 1.00 20.62  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.002  13.862  17.998 1.00 20.43  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.910  15.987  21.547 1.00 14.25  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.204  16.035  22.237 1.00 14.79  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.158  15.600  23.706 1.00 14.77  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.302  16.067  24.462 1.00 15.11  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.760  17.454  22.165 1.00 14.86  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.168  17.664  22.770 1.00 16.14  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.219  16.803  22.044 1.00 16.97  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.571  19.146  22.736 1.00 15.85  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.062  14.689  24.089 1.00 14.66  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.223  14.260  25.476 1.00 15.50  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.522  14.876  26.035 1.00 16.02  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.529  15.496  27.107 1.00 17.52  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.241  12.712  25.615 1.00 16.61  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.665  12.291  27.022 1.00 17.10  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.882  12.121  25.260 1.00 17.73  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.618  14.733  25.280 1.00 15.02  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.961 15.174  25.678 1.00 14.73  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.850 15.254  24.435 1.00 13.61  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.720 14.442  23.517 1.00 12.71  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.574 14.137  26.672 1.00 14.87  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.035 14.321  27.008 1.00 15.81  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.570 15.201  27.901 1.00 17.04  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.141 13.600  26.447 1.00 15.87  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.944 15.114  27.888 1.00 17.24  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.319 14.123  27.021 1.00 16.87  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.251 12.589  25.486 1.00 15.97  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.587 13.625  26.706 1.00 16.98  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.511 12.113  25.157 1.00 16.35  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.660 12.643  25.750 1.00 16.63  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.727 16.235  24.403 1.00 13.07  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.715 16.348  23.317 1.00 12.82  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.031 16.919  23.851 1.00 12.69  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.042 17.692  24.824 1.00 12.14  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.186 17.134  22.093 1.00 13.14  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.614 18.512  22.414 1.00 13.76  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.618 19.625  22.688 1.00 16.36  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.294 20.529  23.490 1.00 19.30  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.726 19.600  22.110 1.00 15.16  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.141 16.573  23.202 1.00 11.69  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.447 17.081  23.622 1.00 11.30  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.340 17.230  22.392 1.00 11.24  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.821 16.230  21.857 1.00 10.70  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.068 16.163  24.680 1.00 14.11  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.319 16.716  25.364 1.00 20.75  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.006 17.588  24.760 1.00 21.82  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.617 16.273  26.487 1.00 21.79  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.554 18.485  21.936 1.00 11.11  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.400 18.764  20.771 0.50 11.61  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.383 18.693  20.749 0.50 11.68  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.813 18.215  20.983 1.00 11.84  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.422 17.691  20.049 1.00 11.40  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.495 20.271  20.501 0.50 13.07  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.344 20.143  20.266 0.50 13.37  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 18.254 20.925  20.292 0.50 14.12  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.010 20.993  21.179 0.50 14.64  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.358 18.364  22.225 1.00 12.54  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.719 17.894  22.496 1.00 13.59  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.875 16.365  22.321 1.00 13.21  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.981 15.899  22.134 1.00 14.46  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.215 18.363  23.864 1.00 15.75  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.674 17.573  24.904 1.00 18.33  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.781 15.606  22.370 1.00 11.42  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.798 14.139  22.186 1.00 11.04  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.243 13.699  20.827 1.00 10.61  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.263 12.506  20.536 1.00 10.97  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.951 13.458  23.294 1.00 11.59  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.509 13.661  24.697 1.00 12.76  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.699 12.961  25.787 1.00 13.56  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.703 11.502  25.628 1.00 13.96  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.481 10.638  26.621 1.00 14.95  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.266 11.077  27.861 1.00 13.91  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.516 9.330   26.392 1.00 13.11  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.664 14.636  20.028 1.00 11.04  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.983 14.323  18.764 1.00 10.63  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.813 13.343  19.013 1.00 10.75  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.554 12.468  18.179 1.00 10.82  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.944 13.771  17.679 1.00 11.30  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.251 13.552  16.333 1.00 11.90  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.447 14.422  15.930 1.00 11.40  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.505 12.497  15.694 1.00 10.76  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.097 13.484  20.145 1.00 10.14  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.943 12.615  20.421 1.00 10.61  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.652 13.400  20.643 1.00 10.58  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.664 14.520  21.167 1.00 10.11  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.155 11.728  21.677 1.00 10.89  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.157 10.597  21.582 1.00 12.10  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.186 9.848   22.895 1.00 12.42  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.789 9.630   20.420 1.00 11.85  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.533 12.781  20.263 1.00 10.50  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.187 13.310  20.499 1.00 10.59  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.276 12.130  20.755 1.00 10.16  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.377 11.086  20.094 1.00 10.35  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.663 14.179  19.327 1.00 11.35  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.276 14.826  19.510 1.00 13.43  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.234 16.183  18.822 1.00 13.93  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.142 13.925  18.936 1.00 13.77  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.411 12.279  21.743 1.00 10.04  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.428 11.267  22.111 1.00 10.27  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.045  11.906  21.998 1.00 11.23  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.806  12.990  22.535 1.00 11.73  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.650 10.697  23.545 1.00 10.21  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.546  9.703   23.917 1.00 10.77  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.028 10.039  23.654 1.00 10.52  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.145  11.220  21.320 1.00 11.57  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.757  11.648  21.163 1.00 13.13  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.800  10.555  21.699 1.00 14.73  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.186  9.381   21.831 1.00 14.56  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.452  12.000  19.706 1.00 14.14  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.647  10.895  18.838 1.00 16.30  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.567  10.939  22.035 1.00 14.78  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.579  9.987   22.550 1.00 16.04  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.819  9.293   21.412 1.00 17.45  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.613  9.872   20.349 1.00 17.80  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.603  10.690  23.496 1.00 16.82  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 1.987  11.787  22.851 1.00 19.30  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.364  8.070   21.646 1.00 18.63  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.628  7.306   20.632 1.00 20.89  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.306  6.808   21.196 1.00 22.83  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.166  6.668   22.410 1.00 23.06  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.463  6.107   20.115 1.00 22.89  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.539  5.117   21.138 1.00 24.80  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.863  6.490   19.651 1.00 22.72  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.656 6.510   20.322 1.00 24.54  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.940 5.976   20.760 1.00 26.41  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.839 4.445   20.902 1.00 27.61  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.447 3.876   21.808 1.00 29.10  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.065 6.381   19.790 1.00 28.60  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.663 6.051   18.453 1.00 30.46  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.399 7.858   19.870 1.00 29.07  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.091 3.781   20.010 1.00 27.11  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.952 2.321   20.075 1.00 27.82  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.248  1.912   20.937 1.00 28.09  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.212  2.666   21.079 1.00 27.29  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.830 1.733   18.676 1.00 27.83  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.186  0.710   21.500 1.00 29.06  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.249  0.175   22.343 1.00 30.66  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.417  -0.334  21.509 1.00 31.06  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.205  -1.053  20.539 1.00 31.46  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.700  -0.966  23.209 1.00 34.13  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.375  -1.071  24.571 1.00 40.82  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 0.924  0.022   25.507 1.00 47.85  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? -0.191 0.552   25.400 1.00 50.79  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 1.781  0.384   26.456 1.00 49.15  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.630  0.040   21.895 1.00 31.36  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.860  -0.399  21.252 1.00 32.70  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.437  -1.582  22.003 1.00 34.11  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.320  -1.651  23.234 1.00 34.43  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.080  -2.512  21.285 1.00 34.46  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.603  -3.709  21.936 1.00 35.22  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.134  -3.887  21.839 1.00 33.82  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.615  -5.001  22.032 1.00 34.80  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 5.854  -4.945  21.447 1.00 37.30  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 4.084  -4.916  21.837 1.00 47.54  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.896  -2.803  21.609 1.00 31.19  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.366 -2.896  21.633 1.00 28.49  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.775 -2.923  23.124 1.00 27.60  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 10.158 -2.252  23.952 1.00 29.33  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.046 -1.687  20.934 1.00 27.39  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.069 -1.738  19.412 1.00 29.06  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.201 -2.848  18.865 1.00 30.99  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.008 -0.643  18.758 1.00 25.14  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.772 -3.705  23.468 1.00 24.78  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.288 -3.792  24.834 1.00 23.39  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.564 -2.945  24.904 1.00 19.54  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.372 -3.029  23.990 1.00 18.93  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.592 -5.273  25.171 1.00 26.34  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.343 -5.921  25.437 1.00 29.56  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.557 -5.452  26.372 1.00 27.54  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.747 -2.129  25.954 1.00 17.16  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 14.964 -1.327  26.085 1.00 15.83  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 15.969 -2.058  26.986 1.00 15.69  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.605 -2.536  28.069 1.00 16.44  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.680 0.075   26.674 1.00 16.14  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.558 0.813   25.899 1.00 17.20  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 15.955 0.923   26.716 1.00 16.77  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.890 1.144   24.404 1.00 17.94  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.218 -2.141  26.551 1.00 14.88  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.276 -2.741  27.350 1.00 13.86  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.625 -1.811  28.539 1.00 13.47  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.644 -0.594  28.399 1.00 13.11  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.515 -2.976  26.486 1.00 13.40  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.898 -2.409  29.695 1.00 13.05  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.335 -1.722  30.923 1.00 12.89  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.603 -2.471  31.331 1.00 14.48  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.550 -3.426  32.111 1.00 15.28  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.252 -1.824  32.006 1.00 13.87  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.901 -1.235  31.569 1.00 15.92  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.925 0.243   31.178 1.00 18.01  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.586 0.699   30.785 1.00 17.32  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.330 1.837   30.147 1.00 18.20  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.314 2.654   29.810 1.00 16.75  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.087 2.157   29.829 1.00 19.09  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.726 -2.131  30.689 1.00 15.14  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 22.970 -2.875  30.827 1.00 15.56  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.174 -1.958  30.502 1.00 15.92  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.002 -0.801  30.096 1.00 15.91  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.921 -4.045  29.839 1.00 15.96  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.977 -3.523  28.094 1.00 17.50  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.387 -2.527  30.574 1.00 16.51  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.585 -1.801  30.166 1.00 17.95  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.333 -2.544  29.037 1.00 17.49  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.566 -2.489  28.960 1.00 17.58  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.494 -1.497  31.366 1.00 22.41  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.156 -2.708  31.991 1.00 30.75  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.782 -3.859  31.622 1.00 30.43  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.069 -2.514  32.827 1.00 36.78  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.584 -3.248  28.161 1.00 16.82  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.147 -3.934  26.999 1.00 16.63  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.932 -2.953  26.117 1.00 16.10  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.539 -1.797  25.948 1.00 16.92  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.046 -4.619  26.182 1.00 16.38  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.432 -6.188  26.869 1.00 18.39  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.015 -3.430  25.534 1.00 14.62  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.806 -2.682  24.563 1.00 14.60  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.947 -3.442  23.228 1.00 13.62  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.850 -3.137  22.434 1.00 13.18  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.189 -2.346  25.116 1.00 18.16  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.195 -1.118  25.971 1.00 23.84  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.620 -0.764  26.365 1.00 28.03  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.044 -0.982  27.499 1.00 29.11  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.402 -0.229  25.423 1.00 27.99  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.121 -4.473  23.014 1.00 12.85  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.058 -5.235  21.767 1.00 12.78  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.550 -5.397  21.463 1.00 12.44  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.703 -5.536  22.358 1.00 12.19  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.786 -6.606  21.840 1.00 14.43  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.068 -7.488  22.694 1.00 16.28  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.245 -6.498  22.295 1.00 15.17  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.243 -5.374  20.198 1.00 11.92  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.880 -5.516  19.731 1.00 12.52  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.826 -5.682  18.229 1.00 12.56  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.839 -5.982  17.588 1.00 12.20  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.624 -5.522  17.674 1.00 12.05  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.350 -5.667  16.249 1.00 12.29  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.466 -4.476  15.831 1.00 12.06  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.480 -4.180  16.508 1.00 11.68  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.652 -7.021  15.954 1.00 14.55  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.210 -7.102  14.497 1.00 15.61  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.539 -8.219  16.323 1.00 15.52  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.808 -3.801  14.728 1.00 11.53  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.998 -2.668  14.257 1.00 10.55  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.477 -2.874  12.840 1.00 10.86  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.096 -3.597  12.057 1.00 10.28  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.738 -1.317  14.367 1.00 10.41  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.758 -1.070  13.269 1.00 11.02  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.994 -1.707  13.283 1.00 11.50  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.485 -0.201  12.213 1.00 12.04  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.955 -1.452  12.307 1.00 12.12  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.422 0.019   11.195 1.00 12.97  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.661 -0.604  11.252 1.00 12.98  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.631 -0.407  10.287 1.00 13.03  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.361 -2.213  12.505 1.00 10.41  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.806 -2.329  11.173 1.00 10.80  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.319 -1.186  10.318 1.00 10.96  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.175 -0.022  10.677 1.00 10.83  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.260 -2.330  11.196 1.00 11.78  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.692 -2.431  9.809  1.00 13.39  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.865 -3.581  9.048  1.00 14.96  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.071 -1.338  9.211  1.00 14.70  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.374 -3.669  7.755  1.00 16.41  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.593 -1.408  7.912  1.00 15.95  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.753 -2.573  7.186  1.00 17.32  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.244 -2.653  5.922  1.00 19.74  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.926 -1.532  9.187  1.00 11.32  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.489 -0.550  8.258  1.00 11.41  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.585 -0.505  6.999  1.00 11.72  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.668 -1.406  6.145  1.00 11.54  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.929 -0.928  7.908  1.00 11.83  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.680 0.094   6.605  1.00 13.28  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.720 0.522   6.888  1.00 12.38  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.773 0.607   5.773  1.00 13.21  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.417 0.761   4.394  1.00 12.56  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.892 0.210   3.428  1.00 12.25  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.723 1.690   5.990  1.00 16.36  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.299 2.979   6.092  1.00 20.50  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.583 1.421   4.323  1.00 11.74  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.319 1.589   3.058  1.00 12.64  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.953 0.287   2.533  1.00 12.40  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.575 0.300   1.459  1.00 12.76  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.396 2.661   3.214  1.00 13.44  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.384 2.309   4.166  1.00 14.24  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.869 -0.807  3.314  1.00 11.62  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.325 -2.132  2.899  1.00 12.01  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.203 -3.190  3.041  1.00 13.80  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.424 -4.346  2.680  1.00 13.65  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.560 -2.583  3.723  1.00 12.21  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.814 -1.758  3.449  1.00 11.45  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.467 -2.106  2.130  1.00 13.08  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.660 -1.287  1.885  1.00 14.76  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.630 -0.070  1.332  1.00 16.25  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.483 0.444   0.898  1.00 15.35  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.756 0.624   1.170  1.00 14.54  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.023 -2.817  3.594  1.00 14.52  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.891 -3.706  3.927  1.00 15.83  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.415 -4.919  4.719  1.00 15.69  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.078 -6.070  4.415  1.00 16.11  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.108 -4.174  2.683  1.00 18.49  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.252 -3.115  2.046  1.00 24.47  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.203 -3.789  1.159  1.00 27.96  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.671 -2.848  0.193  1.00 30.43  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 16.955 -2.856  -1.105 1.00 31.66  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.761 -3.788  -1.613 1.00 32.69  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.456 -1.921  -1.903 1.00 28.96  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.313 -4.655  5.667  1.00 14.06  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 21.978 -5.729  6.414  1.00 14.45  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.243 -5.319  7.847  1.00 13.53  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.398 -4.132  8.121  1.00 13.27  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.369 -6.009  5.788  1.00 16.28  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.382 -7.061  4.695  1.00 23.38  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.822 -7.341  4.264  1.00 29.09  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 24.893 -8.514  3.304  1.00 34.77  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.972 -8.347  2.294  1.00 38.26  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.379 -6.323  8.743  1.00 12.26  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.774 -6.101  10.124 1.00 11.90  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.277 -6.411  10.255 1.00 12.28  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.786 -7.356  9.622  1.00 13.25  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 21.997 -7.018  11.074 1.00 12.90  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.518 -6.782  11.088 1.00 15.18  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.902 -6.080  12.110 1.00 17.53  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.575 -7.225  10.241 1.00 15.87  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.610 -6.120  11.842 1.00 17.58  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.371 -6.778  10.717 1.00 17.55  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.987 -5.631  11.077 1.00 12.15  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.414 -5.849  11.314 1.00 12.03  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.730 -5.898  12.808 1.00 12.27  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.232 -5.080  13.588 1.00 11.97  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.263 -4.711  10.696 1.00 12.38  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.224 -4.642  9.186  1.00 12.69  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.938 -5.547  8.408  1.00 13.77  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.515 -3.642  8.534  1.00 13.36  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 27.898 -5.499  7.017  1.00 15.29  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.480 -3.572  7.142  1.00 14.84  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.159 -4.514  6.386  1.00 16.04  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.161 -4.446  5.007  1.00 17.33  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.607 -6.824  13.213 1.00 12.63  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.047 -6.842  14.622 1.00 12.50  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.105 -5.727  14.850 1.00 13.32  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.915 -5.411  13.945 1.00 14.26  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.658 -8.240  14.775 1.00 13.49  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.221 -8.526  13.382 1.00 14.03  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.280 -7.866  12.397 1.00 12.24  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.068 -5.084  16.019 1.00 12.85  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 30.002 -4.008  16.339 1.00 13.40  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.448 -4.044  17.788 1.00 14.22  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.708 -4.514  18.642 1.00 14.12  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.409 -2.594  16.080 1.00 13.99  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.376 -2.233  14.614 1.00 14.95  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 28.047 -2.443  16.704 1.00 14.06  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.658 -3.492  18.059 1.00 14.19  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.178 -3.194  19.398 1.00 13.72  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.060 -1.666  19.453 1.00 12.32  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.525 -0.983  18.518 1.00 12.54  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.647 -3.572  19.515 1.00 16.61  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.797 -4.975  19.396 1.00 22.57  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.435 -1.136  20.503 1.00 11.30  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.228 0.304   20.573 1.00 12.15  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.719 0.914   21.886 1.00 13.07  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.749 0.227   22.901 1.00 13.24  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.734 0.653   20.291 1.00 12.13  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.684 -0.091  21.110 1.00 11.97  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.199 -1.323  20.700 1.00 12.56  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.180 0.450   22.286 1.00 12.91  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.227 -1.995  21.438 1.00 13.34  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.196 -0.234  23.030 1.00 13.61  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.743 -1.458  22.602 1.00 13.23  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.162 2.197   21.843 1.00 12.63  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.643 2.898   23.037 1.00 13.02  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.466 3.273   23.964 1.00 13.22  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.324 3.383   23.501 1.00 13.55  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.384 4.174   22.644 1.00 14.36  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.548 5.080   21.934 1.00 14.69  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.743 3.484   25.255 1.00 13.32  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.758 3.883   26.268 1.00 13.39  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.196 5.262   25.885 1.00 14.48  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.904 6.069   25.274 1.00 14.87  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.455 3.951   27.649 1.00 15.28  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.800 2.573   28.185 1.00 19.76  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.390 2.660   29.591 1.00 26.63  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.564 1.268   30.157 1.00 32.68  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 32.886 1.289   31.612 1.00 36.42  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.935 5.562   26.245 1.00 14.70  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.367 6.877   25.879 1.00 15.31  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.232 8.045   26.364 1.00 15.82  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.632 8.082   27.535 1.00 16.48  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 26.985 6.890   26.559 1.00 16.36  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.665 5.451   26.882 1.00 17.22  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 27.980 4.718   27.001 1.00 14.92  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.516 8.996   25.463 1.00 15.33  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.374 10.123  25.813 1.00 17.36  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.092 11.374  24.948 1.00 17.25  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.223 11.336  24.076 1.00 16.93  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.842 9.691   25.709 1.00 20.91  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.193 9.520   24.346 1.00 25.74  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.803 12.490  25.240 1.00 17.24  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.713 13.783  24.558 1.00 18.36  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.681 13.726  23.406 1.00 17.97  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.886 13.630  23.647 1.00 18.68  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.214 14.896  25.495 1.00 19.55  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.203 15.701  26.254 1.00 22.64  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.909 16.736  27.125 1.00 23.75  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.217 16.400  25.314 1.00 23.19  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.182 13.783  22.168 1.00 17.61  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.023 13.668  20.968 1.00 18.07  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.785 14.833  20.026 1.00 18.47  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.621 15.213  19.816 1.00 18.40  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.715 12.284  20.313 1.00 18.95  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.195 11.152  21.235 1.00 21.00  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.302 12.165  18.905 1.00 19.21  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.729 9.798   20.869 1.00 23.44  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.858 15.430  19.487 1.00 18.27  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.714 16.552  18.556 1.00 19.23  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.088 16.065  17.248 1.00 17.84  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.509 15.040  16.721 1.00 17.63  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.069 17.217  18.257 1.00 20.75  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.895 18.535  17.534 1.00 23.31  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.155 18.641  16.179 1.00 25.08  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.396 19.642  18.194 1.00 25.61  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 33.966 19.845  15.510 1.00 26.43  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.201 20.844  17.522 1.00 26.89  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.508 20.940  16.190 1.00 26.58  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.056 16.772  16.763 1.00 16.85  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.367 16.424  15.527 1.00 16.95  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.388 17.653  14.635 1.00 17.67  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.907 18.718  15.034 1.00 17.94  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.901 15.939  15.752 1.00 17.28  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.262 15.520  14.423 1.00 17.59  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.847 14.789  16.744 1.00 17.46  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.914 17.486  13.419 1.00 17.83  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.036 18.538  12.418 1.00 18.39  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.664 19.152  12.062 1.00 17.50  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.634 18.473  12.136 1.00 17.52  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.706 17.964  11.149 1.00 22.99  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.502 19.001  10.371 1.00 33.86  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 32.794 18.618  8.932  1.00 44.95  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.014 19.538  8.110  1.00 47.20  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 32.782 17.401  8.623  1.00 47.95  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.662 20.441  11.650 1.00 16.98  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.439 21.133  11.250 1.00 17.27  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.727 20.378  10.110 1.00 17.31  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.391 19.789  9.261  1.00 17.10  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.760 22.556  10.795 1.00 18.10  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.387 20.383  10.102 1.00 16.87  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.544 19.781  9.053  1.00 17.14  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.399 20.791  8.761  1.00 18.68  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.393 21.870  9.366  1.00 19.14  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.962 18.447  9.550  1.00 17.52  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 23.960 18.624  10.542 1.00 17.81  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.429 20.462  7.875  1.00 19.01  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.313 21.402  7.668  1.00 20.30  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.378 21.451  8.890  1.00 19.38  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.600 22.394  9.025  1.00 19.82  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.528 21.101  6.381  1.00 25.51  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 20.669 19.856  6.476  1.00 35.03  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 20.006 19.456  5.174  1.00 45.02  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 18.779 19.678  5.025  1.00 45.82  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 20.715 18.889  4.311  1.00 48.53  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.471 20.447  9.787  1.00 17.80  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.627 20.287  10.955 1.00 17.28  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.173 20.913  12.213 1.00 17.01  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.392 21.312  13.069 1.00 17.42  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.396 18.800  11.195 1.00 16.99  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.826 18.077  9.994  1.00 17.70  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.582 17.147  9.292  1.00 19.03  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.527 18.317  9.564  1.00 18.59  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.047 16.446  8.215  1.00 20.12  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 17.994 17.655  8.460  1.00 19.80  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.748 16.706  7.801  1.00 21.28  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.198 16.035  6.725  1.00 23.02  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.496 20.992  12.346 1.00 16.59  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.122 21.521  13.563 1.00 16.46  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.409 22.257  13.260 1.00 17.13  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.154 21.852  12.354 1.00 16.04  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.526 20.369  14.525 1.00 15.18  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.418 19.477  15.037 1.00 13.69  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.545 19.915  16.022 1.00 13.71  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.323 18.152  14.631 1.00 14.19  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.559 19.074  16.541 1.00 13.54  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.316 17.319  15.106 1.00 13.71  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.464 17.769  16.093 1.00 13.63  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.458 16.962  16.584 1.00 12.50  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.773 23.259  14.087 1.00 18.61  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.122 23.840  13.942 1.00 19.25  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.144 22.828  14.514 1.00 19.10  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.759 21.846  15.192 1.00 18.72  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 26.059 25.093  14.826 1.00 20.39  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 25.055 24.773  15.871 1.00 21.08  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 24.048 23.823  15.248 1.00 18.67  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.456 23.090  14.325 1.00 19.15  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.488 22.221  14.907 1.00 19.36  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.341 22.263  16.446 1.00 18.69  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.087 23.336  16.997 1.00 18.50  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.874 22.691  14.487 1.00 19.99  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.333 21.091  17.095 1.00 17.95  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.055 21.036  18.531 1.00 17.38  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.508 19.689  19.145 1.00 17.17  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.860 18.766  18.409 1.00 17.54  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.520 21.219  18.738 1.00 17.20  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.723 19.918  18.448 1.00 17.46  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.305 20.114  17.956 1.00 16.74  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.418 19.003  18.334 1.00 16.30  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.363 17.828  17.714 1.00 15.95  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.482 16.909  18.095 1.00 14.06  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.182 17.564  16.706 1.00 14.31  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.432 19.557  20.480 1.00 16.48  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.686 18.268  21.124 1.00 16.69  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.338 17.586  21.300 1.00 15.28  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.419 18.189  21.838 1.00 15.51  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.342 18.424  22.504 1.00 17.76  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.778 18.871  22.425 1.00 19.60  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.806 17.948  22.317 1.00 20.76  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.103 20.217  22.374 1.00 21.41  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.130 18.353  22.214 1.00 21.85  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.422 20.638  22.241 1.00 22.95  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.435 19.701  22.172 1.00 23.74  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.745 20.128  22.081 1.00 25.82  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.194 16.373  20.808 1.00 13.74  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.960 15.604  21.001 1.00 12.59  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.216 14.668  22.191 1.00 12.38  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.195 13.936  22.177 1.00 13.70  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.579 14.791  19.747 1.00 12.80  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.368 13.866  19.963 1.00 13.98  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.721 13.422  18.670 1.00 13.82  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.585 14.204  17.713 1.00 13.41  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.260 12.163  18.640 1.00 12.27  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.352 14.697  23.219 1.00 11.81  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.516 13.853  24.407 1.00 11.47  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.829 12.485  24.264 1.00 11.63  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 24.973 12.325  23.388 1.00 13.34  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.958 14.583  25.624 1.00 13.85  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.586 14.892  25.434 1.00 15.73  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.200 11.506  25.124 1.00 10.55  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.616 10.162  25.171 1.00 10.18  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.775 9.439   23.801 1.00 10.27  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.906 8.637   23.421 1.00 10.74  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.125 10.230  25.607 1.00 11.40  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.910 10.858  26.956 1.00 14.95  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.784 10.083  28.103 1.00 17.39  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.829 12.170  27.304 1.00 15.77  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.620 10.945  29.105 1.00 17.06  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.643 12.209  28.673 1.00 16.63  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.865 9.746   23.066 1.00 9.88   ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.146 9.163   21.757 1.00 10.90  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.179 8.029   21.905 1.00 11.27  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.159 8.172   22.648 1.00 11.63  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.703 10.265  20.810 1.00 11.34  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.880 9.881   19.328 1.00 13.23  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.556 9.418   18.695 1.00 14.20  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.472 11.073  18.525 1.00 14.69  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.987 6.936   21.156 1.00 10.51  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.859 5.775   21.210 1.00 11.23  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.365 5.511   19.808 1.00 13.34  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.550 5.421   18.892 1.00 13.58  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.054 4.567   21.693 1.00 11.10  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.496 4.726   23.130 1.00 10.95  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.358 3.372   23.614 1.00 15.86  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 25.064 3.574   22.427 1.00 14.38  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.697 5.405   19.620 1.00 13.55  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.253 5.162   18.288 1.00 13.49  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.655 3.720   18.083 1.00 12.46  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.109 3.068   19.025 1.00 11.37  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.501 6.024   18.045 1.00 15.20  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.315 7.543   18.037 1.00 19.26  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.585 8.241   17.547 1.00 19.98  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.147 7.976   17.136 1.00 20.45  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.590 3.275   16.812 1.00 12.13  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.000 1.952   16.384 1.00 12.56  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.578 2.002   14.958 1.00 11.98  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.275 2.902   14.189 1.00 11.66  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.785 1.029   16.399 1.00 12.99  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.384 1.006   14.604 1.00 11.47  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.898 0.852   13.251 1.00 13.05  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.825 0.052   12.519 1.00 13.06  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.478 -1.044  12.936 1.00 13.06  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.249 0.105   13.245 1.00 14.77  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.659 -0.265  11.824 1.00 15.52  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.325 0.943   13.946 1.00 15.21  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.275 0.626   11.460 1.00 12.62  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.222 0.011   10.670 1.00 12.77  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.703 0.974   9.614  1.00 13.06  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.847 2.194   9.751  1.00 13.29  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.125 0.439   8.544  1.00 12.27  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.578 1.256   7.478  1.00 11.70  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.344 2.069   7.865  1.00 10.63  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.378 1.555   8.408  1.00 10.71  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.294 0.450   6.200  1.00 12.68  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.716 1.306   5.111  1.00 14.34  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.474 2.285   4.489  1.00 15.63  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.437 1.375   4.653  1.00 15.95  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.651 2.877   3.631  1.00 17.82  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.406 2.364   3.707  1.00 17.50  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.339 3.322   7.438  1.00 10.52  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.195 4.210   7.594  1.00 10.17  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.395 5.382   6.606  1.00 10.47  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.533 5.734   6.242  1.00 10.96  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 27.035 4.686   9.038  1.00 9.52   ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.962 5.702   9.386  1.00 11.53  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 26.285 5.872   6.076  1.00 10.25  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 26.256 6.992   5.151  1.00 11.60  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.993 7.817   5.441  1.00 13.35  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 24.081 7.352   6.171  1.00 12.81  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 26.401 6.552   3.675  1.00 13.65  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 25.373 5.546   3.209  1.00 17.52  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.618 5.056   1.789  1.00 17.87  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 25.137 5.718   0.836  1.00 18.29  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.281 4.005   1.632  1.00 16.46  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.906 9.074   4.933  1.00 14.92  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.671 9.853   5.144  1.00 15.75  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 22.440 9.057   4.679  1.00 15.34  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 22.462 8.417   3.608  1.00 15.43  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.917 11.145  4.332  1.00 17.23  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 25.404 11.252  4.236  1.00 17.55  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.874 9.813   4.102  1.00 15.24  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.441 8.997   5.551  1.00 14.81  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 20.238 8.192   5.339  1.00 14.04  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 20.134 7.047   6.348  1.00 13.15  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 19.045 6.496   6.563  1.00 13.68  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.269 6.646   6.972  1.00 11.56  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.283 5.531   7.913  1.00 11.15  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.819 5.873   9.331  1.00 10.36  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.675 4.959   10.156 1.00 10.98  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.680 4.862   7.967  1.00 12.22  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.934 3.940   6.784  1.00 12.87  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.976 3.313   6.312  1.00 11.92  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 24.096 3.865   6.323  1.00 11.47  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.578 7.157   9.638  1.00 10.09  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.146 7.507   11.014 1.00 10.05  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.829 6.785   11.384 1.00 10.45  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.961 6.612   10.517 1.00 10.34  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.047 9.021   11.207 1.00 11.03  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.637 9.894   11.083 1.00 14.28  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.696 6.351   12.635 1.00 10.53  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.473 5.683   13.061 1.00 10.97  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.550 4.175   13.060 1.00 11.51  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.691 3.540   13.683 1.00 11.70  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.589 3.599   12.428 1.00 11.43  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.819 2.148   12.470 1.00 11.19  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.060 1.719   13.912 1.00 11.89  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.774 2.399   14.648 1.00 11.88  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.402 0.659   14.351 1.00 11.93  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.507 0.218   15.736 1.00 12.17  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.808 -0.557  16.027 1.00 11.33  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.214 -1.404  15.219 1.00 11.43  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.223 -0.589  16.129 1.00 14.03  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.063 0.386   16.410 1.00 16.23  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.463 -1.484  17.354 1.00 14.53  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.702 -0.289  16.709 1.00 17.77  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.424 -0.278  17.197 1.00 10.36  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.549 -1.038  17.762 1.00 10.37  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.958 -1.881  18.896 1.00 11.35  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.254 -1.335  19.759 1.00 11.87  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.615 -0.088  18.351 1.00 10.64  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.777 -0.769  19.138 1.00 11.38  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.588 -1.706  18.216 1.00 11.86  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.721 0.297   19.736 1.00 11.68  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.251 -3.181  18.927 1.00 11.70  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.696 -4.049  19.962 1.00 12.91  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.770 -4.953  20.532 1.00 13.24  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.610 -5.465  19.780 1.00 12.67  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.634 -4.978  19.333 1.00 15.06  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.208 -4.470  19.252 1.00 19.60  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.314 -5.616  18.714 1.00 24.22  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 15.897 -5.236  18.727 1.00 26.06  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.054 -5.526  19.706 1.00 27.22  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.448 -6.274  20.732 1.00 25.23  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 13.795 -5.108  19.651 1.00 29.80  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.617 -5.312  21.807 1.00 12.81  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.480 -6.328  22.410 1.00 13.91  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.505 -7.476  22.848 1.00 14.69  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.298 -7.402  22.593 1.00 15.03  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.199 -5.724  23.609 1.00 14.59  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.051 -5.221  24.906 1.00 14.50  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 22.005 -8.508  23.515 1.00 15.10  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.169 -9.601  24.015 1.00 15.74  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.086 -9.117  25.007 1.00 15.75  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.121 -9.863  25.260 1.00 16.26  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 22.049 -10.666 24.705 1.00 17.56  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.729 -10.139 25.979 1.00 23.09  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.652 -11.171 26.558 1.00 29.83  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.876 -11.138 26.339 1.00 31.48  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.075 -12.117 27.317 1.00 27.59  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.239 -7.904  25.598 1.00 15.07  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.258 -7.408  26.576 1.00 15.24  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.108 -6.581  25.961 1.00 14.12  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.079 -6.388  26.632 1.00 14.16  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.929 -6.616  27.728 1.00 15.72  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 21.057 -7.358  28.384 1.00 19.22  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.390 -7.043  28.113 1.00 21.19  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 21.028 -8.423  29.228 1.00 21.19  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 23.121 -7.902  28.810 1.00 22.04  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.351 -8.765  29.487 1.00 22.60  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.280 -6.132  24.720 1.00 12.53  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.270 -5.336  24.039 1.00 12.57  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.861 -4.167  23.269 1.00 12.09  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.026 -4.203  22.860 1.00 12.25  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.042 -3.140  23.025 1.00 11.51  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.459 -1.982  22.258 1.00 11.69  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.421 -1.095  23.060 1.00 11.59  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.080 -0.675  24.174 1.00 11.99  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.230 -1.171  21.777 1.00 13.23  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.672 0.122   21.082 1.00 13.78  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.344 -2.010  20.854 1.00 13.72  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.596 -0.797  22.469 1.00 10.87  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.632 0.024   23.089 1.00 11.77  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.528 1.499   22.679 1.00 12.16  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.701 2.406   23.508 1.00 12.22  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.042 -0.548  22.753 1.00 12.69  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.148 0.381   23.266 1.00 12.76  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.204 -1.951  23.349 1.00 13.44  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.319 1.720   21.397 1.00 11.56  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.264 3.071   20.839 1.00 12.34  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.974 3.083   19.354 1.00 12.07  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.599 2.057   18.781 1.00 12.44  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.105 4.254   18.719 1.00 10.99  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.868 4.363   17.281 1.00 10.53  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.016 5.081   16.593 1.00 10.38  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.642 5.977   17.187 1.00 9.78   ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.530 5.117   16.979 1.00 11.26  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.443 6.447   17.756 1.00 12.18  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.294 4.240   17.190 1.00 11.57  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.252 7.339   17.289 1.00 14.56  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.258 4.760   15.311 1.00 9.83   ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.275 5.474   14.527 1.00 8.36   ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.007 6.993   14.497 1.00 8.29   ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.883 7.416   14.252 1.00 9.15   ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.370 4.922   13.083 1.00 8.53   ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.381 5.734   12.264 1.00 9.13   ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.766 3.438   13.101 1.00 8.36   ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.032 7.796   14.754 1.00 8.31   ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.897 9.243   14.790 1.00 9.38   ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 23.991 9.986   14.034 1.00 9.60   ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.764 11.114  13.609 1.00 10.74  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.830 9.718   16.244 1.00 10.61  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.780 11.131  16.372 1.00 11.03  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.205 9.417   13.931 1.00 9.53   ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.315 10.054  13.197 1.00 10.64  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.069 8.971   12.380 1.00 11.66  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.848 7.766   12.584 1.00 10.27  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.316 10.802  14.169 1.00 11.96  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.131 9.847   14.871 1.00 12.70  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.646 11.750  15.153 1.00 11.93  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.012 9.392   11.554 1.00 12.33  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.872 8.463   10.841 1.00 14.33  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.951 9.165   10.054 1.00 16.07  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 30.048 10.398  10.082 1.00 16.41  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.716 8.372   9.312  1.00 16.07  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.733 8.924   8.431  1.00 18.48  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 33.011 8.129   8.397  1.00 20.20  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.459 7.641   9.438  1.00 22.26  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.578 7.955   7.196  1.00 19.68  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.850 7.287   6.922  1.00 19.12  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 35.044 5.924   7.606  1.00 17.28  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.100 5.663   8.202  1.00 16.95  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.993 8.231   7.275  1.00 22.00  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.874 9.567   6.585  1.00 27.41  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.991 9.640   5.367  1.00 29.14  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.627 10.647  7.357  1.00 29.22  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.056 5.052   7.484  1.00 16.13  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.148 3.733   8.101  1.00 15.28  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.759 3.715   9.565  1.00 15.50  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.976 2.705   10.251 1.00 16.60  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.128 4.786   10.057 1.00 13.51  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.646 4.831   11.427 1.00 13.05  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.123 4.972   11.474 1.00 11.77  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.520 5.434   10.517 1.00 10.65  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.289 6.017   12.174 1.00 14.07  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.796 5.880   12.401 1.00 17.15  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.420 7.234   12.618 1.00 19.12  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.065 4.958   13.586 1.00 17.01  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.510 4.562   12.623 1.00 10.77  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.096 4.748   12.877 1.00 10.54  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.899 5.151   14.350 1.00 10.86  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.535 4.586   15.234 1.00 11.58  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.235 3.559   12.436 1.00 10.58  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.686 2.261   13.107 1.00 10.95  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.746 3.827   12.671 1.00 11.54  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.071 6.160   14.581 1.00 10.36  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.806 6.654   15.923 1.00 11.27  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.358 6.425   16.296 1.00 10.45  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.463 6.627   15.468 1.00 9.57   ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.124 6.000   17.543 1.00 10.35  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.789 5.679   18.037 1.00 10.18  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.432 6.515   19.270 1.00 10.20  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.209 6.598   20.227 1.00 10.49  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.707 4.194   18.439 1.00 9.36   ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.239 3.209   17.422 1.00 9.46   ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.415 2.700   16.432 1.00 9.31   ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.539 2.723   17.517 1.00 10.29  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.891 1.779   15.512 1.00 10.03  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.017 1.791   16.601 1.00 10.78  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.187 1.325   15.601 1.00 10.43  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.227 7.082   19.255 1.00 9.37   ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.665 7.820   20.362 1.00 9.28   ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.135 6.788   21.370 1.00 10.07  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.191 6.044   21.066 1.00 10.20  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.524 8.694   19.871 1.00 8.92   ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.753 6.722   22.539 1.00 9.64   ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.317 5.804   23.604 1.00 11.05  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.943 6.164   24.159 1.00 11.62  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.626 7.356   24.308 1.00 11.95  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.325 5.860   24.756 1.00 13.89  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.083 4.829   25.836 1.00 19.71  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 23.013 3.637   25.507 1.00 20.11  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 22.918 5.227   27.013 1.00 22.79  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.121 5.135   24.483 1.00 10.17  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.808 5.351   25.132 1.00 10.95  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.676 4.552   26.448 1.00 11.60  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.638 4.629   27.092 1.00 11.68  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.599 5.067   24.205 1.00 11.42  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.661 5.925   22.931 1.00 11.61  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.510 3.576   23.852 1.00 10.71  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.723 3.796   26.861 1.00 11.18  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.647 2.937   28.048 1.00 10.71  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.462 3.668   29.367 1.00 11.96  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 18.936 3.080   30.314 1.00 12.59  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.886 2.036   28.128 1.00 10.45  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 21.005 1.046   26.972 1.00 10.62  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.312 0.282   27.130 1.00 13.02  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.448 1.128   26.769 1.00 14.14  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.705 0.700   26.665 1.00 14.54  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 25.007 -0.568  26.939 1.00 11.80  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.661 1.529   26.253 1.00 14.85  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.903 4.925   29.453 1.00 12.22  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.733 5.719   30.663 1.00 12.89  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.321 6.312   30.815 1.00 14.45  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.022 6.867   31.876 1.00 14.89  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.772 6.858   30.722 1.00 13.42  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.597 7.889   29.614 1.00 16.78  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.394 7.477   28.455 1.00 15.93  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.664 9.115   29.911 1.00 17.59  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.474 6.262   29.766 1.00 15.02  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.124 6.843   29.836 1.00 14.54  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.177 5.851   30.502 1.00 14.06  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.373 5.182   29.838 1.00 12.98  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.635 7.238   28.433 1.00 14.51  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.638 8.133   27.672 1.00 16.81  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.288 8.276   26.218 1.00 17.69  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.853 9.471   28.363 1.00 17.26  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.272 5.752   31.831 1.00 15.20  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.505 4.749   32.588 1.00 15.58  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 12.991 4.909   32.505 1.00 15.64  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.252 3.914   32.619 1.00 15.18  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.964 4.696   34.046 1.00 15.72  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.486 4.628   34.281 1.00 17.40  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.770 4.455   35.771 1.00 18.57  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.145 3.500   33.427 1.00 17.64  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.531 6.159   32.295 1.00 16.35  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.112 6.492   32.214 1.00 17.17  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.420 5.921   30.957 1.00 17.85  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.194  5.904   30.907 1.00 18.54  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.921 8.024   32.304 1.00 16.79  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.758 8.818   31.332 1.00 16.40  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.002 9.348   31.545 1.00 17.09  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.395 9.173   29.999 1.00 16.34  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.423 10.028  30.428 1.00 17.32  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.440 9.959   29.470 1.00 16.94  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.241 8.990   29.234 1.00 16.87  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.382 10.518  28.193 1.00 17.51  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.185 9.547   27.966 1.00 17.46  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.246 10.295  27.457 1.00 17.84  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.188 5.466   29.929 1.00 17.28  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.571 4.896   28.724 1.00 19.08  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.718  3.656   29.045 1.00 23.01  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.762  3.369   28.317 1.00 22.40  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.650 4.487   27.706 1.00 18.66  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.338 5.603   26.951 1.00 18.33  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.438 5.039   26.057 1.00 19.29  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.349 6.394   26.107 1.00 18.14  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.067 2.932   30.135 1.00 26.51  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.414  1.710   30.606 1.00 30.77  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.299  1.931   31.599 1.00 34.12  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.837  0.944   32.173 1.00 34.78  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.434 0.827   31.328 1.00 34.73  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.515 0.287   30.473 1.00 42.34  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.229 -0.067  29.320 1.00 44.35  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.652 0.201   30.960 1.00 46.62  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 7.893  3.182   31.854 1.00 36.36  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.800  3.463   32.783 1.00 38.96  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 5.765  4.447   32.197 1.00 40.31  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 6.092  5.372   31.436 1.00 41.01  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.333  3.941   34.142 1.00 41.69  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.087  5.253   34.071 1.00 48.04  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.023  5.523   35.230 1.00 56.35  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 8.981  6.654   35.768 1.00 58.02  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.806  4.613   35.589 1.00 58.85  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.392 -24.682 24.023 1.00 24.25  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.541 -24.525 23.124 1.00 23.78  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.605 -25.712 22.139 1.00 22.30  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 20.020 -26.774 22.400 1.00 22.67  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.830 -24.445 23.935 1.00 25.48  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.030 -25.687 24.595 1.00 29.63  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.314 -25.525 21.028 1.00 20.08  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.434 -26.557 20.002 1.00 18.86  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.695 -25.975 18.625 1.00 17.97  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.324 -24.834 18.341 1.00 18.38  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.337 -26.750 17.747 1.00 16.32  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.647 -26.275 16.392 1.00 15.15  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.610 -27.433 15.367 1.00 15.37  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.632 -28.606 15.754 1.00 15.14  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.042 -25.632 16.389 1.00 14.84  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.588 -27.103 14.053 1.00 15.91  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.680 -28.099 12.991 1.00 15.37  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.069 -27.910 12.345 1.00 14.84  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.461 -26.785 12.035 1.00 14.21  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.567 -27.905 11.930 1.00 15.84  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.170 -27.900 12.560 1.00 16.86  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.688 -28.963 10.814 1.00 15.56  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.140 -27.248 11.665 1.00 18.79  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.794 -29.002 12.127 1.00 15.01  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.117 -28.945 11.518 1.00 15.39  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.061 -29.684 10.189 1.00 16.53  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 25.974 -30.919 10.165 1.00 16.93  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.178 -29.567 12.464 1.00 14.67  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.336 -28.761 13.738 1.00 14.02  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.143 -27.629 13.775 1.00 14.74  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.614 -29.078 14.878 1.00 14.50  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.260 -26.861 14.934 1.00 14.78  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.717 -28.317 16.037 1.00 15.53  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.546 -27.212 16.064 1.00 15.90  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.619 -26.460 17.213 1.00 17.33  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.098 -28.940 9.085  1.00 16.48  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.034 -29.563 7.760  1.00 16.76  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.129 -28.959 6.871  1.00 17.37  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.226 -27.730 6.752  1.00 16.79  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.619 -29.445 7.141  1.00 17.50  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.127 -27.990 7.138  1.00 17.56  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.599 -30.034 5.736  1.00 18.20  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 28.002 -29.805 6.317  1.00 17.52  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.101 -29.333 5.480  1.00 19.05  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 30.001 -28.387 6.257  1.00 20.47  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.319 -28.673 7.412  1.00 21.09  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.285 -27.194 5.710  1.00 20.11  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.057 -26.214 6.475  1.00 20.47  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.147 -25.126 7.062  1.00 19.08  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.570 -23.977 7.184  1.00 18.92  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.197 -25.632 5.664  1.00 23.34  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.286 -26.656 5.455  1.00 30.50  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 34.081 -26.951 6.363  1.00 32.54  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.316 -27.249 4.275  1.00 31.98  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.928 -25.502 7.468  1.00 17.51  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.968 -24.563 8.046  1.00 16.88  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.487 -25.001 9.420  1.00 15.60  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.351 -26.197 9.687  1.00 15.12  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.718 -24.420 7.139  1.00 16.90  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 27.024 -23.864 5.770  1.00 18.12  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.635 -22.626 5.623  1.00 19.86  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.681 -24.565 4.621  1.00 19.36  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.906 -22.102 4.365  1.00 21.59  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.950 -24.054 3.356  1.00 20.65  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.557 -22.818 3.235  1.00 22.69  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.815 -22.290 1.990  1.00 25.83  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.178 -24.004 10.271 1.00 13.78  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.564 -24.186 11.582 1.00 13.40  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.287 -23.338 11.565 1.00 13.00  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.352 -22.138 11.305 1.00 12.08  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.518 -23.754 12.725 1.00 12.95  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.846 -23.510 14.082 1.00 12.91  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.859 -23.218 15.208 1.00 15.66  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.415 -22.163 16.131 1.00 16.83  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 26.906 -22.382 17.342 1.00 17.46  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.716 -23.626 17.777 1.00 15.78  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.555 -21.358 18.118 1.00 15.48  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.125 -23.967 11.780 1.00 13.39  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.817 -23.296 11.791 1.00 13.02  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.364 -23.162 13.249 1.00 13.16  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.220 -24.174 13.938 1.00 13.19  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.755 -24.089 10.988 1.00 13.35  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.428 -23.315 10.919 1.00 13.45  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.266 -24.451 9.595  1.00 12.73  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.116 -21.949 13.713 1.00 12.08  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.654 -21.728 15.091 1.00 12.12  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.461 -20.758 15.118 1.00 11.94  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.225 -20.020 14.148 1.00 10.93  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.809 -21.152 15.969 1.00 13.64  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 23.815 -22.227 16.313 1.00 16.08  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.478 -19.957 15.298 1.00 13.47  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.734 -20.690 16.254 1.00 11.76  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.706 -19.658 16.424 1.00 11.39  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.453 -18.309 16.429 1.00 12.41  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.476 -18.179 17.127 1.00 13.41  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 17.978 -19.804 17.789 1.00 12.43  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.125 -21.043 17.937 1.00 14.25  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.591 -22.065 18.449 1.00 15.08  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 15.853 -20.971 17.514 1.00 13.08  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.022 -17.362 15.589 1.00 12.06  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.659 -16.038 15.495 1.00 12.10  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.803 -15.356 16.870 1.00 11.85  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 20.863 -14.789 17.149 1.00 11.91  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 18.897 -15.137 14.507 1.00 11.91  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.630 -13.847 14.113 1.00 12.26  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.666 -12.908 13.395 1.00 14.10  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.310 -11.692 12.863 1.00 13.92  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.441 -10.558 13.543 1.00 15.33  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.071 -10.492 14.818 1.00 13.79  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.998 -9.497  12.975 1.00 17.84  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.780 -15.468 17.742 1.00 11.47  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 18.860 -14.820 19.059 1.00 12.68  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 19.877 -15.458 20.024 1.00 13.61  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.212 -14.831 21.033 1.00 14.67  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.493 -14.682 19.732 1.00 13.00  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 16.931 -15.950 20.271 1.00 13.01  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.265 -16.848 19.451 1.00 13.13  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 16.857 -16.384 21.554 1.00 13.63  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.856 -17.829 20.245 1.00 13.67  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.194 -17.595 21.523 1.00 14.38  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.375 -16.672 19.704 1.00 13.16  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.392 -17.356 20.518 1.00 14.22  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.787 -17.369 19.856 1.00 15.64  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.725 -17.984 20.384 1.00 16.07  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 20.947 -18.794 20.842 1.00 13.77  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.630 -18.908 21.634 1.00 14.57  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.326 -20.367 21.964 1.00 15.55  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.648 -18.049 22.942 1.00 14.63  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 22.931 -16.701 18.700 1.00 15.77  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.216 -16.647 18.006 1.00 15.80  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.305 -15.999 18.894 1.00 15.40  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.035 -15.044 19.620 1.00 14.73  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.066 -15.857 16.714 1.00 15.70  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.525 -16.539 18.837 1.00 15.22  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.651 -16.040 19.627 1.00 15.50  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.451 -14.934 18.877 1.00 15.56  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.220 -14.707 17.686 1.00 14.55  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.568 -17.240 19.955 1.00 16.54  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.184 -17.705 18.749 1.00 17.22  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 27.824 -18.373 20.674 1.00 16.81  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.467 -14.311 19.548 1.00 15.81  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.374 -13.362 18.894 1.00 16.06  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.081 -14.069 17.707 1.00 15.25  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.230 -13.469 16.642 1.00 13.99  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.444 -12.852 19.890 1.00 17.97  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.883 -12.093 21.055 1.00 23.51  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.073 -10.979 20.880 1.00 26.51  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.079 -12.280 22.381 1.00 26.19  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.795 -10.539 22.096 1.00 27.24  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.358 -11.300 23.032 1.00 27.82  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.460 -15.355 17.883 1.00 15.44  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.128 -16.145 16.830 1.00 16.59  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.223 -16.385 15.636 1.00 15.96  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.679 -16.274 14.495 1.00 16.27  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.662 -17.478 17.363 1.00 18.70  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.517 -18.180 16.330 1.00 23.94  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.594 -17.696 15.970 1.00 24.90  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.046 -19.300 15.790 1.00 24.59  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 29.933 -16.683 15.877 1.00 15.34  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 28.967 -16.871 14.786 1.00 14.78  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.875 -15.579 13.932 1.00 14.84  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.943 -15.637 12.703 1.00 14.37  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.581 -17.217 15.354 1.00 15.35  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.444 -18.630 15.881 1.00 17.18  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 27.993 -19.557 15.241 1.00 16.83  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.780 -18.808 16.931 1.00 17.41  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.760 -14.414 14.598 1.00 14.22  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.668 -13.143 13.880 1.00 15.39  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.960 -12.777 13.152 1.00 15.78  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.901 -12.145 12.104 1.00 16.58  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.214 -12.010 14.825 1.00 15.59  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.730 -11.978 15.045 1.00 15.77  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.052 -12.445 16.129 1.00 16.64  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.736 -11.432 14.152 1.00 15.64  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.697 -12.256 15.959 1.00 17.32  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.479 -11.611 14.763 1.00 16.27  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.794 -10.803 12.901 1.00 16.06  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.292 -11.174 14.177 1.00 16.37  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.610 -10.376 12.314 1.00 16.84  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.377 -10.586 12.941 1.00 16.95  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.109 -13.208 13.669 1.00 15.62  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.407 -12.931 13.034 1.00 16.99  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.676 -13.849 11.806 1.00 17.78  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.576 -13.560 11.013 1.00 17.39  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.531 -13.088 14.060 1.00 16.82  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.935 -14.971 11.695 1.00 17.15  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 32.034 -15.927 10.586 1.00 17.43  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.649 -16.052 9.889  1.00 17.30  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.260 -17.125 9.451  1.00 16.96  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.506 -17.272 11.122 1.00 18.69  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.935 -17.190 11.634 1.00 21.71  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.899 -17.173 10.852 1.00 21.58  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.112 -17.107 12.964 1.00 21.65  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.921 -14.938 9.805  1.00 17.34  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.569 -14.862 9.260  1.00 17.82  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.459 -15.267 7.797  1.00 17.18  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.212 -14.754 6.965  1.00 18.11  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 28.034 -13.423 9.425  1.00 17.87  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.590 -13.176 8.965  1.00 18.22  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.601 -14.033 9.769  1.00 17.94  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.227 -11.698 9.098  1.00 18.53  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.510 -16.158 7.476  1.00 15.18  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.220 -16.542 6.092  1.00 15.33  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.887 -15.885 5.664  1.00 15.61  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.798 -15.232 4.610  1.00 15.77  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.159 -18.088 5.922  1.00 15.39  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.581 -18.483 4.558  1.00 15.88  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.535 -18.718 6.149  1.00 15.12  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.865 -16.023 6.518  1.00 14.80  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.501 -15.551 6.262  1.00 14.72  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.735 -15.474 7.577  1.00 14.43  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.933 -16.299 8.461  1.00 14.26  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.781 -16.546 5.300  1.00 14.81  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.299 -16.320 5.097  1.00 15.98  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.711 -15.403 4.268  1.00 17.45  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.221 -17.033 5.735  1.00 16.20  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.335 -15.473 4.386  1.00 17.61  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.012 -16.471 5.272  1.00 17.29  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.163 -18.065 6.685  1.00 16.48  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.760 -16.947 5.684  1.00 17.56  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 18.922 -18.522 7.101  1.00 16.88  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.743 -17.950 6.621  1.00 17.14  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.872 -14.485 7.705  1.00 14.22  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 20.990 -14.366 8.866  1.00 13.78  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.644 -13.756 8.450  1.00 14.14  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.584 -12.955 7.512  1.00 13.74  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.638 -13.622 10.059 1.00 13.69  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.217 -12.253 9.719  1.00 16.09  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.224 -11.112 9.578  1.00 19.60  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.514 -10.179 8.797  1.00 20.83  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.160 -11.141 10.241 1.00 19.14  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.578 -14.101 9.174  1.00 13.68  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.259 -13.554 8.881  1.00 13.60  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.483 -13.433 10.191 1.00 12.95  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.026 -14.439 10.740 1.00 12.59  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.526 -14.420 7.863  1.00 15.27  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.231 -13.834 7.308  1.00 19.40  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.612 -12.979 7.990  1.00 18.53  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.832 -14.239 6.204  1.00 22.46  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.336 -12.190 10.687 1.00 11.84  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.608 -11.911 11.919 0.50 11.94  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.626 -11.983 11.942 0.50 12.18  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.163 -12.406 11.827 1.00 12.44  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.627 -12.927 12.795 1.00 13.52  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.605 -10.408 12.201 0.50 12.96  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.749 -10.538 12.431 0.50 14.07  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 14.972 -10.143 13.435 0.50 14.24  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.042 -9.657  11.579 0.50 16.63  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.515 -12.225 10.642 1.00 12.43  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.117 -12.656 10.493 1.00 13.30  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 11.935 -14.179 10.659 1.00 12.85  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.830 -14.622 10.961 1.00 14.20  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.506 -12.158 9.186  1.00 15.25  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.950 -12.925 8.078  1.00 18.54  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.003 -14.961 10.490 1.00 11.21  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 12.957 -16.430 10.642 1.00 11.24  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.637 -16.924 11.944 1.00 11.34  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.605 -18.127 12.221 1.00 11.05  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.680 -17.111 9.451  1.00 11.68  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 12.999 -16.846 8.113  1.00 11.82  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.722 -17.528 6.952  1.00 13.35  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.677 -18.992 7.075  1.00 13.30  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.751 -19.833 6.046  1.00 14.96  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.875 -19.369 4.803  1.00 13.20  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.665 -21.144 6.247  1.00 13.50  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.315 -16.025 12.693 1.00 11.45  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.099 -16.371 13.892 1.00 10.83  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.201 -17.373 13.526 1.00 11.01  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.510 -18.269 14.316 1.00 10.98  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.225 -16.929 15.050 1.00 10.41  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.023 -17.211 16.329 1.00 12.32  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 15.880 -16.370 16.696 1.00 13.47  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.814 -18.295 16.948 1.00 12.59  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.819 -17.233 12.328 1.00 10.65  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 17.924 -18.114 11.946 1.00 11.37  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.215 -17.348 11.630 1.00 11.70  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.177 -16.243 11.090 1.00 12.19  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.564 -18.938 10.695 1.00 11.80  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.551 -20.074 10.874 1.00 12.16  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.376 -20.807 9.562  1.00 12.24  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.014 -21.070 11.933 1.00 13.89  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.356 -18.010 11.880 1.00 11.23  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.686 -17.495 11.547 1.00 11.24  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.553 -18.692 11.188 1.00 11.72  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.474 -19.744 11.819 1.00 11.81  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.321 -16.681 12.684 1.00 10.83  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.711 -16.045 12.406 1.00 11.98  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.831 -14.692 13.095 1.00 11.57  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.876 -16.992 12.842 1.00 12.44  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.325 -18.545 10.134 1.00 11.56  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.256 -19.554 9.651  1.00 11.73  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.660 -18.944 9.659  1.00 12.39  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.877 -17.845 9.133  1.00 12.24  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.895 -20.074 8.232  1.00 11.69  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.942 -21.076 7.736  1.00 12.82  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.513 -20.698 8.227  1.00 11.92  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.600 -19.659 10.253 1.00 13.07  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.007 -19.267 10.292 1.00 13.84  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.884 -20.373 9.649  1.00 15.63  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.444 -21.534 9.512  1.00 15.31  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.441 -18.962 11.724 1.00 14.47  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.304 -20.094 12.574 1.00 17.24  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.104 -20.011 9.237  1.00 16.85  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.009 -20.976 8.621  1.00 18.77  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.846 -21.727 9.680  1.00 21.04  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.155 -21.174 10.740 1.00 21.57  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.929 -20.274 7.632  1.00 19.94  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.637 -19.224 8.266  1.00 22.00  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.201 -22.982 9.390  1.00 22.30  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 32.989 -23.815 10.307 1.00 24.97  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.240 -24.357 9.614  1.00 27.43  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.272 -24.462 8.385  1.00 27.94  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.157 -25.005 10.831 1.00 26.62  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.960 -25.953 9.779  1.00 28.54  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.816 -24.584 11.402 1.00 26.69  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.255 -24.734 10.397 1.00 28.82  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.469 -25.324 9.835  1.00 30.78  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.281 -26.834 9.656  1.00 31.44  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.770 -27.400 8.676  1.00 31.99  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.694 -24.989 10.695 1.00 33.50  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.393 -25.282 12.066 1.00 35.86  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.112 -23.532 10.562 1.00 34.19  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.580 -27.493 10.597 1.00 30.63  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.365 -28.936 10.510 1.00 30.88  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.108 -29.281 9.706  1.00 31.18  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.171 -28.489 9.644  1.00 31.77  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.286 -29.546 11.904 1.00 30.74  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.087 -30.473 9.108  1.00 30.83  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.958 -30.930 8.308  1.00 30.54  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.837 -31.436 9.196  1.00 29.03  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.080 -32.225 10.099 1.00 29.76  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.403 -32.056 7.363  1.00 32.99  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.619 -32.088 6.052  1.00 39.21  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 33.048 -30.967 5.124  1.00 46.81  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 34.194 -30.485 5.165  1.00 49.42  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 32.143 -30.530 4.256  1.00 47.48  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.619 -30.998 8.917  1.00 26.69  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.424 -31.416 9.640  1.00 25.08  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.746 -32.553 8.902  1.00 22.72  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.758 -32.588 7.666  1.00 23.28  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.152 -33.485 9.640  1.00 20.61  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.551 -34.661 9.017  1.00 20.47  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.032 -34.780 9.220  1.00 19.91  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.501 -35.882 9.053  1.00 19.64  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.273 -35.931 9.463  1.00 21.95  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.062 -35.923 9.158  1.00 27.59  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.333 -33.680 9.576  1.00 18.48  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.872 -33.736 9.699  1.00 19.23  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.318 -33.718 8.268  1.00 20.00  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.857 -33.027 7.386  1.00 20.87  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.295 -32.525 10.491 1.00 20.06  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.455 -32.595 12.006 1.00 23.84  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.484 -33.721 12.555 1.00 24.79  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.557 -31.519 12.642 1.00 23.72  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.271 -34.489 8.029  1.00 19.84  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.609 -34.539 6.727  1.00 20.43  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.366 -33.655 6.824  1.00 18.20  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.641 -33.762 7.805  1.00 18.48  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.190 -35.998 6.431  1.00 24.65  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.359 -36.763 6.123  1.00 27.21  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.156 -36.108 5.286  1.00 25.69  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.124 -32.777 5.842  1.00 16.86  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.934 -31.929 5.860  1.00 15.70  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.819 -32.603 5.047  1.00 14.51  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.072 -33.075 3.926  1.00 14.72  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.217 -30.519 5.288  1.00 16.12  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.431 -29.834 5.949  1.00 16.87  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.963 -29.642 5.386  1.00 16.44  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.272 -29.546 7.444  1.00 18.01  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.610 -32.658 5.605  1.00 12.44  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.464 -33.197 4.888  1.00 11.81  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.039 -32.231 3.766  1.00 11.51  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.066 -31.021 3.943  1.00 11.45  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.306 -33.401 5.855  1.00 12.13  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.639 -32.788 2.618  1.00 11.52  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.133 -32.061 1.450  1.00 10.82  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.794 -32.755 1.158  1.00 10.54  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.740 -33.727 0.407  1.00 10.93  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.122 -32.183 0.283  1.00 12.93  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.520 -31.650 0.610  1.00 14.07  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.570 -30.184 1.014  1.00 14.86  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.952 -29.770 1.300  1.00 14.79  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.289 -28.657 1.951  1.00 16.48  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.355 -27.824 2.381  1.00 14.73  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.568 -28.367 2.166  1.00 16.53  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.725 -32.303 1.833  1.00 10.30  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.446 -32.987 1.795  1.00 10.63  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.299  -32.043 2.277  1.00 11.85  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.545  -30.916 2.720  1.00 11.13  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.550 -34.182 2.748  1.00 10.40  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.675 -33.685 4.494  1.00 12.48  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.064  -32.570 2.308  1.00 12.07  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.937  -31.841 2.885  1.00 12.90  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.300  -32.623 4.057  1.00 13.22  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.092  -32.519 4.284  1.00 12.52  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.898  -31.452 1.829  1.00 14.44  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.154  -32.622 1.210  1.00 19.74  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.496  -33.788 1.525  1.00 18.89  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.237  -32.376 0.404  1.00 24.36  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.110  -33.426 4.791  1.00 12.41  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.651  -34.178 5.974  1.00 11.74  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.970  -33.257 6.973  1.00 11.00  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.368  -32.090 7.152  1.00 10.89  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.819  -34.896 6.656  1.00 12.19  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.339  -36.431 5.854  1.00 15.64  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.966  -33.791 7.635  1.00 10.88  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.271  -33.111 8.715  1.00 11.77  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.259  -33.934 10.002 1.00 12.52  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.445  -33.674 10.880 1.00 12.28  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.841  -32.720 8.307  1.00 11.18  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.768  -31.416 7.499  1.00 12.32  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.333  -31.032 7.225  1.00 13.86  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.813  -31.217 6.122  1.00 15.44  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.672  -30.513 8.235  1.00 11.16  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.117  -34.972 10.099 1.00 12.89  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.277  -35.788 11.297 1.00 13.77  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.783  -35.977 11.491 1.00 12.97  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.553  -36.091 10.525 1.00 12.60  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.540  -37.153 11.244 1.00 17.00  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.168  -38.001 10.272 1.00 19.64  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.054  -37.025 10.882 1.00 18.10  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.193  -35.989 12.739 1.00 12.60  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.602  -36.112 13.081 1.00 13.13  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.799  -36.290 14.566 1.00 12.67  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.846  -36.597 15.285 1.00 13.03  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.054 -36.144 15.015 1.00 11.20  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.448 -36.321 16.404 1.00 10.61  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.354 -35.145 16.780 1.00 10.67  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.297 -34.845 16.038 1.00 10.48  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.184 -37.673 16.614 1.00 11.20  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.729 -37.785 18.044 1.00 11.79  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.275 -38.865 16.285 1.00 11.83  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.081 -34.484 17.911 1.00 10.81  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.934 -33.368 18.350 1.00 10.78  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.563 -33.599 19.717 1.00 11.31  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.001 -34.344 20.533 1.00 10.91  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.199 -32.018 18.310 1.00 10.28  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.270 -31.779 19.484 1.00 11.54  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.023  -32.394 19.548 1.00 12.70  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.631 -30.928 20.524 1.00 13.09  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.147  -32.139 20.598 1.00 14.09  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.777  -30.705 21.607 1.00 14.14  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.532  -31.302 21.629 1.00 14.59  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.676  -31.063 22.674 1.00 15.89  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.725 -32.968 19.966 1.00 11.84  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.370 -33.104 21.259 1.00 11.82  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.918 -31.978 22.161 1.00 11.16  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.032 -30.818 21.802 1.00 10.69  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.903 -33.117 21.139 1.00 12.63  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.561 -33.232 22.494 1.00 12.55  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.456 -34.398 23.242 1.00 13.16  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.229 -32.154 23.057 1.00 13.74  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.040 -34.503 24.502 1.00 14.19  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.795 -32.237 24.321 1.00 14.79  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.686 -33.408 25.049 1.00 16.01  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.295 -33.489 26.275 1.00 18.53  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.390 -32.332 23.321 1.00 12.37  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 12.916 -31.367 24.318 1.00 12.42  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 13.907 -31.334 25.519 1.00 12.64  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 13.889 -32.238 26.359 1.00 13.69  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.507 -31.727 24.759 1.00 12.78  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 10.869 -30.694 26.114 1.00 16.16  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 14.783 -30.327 25.558 1.00 11.86  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 15.803 -30.177 26.600 1.00 13.99  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.238 -30.140 28.030 1.00 14.34  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.789 -30.796 28.937 1.00 15.08  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 16.652 -28.937 26.327 1.00 17.34  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 17.639 -28.805 27.333 1.00 23.56  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.098 -29.441 28.232 1.00 13.40  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.455 -29.315 29.551 1.00 13.90  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 12.855 -30.623 30.103 1.00 15.11  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.370 -30.668 31.250 1.00 16.38  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.402 -28.225 29.528 1.00 14.68  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.374 -28.555 28.618 1.00 15.51  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.833 -31.671 29.271 1.00 14.29  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.398 -33.001 29.692 1.00 14.23  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.506 -34.067 29.473 1.00 15.65  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.290 -35.231 29.832 1.00 15.83  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.117 -33.413 28.941 1.00 14.94  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.899  -32.574 29.312 1.00 15.34  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.339  -32.971 30.670 1.00 17.94  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.192  -32.145 31.031 1.00 21.20  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.276  -30.977 31.657 1.00 23.79  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.459  -30.502 32.040 1.00 22.92  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.179  -30.282 31.925 1.00 24.66  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.660 -33.688 28.845 1.00 16.30  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.776 -34.568 28.445 1.00 17.37  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 15.207 -35.767 27.680 1.00 17.59  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.559 -36.919 27.960 1.00 18.26  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.606 -35.031 29.656 1.00 20.83  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.465 -33.947 30.280 1.00 28.15  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.597 -34.542 31.091 1.00 35.72  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 18.982 -33.654 32.189 1.00 41.66  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 18.794 -33.924 33.478 1.00 45.05  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.261 -35.081 33.851 1.00 46.09  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 19.139 -33.040 34.404 1.00 44.17  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.228 -35.497 26.785 1.00 16.94  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.507 -36.550 26.077 1.00 16.87  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.157 -36.123 24.664 1.00 14.59  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.979 -34.928 24.417 1.00 13.05  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 12.147 -36.814 26.791 1.00 20.27  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 12.175 -37.883 27.852 1.00 29.11  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.765 -38.138 28.357 1.00 36.63  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 10.693 -39.347 29.268 1.00 42.75  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 9.608  -39.205 30.277 1.00 45.33  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.963 -37.100 23.775 1.00 13.94  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.457 -36.869 22.426 1.00 14.06  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.955 -37.161 22.398 1.00 15.27  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.487 -38.110 23.052 1.00 16.79  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.155 -37.762 21.395 1.00 14.31  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.630 -37.553 21.287 1.00 15.59  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.182 -36.845 20.234 1.00 18.43  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.625 -38.019 22.072 1.00 15.19  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.490 -36.896 20.416 1.00 17.61  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.801 -37.575 21.523 1.00 17.33  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.196 -36.374 21.615 1.00 14.27  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.758  -36.589 21.483 1.00 14.55  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.345  -36.633 20.019 1.00 14.13  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.772  -35.782 19.228 1.00 13.78  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.941  -35.454 22.152 1.00 15.07  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.080  -35.387 23.651 1.00 16.76  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.406  -36.285 24.470 1.00 18.28  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.857  -34.405 24.258 1.00 17.55  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.524  -36.228 25.851 1.00 19.30  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.966  -34.327 25.642 1.00 18.44  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.314  -35.256 26.435 1.00 20.03  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.394  -35.208 27.817 1.00 21.44  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.483  -37.599 19.657 1.00 14.29  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.924  -37.601 18.290 1.00 14.12  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.822  -36.515 18.187 1.00 14.61  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 5.075  -36.309 19.155 1.00 15.01  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.368  -39.016 18.152 1.00 14.97  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 5.967  -39.394 19.558 1.00 15.62  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.938  -38.699 20.486 1.00 13.59  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.749  -35.796 17.071 1.00 14.25  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.751  -34.722 16.874 1.00 14.81  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.257  -34.700 15.441 1.00 13.96  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 4.980  -35.084 14.526 1.00 14.00  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.341  -33.292 17.151 1.00 16.71  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.420  -32.996 18.647 1.00 18.19  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.679  -33.068 16.425 1.00 16.86  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 3.032  -34.214 15.250 1.00 13.00  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.536  -33.802 13.943 1.00 13.02  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.822  -32.280 14.003 1.00 11.17  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.735  -31.663 15.086 1.00 10.99  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 1.025  -34.009 13.812 1.00 15.90  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.740  -35.376 13.588 1.00 20.15  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.129  -31.672 12.872 1.00 9.41   ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.398  -30.224 12.828 1.00 9.31   ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.818  -29.565 11.574 1.00 10.45  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.619  -30.234 10.561 1.00 11.16  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.893  -29.896 13.002 1.00 8.62   ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.831  -30.636 12.075 1.00 8.79   ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.306  -31.899 12.406 1.00 9.62   ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.243  -30.064 10.889 1.00 10.25  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.198  -32.573 11.569 1.00 11.05  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.118  -30.730 10.043 1.00 11.11  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.591  -31.988 10.378 1.00 11.11  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.595  -28.265 11.629 1.00 10.39  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 1.971  -27.569 10.522 1.00 11.75  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.949  -27.279 9.365  1.00 13.75  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.141  -27.624 9.413  1.00 14.52  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.293  -26.302 11.036 1.00 12.82  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.276  -25.358 11.415 1.00 14.03  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.419  -26.729 8.271  1.00 13.62  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.256  -26.323 7.151  1.00 14.95  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.942  -24.972 7.490  1.00 15.74  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.357  -24.173 8.225  1.00 15.70  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.389  -26.197 5.895  1.00 18.44  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.855  -27.558 5.451  1.00 25.00  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 1.136  -27.468 4.115  1.00 33.60  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.883  -28.836 3.526  1.00 41.14  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 0.221  -28.742 2.187  1.00 45.86  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.170  -24.700 7.007  1.00 16.04  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.830  -23.417 7.351  1.00 16.64  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 4.979  -22.199 6.989  1.00 17.53  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.442  -22.110 5.875  1.00 18.42  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.141  -23.434 6.565  1.00 17.56  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.379  -24.860 6.197  1.00 18.86  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 6.015  -25.541 6.133  1.00 16.79  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.834  -21.275 7.935  1.00 16.82  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 3.977  -20.114 7.722  1.00 17.18  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.361  -18.908 8.610  1.00 16.43  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.315  -18.991 9.394  1.00 14.82  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.526  -20.516 7.949  1.00 19.45  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.288  -20.732 9.332  1.00 22.34  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.652  -17.762 8.413  1.00 16.64  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.828  -16.513 9.134  1.00 16.78  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 2.968  -16.609 10.385 1.00 17.20  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.737  -16.673 10.257 1.00 17.48  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.258  -15.372 8.290  1.00 17.56  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.216  -14.561 7.452  1.00 20.54  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.436  -13.458 6.693  1.00 22.12  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.289  -13.905 8.316  1.00 20.62  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.584  -16.606 11.578 1.00 15.99  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.863  -16.753 12.845 1.00 17.23  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.239  -15.638 13.823 1.00 17.72  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.410  -15.293 13.925 1.00 16.44  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.195  -18.155 13.401 1.00 18.63  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.583  -19.235 12.478 1.00 20.92  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.745  -18.325 14.875 1.00 18.88  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 3.049  -20.609 12.735 1.00 23.45  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.249  -15.049 14.519 1.00 19.11  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.516  -13.977 15.472 1.00 20.17  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.302  -14.504 16.673 1.00 19.18  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 2.982  -15.559 17.199 1.00 19.63  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.207  -13.321 15.966 1.00 21.75  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.480  -12.025 16.687 1.00 23.40  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.385  -11.946 18.066 1.00 25.09  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 1.902  -10.903 15.994 1.00 24.84  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.652  -10.756 18.730 1.00 25.85  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.189  -9.718  16.664 1.00 25.91  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 2.047  -9.648  18.025 1.00 25.85  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.365  -13.796 17.065 1.00 18.10  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.200  -14.158 18.209 1.00 18.11  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.301  -12.950 19.125 1.00 19.10  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.713  -11.869 18.691 1.00 18.97  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.618  -14.621 17.805 1.00 17.25  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.446  -14.994 19.045 1.00 17.48  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.559  -15.788 16.808 1.00 16.28  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 4.968  -13.143 20.396 1.00 19.80  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.018  -12.117 21.437 1.00 19.82  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.381  -11.472 21.563 1.00 18.45  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.390  -12.125 21.317 1.00 18.26  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.678  -12.759 22.788 1.00 24.34  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.288  -13.356 22.853 1.00 31.27  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.170  -12.335 22.916 1.00 40.31  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 1.017  -12.711 22.604 1.00 42.31  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.438  -11.162 23.264 1.00 42.38  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.419  -10.214 22.033 1.00 17.91  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.672  -9.503  22.275 1.00 17.61  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.541  -10.237 23.309 1.00 16.47  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.034  -10.851 24.241 1.00 15.96  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.379  -8.100  22.786 1.00 18.01  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 9.857  -10.148 23.134 1.00 15.55  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 10.845 -10.692 24.068 1.00 16.06  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.034 -9.703  24.135 1.00 17.25  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.016 -8.664  23.433 1.00 18.25  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.293 -12.089 23.633 1.00 15.11  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.087 -12.011 22.460 1.00 15.32  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.057 -9.983  24.974 1.00 17.31  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.234 -9.086  25.005 1.00 18.61  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.029 -9.158  23.677 1.00 18.46  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 15.855 -8.286  23.421 1.00 19.08  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.163 -9.405  26.180 1.00 22.13  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.794 -10.782 26.077 1.00 29.65  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 15.101 -11.850 26.903 1.00 42.06  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.735 -12.363 27.853 1.00 46.15  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.914 -12.152 26.621 1.00 44.19  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 14.781 -10.179 22.850 1.00 17.62  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.450 -10.449 21.595 1.00 17.56  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.772 -9.791  20.402 1.00 17.81  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.445 -9.489  19.419 1.00 18.19  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.507 -11.977 21.381 1.00 17.15  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.170 -12.700 22.525 1.00 17.58  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.517 -12.519 22.800 1.00 18.50  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.460 -13.583 23.318 1.00 18.70  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.133 -13.167 23.863 1.00 19.40  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.076 -14.275 24.359 1.00 19.96  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.422 -14.078 24.616 1.00 21.04  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.058 -14.742 25.639 1.00 22.64  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.440 -9.662  20.440 1.00 17.42  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.668 -9.132  19.321 1.00 17.54  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.449 -8.381  19.791 1.00 20.21  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 10.811 -8.803  20.762 1.00 20.62  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.109 -10.296 18.457 1.00 15.42  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.116 -11.237 17.835 1.00 13.96  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.381 -12.474 18.401 1.00 13.84  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 13.828 -10.876 16.702 1.00 13.82  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.269 -13.363 17.812 1.00 13.25  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 14.743 -11.745 16.121 1.00 13.82  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 14.923 -13.009 16.648 1.00 13.98  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 15.870 -13.835 16.071 1.00 14.69  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 10.991 -7.371  19.025 1.00 21.35  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.671  -6.800  19.329 1.00 21.86  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.576  -7.794  18.901 1.00 21.76  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 8.863  -8.767  18.170 1.00 21.10  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.626  -5.537  18.461 1.00 23.36  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.509 -5.853  17.304 1.00 23.72  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.565 -6.824  17.769 1.00 21.29  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.303  -7.531  19.257 1.00 21.73  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.192  -8.386  18.804 1.00 22.03  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.148  -8.321  17.262 1.00 21.73  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.353  -7.234  16.693 1.00 21.66  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 4.875  -7.905  19.397 1.00 22.08  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.065  -9.490  16.604 1.00 20.50  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.175  -9.513  15.148 1.00 19.95  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.649  -10.843 14.575 1.00 20.11  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.382  -11.781 15.327 1.00 20.06  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.675  -9.336  14.771 1.00 19.47  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.504  -10.652 14.928 1.00 17.37  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 9.962  -10.482 15.246 1.00 18.05  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.789 -11.595 14.765 1.00 18.26  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 10.906 -12.775 15.375 1.00 19.73  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.730 -13.701 14.893 1.00 17.00  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.186 -13.046 16.463 1.00 18.62  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.566  -10.943 13.238 1.00 20.10  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.221  -12.207 12.599 1.00 20.17  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.550  -12.885 12.251 1.00 17.20  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.405  -12.262 11.609 1.00 16.86  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.423  -11.979 11.310 1.00 21.96  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.006  -11.536 11.576 1.00 25.93  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 1.995  -12.462 11.772 1.00 27.97  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.691  -10.192 11.712 1.00 28.42  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.691  -12.059 12.046 1.00 30.38  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.399  -9.779  12.007 1.00 30.10  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.400  -10.717 12.171 1.00 31.94  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.889 -10.309 12.432 1.00 35.63  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.740  -14.126 12.706 1.00 14.69  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 7.939  -14.890 12.356 1.00 13.92  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.559  -15.784 11.183 1.00 14.26  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.554  -16.492 11.265 1.00 15.08  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.434  -15.744 13.555 1.00 13.98  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.603  -16.679 13.183 1.00 13.15  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.377 -17.163 14.406 1.00 13.07  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.638 -16.396 15.357 1.00 12.74  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.811 -18.432 14.375 1.00 11.18  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.327  -15.741 10.088 1.00 13.31  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.026  -16.531 8.892  1.00 13.00  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.697  -17.918 8.929  1.00 12.54  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.626  -18.116 9.718  1.00 12.36  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.488  -15.769 7.653  1.00 14.14  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 9.890  -15.538 7.717  1.00 15.62  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.229  -18.859 8.058  1.00 12.19  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.765  -20.214 7.926  1.00 12.07  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.702  -20.984 9.269  1.00 12.93  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.582  -21.804 9.555  1.00 13.62  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.209 -20.158 7.379  1.00 12.56  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.319 -19.500 6.026  1.00 14.66  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.314 -20.244 4.859  1.00 16.92  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.392 -18.184 5.704  1.00 14.89  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.418 -19.363 3.867  1.00 17.17  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.454 -18.112 4.327  1.00 16.54  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.689  -20.674 10.111 1.00 12.33  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.518  -21.294 11.420 1.00 11.99  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.461  -22.390 11.338 1.00 11.96  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.436  -22.213 10.685 1.00 11.55  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.092  -20.211 12.458 1.00 11.86  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.044  -20.626 13.925 1.00 13.74  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.417  -21.109 14.423 1.00 15.17  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.569  -19.454 14.810 1.00 14.27  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.695  -23.515 12.035 1.00 11.88  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.771  -24.659 12.035 1.00 12.31  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.372  -24.950 13.463 1.00 12.74  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.253  -25.052 14.312 1.00 13.45  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.476  -25.878 11.448 1.00 13.45  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.863  -25.683 9.995  1.00 15.60  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.897  -27.036 9.418  1.00 16.17  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.347  -26.877 10.499 1.00 15.09  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.068  -25.079 13.741 1.00 11.35  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.608  -25.347 15.099 1.00 11.28  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.210  -26.799 15.314 1.00 11.60  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.716  -27.459 14.403 1.00 10.93  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.401  -24.470 15.470 1.00 12.29  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.593  -22.959 15.480 1.00 14.72  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.349  -22.278 16.075 1.00 15.42  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.838  -22.539 16.289 1.00 16.03  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.373  -27.264 16.561 1.00 11.32  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 2.971  -28.583 17.014 1.00 12.48  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.433  -28.500 18.457 1.00 12.63  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.764  -27.573 19.208 1.00 12.67  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.155  -29.535 16.968 1.00 12.88  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.605  -29.463 18.828 1.00 11.95  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.092  -29.575 20.181 1.00 13.05  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.166  -30.371 20.905 1.00 14.68  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.426  -31.521 20.554 1.00 15.17  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.299 -30.268 20.221 1.00 13.25  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.752 -30.485 21.663 1.00 13.41  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.339 -29.433 19.464 1.00 13.06  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.887  -29.700 21.789 1.00 14.59  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 3.961  -30.351 22.527 1.00 15.42  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.557  -29.459 23.592 1.00 15.45  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.396  -28.232 23.554 1.00 15.60  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.265  -30.077 24.541 1.00 14.90  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 5.899  -29.319 25.592 1.00 15.07  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.132  -28.542 25.109 1.00 14.63  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 7.992  -29.065 24.385 1.00 14.59  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.259  -30.226 26.794 1.00 16.01  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 6.915  -29.463 27.897 1.00 18.24  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.181  -28.646 28.741 1.00 20.58  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.233  -29.344 28.203 1.00 19.36  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.068  -28.101 29.570 1.00 21.66  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.320  -28.485 29.271 1.00 20.83  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.245  -27.308 25.585 1.00 13.75  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.415  -26.470 25.392 1.00 13.78  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.411  -25.370 26.460 1.00 15.32  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.355  -24.949 26.949 1.00 16.36  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.466  -25.861 23.986 1.00 14.66  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 7.417  -24.930 23.806 1.00 17.89  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 9.589  -24.943 26.842 1.00 15.13  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 9.740  -23.846 27.773 1.00 16.54  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.024 -23.090 27.433 1.00 16.91  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 11.833 -23.586 26.627 1.00 16.15  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 9.619  -24.303 29.252 1.00 19.32  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 10.547 -25.419 29.665 1.00 21.88  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.207 -25.978 31.039 1.00 24.39  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 10.595 -25.345 32.040 1.00 26.61  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.555  -27.040 31.122 1.00 24.35  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.224 -21.873 27.985 1.00 18.07  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.487 -21.159 27.742 1.00 19.67  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 13.683 -22.033 28.144 1.00 20.80  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 13.742 -22.592 29.264 1.00 22.96  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 12.378 -19.915 28.641 1.00 20.37  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 10.906 -19.727 28.863 1.00 20.67  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 10.369 -21.143 28.939 1.00 18.57  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.575 -22.199 27.196 1.00 18.52  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 15.712 -23.094 27.326 1.00 17.25  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 15.653 -24.195 26.273 1.00 15.65  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 16.677 -24.807 25.958 1.00 15.55  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.452 -24.441 25.683 1.00 13.58  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.298 -25.471 24.667 1.00 13.24  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 14.702 -25.070 23.236 1.00 13.00  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 14.827 -25.968 22.385 1.00 13.26  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 12.863 -26.031 24.681 1.00 14.13  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 12.637 -26.916 25.901 1.00 15.70  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.607 -27.541 26.368 1.00 15.61  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.507 -26.960 26.397 1.00 17.66  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 14.964 -23.770 22.964 1.00 12.33  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.353 -23.362 21.588 1.00 12.78  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.625 -24.089 21.137 1.00 13.01  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.543 -24.250 21.946 1.00 12.47  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.526 -21.849 21.465 1.00 14.21  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.001 -20.899 21.701 1.00 16.27  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.665 -24.504 19.877 1.00 12.18  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.834 -25.193 19.347 1.00 12.69  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.688 -26.698 19.270 1.00 12.89  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.470 -27.355 18.575 1.00 12.20  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.671 -27.253 19.955 1.00 11.91  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.398 -28.687 19.871 1.00 12.68  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.029 -29.081 18.442 1.00 12.82  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.267 -28.372 17.783 1.00 12.05  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.616 -30.161 17.923 1.00 13.45  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.381 -30.557 16.534 1.00 14.27  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.044 -31.302 16.342 1.00 13.25  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.662 -32.123 17.189 1.00 14.03  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.606 -31.367 15.986 1.00 17.11  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.795 -30.416 15.660 1.00 19.90  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.247 -32.208 14.756 1.00 18.35  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.100 -31.133 15.152 1.00 22.33  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.337 -30.985 15.232 1.00 11.49  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.141 -31.701 14.759 1.00 11.22  ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.602 -32.543 13.550 1.00 11.63  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.216 -31.998 12.621 1.00 10.44  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 12.044 -30.723 14.300 1.00 10.75  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.821 -31.355 13.610 1.00 13.06  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 10.043 -32.310 14.572 1.00 13.70  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.853  -30.249 13.115 1.00 13.85  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.364 -33.873 13.578 1.00 12.12  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.789 -34.770 12.497 1.00 13.12  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.616 -35.594 11.943 1.00 12.96  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.771 -36.045 12.705 1.00 13.18  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.828 -35.795 13.004 1.00 15.59  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.173 -35.277 13.442 1.00 21.29  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.063 -36.452 13.899 1.00 25.57  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.329 -37.394 12.807 1.00 28.16  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.334 -37.272 11.940 1.00 30.34  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.195 -36.269 12.047 1.00 30.39  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.489 -38.160 10.965 1.00 30.35  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.611 -35.854 10.633 1.00 12.40  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.643 -36.766 10.036 1.00 13.38  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.453 -37.952 9.461  1.00 13.84  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.678 -37.997 9.626  1.00 14.27  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.849 -36.060 8.945  1.00 13.84  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.874 -35.535 7.560  1.00 13.44  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.790 -38.896 8.768  1.00 14.34  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.489 -40.015 8.157  1.00 15.93  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.548 -39.550 7.102  1.00 16.72  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.433 -40.337 6.750  1.00 18.02  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.478 -40.962 7.489  1.00 18.61  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.782 -40.334 6.280  1.00 21.61  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.792  -41.296 5.678  1.00 28.19  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.590  -41.211 5.935  1.00 30.03  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.281 -42.229 4.860  1.00 29.86  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.462 -38.302 6.607  1.00 15.81  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.406 -37.823 5.595  1.00 15.71  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.637 -37.094 6.166  1.00 15.82  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.600 -36.883 5.437  1.00 16.82  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.693 -36.939 4.539  1.00 15.85  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.499 -37.585 3.907  1.00 16.51  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.215 -37.219 4.267  1.00 16.86  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.435 -38.580 2.992  1.00 17.23  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.403 -37.999 3.561  1.00 17.66  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.091 -38.838 2.778  1.00 18.63  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.597 -36.704 7.438  1.00 14.63  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.695 -35.956 8.048  1.00 13.38  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.227 -34.783 8.891  1.00 12.43  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.091 -34.776 9.386  1.00 13.67  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.091 -33.788 9.065  1.00 11.46  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.787 -32.610 9.878  1.00 11.81  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.789 -31.684 9.203  1.00 12.28  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 16.030 -31.243 8.066  1.00 13.60  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.083 -31.853 10.255 1.00 12.27  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.755 -30.580 11.021 1.00 12.98  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.030 -32.761 11.065 1.00 12.17  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.683 -31.363 9.910  1.00 10.94  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.624 -30.490 9.400  1.00 10.44  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.789 -29.037 9.835  1.00 10.59  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.550 -28.109 9.062  1.00 9.28   ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.227 -31.037 9.850  1.00 10.21  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.104 -30.072 9.459  1.00 10.90  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 11.984 -32.404 9.244  1.00 10.83  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.136 -28.859 11.094 1.00 11.12  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.284 -27.532 11.665 1.00 11.14  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.697 -27.581 13.120 1.00 10.27  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.107 -28.629 13.623 1.00 10.63  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.658 -26.431 13.786 1.00 9.78   ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.027 -26.359 15.198 1.00 10.05  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.959 -25.625 15.998 1.00 9.53   ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.348 -24.671 15.492 1.00 9.86   ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.396 -25.651 15.387 1.00 12.02  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.443 -24.301 14.627 1.00 13.01  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.588 -26.560 15.032 1.00 13.45  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.719 -23.449 14.980 1.00 14.89  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.800 -25.983 17.287 1.00 8.37   ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.858 -25.274 18.168 1.00 8.35   ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.202 -23.763 18.218 1.00 8.73   ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.367 -23.403 18.404 1.00 9.52   ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.850 -25.854 19.598 1.00 9.22   ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 11.948 -25.029 20.506 1.00 8.33   ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.417 -27.320 19.583 1.00 10.18  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.186 -22.908 18.041 1.00 8.83   ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.374 -21.467 18.024 1.00 9.55   ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.382 -20.709 18.888 1.00 10.92  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.710 -19.618 19.364 1.00 11.83  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.335 -20.960 16.582 1.00 11.01  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.431 -19.542 16.483 1.00 12.52  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.153 -21.228 19.055 1.00 11.38  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.125  -20.584 19.894 1.00 12.64  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.376  -21.646 20.730 1.00 13.04  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.493  -22.850 20.473 1.00 12.81  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.092  -19.779 19.022 1.00 14.03  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.213  -20.680 18.346 1.00 13.93  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.731  -18.829 18.031 1.00 15.28  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.568  -21.199 21.675 1.00 14.48  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.698  -22.093 22.427 1.00 15.75  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.724  -21.317 23.289 1.00 17.46  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 5.815  -20.087 23.388 1.00 17.53  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.830  -22.027 23.952 1.00 18.80  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.867  -21.395 24.841 1.00 20.43  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.515  -22.065 24.793 1.00 21.97  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.090  -22.510 23.729 1.00 22.15  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.828  -22.116 25.959 1.00 22.82  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.497  -22.704 26.131 1.00 23.61  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.322  -24.086 25.476 1.00 22.25  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.670 -24.334 24.784 1.00 22.75  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.592 -21.744 25.674 1.00 26.78  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.652 -20.473 26.489 1.00 32.73  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.498 -20.456 27.727 1.00 35.11  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.879 -19.379 25.800 1.00 33.49  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.291  -24.963 25.688 1.00 20.46  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.216  -26.320 25.174 1.00 19.08  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.503  -26.460 23.697 1.00 17.03  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.188  -27.494 23.118 1.00 16.97  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.132  -25.455 23.088 1.00 15.81  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.532  -25.503 21.690 1.00 15.57  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 4.063  -25.343 21.611 1.00 15.33  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.691  -24.778 22.522 1.00 16.87  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.844  -24.372 20.879 1.00 16.12  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.287  -24.379 20.872 1.00 17.99  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.271 -23.045 20.334 1.00 19.02  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.244 -25.550 20.047 1.00 17.64  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.667  -25.897 20.563 1.00 12.83  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.094  -25.761 20.292 1.00 12.29  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.217  -25.348 18.824 1.00 12.75  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.505  -25.881 17.955 1.00 11.98  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.961  -27.015 20.651 1.00 13.48  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.433  -28.299 20.006 1.00 13.49  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.454  -26.790 20.327 1.00 14.20  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.061  -24.356 18.558 1.00 12.23  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.271  -23.858 17.208 1.00 11.75  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.689  -24.134 16.744 1.00 11.05  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.647  -23.977 17.509 1.00 10.10  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.821  -24.561 15.477 1.00 11.29  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.094 -24.915 14.875 1.00 10.70  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.367 -24.060 13.638 1.00 11.12  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.512  -23.922 12.767 1.00 11.31  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.098 -26.382 14.441 1.00 10.01  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.612  -27.369 15.484 1.00 9.91   ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.490 -27.922 16.395 1.00 9.92   ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.298  -27.819 15.480 1.00 10.28  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.047 -28.865 17.325 1.00 9.77   ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.853  -28.759 16.421 1.00 10.59  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.731  -29.263 17.345 1.00 10.25  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.586 -23.525 13.567 1.00 10.04  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.075 -22.756 12.427 1.00 9.80   ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.473 -23.763 11.361 1.00 10.83  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.423 -24.523 11.555 1.00 10.34  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.295 -21.938 12.831 1.00 10.20  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.767 -23.754 10.241 1.00 10.44  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.054 -24.664 9.125  1.00 11.34  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.387 -24.342 8.462  1.00 11.04  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.727 -23.166 8.295  1.00 11.54  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.928 -24.558 8.076  1.00 13.15  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.043 -25.571 6.967  1.00 17.60  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.121 -26.773 7.275  1.00 16.48  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.108 -25.155 5.788  1.00 19.60  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.134 -25.381 8.056  1.00 10.46  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.392 -25.197 7.291  1.00 10.67  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.373 -25.969 5.958  1.00 11.18  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.341 -25.894 5.220  1.00 12.03  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.679 -25.541 8.097  1.00 10.42  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.775 -24.710 9.385  1.00 10.98  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.749 -27.034 8.408  1.00 9.33   ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.277 -26.686 5.632  1.00 10.75  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.186 -27.508 4.426  1.00 10.92  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.277 -26.749 3.110  1.00 11.39  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.692 -27.331 2.114  1.00 12.59  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.917 -28.351 4.447  1.00 10.04  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.884 -29.352 5.604  1.00 8.80   ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.542 -30.083 5.561  1.00 9.67   ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.462 -29.213 6.035  1.00 11.00  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.217  -29.613 6.257  1.00 12.87  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.855  -30.862 5.992  1.00 10.96  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.322  -28.770 6.759  1.00 12.45  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.878 -25.491 3.090  1.00 11.17  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.964 -24.666 1.884  1.00 12.48  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.369 -24.091 1.635  1.00 14.07  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.588 -23.512 0.567  1.00 15.03  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.954 -23.513 1.924  1.00 14.02  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.251 -22.508 3.026  1.00 18.83  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.558 -22.948 4.167  1.00 20.29  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.192 -21.278 2.745  1.00 18.71  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.309 -24.210 2.600  1.00 13.65  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.666 -23.657 2.422  1.00 14.18  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.517 -24.655 1.648  1.00 14.18  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.365 -25.354 2.220  1.00 14.52  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.296 -23.298 3.778  1.00 14.62  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.386 -22.414 4.637  1.00 16.62  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.880 -22.319 6.041  1.00 17.69  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.147 -21.046 3.992  1.00 17.06  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.282 -24.725 0.339  1.00 13.85  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.939 -25.712 -0.510 1.00 14.47  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.447 -25.560 -0.589 1.00 16.35  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.147 -26.558 -0.818 1.00 16.70  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.322 -25.751 -1.919 1.00 14.33  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.796 -25.775 -2.001 1.00 14.99  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.338 -25.915 -3.431 1.00 16.22  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.203 -26.891 -1.124 1.00 16.08  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.944 -24.320 -0.398 1.00 17.18  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.372 -24.002 -0.464 1.00 18.21  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.199 -24.612 0.697  1.00 19.26  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.425 -24.644 0.607  1.00 19.08  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.571 -22.477 -0.545 1.00 18.37  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.882 -21.706 0.548  1.00 18.31  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.629 -21.159 0.510  1.00 19.04  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.424 -21.388 1.842  1.00 17.87  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.363 -20.509 1.695  1.00 19.10  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.461 -20.614 2.518  1.00 18.54  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.673 -21.614 2.462  1.00 18.55  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.683 -20.109 3.801  1.00 19.10  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.893 -21.105 3.737  1.00 19.43  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.905 -20.366 4.391  1.00 19.52  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.543 -25.083 1.784  1.00 19.53  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.269 -25.700 2.908  1.00 21.12  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 24.053 -26.947 2.457  1.00 24.97  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 25.065 -27.282 3.075  1.00 24.93  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.290 -26.123 4.013  1.00 19.78  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.710 -25.021 4.886  1.00 20.10  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.676 -25.599 5.856  1.00 20.36  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.817 -24.282 5.632  1.00 20.35  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.564 -27.632 1.397  1.00 27.76  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.138 -28.852 0.830  1.00 31.78  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.155 -28.617 -0.266 1.00 35.29  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.543 -29.586 -0.908 1.00 35.91  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 23.034 -29.705 0.201  1.00 34.46  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 22.021 -30.240 1.164  1.00 39.09  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 22.411 -30.617 2.284  1.00 39.80  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.842 -30.305 0.793  1.00 42.27  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.551 -27.364 -0.536 1.00 37.35  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.541 -27.089 -1.580 1.00 39.68  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.631 -26.129 -1.083 1.00 41.17  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.473 -25.687 -1.870 1.00 42.00  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.863 -26.563 -2.857 1.00 42.72  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.168 -25.227 -2.675 1.00 48.61  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.100 -24.927 -3.715 1.00 56.90  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 24.081 -23.785 -4.233 1.00 57.83  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.277 -25.828 -4.005 1.00 59.22  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BSF C 2 .   ? 23.775 13.681  14.924 1.00 11.30  ? 201 A1BSF A N1  1 
HETATM 2156 C  C4  . A1BSF C 2 .   ? 28.230 9.141   7.188  1.00 13.13  ? 201 A1BSF A C4  1 
HETATM 2157 C  C5  . A1BSF C 2 .   ? 28.527 10.433  6.827  1.00 13.50  ? 201 A1BSF A C5  1 
HETATM 2158 C  C6  . A1BSF C 2 .   ? 27.734 11.475  7.282  1.00 13.59  ? 201 A1BSF A C6  1 
HETATM 2159 C  C7  . A1BSF C 2 .   ? 26.619 11.232  8.086  1.00 13.58  ? 201 A1BSF A C7  1 
HETATM 2160 C  C8  . A1BSF C 2 .   ? 25.759 12.403  8.506  1.00 13.01  ? 201 A1BSF A C8  1 
HETATM 2161 C  C10 . A1BSF C 2 .   ? 24.161 14.501  9.653  1.00 12.48  ? 201 A1BSF A C10 1 
HETATM 2162 C  C13 . A1BSF C 2 .   ? 23.986 14.131  12.559 1.00 12.05  ? 201 A1BSF A C13 1 
HETATM 2163 C  C15 . A1BSF C 2 .   ? 25.324 14.261  11.817 1.00 12.25  ? 201 A1BSF A C15 1 
HETATM 2164 O  O1  . A1BSF C 2 .   ? 24.556 15.696  14.291 1.00 12.93  ? 201 A1BSF A O1  1 
HETATM 2165 C  C14 . A1BSF C 2 .   ? 24.111 14.579  14.006 1.00 12.34  ? 201 A1BSF A C14 1 
HETATM 2166 C  C12 . A1BSF C 2 .   ? 22.904 14.927  11.799 1.00 12.18  ? 201 A1BSF A C12 1 
HETATM 2167 C  C11 . A1BSF C 2 .   ? 22.800 14.451  10.345 1.00 12.44  ? 201 A1BSF A C11 1 
HETATM 2168 N  N   . A1BSF C 2 .   ? 25.189 13.789  10.437 1.00 12.30  ? 201 A1BSF A N   1 
HETATM 2169 C  C9  . A1BSF C 2 .   ? 25.960 12.783  9.963  1.00 12.54  ? 201 A1BSF A C9  1 
HETATM 2170 O  O   . A1BSF C 2 .   ? 26.782 12.205  10.664 1.00 12.30  ? 201 A1BSF A O   1 
HETATM 2171 C  C2  . A1BSF C 2 .   ? 26.299 9.905   8.432  1.00 12.98  ? 201 A1BSF A C2  1 
HETATM 2172 C  C1  . A1BSF C 2 .   ? 25.032 9.560   9.198  1.00 13.06  ? 201 A1BSF A C1  1 
HETATM 2173 C  C   . A1BSF C 2 .   ? 24.829 8.095   9.563  1.00 13.01  ? 201 A1BSF A C   1 
HETATM 2174 C  C3  . A1BSF C 2 .   ? 27.129 8.877   7.990  1.00 12.69  ? 201 A1BSF A C3  1 
HETATM 2175 ZN ZN  . ZN    D 3 .   ? 23.167 -5.551  26.978 1.00 17.06  2 202 ZN    A ZN  1 
HETATM 2176 N  N1  . A1BSF E 2 .   ? 11.747 -16.896 17.998 1.00 14.29  ? 201 A1BSF C N1  1 
HETATM 2177 C  C4  . A1BSF E 2 .   ? 7.739  -21.465 26.064 1.00 16.17  ? 201 A1BSF C C4  1 
HETATM 2178 C  C5  . A1BSF E 2 .   ? 7.580  -20.160 26.474 1.00 16.29  ? 201 A1BSF C C5  1 
HETATM 2179 C  C6  . A1BSF E 2 .   ? 8.388  -19.167 25.947 1.00 15.91  ? 201 A1BSF C C6  1 
HETATM 2180 C  C7  . A1BSF E 2 .   ? 9.378  -19.464 25.012 1.00 15.36  ? 201 A1BSF C C7  1 
HETATM 2181 C  C8  . A1BSF E 2 .   ? 10.285 -18.350 24.530 1.00 14.83  ? 201 A1BSF C C8  1 
HETATM 2182 C  C10 . A1BSF E 2 .   ? 11.797 -16.212 23.300 1.00 13.42  ? 201 A1BSF C C10 1 
HETATM 2183 C  C13 . A1BSF E 2 .   ? 11.795 -16.607 20.392 1.00 13.07  ? 201 A1BSF C C13 1 
HETATM 2184 C  C15 . A1BSF E 2 .   ? 10.516 -16.441 21.218 1.00 12.93  ? 201 A1BSF C C15 1 
HETATM 2185 O  O1  . A1BSF E 2 .   ? 11.137 -14.894 18.839 1.00 13.43  ? 201 A1BSF C O1  1 
HETATM 2186 C  C14 . A1BSF E 2 .   ? 11.529 -16.055 19.001 1.00 13.90  ? 201 A1BSF C C14 1 
HETATM 2187 C  C12 . A1BSF E 2 .   ? 12.969 -15.879 21.077 1.00 13.14  ? 201 A1BSF C C12 1 
HETATM 2188 C  C11 . A1BSF E 2 .   ? 13.129 -16.290 22.547 1.00 12.75  ? 201 A1BSF C C11 1 
HETATM 2189 N  N   . A1BSF E 2 .   ? 10.737 -16.935 22.579 1.00 13.47  ? 201 A1BSF C N   1 
HETATM 2190 C  C9  . A1BSF E 2 .   ? 9.966  -17.914 23.110 1.00 14.15  ? 201 A1BSF C C9  1 
HETATM 2191 O  O   . A1BSF E 2 .   ? 9.032  -18.410 22.496 1.00 13.46  ? 201 A1BSF C O   1 
HETATM 2192 C  C2  . A1BSF E 2 .   ? 9.551  -20.800 24.603 1.00 15.65  ? 201 A1BSF C C2  1 
HETATM 2193 C  C1  . A1BSF E 2 .   ? 10.664 -21.201 23.652 1.00 15.87  ? 201 A1BSF C C1  1 
HETATM 2194 C  C   . A1BSF E 2 .   ? 10.805 -22.670 23.296 1.00 15.81  ? 201 A1BSF C C   1 
HETATM 2195 C  C3  . A1BSF E 2 .   ? 8.714  -21.784 25.132 1.00 15.97  ? 201 A1BSF C C3  1 
HETATM 2196 ZN ZN  . ZN    F 3 .   ? 10.565 -35.701 5.575  1.00 13.96  2 202 ZN    C ZN  1 
HETATM 2197 O  O   . HOH   G 4 .   ? 7.079  7.487   31.630 1.00 34.12  ? 301 HOH   A O   1 
HETATM 2198 O  O   . HOH   G 4 .   ? 19.635 10.343  17.596 1.00 226.04 ? 302 HOH   A O   1 
HETATM 2199 O  O   . HOH   G 4 .   ? 11.591 -2.027  27.849 1.00 22.49  ? 303 HOH   A O   1 
HETATM 2200 O  O   . HOH   G 4 .   ? 31.767 7.166   23.203 1.00 23.48  ? 304 HOH   A O   1 
HETATM 2201 O  O   . HOH   G 4 .   ? 23.674 7.313   28.226 1.00 17.35  ? 305 HOH   A O   1 
HETATM 2202 O  O   . HOH   G 4 .   ? 11.272 11.759  9.459  1.00 30.33  ? 306 HOH   A O   1 
HETATM 2203 O  O   . HOH   G 4 .   ? -1.752 15.614  20.254 1.00 22.33  ? 307 HOH   A O   1 
HETATM 2204 O  O   . HOH   G 4 .   ? 14.793 22.328  24.505 1.00 17.52  ? 308 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 4 .   ? 30.235 20.262  7.541  1.00 34.11  ? 309 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 4 .   ? 12.986 13.239  16.745 1.00 112.09 ? 310 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 4 .   ? 6.244  3.083   28.904 1.00 36.83  ? 311 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 4 .   ? 11.104 21.360  24.625 1.00 25.54  ? 312 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 4 .   ? 12.328 17.907  12.822 1.00 31.32  ? 313 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 4 .   ? 27.996 3.093   -0.132 1.00 16.75  ? 314 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 4 .   ? 23.741 1.737   -0.740 1.00 12.83  ? 315 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 4 .   ? 29.037 -7.316  25.321 1.00 51.32  ? 316 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 4 .   ? 17.852 -7.834  21.705 1.00 27.34  ? 317 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 4 .   ? 32.027 5.464   14.935 1.00 184.21 ? 318 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 4 .   ? 6.821  15.454  29.153 1.00 32.67  ? 319 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 4 .   ? 18.610 13.403  6.442  1.00 24.36  ? 320 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 4 .   ? 31.115 -1.908  29.546 1.00 40.47  ? 321 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 4 .   ? 31.037 12.665  9.010  1.00 33.64  ? 322 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 4 .   ? 34.876 13.830  16.273 1.00 21.74  ? 323 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 4 .   ? 18.743 -11.649 27.251 1.00 23.15  ? 324 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 4 .   ? 23.501 16.466  27.343 1.00 41.19  ? 325 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 4 .   ? 21.451 10.052  32.321 1.00 28.55  ? 326 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 4 .   ? 25.470 17.772  12.821 1.00 12.78  ? 327 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 4 .   ? 28.207 -6.303  3.342  1.00 21.97  ? 328 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 4 .   ? 26.599 -7.997  23.678 1.00 45.75  ? 329 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 4 .   ? 16.060 -0.448  4.884  1.00 26.56  ? 330 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 4 .   ? 5.101  3.059   20.909 1.00 20.59  ? 331 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 4 .   ? 4.075  20.342  15.305 1.00 29.82  ? 332 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 4 .   ? 15.082 8.700   13.370 1.00 11.55  ? 333 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 4 .   ? 17.067 20.807  22.855 1.00 21.12  ? 334 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 4 .   ? 17.449 2.272   9.370  1.00 17.74  ? 335 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 4 .   ? 27.015 19.123  14.937 1.00 16.24  ? 336 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 4 .   ? 21.525 9.771   23.354 1.00 10.13  ? 337 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 4 .   ? 25.116 4.200   -1.455 1.00 15.44  ? 338 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 4 .   ? 23.902 3.729   29.098 1.00 18.58  ? 339 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 4 .   ? 35.106 14.815  24.760 1.00 32.80  ? 340 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 4 .   ? 24.160 8.344   1.444  1.00 18.89  ? 341 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 4 .   ? 3.526  18.048  23.737 1.00 25.90  ? 342 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 4 .   ? 34.493 -0.793  16.586 1.00 11.75  ? 343 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 4 .   ? 16.316 18.817  27.010 1.00 30.57  ? 344 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 4 .   ? 30.004 7.088   4.326  1.00 19.19  ? 345 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 4 .   ? 32.179 2.731   4.935  1.00 21.09  ? 346 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 4 .   ? 25.435 1.573   29.901 1.00 16.92  ? 347 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 4 .   ? 13.003 1.286   33.511 1.00 29.68  ? 348 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 4 .   ? 28.362 0.729   26.829 1.00 12.99  ? 349 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 4 .   ? 11.335 -0.244  15.653 1.00 19.36  ? 350 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 4 .   ? 17.927 16.486  28.711 1.00 40.01  ? 351 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 4 .   ? 30.918 5.553   7.746  1.00 19.17  ? 352 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 4 .   ? 20.380 2.287   9.289  1.00 10.78  ? 353 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 4 .   ? 4.692  10.639  15.239 1.00 37.48  ? 354 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 4 .   ? 19.944 12.054  8.569  1.00 14.10  ? 355 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 4 .   ? 17.195 0.626   2.728  1.00 23.74  ? 356 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 4 .   ? 24.396 -5.276  0.891  1.00 31.56  ? 357 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 4 .   ? 17.164 18.583  15.637 1.00 9.60   ? 358 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 4 .   ? 21.924 -6.007  0.438  1.00 40.29  ? 359 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 4 .   ? 29.176 13.658  11.153 1.00 24.85  ? 360 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 4 .   ? 29.807 -2.365  8.153  1.00 17.89  ? 361 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 4 .   ? 16.952 4.632   5.936  1.00 20.25  ? 362 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 4 .   ? 24.743 -9.134  22.992 1.00 36.88  ? 363 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 4 .   ? 26.996 -6.062  0.914  1.00 33.02  ? 364 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 4 .   ? 23.527 10.941  21.346 1.00 13.23  ? 365 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 4 .   ? 4.130  20.151  21.719 1.00 26.88  ? 366 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 4 .   ? 4.043  4.258   28.081 1.00 42.62  ? 367 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 4 .   ? 22.796 10.625  22.619 1.00 51.15  ? 368 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 4 .   ? 34.800 -6.477  21.624 1.00 31.94  ? 369 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 4 .   ? 29.872 -2.341  3.378  1.00 26.44  ? 370 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 4 .   ? 22.146 -8.271  19.335 1.00 34.31  ? 371 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 4 .   ? 4.113  9.916   17.856 1.00 29.79  ? 372 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 4 .   ? 16.923 8.994   6.748  1.00 14.77  ? 373 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 4 .   ? 13.575 18.874  14.756 1.00 23.36  ? 374 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 4 .   ? 28.891 21.968  21.992 1.00 27.30  ? 375 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 4 .   ? 30.286 -5.858  26.504 1.00 25.93  ? 376 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 4 .   ? 5.138  10.833  12.887 1.00 30.97  ? 377 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 4 .   ? 19.957 -4.926  15.258 1.00 23.80  ? 378 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 4 .   ? 29.770 25.994  16.020 1.00 26.72  ? 379 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 4 .   ? 9.134  3.832   11.779 1.00 29.18  ? 380 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 4 .   ? 29.309 25.654  13.232 1.00 28.17  ? 381 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 4 .   ? 29.727 6.331   29.876 1.00 28.97  ? 382 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 4 .   ? 34.061 0.306   8.579  1.00 15.74  ? 383 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 4 .   ? 35.559 14.536  20.169 1.00 19.01  ? 384 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 4 .   ? 32.987 -2.655  15.326 1.00 16.80  ? 385 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 4 .   ? 21.272 25.087  9.988  1.00 22.35  ? 386 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 4 .   ? 20.280 20.510  24.488 1.00 28.15  ? 387 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 4 .   ? 30.826 -3.272  11.937 1.00 23.26  ? 388 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 4 .   ? 27.960 16.123  10.470 1.00 19.94  ? 389 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 4 .   ? 14.480 1.581   13.508 1.00 24.27  ? 390 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 4 .   ? 3.899  14.882  10.574 1.00 22.07  ? 391 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 4 .   ? 5.598  -2.257  26.143 1.00 43.29  ? 392 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 4 .   ? 20.573 23.799  14.710 1.00 35.66  ? 393 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 4 .   ? 25.230 -5.290  32.215 1.00 30.07  ? 394 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 4 .   ? 27.897 11.925  27.549 1.00 21.32  ? 395 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 4 .   ? 15.570 12.112  30.635 1.00 33.60  ? 396 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 4 .   ? 15.116 23.222  17.153 1.00 17.38  ? 397 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 4 .   ? 17.668 20.133  13.570 1.00 20.72  ? 398 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 4 .   ? 18.428 -5.244  30.613 1.00 24.72  ? 399 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 4 .   ? 31.202 4.091   6.800  1.00 35.92  ? 400 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 4 .   ? 22.920 20.708  20.362 1.00 19.05  ? 401 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 4 .   ? 34.585 3.194   26.291 1.00 24.59  ? 402 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 4 .   ? 19.623 9.562   8.039  1.00 17.80  ? 403 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 4 .   ? 2.129  14.115  24.816 1.00 40.48  ? 404 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 4 .   ? 0.790  17.149  23.111 1.00 45.35  ? 405 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 4 .   ? 6.730  16.363  8.966  1.00 24.49  ? 406 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 4 .   ? 31.636 14.584  12.746 1.00 20.75  ? 407 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 4 .   ? 12.262 18.462  26.458 1.00 21.02  ? 408 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 4 .   ? 16.145 -0.495  12.626 1.00 20.54  ? 409 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 4 .   ? 23.865 17.943  6.167  1.00 29.50  ? 410 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 4 .   ? 2.516  8.553   26.164 1.00 25.33  ? 411 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 4 .   ? 32.129 22.277  11.271 1.00 34.43  ? 412 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 4 .   ? 11.265 2.075   12.449 1.00 22.42  ? 413 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 4 .   ? 23.311 -11.545 30.520 1.00 50.88  ? 414 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 4 .   ? 20.052 13.953  29.060 1.00 28.72  ? 415 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 4 .   ? 32.030 8.925   4.659  1.00 29.36  ? 416 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 4 .   ? 14.280 -4.072  16.313 1.00 31.62  ? 417 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 4 .   ? 32.656 12.262  27.782 1.00 31.06  ? 418 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 4 .   ? 31.028 9.939   13.625 1.00 38.02  ? 419 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 4 .   ? 13.181 8.562   11.155 1.00 14.23  ? 420 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 4 .   ? 9.252  9.626   10.257 1.00 31.50  ? 421 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 4 .   ? 29.019 -0.461  35.281 1.00 67.25  ? 422 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 4 .   ? 15.884 8.305   33.796 1.00 31.09  ? 423 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 4 .   ? 19.662 -9.675  20.406 1.00 23.10  ? 424 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 4 .   ? 8.124  -5.607  25.244 1.00 115.00 ? 425 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 4 .   ? 18.095 -3.774  14.568 1.00 35.87  ? 426 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 4 .   ? 32.751 5.440   4.523  1.00 32.31  ? 427 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 4 .   ? 19.235 -6.315  32.868 1.00 59.10  ? 428 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 4 .   ? 17.995 22.665  16.196 1.00 32.61  ? 429 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 4 .   ? 16.810 7.663   4.438  1.00 25.33  ? 430 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 4 .   ? 35.825 -5.018  16.779 1.00 30.86  ? 431 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 4 .   ? 31.653 -7.141  18.041 1.00 34.72  ? 432 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 4 .   ? 3.630  2.340   18.760 1.00 30.03  ? 433 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 4 .   ? 26.362 -6.533  29.923 1.00 31.77  ? 434 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 4 .   ? 2.447  21.270  8.323  1.00 45.99  ? 435 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 4 .   ? 12.173 -2.607  15.511 1.00 33.10  ? 436 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 4 .   ? 8.061  -2.414  17.337 1.00 16.35  ? 437 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 4 .   ? 26.049 21.723  5.837  1.00 40.00  ? 438 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 4 .   ? 22.335 11.748  7.630  1.00 31.00  ? 439 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 4 .   ? 29.485 1.035   32.898 1.00 63.55  ? 440 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 4 .   ? 4.938  22.896  6.589  1.00 42.57  ? 441 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 4 .   ? 5.783  0.461   29.261 1.00 44.41  ? 442 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 4 .   ? 25.694 18.581  26.792 1.00 42.14  ? 443 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 4 .   ? 27.716 16.333  7.851  1.00 31.73  ? 444 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 4 .   ? 8.684  -3.002  27.403 1.00 38.81  ? 445 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 4 .   ? 13.921 21.703  14.881 1.00 20.83  ? 446 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 4 .   ? 33.044 0.627   6.002  1.00 20.87  ? 447 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 4 .   ? 9.056  21.369  12.483 1.00 35.14  ? 448 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 4 .   ? 7.292  19.262  26.836 1.00 39.74  ? 449 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 4 .   ? 30.811 -3.121  5.859  1.00 26.26  ? 450 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 4 .   ? 23.161 22.783  18.568 1.00 26.33  ? 451 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 4 .   ? 2.012  16.389  9.398  1.00 32.22  ? 452 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 4 .   ? 17.831 13.109  30.448 1.00 37.73  ? 453 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 4 .   ? 28.220 1.670   29.447 1.00 24.75  ? 454 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 4 .   ? 33.778 -2.445  9.195  1.00 20.19  ? 455 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 4 .   ? 2.713  3.871   17.133 1.00 27.20  ? 456 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 4 .   ? 25.403 6.587   30.224 1.00 45.07  ? 457 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 4 .   ? 1.736  20.457  12.618 1.00 39.41  ? 458 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 4 .   ? 34.939 11.603  15.615 1.00 37.35  ? 459 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 4 .   ? 13.003 10.014  8.564  1.00 27.63  ? 460 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 4 .   ? 25.385 15.231  6.242  1.00 37.44  ? 461 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 4 .   ? 15.802 -2.878  13.419 1.00 37.72  ? 462 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 4 .   ? 31.398 -3.865  9.492  1.00 20.83  ? 463 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 4 .   ? 28.393 4.153   30.605 1.00 27.56  ? 464 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 4 .   ? 23.212 13.994  6.213  1.00 29.73  ? 465 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 4 .   ? 32.057 25.253  12.288 1.00 37.47  ? 466 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 4 .   ? 31.966 24.064  20.889 1.00 48.96  ? 467 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 4 .   ? 28.786 -9.330  6.828  1.00 32.04  ? 468 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 4 .   ? 0.760  17.546  27.419 1.00 57.41  ? 469 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 4 .   ? -0.537 -29.258 9.558  1.00 229.00 ? 301 HOH   C O   1 
HETATM 2367 O  O   . HOH   H 4 .   ? 5.805  -28.303 7.993  1.00 218.79 ? 302 HOH   C O   1 
HETATM 2368 O  O   . HOH   H 4 .   ? 10.321 -28.920 1.543  1.00 208.23 ? 303 HOH   C O   1 
HETATM 2369 O  O   . HOH   H 4 .   ? 22.207 -32.588 3.774  1.00 24.85  ? 304 HOH   C O   1 
HETATM 2370 O  O   . HOH   H 4 .   ? 35.627 -15.425 15.954 1.00 32.50  ? 305 HOH   C O   1 
HETATM 2371 O  O   . HOH   H 4 .   ? 24.212 -37.411 10.565 1.00 37.94  ? 306 HOH   C O   1 
HETATM 2372 O  O   . HOH   H 4 .   ? 22.805 -36.133 12.473 1.00 31.86  ? 307 HOH   C O   1 
HETATM 2373 O  O   . HOH   H 4 .   ? 30.936 -10.616 10.356 1.00 29.34  ? 308 HOH   C O   1 
HETATM 2374 O  O   . HOH   H 4 .   ? 20.096 -8.445  7.582  1.00 23.54  ? 309 HOH   C O   1 
HETATM 2375 O  O   . HOH   H 4 .   ? 10.249 -23.009 4.705  1.00 25.91  ? 310 HOH   C O   1 
HETATM 2376 O  O   . HOH   H 4 .   ? 1.042  -33.703 20.567 1.00 32.83  ? 311 HOH   C O   1 
HETATM 2377 O  O   . HOH   H 4 .   ? 17.198 -37.870 3.123  1.00 34.51  ? 312 HOH   C O   1 
HETATM 2378 O  O   . HOH   H 4 .   ? 12.737 -13.686 4.788  1.00 38.02  ? 313 HOH   C O   1 
HETATM 2379 O  O   . HOH   H 4 .   ? 20.311 -22.469 18.633 1.00 12.00  ? 314 HOH   C O   1 
HETATM 2380 O  O   . HOH   H 4 .   ? 27.508 -27.901 2.407  1.00 29.66  ? 315 HOH   C O   1 
HETATM 2381 O  O   . HOH   H 4 .   ? 31.267 -10.849 16.444 1.00 17.76  ? 316 HOH   C O   1 
HETATM 2382 O  O   . HOH   H 4 .   ? 23.765 -9.254  7.782  1.00 19.42  ? 317 HOH   C O   1 
HETATM 2383 O  O   . HOH   H 4 .   ? 23.502 -31.134 15.253 1.00 25.23  ? 318 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 4 .   ? 3.784  -23.570 3.762  1.00 26.16  ? 319 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 4 .   ? 30.033 -25.482 17.731 1.00 31.22  ? 320 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 4 .   ? 5.130  -31.295 -1.858 1.00 29.37  ? 321 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 4 .   ? 26.006 -33.319 5.824  1.00 42.43  ? 322 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 4 .   ? 16.063 -39.190 9.833  1.00 38.38  ? 323 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 4 .   ? 10.460 -12.901 20.494 1.00 14.15  ? 324 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 4 .   ? 1.968  -33.086 18.430 1.00 37.55  ? 325 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 4 .   ? 16.046 -20.241 7.148  1.00 203.59 ? 326 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 4 .   ? 7.265  -37.180 29.239 1.00 28.96  ? 327 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 4 .   ? 17.837 -10.003 9.523  1.00 14.10  ? 328 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 4 .   ? 21.162 -28.603 -2.565 1.00 62.32  ? 329 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 4 .   ? 18.683 -31.206 31.112 1.00 31.50  ? 330 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 4 .   ? 30.955 -21.447 13.135 1.00 35.74  ? 331 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 4 .   ? 29.385 -27.952 9.880  1.00 18.95  ? 332 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 4 .   ? 12.140 -29.401 33.628 1.00 17.35  ? 333 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 4 .   ? 18.658 -29.910 29.587 1.00 24.62  ? 334 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 4 .   ? 21.158 -27.390 -4.650 1.00 54.20  ? 335 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 4 .   ? 8.294  -28.522 2.969  1.00 14.46  ? 336 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 4 .   ? 18.454 -11.938 5.262  1.00 27.66  ? 337 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 4 .   ? -0.626 -17.274 11.462 1.00 28.03  ? 338 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 4 .   ? 11.331 -36.166 31.472 1.00 23.08  ? 339 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 4 .   ? 10.349 -13.864 5.619  1.00 47.21  ? 340 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 4 .   ? 13.084 -27.335 -0.085 1.00 174.66 ? 341 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 4 .   ? 8.625  -11.470 18.468 1.00 13.85  ? 342 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 4 .   ? 3.879  -8.924  22.656 1.00 26.05  ? 343 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 4 .   ? 0.163  -15.304 22.551 1.00 27.69  ? 344 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 4 .   ? 15.809 -21.939 -1.655 1.00 30.08  ? 345 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 4 .   ? 34.631 -11.031 10.878 1.00 41.65  ? 346 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 4 .   ? 0.623  -29.617 24.765 1.00 31.88  ? 347 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 4 .   ? 15.055 -28.663 23.168 1.00 12.83  ? 348 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 4 .   ? 18.048 -28.614 22.933 1.00 21.88  ? 349 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 4 .   ? 0.890  -31.705 17.125 1.00 12.76  ? 350 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 4 .   ? 26.344 -22.864 -0.264 1.00 44.44  ? 351 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 4 .   ? 5.817  -23.419 28.649 1.00 28.34  ? 352 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 4 .   ? 0.576  -16.758 17.856 1.00 27.97  ? 353 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 4 .   ? 27.604 -15.106 2.512  1.00 36.83  ? 354 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 4 .   ? 17.511 -17.452 25.919 1.00 26.93  ? 355 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 4 .   ? 9.844  -26.274 3.579  1.00 11.78  ? 356 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 4 .   ? 32.730 -16.891 6.747  1.00 45.12  ? 357 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 4 .   ? 23.448 -12.780 19.270 1.00 28.51  ? 358 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 4 .   ? 16.457 -14.006 3.943  1.00 32.28  ? 359 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 4 .   ? 30.411 -20.174 19.215 1.00 22.81  ? 360 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 4 .   ? 9.688  -40.238 0.804  1.00 40.42  ? 361 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 4 .   ? 12.721 -6.295  22.069 1.00 24.08  ? 362 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 4 .   ? 12.949 -20.692 9.428  1.00 9.25   ? 363 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 4 .   ? 19.741 -31.143 26.930 1.00 30.98  ? 364 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 4 .   ? 11.317 -19.630 11.465 1.00 10.05  ? 365 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 4 .   ? 18.252 -12.406 16.755 1.00 11.90  ? 366 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 4 .   ? 16.066 -18.700 24.142 1.00 16.08  ? 367 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 4 .   ? 15.314 -7.839  17.104 1.00 41.42  ? 368 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 4 .   ? 26.227 -21.514 20.951 1.00 31.56  ? 369 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 4 .   ? 14.416 -10.223 8.724  1.00 26.74  ? 370 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 4 .   ? 21.993 -12.163 17.256 1.00 22.75  ? 371 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 4 .   ? 19.046 -22.178 25.370 1.00 25.96  ? 372 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 4 .   ? 29.732 -26.435 3.003  1.00 32.09  ? 373 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 4 .   ? 14.789 -35.841 17.044 1.00 17.19  ? 374 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 4 .   ? 3.768  -36.290 6.893  1.00 22.16  ? 375 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 4 .   ? 26.059 -14.947 15.435 1.00 170.20 ? 376 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 4 .   ? 5.752  -32.928 24.470 1.00 17.81  ? 377 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 4 .   ? 6.394  -18.294 5.893  1.00 15.70  ? 378 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 4 .   ? 17.963 -10.824 18.906 1.00 32.97  ? 379 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 4 .   ? 8.606  -38.591 9.490  1.00 20.14  ? 380 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 4 .   ? 24.877 -23.728 20.022 1.00 19.14  ? 381 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 4 .   ? 10.385 -27.468 34.012 1.00 22.63  ? 382 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 4 .   ? -0.517 -15.838 14.088 1.00 26.09  ? 383 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 4 .   ? 5.205  -17.816 25.101 1.00 32.64  ? 384 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 4 .   ? 26.089 -26.875 19.659 1.00 39.50  ? 385 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 4 .   ? 23.871 -28.861 19.048 1.00 28.10  ? 386 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 4 .   ? 5.486  -29.303 7.236  1.00 13.50  ? 387 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 4 .   ? 6.709  -16.633 22.383 1.00 29.00  ? 388 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 4 .   ? 18.796 -31.450 19.398 1.00 17.95  ? 389 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 4 .   ? 30.567 -9.415  18.441 1.00 42.02  ? 390 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 4 .   ? 8.152  -14.427 23.011 1.00 22.95  ? 391 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 4 .   ? 8.121  -23.867 32.735 1.00 43.28  ? 392 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 4 .   ? 5.689  -33.273 29.896 1.00 40.63  ? 393 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 4 .   ? 9.467  -10.132 11.309 1.00 37.19  ? 394 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 4 .   ? 28.714 -33.329 12.565 1.00 27.73  ? 395 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 4 .   ? 7.988  -35.185 0.658  1.00 18.18  ? 396 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 4 .   ? 14.298 -16.646 3.628  1.00 29.30  ? 397 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 4 .   ? 4.251  -24.597 25.995 1.00 24.43  ? 398 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 4 .   ? 6.069  -8.531  11.524 1.00 30.46  ? 399 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 4 .   ? 22.291 -12.214 5.785  1.00 26.49  ? 400 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 4 .   ? 20.898 -11.912 21.219 1.00 27.19  ? 401 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 4 .   ? 8.357  -39.647 24.518 1.00 40.64  ? 402 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 4 .   ? 34.396 -20.636 12.696 1.00 36.31  ? 403 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 4 .   ? 21.991 -14.791 23.491 1.00 26.03  ? 404 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 4 .   ? 16.927 -8.363  15.133 1.00 31.01  ? 405 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 4 .   ? 32.065 -16.572 20.607 1.00 20.74  ? 406 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 4 .   ? 19.397 -7.468  15.165 1.00 21.98  ? 407 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 4 .   ? 31.291 -22.057 4.930  1.00 30.39  ? 408 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 4 .   ? 22.217 -22.586 20.773 1.00 14.77  ? 409 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 4 .   ? 18.125 -38.704 24.095 1.00 33.86  ? 410 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 4 .   ? 4.461  -16.082 21.272 1.00 26.69  ? 411 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 4 .   ? 29.122 -14.872 22.592 1.00 22.04  ? 412 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 4 .   ? 1.969  -17.840 5.779  1.00 36.83  ? 413 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 4 .   ? 19.943 -20.361 9.859  1.00 115.46 ? 414 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 4 .   ? 4.408  -20.750 19.740 1.00 25.83  ? 415 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 4 .   ? 11.955 -9.836  12.446 1.00 30.76  ? 416 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 4 .   ? 15.313 -35.705 1.682  1.00 19.43  ? 417 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 4 .   ? 31.012 -28.989 11.910 1.00 28.65  ? 418 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 4 .   ? 12.296 -39.197 12.959 1.00 24.14  ? 419 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 4 .   ? 15.795 -20.294 0.536  1.00 57.52  ? 420 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 4 .   ? 26.951 -34.694 12.419 1.00 49.14  ? 421 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 4 .   ? 16.488 -21.251 24.714 1.00 31.33  ? 422 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 4 .   ? 1.143  -34.607 17.899 1.00 19.51  ? 423 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 4 .   ? 6.632  -39.503 14.319 1.00 27.33  ? 424 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 4 .   ? 28.003 -9.347  18.899 1.00 48.62  ? 425 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 4 .   ? 20.449 -9.190  17.527 1.00 29.20  ? 426 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 4 .   ? 17.758 -18.442 1.719  1.00 40.28  ? 427 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 4 .   ? 26.363 -33.109 14.151 1.00 33.04  ? 428 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 4 .   ? 31.439 -26.359 -3.296 1.00 53.34  ? 429 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 4 .   ? 13.400 -19.339 0.010  1.00 79.62  ? 430 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 4 .   ? 6.976  -20.406 4.382  1.00 37.54  ? 431 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 4 .   ? 7.026  -36.497 2.916  1.00 19.61  ? 432 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 4 .   ? 21.348 -35.565 35.344 1.00 49.41  ? 433 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 4 .   ? 3.997  -18.501 18.748 1.00 38.94  ? 434 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 4 .   ? 18.652 -22.261 -2.099 1.00 25.41  ? 435 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 4 .   ? 17.018 -34.647 17.902 1.00 30.77  ? 436 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 4 .   ? 0.030  -34.525 10.209 1.00 43.71  ? 437 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 4 .   ? 24.497 -15.839 23.211 1.00 55.53  ? 438 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 4 .   ? 33.357 -9.434  20.338 1.00 49.86  ? 439 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 4 .   ? 9.811  -10.243 27.434 1.00 38.17  ? 440 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 4 .   ? 30.574 -31.100 13.371 1.00 26.30  ? 441 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 4 .   ? 29.010 -22.174 20.897 1.00 26.34  ? 442 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 4 .   ? 2.617  -29.060 27.176 1.00 40.91  ? 443 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 4 .   ? 30.999 -11.294 7.413  1.00 54.81  ? 444 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 4 .   ? 15.864 -41.067 11.478 1.00 28.29  ? 445 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 4 .   ? 13.633 -18.729 25.379 1.00 34.96  ? 446 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 4 .   ? 9.618  -14.195 26.062 1.00 35.26  ? 447 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 4 .   ? 31.648 -23.154 15.260 1.00 30.85  ? 448 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 4 .   ? 15.759 -40.079 2.843  1.00 36.46  ? 449 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 4 .   ? 32.876 -9.259  11.713 1.00 32.75  ? 450 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 4 .   ? 32.422 -19.236 20.903 1.00 23.61  ? 451 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 4 .   ? 31.818 -27.056 13.843 1.00 27.87  ? 452 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 4 .   ? 8.557  -24.073 2.559  1.00 24.99  ? 453 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 4 .   ? 25.947 -17.930 24.150 1.00 33.34  ? 454 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 4 .   ? 19.685 -19.758 -2.775 1.00 30.07  ? 455 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 4 .   ? 5.319  -25.234 2.428  1.00 27.94  ? 456 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 4 .   ? 29.709 -8.512  9.120  1.00 26.14  ? 457 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 4 .   ? 13.211 -16.804 26.770 1.00 26.57  ? 458 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 4 .   ? 26.247 -14.265 -0.016 1.00 47.86  ? 459 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 4 .   ? 5.697  -27.920 2.875  1.00 25.57  ? 460 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 4 .   ? 35.791 -10.273 8.367  1.00 64.46  ? 461 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 4 .   ? 5.400  -39.852 23.309 1.00 24.85  ? 462 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 4 .   ? 28.268 -31.137 18.247 1.00 58.78  ? 463 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 4 .   ? 20.623 -21.952 6.335  1.00 257.03 ? 464 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 4 .   ? 30.238 -30.437 15.859 1.00 45.08  ? 465 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 4 .   ? 19.618 -23.331 8.055  1.00 300.00 ? 466 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 4 .   ? 10.060 -16.371 28.033 1.00 43.24  ? 467 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 4 .   ? 34.560 -30.964 15.229 1.00 43.15  ? 468 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   ? 0.2073 0.1964 0.1965 0.0072  -0.0098 0.0047  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2040 0.1953 0.2036 0.0048  -0.0111 0.0033  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2069 0.1983 0.2120 0.0018  -0.0102 0.0012  7   SER   A C   
4    O O   . SER   A 1   ? 0.2165 0.2058 0.2172 0.0022  -0.0102 0.0000  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2224 0.2141 0.2233 0.0070  -0.0170 0.0014  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2447 0.2349 0.2432 0.0080  -0.0214 -0.0023 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1898 0.1833 0.2043 -0.0007 -0.0087 0.0012  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1798 0.1730 0.2001 -0.0031 -0.0067 0.0001  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1824 0.1776 0.2090 -0.0049 -0.0025 0.0016  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1841 0.1804 0.2090 -0.0044 -0.0005 0.0032  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1683 0.1634 0.2024 -0.0068 -0.0006 0.0012  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1662 0.1629 0.2053 -0.0077 0.0041  0.0028  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1650 0.1597 0.2066 -0.0088 0.0082  0.0036  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1652 0.1575 0.2079 -0.0095 0.0068  0.0025  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1676 0.1674 0.2169 -0.0081 0.0028  0.0023  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1548 0.1500 0.1972 -0.0086 0.0134  0.0055  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1490 0.1421 0.1936 -0.0090 0.0183  0.0073  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1479 0.1431 0.2043 -0.0101 0.0212  0.0080  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1454 0.1435 0.2033 -0.0093 0.0219  0.0081  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1529 0.1448 0.1876 -0.0067 0.0224  0.0092  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1494 0.1405 0.1740 -0.0056 0.0195  0.0083  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1637 0.1525 0.1991 -0.0061 0.0281  0.0119  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1517 0.1438 0.1682 -0.0033 0.0215  0.0089  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1452 0.1391 0.2110 -0.0118 0.0233  0.0085  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1479 0.1444 0.2273 -0.0130 0.0269  0.0096  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1574 0.1509 0.2371 -0.0124 0.0352  0.0134  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1723 0.1620 0.2551 -0.0137 0.0369  0.0143  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1431 0.1415 0.2368 -0.0159 0.0222  0.0068  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1599 0.1614 0.2522 -0.0153 0.0142  0.0034  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1806 0.1870 0.2785 -0.0145 0.0131  0.0032  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1824 0.1817 0.2665 -0.0149 0.0082  0.0009  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1974 0.2059 0.2929 -0.0133 0.0062  0.0008  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1985 0.2000 0.2793 -0.0135 0.0017  -0.0013 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2158 0.2217 0.3022 -0.0126 0.0006  -0.0012 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2501 0.2575 0.3324 -0.0106 -0.0055 -0.0027 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1511 0.1454 0.2266 -0.0099 0.0407  0.0158  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1663 0.1573 0.2395 -0.0081 0.0492  0.0201  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1799 0.1738 0.2612 -0.0072 0.0554  0.0221  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1833 0.1802 0.2613 -0.0055 0.0542  0.0206  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1854 0.1732 0.2403 -0.0043 0.0504  0.0212  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1924 0.1832 0.2387 -0.0023 0.0470  0.0187  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2035 0.1877 0.2542 -0.0012 0.0593  0.0260  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1799 0.1730 0.2731 -0.0084 0.0621  0.0253  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1874 0.1836 0.2901 -0.0074 0.0691  0.0277  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1896 0.1924 0.3036 -0.0091 0.0637  0.0240  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1892 0.1942 0.3125 -0.0125 0.0565  0.0208  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1926 0.1980 0.3033 -0.0061 0.0658  0.0240  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1959 0.2071 0.3161 -0.0070 0.0604  0.0207  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1774 0.1879 0.2836 -0.0055 0.0533  0.0175  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1659 0.1794 0.2739 -0.0042 0.0517  0.0159  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2358 0.2509 0.3663 -0.0052 0.0673  0.0226  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2876 0.3052 0.4379 -0.0080 0.0727  0.0252  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3063 0.3285 0.4734 -0.0115 0.0674  0.0228  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2961 0.3104 0.4448 -0.0062 0.0831  0.0300  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1679 0.1746 0.2616 -0.0058 0.0494  0.0166  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1693 0.1752 0.2509 -0.0048 0.0435  0.0139  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1549 0.1604 0.2357 -0.0071 0.0358  0.0117  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1624 0.1661 0.2454 -0.0090 0.0353  0.0121  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1754 0.1774 0.2405 -0.0018 0.0463  0.0146  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1837 0.1853 0.2456 0.0018  0.0534  0.0161  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1888 0.1928 0.2539 0.0032  0.0536  0.0145  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2023 0.2008 0.2570 0.0044  0.0600  0.0191  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2034 0.2066 0.2645 0.0071  0.0602  0.0154  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2138 0.2115 0.2637 0.0086  0.0667  0.0204  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2228 0.2229 0.2760 0.0099  0.0668  0.0183  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2352 0.2343 0.2826 0.0146  0.0734  0.0191  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1376 0.1442 0.2143 -0.0067 0.0302  0.0095  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1359 0.1416 0.2083 -0.0078 0.0234  0.0077  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1388 0.1424 0.1979 -0.0062 0.0225  0.0072  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1449 0.1492 0.2027 -0.0048 0.0231  0.0068  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1437 0.1528 0.2250 -0.0083 0.0177  0.0060  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1570 0.1650 0.2307 -0.0079 0.0112  0.0045  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1636 0.1747 0.2450 -0.0075 0.0053  0.0029  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1954 0.2055 0.2688 -0.0053 0.0015  0.0030  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2131 0.2217 0.2796 -0.0045 -0.0034 0.0022  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1930 0.2005 0.2587 -0.0057 -0.0057 0.0006  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2075 0.2148 0.2671 -0.0022 -0.0055 0.0031  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1293 0.1304 0.1797 -0.0064 0.0214  0.0072  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1347 0.1346 0.1745 -0.0052 0.0204  0.0066  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1347 0.1346 0.1723 -0.0058 0.0152  0.0057  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1409 0.1398 0.1778 -0.0065 0.0130  0.0056  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1365 0.1343 0.1681 -0.0042 0.0231  0.0074  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1301 0.1279 0.1531 -0.0031 0.0217  0.0061  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1349 0.1321 0.1677 -0.0028 0.0290  0.0091  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1343 0.1345 0.1701 -0.0053 0.0135  0.0053  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1336 0.1332 0.1663 -0.0052 0.0096  0.0053  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1350 0.1338 0.1621 -0.0048 0.0102  0.0053  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1364 0.1353 0.1635 -0.0047 0.0125  0.0045  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1429 0.1436 0.1813 -0.0046 0.0066  0.0054  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1656 0.1676 0.2102 -0.0051 0.0043  0.0045  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1480 0.1495 0.1913 -0.0039 0.0086  0.0055  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1277 0.1257 0.1509 -0.0045 0.0082  0.0060  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1298 0.1273 0.1506 -0.0046 0.0091  0.0063  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1397 0.1363 0.1650 -0.0042 0.0093  0.0067  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1402 0.1366 0.1679 -0.0032 0.0075  0.0077  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1393 0.1360 0.1557 -0.0039 0.0078  0.0079  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1618 0.1590 0.1735 -0.0037 0.0076  0.0076  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1736 0.1701 0.1836 -0.0031 0.0058  0.0074  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1636 0.1620 0.1738 -0.0042 0.0092  0.0072  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1311 0.1273 0.1580 -0.0048 0.0113  0.0054  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1284 0.1228 0.1596 -0.0043 0.0119  0.0054  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1274 0.1198 0.1589 -0.0033 0.0109  0.0083  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1387 0.1301 0.1734 -0.0018 0.0102  0.0093  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1541 0.1476 0.1861 -0.0051 0.0136  0.0028  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1563 0.1474 0.1930 -0.0043 0.0148  0.0020  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1566 0.1460 0.1942 -0.0053 0.0156  -0.0012 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1862 0.1725 0.2278 -0.0044 0.0168  -0.0029 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1917 0.1743 0.2377 -0.0044 0.0173  -0.0015 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1683 0.1498 0.2146 -0.0050 0.0170  0.0022  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1837 0.1630 0.2332 -0.0034 0.0185  -0.0035 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1193 0.1110 0.1471 -0.0036 0.0109  0.0099  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1310 0.1201 0.1575 -0.0019 0.0108  0.0134  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1461 0.1356 0.1694 0.0007  0.0077  0.0148  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1741 0.1612 0.1955 0.0032  0.0071  0.0177  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1272 0.1154 0.1512 -0.0026 0.0129  0.0152  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1314 0.1216 0.1495 -0.0021 0.0119  0.0154  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1389 0.1320 0.1566 -0.0037 0.0118  0.0127  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1523 0.1415 0.1642 0.0003  0.0113  0.0180  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1489 0.1425 0.1611 -0.0025 0.0111  0.0137  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1470 0.1384 0.1553 -0.0001 0.0108  0.0166  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1369 0.1290 0.1600 0.0004  0.0055  0.0128  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1369 0.1299 0.1589 0.0025  0.0015  0.0128  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1485 0.1440 0.1785 0.0024  0.0000  0.0111  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1412 0.1385 0.1731 0.0037  -0.0038 0.0103  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1386 0.1326 0.1559 0.0021  -0.0001 0.0115  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1508 0.1430 0.1604 0.0028  0.0014  0.0132  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.1487 0.1413 0.1536 0.0031  -0.0004 0.0115  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.1737 0.1633 0.1784 0.0061  0.0011  0.0164  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1439 0.1395 0.1790 0.0011  0.0030  0.0104  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1444 0.1426 0.1877 0.0014  0.0028  0.0092  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1540 0.1526 0.2005 0.0044  -0.0004 0.0106  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1529 0.1484 0.1959 0.0065  -0.0006 0.0129  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1482 0.1456 0.1943 0.0005  0.0070  0.0082  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1559 0.1583 0.2097 0.0049  -0.0031 0.0093  24  THR   A N   
135  C CA  . THR   A 18  ? 0.1718 0.1758 0.2297 0.0083  -0.0071 0.0100  24  THR   A CA  
136  C C   . THR   A 18  ? 0.1846 0.1893 0.2505 0.0094  -0.0046 0.0105  24  THR   A C   
137  O O   . THR   A 18  ? 0.1756 0.1798 0.2438 0.0075  0.0003  0.0097  24  THR   A O   
138  C CB  . THR   A 18  ? 0.1855 0.1942 0.2494 0.0080  -0.0120 0.0076  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2030 0.2152 0.2775 0.0055  -0.0089 0.0060  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.1919 0.1992 0.2479 0.0071  -0.0144 0.0065  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1913 0.1975 0.2615 0.0131  -0.0081 0.0115  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2013 0.2087 0.2803 0.0148  -0.0060 0.0118  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1682 0.1808 0.2578 0.0124  -0.0035 0.0094  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1644 0.1764 0.2577 0.0122  0.0015  0.0092  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2470 0.2565 0.3297 0.0197  -0.0112 0.0132  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3590 0.3631 0.4310 0.0231  -0.0130 0.0165  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4097 0.4070 0.4763 0.0232  -0.0082 0.0191  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3956 0.4000 0.4618 0.0269  -0.0189 0.0176  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4292 0.4227 0.4872 0.0268  -0.0104 0.0225  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4275 0.4250 0.4838 0.0296  -0.0168 0.0218  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1578 0.1749 0.2520 0.0107  -0.0067 0.0076  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1598 0.1815 0.2650 0.0083  -0.0037 0.0060  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1532 0.1718 0.2532 0.0055  0.0030  0.0060  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1552 0.1755 0.2616 0.0053  0.0082  0.0059  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.1890 0.2152 0.3008 0.0067  -0.0086 0.0039  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.2383 0.2706 0.3620 0.0093  -0.0146 0.0027  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.2680 0.3025 0.3925 0.0097  -0.0217 0.0006  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.2371 0.2725 0.3703 0.0114  -0.0123 0.0036  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1451 0.1593 0.2332 0.0040  0.0031  0.0062  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1473 0.1587 0.2293 0.0021  0.0085  0.0060  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1431 0.1522 0.2242 0.0037  0.0128  0.0060  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1420 0.1513 0.2243 0.0035  0.0177  0.0054  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1434 0.1511 0.2138 0.0009  0.0071  0.0061  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1740 0.1829 0.2435 -0.0007 0.0043  0.0055  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1599 0.1711 0.2361 -0.0022 0.0060  0.0049  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1762 0.1831 0.2384 -0.0003 0.0009  0.0057  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1463 0.1526 0.2250 0.0056  0.0110  0.0068  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1570 0.1601 0.2354 0.0071  0.0146  0.0063  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1731 0.1794 0.2615 0.0092  0.0172  0.0060  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1795 0.1839 0.2673 0.0102  0.0217  0.0047  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1544 0.1529 0.2287 0.0085  0.0126  0.0077  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1569 0.1515 0.2223 0.0063  0.0128  0.0076  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1632 0.1570 0.2231 0.0057  0.0100  0.0093  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1511 0.1422 0.2126 0.0050  0.0160  0.0055  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1712 0.1618 0.2252 0.0037  0.0117  0.0087  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1687 0.1576 0.2241 0.0032  0.0148  0.0062  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1608 0.1503 0.2234 0.0056  0.0194  0.0028  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1740 0.1602 0.2261 0.0015  0.0166  0.0040  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1715 0.1577 0.2293 0.0042  0.0206  0.0002  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1697 0.1547 0.2231 0.0020  0.0190  0.0007  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1727 0.1844 0.2708 0.0102  0.0144  0.0068  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1699 0.1859 0.2799 0.0122  0.0170  0.0067  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1648 0.1838 0.2791 0.0105  0.0225  0.0061  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1722 0.1939 0.2947 0.0123  0.0269  0.0062  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1698 0.1913 0.2900 0.0138  0.0114  0.0074  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1563 0.1746 0.2649 0.0076  0.0226  0.0060  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1557 0.1753 0.2662 0.0063  0.0282  0.0063  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1505 0.1648 0.2465 0.0056  0.0310  0.0057  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1441 0.1581 0.2372 0.0041  0.0334  0.0063  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1602 0.1840 0.2790 0.0036  0.0256  0.0067  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2021 0.2324 0.3372 0.0043  0.0228  0.0065  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2008 0.2352 0.3475 0.0051  0.0276  0.0073  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2028 0.2345 0.3390 0.0044  0.0148  0.0057  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1480 0.1578 0.2355 0.0070  0.0305  0.0044  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1606 0.1659 0.2355 0.0066  0.0316  0.0029  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1619 0.1667 0.2326 0.0081  0.0378  0.0025  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1647 0.1701 0.2392 0.0107  0.0424  0.0024  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1643 0.1654 0.2350 0.0078  0.0303  0.0011  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1856 0.1825 0.2452 0.0072  0.0302  -0.0013 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1976 0.1948 0.2525 0.0044  0.0267  -0.0004 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1837 0.1761 0.2423 0.0081  0.0293  -0.0035 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1638 0.1672 0.2261 0.0070  0.0381  0.0026  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1773 0.1793 0.2323 0.0092  0.0436  0.0025  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1894 0.1875 0.2319 0.0103  0.0418  -0.0009 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2109 0.2069 0.2477 0.0136  0.0447  -0.0031 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1910 0.1941 0.2458 0.0079  0.0457  0.0053  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2017 0.2023 0.2455 0.0111  0.0509  0.0056  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1992 0.2063 0.2683 0.0068  0.0481  0.0079  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1780 0.1755 0.2171 0.0078  0.0367  -0.0015 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1783 0.1733 0.2081 0.0080  0.0342  -0.0048 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1636 0.1587 0.1948 0.0048  0.0290  -0.0046 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1505 0.1474 0.1850 0.0028  0.0275  -0.0019 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1833 0.1782 0.2036 0.0098  0.0361  -0.0046 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.1984 0.1922 0.2101 0.0100  0.0325  -0.0080 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2166 0.2084 0.2223 0.0123  0.0316  -0.0126 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1996 0.1945 0.2089 0.0079  0.0290  -0.0074 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2204 0.2128 0.2217 0.0114  0.0273  -0.0150 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2145 0.2089 0.2176 0.0088  0.0261  -0.0116 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1995 0.1958 0.2116 0.0054  0.0279  -0.0041 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2162 0.2122 0.2167 0.0075  0.0225  -0.0121 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2053 0.2025 0.2135 0.0044  0.0247  -0.0045 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2105 0.2079 0.2136 0.0053  0.0222  -0.0082 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1581 0.1511 0.1873 0.0043  0.0265  -0.0075 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1547 0.1476 0.1849 0.0015  0.0227  -0.0070 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1548 0.1465 0.1809 0.0011  0.0208  -0.0109 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1491 0.1388 0.1733 0.0029  0.0215  -0.0147 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1567 0.1487 0.1940 0.0005  0.0214  -0.0049 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1643 0.1532 0.2053 0.0020  0.0227  -0.0067 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1986 0.1840 0.2389 0.0012  0.0216  -0.0102 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2367 0.2192 0.2775 0.0029  0.0230  -0.0134 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1837 0.1689 0.2235 -0.0011 0.0195  -0.0100 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1420 0.1348 0.1674 -0.0010 0.0183  -0.0103 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1374 0.1302 0.1616 -0.0018 0.0161  -0.0141 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1352 0.1284 0.1636 -0.0047 0.0145  -0.0121 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1282 0.1238 0.1544 -0.0053 0.0138  -0.0097 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1749 0.1699 0.1913 0.0002  0.0155  -0.0161 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2591 0.2549 0.2745 0.0001  0.0124  -0.0214 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2705 0.2657 0.2929 -0.0027 0.0107  -0.0227 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2743 0.2713 0.2823 0.0031  0.0116  -0.0241 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1323 0.1227 0.1669 -0.0062 0.0144  -0.0128 36  SER   A N   
241  C CA  A SER   A 30  ? 0.1373 0.1276 0.1764 -0.0086 0.0140  -0.0103 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1382 0.1286 0.1770 -0.0086 0.0140  -0.0101 36  SER   A CA  
243  C C   . SER   A 30  ? 0.1392 0.1332 0.1776 -0.0098 0.0123  -0.0121 36  SER   A C   
244  O O   . SER   A 30  ? 0.1329 0.1286 0.1716 -0.0108 0.0125  -0.0088 36  SER   A O   
245  C CB  A SER   A 30  ? 0.1548 0.1406 0.2011 -0.0099 0.0149  -0.0111 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1588 0.1446 0.2046 -0.0097 0.0151  -0.0099 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1689 0.1510 0.2167 -0.0084 0.0163  -0.0096 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1741 0.1587 0.2236 -0.0108 0.0141  -0.0154 36  SER   A OG  
249  N N   . SER   A 31  ? 0.1479 0.1432 0.1852 -0.0093 0.0104  -0.0175 37  SER   A N   
250  C CA  . SER   A 31  ? 0.1596 0.1593 0.1973 -0.0101 0.0081  -0.0198 37  SER   A CA  
251  C C   . SER   A 31  ? 0.1559 0.1592 0.1868 -0.0086 0.0080  -0.0167 37  SER   A C   
252  O O   . SER   A 31  ? 0.1701 0.1770 0.2022 -0.0092 0.0067  -0.0168 37  SER   A O   
253  C CB  . SER   A 31  ? 0.1869 0.1875 0.2241 -0.0091 0.0051  -0.0268 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2227 0.2241 0.2497 -0.0053 0.0047  -0.0280 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1357 0.1377 0.1605 -0.0066 0.0096  -0.0140 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1322 0.1362 0.1512 -0.0053 0.0099  -0.0111 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1268 0.1296 0.1467 -0.0062 0.0113  -0.0063 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1324 0.1361 0.1484 -0.0054 0.0114  -0.0042 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1416 0.1450 0.1536 -0.0023 0.0110  -0.0116 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1576 0.1621 0.1651 0.0001  0.0093  -0.0163 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1710 0.1742 0.1701 0.0039  0.0115  -0.0159 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1772 0.1812 0.1719 0.0050  0.0129  -0.0119 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1927 0.1960 0.1792 0.0088  0.0147  -0.0110 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1818 0.1842 0.1624 0.0123  0.0152  -0.0139 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1704 0.1735 0.1541 0.0095  0.0162  -0.0073 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1316 0.1318 0.1562 -0.0074 0.0122  -0.0048 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1269 0.1257 0.1514 -0.0074 0.0127  -0.0007 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1293 0.1281 0.1509 -0.0060 0.0130  0.0001  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1308 0.1297 0.1507 -0.0058 0.0124  0.0024  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1353 0.1353 0.1586 -0.0078 0.0125  0.0017  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1441 0.1422 0.1658 -0.0070 0.0124  0.0052  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1377 0.1334 0.1621 -0.0068 0.0127  0.0063  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1308 0.1297 0.1485 -0.0062 0.0118  0.0066  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1218 0.1202 0.1432 -0.0050 0.0140  -0.0017 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1279 0.1264 0.1487 -0.0040 0.0153  -0.0004 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1264 0.1238 0.1518 -0.0033 0.0167  -0.0005 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1204 0.1165 0.1472 -0.0029 0.0173  -0.0026 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1330 0.1323 0.1485 -0.0024 0.0168  -0.0014 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1495 0.1499 0.1603 -0.0022 0.0159  -0.0007 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1555 0.1559 0.1606 0.0003  0.0178  -0.0011 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1461 0.1460 0.1583 -0.0032 0.0153  0.0019  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1240 0.1221 0.1527 -0.0032 0.0172  0.0013  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1232 0.1214 0.1578 -0.0022 0.0188  0.0016  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1163 0.1161 0.1536 -0.0021 0.0205  0.0029  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1185 0.1189 0.1558 -0.0032 0.0189  0.0040  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1313 0.1290 0.1710 -0.0023 0.0165  0.0027  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1551 0.1535 0.2019 -0.0009 0.0178  0.0029  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1614 0.1576 0.2105 -0.0001 0.0164  0.0033  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1561 0.1576 0.2093 -0.0010 0.0166  0.0043  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1137 0.1139 0.1537 -0.0007 0.0243  0.0028  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1146 0.1163 0.1595 -0.0006 0.0273  0.0045  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1226 0.1263 0.1777 0.0000  0.0285  0.0049  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1292 0.1322 0.1842 0.0018  0.0302  0.0038  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1163 0.1167 0.1549 0.0013  0.0323  0.0049  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1207 0.1222 0.1662 0.0013  0.0368  0.0075  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1239 0.1229 0.1530 0.0012  0.0306  0.0045  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1230 0.1293 0.1872 -0.0013 0.0274  0.0060  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1377 0.1473 0.2139 -0.0007 0.0281  0.0064  43  SER   A CA  
299  C C   . SER   A 37  ? 0.1541 0.1661 0.2394 -0.0015 0.0325  0.0080  43  SER   A C   
300  O O   . SER   A 37  ? 0.1531 0.1638 0.2362 -0.0030 0.0335  0.0089  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1482 0.1596 0.2294 -0.0013 0.0217  0.0059  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1752 0.1872 0.2570 -0.0033 0.0179  0.0058  43  SER   A OG  
303  N N   . SER   A 38  ? 0.1499 0.1654 0.2464 -0.0004 0.0357  0.0086  44  SER   A N   
304  C CA  . SER   A 38  ? 0.1611 0.1792 0.2689 -0.0013 0.0408  0.0106  44  SER   A CA  
305  C C   . SER   A 38  ? 0.1729 0.1952 0.2948 -0.0041 0.0357  0.0099  44  SER   A C   
306  O O   . SER   A 38  ? 0.1755 0.2000 0.3006 -0.0040 0.0291  0.0081  44  SER   A O   
307  C CB  . SER   A 38  ? 0.1682 0.1885 0.2823 0.0014  0.0473  0.0116  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.1962 0.2196 0.3173 0.0026  0.0436  0.0102  44  SER   A OG  
309  N N   . THR   A 39  ? 0.1847 0.2078 0.3152 -0.0064 0.0389  0.0112  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2071 0.2341 0.3524 -0.0094 0.0338  0.0096  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2239 0.2554 0.3883 -0.0106 0.0397  0.0113  45  THR   A C   
312  O O   . THR   A 39  ? 0.2276 0.2576 0.3912 -0.0094 0.0489  0.0145  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2359 0.2587 0.3751 -0.0119 0.0305  0.0087  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2609 0.2807 0.4006 -0.0128 0.0383  0.0117  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2414 0.2598 0.3621 -0.0106 0.0260  0.0077  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2377 0.2749 0.4197 -0.0127 0.0346  0.0090  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2524 0.2950 0.4562 -0.0145 0.0399  0.0103  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2668 0.3061 0.4763 -0.0184 0.0427  0.0112  46  THR   A C   
319  O O   . THR   A 40  ? 0.2818 0.3216 0.5023 -0.0194 0.0519  0.0146  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2712 0.3223 0.4934 -0.0148 0.0326  0.0070  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.2960 0.3465 0.5148 -0.0161 0.0214  0.0028  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2768 0.3311 0.4968 -0.0106 0.0323  0.0073  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2639 0.2996 0.4664 -0.0203 0.0353  0.0083  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2726 0.3042 0.4803 -0.0238 0.0374  0.0087  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2853 0.3085 0.4735 -0.0224 0.0438  0.0124  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2825 0.3029 0.4516 -0.0193 0.0426  0.0128  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2716 0.3033 0.4825 -0.0262 0.0262  0.0032  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2971 0.3162 0.4910 -0.0245 0.0502  0.0152  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3257 0.3369 0.5024 -0.0227 0.0563  0.0191  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3369 0.3430 0.5002 -0.0232 0.0488  0.0161  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3388 0.3449 0.5115 -0.0264 0.0427  0.0124  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3668 0.3747 0.5551 -0.0243 0.0667  0.0238  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4591 0.4610 0.6308 -0.0202 0.0767  0.0299  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.5479 0.5535 0.7167 -0.0162 0.0830  0.0325  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5774 0.5897 0.7625 -0.0172 0.0838  0.0317  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5727 0.5740 0.7207 -0.0113 0.0873  0.0352  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3491 0.3512 0.4913 -0.0199 0.0493  0.0174  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3722 0.3697 0.5005 -0.0196 0.0436  0.0153  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3943 0.3847 0.5170 -0.0192 0.0500  0.0191  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3998 0.3884 0.5200 -0.0170 0.0590  0.0240  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4012 0.3872 0.5209 -0.0205 0.0456  0.0170  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4147 0.3933 0.5300 -0.0199 0.0516  0.0207  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4050 0.3793 0.5006 -0.0169 0.0488  0.0205  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4205 0.3884 0.5133 -0.0165 0.0515  0.0224  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4362 0.4119 0.5692 -0.0242 0.0517  0.0195  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5555 0.5363 0.7143 -0.0277 0.0574  0.0210  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3747 0.3525 0.4578 -0.0146 0.0442  0.0186  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3473 0.3221 0.4132 -0.0116 0.0422  0.0187  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3400 0.3125 0.3962 -0.0076 0.0499  0.0238  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3605 0.3354 0.4184 -0.0065 0.0545  0.0258  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3346 0.3140 0.3921 -0.0106 0.0354  0.0153  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3544 0.3348 0.4150 -0.0126 0.0275  0.0108  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3794 0.3557 0.4424 -0.0138 0.0259  0.0095  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3036 0.2883 0.3632 -0.0126 0.0228  0.0084  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3093 0.2770 0.3551 -0.0050 0.0513  0.0257  52  THR   A N   
356  C CA  . THR   A 46  ? 0.2965 0.2617 0.3307 -0.0002 0.0576  0.0303  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2515 0.2198 0.2710 0.0030  0.0527  0.0280  52  THR   A C   
358  O O   . THR   A 46  ? 0.2445 0.2134 0.2612 0.0021  0.0468  0.0250  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3369 0.2944 0.3694 0.0012  0.0621  0.0341  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3740 0.3286 0.4208 -0.0014 0.0687  0.0372  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3586 0.3133 0.3746 0.0076  0.0661  0.0382  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2235 0.1940 0.2345 0.0066  0.0552  0.0291  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2096 0.1832 0.2086 0.0094  0.0504  0.0265  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2132 0.1836 0.1995 0.0147  0.0525  0.0293  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2253 0.1920 0.2075 0.0182  0.0592  0.0337  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2129 0.1908 0.2096 0.0106  0.0503  0.0247  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2209 0.2020 0.2306 0.0062  0.0489  0.0226  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2229 0.2042 0.2100 0.0125  0.0447  0.0211  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2278 0.2114 0.2422 0.0024  0.0415  0.0188  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2046 0.1762 0.1846 0.0157  0.0473  0.0271  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.1963 0.1660 0.1644 0.0212  0.0480  0.0292  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.1937 0.1666 0.1515 0.0259  0.0480  0.0284  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.1870 0.1647 0.1463 0.0243  0.0444  0.0243  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.1904 0.1621 0.1565 0.0209  0.0420  0.0266  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.1931 0.1626 0.1402 0.0320  0.0520  0.0321  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.1944 0.1661 0.1291 0.0379  0.0515  0.0311  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2184 0.1894 0.1423 0.0435  0.0492  0.0322  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2330 0.1986 0.1489 0.0488  0.0544  0.0375  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2096 0.1770 0.1404 0.0413  0.0599  0.0356  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2309 0.1992 0.1746 0.0358  0.0630  0.0351  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2542 0.2286 0.2015 0.0329  0.0572  0.0288  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2412 0.2161 0.2008 0.0284  0.0605  0.0291  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2485 0.2277 0.2152 0.0246  0.0563  0.0246  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2300 0.2129 0.1934 0.0241  0.0491  0.0197  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2558 0.2356 0.2338 0.0213  0.0593  0.0252  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2247 0.2010 0.1497 0.0423  0.0417  0.0277  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2321 0.2089 0.1503 0.0468  0.0388  0.0284  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2335 0.2187 0.1526 0.0462  0.0304  0.0221  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2298 0.2193 0.1553 0.0418  0.0274  0.0177  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2364 0.2087 0.1615 0.0438  0.0407  0.0313  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2499 0.2263 0.1889 0.0354  0.0357  0.0266  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2418 0.2293 0.1565 0.0502  0.0269  0.0220  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2559 0.2518 0.1744 0.0492  0.0195  0.0165  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2477 0.2443 0.1724 0.0472  0.0181  0.0172  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2466 0.2494 0.1718 0.0494  0.0132  0.0147  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3142 0.3147 0.2227 0.0563  0.0149  0.0139  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4239 0.4221 0.3225 0.0640  0.0156  0.0179  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4221 0.4134 0.3207 0.0640  0.0208  0.0235  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5011 0.5042 0.3921 0.0702  0.0104  0.0153  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2394 0.2301 0.1694 0.0434  0.0223  0.0202  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2353 0.2257 0.1708 0.0414  0.0213  0.0204  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2234 0.2218 0.1665 0.0378  0.0163  0.0156  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2313 0.2327 0.1789 0.0338  0.0149  0.0127  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2329 0.2158 0.1736 0.0371  0.0257  0.0229  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2638 0.2361 0.1989 0.0411  0.0325  0.0293  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2031 0.2044 0.1478 0.0392  0.0142  0.0152  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.1980 0.2061 0.1507 0.0359  0.0109  0.0117  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1855 0.1906 0.1416 0.0342  0.0125  0.0129  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1764 0.1869 0.1376 0.0334  0.0107  0.0112  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2400 0.2568 0.1931 0.0397  0.0064  0.0092  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3101 0.3320 0.2637 0.0393  0.0031  0.0055  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3588 0.3904 0.3157 0.0423  -0.0023 0.0020  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3741 0.4078 0.3242 0.0480  -0.0051 0.0012  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3527 0.3904 0.3204 0.0388  -0.0038 -0.0002 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1795 0.1760 0.1329 0.0342  0.0160  0.0158  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1792 0.1713 0.1350 0.0327  0.0173  0.0161  60  THR   A CA  
417  C C   . THR   A 54  ? 0.1767 0.1615 0.1344 0.0286  0.0198  0.0169  60  THR   A C   
418  O O   . THR   A 54  ? 0.1754 0.1565 0.1313 0.0289  0.0222  0.0189  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2029 0.1912 0.1544 0.0378  0.0186  0.0184  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2304 0.2110 0.1771 0.0401  0.0219  0.0218  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2099 0.2063 0.1603 0.0426  0.0158  0.0178  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1694 0.1526 0.1309 0.0253  0.0193  0.0152  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1777 0.1552 0.1427 0.0215  0.0204  0.0150  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1782 0.1539 0.1452 0.0195  0.0188  0.0127  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1739 0.1511 0.1387 0.0218  0.0180  0.0120  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1713 0.1440 0.1425 0.0158  0.0183  0.0114  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1747 0.1452 0.1471 0.0143  0.0161  0.0087  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1693 0.1429 0.1458 0.0107  0.0142  0.0073  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1632 0.1366 0.1440 0.0085  0.0151  0.0080  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2056 0.1674 0.1796 0.0140  0.0168  0.0080  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2196 0.1791 0.1944 0.0126  0.0134  0.0041  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2208 0.1784 0.1904 0.0180  0.0190  0.0096  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1622 0.1386 0.1372 0.0106  0.0120  0.0057  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1478 0.1268 0.1262 0.0079  0.0101  0.0048  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1531 0.1290 0.1303 0.0078  0.0071  0.0022  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1484 0.1215 0.1206 0.0103  0.0066  0.0010  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1440 0.1294 0.1222 0.0079  0.0104  0.0058  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1523 0.1396 0.1267 0.0098  0.0102  0.0056  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1591 0.1474 0.1304 0.0127  0.0116  0.0062  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1652 0.1533 0.1391 0.0093  0.0090  0.0053  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1671 0.1576 0.1357 0.0148  0.0124  0.0065  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1779 0.1673 0.1477 0.0117  0.0099  0.0060  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1783 0.1690 0.1459 0.0142  0.0118  0.0066  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1794 0.1718 0.1437 0.0168  0.0137  0.0076  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1459 0.1223 0.1271 0.0056  0.0049  0.0011  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1523 0.1263 0.1319 0.0061  0.0011  -0.0017 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1547 0.1322 0.1295 0.0077  0.0005  -0.0008 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1509 0.1322 0.1285 0.0063  0.0013  0.0010  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1623 0.1353 0.1499 0.0032  -0.0015 -0.0036 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1840 0.1551 0.1695 0.0044  -0.0067 -0.0072 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2070 0.1730 0.1885 0.0062  -0.0089 -0.0106 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1994 0.1736 0.1855 0.0045  -0.0095 -0.0074 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2272 0.1913 0.2052 0.0081  -0.0144 -0.0146 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2171 0.1896 0.1994 0.0066  -0.0148 -0.0108 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2375 0.2051 0.2154 0.0085  -0.0174 -0.0146 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2702 0.2361 0.2436 0.0111  -0.0234 -0.0187 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1626 0.1380 0.1297 0.0109  -0.0004 -0.0019 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1648 0.1425 0.1263 0.0132  0.0000  -0.0004 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1711 0.1459 0.1284 0.0150  -0.0046 -0.0030 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.1723 0.1430 0.1231 0.0179  -0.0068 -0.0060 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1720 0.1500 0.1274 0.0165  0.0032  0.0009  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.1923 0.1720 0.1402 0.0201  0.0052  0.0034  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1777 0.1546 0.1383 0.0138  -0.0065 -0.0024 66  SER   A N   
464  C CA  . SER   A 60  ? 0.1900 0.1649 0.1471 0.0159  -0.0118 -0.0050 66  SER   A CA  
465  C C   . SER   A 60  ? 0.1867 0.1595 0.1310 0.0214  -0.0121 -0.0046 66  SER   A C   
466  O O   . SER   A 60  ? 0.1859 0.1554 0.1243 0.0244  -0.0170 -0.0085 66  SER   A O   
467  C CB  . SER   A 60  ? 0.2267 0.2046 0.1904 0.0140  -0.0136 -0.0041 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.2785 0.2591 0.2412 0.0143  -0.0098 0.0004  66  SER   A OG  
469  N N   . SER   A 61  ? 0.1770 0.1517 0.1173 0.0229  -0.0066 -0.0002 67  SER   A N   
470  C CA  . SER   A 61  ? 0.1932 0.1659 0.1212 0.0285  -0.0050 0.0013  67  SER   A CA  
471  C C   . SER   A 61  ? 0.1940 0.1630 0.1142 0.0319  -0.0051 -0.0017 67  SER   A C   
472  O O   . SER   A 61  ? 0.2030 0.1699 0.1118 0.0373  -0.0034 -0.0008 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2018 0.1779 0.1308 0.0285  0.0017  0.0071  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2090 0.1880 0.1440 0.0259  0.0058  0.0081  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.1827 0.1504 0.1086 0.0291  -0.0062 -0.0048 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1911 0.1542 0.1108 0.0320  -0.0068 -0.0083 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2137 0.1726 0.1380 0.0300  -0.0129 -0.0143 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2150 0.1687 0.1348 0.0322  -0.0142 -0.0181 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.1921 0.1570 0.1149 0.0313  -0.0012 -0.0058 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.1821 0.1512 0.1016 0.0337  0.0049  -0.0008 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2083 0.1741 0.1148 0.0403  0.0064  -0.0013 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2283 0.1985 0.1338 0.0423  0.0133  0.0042  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2474 0.2193 0.1507 0.0433  0.0155  0.0081  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2378 0.2075 0.1380 0.0433  0.0108  0.0070  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2240 0.1999 0.1287 0.0446  0.0224  0.0132  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2190 0.1797 0.1530 0.0257  -0.0162 -0.0151 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2336 0.1915 0.1764 0.0224  -0.0210 -0.0200 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2318 0.1863 0.1782 0.0209  -0.0179 -0.0206 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2388 0.1876 0.1857 0.0212  -0.0211 -0.0255 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2704 0.2244 0.2077 0.0256  -0.0285 -0.0263 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3455 0.3027 0.2817 0.0269  -0.0329 -0.0264 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.3909 0.3448 0.3267 0.0285  -0.0419 -0.0341 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4238 0.3798 0.3525 0.0326  -0.0467 -0.0344 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4458 0.3986 0.3585 0.0397  -0.0499 -0.0366 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4640 0.4114 0.3665 0.0432  -0.0489 -0.0394 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4132 0.3680 0.3191 0.0439  -0.0537 -0.0359 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2095 0.1671 0.1578 0.0197  -0.0119 -0.0157 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2148 0.1695 0.1648 0.0195  -0.0086 -0.0152 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.1992 0.1583 0.1565 0.0164  -0.0041 -0.0106 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.1937 0.1584 0.1520 0.0154  -0.0026 -0.0075 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2418 0.1955 0.1813 0.0245  -0.0056 -0.0143 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3367 0.2834 0.2683 0.0285  -0.0087 -0.0195 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4121 0.3586 0.3344 0.0336  -0.0044 -0.0179 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.4896 0.4280 0.4035 0.0379  -0.0070 -0.0234 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.5378 0.4766 0.4393 0.0443  -0.0040 -0.0225 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1830 0.1388 0.1441 0.0154  -0.0019 -0.0102 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1758 0.1351 0.1413 0.0139  0.0023  -0.0060 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.1822 0.1427 0.1418 0.0176  0.0055  -0.0039 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.1977 0.1535 0.1522 0.0208  0.0055  -0.0058 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1875 0.1423 0.1604 0.0114  0.0033  -0.0059 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2136 0.1680 0.1950 0.0075  0.0008  -0.0077 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2399 0.1982 0.2279 0.0047  0.0028  -0.0049 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2224 0.1732 0.2073 0.0063  -0.0036 -0.0122 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2382 0.1955 0.2342 0.0018  0.0001  -0.0074 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2396 0.1927 0.2345 0.0026  -0.0043 -0.0120 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1780 0.1448 0.1388 0.0175  0.0082  -0.0004 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1767 0.1463 0.1342 0.0208  0.0110  0.0015  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1776 0.1499 0.1387 0.0205  0.0130  0.0042  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1713 0.1470 0.1364 0.0178  0.0130  0.0054  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1795 0.1557 0.1353 0.0219  0.0119  0.0028  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1862 0.1600 0.1359 0.0240  0.0108  0.0010  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2032 0.1735 0.1464 0.0283  0.0117  -0.0003 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.1944 0.1693 0.1438 0.0224  0.0090  0.0007  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2258 0.1935 0.1615 0.0311  0.0108  -0.0021 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2165 0.1889 0.1584 0.0254  0.0079  -0.0007 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2354 0.2040 0.1699 0.0298  0.0088  -0.0023 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2559 0.2217 0.1810 0.0337  0.0079  -0.0037 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1834 0.1544 0.1421 0.0239  0.0148  0.0053  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1803 0.1543 0.1405 0.0248  0.0163  0.0079  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1869 0.1707 0.1487 0.0255  0.0163  0.0088  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.1977 0.1850 0.1589 0.0268  0.0166  0.0083  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1955 0.1645 0.1524 0.0290  0.0179  0.0086  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2040 0.1717 0.1575 0.0311  0.0175  0.0064  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1816 0.1482 0.1354 0.0278  0.0154  0.0040  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1786 0.1667 0.1429 0.0245  0.0161  0.0100  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1815 0.1786 0.1491 0.0245  0.0154  0.0100  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1907 0.1913 0.1582 0.0267  0.0149  0.0108  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1919 0.1880 0.1566 0.0270  0.0155  0.0120  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1866 0.1868 0.1583 0.0202  0.0145  0.0091  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.1991 0.1985 0.1705 0.0193  0.0148  0.0086  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.1887 0.1849 0.1605 0.0176  0.0142  0.0091  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1865 0.1956 0.1573 0.0283  0.0137  0.0103  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1785 0.1929 0.1498 0.0303  0.0118  0.0100  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1570 0.1769 0.1343 0.0262  0.0102  0.0079  75  SER   A C   
545  O O   . SER   A 69  ? 0.1566 0.1803 0.1396 0.0240  0.0106  0.0072  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2122 0.2332 0.1856 0.0347  0.0108  0.0099  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2914 0.3068 0.2593 0.0388  0.0125  0.0118  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1446 0.1643 0.1206 0.0254  0.0090  0.0071  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1522 0.1757 0.1338 0.0216  0.0076  0.0049  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1617 0.1909 0.1441 0.0232  0.0043  0.0023  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1664 0.1944 0.1421 0.0274  0.0036  0.0029  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1544 0.1716 0.1347 0.0180  0.0092  0.0055  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1566 0.1676 0.1306 0.0194  0.0107  0.0071  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1674 0.1719 0.1379 0.0204  0.0129  0.0094  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1691 0.1804 0.1410 0.0198  0.0102  0.0063  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1806 0.1791 0.1472 0.0213  0.0151  0.0113  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1818 0.1871 0.1483 0.0214  0.0128  0.0085  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1797 0.1788 0.1443 0.0219  0.0154  0.0112  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1514 0.1865 0.1419 0.0203  0.0024  -0.0007 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1540 0.1946 0.1462 0.0216  -0.0017 -0.0045 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1604 0.1960 0.1460 0.0216  -0.0017 -0.0052 77  SER   A C   
562  O O   . SER   A 71  ? 0.1670 0.1967 0.1511 0.0188  0.0014  -0.0033 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1646 0.2118 0.1691 0.0179  -0.0034 -0.0076 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1690 0.2123 0.1768 0.0130  -0.0010 -0.0071 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1620 0.2005 0.1437 0.0250  -0.0052 -0.0082 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1665 0.2010 0.1412 0.0261  -0.0050 -0.0092 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1781 0.2121 0.1600 0.0207  -0.0048 -0.0117 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1780 0.2167 0.1704 0.0172  -0.0065 -0.0141 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.1908 0.2298 0.1599 0.0316  -0.0099 -0.0129 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2512 0.2889 0.2106 0.0381  -0.0095 -0.0096 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3396 0.3810 0.2910 0.0446  -0.0145 -0.0130 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4210 0.4595 0.3610 0.0518  -0.0132 -0.0086 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4715 0.5121 0.4003 0.0595  -0.0176 -0.0112 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1843 0.2127 0.1616 0.0200  -0.0023 -0.0110 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1900 0.2175 0.1741 0.0154  -0.0021 -0.0132 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1925 0.2254 0.1831 0.0146  -0.0068 -0.0192 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2018 0.2372 0.1872 0.0186  -0.0104 -0.0229 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2077 0.2293 0.1845 0.0166  0.0009  -0.0120 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2227 0.2409 0.1907 0.0205  0.0038  -0.0075 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.1926 0.2152 0.1590 0.0237  0.0008  -0.0079 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1820 0.2166 0.1840 0.0096  -0.0068 -0.0203 80  SER   A N   
582  C CA  . SER   A 74  ? 0.2029 0.2425 0.2141 0.0079  -0.0110 -0.0261 80  SER   A CA  
583  C C   . SER   A 74  ? 0.1987 0.2362 0.2206 0.0024  -0.0090 -0.0264 80  SER   A C   
584  O O   . SER   A 74  ? 0.1966 0.2292 0.2174 0.0004  -0.0048 -0.0219 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2433 0.2907 0.2606 0.0090  -0.0141 -0.0274 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3016 0.3498 0.3265 0.0058  -0.0106 -0.0233 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1940 0.2350 0.2261 0.0001  -0.0123 -0.0318 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2051 0.2440 0.2486 -0.0050 -0.0107 -0.0325 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1951 0.2380 0.2496 -0.0078 -0.0086 -0.0295 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1992 0.2493 0.2613 -0.0077 -0.0117 -0.0324 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2169 0.2580 0.2677 -0.0058 -0.0157 -0.0406 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2598 0.2950 0.3053 -0.0052 -0.0162 -0.0440 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2704 0.3082 0.3239 -0.0059 -0.0220 -0.0530 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2681 0.2965 0.3167 -0.0086 -0.0109 -0.0398 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1917 0.2305 0.2470 -0.0100 -0.0034 -0.0237 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1937 0.2354 0.2573 -0.0119 -0.0001 -0.0197 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1974 0.2350 0.2694 -0.0158 0.0040  -0.0172 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2006 0.2315 0.2671 -0.0160 0.0057  -0.0154 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2089 0.2493 0.2617 -0.0089 0.0024  -0.0144 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2356 0.2803 0.2819 -0.0049 -0.0012 -0.0164 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2103 0.2515 0.2681 -0.0101 0.0069  -0.0094 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2713 0.3131 0.3064 -0.0018 0.0007  -0.0122 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1890 0.2304 0.2749 -0.0187 0.0057  -0.0170 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.1998 0.2366 0.2941 -0.0221 0.0105  -0.0137 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.1869 0.2189 0.2722 -0.0204 0.0157  -0.0061 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.1847 0.2197 0.2654 -0.0182 0.0170  -0.0032 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2112 0.2535 0.3238 -0.0255 0.0122  -0.0145 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2423 0.2787 0.3646 -0.0291 0.0172  -0.0117 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2644 0.2990 0.3895 -0.0294 0.0243  -0.0043 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2714 0.3033 0.3983 -0.0314 0.0150  -0.0161 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2810 0.3093 0.4139 -0.0321 0.0295  -0.0008 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2869 0.3124 0.4224 -0.0343 0.0199  -0.0131 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.2825 0.3063 0.4213 -0.0347 0.0272  -0.0052 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.1777 0.2024 0.2599 -0.0210 0.0181  -0.0034 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.1836 0.2036 0.2568 -0.0190 0.0221  0.0031  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.1917 0.2070 0.2725 -0.0209 0.0270  0.0071  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.1949 0.2062 0.2806 -0.0228 0.0266  0.0052  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.1936 0.2090 0.2539 -0.0166 0.0198  0.0030  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2019 0.2131 0.2535 -0.0143 0.0227  0.0089  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.1970 0.2160 0.2504 -0.0147 0.0157  -0.0005 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.1939 0.2091 0.2746 -0.0199 0.0322  0.0129  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2005 0.2109 0.2871 -0.0208 0.0383  0.0183  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.1946 0.1968 0.2735 -0.0193 0.0385  0.0207  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.1994 0.2000 0.2662 -0.0167 0.0351  0.0201  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2596 0.2712 0.3427 -0.0181 0.0438  0.0246  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3939 0.4038 0.4889 -0.0199 0.0513  0.0297  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5375 0.5456 0.6249 -0.0158 0.0580  0.0373  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5659 0.5694 0.6580 -0.0159 0.0650  0.0433  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5785 0.5890 0.6543 -0.0123 0.0564  0.0375  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.1870 0.1839 0.2740 -0.0210 0.0428  0.0238  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.1954 0.1845 0.2763 -0.0191 0.0434  0.0267  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2020 0.1887 0.2672 -0.0139 0.0441  0.0320  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.2000 0.1885 0.2614 -0.0119 0.0474  0.0358  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2042 0.1875 0.2962 -0.0211 0.0492  0.0305  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2005 0.1834 0.2570 -0.0115 0.0409  0.0317  87  SER   A N   
636  C CA  . SER   A 81  ? 0.2094 0.1898 0.2519 -0.0065 0.0402  0.0357  87  SER   A CA  
637  C C   . SER   A 81  ? 0.2317 0.2054 0.2726 -0.0046 0.0403  0.0382  87  SER   A C   
638  O O   . SER   A 81  ? 0.2352 0.2062 0.2859 -0.0074 0.0415  0.0369  87  SER   A O   
639  C CB  . SER   A 81  ? 0.2156 0.2001 0.2500 -0.0055 0.0343  0.0312  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2188 0.2030 0.2548 -0.0067 0.0302  0.0269  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.2406 0.2118 0.2699 0.0002  0.0385  0.0412  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.2591 0.2248 0.2876 0.0025  0.0379  0.0432  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.2453 0.2127 0.2782 0.0003  0.0331  0.0372  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.2513 0.2145 0.2872 0.0011  0.0331  0.0378  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.3302 0.2933 0.3456 0.0088  0.0367  0.0477  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.4519 0.4193 0.4598 0.0104  0.0299  0.0435  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.5834 0.5488 0.5783 0.0168  0.0276  0.0468  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.5946 0.5589 0.5874 0.0196  0.0234  0.0463  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.6306 0.5959 0.6175 0.0194  0.0297  0.0493  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.2233 0.1965 0.2564 -0.0020 0.0295  0.0317  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.2153 0.1905 0.2508 -0.0035 0.0255  0.0263  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2085 0.1843 0.2535 -0.0075 0.0262  0.0218  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2130 0.1880 0.2607 -0.0079 0.0245  0.0185  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.2120 0.1923 0.2414 -0.0030 0.0218  0.0234  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.2241 0.2040 0.2442 0.0010  0.0200  0.0264  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.2425 0.2241 0.2564 0.0021  0.0204  0.0277  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.2369 0.2150 0.2546 0.0039  0.0174  0.0275  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.2597 0.2406 0.2642 0.0061  0.0180  0.0294  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.2550 0.2330 0.2643 0.0079  0.0146  0.0293  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.2757 0.2548 0.2779 0.0090  0.0147  0.0299  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.3009 0.2796 0.2941 0.0132  0.0113  0.0307  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2009 0.1784 0.2512 -0.0102 0.0285  0.0213  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.1956 0.1744 0.2553 -0.0140 0.0280  0.0159  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2011 0.1791 0.2707 -0.0167 0.0320  0.0174  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.1873 0.1668 0.2555 -0.0161 0.0349  0.0217  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.1780 0.1635 0.2353 -0.0149 0.0244  0.0108  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.1614 0.1484 0.2106 -0.0128 0.0210  0.0089  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.1617 0.1473 0.2119 -0.0127 0.0195  0.0052  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1693 0.1594 0.2107 -0.0111 0.0197  0.0102  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1610 0.1484 0.2053 -0.0109 0.0173  0.0038  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1645 0.1558 0.2005 -0.0097 0.0172  0.0086  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1633 0.1536 0.2012 -0.0097 0.0163  0.0056  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1497 0.1413 0.1837 -0.0083 0.0147  0.0045  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2168 0.1931 0.2972 -0.0200 0.0321  0.0132  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2205 0.1975 0.3133 -0.0235 0.0354  0.0135  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2153 0.2009 0.3095 -0.0250 0.0327  0.0095  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2119 0.2016 0.2977 -0.0234 0.0282  0.0059  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2328 0.2056 0.3364 -0.0263 0.0347  0.0085  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2438 0.2174 0.3399 -0.0247 0.0295  0.0029  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2175 0.1918 0.2999 -0.0205 0.0290  0.0074  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2111 0.1996 0.3169 -0.0279 0.0354  0.0098  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2097 0.2071 0.3186 -0.0291 0.0324  0.0056  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2000 0.1998 0.3103 -0.0302 0.0258  -0.0034 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.1967 0.1922 0.3139 -0.0321 0.0250  -0.0071 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2116 0.2118 0.3361 -0.0324 0.0367  0.0072  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.1917 0.1971 0.2932 -0.0281 0.0214  -0.0065 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.1847 0.1918 0.2837 -0.0276 0.0156  -0.0142 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.1820 0.1964 0.2739 -0.0253 0.0117  -0.0166 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.1870 0.2044 0.2751 -0.0240 0.0136  -0.0122 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.1880 0.1887 0.2768 -0.0252 0.0153  -0.0136 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.1957 0.1975 0.2703 -0.0216 0.0151  -0.0100 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.1908 0.1868 0.2586 -0.0197 0.0168  -0.0063 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.1884 0.1858 0.2451 -0.0168 0.0149  -0.0063 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.1855 0.1851 0.2353 -0.0152 0.0152  -0.0029 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.1641 0.1642 0.2059 -0.0130 0.0138  -0.0030 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.1638 0.1648 0.2152 -0.0156 0.0172  0.0008  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1736 0.1901 0.2623 -0.0241 0.0065  -0.0234 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.1774 0.1995 0.2572 -0.0209 0.0031  -0.0250 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1658 0.1839 0.2310 -0.0176 0.0036  -0.0226 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.1711 0.1847 0.2335 -0.0171 0.0032  -0.0248 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.1885 0.2151 0.2710 -0.0203 -0.0030 -0.0334 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2045 0.2372 0.3029 -0.0235 -0.0046 -0.0365 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2159 0.2564 0.3163 -0.0224 -0.0058 -0.0358 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2233 0.2538 0.3363 -0.0276 -0.0042 -0.0397 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2220 0.2691 0.3392 -0.0254 -0.0070 -0.0385 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2351 0.2715 0.3655 -0.0311 -0.0052 -0.0423 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2413 0.2866 0.3741 -0.0300 -0.0066 -0.0418 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2590 0.3111 0.4109 -0.0334 -0.0076 -0.0447 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1485 0.1680 0.2056 -0.0155 0.0049  -0.0183 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1390 0.1552 0.1841 -0.0127 0.0054  -0.0162 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1375 0.1574 0.1754 -0.0095 0.0021  -0.0195 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1526 0.1772 0.1908 -0.0087 0.0009  -0.0195 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1436 0.1584 0.1843 -0.0121 0.0084  -0.0099 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1628 0.1750 0.1934 -0.0096 0.0086  -0.0083 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1626 0.1722 0.1904 -0.0094 0.0108  -0.0032 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1570 0.1641 0.1886 -0.0106 0.0126  -0.0008 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1453 0.1547 0.1661 -0.0075 0.0107  -0.0017 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1335 0.1508 0.1643 -0.0073 0.0012  -0.0219 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1313 0.1510 0.1534 -0.0033 -0.0013 -0.0244 96  SER   A CA  
720  C C   . SER   A 90  ? 0.1370 0.1551 0.1497 -0.0008 0.0012  -0.0196 96  SER   A C   
721  O O   . SER   A 90  ? 0.1597 0.1746 0.1726 -0.0022 0.0042  -0.0154 96  SER   A O   
722  C CB  . SER   A 90  ? 0.1635 0.1808 0.1819 -0.0015 -0.0028 -0.0294 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1898 0.2018 0.2060 -0.0016 0.0007  -0.0269 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1252 0.1456 0.1302 0.0030  -0.0003 -0.0202 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1240 0.1422 0.1204 0.0057  0.0022  -0.0159 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1242 0.1424 0.1237 0.0036  0.0041  -0.0114 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1325 0.1472 0.1284 0.0040  0.0067  -0.0077 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1427 0.1559 0.1345 0.0066  0.0055  -0.0145 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.1896 0.2021 0.1763 0.0096  0.0044  -0.0187 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2243 0.2362 0.2003 0.0147  0.0050  -0.0184 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.1990 0.2110 0.1894 0.0085  0.0028  -0.0232 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2214 0.2326 0.1940 0.0169  0.0037  -0.0230 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2132 0.2244 0.1945 0.0132  0.0021  -0.0264 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1156 0.1375 0.1222 0.0016  0.0027  -0.0119 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1279 0.1498 0.1365 0.0004  0.0046  -0.0081 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1323 0.1578 0.1381 0.0032  0.0035  -0.0076 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1346 0.1651 0.1423 0.0046  0.0005  -0.0108 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1297 0.1532 0.1481 -0.0031 0.0051  -0.0082 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1536 0.1761 0.1731 -0.0039 0.0077  -0.0040 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1696 0.1867 0.1833 -0.0036 0.0094  -0.0010 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.1684 0.1921 0.1975 -0.0068 0.0092  -0.0035 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1248 0.1480 0.1266 0.0041  0.0055  -0.0040 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1342 0.1597 0.1329 0.0072  0.0050  -0.0030 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1597 0.1856 0.1616 0.0061  0.0068  -0.0007 99  MET   A C   
745  O O   . MET   A 93  ? 0.1648 0.1861 0.1651 0.0048  0.0087  0.0015  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1371 0.1576 0.1270 0.0099  0.0064  -0.0008 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1373 0.1566 0.1220 0.0120  0.0058  -0.0023 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2047 0.2171 0.1808 0.0147  0.0093  0.0015  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.1859 0.1938 0.1668 0.0102  0.0116  0.0032  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1589 0.1905 0.1654 0.0071  0.0061  -0.0012 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1571 0.1893 0.1660 0.0068  0.0087  0.0013  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1463 0.1777 0.1495 0.0105  0.0093  0.0029  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1326 0.1661 0.1333 0.0135  0.0074  0.0019  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1727 0.2120 0.1927 0.0053  0.0087  0.0001  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2213 0.2611 0.2494 0.0013  0.0088  -0.0013 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2241 0.2703 0.2647 -0.0004 0.0102  -0.0015 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2398 0.2727 0.2643 -0.0005 0.0114  0.0014  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1439 0.1722 0.1449 0.0108  0.0119  0.0053  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1516 0.1782 0.1475 0.0143  0.0130  0.0067  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1437 0.1708 0.1408 0.0147  0.0160  0.0084  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1391 0.1653 0.1384 0.0124  0.0175  0.0093  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1625 0.1810 0.1502 0.0149  0.0130  0.0073  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1377 0.1657 0.1327 0.0183  0.0173  0.0092  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1581 0.1856 0.1520 0.0199  0.0207  0.0110  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1647 0.1831 0.1485 0.0210  0.0207  0.0111  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1678 0.1819 0.1465 0.0227  0.0193  0.0103  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1773 0.2101 0.1738 0.0239  0.0221  0.0114  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1887 0.2195 0.1815 0.0266  0.0263  0.0132  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1754 0.2183 0.1842 0.0226  0.0214  0.0105  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1610 0.1762 0.1422 0.0199  0.0219  0.0120  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.1685 0.1757 0.1409 0.0208  0.0209  0.0113  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.1734 0.1789 0.1440 0.0198  0.0218  0.0126  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.1730 0.1822 0.1497 0.0174  0.0230  0.0140  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.1683 0.1678 0.1302 0.0222  0.0212  0.0119  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.1632 0.1603 0.1211 0.0225  0.0216  0.0132  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.1490 0.1449 0.1099 0.0189  0.0186  0.0127  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.1509 0.1440 0.1120 0.0173  0.0150  0.0103  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.1815 0.1725 0.1279 0.0269  0.0208  0.0119  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2052 0.1937 0.1459 0.0283  0.0208  0.0133  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2206 0.2118 0.1615 0.0298  0.0258  0.0175  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2286 0.2127 0.1648 0.0283  0.0163  0.0114  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2518 0.2393 0.1862 0.0313  0.0244  0.0184  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2499 0.2335 0.1815 0.0305  0.0182  0.0144  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.1465 0.1438 0.1094 0.0181  0.0204  0.0152  105 SER   A N   
785  C CA  . SER   A 99  ? 0.1418 0.1377 0.1070 0.0155  0.0180  0.0152  105 SER   A CA  
786  C C   . SER   A 99  ? 0.1462 0.1418 0.1098 0.0169  0.0212  0.0189  105 SER   A C   
787  O O   . SER   A 99  ? 0.1510 0.1491 0.1162 0.0181  0.0261  0.0218  105 SER   A O   
788  C CB  . SER   A 99  ? 0.1292 0.1286 0.1038 0.0113  0.0171  0.0142  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.1507 0.1546 0.1327 0.0097  0.0203  0.0161  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.1458 0.1378 0.1057 0.0174  0.0187  0.0191  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.1644 0.1549 0.1216 0.0194  0.0214  0.0230  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.1859 0.1750 0.1463 0.0173  0.0181  0.0226  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.1781 0.1673 0.1415 0.0151  0.0136  0.0191  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.1960 0.1826 0.1400 0.0254  0.0223  0.0244  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2492 0.2319 0.1846 0.0279  0.0160  0.0201  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.2597 0.2384 0.1808 0.0345  0.0166  0.0205  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.2687 0.2445 0.1820 0.0383  0.0161  0.0227  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.2435 0.2216 0.1604 0.0365  0.0174  0.0186  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2061 0.1938 0.1670 0.0181  0.0207  0.0266  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2161 0.2024 0.1799 0.0169  0.0174  0.0263  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2140 0.1980 0.1710 0.0192  0.0111  0.0229  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2194 0.2009 0.1658 0.0238  0.0097  0.0226  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2362 0.2199 0.1984 0.0191  0.0219  0.0318  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2388 0.2244 0.2037 0.0188  0.0284  0.0348  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2110 0.1980 0.1700 0.0205  0.0270  0.0319  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2046 0.1898 0.1684 0.0161  0.0072  0.0199  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.1958 0.1801 0.1576 0.0170  0.0011  0.0160  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.1822 0.1681 0.1492 0.0137  -0.0004 0.0120  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.1879 0.1737 0.1583 0.0127  -0.0047 0.0088  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1612 0.1486 0.1295 0.0121  0.0032  0.0124  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1545 0.1427 0.1263 0.0099  0.0025  0.0096  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1406 0.1312 0.1216 0.0060  0.0030  0.0090  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1477 0.1383 0.1312 0.0045  0.0027  0.0071  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1689 0.1578 0.1375 0.0109  0.0057  0.0101  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.1815 0.1671 0.1406 0.0149  0.0045  0.0090  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.1713 0.1540 0.1277 0.0159  0.0001  0.0061  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.1649 0.1511 0.1197 0.0172  0.0080  0.0109  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1353 0.1272 0.1207 0.0047  0.0042  0.0106  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1317 0.1255 0.1246 0.0017  0.0049  0.0097  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1359 0.1290 0.1322 0.0008  0.0022  0.0075  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1351 0.1270 0.1306 0.0020  -0.0011 0.0066  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1425 0.1369 0.1396 0.0008  0.0064  0.0113  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1832 0.1788 0.1807 0.0006  0.0105  0.0137  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1352 0.1294 0.1354 -0.0010 0.0036  0.0065  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1394 0.1330 0.1444 -0.0021 0.0024  0.0051  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1475 0.1389 0.1510 -0.0020 0.0019  0.0038  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1483 0.1391 0.1573 -0.0034 0.0023  0.0031  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1492 0.1393 0.1460 -0.0004 0.0017  0.0038  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1477 0.1349 0.1426 0.0001  0.0017  0.0026  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1557 0.1432 0.1527 -0.0008 0.0052  0.0037  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1550 0.1453 0.1509 -0.0006 0.0072  0.0050  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1560 0.1408 0.1565 -0.0017 0.0057  0.0032  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1589 0.1431 0.1603 -0.0018 0.0095  0.0049  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1508 0.1339 0.1456 0.0006  0.0111  0.0058  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1542 0.1343 0.1460 0.0017  0.0097  0.0048  113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1809 0.1623 0.1900 -0.0036 0.0107  0.0048  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2053 0.1897 0.2217 -0.0054 0.0108  0.0048  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1885 0.1671 0.1964 -0.0026 0.0153  0.0072  113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2218 0.2046 0.2486 -0.0075 0.0122  0.0048  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1387 0.1239 0.1312 0.0018  0.0135  0.0074  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1408 0.1254 0.1278 0.0046  0.0150  0.0086  114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1543 0.1352 0.1419 0.0052  0.0184  0.0106  114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1597 0.1417 0.1495 0.0046  0.0203  0.0115  114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1433 0.1334 0.1276 0.0059  0.0148  0.0086  114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1541 0.1449 0.1333 0.0094  0.0157  0.0096  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1615 0.1507 0.1383 0.0111  0.0152  0.0095  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1560 0.1532 0.1348 0.0102  0.0145  0.0086  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1610 0.1373 0.1463 0.0069  0.0198  0.0116  115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1776 0.1493 0.1635 0.0079  0.0239  0.0145  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1849 0.1544 0.1638 0.0121  0.0256  0.0165  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1788 0.1476 0.1551 0.0135  0.0237  0.0154  115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2043 0.1703 0.1975 0.0052  0.0245  0.0139  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2585 0.2253 0.2609 0.0015  0.0247  0.0131  115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3161 0.2771 0.3270 -0.0009 0.0250  0.0122  115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3353 0.2977 0.3573 -0.0043 0.0254  0.0116  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3484 0.3091 0.3768 -0.0052 0.0309  0.0147  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3261 0.2824 0.3499 -0.0025 0.0365  0.0189  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3764 0.3396 0.4162 -0.0082 0.0312  0.0140  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1811 0.1485 0.1570 0.0147  0.0296  0.0199  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.1985 0.1625 0.1676 0.0194  0.0315  0.0226  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2101 0.1655 0.1825 0.0192  0.0369  0.0262  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2122 0.1658 0.1930 0.0150  0.0383  0.0258  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2080 0.1767 0.1694 0.0236  0.0315  0.0237  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2076 0.1753 0.1683 0.0240  0.0361  0.0263  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2189 0.1692 0.1856 0.0236  0.0402  0.0298  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2289 0.1703 0.1989 0.0238  0.0464  0.0341  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2283 0.1698 0.2005 0.0230  0.0513  0.0371  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2347 0.1695 0.2135 0.0215  0.0570  0.0403  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.2567 0.1927 0.2179 0.0301  0.0493  0.0383  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3290 0.2695 0.2787 0.0361  0.0498  0.0409  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.4190 0.3548 0.3598 0.0430  0.0517  0.0448  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.4401 0.3804 0.3757 0.0463  0.0472  0.0429  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.3941 0.3208 0.3334 0.0455  0.0589  0.0509  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2189 0.1676 0.1861 0.0243  0.0497  0.0360  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2208 0.1696 0.1887 0.0246  0.0547  0.0387  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2015 0.1538 0.1811 0.0185  0.0536  0.0357  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2011 0.1524 0.1846 0.0180  0.0589  0.0383  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2296 0.1829 0.1848 0.0302  0.0542  0.0393  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2786 0.2296 0.2221 0.0370  0.0544  0.0420  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.3034 0.2601 0.2415 0.0393  0.0478  0.0386  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3081 0.2517 0.2454 0.0421  0.0605  0.0481  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3185 0.2717 0.2472 0.0457  0.0494  0.0422  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3289 0.2737 0.2560 0.0479  0.0571  0.0482  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.1784 0.1344 0.1631 0.0146  0.0473  0.0308  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.1743 0.1338 0.1693 0.0095  0.0454  0.0278  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1666 0.1329 0.1598 0.0083  0.0387  0.0232  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1702 0.1380 0.1573 0.0100  0.0351  0.0216  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1559 0.1262 0.1553 0.0054  0.0375  0.0213  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1565 0.1323 0.1554 0.0041  0.0320  0.0175  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1568 0.1365 0.1468 0.0072  0.0312  0.0171  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1627 0.1429 0.1500 0.0091  0.0344  0.0185  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1720 0.1503 0.1805 0.0005  0.0310  0.0159  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1777 0.1609 0.1848 -0.0002 0.0261  0.0129  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1757 0.1512 0.1942 -0.0027 0.0300  0.0150  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1481 0.1307 0.1342 0.0078  0.0269  0.0150  121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1602 0.1471 0.1400 0.0102  0.0251  0.0137  121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1624 0.1537 0.1460 0.0078  0.0223  0.0108  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1630 0.1570 0.1443 0.0090  0.0221  0.0095  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1730 0.1611 0.1482 0.0124  0.0227  0.0133  121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.1730 0.1669 0.1448 0.0143  0.0199  0.0111  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1857 0.1689 0.1561 0.0158  0.0258  0.0165  121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1529 0.1446 0.1417 0.0048  0.0200  0.0097  122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1605 0.1555 0.1528 0.0027  0.0177  0.0077  122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1561 0.1504 0.1522 0.0005  0.0155  0.0072  122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1615 0.1528 0.1584 0.0002  0.0154  0.0077  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1408 0.1375 0.1391 -0.0007 0.0136  0.0061  123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1348 0.1307 0.1347 -0.0017 0.0115  0.0060  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1327 0.1309 0.1309 -0.0014 0.0105  0.0059  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1239 0.1247 0.1230 -0.0016 0.0110  0.0054  123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1422 0.1379 0.1477 -0.0032 0.0107  0.0057  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1525 0.1502 0.1601 -0.0036 0.0118  0.0054  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1453 0.1391 0.1552 -0.0040 0.0114  0.0059  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1808 0.1785 0.1939 -0.0045 0.0110  0.0053  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1268 0.1238 0.1228 -0.0009 0.0092  0.0063  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1081 0.1069 0.1029 -0.0003 0.0094  0.0070  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1054 0.1053 0.1043 -0.0017 0.0097  0.0074  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1162 0.1146 0.1170 -0.0022 0.0087  0.0075  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1124 0.1089 0.1027 0.0013  0.0084  0.0075  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1198 0.1180 0.1090 0.0022  0.0099  0.0092  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1121 0.1069 0.0986 0.0028  0.0083  0.0068  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1040 0.1065 0.1051 -0.0022 0.0109  0.0075  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1159 0.1187 0.1217 -0.0036 0.0115  0.0077  125 SER   A CA  
923  C C   . SER   A 119 ? 0.1176 0.1216 0.1256 -0.0038 0.0134  0.0094  125 SER   A C   
924  O O   . SER   A 119 ? 0.1314 0.1340 0.1425 -0.0045 0.0143  0.0107  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1299 0.1343 0.1390 -0.0047 0.0114  0.0053  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1336 0.1377 0.1479 -0.0062 0.0120  0.0048  125 SER   A OG  
927  N N   . THR   A 120 ? 0.1160 0.1228 0.1234 -0.0031 0.0143  0.0096  126 THR   A N   
928  C CA  . THR   A 120 ? 0.1282 0.1367 0.1392 -0.0032 0.0170  0.0116  126 THR   A CA  
929  C C   . THR   A 120 ? 0.1427 0.1519 0.1484 -0.0007 0.0182  0.0131  126 THR   A C   
930  O O   . THR   A 120 ? 0.1271 0.1357 0.1276 0.0008  0.0165  0.0119  126 THR   A O   
931  C CB  . THR   A 120 ? 0.1405 0.1535 0.1605 -0.0055 0.0173  0.0095  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.1486 0.1658 0.1681 -0.0045 0.0160  0.0075  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.1390 0.1510 0.1632 -0.0075 0.0158  0.0069  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1500 0.1605 0.1580 -0.0001 0.0216  0.0157  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.1762 0.1881 0.1801 0.0027  0.0234  0.0171  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.1959 0.2099 0.2047 0.0030  0.0284  0.0204  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.1977 0.2118 0.2139 0.0006  0.0303  0.0217  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.1970 0.2119 0.2015 0.0061  0.0308  0.0220  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.2257 0.2424 0.2342 0.0071  0.0367  0.0260  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2448 0.2668 0.2559 0.0090  0.0391  0.0260  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.2676 0.2943 0.2838 0.0079  0.0361  0.0227  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2399 0.2611 0.2468 0.0126  0.0444  0.0299  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2303 0.2564 0.2400 0.0152  0.0482  0.0308  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2073 0.2355 0.2138 0.0168  0.0440  0.0269  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.1976 0.2329 0.2134 0.0166  0.0445  0.0259  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2584 0.2919 0.2856 0.0120  0.0523  0.0323  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3265 0.3571 0.3577 0.0106  0.0576  0.0370  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3524 0.3792 0.3758 0.0144  0.0632  0.0418  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3451 0.3769 0.3881 0.0055  0.0562  0.0357  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.1989 0.2210 0.1929 0.0188  0.0401  0.0249  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.1892 0.2116 0.1796 0.0205  0.0367  0.0217  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1896 0.2140 0.1853 0.0172  0.0316  0.0184  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2036 0.2290 0.1980 0.0186  0.0293  0.0164  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1629 0.1872 0.1634 0.0132  0.0300  0.0180  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1556 0.1810 0.1594 0.0106  0.0255  0.0149  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1435 0.1626 0.1413 0.0092  0.0228  0.0141  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1319 0.1469 0.1258 0.0094  0.0240  0.0159  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1622 0.1939 0.1787 0.0072  0.0256  0.0141  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1953 0.2352 0.2211 0.0081  0.0271  0.0138  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2138 0.2589 0.2538 0.0044  0.0284  0.0136  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1928 0.2359 0.2177 0.0098  0.0228  0.0107  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1313 0.1496 0.1283 0.0082  0.0193  0.0116  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1309 0.1445 0.1249 0.0066  0.0171  0.0108  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1327 0.1487 0.1312 0.0046  0.0150  0.0086  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1405 0.1596 0.1397 0.0059  0.0140  0.0073  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1361 0.1439 0.1220 0.0084  0.0157  0.0104  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1415 0.1494 0.1250 0.0105  0.0152  0.0094  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1497 0.1537 0.1350 0.0064  0.0136  0.0095  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1259 0.1406 0.1271 0.0022  0.0144  0.0082  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1358 0.1521 0.1401 0.0008  0.0126  0.0058  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1283 0.1400 0.1288 0.0004  0.0117  0.0055  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1187 0.1269 0.1181 -0.0002 0.0119  0.0067  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1275 0.1395 0.1263 0.0012  0.0108  0.0040  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1275 0.1356 0.1238 0.0011  0.0108  0.0041  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1268 0.1359 0.1247 0.0006  0.0105  0.0022  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1297 0.1419 0.1269 0.0019  0.0095  0.0004  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1195 0.1254 0.1107 0.0033  0.0113  0.0049  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1221 0.1267 0.1107 0.0046  0.0115  0.0061  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1220 0.1223 0.1095 0.0041  0.0114  0.0067  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1319 0.1395 0.1193 0.0068  0.0115  0.0061  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1328 0.1313 0.1170 0.0057  0.0114  0.0070  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1396 0.1456 0.1242 0.0085  0.0120  0.0070  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1377 0.1387 0.1201 0.0080  0.0120  0.0073  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1166 0.1233 0.1163 -0.0008 0.0111  0.0023  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1152 0.1217 0.1155 -0.0007 0.0113  0.0006  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1275 0.1323 0.1228 0.0016  0.0128  0.0013  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1301 0.1320 0.1254 0.0013  0.0143  0.0033  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1100 0.1145 0.1145 -0.0025 0.0119  0.0010  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1229 0.1294 0.1141 0.0040  0.0124  -0.0002 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1435 0.1479 0.1284 0.0071  0.0146  0.0011  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1515 0.1532 0.1371 0.0070  0.0174  0.0016  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1544 0.1568 0.1429 0.0060  0.0168  -0.0006 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1805 0.1876 0.1598 0.0106  0.0127  -0.0012 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2579 0.2625 0.2287 0.0150  0.0152  0.0010  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2643 0.2663 0.2336 0.0157  0.0171  0.0043  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.2986 0.3032 0.2640 0.0181  0.0156  -0.0005 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1347 0.1331 0.1185 0.0082  0.0209  0.0047  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1449 0.1413 0.1300 0.0086  0.0248  0.0058  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1566 0.1505 0.1338 0.0130  0.0288  0.0080  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1581 0.1502 0.1357 0.0141  0.0331  0.0095  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1485 0.1433 0.1422 0.0054  0.0262  0.0076  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1483 0.1450 0.1479 0.0022  0.0224  0.0058  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1403 0.1322 0.1344 0.0052  0.0277  0.0104  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1538 0.1476 0.1235 0.0161  0.0278  0.0086  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1517 0.1425 0.1126 0.0211  0.0319  0.0117  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.1701 0.1612 0.1233 0.0254  0.0333  0.0102  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.1814 0.1690 0.1281 0.0294  0.0386  0.0136  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1505 0.1416 0.1051 0.0241  0.0297  0.0124  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.1514 0.1407 0.1116 0.0212  0.0295  0.0144  138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.1836 0.1737 0.1373 0.0248  0.0272  0.0148  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.1953 0.1917 0.1504 0.0241  0.0215  0.0105  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2002 0.1994 0.1529 0.0264  0.0184  0.0098  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.1684 0.1642 0.1156 0.0301  0.0203  0.0132  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2007 0.2060 0.1575 0.0249  0.0138  0.0060  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.1721 0.1667 0.1255 0.0249  0.0289  0.0051  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.1831 0.1776 0.1290 0.0290  0.0296  0.0025  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2022 0.1946 0.1524 0.0279  0.0344  0.0033  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2105 0.2019 0.1534 0.0321  0.0362  0.0017  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.1885 0.1872 0.1343 0.0287  0.0227  -0.0041 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2264 0.2269 0.1844 0.0226  0.0203  -0.0066 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2131 0.2135 0.1787 0.0184  0.0209  -0.0038 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.2359 0.2373 0.1951 0.0223  0.0179  -0.0113 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2056 0.1977 0.1674 0.0228  0.0360  0.0054  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.1978 0.1889 0.1657 0.0218  0.0402  0.0061  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.1933 0.1812 0.1596 0.0243  0.0480  0.0115  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.1767 0.1638 0.1528 0.0210  0.0508  0.0149  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.1925 0.1852 0.1735 0.0158  0.0379  0.0057  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2201 0.2155 0.2031 0.0132  0.0313  0.0015  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2274 0.2238 0.2208 0.0085  0.0292  0.0022  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2266 0.2225 0.2066 0.0150  0.0296  -0.0031 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2125 0.1983 0.1667 0.0305  0.0515  0.0123  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2197 0.2016 0.1706 0.0340  0.0600  0.0184  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2169 0.1985 0.1789 0.0319  0.0666  0.0211  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2103 0.1893 0.1771 0.0318  0.0734  0.0267  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2281 0.2077 0.1614 0.0422  0.0623  0.0187  141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.2526 0.2336 0.1748 0.0452  0.0551  0.0152  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.2744 0.2528 0.1783 0.0544  0.0578  0.0160  141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.2543 0.2352 0.1809 0.0422  0.0529  0.0180  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2233 0.2075 0.1906 0.0303  0.0646  0.0171  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2295 0.2145 0.2082 0.0288  0.0701  0.0189  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2319 0.2186 0.2278 0.0223  0.0695  0.0211  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2364 0.2242 0.2437 0.0211  0.0746  0.0234  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2240 0.2108 0.2030 0.0294  0.0674  0.0137  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2174 0.2065 0.1993 0.0254  0.0583  0.0086  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2293 0.2184 0.2017 0.0268  0.0523  0.0040  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2112 0.2028 0.2067 0.0197  0.0545  0.0079  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2288 0.2201 0.2090 0.0220  0.0459  0.0009  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2193 0.2118 0.2125 0.0180  0.0472  0.0034  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2126 0.2061 0.2224 0.0163  0.0565  0.0103  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2226 0.2170 0.2257 0.0134  0.0427  0.0021  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2163 0.2120 0.2353 0.0121  0.0509  0.0084  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2224 0.2182 0.2372 0.0109  0.0444  0.0047  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2237 0.2110 0.2220 0.0185  0.0632  0.0199  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2411 0.2298 0.2542 0.0130  0.0617  0.0210  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.2893 0.2756 0.3094 0.0127  0.0692  0.0264  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.2759 0.2640 0.3114 0.0087  0.0697  0.0270  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2363 0.2250 0.2476 0.0102  0.0546  0.0191  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2316 0.2231 0.2418 0.0086  0.0472  0.0145  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2446 0.2359 0.2524 0.0067  0.0418  0.0136  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2241 0.2184 0.2465 0.0055  0.0455  0.0131  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3386 0.3207 0.3478 0.0173  0.0749  0.0301  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.3923 0.3707 0.4062 0.0179  0.0833  0.0361  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4339 0.4120 0.4506 0.0209  0.0930  0.0398  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.4428 0.4171 0.4616 0.0224  0.1014  0.0456  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.4492 0.4225 0.4478 0.0225  0.0852  0.0391  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5466 0.5194 0.5429 0.0202  0.0778  0.0369  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.5675 0.5413 0.5765 0.0146  0.0743  0.0356  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6062 0.5775 0.5878 0.0244  0.0754  0.0364  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.4612 0.4428 0.4775 0.0224  0.0926  0.0368  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.4931 0.4748 0.5123 0.0258  0.1022  0.0401  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.5032 0.4905 0.5378 0.0226  0.1008  0.0372  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.5107 0.5011 0.5464 0.0203  0.0923  0.0318  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.5358 0.5144 0.5339 0.0339  0.1056  0.0402  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.6187 0.5995 0.6073 0.0352  0.0971  0.0330  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.7324 0.7100 0.6988 0.0427  0.0968  0.0315  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.7556 0.7338 0.7150 0.0462  0.0960  0.0273  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.7686 0.7429 0.7245 0.0453  0.0970  0.0341  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3241 0.3017 0.2954 0.0094  -0.0200 -0.0107 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3127 0.2944 0.2964 0.0098  -0.0219 -0.0107 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.2900 0.2759 0.2813 0.0103  -0.0193 -0.0097 7   SER   C C   
1081 O O   . SER   B 1   ? 0.2970 0.2808 0.2837 0.0102  -0.0183 -0.0085 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3348 0.3133 0.3201 0.0094  -0.0290 -0.0100 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.3893 0.3645 0.3719 0.0094  -0.0321 -0.0078 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2566 0.2476 0.2588 0.0105  -0.0182 -0.0103 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2377 0.2321 0.2467 0.0108  -0.0151 -0.0103 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2219 0.2223 0.2386 0.0100  -0.0113 -0.0116 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2274 0.2289 0.2422 0.0091  -0.0102 -0.0120 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.1971 0.2007 0.2221 0.0102  -0.0092 -0.0123 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.1786 0.1875 0.2097 0.0087  -0.0051 -0.0136 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1796 0.1904 0.2139 0.0085  -0.0006 -0.0150 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.1776 0.1855 0.2123 0.0099  -0.0014 -0.0150 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.1703 0.1824 0.2113 0.0086  -0.0075 -0.0141 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1846 0.1994 0.2206 0.0062  0.0041  -0.0162 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1764 0.1926 0.2149 0.0055  0.0089  -0.0183 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1643 0.1854 0.2140 0.0051  0.0111  -0.0202 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1546 0.1790 0.2064 0.0033  0.0112  -0.0197 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1849 0.2016 0.2153 0.0023  0.0127  -0.0181 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.2019 0.2154 0.2233 0.0025  0.0107  -0.0160 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1809 0.1981 0.2123 0.0009  0.0177  -0.0209 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.2277 0.2429 0.2433 -0.0004 0.0126  -0.0150 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1637 0.1854 0.2213 0.0068  0.0130  -0.0225 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1625 0.1897 0.2325 0.0068  0.0161  -0.0249 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.1767 0.2051 0.2463 0.0051  0.0235  -0.0284 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.1824 0.2075 0.2531 0.0070  0.0248  -0.0304 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1492 0.1766 0.2315 0.0108  0.0118  -0.0249 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1416 0.1676 0.2234 0.0116  0.0042  -0.0217 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1471 0.1778 0.2353 0.0102  0.0026  -0.0210 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.1528 0.1723 0.2260 0.0131  -0.0011 -0.0192 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.1491 0.1775 0.2352 0.0105  -0.0045 -0.0185 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.1674 0.1848 0.2378 0.0133  -0.0077 -0.0167 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.1686 0.1901 0.2453 0.0121  -0.0095 -0.0165 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.1891 0.2074 0.2618 0.0119  -0.0161 -0.0145 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.1757 0.2079 0.2427 0.0010  0.0282  -0.0292 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.1799 0.2127 0.2441 -0.0016 0.0356  -0.0329 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.1828 0.2224 0.2547 -0.0042 0.0411  -0.0349 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.1751 0.2176 0.2454 -0.0071 0.0398  -0.0324 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.1958 0.2248 0.2443 -0.0052 0.0363  -0.0315 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.1981 0.2285 0.2407 -0.0080 0.0334  -0.0275 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2062 0.2352 0.2501 -0.0088 0.0437  -0.0354 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.1809 0.2231 0.2620 -0.0032 0.0470  -0.0395 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.1948 0.2444 0.2845 -0.0058 0.0533  -0.0420 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2071 0.2622 0.3086 -0.0047 0.0487  -0.0392 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2124 0.2666 0.3224 0.0000  0.0425  -0.0379 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2016 0.2609 0.3015 -0.0094 0.0505  -0.0376 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2014 0.2650 0.3114 -0.0090 0.0453  -0.0346 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.1894 0.2480 0.2877 -0.0105 0.0382  -0.0297 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.1856 0.2468 0.2865 -0.0130 0.0358  -0.0272 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2316 0.3038 0.3516 -0.0129 0.0515  -0.0361 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3147 0.3929 0.4515 -0.0098 0.0573  -0.0411 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.3341 0.4154 0.4868 -0.0052 0.0529  -0.0410 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.3341 0.4135 0.4677 -0.0122 0.0669  -0.0456 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.1758 0.2274 0.2623 -0.0087 0.0347  -0.0284 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1728 0.2196 0.2489 -0.0094 0.0287  -0.0244 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1586 0.2005 0.2335 -0.0046 0.0220  -0.0231 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1529 0.1928 0.2289 -0.0016 0.0224  -0.0248 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.1792 0.2225 0.2404 -0.0128 0.0311  -0.0234 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.1945 0.2411 0.2530 -0.0186 0.0369  -0.0237 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2143 0.2639 0.2762 -0.0218 0.0361  -0.0215 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2127 0.2589 0.2641 -0.0215 0.0431  -0.0261 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2366 0.2888 0.2948 -0.0279 0.0414  -0.0213 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2298 0.2784 0.2766 -0.0276 0.0485  -0.0263 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2534 0.3051 0.3036 -0.0309 0.0477  -0.0236 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.2944 0.3481 0.3389 -0.0376 0.0530  -0.0232 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1377 0.1770 0.2090 -0.0044 0.0161  -0.0202 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1362 0.1701 0.2030 -0.0010 0.0100  -0.0187 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1365 0.1663 0.1910 -0.0024 0.0087  -0.0165 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1250 0.1554 0.1786 -0.0049 0.0079  -0.0151 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1277 0.1620 0.2026 0.0008  0.0039  -0.0178 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1319 0.1597 0.1988 0.0029  -0.0025 -0.0160 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1644 0.1920 0.2384 0.0040  -0.0090 -0.0153 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.1838 0.2061 0.2495 0.0035  -0.0141 -0.0139 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.1965 0.2128 0.2542 0.0054  -0.0186 -0.0132 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.1762 0.1906 0.2327 0.0077  -0.0192 -0.0131 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.1756 0.1870 0.2257 0.0047  -0.0223 -0.0127 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1456 0.1716 0.1916 -0.0011 0.0086  -0.0162 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1453 0.1682 0.1815 -0.0019 0.0076  -0.0143 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1496 0.1681 0.1823 0.0011  0.0028  -0.0135 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1510 0.1675 0.1826 0.0033  0.0019  -0.0140 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1518 0.1742 0.1813 -0.0031 0.0111  -0.0145 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1562 0.1767 0.1781 -0.0039 0.0098  -0.0122 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1422 0.1680 0.1736 -0.0063 0.0164  -0.0161 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1374 0.1539 0.1675 0.0010  -0.0001 -0.0123 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1413 0.1530 0.1664 0.0034  -0.0039 -0.0122 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1418 0.1511 0.1607 0.0034  -0.0040 -0.0113 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1282 0.1391 0.1478 0.0014  -0.0026 -0.0102 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.1594 0.1698 0.1890 0.0038  -0.0085 -0.0125 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.1876 0.1996 0.2236 0.0049  -0.0098 -0.0131 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1549 0.1673 0.1894 0.0013  -0.0087 -0.0120 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1429 0.1482 0.1558 0.0055  -0.0056 -0.0116 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1403 0.1433 0.1493 0.0062  -0.0056 -0.0114 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1529 0.1538 0.1648 0.0053  -0.0084 -0.0115 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1657 0.1648 0.1791 0.0052  -0.0115 -0.0124 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1570 0.1560 0.1592 0.0085  -0.0063 -0.0126 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1809 0.1812 0.1795 0.0090  -0.0037 -0.0122 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.1922 0.1915 0.1895 0.0091  -0.0045 -0.0122 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1657 0.1680 0.1633 0.0093  -0.0009 -0.0115 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1479 0.1492 0.1611 0.0042  -0.0079 -0.0102 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1484 0.1470 0.1643 0.0029  -0.0106 -0.0099 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1485 0.1408 0.1610 0.0047  -0.0139 -0.0121 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1490 0.1395 0.1641 0.0033  -0.0170 -0.0125 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1459 0.1442 0.1624 0.0018  -0.0101 -0.0077 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1502 0.1458 0.1698 -0.0007 -0.0127 -0.0065 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1743 0.1677 0.1937 -0.0009 -0.0133 -0.0042 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1722 0.1625 0.1941 -0.0040 -0.0159 -0.0022 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.1922 0.1758 0.2144 -0.0030 -0.0192 -0.0032 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.1750 0.1545 0.1945 0.0009  -0.0199 -0.0066 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2243 0.2048 0.2489 -0.0063 -0.0217 -0.0010 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1466 0.1360 0.1533 0.0076  -0.0130 -0.0136 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1659 0.1485 0.1674 0.0090  -0.0155 -0.0163 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.1791 0.1601 0.1781 0.0083  -0.0185 -0.0173 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.1960 0.1709 0.1904 0.0083  -0.0216 -0.0194 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1726 0.1525 0.1686 0.0119  -0.0129 -0.0181 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.1736 0.1558 0.1650 0.0129  -0.0102 -0.0184 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.1722 0.1604 0.1662 0.0127  -0.0071 -0.0164 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.1854 0.1638 0.1687 0.0135  -0.0104 -0.0204 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.1808 0.1690 0.1694 0.0133  -0.0055 -0.0170 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.1941 0.1765 0.1758 0.0138  -0.0073 -0.0193 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.1706 0.1567 0.1728 0.0076  -0.0179 -0.0159 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.1845 0.1696 0.1863 0.0071  -0.0215 -0.0162 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.1975 0.1870 0.2096 0.0050  -0.0237 -0.0150 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2019 0.1920 0.2168 0.0047  -0.0270 -0.0147 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.1794 0.1661 0.1779 0.0082  -0.0197 -0.0156 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.1941 0.1771 0.1825 0.0098  -0.0172 -0.0167 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2073 0.1913 0.1924 0.0101  -0.0160 -0.0156 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2002 0.1756 0.1800 0.0099  -0.0201 -0.0191 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.1961 0.1889 0.2141 0.0033  -0.0218 -0.0140 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.1915 0.1892 0.2196 0.0009  -0.0226 -0.0130 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.1867 0.1814 0.2172 -0.0004 -0.0286 -0.0136 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.1824 0.1704 0.2067 -0.0004 -0.0315 -0.0147 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.1883 0.1885 0.2197 -0.0014 -0.0198 -0.0117 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.1797 0.1793 0.2195 -0.0014 -0.0305 -0.0130 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.1823 0.1803 0.2263 -0.0031 -0.0369 -0.0131 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.1794 0.1802 0.2317 -0.0068 -0.0373 -0.0123 24  THR   C C   
1214 O O   . THR   B 18  ? 0.1645 0.1690 0.2195 -0.0081 -0.0323 -0.0114 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.1912 0.1939 0.2432 -0.0021 -0.0392 -0.0125 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.1928 0.2044 0.2572 -0.0029 -0.0346 -0.0119 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.1986 0.1980 0.2423 0.0009  -0.0391 -0.0127 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.1817 0.1809 0.2382 -0.0090 -0.0435 -0.0122 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.1806 0.1831 0.2464 -0.0132 -0.0443 -0.0111 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.1622 0.1760 0.2413 -0.0142 -0.0390 -0.0100 25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.1438 0.1609 0.2268 -0.0174 -0.0352 -0.0089 25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2043 0.2045 0.2741 -0.0155 -0.0524 -0.0112 25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.2828 0.2713 0.3390 -0.0152 -0.0575 -0.0130 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.3261 0.3072 0.3739 -0.0157 -0.0560 -0.0140 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.3209 0.3036 0.3706 -0.0147 -0.0639 -0.0141 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.3422 0.3136 0.3792 -0.0152 -0.0608 -0.0162 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.3495 0.3214 0.3861 -0.0149 -0.0656 -0.0163 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.1609 0.1798 0.2460 -0.0117 -0.0385 -0.0103 26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.1677 0.1969 0.2656 -0.0121 -0.0329 -0.0102 26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1612 0.1917 0.2536 -0.0120 -0.0249 -0.0104 26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1606 0.1976 0.2601 -0.0149 -0.0196 -0.0101 26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.1907 0.2236 0.2963 -0.0087 -0.0347 -0.0107 26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.2484 0.2919 0.3695 -0.0090 -0.0290 -0.0113 26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.2539 0.3042 0.3880 -0.0120 -0.0290 -0.0108 26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.2563 0.3016 0.3765 -0.0063 -0.0233 -0.0125 26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1595 0.1840 0.2392 -0.0093 -0.0239 -0.0108 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1543 0.1793 0.2279 -0.0095 -0.0174 -0.0107 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1558 0.1801 0.2278 -0.0137 -0.0160 -0.0091 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.1477 0.1766 0.2218 -0.0164 -0.0105 -0.0085 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1678 0.1864 0.2289 -0.0062 -0.0177 -0.0111 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.1910 0.2101 0.2518 -0.0028 -0.0175 -0.0121 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.1820 0.2070 0.2506 -0.0026 -0.0141 -0.0127 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.1986 0.2119 0.2510 -0.0005 -0.0207 -0.0124 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1515 0.1693 0.2194 -0.0145 -0.0210 -0.0085 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.1676 0.1832 0.2340 -0.0184 -0.0207 -0.0066 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.1666 0.1889 0.2441 -0.0233 -0.0194 -0.0055 28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.1768 0.1998 0.2534 -0.0273 -0.0164 -0.0035 28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.1756 0.1815 0.2351 -0.0177 -0.0264 -0.0068 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.1836 0.1833 0.2323 -0.0142 -0.0256 -0.0074 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.1983 0.1938 0.2404 -0.0101 -0.0272 -0.0095 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.1842 0.1817 0.2283 -0.0149 -0.0231 -0.0056 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2105 0.2023 0.2453 -0.0079 -0.0251 -0.0094 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.1964 0.1892 0.2327 -0.0106 -0.0232 -0.0069 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.1886 0.1875 0.2342 -0.0190 -0.0212 -0.0027 28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2001 0.1901 0.2320 -0.0098 -0.0217 -0.0055 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2016 0.1968 0.2413 -0.0184 -0.0203 -0.0009 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.2062 0.1975 0.2401 -0.0136 -0.0206 -0.0023 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.1593 0.1868 0.2474 -0.0233 -0.0214 -0.0064 29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.1696 0.2052 0.2707 -0.0279 -0.0197 -0.0055 29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.1747 0.2194 0.2816 -0.0289 -0.0111 -0.0062 29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.1644 0.2160 0.2802 -0.0334 -0.0075 -0.0055 29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1629 0.2013 0.2750 -0.0273 -0.0255 -0.0063 29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1684 0.2130 0.2701 -0.0249 -0.0078 -0.0078 30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1687 0.2200 0.2734 -0.0254 0.0003  -0.0092 30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1737 0.2200 0.2638 -0.0253 0.0036  -0.0086 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1695 0.2176 0.2573 -0.0234 0.0081  -0.0104 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.1804 0.2360 0.2938 -0.0208 0.0006  -0.0118 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2109 0.2730 0.3410 -0.0213 -0.0025 -0.0120 30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2024 0.2732 0.3444 -0.0244 0.0025  -0.0126 30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2109 0.2692 0.3424 -0.0187 -0.0108 -0.0114 30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.1794 0.2192 0.2603 -0.0273 0.0008  -0.0061 31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.1914 0.2261 0.2597 -0.0271 0.0022  -0.0048 31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.1830 0.2217 0.2482 -0.0310 0.0092  -0.0045 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.1923 0.2347 0.2609 -0.0363 0.0123  -0.0033 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.1965 0.2238 0.2588 -0.0288 -0.0027 -0.0019 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2064 0.2282 0.2576 -0.0283 -0.0028 0.0000  31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2052 0.2246 0.2518 -0.0224 -0.0037 -0.0021 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2140 0.2284 0.2618 -0.0298 -0.0076 0.0027  31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.1604 0.1980 0.2183 -0.0289 0.0117  -0.0055 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.1636 0.2033 0.2155 -0.0329 0.0178  -0.0053 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.1733 0.2066 0.2132 -0.0343 0.0151  -0.0018 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.1773 0.2099 0.2119 -0.0398 0.0165  0.0010  32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.1631 0.2059 0.2157 -0.0302 0.0226  -0.0091 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.1725 0.2153 0.2154 -0.0344 0.0279  -0.0090 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.1529 0.2025 0.2191 -0.0291 0.0257  -0.0123 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.1658 0.1946 0.2021 -0.0294 0.0109  -0.0018 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.1694 0.1931 0.1968 -0.0294 0.0081  0.0011  33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.1671 0.1867 0.1946 -0.0235 0.0035  0.0004  33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.1635 0.1843 0.1941 -0.0196 0.0036  -0.0025 33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.1724 0.1976 0.1928 -0.0310 0.0120  0.0007  33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.1911 0.2123 0.2039 -0.0304 0.0088  0.0035  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2125 0.2307 0.2199 -0.0342 0.0064  0.0078  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.1948 0.2150 0.2059 -0.0258 0.0075  0.0024  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2165 0.2323 0.2203 -0.0318 0.0033  0.0094  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2113 0.2286 0.2171 -0.0268 0.0043  0.0060  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.1971 0.2183 0.2107 -0.0212 0.0084  -0.0009 33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2154 0.2321 0.2195 -0.0234 0.0027  0.0061  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2037 0.2235 0.2141 -0.0182 0.0069  -0.0007 33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2089 0.2270 0.2153 -0.0193 0.0043  0.0026  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1672 0.1817 0.1913 -0.0229 -0.0005 0.0030  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.1633 0.1739 0.1865 -0.0175 -0.0039 0.0020  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.1704 0.1776 0.1893 -0.0172 -0.0061 0.0050  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.1664 0.1720 0.1837 -0.0211 -0.0073 0.0085  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.1619 0.1690 0.1891 -0.0153 -0.0075 0.0006  34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.1928 0.1967 0.2220 -0.0189 -0.0101 0.0029  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2403 0.2378 0.2665 -0.0184 -0.0136 0.0056  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2566 0.2519 0.2830 -0.0226 -0.0150 0.0089  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2362 0.2308 0.2604 -0.0138 -0.0148 0.0046  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1653 0.1714 0.1829 -0.0127 -0.0069 0.0039  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1656 0.1694 0.1817 -0.0117 -0.0091 0.0065  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1578 0.1591 0.1752 -0.0060 -0.0103 0.0042  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1528 0.1566 0.1689 -0.0035 -0.0081 0.0021  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.1868 0.1944 0.1991 -0.0140 -0.0072 0.0083  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2397 0.2458 0.2515 -0.0141 -0.0104 0.0120  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.2287 0.2315 0.2441 -0.0103 -0.0132 0.0123  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2791 0.2873 0.2869 -0.0179 -0.0101 0.0146  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1448 0.1406 0.1643 -0.0041 -0.0135 0.0044  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1469 0.1395 0.1671 0.0012  -0.0140 0.0016  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1500 0.1429 0.1701 0.0012  -0.0138 0.0015  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.1520 0.1478 0.1728 0.0036  -0.0127 0.0023  36  SER   C C   
1321 O O   . SER   B 30  ? 0.1657 0.1624 0.1857 0.0071  -0.0106 -0.0005 36  SER   C O   
1322 C CB  A SER   B 30  ? 0.1614 0.1469 0.1840 0.0023  -0.0175 0.0020  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.1757 0.1612 0.1978 0.0026  -0.0172 0.0011  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.1788 0.1607 0.2014 0.0073  -0.0172 -0.0017 36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2079 0.1912 0.2327 0.0020  -0.0197 0.0048  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1509 0.1485 0.1729 0.0014  -0.0141 0.0065  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1600 0.1614 0.1841 0.0034  -0.0136 0.0076  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1535 0.1604 0.1744 0.0030  -0.0098 0.0059  37  SER   C C   
1329 O O   . SER   B 31  ? 0.1689 0.1788 0.1917 0.0053  -0.0087 0.0056  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.1840 0.1857 0.2097 0.0005  -0.0170 0.0129  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2263 0.2312 0.2468 -0.0050 -0.0162 0.0150  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1337 0.1416 0.1506 0.0002  -0.0079 0.0047  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1337 0.1455 0.1477 -0.0002 -0.0047 0.0029  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1359 0.1462 0.1486 0.0024  -0.0030 -0.0009 38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1323 0.1449 0.1428 0.0025  -0.0008 -0.0022 38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1397 0.1537 0.1505 -0.0051 -0.0034 0.0041  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1415 0.1567 0.1510 -0.0088 -0.0052 0.0080  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1620 0.1788 0.1666 -0.0142 -0.0031 0.0084  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1613 0.1805 0.1634 -0.0142 0.0003  0.0057  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1835 0.2042 0.1808 -0.0184 0.0024  0.0057  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.1628 0.1829 0.1559 -0.0235 0.0015  0.0084  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.1652 0.1871 0.1608 -0.0180 0.0051  0.0031  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1384 0.1446 0.1520 0.0040  -0.0047 -0.0024 39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1320 0.1359 0.1437 0.0057  -0.0044 -0.0056 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1334 0.1399 0.1449 0.0033  -0.0033 -0.0059 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1337 0.1401 0.1435 0.0045  -0.0025 -0.0077 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1277 0.1312 0.1365 0.0089  -0.0026 -0.0076 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1543 0.1544 0.1594 0.0101  -0.0032 -0.0104 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1701 0.1663 0.1756 0.0100  -0.0058 -0.0114 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1586 0.1596 0.1602 0.0107  -0.0016 -0.0112 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1276 0.1361 0.1410 -0.0003 -0.0030 -0.0042 40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1353 0.1466 0.1500 -0.0024 -0.0012 -0.0051 40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1382 0.1494 0.1569 -0.0047 -0.0023 -0.0049 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1449 0.1544 0.1640 -0.0067 -0.0038 -0.0029 40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1402 0.1550 0.1531 -0.0053 0.0018  -0.0041 40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1454 0.1614 0.1552 -0.0040 0.0033  -0.0046 40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1464 0.1649 0.1537 -0.0076 0.0059  -0.0039 40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1674 0.1826 0.1776 -0.0014 0.0039  -0.0070 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1304 0.1436 0.1526 -0.0049 -0.0014 -0.0067 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1281 0.1430 0.1560 -0.0075 -0.0018 -0.0066 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1311 0.1507 0.1635 -0.0082 0.0016  -0.0084 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1322 0.1519 0.1646 -0.0054 0.0018  -0.0100 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1232 0.1346 0.1536 -0.0061 -0.0061 -0.0074 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1347 0.1482 0.1722 -0.0093 -0.0071 -0.0070 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1315 0.1394 0.1685 -0.0094 -0.0118 -0.0065 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1367 0.1544 0.1815 -0.0085 -0.0068 -0.0089 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1266 0.1500 0.1626 -0.0119 0.0045  -0.0081 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1251 0.1535 0.1669 -0.0127 0.0086  -0.0102 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1293 0.1612 0.1805 -0.0147 0.0083  -0.0104 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1275 0.1592 0.1783 -0.0183 0.0079  -0.0084 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1255 0.1561 0.1627 -0.0162 0.0141  -0.0104 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1359 0.1714 0.1800 -0.0167 0.0193  -0.0136 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1321 0.1597 0.1611 -0.0147 0.0139  -0.0100 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1339 0.1687 0.1938 -0.0124 0.0080  -0.0125 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1383 0.1779 0.2098 -0.0140 0.0077  -0.0128 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1556 0.2020 0.2364 -0.0140 0.0134  -0.0156 43  SER   C C   
1377 O O   . SER   B 37  ? 0.1526 0.1983 0.2310 -0.0116 0.0161  -0.0175 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1458 0.1829 0.2213 -0.0112 0.0007  -0.0125 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.1811 0.2167 0.2571 -0.0069 -0.0012 -0.0139 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1652 0.2179 0.2571 -0.0167 0.0157  -0.0161 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.1835 0.2433 0.2862 -0.0165 0.0219  -0.0192 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2071 0.2693 0.3231 -0.0117 0.0180  -0.0206 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2132 0.2738 0.3326 -0.0106 0.0108  -0.0187 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.1940 0.2605 0.3032 -0.0220 0.0271  -0.0192 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2173 0.2852 0.3337 -0.0235 0.0217  -0.0169 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2195 0.2850 0.3428 -0.0090 0.0225  -0.0238 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2481 0.3156 0.3850 -0.0042 0.0186  -0.0248 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.2702 0.3472 0.4250 -0.0041 0.0250  -0.0281 45  THR   C C   
1389 O O   . THR   B 39  ? 0.2760 0.3564 0.4292 -0.0072 0.0339  -0.0306 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.2736 0.3344 0.4036 0.0003  0.0167  -0.0255 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.2978 0.3597 0.4269 0.0003  0.0249  -0.0290 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.2830 0.3354 0.3955 0.0002  0.0122  -0.0228 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.2807 0.3619 0.4524 -0.0007 0.0207  -0.0281 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.2957 0.3866 0.4874 0.0003  0.0267  -0.0315 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3038 0.3925 0.4982 0.0052  0.0304  -0.0351 46  THR   C C   
1396 O O   . THR   B 40  ? 0.3062 0.4004 0.5089 0.0051  0.0396  -0.0395 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3214 0.4189 0.5324 0.0015  0.0199  -0.0297 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.3548 0.4452 0.5627 0.0054  0.0091  -0.0268 46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3286 0.4302 0.5403 -0.0043 0.0187  -0.0272 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.2989 0.3790 0.4858 0.0092  0.0234  -0.0334 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3027 0.3791 0.4916 0.0137  0.0259  -0.0364 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3151 0.3849 0.4848 0.0117  0.0318  -0.0381 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3294 0.3952 0.4825 0.0082  0.0305  -0.0356 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3023 0.3726 0.4931 0.0184  0.0155  -0.0333 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.3102 0.3786 0.4827 0.0141  0.0378  -0.0424 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.3143 0.3763 0.4695 0.0120  0.0432  -0.0445 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.3028 0.3549 0.4453 0.0141  0.0361  -0.0415 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.3107 0.3596 0.4606 0.0187  0.0306  -0.0406 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.3424 0.4058 0.5054 0.0135  0.0524  -0.0508 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.4275 0.4882 0.5741 0.0085  0.0610  -0.0539 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.5216 0.5899 0.6671 0.0026  0.0670  -0.0543 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.5464 0.6235 0.7079 0.0028  0.0684  -0.0546 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.5373 0.6024 0.6643 -0.0030 0.0705  -0.0539 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.2810 0.3283 0.4048 0.0105  0.0363  -0.0398 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.2677 0.3065 0.3785 0.0116  0.0310  -0.0371 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.2420 0.2756 0.3456 0.0114  0.0361  -0.0404 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.2493 0.2850 0.3500 0.0083  0.0439  -0.0440 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2189 0.2453 0.3188 0.0141  0.0318  -0.0392 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2211 0.2416 0.3150 0.0140  0.0360  -0.0424 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2220 0.2359 0.2986 0.0116  0.0333  -0.0396 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2221 0.2297 0.2944 0.0120  0.0345  -0.0413 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.2366 0.2539 0.3435 0.0192  0.0348  -0.0445 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.2972 0.3234 0.4278 0.0225  0.0387  -0.0484 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2064 0.2216 0.2741 0.0092  0.0299  -0.0355 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2224 0.2329 0.2755 0.0069  0.0280  -0.0331 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2348 0.2458 0.2795 0.0023  0.0343  -0.0357 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2434 0.2595 0.2900 -0.0001 0.0385  -0.0374 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2343 0.2462 0.2816 0.0061  0.0230  -0.0285 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.2822 0.2914 0.3321 0.0095  0.0162  -0.0254 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.2953 0.2995 0.3469 0.0118  0.0142  -0.0254 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.2802 0.2915 0.3297 0.0095  0.0126  -0.0230 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2376 0.2433 0.2729 0.0006  0.0346  -0.0359 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2485 0.2537 0.2740 -0.0044 0.0393  -0.0379 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2233 0.2295 0.2387 -0.0074 0.0358  -0.0334 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2283 0.2322 0.2416 -0.0058 0.0312  -0.0301 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3055 0.3036 0.3274 -0.0046 0.0411  -0.0409 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3349 0.3322 0.3668 -0.0019 0.0455  -0.0460 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3238 0.3199 0.3325 -0.0105 0.0438  -0.0419 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2072 0.2166 0.2167 -0.0117 0.0379  -0.0329 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.1948 0.2052 0.1964 -0.0142 0.0344  -0.0286 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.1843 0.1913 0.1756 -0.0185 0.0352  -0.0290 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.1888 0.1944 0.1760 -0.0219 0.0397  -0.0325 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.1988 0.2139 0.1997 -0.0168 0.0347  -0.0268 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2037 0.2222 0.2150 -0.0135 0.0341  -0.0268 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2048 0.2205 0.1994 -0.0185 0.0304  -0.0221 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2170 0.2349 0.2324 -0.0091 0.0286  -0.0240 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.1597 0.1657 0.1472 -0.0186 0.0312  -0.0256 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.1555 0.1591 0.1341 -0.0230 0.0309  -0.0252 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.1529 0.1594 0.1250 -0.0280 0.0308  -0.0234 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1501 0.1604 0.1244 -0.0274 0.0287  -0.0204 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1598 0.1630 0.1379 -0.0218 0.0267  -0.0217 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.1568 0.1605 0.1202 -0.0333 0.0326  -0.0252 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.1504 0.1554 0.1053 -0.0392 0.0318  -0.0232 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.1499 0.1525 0.0981 -0.0429 0.0287  -0.0218 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.1588 0.1566 0.0998 -0.0466 0.0312  -0.0254 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.1794 0.1828 0.1292 -0.0428 0.0377  -0.0276 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.1897 0.1963 0.1484 -0.0391 0.0412  -0.0294 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.1968 0.2081 0.1597 -0.0379 0.0376  -0.0246 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.1921 0.2063 0.1637 -0.0350 0.0409  -0.0266 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2101 0.2278 0.1883 -0.0325 0.0382  -0.0234 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.1881 0.2065 0.1652 -0.0320 0.0325  -0.0185 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2070 0.2276 0.1936 -0.0305 0.0411  -0.0254 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.1448 0.1506 0.0961 -0.0416 0.0236  -0.0170 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.1505 0.1552 0.0983 -0.0444 0.0205  -0.0152 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.1624 0.1729 0.1148 -0.0436 0.0152  -0.0094 56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.1503 0.1644 0.1081 -0.0403 0.0141  -0.0071 56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.1475 0.1487 0.0991 -0.0410 0.0219  -0.0177 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.1690 0.1738 0.1315 -0.0336 0.0204  -0.0151 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.1653 0.1765 0.1168 -0.0460 0.0121  -0.0072 57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.1716 0.1889 0.1298 -0.0446 0.0078  -0.0022 57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.1736 0.1917 0.1369 -0.0420 0.0080  -0.0019 57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.1620 0.1847 0.1292 -0.0431 0.0050  0.0015  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.1914 0.2112 0.1460 -0.0503 0.0030  0.0015  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.2616 0.2786 0.2098 -0.0561 0.0016  0.0008  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.2532 0.2654 0.1991 -0.0559 0.0049  -0.0030 57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.3203 0.3394 0.2658 -0.0611 -0.0032 0.0042  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.1647 0.1785 0.1284 -0.0390 0.0114  -0.0053 58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1551 0.1685 0.1224 -0.0368 0.0117  -0.0048 58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1411 0.1610 0.1157 -0.0333 0.0103  -0.0013 58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1378 0.1604 0.1157 -0.0301 0.0101  -0.0006 58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1628 0.1703 0.1301 -0.0332 0.0148  -0.0083 58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2116 0.2103 0.1723 -0.0366 0.0170  -0.0129 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1381 0.1601 0.1151 -0.0340 0.0098  0.0005  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1452 0.1730 0.1290 -0.0307 0.0098  0.0031  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1557 0.1809 0.1392 -0.0291 0.0119  0.0027  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1496 0.1795 0.1374 -0.0279 0.0126  0.0046  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1335 0.1687 0.1224 -0.0335 0.0071  0.0066  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1458 0.1848 0.1375 -0.0331 0.0043  0.0083  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.1602 0.2071 0.1592 -0.0351 0.0011  0.0122  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.1806 0.2284 0.1778 -0.0402 -0.0025 0.0140  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1213 0.1739 0.1289 -0.0314 0.0024  0.0135  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1645 0.1821 0.1431 -0.0293 0.0131  0.0002  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1775 0.1909 0.1548 -0.0279 0.0143  0.0002  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1703 0.1770 0.1456 -0.0246 0.0149  -0.0026 60  THR   C C   
1495 O O   . THR   B 54  ? 0.1670 0.1709 0.1409 -0.0251 0.0152  -0.0052 60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2205 0.2306 0.1949 -0.0326 0.0141  0.0011  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2577 0.2609 0.2277 -0.0349 0.0137  -0.0018 60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2308 0.2483 0.2085 -0.0367 0.0130  0.0040  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1662 0.1708 0.1416 -0.0214 0.0152  -0.0021 61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1748 0.1740 0.1501 -0.0179 0.0150  -0.0042 61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1704 0.1667 0.1443 -0.0156 0.0144  -0.0027 61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1754 0.1726 0.1470 -0.0174 0.0148  -0.0003 61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1526 0.1453 0.1276 -0.0120 0.0132  -0.0040 62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1473 0.1360 0.1199 -0.0101 0.0116  -0.0025 62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1466 0.1372 0.1217 -0.0064 0.0105  -0.0034 62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1425 0.1337 0.1221 -0.0048 0.0103  -0.0056 62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1578 0.1379 0.1297 -0.0099 0.0097  -0.0026 62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.1679 0.1432 0.1369 -0.0080 0.0068  -0.0005 62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1680 0.1448 0.1367 -0.0140 0.0104  -0.0016 62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1491 0.1406 0.1210 -0.0053 0.0101  -0.0021 63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1479 0.1402 0.1213 -0.0022 0.0086  -0.0031 63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1581 0.1446 0.1270 -0.0010 0.0056  -0.0019 63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1562 0.1392 0.1190 -0.0029 0.0054  0.0003  63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1394 0.1378 0.1136 -0.0017 0.0105  -0.0034 63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1570 0.1558 0.1258 -0.0022 0.0119  -0.0022 63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1716 0.1725 0.1385 -0.0050 0.0144  -0.0006 63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1783 0.1753 0.1436 -0.0003 0.0110  -0.0029 63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.1902 0.1924 0.1526 -0.0056 0.0169  0.0001  63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1936 0.1907 0.1529 -0.0009 0.0133  -0.0024 63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.1987 0.1988 0.1569 -0.0035 0.0166  -0.0010 63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2165 0.2176 0.1695 -0.0044 0.0199  -0.0008 63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1643 0.1498 0.1359 0.0015  0.0028  -0.0029 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1674 0.1472 0.1344 0.0023  -0.0011 -0.0015 64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1607 0.1416 0.1216 0.0024  -0.0005 -0.0017 64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1523 0.1371 0.1166 0.0038  0.0004  -0.0036 64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1760 0.1539 0.1499 0.0047  -0.0052 -0.0023 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.1787 0.1506 0.1476 0.0052  -0.0105 -0.0003 64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.1904 0.1557 0.1538 0.0038  -0.0131 0.0025  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.1938 0.1661 0.1623 0.0064  -0.0132 -0.0011 64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2075 0.1666 0.1650 0.0036  -0.0187 0.0049  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2111 0.1774 0.1736 0.0061  -0.0187 0.0009  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2307 0.1904 0.1873 0.0046  -0.0215 0.0040  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.2669 0.2202 0.2169 0.0039  -0.0278 0.0065  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.1805 0.1574 0.1319 0.0007  -0.0007 0.0001  65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.1838 0.1606 0.1277 0.0004  0.0006  -0.0007 65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.1913 0.1609 0.1282 0.0005  -0.0049 0.0003  65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2092 0.1728 0.1381 -0.0017 -0.0071 0.0030  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.1901 0.1682 0.1275 -0.0022 0.0053  0.0004  65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2367 0.2139 0.1635 -0.0028 0.0082  -0.0011 65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.1804 0.1501 0.1202 0.0025  -0.0076 -0.0016 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2113 0.1747 0.1456 0.0024  -0.0138 -0.0007 66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2229 0.1805 0.1415 -0.0004 -0.0136 0.0001  66  SER   C C   
1543 O O   . SER   B 60  ? 0.2370 0.1875 0.1482 -0.0021 -0.0189 0.0029  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.2511 0.2166 0.1913 0.0044  -0.0159 -0.0033 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.3335 0.2930 0.2687 0.0039  -0.0225 -0.0023 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2118 0.1722 0.1253 -0.0009 -0.0074 -0.0022 67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2247 0.1803 0.1230 -0.0037 -0.0054 -0.0023 67  SER   C CA  
1548 C C   . SER   B 61  ? 0.2440 0.1962 0.1338 -0.0073 -0.0045 0.0014  67  SER   C C   
1549 O O   . SER   B 61  ? 0.2665 0.2140 0.1420 -0.0105 -0.0028 0.0019  67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2332 0.1936 0.1310 -0.0027 0.0018  -0.0062 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2385 0.2064 0.1446 -0.0023 0.0073  -0.0059 67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2302 0.1844 0.1283 -0.0072 -0.0050 0.0039  68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2331 0.1830 0.1245 -0.0108 -0.0053 0.0079  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2514 0.1957 0.1476 -0.0102 -0.0128 0.0113  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.2572 0.1962 0.1481 -0.0130 -0.0144 0.0151  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2382 0.1949 0.1347 -0.0118 0.0016  0.0079  68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.2429 0.2049 0.1352 -0.0127 0.0092  0.0052  68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.2828 0.2395 0.1591 -0.0173 0.0113  0.0071  68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3231 0.2856 0.1967 -0.0178 0.0196  0.0039  68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.3581 0.3197 0.2262 -0.0164 0.0214  0.0000  68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.3507 0.3058 0.2144 -0.0151 0.0150  -0.0007 68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.3674 0.3346 0.2349 -0.0164 0.0295  -0.0033 68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2555 0.2013 0.1626 -0.0065 -0.0172 0.0099  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.2672 0.2097 0.1831 -0.0048 -0.0234 0.0120  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.2682 0.2111 0.1889 -0.0055 -0.0208 0.0134  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.2793 0.2154 0.1990 -0.0065 -0.0252 0.0169  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3170 0.2501 0.2245 -0.0063 -0.0317 0.0158  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4108 0.3428 0.3159 -0.0055 -0.0363 0.0145  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5101 0.4340 0.4131 -0.0061 -0.0464 0.0186  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.5906 0.5103 0.4821 -0.0080 -0.0506 0.0184  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.6423 0.5532 0.5162 -0.0124 -0.0542 0.0216  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.6598 0.5653 0.5261 -0.0153 -0.0544 0.0258  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.6361 0.5431 0.4989 -0.0143 -0.0577 0.0206  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2562 0.2064 0.1810 -0.0056 -0.0138 0.0110  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2542 0.2049 0.1819 -0.0072 -0.0109 0.0120  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2190 0.1781 0.1571 -0.0055 -0.0062 0.0087  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.1968 0.1620 0.1370 -0.0041 -0.0036 0.0060  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3011 0.2514 0.2177 -0.0116 -0.0066 0.0140  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4197 0.3605 0.3257 -0.0151 -0.0103 0.0187  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5176 0.4598 0.4143 -0.0199 -0.0047 0.0202  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6020 0.5343 0.4879 -0.0244 -0.0081 0.0255  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.6390 0.5717 0.5117 -0.0293 -0.0030 0.0270  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2092 0.1679 0.1526 -0.0062 -0.0053 0.0088  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2059 0.1715 0.1567 -0.0059 -0.0010 0.0062  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2217 0.1903 0.1681 -0.0097 0.0034  0.0074  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2448 0.2084 0.1849 -0.0128 0.0029  0.0104  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2072 0.1704 0.1660 -0.0047 -0.0022 0.0050  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2216 0.1833 0.1875 -0.0010 -0.0059 0.0035  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2529 0.2203 0.2271 0.0012  -0.0040 0.0001  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2185 0.1739 0.1849 0.0006  -0.0113 0.0053  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2413 0.2064 0.2216 0.0041  -0.0078 -0.0003 71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2414 0.1994 0.2178 0.0040  -0.0126 0.0028  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.2048 0.1817 0.1554 -0.0097 0.0074  0.0055  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.2074 0.1888 0.1566 -0.0132 0.0113  0.0066  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1979 0.1844 0.1543 -0.0139 0.0129  0.0051  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1904 0.1809 0.1523 -0.0114 0.0129  0.0028  72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2128 0.2003 0.1597 -0.0129 0.0148  0.0062  72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2389 0.2216 0.1762 -0.0135 0.0144  0.0075  72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2619 0.2412 0.1914 -0.0176 0.0156  0.0105  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2503 0.2315 0.1852 -0.0105 0.0127  0.0059  72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2801 0.2543 0.1987 -0.0188 0.0152  0.0118  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2669 0.2428 0.1909 -0.0117 0.0121  0.0069  72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2911 0.2634 0.2065 -0.0159 0.0133  0.0100  72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3151 0.2817 0.2178 -0.0179 0.0129  0.0112  72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.2002 0.1865 0.1561 -0.0177 0.0140  0.0065  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1946 0.1859 0.1559 -0.0193 0.0152  0.0053  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1963 0.1976 0.1611 -0.0196 0.0181  0.0055  73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2013 0.2053 0.1639 -0.0204 0.0203  0.0070  73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.2078 0.1944 0.1664 -0.0238 0.0149  0.0071  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2191 0.2030 0.1715 -0.0255 0.0154  0.0102  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1953 0.1765 0.1448 -0.0215 0.0140  0.0097  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1882 0.1948 0.1586 -0.0188 0.0180  0.0040  74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1905 0.2063 0.1661 -0.0185 0.0198  0.0044  74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1768 0.1968 0.1569 -0.0209 0.0188  0.0045  74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1790 0.1950 0.1579 -0.0215 0.0171  0.0030  74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.2132 0.2310 0.1908 -0.0139 0.0198  0.0028  74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2342 0.2500 0.2072 -0.0121 0.0214  0.0028  74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.2163 0.2301 0.1942 -0.0118 0.0174  0.0008  74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1601 0.1882 0.1456 -0.0222 0.0198  0.0060  75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1570 0.1901 0.1474 -0.0239 0.0179  0.0065  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1310 0.1677 0.1257 -0.0193 0.0178  0.0057  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1279 0.1660 0.1236 -0.0162 0.0200  0.0053  75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1891 0.2299 0.1852 -0.0275 0.0183  0.0091  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2454 0.2826 0.2377 -0.0324 0.0177  0.0099  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1078 0.1454 0.1043 -0.0194 0.0154  0.0055  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1044 0.1444 0.1049 -0.0155 0.0148  0.0051  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1156 0.1604 0.1210 -0.0173 0.0118  0.0071  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1255 0.1698 0.1286 -0.0217 0.0099  0.0079  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.0991 0.1329 0.0953 -0.0127 0.0146  0.0027  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1045 0.1333 0.0961 -0.0150 0.0136  0.0014  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1184 0.1417 0.1054 -0.0161 0.0145  0.0003  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1229 0.1520 0.1146 -0.0162 0.0120  0.0013  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1392 0.1576 0.1229 -0.0177 0.0143  -0.0017 76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1367 0.1613 0.1240 -0.0183 0.0122  -0.0006 76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1396 0.1590 0.1234 -0.0189 0.0135  -0.0024 76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1116 0.1601 0.1230 -0.0142 0.0110  0.0077  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1256 0.1784 0.1423 -0.0157 0.0073  0.0104  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1543 0.2025 0.1655 -0.0175 0.0047  0.0102  77  SER   C C   
1639 O O   . SER   B 71  ? 0.1683 0.2106 0.1728 -0.0173 0.0062  0.0077  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1341 0.1922 0.1606 -0.0114 0.0074  0.0113  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1516 0.2051 0.1762 -0.0075 0.0078  0.0094  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1509 0.2020 0.1648 -0.0200 0.0006  0.0132  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1710 0.2180 0.1790 -0.0223 -0.0017 0.0135  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1805 0.2260 0.1914 -0.0179 -0.0019 0.0132  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.1763 0.2250 0.1952 -0.0138 -0.0019 0.0139  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2140 0.2639 0.2228 -0.0272 -0.0068 0.0173  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2986 0.3486 0.3028 -0.0324 -0.0070 0.0172  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.4073 0.4592 0.4102 -0.0382 -0.0127 0.0210  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.5065 0.5556 0.5011 -0.0443 -0.0127 0.0198  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.5679 0.6169 0.5577 -0.0509 -0.0186 0.0230  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1880 0.2286 0.1929 -0.0187 -0.0016 0.0118  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1952 0.2340 0.2029 -0.0151 -0.0020 0.0117  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2032 0.2447 0.2180 -0.0141 -0.0063 0.0155  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2143 0.2572 0.2284 -0.0182 -0.0102 0.0190  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2108 0.2450 0.2112 -0.0179 -0.0013 0.0105  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2299 0.2627 0.2239 -0.0213 0.0011  0.0083  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.2020 0.2384 0.1977 -0.0231 -0.0004 0.0101  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1919 0.2338 0.2135 -0.0089 -0.0058 0.0149  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.1926 0.2369 0.2231 -0.0069 -0.0096 0.0182  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.1827 0.2240 0.2177 -0.0015 -0.0089 0.0164  80  SER   C C   
1661 O O   . SER   B 74  ? 0.1650 0.2025 0.1955 0.0003  -0.0057 0.0128  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2163 0.2676 0.2550 -0.0063 -0.0100 0.0196  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.2512 0.3042 0.2933 -0.0019 -0.0051 0.0162  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.1820 0.2243 0.2259 0.0009  -0.0126 0.0192  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.1831 0.2220 0.2324 0.0060  -0.0126 0.0177  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.1848 0.2276 0.2413 0.0110  -0.0084 0.0146  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.1831 0.2323 0.2489 0.0119  -0.0093 0.0166  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.1907 0.2290 0.2475 0.0062  -0.0187 0.0225  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.2324 0.2642 0.2838 0.0033  -0.0226 0.0250  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.2498 0.2809 0.3097 0.0037  -0.0294 0.0305  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.2364 0.2619 0.2851 0.0062  -0.0200 0.0211  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1719 0.2112 0.2244 0.0139  -0.0039 0.0099  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.1852 0.2275 0.2419 0.0180  0.0011  0.0063  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.1930 0.2295 0.2507 0.0228  0.0027  0.0025  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.1815 0.2112 0.2320 0.0221  0.0017  0.0012  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2056 0.2489 0.2535 0.0155  0.0051  0.0042  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2325 0.2815 0.2808 0.0110  0.0037  0.0076  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2084 0.2526 0.2564 0.0188  0.0109  0.0002  82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.2679 0.3161 0.3071 0.0078  0.0063  0.0063  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2066 0.2458 0.2735 0.0274  0.0053  0.0006  83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2221 0.2550 0.2895 0.0320  0.0073  -0.0038 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2149 0.2435 0.2702 0.0317  0.0118  -0.0085 83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2205 0.2532 0.2720 0.0303  0.0158  -0.0095 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2362 0.2735 0.3169 0.0373  0.0102  -0.0055 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.2592 0.2886 0.3414 0.0421  0.0111  -0.0098 83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.2826 0.3097 0.3609 0.0450  0.0177  -0.0161 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.2783 0.3015 0.3641 0.0430  0.0052  -0.0076 83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.2950 0.3138 0.3736 0.0491  0.0185  -0.0206 83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.2945 0.3091 0.3810 0.0471  0.0058  -0.0117 83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.2956 0.3081 0.3787 0.0503  0.0125  -0.0184 83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2062 0.2262 0.2552 0.0324  0.0104  -0.0109 84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2120 0.2268 0.2494 0.0318  0.0133  -0.0151 84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2270 0.2346 0.2641 0.0358  0.0146  -0.0198 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2261 0.2284 0.2665 0.0369  0.0106  -0.0192 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2053 0.2163 0.2340 0.0278  0.0097  -0.0135 84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2136 0.2194 0.2313 0.0274  0.0117  -0.0173 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.1909 0.2080 0.2195 0.0238  0.0087  -0.0094 84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2379 0.2445 0.2700 0.0375  0.0201  -0.0245 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.2415 0.2406 0.2710 0.0409  0.0225  -0.0302 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.2300 0.2192 0.2517 0.0395  0.0178  -0.0313 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.2302 0.2186 0.2450 0.0357  0.0147  -0.0289 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3018 0.3010 0.3221 0.0408  0.0292  -0.0346 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.3837 0.3928 0.4118 0.0420  0.0349  -0.0342 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.4929 0.5044 0.5344 0.0474  0.0383  -0.0370 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.5112 0.5326 0.5639 0.0484  0.0413  -0.0352 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.5217 0.5251 0.5634 0.0506  0.0378  -0.0408 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.2254 0.2068 0.2482 0.0427  0.0178  -0.0353 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.2275 0.1988 0.2429 0.0413  0.0134  -0.0368 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.2191 0.1868 0.2198 0.0381  0.0141  -0.0393 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.2143 0.1835 0.2086 0.0383  0.0193  -0.0422 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.2343 0.1973 0.2528 0.0454  0.0142  -0.0417 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.2108 0.1738 0.2064 0.0349  0.0086  -0.0378 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.2230 0.1815 0.2057 0.0318  0.0074  -0.0396 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.2418 0.1915 0.2221 0.0303  0.0017  -0.0407 87  SER   C C   
1715 O O   . SER   B 81  ? 0.2528 0.1998 0.2410 0.0316  -0.0007 -0.0398 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2091 0.1745 0.1903 0.0284  0.0062  -0.0352 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2089 0.1765 0.1965 0.0264  0.0014  -0.0309 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.2478 0.1923 0.2174 0.0273  -0.0010 -0.0422 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.2673 0.2041 0.2355 0.0252  -0.0070 -0.0428 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.2607 0.2026 0.2382 0.0228  -0.0114 -0.0372 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.2695 0.2064 0.2492 0.0211  -0.0159 -0.0368 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.3182 0.2490 0.2736 0.0222  -0.0098 -0.0453 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.4118 0.3492 0.3657 0.0193  -0.0116 -0.0413 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.5712 0.5106 0.5164 0.0196  -0.0072 -0.0423 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.6278 0.5632 0.5624 0.0170  -0.0098 -0.0430 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.5951 0.5399 0.5440 0.0221  -0.0014 -0.0422 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.2452 0.1966 0.2277 0.0222  -0.0098 -0.0330 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.2402 0.1971 0.2300 0.0196  -0.0126 -0.0281 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.2394 0.1987 0.2384 0.0208  -0.0123 -0.0252 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.2422 0.2028 0.2461 0.0181  -0.0153 -0.0218 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.2326 0.1975 0.2216 0.0183  -0.0108 -0.0256 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.2418 0.2041 0.2220 0.0171  -0.0120 -0.0275 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.2550 0.2140 0.2339 0.0144  -0.0170 -0.0274 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.2579 0.2212 0.2314 0.0181  -0.0085 -0.0288 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.2699 0.2262 0.2411 0.0131  -0.0192 -0.0286 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.2779 0.2382 0.2425 0.0164  -0.0103 -0.0297 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.2930 0.2497 0.2566 0.0140  -0.0160 -0.0295 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.3171 0.2706 0.2724 0.0123  -0.0190 -0.0298 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2331 0.1940 0.2349 0.0244  -0.0086 -0.0262 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2305 0.1942 0.2416 0.0256  -0.0089 -0.0229 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.2641 0.2250 0.2789 0.0305  -0.0062 -0.0260 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.2702 0.2319 0.2811 0.0328  -0.0017 -0.0298 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.1993 0.1730 0.2136 0.0245  -0.0070 -0.0190 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.1801 0.1581 0.1922 0.0202  -0.0083 -0.0161 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.1794 0.1605 0.1861 0.0193  -0.0063 -0.0171 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.1771 0.1555 0.1926 0.0169  -0.0115 -0.0124 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.1707 0.1556 0.1769 0.0160  -0.0072 -0.0149 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.1760 0.1587 0.1903 0.0132  -0.0118 -0.0105 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.1782 0.1644 0.1886 0.0131  -0.0095 -0.0118 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.1858 0.1758 0.1964 0.0099  -0.0097 -0.0103 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.2763 0.2352 0.2997 0.0321  -0.0085 -0.0239 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.2806 0.2391 0.3108 0.0374  -0.0055 -0.0263 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.2740 0.2434 0.3095 0.0383  -0.0022 -0.0237 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.2639 0.2399 0.2980 0.0346  -0.0032 -0.0196 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.2985 0.2518 0.3372 0.0381  -0.0105 -0.0233 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3025 0.2586 0.3402 0.0326  -0.0148 -0.0172 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.2742 0.2323 0.3023 0.0289  -0.0137 -0.0186 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.2703 0.2420 0.3131 0.0431  0.0016  -0.0261 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.2683 0.2509 0.3180 0.0437  0.0043  -0.0233 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.2609 0.2472 0.3177 0.0413  -0.0014 -0.0161 92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.2603 0.2408 0.3219 0.0418  -0.0061 -0.0141 92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.2652 0.2496 0.3242 0.0495  0.0090  -0.0270 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2431 0.2374 0.2984 0.0377  -0.0014 -0.0123 93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2341 0.2310 0.2927 0.0341  -0.0067 -0.0058 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2331 0.2396 0.2915 0.0312  -0.0054 -0.0028 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2322 0.2428 0.2871 0.0316  -0.0006 -0.0055 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2329 0.2239 0.2830 0.0297  -0.0101 -0.0046 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2084 0.2027 0.2489 0.0258  -0.0077 -0.0053 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2214 0.2099 0.2546 0.0234  -0.0090 -0.0070 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2245 0.2170 0.2523 0.0190  -0.0087 -0.0053 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.2437 0.2394 0.2665 0.0187  -0.0055 -0.0074 93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2095 0.2078 0.2286 0.0150  -0.0055 -0.0061 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2299 0.2260 0.2515 0.0219  -0.0021 -0.0107 93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2312 0.2405 0.2919 0.0277  -0.0099 0.0030  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2302 0.2471 0.2889 0.0240  -0.0093 0.0057  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.1971 0.2118 0.2447 0.0190  -0.0094 0.0059  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.1951 0.2051 0.2402 0.0166  -0.0128 0.0078  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2492 0.2698 0.3152 0.0222  -0.0144 0.0117  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.2935 0.3186 0.3730 0.0270  -0.0143 0.0120  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.3149 0.3488 0.3989 0.0274  -0.0113 0.0118  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.3236 0.3441 0.4121 0.0315  -0.0168 0.0120  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.3389 0.3783 0.4372 0.0319  -0.0107 0.0118  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.3386 0.3637 0.4414 0.0366  -0.0162 0.0117  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3567 0.3919 0.4649 0.0368  -0.0129 0.0116  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.3962 0.4373 0.5205 0.0419  -0.0120 0.0114  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1661 0.1840 0.2078 0.0177  -0.0056 0.0037  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1597 0.1764 0.1928 0.0135  -0.0054 0.0037  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1627 0.1844 0.1947 0.0092  -0.0064 0.0073  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1704 0.1974 0.2051 0.0096  -0.0049 0.0077  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1627 0.1786 0.1898 0.0145  -0.0013 -0.0005 95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1545 0.1701 0.1750 0.0107  -0.0011 -0.0006 95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1562 0.1688 0.1714 0.0120  0.0010  -0.0042 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1538 0.1620 0.1683 0.0146  0.0008  -0.0068 95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1332 0.1475 0.1443 0.0099  0.0025  -0.0045 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1525 0.1727 0.1806 0.0048  -0.0087 0.0098  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1484 0.1721 0.1736 0.0000  -0.0098 0.0128  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1444 0.1693 0.1627 -0.0025 -0.0061 0.0104  96  SER   C C   
1798 O O   . SER   B 90  ? 0.1438 0.1662 0.1597 -0.0010 -0.0038 0.0071  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1644 0.1853 0.1875 -0.0040 -0.0136 0.0167  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.1859 0.2029 0.2046 -0.0054 -0.0124 0.0149  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1400 0.1680 0.1553 -0.0064 -0.0062 0.0120  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1403 0.1687 0.1495 -0.0089 -0.0030 0.0098  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1509 0.1798 0.1607 -0.0054 0.0003  0.0064  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1615 0.1886 0.1673 -0.0058 0.0027  0.0038  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1493 0.1745 0.1535 -0.0116 -0.0019 0.0086  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.1771 0.2014 0.1785 -0.0162 -0.0046 0.0121  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2078 0.2326 0.2026 -0.0217 -0.0041 0.0129  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.1799 0.2021 0.1836 -0.0165 -0.0080 0.0150  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2123 0.2355 0.2046 -0.0254 -0.0071 0.0164  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2030 0.2246 0.2009 -0.0224 -0.0097 0.0181  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1407 0.1719 0.1559 -0.0019 0.0004  0.0064  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1365 0.1678 0.1511 0.0010  0.0036  0.0037  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1346 0.1703 0.1497 -0.0008 0.0049  0.0046  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1264 0.1662 0.1461 -0.0021 0.0030  0.0074  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1335 0.1642 0.1531 0.0057  0.0040  0.0025  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.1584 0.1881 0.1756 0.0084  0.0075  -0.0007 98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.1805 0.2052 0.1907 0.0079  0.0079  -0.0029 98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.1640 0.1926 0.1854 0.0128  0.0084  -0.0024 98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1354 0.1699 0.1461 -0.0011 0.0076  0.0026  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1399 0.1777 0.1503 -0.0034 0.0089  0.0035  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1452 0.1833 0.1555 -0.0009 0.0121  0.0019  99  MET   C C   
1822 O O   . MET   B 93  ? 0.1573 0.1908 0.1630 0.0008  0.0132  -0.0003 99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1575 0.1922 0.1615 -0.0069 0.0092  0.0027  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.1855 0.2197 0.1878 -0.0103 0.0070  0.0039  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.1965 0.2261 0.1916 -0.0135 0.0087  0.0015  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.1845 0.2098 0.1792 -0.0094 0.0103  -0.0014 99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1241 0.1677 0.1394 -0.0009 0.0134  0.0031  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1232 0.1676 0.1378 0.0009  0.0173  0.0016  100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1284 0.1733 0.1392 -0.0026 0.0190  0.0023  100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1185 0.1660 0.1308 -0.0062 0.0175  0.0043  100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1308 0.1814 0.1546 0.0035  0.0190  0.0018  100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1604 0.2099 0.1890 0.0077  0.0178  0.0008  100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1640 0.2195 0.2023 0.0109  0.0208  0.0002  100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.1822 0.2239 0.2031 0.0099  0.0183  -0.0023 100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1277 0.1696 0.1329 -0.0020 0.0220  0.0009  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1438 0.1854 0.1448 -0.0052 0.0238  0.0018  101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1463 0.1887 0.1451 -0.0041 0.0283  0.0008  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1479 0.1883 0.1453 -0.0006 0.0296  -0.0014 101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1543 0.1880 0.1472 -0.0066 0.0220  0.0013  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1370 0.1820 0.1350 -0.0074 0.0308  0.0023  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1521 0.1976 0.1462 -0.0075 0.0356  0.0016  102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.1801 0.2158 0.1619 -0.0087 0.0343  0.0015  102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.1886 0.2207 0.1670 -0.0119 0.0321  0.0033  102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1502 0.2034 0.1497 -0.0112 0.0389  0.0038  102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1543 0.2074 0.1479 -0.0122 0.0447  0.0030  102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1396 0.2031 0.1534 -0.0097 0.0392  0.0042  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.1826 0.2133 0.1583 -0.0059 0.0346  -0.0008 103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2000 0.2213 0.1647 -0.0068 0.0323  -0.0006 103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2041 0.2208 0.1621 -0.0041 0.0328  -0.0031 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2035 0.2232 0.1661 -0.0009 0.0342  -0.0056 103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2035 0.2123 0.1504 -0.0057 0.0312  -0.0024 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2103 0.2135 0.1489 -0.0040 0.0307  -0.0047 104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2047 0.2048 0.1464 -0.0007 0.0257  -0.0063 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2038 0.2019 0.1486 -0.0007 0.0213  -0.0049 104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.2295 0.2247 0.1543 -0.0074 0.0296  -0.0028 104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.2632 0.2519 0.1779 -0.0064 0.0286  -0.0051 104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.2940 0.2842 0.2038 -0.0062 0.0343  -0.0082 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.2815 0.2628 0.1914 -0.0055 0.0224  -0.0051 104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3135 0.2960 0.2136 -0.0057 0.0313  -0.0099 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3046 0.2819 0.2049 -0.0053 0.0237  -0.0079 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.1942 0.1935 0.1347 0.0018  0.0268  -0.0094 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.1955 0.1910 0.1372 0.0043  0.0222  -0.0110 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.2185 0.2103 0.1534 0.0057  0.0239  -0.0146 105 SER   C C   
1864 O O   . SER   B 99  ? 0.2310 0.2256 0.1648 0.0060  0.0297  -0.0166 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.2006 0.2015 0.1548 0.0065  0.0211  -0.0112 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.2378 0.2441 0.1980 0.0084  0.0251  -0.0129 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2198 0.2051 0.1501 0.0063  0.0191  -0.0155 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.2416 0.2220 0.1648 0.0074  0.0197  -0.0193 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.2463 0.2232 0.1728 0.0089  0.0136  -0.0201 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.2342 0.2123 0.1670 0.0088  0.0093  -0.0175 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.2843 0.2583 0.1914 0.0043  0.0211  -0.0197 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.3212 0.2894 0.2207 0.0013  0.0151  -0.0160 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.3604 0.3227 0.2434 -0.0025 0.0169  -0.0154 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.3947 0.3501 0.2661 -0.0034 0.0157  -0.0179 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.3602 0.3243 0.2408 -0.0051 0.0195  -0.0125 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.2638 0.2364 0.1866 0.0103  0.0135  -0.0238 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.2844 0.2532 0.2099 0.0110  0.0073  -0.0243 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.3018 0.2663 0.2222 0.0086  0.0008  -0.0216 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.3352 0.2941 0.2431 0.0062  -0.0001 -0.0211 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.2977 0.2604 0.2157 0.0119  0.0086  -0.0291 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.3004 0.2668 0.2183 0.0132  0.0167  -0.0314 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.2734 0.2436 0.1887 0.0108  0.0190  -0.0280 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2687 0.2359 0.1992 0.0091  -0.0033 -0.0195 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2534 0.2183 0.1837 0.0077  -0.0092 -0.0166 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2282 0.1988 0.1676 0.0079  -0.0083 -0.0137 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2252 0.1957 0.1699 0.0077  -0.0127 -0.0118 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.1994 0.1751 0.1415 0.0083  -0.0025 -0.0136 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.1911 0.1715 0.1404 0.0080  -0.0014 -0.0113 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.1823 0.1680 0.1435 0.0091  -0.0015 -0.0114 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.1829 0.1713 0.1495 0.0086  -0.0012 -0.0099 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2023 0.1857 0.1490 0.0070  0.0041  -0.0106 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2277 0.2059 0.1629 0.0047  0.0039  -0.0092 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2295 0.2025 0.1613 0.0038  -0.0012 -0.0075 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2539 0.2334 0.1839 0.0036  0.0087  -0.0096 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.1724 0.1588 0.1372 0.0104  -0.0021 -0.0132 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.1733 0.1643 0.1482 0.0107  -0.0021 -0.0129 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.1743 0.1656 0.1544 0.0101  -0.0052 -0.0119 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.1694 0.1568 0.1475 0.0101  -0.0092 -0.0118 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.1909 0.1811 0.1680 0.0117  -0.0029 -0.0146 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2174 0.2083 0.1925 0.0133  0.0013  -0.0162 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1601 0.1558 0.1468 0.0095  -0.0033 -0.0112 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1642 0.1609 0.1573 0.0092  -0.0050 -0.0109 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.1671 0.1631 0.1596 0.0089  -0.0041 -0.0100 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.1557 0.1532 0.1547 0.0088  -0.0041 -0.0102 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1578 0.1516 0.1429 0.0084  -0.0030 -0.0090 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1686 0.1609 0.1525 0.0076  -0.0022 -0.0079 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1673 0.1637 0.1560 0.0065  0.0013  -0.0084 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1562 0.1564 0.1452 0.0058  0.0038  -0.0086 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1744 0.1697 0.1669 0.0064  0.0013  -0.0087 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1828 0.1811 0.1786 0.0049  0.0046  -0.0098 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1716 0.1696 0.1623 0.0027  0.0069  -0.0087 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1843 0.1784 0.1706 0.0025  0.0059  -0.0073 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2167 0.2139 0.2195 0.0058  0.0045  -0.0114 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2485 0.2491 0.2586 0.0069  0.0039  -0.0127 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2321 0.2298 0.2353 0.0038  0.0082  -0.0129 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2761 0.2769 0.2954 0.0081  0.0043  -0.0148 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1479 0.1499 0.1389 0.0007  0.0094  -0.0090 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1454 0.1480 0.1331 -0.0020 0.0113  -0.0082 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1503 0.1518 0.1399 -0.0037 0.0128  -0.0101 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1334 0.1372 0.1259 -0.0040 0.0139  -0.0117 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1377 0.1456 0.1252 -0.0033 0.0123  -0.0071 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1669 0.1768 0.1526 -0.0066 0.0136  -0.0060 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1769 0.1846 0.1591 -0.0075 0.0138  -0.0045 114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1743 0.1900 0.1619 -0.0074 0.0136  -0.0045 114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1586 0.1557 0.1460 -0.0050 0.0131  -0.0103 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1718 0.1665 0.1603 -0.0065 0.0150  -0.0129 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1718 0.1652 0.1554 -0.0104 0.0160  -0.0124 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.1760 0.1680 0.1567 -0.0113 0.0149  -0.0100 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2040 0.1927 0.1958 -0.0040 0.0140  -0.0142 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.2737 0.2631 0.2720 -0.0003 0.0126  -0.0150 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3285 0.3117 0.3313 0.0021  0.0109  -0.0159 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.3614 0.3420 0.3665 0.0012  0.0142  -0.0194 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.3860 0.3689 0.3978 0.0023  0.0172  -0.0231 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.3830 0.3711 0.4007 0.0042  0.0168  -0.0233 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.3869 0.3667 0.3994 0.0012  0.0209  -0.0269 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1651 0.1585 0.1475 -0.0133 0.0181  -0.0147 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1799 0.1709 0.1574 -0.0175 0.0185  -0.0147 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.1881 0.1722 0.1657 -0.0177 0.0204  -0.0187 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.1924 0.1748 0.1750 -0.0141 0.0213  -0.0209 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1850 0.1811 0.1597 -0.0213 0.0188  -0.0140 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1799 0.1767 0.1540 -0.0224 0.0215  -0.0175 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.1973 0.1775 0.1700 -0.0218 0.0211  -0.0198 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2201 0.1929 0.1924 -0.0220 0.0234  -0.0244 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2289 0.2033 0.2029 -0.0215 0.0272  -0.0288 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.2463 0.2155 0.2228 -0.0201 0.0299  -0.0332 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.2578 0.2260 0.2231 -0.0275 0.0232  -0.0250 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.2963 0.2690 0.2557 -0.0326 0.0238  -0.0251 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.3835 0.3514 0.3361 -0.0384 0.0229  -0.0256 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4062 0.3775 0.3574 -0.0415 0.0200  -0.0216 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4086 0.3687 0.3573 -0.0402 0.0255  -0.0308 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2154 0.1968 0.1883 -0.0227 0.0275  -0.0276 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2134 0.1966 0.1868 -0.0232 0.0314  -0.0312 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2106 0.1976 0.1931 -0.0182 0.0320  -0.0315 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2220 0.2102 0.2068 -0.0181 0.0360  -0.0350 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2162 0.2038 0.1824 -0.0284 0.0313  -0.0298 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2283 0.2129 0.1859 -0.0339 0.0300  -0.0293 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2321 0.2202 0.1883 -0.0357 0.0257  -0.0243 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2418 0.2201 0.1926 -0.0378 0.0323  -0.0334 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2458 0.2302 0.1949 -0.0409 0.0250  -0.0251 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2618 0.2396 0.2065 -0.0426 0.0288  -0.0305 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.1933 0.1821 0.1804 -0.0145 0.0284  -0.0279 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.1736 0.1658 0.1688 -0.0103 0.0279  -0.0276 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1601 0.1569 0.1553 -0.0093 0.0243  -0.0232 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1774 0.1740 0.1681 -0.0103 0.0219  -0.0202 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1448 0.1454 0.1452 -0.0072 0.0241  -0.0231 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1479 0.1519 0.1487 -0.0059 0.0208  -0.0196 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1546 0.1621 0.1500 -0.0092 0.0207  -0.0176 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1710 0.1806 0.1652 -0.0120 0.0230  -0.0187 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1505 0.1570 0.1588 -0.0031 0.0202  -0.0202 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1589 0.1678 0.1665 -0.0021 0.0169  -0.0173 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.1481 0.1512 0.1630 0.0005  0.0188  -0.0215 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1382 0.1464 0.1310 -0.0089 0.0182  -0.0146 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1317 0.1435 0.1215 -0.0114 0.0173  -0.0121 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1317 0.1463 0.1244 -0.0094 0.0155  -0.0105 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1144 0.1316 0.1065 -0.0113 0.0151  -0.0092 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1299 0.1416 0.1167 -0.0124 0.0161  -0.0101 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1372 0.1534 0.1236 -0.0140 0.0146  -0.0072 121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1400 0.1483 0.1232 -0.0153 0.0176  -0.0116 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1379 0.1514 0.1330 -0.0058 0.0140  -0.0103 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1370 0.1519 0.1342 -0.0038 0.0122  -0.0092 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1267 0.1390 0.1246 -0.0005 0.0105  -0.0095 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1322 0.1417 0.1299 0.0003  0.0103  -0.0103 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1202 0.1328 0.1187 0.0012  0.0088  -0.0089 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1251 0.1345 0.1223 0.0038  0.0068  -0.0093 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1195 0.1290 0.1136 0.0049  0.0067  -0.0086 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1224 0.1343 0.1181 0.0048  0.0071  -0.0080 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1490 0.1575 0.1502 0.0049  0.0046  -0.0103 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1599 0.1708 0.1636 0.0040  0.0046  -0.0099 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.1657 0.1741 0.1714 0.0047  0.0047  -0.0114 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.1828 0.1927 0.1904 0.0047  0.0021  -0.0106 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1074 0.1137 0.0970 0.0061  0.0061  -0.0087 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1083 0.1144 0.0946 0.0073  0.0070  -0.0089 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1125 0.1181 0.1010 0.0088  0.0057  -0.0100 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1231 0.1261 0.1125 0.0092  0.0030  -0.0107 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1231 0.1248 0.1024 0.0077  0.0066  -0.0091 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1132 0.1146 0.0886 0.0088  0.0085  -0.0101 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1362 0.1376 0.1131 0.0059  0.0078  -0.0076 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1124 0.1204 0.1027 0.0097  0.0072  -0.0099 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1211 0.1278 0.1139 0.0112  0.0058  -0.0108 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1392 0.1450 0.1306 0.0134  0.0077  -0.0123 125 SER   C C   
2001 O O   . SER   B 119 ? 0.1522 0.1542 0.1431 0.0150  0.0064  -0.0141 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1366 0.1466 0.1353 0.0099  0.0051  -0.0090 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1553 0.1635 0.1569 0.0111  0.0035  -0.0093 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1439 0.1533 0.1353 0.0135  0.0109  -0.0118 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.1599 0.1695 0.1510 0.0158  0.0140  -0.0137 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.1662 0.1772 0.1522 0.0148  0.0176  -0.0138 126 THR   C C   
2007 O O   . THR   B 120 ? 0.1634 0.1756 0.1475 0.0124  0.0174  -0.0119 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.1725 0.1872 0.1732 0.0173  0.0147  -0.0126 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.1680 0.1890 0.1723 0.0154  0.0160  -0.0100 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.1874 0.2006 0.1928 0.0174  0.0108  -0.0114 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.1849 0.1959 0.1692 0.0165  0.0214  -0.0162 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2017 0.2149 0.1817 0.0151  0.0257  -0.0161 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2228 0.2373 0.2034 0.0174  0.0309  -0.0193 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2236 0.2356 0.2068 0.0204  0.0307  -0.0219 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.2396 0.2572 0.2173 0.0159  0.0358  -0.0193 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.2596 0.2790 0.2376 0.0179  0.0421  -0.0229 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.2740 0.3024 0.2583 0.0166  0.0474  -0.0215 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.2710 0.3058 0.2648 0.0157  0.0454  -0.0180 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.2866 0.3154 0.2651 0.0160  0.0541  -0.0242 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.2917 0.3295 0.2758 0.0144  0.0604  -0.0233 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.2727 0.3145 0.2582 0.0100  0.0580  -0.0181 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.2718 0.3231 0.2696 0.0095  0.0594  -0.0159 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3233 0.3697 0.3243 0.0186  0.0638  -0.0250 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4008 0.4426 0.4003 0.0230  0.0674  -0.0309 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4363 0.4736 0.4240 0.0221  0.0729  -0.0348 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4067 0.4486 0.4171 0.0274  0.0640  -0.0316 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2565 0.2910 0.2299 0.0068  0.0541  -0.0161 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2387 0.2747 0.2115 0.0025  0.0519  -0.0117 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2088 0.2474 0.1909 0.0029  0.0461  -0.0090 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2065 0.2478 0.1906 -0.0005 0.0449  -0.0058 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.1925 0.2293 0.1791 0.0064  0.0425  -0.0103 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.1867 0.2248 0.1799 0.0063  0.0371  -0.0080 131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.1889 0.2185 0.1752 0.0071  0.0323  -0.0087 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2126 0.2364 0.1921 0.0088  0.0325  -0.0113 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.1871 0.2316 0.1936 0.0094  0.0368  -0.0082 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2039 0.2584 0.2210 0.0094  0.0412  -0.0075 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2111 0.2703 0.2413 0.0137  0.0405  -0.0083 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.1967 0.2563 0.2172 0.0049  0.0395  -0.0036 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1569 0.1857 0.1447 0.0055  0.0281  -0.0066 132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1534 0.1760 0.1376 0.0061  0.0239  -0.0071 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1556 0.1813 0.1476 0.0062  0.0211  -0.0058 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1428 0.1733 0.1392 0.0040  0.0211  -0.0038 132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.1730 0.1898 0.1492 0.0038  0.0220  -0.0061 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.1720 0.1911 0.1494 0.0004  0.0223  -0.0037 132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.1840 0.1959 0.1595 0.0049  0.0177  -0.0068 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1495 0.1725 0.1428 0.0082  0.0186  -0.0070 133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1408 0.1659 0.1399 0.0078  0.0159  -0.0056 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1343 0.1552 0.1304 0.0067  0.0132  -0.0058 133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1251 0.1413 0.1174 0.0079  0.0122  -0.0074 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1360 0.1588 0.1341 0.0042  0.0120  -0.0043 134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1300 0.1499 0.1266 0.0029  0.0106  -0.0048 134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1336 0.1551 0.1336 0.0018  0.0090  -0.0038 134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1343 0.1592 0.1364 0.0000  0.0086  -0.0019 134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1222 0.1418 0.1164 0.0002  0.0114  -0.0045 134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1226 0.1408 0.1131 0.0002  0.0128  -0.0044 134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1256 0.1389 0.1125 0.0013  0.0122  -0.0054 134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1259 0.1476 0.1169 -0.0014 0.0144  -0.0030 134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1259 0.1370 0.1082 0.0006  0.0131  -0.0048 134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1318 0.1519 0.1188 -0.0021 0.0159  -0.0026 134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1310 0.1454 0.1131 -0.0012 0.0152  -0.0034 134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1208 0.1397 0.1211 0.0023  0.0078  -0.0048 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1167 0.1363 0.1191 0.0005  0.0065  -0.0038 135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1302 0.1506 0.1307 -0.0030 0.0078  -0.0039 135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1247 0.1434 0.1246 -0.0029 0.0089  -0.0058 135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1224 0.1391 0.1261 0.0018  0.0052  -0.0051 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1247 0.1473 0.1244 -0.0060 0.0075  -0.0020 136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1373 0.1600 0.1336 -0.0099 0.0090  -0.0025 136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1338 0.1554 0.1301 -0.0114 0.0100  -0.0037 136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1395 0.1612 0.1376 -0.0115 0.0085  -0.0024 136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1600 0.1850 0.1546 -0.0134 0.0076  0.0003  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2184 0.2427 0.2076 -0.0179 0.0091  -0.0006 136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2053 0.2281 0.1929 -0.0178 0.0111  -0.0028 136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2448 0.2692 0.2307 -0.0219 0.0083  0.0008  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1273 0.1480 0.1220 -0.0129 0.0128  -0.0062 137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1297 0.1505 0.1251 -0.0149 0.0150  -0.0078 137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1381 0.1587 0.1280 -0.0196 0.0180  -0.0090 137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1488 0.1697 0.1385 -0.0219 0.0209  -0.0107 137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1249 0.1451 0.1258 -0.0118 0.0162  -0.0105 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1310 0.1506 0.1355 -0.0080 0.0129  -0.0095 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1119 0.1302 0.1126 -0.0106 0.0180  -0.0130 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1345 0.1544 0.1197 -0.0215 0.0174  -0.0084 138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1393 0.1578 0.1178 -0.0263 0.0200  -0.0100 138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.1470 0.1660 0.1199 -0.0316 0.0201  -0.0084 138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.1647 0.1821 0.1317 -0.0357 0.0237  -0.0110 138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1296 0.1472 0.1046 -0.0276 0.0183  -0.0091 138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1133 0.1293 0.0918 -0.0236 0.0189  -0.0108 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1256 0.1412 0.1008 -0.0258 0.0172  -0.0093 138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1401 0.1596 0.1182 -0.0247 0.0136  -0.0053 138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1632 0.1843 0.1414 -0.0257 0.0118  -0.0033 138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1412 0.1598 0.1155 -0.0285 0.0126  -0.0046 138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1550 0.1803 0.1379 -0.0240 0.0093  -0.0001 138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1433 0.1638 0.1172 -0.0318 0.0164  -0.0043 139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.1619 0.1823 0.1301 -0.0372 0.0157  -0.0019 139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.1814 0.2021 0.1512 -0.0380 0.0190  -0.0034 139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.1956 0.2158 0.1595 -0.0433 0.0194  -0.0016 139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.1806 0.2019 0.1503 -0.0371 0.0097  0.0036  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2385 0.2605 0.2167 -0.0317 0.0079  0.0045  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2550 0.2774 0.2386 -0.0268 0.0094  0.0018  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2368 0.2582 0.2158 -0.0327 0.0047  0.0081  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.1729 0.1947 0.1509 -0.0332 0.0211  -0.0062 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.1779 0.2011 0.1596 -0.0340 0.0241  -0.0075 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.1787 0.2022 0.1581 -0.0367 0.0306  -0.0121 140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.1802 0.2047 0.1667 -0.0331 0.0337  -0.0160 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.1798 0.2041 0.1716 -0.0282 0.0225  -0.0081 140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2049 0.2281 0.1985 -0.0251 0.0168  -0.0046 140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2160 0.2391 0.2170 -0.0197 0.0154  -0.0059 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2115 0.2340 0.2027 -0.0283 0.0139  -0.0004 140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.1782 0.2005 0.1475 -0.0430 0.0327  -0.0119 141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.1877 0.2094 0.1528 -0.0461 0.0397  -0.0170 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2080 0.2330 0.1803 -0.0459 0.0455  -0.0202 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2115 0.2369 0.1861 -0.0453 0.0516  -0.0257 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.1917 0.2106 0.1422 -0.0539 0.0404  -0.0159 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2030 0.2195 0.1469 -0.0552 0.0339  -0.0118 141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2247 0.2380 0.1536 -0.0635 0.0344  -0.0111 141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2158 0.2313 0.1640 -0.0503 0.0328  -0.0141 141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2161 0.2437 0.1930 -0.0463 0.0435  -0.0170 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2251 0.2568 0.2101 -0.0466 0.0484  -0.0192 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2325 0.2670 0.2321 -0.0396 0.0492  -0.0227 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2260 0.2647 0.2342 -0.0396 0.0540  -0.0255 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2267 0.2594 0.2121 -0.0494 0.0451  -0.0141 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2251 0.2561 0.2145 -0.0449 0.0370  -0.0099 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2378 0.2652 0.2205 -0.0456 0.0310  -0.0054 142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2150 0.2476 0.2162 -0.0392 0.0341  -0.0102 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2364 0.2631 0.2261 -0.0404 0.0255  -0.0033 142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2250 0.2544 0.2249 -0.0368 0.0272  -0.0062 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2184 0.2549 0.2315 -0.0363 0.0366  -0.0133 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2295 0.2587 0.2376 -0.0318 0.0231  -0.0057 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2268 0.2632 0.2481 -0.0315 0.0316  -0.0122 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2305 0.2629 0.2484 -0.0295 0.0251  -0.0087 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2357 0.2680 0.2382 -0.0340 0.0444  -0.0222 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2512 0.2851 0.2661 -0.0278 0.0440  -0.0248 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.2982 0.3331 0.3175 -0.0272 0.0509  -0.0306 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.2925 0.3303 0.3245 -0.0232 0.0519  -0.0329 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2358 0.2660 0.2498 -0.0232 0.0383  -0.0232 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2402 0.2696 0.2541 -0.0214 0.0317  -0.0187 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2452 0.2713 0.2571 -0.0176 0.0278  -0.0178 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2390 0.2711 0.2632 -0.0192 0.0301  -0.0184 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3379 0.3701 0.3469 -0.0311 0.0552  -0.0330 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.3883 0.4199 0.3992 -0.0310 0.0623  -0.0393 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4312 0.4669 0.4428 -0.0355 0.0706  -0.0426 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4394 0.4742 0.4507 -0.0362 0.0775  -0.0484 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4287 0.4542 0.4263 -0.0337 0.0628  -0.0405 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.4890 0.5105 0.4858 -0.0298 0.0564  -0.0383 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.4943 0.5161 0.5018 -0.0239 0.0540  -0.0386 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5342 0.5522 0.5196 -0.0330 0.0537  -0.0362 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4559 0.4956 0.4678 -0.0390 0.0703  -0.0393 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.4838 0.5279 0.4962 -0.0441 0.0787  -0.0421 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.4957 0.5467 0.5219 -0.0431 0.0781  -0.0402 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5042 0.5599 0.5319 -0.0478 0.0846  -0.0415 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5295 0.5703 0.5232 -0.0527 0.0803  -0.0400 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6064 0.6460 0.5943 -0.0551 0.0723  -0.0323 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7196 0.7540 0.6885 -0.0622 0.0705  -0.0291 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.7333 0.7678 0.6963 -0.0676 0.0687  -0.0243 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.7534 0.7832 0.7136 -0.0626 0.0702  -0.0310 145 GLU   C OE2 
2155 N N1  . A1BSF C .   ? 0.1341 0.1363 0.1588 -0.0085 0.0155  0.0081  201 A1BSF A N1  
2156 C C4  . A1BSF C .   ? 0.1706 0.1717 0.1564 0.0102  0.0296  0.0263  201 A1BSF A C4  
2157 C C5  . A1BSF C .   ? 0.1738 0.1744 0.1648 0.0094  0.0338  0.0301  201 A1BSF A C5  
2158 C C6  . A1BSF C .   ? 0.1739 0.1727 0.1699 0.0068  0.0324  0.0299  201 A1BSF A C6  
2159 C C7  . A1BSF C .   ? 0.1740 0.1722 0.1696 0.0052  0.0270  0.0261  201 A1BSF A C7  
2160 C C8  . A1BSF C .   ? 0.1659 0.1620 0.1666 0.0030  0.0261  0.0262  201 A1BSF A C8  
2161 C C10 . A1BSF C .   ? 0.1567 0.1491 0.1685 -0.0010 0.0240  0.0248  201 A1BSF A C10 
2162 C C13 . A1BSF C .   ? 0.1460 0.1442 0.1675 -0.0064 0.0192  0.0153  201 A1BSF A C13 
2163 C C15 . A1BSF C .   ? 0.1474 0.1471 0.1711 -0.0063 0.0228  0.0180  201 A1BSF A C15 
2164 O O1  . A1BSF C .   ? 0.1521 0.1518 0.1875 -0.0108 0.0194  0.0104  201 A1BSF A O1  
2165 C C14 . A1BSF C .   ? 0.1469 0.1471 0.1748 -0.0089 0.0180  0.0110  201 A1BSF A C14 
2166 C C12 . A1BSF C .   ? 0.1497 0.1434 0.1697 -0.0049 0.0194  0.0180  201 A1BSF A C12 
2167 C C11 . A1BSF C .   ? 0.1565 0.1481 0.1682 -0.0015 0.0199  0.0218  201 A1BSF A C11 
2168 N N   . A1BSF C .   ? 0.1516 0.1488 0.1669 -0.0029 0.0240  0.0219  201 A1BSF A N   
2169 C C9  . A1BSF C .   ? 0.1554 0.1548 0.1662 -0.0012 0.0249  0.0226  201 A1BSF A C9  
2170 O O   . A1BSF C .   ? 0.1499 0.1535 0.1639 -0.0024 0.0246  0.0202  201 A1BSF A O   
2171 C C2  . A1BSF C .   ? 0.1680 0.1668 0.1586 0.0059  0.0232  0.0227  201 A1BSF A C2  
2172 C C1  . A1BSF C .   ? 0.1693 0.1671 0.1598 0.0045  0.0184  0.0193  201 A1BSF A C1  
2173 C C   . A1BSF C .   ? 0.1699 0.1679 0.1564 0.0052  0.0156  0.0163  201 A1BSF A C   
2174 C C3  . A1BSF C .   ? 0.1653 0.1654 0.1512 0.0083  0.0245  0.0228  201 A1BSF A C3  
2176 N N1  . A1BSF E .   ? 0.1800 0.1804 0.1824 0.0168  0.0027  -0.0134 201 A1BSF C N1  
2177 C C4  . A1BSF E .   ? 0.2233 0.2180 0.1729 0.0149  0.0282  -0.0239 201 A1BSF C C4  
2178 C C5  . A1BSF E .   ? 0.2257 0.2177 0.1756 0.0177  0.0300  -0.0280 201 A1BSF C C5  
2179 C C6  . A1BSF E .   ? 0.2204 0.2092 0.1748 0.0195  0.0254  -0.0289 201 A1BSF C C6  
2180 C C7  . A1BSF E .   ? 0.2119 0.2011 0.1706 0.0185  0.0197  -0.0256 201 A1BSF C C7  
2181 C C8  . A1BSF E .   ? 0.2050 0.1907 0.1679 0.0198  0.0152  -0.0265 201 A1BSF C C8  
2182 C C10 . A1BSF E .   ? 0.1854 0.1657 0.1589 0.0214  0.0071  -0.0268 201 A1BSF C C10 
2183 C C13 . A1BSF E .   ? 0.1710 0.1631 0.1625 0.0196  0.0046  -0.0192 201 A1BSF C C13 
2184 C C15 . A1BSF E .   ? 0.1695 0.1621 0.1596 0.0221  0.0091  -0.0217 201 A1BSF C C15 
2185 O O1  . A1BSF E .   ? 0.1707 0.1643 0.1753 0.0213  0.0026  -0.0169 201 A1BSF C O1  
2186 C C14 . A1BSF E .   ? 0.1774 0.1731 0.1777 0.0194  0.0033  -0.0164 201 A1BSF C C14 
2187 C C12 . A1BSF E .   ? 0.1758 0.1606 0.1628 0.0193  0.0011  -0.0214 201 A1BSF C C12 
2188 C C11 . A1BSF E .   ? 0.1759 0.1560 0.1526 0.0192  0.0018  -0.0242 201 A1BSF C C11 
2189 N N   . A1BSF E .   ? 0.1813 0.1696 0.1608 0.0216  0.0105  -0.0243 201 A1BSF C N   
2190 C C9  . A1BSF E .   ? 0.1902 0.1815 0.1658 0.0210  0.0144  -0.0242 201 A1BSF C C9  
2191 O O   . A1BSF E .   ? 0.1774 0.1754 0.1588 0.0211  0.0170  -0.0222 201 A1BSF C O   
2192 C C2  . A1BSF E .   ? 0.2145 0.2068 0.1731 0.0160  0.0185  -0.0220 201 A1BSF C C2  
2193 C C1  . A1BSF E .   ? 0.2158 0.2083 0.1788 0.0149  0.0133  -0.0192 201 A1BSF C C1  
2194 C C   . A1BSF E .   ? 0.2145 0.2092 0.1770 0.0125  0.0126  -0.0161 201 A1BSF C C   
2195 C C3  . A1BSF E .   ? 0.2194 0.2140 0.1735 0.0143  0.0225  -0.0211 201 A1BSF C C3  
# 
