data_7I5F
# 
_entry.id   7I5F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I5F         pdb_00007i5f 10.2210/pdb7i5f/pdb 
WWPDB D_1001408338 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I5F 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                       15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '5-chloro-2-methoxyphenyl (3S)-3-carbamoylpiperidine-1-carboxylate' 312.749   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                          65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                78.133    4   ?         ? ? ? 
5 water       nat water                                                               18.015    329 ?         ? ? ? 
# 
_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 '5-chloro-2-methoxyphenyl (3S)-3-carbamoylpiperidine-1-carboxylate' A1B3W 
3 'ZINC ION'                                                          ZN    
4 'DIMETHYL SULFOXIDE'                                                DMS   
5 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 
A1B3W non-polymer         . '5-chloro-2-methoxyphenyl (3S)-3-carbamoylpiperidine-1-carboxylate' ? 'C14 H17 Cl N2 O4' 312.749 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                ? 'C2 H6 O S'        78.133  
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        A1B3W 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3W 
_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 A1B3W 1   201 201 A1B3W LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 4 DMS   1   204 8   DMS   DMS A . 
G 2 A1B3W 1   201 201 A1B3W LIG C . 
H 4 DMS   1   202 7   DMS   DMS C . 
I 3 ZN    1   203 1   ZN    ZN  C . 
J 4 DMS   1   204 6   DMS   DMS C . 
K 5 HOH   1   301 61  HOH   HOH A . 
K 5 HOH   2   302 6   HOH   HOH A . 
K 5 HOH   3   303 95  HOH   HOH A . 
K 5 HOH   4   304 164 HOH   HOH A . 
K 5 HOH   5   305 25  HOH   HOH A . 
K 5 HOH   6   306 84  HOH   HOH A . 
K 5 HOH   7   307 251 HOH   HOH A . 
K 5 HOH   8   308 64  HOH   HOH A . 
K 5 HOH   9   309 176 HOH   HOH A . 
K 5 HOH   10  310 116 HOH   HOH A . 
K 5 HOH   11  311 260 HOH   HOH A . 
K 5 HOH   12  312 190 HOH   HOH A . 
K 5 HOH   13  313 59  HOH   HOH A . 
K 5 HOH   14  314 93  HOH   HOH A . 
K 5 HOH   15  315 5   HOH   HOH A . 
K 5 HOH   16  316 34  HOH   HOH A . 
K 5 HOH   17  317 245 HOH   HOH A . 
K 5 HOH   18  318 66  HOH   HOH A . 
K 5 HOH   19  319 60  HOH   HOH A . 
K 5 HOH   20  320 14  HOH   HOH A . 
K 5 HOH   21  321 13  HOH   HOH A . 
K 5 HOH   22  322 134 HOH   HOH A . 
K 5 HOH   23  323 62  HOH   HOH A . 
K 5 HOH   24  324 103 HOH   HOH A . 
K 5 HOH   25  325 102 HOH   HOH A . 
K 5 HOH   26  326 56  HOH   HOH A . 
K 5 HOH   27  327 48  HOH   HOH A . 
K 5 HOH   28  328 140 HOH   HOH A . 
K 5 HOH   29  329 241 HOH   HOH A . 
K 5 HOH   30  330 24  HOH   HOH A . 
K 5 HOH   31  331 109 HOH   HOH A . 
K 5 HOH   32  332 22  HOH   HOH A . 
K 5 HOH   33  333 7   HOH   HOH A . 
K 5 HOH   34  334 22  HOH   HOH A . 
K 5 HOH   35  335 33  HOH   HOH A . 
K 5 HOH   36  336 49  HOH   HOH A . 
K 5 HOH   37  337 56  HOH   HOH A . 
K 5 HOH   38  338 63  HOH   HOH A . 
K 5 HOH   39  339 70  HOH   HOH A . 
K 5 HOH   40  340 71  HOH   HOH A . 
K 5 HOH   41  341 19  HOH   HOH A . 
K 5 HOH   42  342 85  HOH   HOH A . 
K 5 HOH   43  343 72  HOH   HOH A . 
K 5 HOH   44  344 17  HOH   HOH A . 
K 5 HOH   45  345 23  HOH   HOH A . 
K 5 HOH   46  346 125 HOH   HOH A . 
K 5 HOH   47  347 128 HOH   HOH A . 
K 5 HOH   48  348 53  HOH   HOH A . 
K 5 HOH   49  349 261 HOH   HOH A . 
K 5 HOH   50  350 66  HOH   HOH A . 
K 5 HOH   51  351 42  HOH   HOH A . 
K 5 HOH   52  352 234 HOH   HOH A . 
K 5 HOH   53  353 88  HOH   HOH A . 
K 5 HOH   54  354 171 HOH   HOH A . 
K 5 HOH   55  355 45  HOH   HOH A . 
K 5 HOH   56  356 18  HOH   HOH A . 
K 5 HOH   57  357 10  HOH   HOH A . 
K 5 HOH   58  358 27  HOH   HOH A . 
K 5 HOH   59  359 14  HOH   HOH A . 
K 5 HOH   60  360 119 HOH   HOH A . 
K 5 HOH   61  361 115 HOH   HOH A . 
K 5 HOH   62  362 53  HOH   HOH A . 
K 5 HOH   63  363 30  HOH   HOH A . 
K 5 HOH   64  364 153 HOH   HOH A . 
K 5 HOH   65  365 38  HOH   HOH A . 
K 5 HOH   66  366 99  HOH   HOH A . 
K 5 HOH   67  367 26  HOH   HOH A . 
K 5 HOH   68  368 91  HOH   HOH A . 
K 5 HOH   69  369 113 HOH   HOH A . 
K 5 HOH   70  370 23  HOH   HOH A . 
K 5 HOH   71  371 149 HOH   HOH A . 
K 5 HOH   72  372 10  HOH   HOH A . 
K 5 HOH   73  373 29  HOH   HOH A . 
K 5 HOH   74  374 237 HOH   HOH A . 
K 5 HOH   75  375 115 HOH   HOH A . 
K 5 HOH   76  376 6   HOH   HOH A . 
K 5 HOH   77  377 19  HOH   HOH A . 
K 5 HOH   78  378 76  HOH   HOH A . 
K 5 HOH   79  379 244 HOH   HOH A . 
K 5 HOH   80  380 26  HOH   HOH A . 
K 5 HOH   81  381 150 HOH   HOH A . 
K 5 HOH   82  382 79  HOH   HOH A . 
K 5 HOH   83  383 75  HOH   HOH A . 
K 5 HOH   84  384 35  HOH   HOH A . 
K 5 HOH   85  385 107 HOH   HOH A . 
K 5 HOH   86  386 55  HOH   HOH A . 
K 5 HOH   87  387 235 HOH   HOH A . 
K 5 HOH   88  388 133 HOH   HOH A . 
K 5 HOH   89  389 119 HOH   HOH A . 
K 5 HOH   90  390 86  HOH   HOH A . 
K 5 HOH   91  391 73  HOH   HOH A . 
K 5 HOH   92  392 21  HOH   HOH A . 
K 5 HOH   93  393 112 HOH   HOH A . 
K 5 HOH   94  394 111 HOH   HOH A . 
K 5 HOH   95  395 197 HOH   HOH A . 
K 5 HOH   96  396 153 HOH   HOH A . 
K 5 HOH   97  397 85  HOH   HOH A . 
K 5 HOH   98  398 12  HOH   HOH A . 
K 5 HOH   99  399 101 HOH   HOH A . 
K 5 HOH   100 400 147 HOH   HOH A . 
K 5 HOH   101 401 32  HOH   HOH A . 
K 5 HOH   102 402 4   HOH   HOH A . 
K 5 HOH   103 403 92  HOH   HOH A . 
K 5 HOH   104 404 40  HOH   HOH A . 
K 5 HOH   105 405 228 HOH   HOH A . 
K 5 HOH   106 406 157 HOH   HOH A . 
K 5 HOH   107 407 240 HOH   HOH A . 
K 5 HOH   108 408 96  HOH   HOH A . 
K 5 HOH   109 409 47  HOH   HOH A . 
K 5 HOH   110 410 101 HOH   HOH A . 
K 5 HOH   111 411 152 HOH   HOH A . 
K 5 HOH   112 412 12  HOH   HOH A . 
K 5 HOH   113 413 35  HOH   HOH A . 
K 5 HOH   114 414 52  HOH   HOH A . 
K 5 HOH   115 415 16  HOH   HOH A . 
K 5 HOH   116 416 142 HOH   HOH A . 
K 5 HOH   117 417 246 HOH   HOH A . 
K 5 HOH   118 418 102 HOH   HOH A . 
K 5 HOH   119 419 36  HOH   HOH A . 
K 5 HOH   120 420 202 HOH   HOH A . 
K 5 HOH   121 421 90  HOH   HOH A . 
K 5 HOH   122 422 77  HOH   HOH A . 
K 5 HOH   123 423 151 HOH   HOH A . 
K 5 HOH   124 424 15  HOH   HOH A . 
K 5 HOH   125 425 106 HOH   HOH A . 
K 5 HOH   126 426 208 HOH   HOH A . 
K 5 HOH   127 427 209 HOH   HOH A . 
K 5 HOH   128 428 129 HOH   HOH A . 
K 5 HOH   129 429 100 HOH   HOH A . 
K 5 HOH   130 430 212 HOH   HOH A . 
K 5 HOH   131 431 99  HOH   HOH A . 
K 5 HOH   132 432 108 HOH   HOH A . 
K 5 HOH   133 433 157 HOH   HOH A . 
K 5 HOH   134 434 144 HOH   HOH A . 
K 5 HOH   135 435 177 HOH   HOH A . 
K 5 HOH   136 436 178 HOH   HOH A . 
K 5 HOH   137 437 253 HOH   HOH A . 
K 5 HOH   138 438 181 HOH   HOH A . 
K 5 HOH   139 439 126 HOH   HOH A . 
K 5 HOH   140 440 60  HOH   HOH A . 
K 5 HOH   141 441 136 HOH   HOH A . 
K 5 HOH   142 442 24  HOH   HOH A . 
K 5 HOH   143 443 172 HOH   HOH A . 
K 5 HOH   144 444 92  HOH   HOH A . 
K 5 HOH   145 445 146 HOH   HOH A . 
K 5 HOH   146 446 149 HOH   HOH A . 
K 5 HOH   147 447 138 HOH   HOH A . 
K 5 HOH   148 448 154 HOH   HOH A . 
K 5 HOH   149 449 72  HOH   HOH A . 
K 5 HOH   150 450 90  HOH   HOH A . 
K 5 HOH   151 451 59  HOH   HOH A . 
K 5 HOH   152 452 82  HOH   HOH A . 
K 5 HOH   153 453 250 HOH   HOH A . 
K 5 HOH   154 454 158 HOH   HOH A . 
K 5 HOH   155 455 221 HOH   HOH A . 
K 5 HOH   156 456 161 HOH   HOH A . 
K 5 HOH   157 457 187 HOH   HOH A . 
K 5 HOH   158 458 154 HOH   HOH A . 
K 5 HOH   159 459 206 HOH   HOH A . 
K 5 HOH   160 460 264 HOH   HOH A . 
K 5 HOH   161 461 156 HOH   HOH A . 
K 5 HOH   162 462 262 HOH   HOH A . 
L 5 HOH   1   301 192 HOH   HOH C . 
L 5 HOH   2   302 34  HOH   HOH C . 
L 5 HOH   3   303 120 HOH   HOH C . 
L 5 HOH   4   304 128 HOH   HOH C . 
L 5 HOH   5   305 91  HOH   HOH C . 
L 5 HOH   6   306 89  HOH   HOH C . 
L 5 HOH   7   307 247 HOH   HOH C . 
L 5 HOH   8   308 174 HOH   HOH C . 
L 5 HOH   9   309 103 HOH   HOH C . 
L 5 HOH   10  310 137 HOH   HOH C . 
L 5 HOH   11  311 123 HOH   HOH C . 
L 5 HOH   12  312 8   HOH   HOH C . 
L 5 HOH   13  313 121 HOH   HOH C . 
L 5 HOH   14  314 28  HOH   HOH C . 
L 5 HOH   15  315 64  HOH   HOH C . 
L 5 HOH   16  316 97  HOH   HOH C . 
L 5 HOH   17  317 33  HOH   HOH C . 
L 5 HOH   18  318 51  HOH   HOH C . 
L 5 HOH   19  319 233 HOH   HOH C . 
L 5 HOH   20  320 159 HOH   HOH C . 
L 5 HOH   21  321 43  HOH   HOH C . 
L 5 HOH   22  322 32  HOH   HOH C . 
L 5 HOH   23  323 69  HOH   HOH C . 
L 5 HOH   24  324 236 HOH   HOH C . 
L 5 HOH   25  325 155 HOH   HOH C . 
L 5 HOH   26  326 252 HOH   HOH C . 
L 5 HOH   27  327 2   HOH   HOH C . 
L 5 HOH   28  328 138 HOH   HOH C . 
L 5 HOH   29  329 135 HOH   HOH C . 
L 5 HOH   30  330 210 HOH   HOH C . 
L 5 HOH   31  331 130 HOH   HOH C . 
L 5 HOH   32  332 256 HOH   HOH C . 
L 5 HOH   33  333 30  HOH   HOH C . 
L 5 HOH   34  334 50  HOH   HOH C . 
L 5 HOH   35  335 195 HOH   HOH C . 
L 5 HOH   36  336 148 HOH   HOH C . 
L 5 HOH   37  337 254 HOH   HOH C . 
L 5 HOH   38  338 124 HOH   HOH C . 
L 5 HOH   39  339 80  HOH   HOH C . 
L 5 HOH   40  340 97  HOH   HOH C . 
L 5 HOH   41  341 54  HOH   HOH C . 
L 5 HOH   42  342 39  HOH   HOH C . 
L 5 HOH   43  343 20  HOH   HOH C . 
L 5 HOH   44  344 126 HOH   HOH C . 
L 5 HOH   45  345 162 HOH   HOH C . 
L 5 HOH   46  346 11  HOH   HOH C . 
L 5 HOH   47  347 111 HOH   HOH C . 
L 5 HOH   48  348 67  HOH   HOH C . 
L 5 HOH   49  349 46  HOH   HOH C . 
L 5 HOH   50  350 65  HOH   HOH C . 
L 5 HOH   51  351 204 HOH   HOH C . 
L 5 HOH   52  352 78  HOH   HOH C . 
L 5 HOH   53  353 257 HOH   HOH C . 
L 5 HOH   54  354 144 HOH   HOH C . 
L 5 HOH   55  355 73  HOH   HOH C . 
L 5 HOH   56  356 152 HOH   HOH C . 
L 5 HOH   57  357 74  HOH   HOH C . 
L 5 HOH   58  358 98  HOH   HOH C . 
L 5 HOH   59  359 80  HOH   HOH C . 
L 5 HOH   60  360 259 HOH   HOH C . 
L 5 HOH   61  361 122 HOH   HOH C . 
L 5 HOH   62  362 15  HOH   HOH C . 
L 5 HOH   63  363 70  HOH   HOH C . 
L 5 HOH   64  364 29  HOH   HOH C . 
L 5 HOH   65  365 38  HOH   HOH C . 
L 5 HOH   66  366 37  HOH   HOH C . 
L 5 HOH   67  367 71  HOH   HOH C . 
L 5 HOH   68  368 13  HOH   HOH C . 
L 5 HOH   69  369 238 HOH   HOH C . 
L 5 HOH   70  370 98  HOH   HOH C . 
L 5 HOH   71  371 4   HOH   HOH C . 
L 5 HOH   72  372 62  HOH   HOH C . 
L 5 HOH   73  373 78  HOH   HOH C . 
L 5 HOH   74  374 79  HOH   HOH C . 
L 5 HOH   75  375 110 HOH   HOH C . 
L 5 HOH   76  376 9   HOH   HOH C . 
L 5 HOH   77  377 7   HOH   HOH C . 
L 5 HOH   78  378 31  HOH   HOH C . 
L 5 HOH   79  379 230 HOH   HOH C . 
L 5 HOH   80  380 83  HOH   HOH C . 
L 5 HOH   81  381 231 HOH   HOH C . 
L 5 HOH   82  382 146 HOH   HOH C . 
L 5 HOH   83  383 249 HOH   HOH C . 
L 5 HOH   84  384 127 HOH   HOH C . 
L 5 HOH   85  385 57  HOH   HOH C . 
L 5 HOH   86  386 48  HOH   HOH C . 
L 5 HOH   87  387 248 HOH   HOH C . 
L 5 HOH   88  388 117 HOH   HOH C . 
L 5 HOH   89  389 11  HOH   HOH C . 
L 5 HOH   90  390 108 HOH   HOH C . 
L 5 HOH   91  391 86  HOH   HOH C . 
L 5 HOH   92  392 83  HOH   HOH C . 
L 5 HOH   93  393 44  HOH   HOH C . 
L 5 HOH   94  394 1   HOH   HOH C . 
L 5 HOH   95  395 205 HOH   HOH C . 
L 5 HOH   96  396 89  HOH   HOH C . 
L 5 HOH   97  397 143 HOH   HOH C . 
L 5 HOH   98  398 54  HOH   HOH C . 
L 5 HOH   99  399 31  HOH   HOH C . 
L 5 HOH   100 400 124 HOH   HOH C . 
L 5 HOH   101 401 87  HOH   HOH C . 
L 5 HOH   102 402 232 HOH   HOH C . 
L 5 HOH   103 403 16  HOH   HOH C . 
L 5 HOH   104 404 239 HOH   HOH C . 
L 5 HOH   105 405 158 HOH   HOH C . 
L 5 HOH   106 406 242 HOH   HOH C . 
L 5 HOH   107 407 68  HOH   HOH C . 
L 5 HOH   108 408 50  HOH   HOH C . 
L 5 HOH   109 409 43  HOH   HOH C . 
L 5 HOH   110 410 141 HOH   HOH C . 
L 5 HOH   111 411 3   HOH   HOH C . 
L 5 HOH   112 412 258 HOH   HOH C . 
L 5 HOH   113 413 41  HOH   HOH C . 
L 5 HOH   114 414 40  HOH   HOH C . 
L 5 HOH   115 415 45  HOH   HOH C . 
L 5 HOH   116 416 194 HOH   HOH C . 
L 5 HOH   117 417 41  HOH   HOH C . 
L 5 HOH   118 418 37  HOH   HOH C . 
L 5 HOH   119 419 120 HOH   HOH C . 
L 5 HOH   120 420 140 HOH   HOH C . 
L 5 HOH   121 421 137 HOH   HOH C . 
L 5 HOH   122 422 47  HOH   HOH C . 
L 5 HOH   123 423 44  HOH   HOH C . 
L 5 HOH   124 424 118 HOH   HOH C . 
L 5 HOH   125 425 229 HOH   HOH C . 
L 5 HOH   126 426 105 HOH   HOH C . 
L 5 HOH   127 427 160 HOH   HOH C . 
L 5 HOH   128 428 117 HOH   HOH C . 
L 5 HOH   129 429 52  HOH   HOH C . 
L 5 HOH   130 430 105 HOH   HOH C . 
L 5 HOH   131 431 95  HOH   HOH C . 
L 5 HOH   132 432 145 HOH   HOH C . 
L 5 HOH   133 433 200 HOH   HOH C . 
L 5 HOH   134 434 150 HOH   HOH C . 
L 5 HOH   135 435 118 HOH   HOH C . 
L 5 HOH   136 436 94  HOH   HOH C . 
L 5 HOH   137 437 148 HOH   HOH C . 
L 5 HOH   138 438 17  HOH   HOH C . 
L 5 HOH   139 439 116 HOH   HOH C . 
L 5 HOH   140 440 87  HOH   HOH C . 
L 5 HOH   141 441 161 HOH   HOH C . 
L 5 HOH   142 442 27  HOH   HOH C . 
L 5 HOH   143 443 155 HOH   HOH C . 
L 5 HOH   144 444 185 HOH   HOH C . 
L 5 HOH   145 445 9   HOH   HOH C . 
L 5 HOH   146 446 143 HOH   HOH C . 
L 5 HOH   147 447 255 HOH   HOH C . 
L 5 HOH   148 448 131 HOH   HOH C . 
L 5 HOH   149 449 104 HOH   HOH C . 
L 5 HOH   150 450 263 HOH   HOH C . 
L 5 HOH   151 451 198 HOH   HOH C . 
L 5 HOH   152 452 142 HOH   HOH C . 
L 5 HOH   153 453 93  HOH   HOH C . 
L 5 HOH   154 454 166 HOH   HOH C . 
L 5 HOH   155 455 132 HOH   HOH C . 
L 5 HOH   156 456 74  HOH   HOH C . 
L 5 HOH   157 457 199 HOH   HOH C . 
L 5 HOH   158 458 82  HOH   HOH C . 
L 5 HOH   159 459 123 HOH   HOH C . 
L 5 HOH   160 460 203 HOH   HOH C . 
L 5 HOH   161 461 222 HOH   HOH C . 
L 5 HOH   162 462 188 HOH   HOH C . 
L 5 HOH   163 463 141 HOH   HOH C . 
L 5 HOH   164 464 207 HOH   HOH C . 
L 5 HOH   165 465 218 HOH   HOH C . 
L 5 HOH   166 466 151 HOH   HOH C . 
L 5 HOH   167 467 193 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           7I5F 
_cell.length_a           72.420 
_cell.length_b           61.290 
_cell.length_c           65.160 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.65 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5F 
_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          7I5F 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.27 
_exptl_crystal.density_percent_sol   45.87 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-16 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I5F 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.45 
_reflns.d_resolution_high            1.28 
_reflns.number_obs                   65749 
_reflns.percent_possible_obs         89.9 
_reflns.pdbx_Rmerge_I_obs            0.051 
_reflns.pdbx_netI_over_sigmaI        15.0 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     347116 
_reflns.pdbx_chi_squared             0.95 
_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                  1.28 
_reflns_shell.d_res_low                   1.31 
_reflns_shell.number_measured_all         6070 
_reflns_shell.number_unique_obs           2496 
_reflns_shell.Rmerge_I_obs                0.993 
_reflns_shell.pdbx_chi_squared            0.81 
_reflns_shell.pdbx_redundancy             2.4 
_reflns_shell.percent_possible_obs        46.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.228 
_reflns_shell.pdbx_Rpim_I_all             0.704 
_reflns_shell.pdbx_CC_half                0.371 
_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                                 7I5F 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     65743 
_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                             37.45 
_refine.ls_d_res_high                            1.280 
_refine.ls_percent_reflns_obs                    89.8 
_refine.ls_R_factor_obs                          0.1787 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1781 
_refine.ls_R_factor_R_free                       0.1912 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.940 
_refine.ls_number_reflns_R_free                  3247 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_refine.B_iso_mean                               20.26 
_refine.aniso_B[1][1]                            -2.45450 
_refine.aniso_B[2][2]                            1.14120 
_refine.aniso_B[3][3]                            1.31320 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.49020 
_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             0.050 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.050 
_refine.pdbx_overall_SU_R_Blow_DPI               0.053 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.052 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5F 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.number_atoms_solvent             329 
_refine_hist.number_atoms_total               2537 
_refine_hist.d_res_high                       1.280 
_refine_hist.d_res_low                        37.45 
# 
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                  0.012 ? 2.00  2264 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.11  ? 2.00  3078 '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 2264 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.07  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.35 ? ?     ?    '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  2176 '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                       1.28 
_refine_ls_shell.d_res_low                        1.30 
_refine_ls_shell.number_reflns_R_work             1250 
_refine_ls_shell.R_factor_R_work                  0.3042 
_refine_ls_shell.percent_reflns_obs               44.18 
_refine_ls_shell.R_factor_R_free                  0.3068 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.94 
_refine_ls_shell.number_reflns_R_free             65 
_refine_ls_shell.number_reflns_all                1315 
_refine_ls_shell.R_factor_all                     0.3043 
# 
_struct.entry_id                  7I5F 
_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-0036663-001 (A71EV2A-x4829)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5F 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 4 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
# 
_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 7I5F A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I5F 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,E,F,K 
2 1 B,G,H,I,J,L 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 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 ? ? ? ? ? ? ? 2.325 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 56  C ZN 203 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 58  C ZN 203 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 116 C ZN 203 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 I ZN . ZN ? ? C HIS 118 C ZN 203 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
# 
_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_555 109.9 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.2 ? 
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_555 107.6 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.5 ? 
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_555 113.6 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.1 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.9 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.9 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.4 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I5F 
_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 301 ? ? O C HOH 376 ? ? 1.19 
2 1 O C HOH 328 ? ? O C HOH 430 ? ? 1.43 
3 1 O C HOH 345 ? ? O C HOH 435 ? ? 1.59 
4 1 O A HOH 356 ? ? O A HOH 402 ? ? 1.73 
5 1 O A HOH 386 ? ? O A HOH 390 ? ? 1.79 
6 1 O A HOH 355 ? ? O A HOH 363 ? ? 1.98 
7 1 O C HOH 345 ? ? O C HOH 391 ? ? 1.98 
8 1 O A HOH 426 ? ? O C HOH 388 ? ? 2.18 
# 
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 19.6202 6.6888   18.2568 -0.0208 -0.0156 -0.0033 0.0010  0.0047  -0.0009 0.5438 0.9848 0.3756 
-0.2886 -0.2184 0.1384 -0.0101 0.0046 0.0603 0.0468 0.0228 0.0371  0.0384  0.0186  -0.0127 
'X-RAY DIFFRACTION' 2 ? refined 15.2069 -23.7946 14.0950 -0.0158 -0.0105 -0.0048 -0.0010 -0.0022 -0.0035 0.4044 0.7398 0.4112 
0.1355  0.0382  0.1144 -0.0118 0.0121 0.0258 0.0118 0.0236 -0.0381 -0.0231 -0.0042 -0.0119 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 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 
A1B3W N1   N  N N 1   
A1B3W C4   C  Y N 2   
A1B3W C5   C  Y N 3   
A1B3W C6   C  Y N 4   
A1B3W C7   C  N N 5   
A1B3W C8   C  N N 6   
A1B3W C10  C  N N 7   
A1B3W C13  C  N N 8   
A1B3W O3   O  N N 9   
A1B3W C12  C  N N 10  
A1B3W C11  C  N S 11  
A1B3W C9   C  N N 12  
A1B3W N    N  N N 13  
A1B3W O2   O  N N 14  
A1B3W O1   O  N N 15  
A1B3W C1   C  Y N 16  
A1B3W O    O  N N 17  
A1B3W C    C  N N 18  
A1B3W CL   CL N N 19  
A1B3W C3   C  Y N 20  
A1B3W C2   C  Y N 21  
A1B3W H13  H  N N 22  
A1B3W H14  H  N N 23  
A1B3W H6   H  N N 24  
A1B3W H7   H  N N 25  
A1B3W H8   H  N N 26  
A1B3W H11  H  N N 27  
A1B3W H12  H  N N 28  
A1B3W H15  H  N N 29  
A1B3W H16  H  N N 30  
A1B3W H    H  N N 31  
A1B3W H9   H  N N 32  
A1B3W H10  H  N N 33  
A1B3W H2   H  N N 34  
A1B3W H3   H  N N 35  
A1B3W H1   H  N N 36  
A1B3W H5   H  N N 37  
A1B3W H4   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1B3W C   O    sing N N 1   
A1B3W O   C1   sing N N 2   
A1B3W C1  C2   doub Y N 3   
A1B3W C2  C3   sing Y N 4   
A1B3W C3  C4   doub Y N 5   
A1B3W CL  C4   sing N N 6   
A1B3W C4  C5   sing Y N 7   
A1B3W C5  C6   doub Y N 8   
A1B3W C1  C6   sing Y N 9   
A1B3W C6  O1   sing N N 10  
A1B3W O1  C7   sing N N 11  
A1B3W O2  C7   doub N N 12  
A1B3W C7  N    sing N N 13  
A1B3W N   C8   sing N N 14  
A1B3W C8  C9   sing N N 15  
A1B3W C9  C10  sing N N 16  
A1B3W C10 C11  sing N N 17  
A1B3W C11 C12  sing N N 18  
A1B3W N1  C12  sing N N 19  
A1B3W C12 O3   doub N N 20  
A1B3W C13 C11  sing N N 21  
A1B3W N   C13  sing N N 22  
A1B3W N1  H13  sing N N 23  
A1B3W N1  H14  sing N N 24  
A1B3W C5  H6   sing N N 25  
A1B3W C8  H7   sing N N 26  
A1B3W C8  H8   sing N N 27  
A1B3W C10 H11  sing N N 28  
A1B3W C10 H12  sing N N 29  
A1B3W C13 H15  sing N N 30  
A1B3W C13 H16  sing N N 31  
A1B3W C11 H    sing N N 32  
A1B3W C9  H9   sing N N 33  
A1B3W C9  H10  sing N N 34  
A1B3W C   H2   sing N N 35  
A1B3W C   H3   sing N N 36  
A1B3W C   H1   sing N N 37  
A1B3W C3  H5   sing N N 38  
A1B3W C2  H4   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I5F 
_atom_sites.fract_transf_matrix[1][1]   0.013808 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000639 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016316 
_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]   0.015363 
_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  
CL 
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   ? 16.365 6.455   8.197  1.00 16.79  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.123 6.519   8.978  1.00 16.53  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.998 5.370   9.947  1.00 16.19  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.679 4.353   9.823  1.00 17.87  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.943 6.545   8.019  1.00 20.16  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.833 5.310   7.334  1.00 22.90  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.155 5.534   10.955 1.00 16.32  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.866 4.476   11.902 1.00 15.54  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.473 4.992   13.281 1.00 15.20  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.809 6.133   13.631 1.00 16.21  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.711 4.203   14.038 1.00 13.77  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.276 4.615   15.354 1.00 14.67  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.242 3.419   16.291 1.00 15.28  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.224 2.258   15.836 1.00 15.98  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.851 5.193   15.247 1.00 16.12  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.244 3.704   17.614 1.00 13.93  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 11.995 2.708   18.655 1.00 14.73  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.597 2.921   19.169 1.00 14.30  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.226 4.049   19.444 1.00 15.37  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 12.966 2.879   19.822 1.00 14.70  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.434 2.849   19.337 1.00 14.22  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.718 1.791   20.893 1.00 16.49  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.396 3.413   20.442 1.00 16.42  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.803  1.843   19.301 1.00 14.35  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.430  1.957   19.819 1.00 16.19  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.341  1.208   21.116 1.00 16.26  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.456  -0.011  21.109 1.00 18.46  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.461  1.356   18.810 1.00 16.75  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.375  2.175   17.554 1.00 18.39  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.560  3.296   17.487 1.00 19.66  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.161  1.869   16.455 1.00 20.07  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.534  4.091   16.350 1.00 20.67  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.132  2.641   15.312 1.00 21.08  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.295  3.736   15.252 1.00 21.38  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.288  4.550   14.147 1.00 23.07  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.272  1.896   22.252 1.00 16.70  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.256  1.235   23.573 1.00 17.48  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.137  1.855   24.366 1.00 18.31  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.047  3.080   24.461 1.00 18.30  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.629  1.361   24.309 1.00 19.42  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.122 2.820   24.323 1.00 19.71  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.544  0.814   25.738 1.00 20.99  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.215  1.027   24.882 1.00 19.24  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.068  1.534   25.622 1.00 19.55  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.257  2.500   24.767 1.00 19.52  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.018  2.213   23.597 1.00 20.23  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.939  3.691   25.310 1.00 19.78  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.254  4.686   24.490 1.00 20.29  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.215  5.751   24.014 1.00 18.50  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.833  6.910   23.888 1.00 19.26  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.055  5.288   25.215 1.00 23.76  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.935  4.300   25.361 1.00 31.97  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.296  3.890   24.384 1.00 35.68  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.737  3.856   26.572 1.00 32.57  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.455  5.357   23.692 1.00 16.64  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.460  6.298   23.231 1.00 15.78  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.051  5.846   21.902 1.00 15.40  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.189  4.643   21.632 1.00 15.30  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.621  6.382   24.229 1.00 16.40  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.215  6.915   25.585 1.00 17.61  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.552  8.130   25.705 1.00 18.59  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.473  6.199   26.745 1.00 19.55  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.230  8.659   26.956 1.00 19.45  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.120  6.705   27.998 1.00 20.32  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.479  7.927   28.089 1.00 21.27  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.133  8.466   29.321 1.00 23.94  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.448  6.849   21.092 1.00 14.13  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.168  6.687   19.850 1.00 14.85  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.475  7.492   19.996 1.00 14.73  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.423  8.690   20.292 1.00 15.35  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.316  7.194   18.668 1.00 15.86  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.062  7.432   17.375 1.00 17.73  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.153  7.740   16.220 1.00 18.59  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.720  8.752   15.322 1.00 20.30  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.191  8.523   14.108 1.00 23.40  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.291  7.275   13.650 1.00 23.75  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.651  9.532   13.367 1.00 22.82  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.630 6.828   19.834 1.00 14.11  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.926 7.483   19.947 1.00 13.43  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.522 7.609   18.562 1.00 13.56  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.682 6.585   17.865 1.00 13.79  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.922 6.682   20.843 1.00 14.72  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.184 7.503   21.096 1.00 15.07  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.287 6.215   22.151 1.00 15.58  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.857 8.840   18.146 1.00 12.76  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.419 9.061   16.814 1.00 13.20  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.650 9.985   16.937 1.00 12.41  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.851 10.664  17.958 1.00 12.67  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.382 9.719   15.875 1.00 15.74  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.285 8.750   15.540 1.00 17.99  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.813 11.012  16.461 1.00 16.34  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.430 10.088  15.843 1.00 11.62  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.458 11.133  15.785 1.00 11.89  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.739 12.475  15.768 1.00 12.72  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.790 12.681  14.975 1.00 13.10  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.302 11.033  14.486 1.00 12.48  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.092 9.762   14.370 1.00 12.94  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.594 8.747   13.847 1.00 13.72  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.273 9.763   14.927 1.00 13.94  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.202 13.419  16.594 1.00 11.10  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.549 14.735  16.653 1.00 11.83  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.543 15.410  15.279 1.00 12.47  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.535 16.012  14.898 1.00 13.66  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.218 15.580  17.708 1.00 13.27  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.415 16.860  18.014 1.00 12.98  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.299 17.757  18.896 1.00 14.15  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.652 19.000  19.359 1.00 14.18  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.704 20.137  18.692 1.00 15.07  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.109 20.156  17.428 1.00 15.00  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.211 21.259  19.238 1.00 16.08  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.633 15.252  14.515 1.00 11.23  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.718 15.913  13.218 1.00 12.65  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.775 15.327  12.176 1.00 13.91  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.613 15.946  11.106 1.00 16.25  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.179 16.007  12.724 1.00 13.16  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.781 14.734  12.220 1.00 12.57  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.355 13.791  13.065 1.00 13.50  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.932 14.322  10.945 1.00 13.13  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.850 12.825  12.271 1.00 13.39  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.600 13.093  10.986 1.00 13.36  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.223 14.151  12.423 1.00 14.42  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.275 13.498  11.495 1.00 14.13  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.826 13.508  12.036 1.00 15.07  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.933 12.923  11.431 1.00 16.28  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.732 12.058  11.195 1.00 13.74  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.115 11.972  10.559 1.00 14.14  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.479 10.508  10.330 1.00 15.70  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.165 12.751  9.215  1.00 14.74  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.577 14.151  13.203 1.00 14.63  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.243 14.174  13.781 1.00 15.53  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.263 14.843  12.803 1.00 15.82  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.598 15.852  12.185 1.00 15.93  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.264 14.935  15.103 1.00 15.33  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.061  14.314  12.743 1.00 16.48  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.002  14.830  11.854 1.00 17.10  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.176  15.900  12.559 1.00 18.01  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.285  16.121  13.771 1.00 18.03  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.080  13.656  11.434 1.00 19.63  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.368  13.219  12.593 1.00 19.19  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.836  12.509  10.804 1.00 21.69  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.257  16.556  11.796 1.00 19.78  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.328  17.506  12.405 1.00 21.17  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.499  16.818  13.517 1.00 18.29  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.266  17.386  14.607 1.00 19.71  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.342  18.050  11.338 1.00 24.30  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 4.974  18.856  10.249 1.00 32.18  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.793  19.933  10.524 1.00 35.10  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.825  18.752  8.903  1.00 35.17  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.150  20.426  9.346  1.00 36.23  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.597  19.735  8.339  1.00 36.57  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.060  15.553  13.247 1.00 18.42  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.290  14.802  14.223 1.00 18.84  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.108  14.499  15.492 1.00 17.41  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.585  14.548  16.607 1.00 18.14  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.757  13.505  13.629 1.00 22.86  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.867  12.718  14.561 1.00 35.49  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.731  13.109  14.834 1.00 39.71  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 2.365  11.593  15.092 1.00 39.02  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.432  14.212  15.343 1.00 16.45  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.247  13.983  16.529 1.00 17.02  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.268  15.241  17.408 1.00 16.23  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.113  15.157  18.626 1.00 16.22  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.680  13.643  16.130 1.00 16.01  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.876  12.240  15.608 1.00 17.28  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.242  11.324  16.147 1.00 19.14  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.619  12.083  14.595 1.00 17.50  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.476  16.405  16.782 1.00 15.60  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.518  17.668  17.548 1.00 16.36  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.165  18.040  18.167 1.00 17.87  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.138  18.563  19.281 1.00 18.78  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.052  18.796  16.648 1.00 16.08  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.556  18.790  16.538 1.00 16.13  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.316  18.337  15.501 1.00 18.37  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.475  19.316  17.511 1.00 15.90  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.658 18.563  15.769 1.00 17.84  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.779 19.102  17.020 1.00 17.11  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.317  19.871  18.783 1.00 17.16  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 11.916 19.558  17.719 1.00 17.12  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.453 20.267  19.488 1.00 17.15  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.724 20.109  18.949 1.00 17.57  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.072  17.650  17.525 1.00 17.76  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.722  17.928  18.067 1.00 18.64  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.361  17.006  19.258 1.00 20.17  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.423  17.260  20.030 1.00 22.11  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.698  17.738  16.963 1.00 19.77  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.065  15.871  19.381 1.00 18.42  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.872  14.940  20.473 1.00 19.18  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.171  14.813  21.299 1.00 17.41  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.486  13.766  21.848 1.00 16.97  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.452  13.586  19.890 1.00 19.78  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.102  13.641  19.258 1.00 22.77  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.078  13.632  19.961 1.00 25.20  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.064  13.736  17.944 1.00 23.58  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.912  15.928  21.421 1.00 16.54  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.202  15.928  22.076 1.00 17.35  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.162  15.531  23.544 1.00 17.87  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.349  16.071  24.310 1.00 19.44  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.802  17.336  21.960 1.00 17.04  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.157  17.539  22.628 1.00 17.86  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.223  16.673  21.945 1.00 17.55  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.571  19.027  22.578 1.00 19.53  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.041  14.623  23.958 1.00 17.06  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.199  14.257  25.367 1.00 18.17  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.511  14.869  25.879 1.00 19.57  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.566  15.492  26.955 1.00 21.54  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.221  12.699  25.507 1.00 18.81  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.608  12.281  26.923 1.00 19.43  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.854  12.119  25.163 1.00 19.89  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.603  14.701  25.108 1.00 17.44  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.912 15.185  25.531 1.00 17.33  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.814 15.262  24.296 1.00 15.30  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.709 14.417  23.391 1.00 16.34  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.527 14.195  26.567 1.00 17.53  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 12.996 14.377  26.879 1.00 17.67  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.555 15.246  27.774 1.00 19.14  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.082 13.632  26.306 1.00 16.47  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.938 15.134  27.738 1.00 19.29  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.275 14.110  26.884 1.00 17.94  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.156 12.624  25.345 1.00 17.70  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.521 13.570  26.572 1.00 17.98  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.386 12.080  25.034 1.00 19.01  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.555 12.566  25.632 1.00 18.47  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.704 16.224  24.265 1.00 15.17  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.709 16.307  23.206 1.00 14.78  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 14.984 16.931  23.739 1.00 14.43  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 14.960 17.720  24.688 1.00 15.40  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.197 17.045  21.954 1.00 15.56  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.621 18.435  22.218 1.00 15.47  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.588 19.583  22.489 1.00 17.93  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.192 20.483  23.274 1.00 21.67  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.705 19.623  21.931 1.00 16.79  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.092 16.579  23.096 1.00 14.75  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.392 17.079  23.505 1.00 14.40  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.266 17.193  22.266 1.00 14.42  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.760 16.187  21.733 1.00 13.60  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.974 16.195  24.616 1.00 16.30  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.256 16.691  25.225 1.00 21.65  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 19.968 17.467  24.559 1.00 24.45  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.559 16.298  26.368 1.00 22.22  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.520 18.412  21.832 1.00 14.94  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.331 18.692  20.682 0.50 15.50  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.347 18.659  20.662 0.50 15.12  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.760 18.175  20.883 1.00 15.00  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.382 17.693  19.937 1.00 16.09  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.327 20.199  20.424 0.50 18.54  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.360 20.138  20.270 0.50 17.11  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.125 20.538  19.310 0.50 23.21  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.045 20.927  21.221 0.50 20.10  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.277 18.291  22.131 1.00 14.84  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.644 17.822  22.368 1.00 15.28  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.772 16.325  22.231 1.00 14.66  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.891 15.857  22.106 1.00 16.33  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.156 18.261  23.740 1.00 18.77  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.576 17.517  24.796 1.00 25.05  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.676 15.578  22.281 1.00 12.99  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.722 14.107  22.137 1.00 12.96  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.183 13.654  20.758 1.00 13.46  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.218 12.452  20.446 1.00 12.97  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.854 13.435  23.231 1.00 13.88  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.463 13.600  24.630 1.00 14.97  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.620 12.970  25.728 1.00 14.38  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.615 11.503  25.589 1.00 13.86  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.420 10.665  26.608 1.00 14.80  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.238 11.129  27.842 1.00 16.85  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.476 9.348   26.415 1.00 14.90  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.629 14.553  19.956 1.00 12.86  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.934 14.209  18.709 1.00 12.24  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.754 13.270  18.966 1.00 12.32  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.459 12.423  18.099 1.00 12.33  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.859 13.646  17.615 1.00 13.02  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.178 13.411  16.281 1.00 12.19  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.405 14.293  15.845 1.00 11.96  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.477 12.382  15.636 1.00 12.33  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.060 13.426  20.115 1.00 11.79  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.890 12.574  20.369 1.00 11.69  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.622 13.354  20.564 1.00 11.69  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.607 14.464  21.115 1.00 12.71  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.079 11.702  21.650 1.00 12.26  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.143 10.620  21.567 1.00 13.46  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.212 9.895   22.935 1.00 15.02  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.817 9.606   20.475 1.00 14.54  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.493 12.725  20.149 1.00 12.19  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.180 13.273  20.429 1.00 12.88  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.281 12.081  20.708 1.00 12.56  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.362 11.030  20.033 1.00 12.77  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.652 14.108  19.246 1.00 12.83  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.262 14.752  19.434 1.00 13.89  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.178 16.058  18.682 1.00 15.61  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.149 13.810  18.980 1.00 15.25  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.416 12.220  21.697 1.00 12.99  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.425 11.184  22.067 1.00 13.32  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.043  11.808  21.975 1.00 14.94  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.802  12.903  22.526 1.00 15.97  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.669 10.643  23.494 1.00 14.88  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.574  9.608   23.878 1.00 16.16  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.075 10.027  23.584 1.00 15.92  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.152  11.135  21.263 1.00 15.54  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.752  11.561  21.131 1.00 15.14  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.844  10.471  21.669 1.00 16.54  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.227  9.312   21.836 1.00 16.97  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.430  11.868  19.671 1.00 16.22  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.599  10.744  18.811 1.00 17.66  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.608  10.868  21.951 1.00 17.06  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.632  9.904   22.486 1.00 18.71  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.860  9.216   21.362 1.00 20.64  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.623  9.795   20.316 1.00 21.34  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.697  10.618  23.459 1.00 21.54  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 1.974  11.631  22.795 1.00 25.16  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.423  7.967   21.590 1.00 21.52  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.657  7.215   20.598 1.00 23.23  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.339  6.747   21.219 1.00 26.33  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.230  6.659   22.448 1.00 26.23  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.470  5.962   20.165 1.00 23.78  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.582  5.104   21.298 1.00 24.84  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.860  6.287   19.674 1.00 23.22  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.629 6.384   20.374 1.00 28.96  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.881 5.836   20.870 1.00 31.42  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.763 4.303   20.986 1.00 32.74  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.311 3.708   21.914 1.00 34.94  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.055 6.271   19.969 1.00 34.62  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.719 5.954   18.618 1.00 36.40  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.330 7.764   20.051 1.00 36.03  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.045 3.673   20.059 1.00 31.12  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.865 2.231   20.070 1.00 30.43  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.312  1.832   20.972 1.00 29.20  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.277  2.594   21.113 1.00 27.61  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.624 1.739   18.652 1.00 31.33  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.251  0.648   21.555 1.00 28.88  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.311  0.113   22.419 1.00 28.96  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.455  -0.386  21.552 1.00 28.51  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.207  -1.096  20.580 1.00 30.02  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.738  -1.050  23.247 1.00 33.37  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.781  -1.856  24.022 1.00 40.96  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.238  -1.170  25.287 1.00 49.28  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.667  -0.157  25.738 1.00 51.68  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.281  -1.728  25.898 1.00 50.59  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.683  -0.030  21.898 1.00 26.12  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.856  -0.369  21.079 1.00 26.98  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.464  -1.760  21.095 1.00 29.10  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.465  -2.421  22.125 1.00 31.85  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.171  -2.113  20.002 1.00 26.56  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.763  -3.427  19.810 1.00 25.88  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.113  -3.694  20.522 1.00 25.85  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.475  -4.848  20.640 1.00 25.26  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.900  -3.675  18.310 1.00 25.52  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.947  -2.467  17.440 1.00 26.59  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.887  -2.690  20.945 1.00 24.43  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.294 -2.866  21.474 1.00 22.57  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.486 -2.925  23.067 1.00 22.05  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.583  -2.440  23.788 1.00 24.58  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.107 -1.693  20.880 1.00 22.37  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.286 -1.771  19.355 1.00 24.63  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.849 -2.802  18.890 1.00 24.61  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.953 -0.723  18.606 1.00 20.10  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.663 -3.481  23.592 1.00 19.62  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.255 -3.649  24.971 1.00 21.07  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.569 -2.850  25.007 1.00 19.15  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.366 -2.997  24.109 1.00 19.01  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.754 -5.171  25.229 1.00 24.82  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.617 -5.969  25.459 1.00 30.28  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.711 -5.340  26.510 1.00 26.28  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.795 -2.018  26.026 1.00 17.24  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.032 -1.273  26.172 1.00 15.95  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.019 -2.015  27.058 1.00 15.98  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.679 -2.485  28.163 1.00 17.43  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.769 0.127   26.767 1.00 15.65  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.642 0.880   26.034 1.00 16.99  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.062 0.963   26.809 1.00 16.02  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.950 1.138   24.526 1.00 18.17  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.256 -2.160  26.574 1.00 14.76  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.319 -2.772  27.374 1.00 15.16  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.653 -1.871  28.571 1.00 15.77  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.699 -0.644  28.489 1.00 15.45  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.582 -2.928  26.516 1.00 15.20  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.934 -2.507  29.713 1.00 16.32  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.388 -1.765  30.928 1.00 16.06  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.658 -2.508  31.364 1.00 17.69  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.624 -3.434  32.180 1.00 19.36  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.320 -1.784  32.024 1.00 17.31  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.989 -1.212  31.579 1.00 17.74  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.023 0.271   31.227 1.00 17.73  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.680 0.718   30.877 1.00 18.88  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.389 1.871   30.302 1.00 19.68  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.354 2.709   29.957 1.00 17.55  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.136 2.162   29.998 1.00 20.93  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.773 -2.118  30.784 1.00 17.65  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.014 -2.881  30.886 1.00 17.59  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.198 -2.004  30.524 1.00 18.14  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.048 -0.859  30.082 1.00 18.36  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.931 -4.057  29.908 1.00 15.90  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.960 -3.546  28.152 1.00 17.03  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.408 -2.627  30.605 1.00 19.78  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.612 -1.921  30.199 1.00 20.30  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.297 -2.610  29.027 1.00 20.50  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.513 -2.501  28.880 1.00 21.48  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.594 -1.810  31.381 1.00 24.79  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.100 -3.116  31.957 1.00 31.33  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.648 -4.193  31.510 1.00 31.24  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 28.943 -3.070  32.885 1.00 39.06  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.537 -3.281  28.163 1.00 17.84  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.135 -3.928  26.975 1.00 16.70  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.872 -2.915  26.109 1.00 16.68  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.436 -1.764  25.960 1.00 16.38  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.041 -4.587  26.134 1.00 17.77  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.403 -6.144  26.821 1.00 18.74  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 28.999 -3.316  25.554 1.00 15.96  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.744 -2.549  24.570 1.00 15.93  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.905 -3.311  23.262 1.00 15.23  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.776 -2.978  22.443 1.00 15.44  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.115 -2.128  25.083 1.00 18.36  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.048 -0.997  26.109 1.00 22.79  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.453 -0.546  26.467 1.00 26.78  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 32.894 -0.749  27.596 1.00 27.86  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.183 0.101   25.532 1.00 21.54  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.099 -4.394  23.086 1.00 13.86  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 28.998 -5.080  21.794 1.00 14.75  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.509 -5.270  21.490 1.00 14.58  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.646 -5.314  22.399 1.00 15.30  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.716 -6.448  21.810 1.00 16.13  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.105 -7.320  22.754 1.00 19.56  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.204 -6.337  22.149 1.00 17.36  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.205 -5.381  20.214 1.00 14.02  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.829 -5.557  19.774 1.00 13.92  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.792 -5.627  18.256 1.00 12.37  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.814 -5.897  17.611 1.00 13.24  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.569 -5.515  17.711 1.00 11.95  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.307 -5.649  16.275 1.00 11.94  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.448 -4.463  15.891 1.00 11.96  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.472 -4.129  16.555 1.00 12.92  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.582 -6.990  15.986 1.00 13.50  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.155 -7.079  14.494 1.00 14.79  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.514 -8.160  16.331 1.00 15.72  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.799 -3.815  14.759 1.00 12.47  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.968 -2.701  14.258 1.00 11.69  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.453 -2.971  12.870 1.00 11.46  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.075 -3.694  12.086 1.00 11.84  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.685 -1.315  14.335 1.00 12.19  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.714 -1.046  13.245 1.00 11.64  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.963 -1.664  13.273 1.00 12.64  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.429 -0.197  12.183 1.00 12.59  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.921 -1.407  12.300 1.00 12.26  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.393 0.084   11.206 1.00 13.06  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.624 -0.558  11.258 1.00 12.60  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.607 -0.344  10.325 1.00 13.80  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.312 -2.327  12.549 1.00 11.56  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.768 -2.382  11.216 1.00 11.96  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.283 -1.208  10.373 1.00 12.44  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.138 -0.028  10.749 1.00 12.52  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.220 -2.416  11.221 1.00 12.01  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.696 -2.527  9.818  1.00 13.53  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.911 -3.663  9.074  1.00 14.48  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.995 -1.478  9.233  1.00 13.91  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.448 -3.759  7.764  1.00 14.81  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.574 -1.540  7.916  1.00 14.75  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.766 -2.692  7.196  1.00 15.98  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.339 -2.787  5.887  1.00 19.17  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.831 -1.530  9.191  1.00 12.79  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.381 -0.550  8.238  1.00 12.12  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.487 -0.539  6.977  1.00 13.37  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.629 -1.414  6.118  1.00 13.51  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.808 -0.963  7.907  1.00 12.80  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.604 0.087   6.655  1.00 14.24  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.615 0.455   6.879  1.00 12.78  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.704 0.517   5.745  1.00 13.38  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.408 0.679   4.392  1.00 14.15  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.934 0.110   3.396  1.00 15.34  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.651 1.600   5.961  1.00 16.96  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.232 2.878   5.982  1.00 23.27  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.588 1.352   4.359  1.00 12.92  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.336 1.534   3.087  1.00 12.85  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 23.012 0.255   2.593  1.00 13.32  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.591 0.268   1.504  1.00 14.13  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.344 2.654   3.192  1.00 14.32  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.353 2.372   4.146  1.00 14.43  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.935 -0.837  3.364  1.00 12.76  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.379 -2.155  2.962  1.00 12.77  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.273 -3.200  3.040  1.00 14.06  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.513 -4.382  2.752  1.00 15.50  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.583 -2.564  3.820  1.00 14.49  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.826 -1.698  3.568  1.00 14.28  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.471 -2.035  2.226  1.00 15.80  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.680 -1.205  1.957  1.00 17.28  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.651 -0.034  1.339  1.00 16.02  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.508 0.460   0.886  1.00 16.03  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.780 0.645   1.125  1.00 16.41  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.086 -2.823  3.539  1.00 14.97  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.005 -3.772  3.856  1.00 16.44  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.561 -4.956  4.674  1.00 16.98  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.255 -6.135  4.395  1.00 18.44  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.318 -4.287  2.596  1.00 20.05  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.467 -3.256  2.000  1.00 27.23  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.310 -3.965  1.285  1.00 30.69  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.724 -3.013  0.377  1.00 31.17  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.074 -2.885  -0.903 1.00 29.74  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.968 -3.721  -1.448 1.00 31.24  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.569 -1.904  -1.637 1.00 25.88  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.422 -4.659  5.665  1.00 15.50  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.083 -5.759  6.405  1.00 15.70  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.294 -5.340  7.852  1.00 14.73  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.369 -4.153  8.163  1.00 14.33  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.511 -6.028  5.802  1.00 18.85  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.539 -7.112  4.703  1.00 28.63  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.984 -7.370  4.310  1.00 36.15  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.143 -8.631  3.477  1.00 42.36  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 24.909 -8.372  2.034  1.00 47.05  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.428 -6.326  8.714  1.00 14.08  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.821 -6.091  10.102 1.00 13.01  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.306 -6.420  10.239 1.00 14.43  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.820 -7.378  9.654  1.00 16.56  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.039 -7.022  11.058 1.00 13.60  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.577 -6.758  11.080 1.00 14.01  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.957 -6.022  12.073 1.00 18.45  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.641 -7.244  10.248 1.00 13.93  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.653 -6.106  11.805 1.00 16.04  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.431 -6.791  10.715 1.00 18.95  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.016 -5.665  11.084 1.00 13.06  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.451 -5.876  11.308 1.00 13.19  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.757 -5.900  12.800 1.00 13.59  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.179 -5.121  13.571 1.00 13.40  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.272 -4.683  10.744 1.00 13.42  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.268 -4.579  9.247  1.00 13.87  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.970 -5.492  8.454  1.00 15.56  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.563 -3.577  8.609  1.00 15.06  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 27.958 -5.400  7.048  1.00 15.50  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.578 -3.459  7.219  1.00 15.94  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.253 -4.391  6.447  1.00 15.97  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.240 -4.293  5.060  1.00 18.47  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.663 -6.769  13.244 1.00 12.91  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.086 -6.743  14.649 1.00 13.71  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.071 -5.567  14.888 1.00 14.51  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.859 -5.179  13.983 1.00 16.67  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.851 -8.101  14.791 1.00 14.39  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.371 -8.365  13.394 1.00 14.69  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.363 -7.812  12.443 1.00 12.74  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.052 -5.001  16.066 1.00 13.55  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.922 -3.854  16.408 1.00 13.88  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.405 -3.954  17.831 1.00 14.16  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.723 -4.480  18.713 1.00 14.57  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.182 -2.491  16.294 1.00 16.17  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.128 -2.024  14.860 1.00 18.22  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.789 -2.555  16.913 1.00 16.37  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.604 -3.397  18.064 1.00 14.62  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.167 -3.065  19.360 1.00 14.93  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.078 -1.523  19.449 1.00 14.81  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.487 -0.845  18.507 1.00 15.56  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.624 -3.477  19.423 1.00 19.26  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.707 -4.891  19.442 1.00 27.04  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.469 -0.983  20.504 1.00 13.59  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.266 0.472   20.543 1.00 12.95  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.742 1.050   21.858 1.00 13.92  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.793 0.369   22.908 1.00 14.67  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.767 0.850   20.302 1.00 13.33  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.724 0.064   21.092 1.00 12.51  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.233 -1.151  20.616 1.00 14.41  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.231 0.545   22.303 1.00 13.47  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.273 -1.862  21.336 1.00 15.15  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.263 -0.176  23.019 1.00 14.17  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.823 -1.381  22.554 1.00 15.46  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.091 2.331   21.818 1.00 14.19  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.537 3.018   23.037 1.00 14.72  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.415 3.323   23.986 1.00 15.38  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.254 3.349   23.585 1.00 16.04  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.319 4.272   22.662 1.00 16.29  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.449 5.157   21.966 1.00 19.06  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.727 3.550   25.253 1.00 14.78  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.711 3.945   26.227 1.00 15.26  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.148 5.319   25.865 1.00 15.55  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.858 6.138   25.260 1.00 17.41  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.355 3.985   27.621 1.00 18.54  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.698 2.610   28.104 1.00 20.93  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.270 2.720   29.544 1.00 26.43  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.433 1.321   30.043 1.00 33.68  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 32.977 1.314   31.414 1.00 39.15  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.907 5.613   26.244 1.00 15.57  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.337 6.937   25.907 1.00 16.22  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.198 8.094   26.393 1.00 16.71  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.591 8.145   27.565 1.00 17.58  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 26.979 6.939   26.617 1.00 18.37  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.665 5.482   26.947 1.00 20.62  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 27.967 4.770   27.035 1.00 17.22  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.485 9.040   25.481 1.00 15.61  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.379 10.139  25.830 1.00 16.33  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.066 11.384  24.997 1.00 14.71  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.174 11.364  24.125 1.00 14.80  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.830 9.693   25.667 1.00 22.04  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.165 9.590   24.310 1.00 28.81  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.799 12.491  25.287 1.00 15.21  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.640 13.775  24.612 1.00 16.90  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.615 13.758  23.460 1.00 17.38  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.850 13.713  23.703 1.00 19.52  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.041 14.864  25.624 1.00 19.10  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.569 16.263  25.421 1.00 23.65  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 29.056 16.376  25.261 1.00 23.29  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 30.995 17.136  26.613 1.00 26.81  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.105 13.815  22.217 1.00 17.08  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 31.945 13.718  21.021 1.00 18.09  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.684 14.902  20.117 1.00 17.32  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.518 15.248  19.866 1.00 16.51  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.589 12.374  20.296 1.00 19.92  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 31.971 11.184  21.212 1.00 23.37  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.197 12.275  18.886 1.00 20.96  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.830 9.866   20.707 1.00 26.82  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.753 15.506  19.555 1.00 16.33  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.573 16.593  18.616 1.00 18.35  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.020 16.089  17.294 1.00 19.03  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.531 15.104  16.743 1.00 20.34  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 33.947 17.258  18.377 1.00 20.58  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.906 18.329  17.333 1.00 25.61  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.170 18.034  16.010 1.00 27.91  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.489 19.591  17.648 1.00 27.97  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.089 19.012  15.039 1.00 29.49  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.426 20.584  16.674 1.00 29.13  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.720 20.282  15.378 1.00 28.99  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 30.939 16.724  16.798 1.00 17.13  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.300 16.375  15.516 1.00 16.07  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.335 17.630  14.632 1.00 17.29  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.827 18.717  15.031 1.00 17.73  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.826 15.930  15.784 1.00 16.65  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.099 15.612  14.466 1.00 17.39  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.784 14.721  16.722 1.00 16.25  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.825 17.453  13.401 1.00 18.25  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 30.963 18.566  12.451 1.00 18.06  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.593 19.100  12.077 1.00 18.56  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.595 18.389  12.158 1.00 17.53  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.644 18.074  11.154 1.00 24.05  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 32.995 17.442  11.378 1.00 35.88  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.263 16.343  10.373 1.00 48.41  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.228 16.643  9.158  1.00 50.25  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 33.468 15.178  10.791 1.00 51.61  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.549 20.345  11.590 1.00 19.20  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.295 20.969  11.197 1.00 19.10  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.650 20.185  10.072 1.00 18.73  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.333 19.598  9.240  1.00 19.69  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.543 22.407  10.722 1.00 20.69  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.321 20.173  10.052 1.00 18.08  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.528 19.559  8.993  1.00 18.02  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.405 20.570  8.672  1.00 18.70  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.377 21.661  9.257  1.00 19.90  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.921 18.227  9.481  1.00 18.68  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 23.961 18.447  10.505 1.00 18.29  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.476 20.195  7.790  1.00 19.47  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.337 21.078  7.527  1.00 20.81  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.377 21.140  8.706  1.00 20.52  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.520 22.025  8.749  1.00 22.05  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.602 20.610  6.269  1.00 26.04  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.175 19.157  6.334  1.00 32.99  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 22.077 18.118  5.682  1.00 44.27  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 21.562 17.377  4.810  1.00 48.88  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 23.273 18.014  6.053  1.00 42.43  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.513 20.198  9.685  1.00 18.57  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.608 20.111  10.816 1.00 17.85  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.119 20.771  12.069 1.00 17.19  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.323 21.152  12.912 1.00 18.75  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.331 18.635  11.126 1.00 17.83  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.865 17.835  9.924  1.00 17.88  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.748 17.039  9.210  1.00 19.65  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.545 17.880  9.508  1.00 18.57  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.322 16.299  8.113  1.00 20.77  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 18.115 17.172  8.392  1.00 18.99  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.992 16.342  7.734  1.00 20.13  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.555 15.647  6.622  1.00 23.29  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.438 20.855  12.236 1.00 16.46  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.026 21.388  13.460 1.00 17.27  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.306 22.092  13.142 1.00 18.46  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.068 21.653  12.279 1.00 18.50  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.460 20.251  14.451 1.00 16.46  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.347 19.347  14.943 1.00 14.92  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.461 19.777  15.924 1.00 15.25  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.216 18.042  14.472 1.00 14.51  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.467 18.937  16.419 1.00 14.54  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.218 17.190  14.970 1.00 13.17  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.376 17.634  15.969 1.00 13.50  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.342 16.868  16.454 1.00 13.66  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.645 23.111  13.950 1.00 19.99  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.002 23.693  13.849 1.00 20.59  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.017 22.696  14.431 1.00 19.59  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.643 21.720  15.139 1.00 19.52  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.882 24.951  14.724 1.00 22.64  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 24.882 24.571  15.751 1.00 23.48  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.872 23.696  15.069 1.00 20.36  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.313 22.939  14.216 1.00 19.44  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.361 22.116  14.816 1.00 19.44  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.209 22.183  16.364 1.00 19.72  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 28.950 23.257  16.914 1.00 20.91  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.737 22.634  14.380 1.00 20.18  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.174 21.012  17.014 1.00 18.46  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 28.907 21.002  18.459 1.00 18.18  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.369 19.700  19.082 1.00 18.15  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.689 18.764  18.351 1.00 19.02  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.367 21.169  18.658 1.00 18.13  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.621 19.838  18.301 1.00 17.75  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.210 20.043  17.839 1.00 17.19  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.312 18.940  18.186 1.00 16.94  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.301 17.744  17.599 1.00 15.56  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.418 16.822  17.980 1.00 16.06  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.156 17.465  16.621 1.00 16.07  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.322 19.610  20.401 1.00 17.60  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.528 18.316  21.059 1.00 17.91  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.189 17.649  21.226 1.00 16.90  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.262 18.250  21.788 1.00 18.95  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.145 18.471  22.456 1.00 18.70  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.590 18.887  22.377 1.00 20.68  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.596 17.944  22.286 1.00 21.69  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 31.943 20.226  22.371 1.00 22.27  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 33.935 18.323  22.200 1.00 24.61  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.274 20.619  22.264 1.00 25.07  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.262 19.662  22.166 1.00 26.63  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.575 20.085  22.108 1.00 30.75  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.073 16.408  20.763 1.00 14.93  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.876 15.605  20.983 1.00 14.06  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.162 14.703  22.185 1.00 13.95  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.207 14.030  22.229 1.00 15.75  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.525 14.790  19.729 1.00 13.51  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.281 13.922  19.956 1.00 14.16  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.671 13.451  18.657 1.00 12.86  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.540 14.167  17.654 1.00 14.20  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.191 12.183  18.682 1.00 13.25  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.259 14.695  23.155 1.00 14.03  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.398 13.869  24.356 1.00 13.16  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.703 12.514  24.207 1.00 14.35  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 24.909 12.312  23.284 1.00 14.11  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.833 14.612  25.570 1.00 14.95  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.440 14.819  25.379 1.00 17.38  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.122 11.561  25.061 1.00 13.54  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.543 10.217  25.136 1.00 13.59  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.727 9.475   23.791 1.00 13.66  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.891 8.627   23.436 1.00 13.65  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.040 10.278  25.538 1.00 14.62  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.838 10.905  26.902 1.00 16.12  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.682 10.110  28.035 1.00 18.29  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.752 12.206  27.260 1.00 16.62  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.536 10.968  29.059 1.00 18.80  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.589 12.235  28.646 1.00 17.85  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.847 9.739   23.095 1.00 13.29  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.089 9.137   21.779 1.00 13.70  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.138 8.048   21.931 1.00 14.20  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.132 8.216   22.669 1.00 13.81  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.640 10.243  20.844 1.00 14.87  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.878 9.854   19.369 1.00 15.42  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.565 9.394   18.693 1.00 15.78  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.448 11.089  18.565 1.00 17.16  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.896 6.947   21.227 1.00 13.13  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.780 5.771   21.235 1.00 12.64  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.308 5.537   19.848 1.00 13.38  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.506 5.394   18.914 1.00 14.34  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 27.943 4.557   21.666 1.00 13.15  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.403 4.742   23.098 1.00 15.66  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.302 3.423   23.663 1.00 17.16  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 24.940 3.580   22.472 1.00 20.50  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.633 5.429   19.658 1.00 13.34  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.176 5.236   18.314 1.00 14.29  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.640 3.813   18.089 1.00 13.69  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.096 3.135   19.018 1.00 14.24  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.408 6.136   18.057 1.00 17.86  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.192 7.619   18.029 1.00 22.83  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.440 8.347   17.423 1.00 24.25  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 30.988 7.999   17.210 1.00 23.16  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.576 3.377   16.855 1.00 13.46  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.031 2.037   16.458 1.00 13.36  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.505 2.082   15.025 1.00 12.84  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.210 3.049   14.288 1.00 13.72  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.847 1.046   16.499 1.00 15.36  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.332 1.075   14.655 1.00 12.16  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.718 0.883   13.280 1.00 12.23  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.655 0.088   12.572 1.00 13.97  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.272 -0.989  13.004 1.00 14.93  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.097 0.200   13.239 1.00 13.37  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.530 -0.079  11.785 1.00 15.47  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.134 1.068   13.975 1.00 14.85  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.114 0.668   11.509 1.00 13.74  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.067 0.046   10.700 1.00 13.64  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.596 1.029   9.646  1.00 13.55  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.841 2.255   9.760  1.00 14.95  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.033 0.520   8.563  1.00 13.14  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.538 1.382   7.512  1.00 12.53  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.294 2.184   7.919  1.00 11.94  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.357 1.661   8.537  1.00 12.56  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.196 0.554   6.273  1.00 13.94  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.702 1.404   5.145  1.00 13.58  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.528 2.290   4.527  1.00 14.35  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.440 1.548   4.660  1.00 15.04  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.776 2.918   3.618  1.00 15.26  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.502 2.488   3.683  1.00 15.83  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.251 3.435   7.494  1.00 13.10  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 27.033 4.245   7.625  1.00 12.73  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 27.076 5.418   6.648  1.00 12.77  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.147 5.881   6.270  1.00 13.73  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.791 4.729   9.056  1.00 13.99  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.746 5.709   9.431  1.00 13.72  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.889 5.845   6.257  1.00 12.97  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.602 7.006   5.413  1.00 13.51  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.508 7.807   6.170  1.00 14.78  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.823 7.291   7.062  1.00 13.73  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 25.072 6.537   4.037  1.00 14.99  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.139 5.711   3.337  1.00 15.02  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.784 5.130   1.976  1.00 17.22  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 25.052 5.783   1.195  1.00 19.25  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.246 4.003   1.701  1.00 16.99  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.312 9.098   5.821  1.00 15.03  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.334 9.919   6.586  1.00 14.95  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.938 9.327   6.759  1.00 14.82  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.366 9.388   7.852  1.00 14.77  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.299 11.238  5.789  1.00 16.39  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.701 11.333  5.228  1.00 16.71  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 25.082 9.892   4.838  1.00 15.92  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.417 8.694   5.700  1.00 14.32  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 20.086 8.098   5.742  1.00 14.08  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.995 6.868   6.615  1.00 13.93  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.901 6.374   6.855  1.00 14.75  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.147 6.366   7.126  1.00 13.40  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.103 5.239   8.060  1.00 12.40  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.683 5.641   9.471  1.00 12.37  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.380 4.771   10.279 1.00 13.45  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.497 4.564   8.144  1.00 12.70  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.799 3.767   6.906  1.00 14.07  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.878 3.158   6.376  1.00 14.50  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 23.970 3.775   6.460  1.00 13.17  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.552 6.949   9.736  1.00 11.85  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.088 7.419   11.049 1.00 11.68  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.744 6.800   11.376 1.00 12.36  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.868 6.729   10.504 1.00 13.21  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.020 8.950   11.108 1.00 11.94  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.628 9.744   11.234 1.00 14.00  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.621 6.290   12.578 1.00 11.23  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.361 5.657   13.017 1.00 11.77  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.457 4.151   13.092 1.00 12.50  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.619 3.509   13.730 1.00 13.73  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.485 3.567   12.473 1.00 11.98  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.675 2.118   12.549 1.00 12.34  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 18.932 1.712   14.002 1.00 12.38  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.692 2.383   14.705 1.00 12.70  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.339 0.631   14.441 1.00 11.89  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.492 0.195   15.825 1.00 11.27  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.793 -0.577  16.071 1.00 11.85  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.180 -1.440  15.261 1.00 12.58  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.256 -0.649  16.231 1.00 13.30  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.120 0.343   16.518 1.00 15.25  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.510 -1.533  17.474 1.00 15.76  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.711 -0.415  16.843 1.00 18.17  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.413 -0.306  17.215 1.00 11.10  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.518 -1.080  17.784 1.00 12.14  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.902 -1.891  18.950 1.00 12.54  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.205 -1.300  19.813 1.00 13.18  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.562 -0.108  18.357 1.00 12.89  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.691 -0.767  19.189 1.00 12.20  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.548 -1.716  18.310 1.00 14.28  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.579 0.314   19.835 1.00 14.39  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.097 -3.227  18.942 1.00 12.19  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.577 -4.110  19.982 1.00 12.79  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.688 -4.971  20.519 1.00 12.86  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.581 -5.442  19.780 1.00 14.46  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.501 -5.065  19.327 1.00 16.64  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.065 -4.522  19.194 1.00 21.52  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.023 -5.553  18.615 1.00 23.16  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 15.623 -5.047  18.766 1.00 24.30  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 14.822 -5.394  19.744 1.00 22.48  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.283 -6.126  20.773 1.00 19.60  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 13.566 -4.934  19.781 1.00 26.24  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.600 -5.259  21.821 1.00 13.61  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.447 -6.305  22.434 1.00 13.68  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.497 -7.460  22.846 1.00 14.80  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.285 -7.406  22.614 1.00 15.57  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.195 -5.748  23.656 1.00 15.22  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.072 -5.233  24.984 1.00 15.18  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 22.023 -8.480  23.534 1.00 15.43  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.164 -9.582  24.030 1.00 17.39  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.091 -9.131  25.021 1.00 18.14  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.143 -9.896  25.250 1.00 19.07  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 22.021 -10.713 24.652 1.00 18.93  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.634 -10.288 25.978 1.00 23.82  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.677 -11.231 26.488 1.00 33.89  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.892 -11.009 26.333 1.00 38.16  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.210 -12.272 27.144 1.00 33.23  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.179 -7.921  25.602 1.00 16.36  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.201 -7.438  26.591 1.00 16.81  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.058 -6.609  26.020 1.00 16.04  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.068 -6.366  26.707 1.00 17.16  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.902 -6.619  27.703 1.00 16.75  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 21.021 -7.383  28.345 1.00 18.84  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.361 -7.052  28.138 1.00 20.43  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.966 -8.443  29.199 1.00 22.12  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 23.068 -7.956  28.812 1.00 22.65  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.276 -8.827  29.436 1.00 23.78  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.235 -6.103  24.788 1.00 13.67  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.221 -5.268  24.172 1.00 15.02  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.841 -4.155  23.343 1.00 13.29  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.017 -4.223  22.961 1.00 14.16  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.038 -3.135  23.087 1.00 12.90  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.472 -1.970  22.304 1.00 12.48  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.449 -1.114  23.107 1.00 12.60  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.138 -0.725  24.247 1.00 14.30  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.255 -1.129  21.858 1.00 13.84  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.724 0.164   21.148 1.00 14.84  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.363 -1.967  20.919 1.00 14.91  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.579 -0.778  22.506 1.00 12.87  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.624 0.026   23.124 1.00 13.05  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.526 1.486   22.680 1.00 14.01  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.733 2.411   23.482 1.00 13.45  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.005 -0.548  22.788 1.00 13.60  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.146 0.358   23.254 1.00 15.52  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.201 -1.968  23.335 1.00 14.43  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.267 1.687   21.398 1.00 13.24  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.211 3.041   20.848 1.00 13.62  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.921 3.041   19.364 1.00 12.26  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.532 2.003   18.815 1.00 12.66  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.090 4.208   18.733 1.00 11.76  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.826 4.345   17.281 1.00 11.81  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 20.974 5.038   16.595 1.00 11.84  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.657 5.907   17.177 1.00 11.78  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.510 5.135   16.970 1.00 13.30  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.472 6.474   17.720 1.00 15.00  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.276 4.254   17.276 1.00 15.19  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.214 7.356   17.229 1.00 15.50  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.212 4.708   15.324 1.00 11.16  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.259 5.412   14.532 1.00 10.77  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 21.963 6.911   14.511 1.00 10.86  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.809 7.312   14.273 1.00 11.46  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.276 4.890   13.089 1.00 11.45  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.294 5.691   12.254 1.00 12.40  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.686 3.406   13.054 1.00 12.71  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 22.995 7.700   14.796 1.00 11.45  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.866 9.144   14.809 1.00 11.25  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 23.999 9.879   14.082 1.00 12.27  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.768 11.004  13.631 1.00 13.17  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.807 9.609   16.265 1.00 11.71  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.705 11.021  16.438 1.00 12.71  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.192 9.280   13.977 1.00 12.44  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.300 9.975   13.262 1.00 12.88  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.123 8.929   12.498 1.00 12.91  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.910 7.733   12.683 1.00 12.64  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.254 10.708  14.271 1.00 13.92  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.037 9.737   14.981 1.00 14.73  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.558 11.667  15.247 1.00 14.28  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.015 9.386   11.651 1.00 13.29  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.979 8.460   11.071 1.00 14.01  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.908 9.140   10.102 1.00 16.20  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 29.900 10.367  9.980  1.00 18.10  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.703 8.329   9.414  1.00 16.14  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.521 8.757   8.277  1.00 18.38  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.803 7.988   8.225  1.00 17.72  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.288 7.584   9.283  1.00 19.80  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.407 7.838   7.076  1.00 17.73  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.713 7.178   6.888  1.00 17.68  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.897 5.859   7.611  1.00 17.06  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 35.983 5.566   8.114  1.00 17.81  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.816 8.167   7.277  1.00 23.18  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.725 9.440   6.453  1.00 31.04  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.786 9.394   5.233  1.00 32.42  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.533 10.590  7.089  1.00 34.33  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 33.896 5.016   7.547  1.00 16.02  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 33.948 3.721   8.199  1.00 15.77  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.656 3.756   9.680  1.00 14.43  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.888 2.735   10.352 1.00 15.82  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.085 4.827   10.174 1.00 13.22  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.576 4.915   11.552 1.00 12.77  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.054 5.012   11.545 1.00 12.95  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.435 5.464   10.563 1.00 13.75  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.119 6.134   12.264 1.00 14.31  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.623 6.096   12.483 1.00 17.75  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.139 7.510   12.781 1.00 20.57  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 34.948 5.096   13.648 1.00 18.55  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.468 4.588   12.645 1.00 11.94  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.029 4.734   12.861 1.00 11.97  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.855 5.097   14.344 1.00 12.13  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.536 4.555   15.212 1.00 13.30  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.199 3.506   12.473 1.00 12.24  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.674 2.206   13.123 1.00 14.13  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.723 3.747   12.692 1.00 13.27  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.027 6.101   14.623 1.00 11.53  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.770 6.564   15.996 1.00 11.46  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.328 6.366   16.386 1.00 11.84  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.451 6.600   15.555 1.00 12.84  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.096 5.953   17.634 1.00 12.02  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.759 5.620   18.110 1.00 12.22  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.401 6.484   19.310 1.00 12.05  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.197 6.623   20.256 1.00 12.06  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.691 4.131   18.578 1.00 12.67  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.198 3.157   17.532 1.00 12.11  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.361 2.708   16.527 1.00 12.06  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.511 2.676   17.579 1.00 13.09  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.810 1.790   15.583 1.00 12.36  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 26.955 1.750   16.647 1.00 13.50  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.117 1.330   15.629 1.00 12.67  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.189 7.049   19.276 1.00 11.73  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.665 7.798   20.401 1.00 12.04  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.151 6.751   21.416 1.00 11.92  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.217 5.970   21.113 1.00 13.22  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.520 8.685   19.909 1.00 12.12  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.718 6.733   22.610 1.00 11.67  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.283 5.792   23.661 1.00 12.10  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.910 6.154   24.173 1.00 12.16  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.589 7.361   24.321 1.00 13.21  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.278 5.872   24.847 1.00 14.14  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.020 4.846   25.914 1.00 18.70  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.816 3.681   25.580 1.00 17.85  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 22.940 5.233   27.106 1.00 23.42  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.080 5.104   24.497 1.00 11.80  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.814 5.363   25.142 1.00 12.98  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.702 4.591   26.474 1.00 13.78  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.676 4.695   27.140 1.00 14.38  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.595 5.027   24.268 1.00 14.41  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.590 5.884   22.985 1.00 15.36  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.556 3.533   23.935 1.00 15.31  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.735 3.857   26.892 1.00 13.88  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.637 2.966   28.059 1.00 13.48  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.499 3.703   29.354 1.00 15.28  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.006 3.122   30.336 1.00 16.47  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.857 2.019   28.147 1.00 14.30  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.942 1.021   26.962 1.00 14.79  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.199 0.205   27.092 1.00 14.70  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.329 1.072   26.815 1.00 14.33  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.578 0.638   26.653 1.00 14.67  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.897 -0.628  26.942 1.00 16.29  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.527 1.478   26.250 1.00 16.07  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.907 4.984   29.402 1.00 14.23  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.770 5.767   30.636 1.00 15.20  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.361 6.368   30.790 1.00 16.71  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.086 6.939   31.846 1.00 18.12  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.827 6.876   30.672 1.00 16.40  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.646 7.885   29.559 1.00 19.00  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.419 7.466   28.419 1.00 19.26  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.678 9.124   29.849 1.00 22.59  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.503 6.295   29.770 1.00 15.68  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.161 6.923   29.829 1.00 15.15  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.204 5.970   30.483 1.00 15.51  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.440 5.240   29.865 1.00 15.02  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.716 7.294   28.410 1.00 14.96  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.672 8.263   27.661 1.00 16.02  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.225 8.445   26.225 1.00 16.96  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.817 9.601   28.375 1.00 17.23  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.307 5.907   31.827 1.00 16.01  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.551 4.888   32.579 1.00 17.03  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.048 5.024   32.459 1.00 18.08  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.324 4.013   32.520 1.00 19.08  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.948 4.849   34.052 1.00 17.57  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.446 4.835   34.290 1.00 18.25  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.706 4.738   35.820 1.00 20.39  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.146 3.636   33.570 1.00 18.51  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.586 6.270   32.268 1.00 18.25  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.155 6.569   32.172 1.00 18.56  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.518 5.971   30.908 1.00 19.49  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.278  5.894   30.859 1.00 21.99  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.937 8.086   32.258 1.00 18.12  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.757 8.878   31.283 1.00 17.59  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 12.976 9.465   31.488 1.00 18.23  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.376 9.201   29.941 1.00 18.02  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.375 10.144  30.346 1.00 19.01  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.392 10.020  29.395 1.00 18.74  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.255 8.914   29.173 1.00 19.45  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.325 10.520  28.092 1.00 18.79  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.174 9.433   27.896 1.00 18.36  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.187 10.255  27.388 1.00 18.52  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.306 5.526   29.910 1.00 19.01  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.703 4.940   28.694 1.00 19.47  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.838  3.707   29.030 1.00 23.75  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.914  3.390   28.291 1.00 24.71  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.778 4.531   27.674 1.00 19.30  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.436 5.684   26.938 1.00 18.63  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.567 5.170   26.031 1.00 19.57  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.389 6.456   26.066 1.00 18.66  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.150 3.041   30.169 1.00 27.58  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.471  1.842   30.646 1.00 32.73  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.388  2.003   31.638 1.00 37.49  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.908  0.978   32.147 1.00 39.13  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.497 0.913   31.269 1.00 36.71  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.182 0.141   30.213 1.00 46.17  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 10.496 -0.277  29.228 1.00 49.28  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.387 -0.028  30.320 1.00 50.25  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 7.994  3.225   31.943 1.00 39.86  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.920  3.442   32.912 1.00 43.48  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 5.876  4.407   32.372 1.00 46.25  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 4.998  4.851   33.129 1.00 48.23  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.497  3.937   34.246 1.00 46.75  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.278  5.227   34.112 1.00 52.68  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.310  5.450   35.200 1.00 59.79  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 9.634  6.627   35.476 1.00 61.29  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.809  4.448   35.763 1.00 62.42  ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.488 -24.447 23.816 1.00 19.73  ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.629 -24.368 22.893 1.00 19.42  ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.622 -25.509 21.886 1.00 19.02  ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 19.932 -26.517 22.070 1.00 20.07  ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.949 -24.349 23.671 1.00 22.23  ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.130 -25.590 24.328 1.00 27.33  ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.367 -25.344 20.806 1.00 17.36  ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.519 -26.392 19.805 1.00 16.90  ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.774 -25.836 18.410 1.00 15.66  ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.415 -24.683 18.111 1.00 17.34  ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.405 -26.616 17.543 1.00 14.82  ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.725 -26.169 16.178 1.00 15.04  ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.642 -27.340 15.214 1.00 15.72  ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.653 -28.508 15.611 1.00 17.62  ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.167 -25.604 16.164 1.00 16.46  ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.538 -27.021 13.918 1.00 14.31  ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.663 -27.954 12.816 1.00 14.20  ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.023 -27.740 12.172 1.00 14.08  ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.423 -26.614 11.919 1.00 15.37  ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.557 -27.705 11.783 1.00 14.17  ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.183 -27.754 12.424 1.00 15.37  ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.681 -28.730 10.658 1.00 15.76  ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.092 -27.142 11.497 1.00 16.76  ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.767 -28.827 11.924 1.00 14.57  ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.081 -28.752 11.302 1.00 16.16  ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.009 -29.477 9.975  1.00 17.40  ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 25.813 -30.703 9.960  1.00 18.27  ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.135 -29.426 12.205 1.00 17.51  ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.340 -28.650 13.487 1.00 16.68  ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.181 -27.547 13.527 1.00 18.58  ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.620 -28.959 14.634 1.00 18.15  ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.316 -26.789 14.680 1.00 20.45  ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.760 -28.215 15.799 1.00 20.07  ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.625 -27.144 15.823 1.00 21.72  ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.722 -26.368 16.957 1.00 24.37  ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.097 -28.767 8.862  1.00 18.08  ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 25.965 -29.365 7.532  1.00 19.01  ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.038 -28.739 6.645  1.00 19.52  ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.166 -27.514 6.588  1.00 18.72  ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.531 -29.168 6.955  1.00 21.07  ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.062 -27.728 7.044  1.00 22.18  ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.448 -29.686 5.537  1.00 22.13  ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 27.900 -29.566 6.023  1.00 20.56  ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 28.985 -29.048 5.195  1.00 21.24  ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 29.884 -28.133 6.010  1.00 21.26  ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.209 -28.456 7.157  1.00 22.03  ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.179 -26.950 5.501  1.00 20.83  ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 30.952 -25.981 6.283  1.00 20.83  ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.062 -24.901 6.882  1.00 18.91  ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.495 -23.755 7.025  1.00 20.03  ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.113 -25.388 5.494  1.00 23.45  ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.169 -26.428 5.225  1.00 30.85  ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 33.848 -26.929 6.145  1.00 33.39  ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.293 -26.797 3.975  1.00 33.21  ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.853 -25.282 7.284  1.00 16.90  ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.906 -24.347 7.875  1.00 16.36  ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.409 -24.832 9.237  1.00 15.77  ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.267 -26.036 9.495  1.00 16.74  ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.653 -24.219 6.996  1.00 17.01  ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 26.935 -23.653 5.629  1.00 18.49  ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.618 -22.453 5.480  1.00 20.24  ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.523 -24.318 4.484  1.00 19.90  ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.851 -21.904 4.219  1.00 22.51  ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.767 -23.786 3.213  1.00 21.17  ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.434 -22.577 3.091  1.00 23.20  ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.671 -21.993 1.855  1.00 25.55  ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.122 -23.848 10.114 1.00 14.38  ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.518 -24.046 11.417 1.00 15.16  ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.240 -23.191 11.419 1.00 14.39  ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.312 -21.984 11.178 1.00 15.34  ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.479 -23.596 12.548 1.00 16.20  ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.860 -23.344 13.900 1.00 17.15  ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.916 -23.093 14.982 1.00 17.49  ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.476 -22.081 15.969 1.00 18.82  ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.030 -22.341 17.202 1.00 23.01  ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 26.843 -23.599 17.600 1.00 21.19  ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.696 -21.340 18.026 1.00 21.17  ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.082 -23.830 11.648 1.00 14.21  ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.783 -23.134 11.691 1.00 13.81  ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.327 -23.041 13.142 1.00 13.96  ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.203 -24.076 13.826 1.00 15.14  ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.690 -23.898 10.869 1.00 15.05  ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.437 -23.047 10.747 1.00 15.63  ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.212 -24.321 9.493  1.00 15.79  ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.084 -21.818 13.625 1.00 12.81  ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.640 -21.631 15.004 1.00 13.37  ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.446 -20.670 15.038 1.00 12.31  ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.174 -19.924 14.066 1.00 13.35  ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.792 -21.013 15.846 1.00 16.03  ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 23.892 -22.025 16.044 1.00 19.51  ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.328 -19.706 15.262 1.00 16.22  ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.755 -20.616 16.184 1.00 12.14  ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.761 -19.554 16.386 1.00 12.56  ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.530 -18.216 16.346 1.00 12.78  ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.537 -18.055 17.074 1.00 13.41  ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.079 -19.674 17.768 1.00 13.72  ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.246 -20.911 17.930 1.00 13.96  ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.755 -21.949 18.385 1.00 14.19  ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 16.005 -20.848 17.526 1.00 14.75  ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.011 -17.254 15.591 1.00 13.11  ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.686 -15.938 15.498 1.00 13.59  ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.839 -15.309 16.874 1.00 13.67  ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 20.902 -14.766 17.163 1.00 13.65  ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 18.937 -15.033 14.538 1.00 13.61  ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.718 -13.755 14.170 1.00 13.37  ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.759 -12.853 13.390 1.00 13.84  ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.367 -11.590 12.909 1.00 14.06  ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.416 -10.471 13.601 1.00 16.97  ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.111 -10.468 14.891 1.00 17.31  ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.897 -9.356  13.036 1.00 18.10  ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.815 -15.431 17.737 1.00 13.13  ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 18.902 -14.815 19.063 1.00 13.27  ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 19.916 -15.456 19.980 1.00 14.22  ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.257 -14.840 20.994 1.00 15.42  ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.529 -14.708 19.709 1.00 14.30  ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 16.947 -15.988 20.243 1.00 13.34  ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.258 -16.884 19.436 1.00 13.93  ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 16.930 -16.441 21.529 1.00 13.89  ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.821 -17.856 20.253 1.00 13.66  ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.207 -17.638 21.519 1.00 14.42  ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.410 -16.649 19.656 1.00 14.47  ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.435 -17.309 20.486 1.00 15.61  ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.812 -17.304 19.829 1.00 16.03  ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.752 -17.918 20.353 1.00 16.60  ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 20.990 -18.776 20.774 1.00 15.20  ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.656 -18.860 21.549 1.00 15.36  ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.312 -20.339 21.802 1.00 16.36  ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.752 -18.116 22.958 1.00 16.81  ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 22.961 -16.634 18.660 1.00 15.17  ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.242 -16.627 17.956 1.00 15.34  ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.320 -15.977 18.829 1.00 16.13  ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.058 -15.012 19.523 1.00 16.64  ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.108 -15.860 16.627 1.00 15.36  ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.504 -16.547 18.787 1.00 16.61  ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.629 -16.053 19.591 1.00 17.16  ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.422 -14.969 18.839 1.00 17.12  ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.215 -14.755 17.653 1.00 16.56  ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.569 -17.249 19.910 1.00 19.05  ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.173 -17.674 18.685 1.00 20.42  ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 27.855 -18.396 20.583 1.00 19.69  ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.412 -14.351 19.506 1.00 18.13  ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.325 -13.418 18.824 1.00 17.87  ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.033 -14.111 17.638 1.00 16.91  ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.195 -13.516 16.560 1.00 18.38  ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.430 -12.927 19.798 1.00 21.83  ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.932 -12.104 20.941 1.00 31.15  ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.127 -10.986 20.742 1.00 35.53  ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.236 -12.188 22.259 1.00 34.98  ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.963 -10.437 21.938 1.00 36.45  ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.601 -11.131 22.884 1.00 36.77  ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.435 -15.396 17.834 1.00 17.36  ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.116 -16.131 16.770 1.00 18.05  ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.172 -16.367 15.589 1.00 17.28  ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.596 -16.277 14.435 1.00 17.62  ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.643 -17.463 17.281 1.00 20.77  ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.498 -18.204 16.262 1.00 27.07  ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.615 -17.769 15.911 1.00 28.89  ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 32.969 -19.298 15.738 1.00 28.82  ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 29.868 -16.647 15.856 1.00 16.50  ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 28.934 -16.811 14.745 1.00 16.69  ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.819 -15.519 13.920 1.00 17.01  ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.867 -15.549 12.698 1.00 17.71  ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.545 -17.149 15.279 1.00 15.73  ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.392 -18.568 15.799 1.00 16.93  ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 27.975 -19.484 15.191 1.00 18.22  ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.731 -18.737 16.853 1.00 17.12  ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.709 -14.370 14.609 1.00 16.63  ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.611 -13.098 13.895 1.00 16.93  ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.911 -12.698 13.175 1.00 18.64  ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.835 -12.087 12.108 1.00 20.19  ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.177 -11.996 14.879 1.00 16.87  ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.691 -11.962 15.088 1.00 15.67  ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.008 -12.438 16.157 1.00 16.30  ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.712 -11.378 14.193 1.00 15.62  ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.649 -12.207 15.980 1.00 16.35  ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.450 -11.569 14.774 1.00 16.25  ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.787 -10.756 12.946 1.00 17.53  ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.271 -11.072 14.181 1.00 17.25  ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.625 -10.327 12.335 1.00 18.51  ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.383 -10.478 12.959 1.00 18.31  ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.047 -13.142 13.682 1.00 17.57  ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.326 -12.806 13.036 1.00 18.97  ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.575 -13.700 11.774 1.00 19.19  ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.474 -13.428 10.978 1.00 21.28  ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.472 -13.044 14.020 1.00 18.97  ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.861 -14.839 11.686 1.00 17.25  ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 31.931 -15.788 10.567 1.00 17.35  ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.588 -15.902 9.858  1.00 17.45  ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.180 -16.966 9.428  1.00 17.50  ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.437 -17.138 11.083 1.00 17.57  ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.879 -17.041 11.565 1.00 20.96  ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.834 -16.971 10.764 1.00 23.16  ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.048 -16.881 12.879 1.00 20.11  ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.890 -14.790 9.793  1.00 17.36  ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.537 -14.751 9.260  1.00 17.49  ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.417 -15.131 7.789  1.00 17.94  ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.119 -14.579 6.954  1.00 20.04  ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 27.986 -13.334 9.474  1.00 17.60  ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.565 -13.111 8.962  1.00 18.01  ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.546 -13.986 9.729  1.00 18.20  ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.165 -11.655 9.117  1.00 19.11  ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.494 -16.035 7.442  1.00 16.54  ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.185 -16.377 6.066  1.00 17.32  ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.849 -15.730 5.673  1.00 18.49  ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.737 -15.106 4.619  1.00 21.00  ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.116 -17.920 5.892  1.00 18.15  ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.561 -18.290 4.510  1.00 20.02  ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.499 -18.538 6.129  1.00 19.57  ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.835 -15.854 6.539  1.00 16.80  ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.495 -15.374 6.254  1.00 17.86  ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.720 -15.294 7.553  1.00 16.65  ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.893 -16.142 8.435  1.00 16.88  ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.777 -16.316 5.244  1.00 18.73  ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.285 -16.096 5.071  1.00 19.22  ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.663 -15.209 4.231  1.00 21.64  ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.238 -16.848 5.708  1.00 18.23  ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.287 -15.321 4.366  1.00 22.51  ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.003 -16.342 5.243  1.00 20.16  ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.229 -17.863 6.669  1.00 17.94  ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.766 -16.884 5.659  1.00 19.78  ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 19.013 -18.398 7.070  1.00 18.04  ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.800 -17.897 6.591  1.00 18.18  ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.842 -14.308 7.680  1.00 16.82  ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 20.952 -14.244 8.830  1.00 17.28  ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.653 -13.598 8.419  1.00 16.45  ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.597 -12.794 7.479  1.00 16.53  ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.576 -13.518 10.032 1.00 17.15  ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.140 -12.123 9.737  1.00 17.89  ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.166 -10.967 9.633  1.00 19.88  ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.463 -9.992  8.901  1.00 22.61  ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.117 -10.985 10.311 1.00 17.31  ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.590 -13.969 9.120  1.00 16.39  ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.271 -13.426 8.848  1.00 15.42  ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.505 -13.296 10.161 1.00 15.02  ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.062 -14.295 10.722 1.00 14.80  ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.561 -14.280 7.784  1.00 16.43  ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.239 -13.762 7.310  1.00 19.21  ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.595 -13.024 8.058  1.00 23.39  ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.821 -14.149 6.186  1.00 20.18  ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.321 -12.051 10.620 1.00 14.62  ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.625 -11.781 11.843 0.50 14.56  ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.610 -11.815 11.869 0.50 14.84  ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.163 -12.276 11.786 1.00 14.89  ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.645 -12.759 12.781 1.00 15.70  ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.669 -10.279 12.117 0.50 17.52  ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.609 -10.335 12.264 0.50 18.42  ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 14.984 -9.968  13.310 0.50 21.11  ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 16.889 -9.760  12.422 0.50 23.19  ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.525 -12.141 10.609 1.00 13.92  ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.139 -12.581 10.489 1.00 14.17  ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.008 -14.076 10.665 1.00 14.39  ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.885 -14.497 10.949 1.00 16.04  ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.528 -12.124 9.172  1.00 17.91  ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.963 -12.914 8.081  1.00 23.36  ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.071 -14.847 10.475 1.00 13.44  ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.014 -16.315 10.626 1.00 13.23  ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.665 -16.800 11.940 1.00 12.86  ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.653 -18.007 12.209 1.00 12.72  ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.753 -17.000 9.439  1.00 14.40  ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.010 -16.783 8.118  1.00 14.34  ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.728 -17.407 6.943  1.00 14.40  ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.708 -18.869 7.045  1.00 13.41  ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.753 -19.683 5.986  1.00 14.02  ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.794 -19.187 4.745  1.00 16.40  ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.637 -20.994 6.150  1.00 14.96  ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.316 -15.907 12.677 1.00 13.36  ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.138 -16.284 13.835 1.00 12.36  ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.257 -17.268 13.457 1.00 11.97  ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.614 -18.138 14.260 1.00 12.73  ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.306 -16.875 15.017 1.00 12.76  ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.107 -17.149 16.290 1.00 12.70  ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 15.958 -16.292 16.670 1.00 14.15  ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.864 -18.193 16.955 1.00 13.88  ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.844 -17.096 12.249 1.00 11.65  ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 17.967 -17.981 11.853 1.00 12.30  ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.221 -17.227 11.574 1.00 14.17  ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.176 -16.124 11.030 1.00 14.48  ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.646 -18.811 10.592 1.00 12.77  ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.554 -19.880 10.766 1.00 13.84  ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.315 -20.575 9.397  1.00 15.12  ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 16.953 -20.927 11.816 1.00 15.54  ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.368 -17.874 11.874 1.00 13.60  ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.663 -17.339 11.491 1.00 13.50  ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.527 -18.538 11.113 1.00 12.98  ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.459 -19.596 11.754 1.00 13.82  ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.297 -16.506 12.629 1.00 14.30  ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.662 -15.880 12.333 1.00 14.88  ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.849 -14.584 13.110 1.00 15.55  ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.820 -16.863 12.689 1.00 16.21  ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.316 -18.376 10.058 1.00 13.06  ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.222 -19.416 9.580  1.00 13.72  ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.614 -18.829 9.566  1.00 14.39  ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.831 -17.732 9.004  1.00 15.20  ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.826 -19.910 8.155  1.00 13.96  ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.846 -20.940 7.635  1.00 16.19  ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.414 -20.517 8.171  1.00 14.40  ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.551 -19.534 10.192 1.00 15.14  ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 27.953 -19.141 10.205 1.00 14.86  ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.793 -20.241 9.547  1.00 16.46  ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.356 -21.381 9.354  1.00 17.30  ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.407 -18.860 11.632 1.00 15.51  ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.268 -20.020 12.450 1.00 17.00  ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.024 -19.862 9.176  1.00 16.94  ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 30.914 -20.819 8.526  1.00 19.12  ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.762 -21.573 9.559  1.00 21.19  ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.110 -21.022 10.605 1.00 22.36  ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.795 -20.088 7.526  1.00 21.07  ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.627 -19.143 8.171  1.00 23.56  ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.120 -22.835 9.245  1.00 22.31  ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 32.941 -23.661 10.148 1.00 24.47  ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.171 -24.178 9.381  1.00 27.45  ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.163 -24.231 8.147  1.00 27.74  ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.107 -24.903 10.599 1.00 25.95  ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.858 -25.712 9.453  1.00 27.54  ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.775 -24.539 11.217 1.00 27.03  ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.183 -24.634 10.113 1.00 29.40  ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.352 -25.259 9.497  1.00 31.53  ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.116 -26.771 9.381  1.00 32.60  ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.529 -27.383 8.395  1.00 34.95  ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.627 -24.929 10.291 1.00 34.68  ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.388 -25.219 11.667 1.00 38.56  ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.023 -23.461 10.174 1.00 35.45  ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.439 -27.375 10.368 1.00 31.52  ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.151 -28.808 10.357 1.00 31.49  ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 33.942 -29.144 9.493  1.00 31.11  ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.021 -28.338 9.383  1.00 31.14  ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 34.922 -29.306 11.779 1.00 32.24  ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 33.923 -30.336 8.911  1.00 30.33  ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.827 -30.786 8.055  1.00 29.87  ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.682 -31.306 8.918  1.00 28.55  ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 31.888 -32.160 9.779  1.00 30.14  ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.332 -31.900 7.108  1.00 32.87  ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.240 -32.630 6.320  1.00 38.36  ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 31.726 -31.844 5.133  1.00 45.43  ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.296 -30.826 4.721  1.00 48.25  ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 30.639 -32.312 4.546  1.00 47.73  ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.482 -30.802 8.659  1.00 23.51  ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.261 -31.197 9.365  1.00 21.67  ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.581 -32.326 8.636  1.00 21.77  ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.531 -32.332 7.393  1.00 23.36  ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 27.995 -33.245 9.406  1.00 19.99  ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.400 -34.444 8.820  1.00 20.47  ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 25.904 -34.576 8.986  1.00 20.32  ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.355 -35.675 8.694  1.00 21.93  ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.102 -35.697 9.330  1.00 21.79  ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 29.866 -35.751 8.970  1.00 26.88  ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.209 -33.498 9.380  1.00 16.64  ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.736 -33.596 9.445  1.00 17.13  ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.171 -33.598 8.036  1.00 18.60  ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.667 -32.899 7.138  1.00 21.23  ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.115 -32.425 10.256 1.00 17.00  ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.459 -32.434 11.726 1.00 22.40  ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 23.766 -33.521 12.261 1.00 23.48  ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.432 -31.363 12.356 1.00 21.51  ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.136 -34.391 7.827  1.00 17.97  ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.439 -34.421 6.542  1.00 18.84  ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.216 -33.513 6.691  1.00 16.86  ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.444 -33.712 7.624  1.00 17.78  ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 20.928 -35.854 6.254  1.00 23.45  ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.080 -36.682 5.927  1.00 27.85  ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 19.912 -35.914 5.093  1.00 25.39  ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.002 -32.606 5.763  1.00 15.23  ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.811 -31.757 5.771  1.00 14.59  ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.686 -32.421 4.959  1.00 15.28  ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 17.883 -32.886 3.802  1.00 15.53  ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.109 -30.396 5.149  1.00 16.09  ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.359 -29.731 5.765  1.00 18.33  ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.870 -29.446 5.258  1.00 16.06  ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.214 -29.484 7.271  1.00 20.74  ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.500 -32.498 5.555  1.00 13.45  ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.350 -33.035 4.846  1.00 13.36  ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 14.949 -32.092 3.704  1.00 13.09  ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 14.961 -30.859 3.842  1.00 13.96  ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.195 -33.110 5.830  1.00 13.71  ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.513 -32.682 2.580  1.00 12.56  ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 13.991 -31.922 1.406  1.00 12.52  ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.653 -32.589 1.107  1.00 13.38  ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.581 -33.580 0.359  1.00 14.04  ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 14.976 -32.017 0.238  1.00 12.76  ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.376 -31.513 0.585  1.00 14.91  ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.397 -30.023 0.937  1.00 14.72  ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.789 -29.610 1.185  1.00 16.16  ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.147 -28.481 1.772  1.00 16.93  ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.234 -27.647 2.219  1.00 14.85  ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.437 -28.209 1.985  1.00 19.38  ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.591 -32.034 1.708  1.00 12.11  ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.299 -32.711 1.747  1.00 12.77  ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.205  -31.785 2.258  1.00 13.57  ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.470  -30.687 2.714  1.00 13.89  ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.399 -33.923 2.691  1.00 13.02  ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.578 -33.451 4.459  1.00 12.81  ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 7.961  -32.312 2.289  1.00 14.33  ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.840  -31.625 2.894  1.00 14.50  ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.237  -32.407 4.056  1.00 13.89  ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.044  -32.273 4.337  1.00 14.54  ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.766  -31.269 1.862  1.00 17.15  ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.080  -32.439 1.219  1.00 19.97  ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.447  -33.606 1.504  1.00 20.41  ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.152  -32.202 0.382  1.00 26.98  ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.042  -33.193 4.760  1.00 13.38  ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.547  -33.905 5.958  1.00 12.89  ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.891  -32.967 6.957  1.00 12.84  ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.320  -31.822 7.144  1.00 12.28  ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.691  -34.612 6.675  1.00 12.79  ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.274  -36.107 5.815  1.00 14.39  ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.875  -33.522 7.630  1.00 11.92  ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.190  -32.890 8.750  1.00 12.19  ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.201  -33.807 9.979  1.00 12.85  ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.428  -33.571 10.897 1.00 13.04  ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.765  -32.501 8.387  1.00 12.75  ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.756  -31.246 7.486  1.00 14.66  ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.341  -30.840 7.197  1.00 16.20  ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.797  -31.045 6.068  1.00 18.08  ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.652  -30.296 8.217  1.00 13.85  ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.071  -34.818 10.015 1.00 13.91  ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.231  -35.630 11.229 1.00 14.22  ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.728  -35.818 11.415 1.00 13.79  ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.508  -35.897 10.436 1.00 14.31  ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.533  -36.978 11.158 1.00 18.43  ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.102  -37.777 10.145 1.00 21.56  ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.063  -36.868 10.889 1.00 21.05  ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.127  -35.818 12.683 1.00 12.94  ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.553  -35.937 13.002 1.00 13.72  ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.754  -36.036 14.499 1.00 11.82  ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.803  -36.326 15.233 1.00 13.22  ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.019 -35.917 14.912 1.00 11.34  ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.407 -36.086 16.323 1.00 11.79  ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.264 -34.898 16.678 1.00 11.95  ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.204 -34.599 15.952 1.00 12.66  ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.178 -37.425 16.535 1.00 11.92  ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.693 -37.550 17.988 1.00 13.66  ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.279 -38.607 16.184 1.00 14.07  ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.021 -34.270 17.851 1.00 11.50  ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 11.907 -33.177 18.301 1.00 11.48  ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.539 -33.453 19.647 1.00 12.06  ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 11.964 -34.175 20.474 1.00 12.53  ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.200 -31.782 18.317 1.00 11.95  ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.278 -31.505 19.490 1.00 12.12  ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.009  -32.075 19.546 1.00 13.03  ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.680 -30.671 20.537 1.00 12.78  ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.125  -31.793 20.588 1.00 14.56  ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.808  -30.389 21.603 1.00 13.15  ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.532  -30.954 21.619 1.00 13.92  ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.661  -30.682 22.627 1.00 14.95  ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.713 -32.889 19.862 1.00 11.87  ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.389 -32.989 21.142 1.00 12.28  ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.969 -31.827 22.035 1.00 12.63  ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.141 -30.665 21.684 1.00 12.86  ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.921 -33.068 20.976 1.00 13.43  ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.567 -33.209 22.330 1.00 13.30  ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.398 -34.365 23.079 1.00 14.36  ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.356 -32.193 22.859 1.00 15.74  ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.975 -34.509 24.355 1.00 15.11  ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.917 -32.314 24.141 1.00 15.99  ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.731 -33.476 24.870 1.00 16.34  ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.284 -33.611 26.146 1.00 20.18  ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.539 -32.168 23.259 1.00 12.90  ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.133 -31.195 24.278 1.00 12.82  ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.123 -31.257 25.471 1.00 13.88  ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 14.007 -32.167 26.308 1.00 14.69  ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.709 -31.521 24.701 1.00 13.13  ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 11.085 -30.459 26.032 1.00 15.51  ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 15.038 -30.290 25.531 1.00 13.81  ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 16.052 -30.346 26.586 1.00 15.37  ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.485 -30.208 27.991 1.00 15.92  ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.984 -30.872 28.914 1.00 17.09  ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.124 -29.307 26.301 1.00 19.22  ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.667 -27.987 26.425 1.00 24.90  ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.370 -29.444 28.151 1.00 15.01  ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.762 -29.284 29.492 1.00 15.55  ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 13.054 -30.543 30.018 1.00 16.54  ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.604 -30.561 31.182 1.00 17.13  ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.813 -28.094 29.497 1.00 15.44  ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.706 -28.319 28.646 1.00 16.11  ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.970 -31.600 29.209 1.00 14.94  ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.459 -32.900 29.581 1.00 15.24  ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.488 -34.000 29.383 1.00 15.69  ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.206 -35.179 29.652 1.00 16.75  ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.173 -33.207 28.806 1.00 17.28  ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 10.041 -32.241 29.148 1.00 16.91  ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.441  -32.561 30.532 1.00 18.72  ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.338  -31.654 30.909 1.00 19.39  ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.483  -30.522 31.582 1.00 24.43  ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.690  -30.111 31.958 1.00 24.11  ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.418  -29.801 31.915 1.00 26.07  ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.670 -33.664 28.805 1.00 16.34  ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.685 -34.654 28.387 1.00 16.62  ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 15.046 -35.787 27.598 1.00 18.84  ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.300 -36.963 27.854 1.00 20.91  ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.483 -35.209 29.594 1.00 19.38  ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.260 -34.151 30.327 1.00 23.40  ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.565 -33.759 29.703 1.00 31.96  ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 19.410 -33.079 30.681 1.00 37.72  ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 19.399 -31.763 30.892 1.00 41.80  ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.601 -30.974 30.182 1.00 40.95  ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 20.189 -31.228 31.810 1.00 43.16  ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.138 -35.426 26.672 1.00 17.94  ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.370 -36.440 25.964 1.00 18.26  ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.102 -35.977 24.547 1.00 15.49  ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.996 -34.769 24.282 1.00 14.87  ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.951 -36.636 26.660 1.00 23.06  ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.897 -37.750 27.707 1.00 34.93  ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.459 -37.929 28.164 1.00 41.59  ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 10.218 -39.228 28.917 1.00 47.81  ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.647 -39.156 30.341 1.00 49.78  ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.875 -36.950 23.684 1.00 13.34  ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.365 -36.685 22.333 1.00 13.08  ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.876 -36.928 22.329 1.00 16.12  ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.378 -37.907 22.955 1.00 18.74  ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.035 -37.631 21.318 1.00 13.33  ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.506 -37.381 21.169 1.00 13.91  ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.051 -36.635 20.125 1.00 17.04  ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.509 -37.875 21.924 1.00 14.40  ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.368 -36.734 20.284 1.00 14.81  ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.681 -37.415 21.355 1.00 18.40  ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.118 -36.136 21.549 1.00 13.12  ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.664  -36.321 21.434 1.00 13.50  ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.286  -36.421 19.972 1.00 13.35  ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.708  -35.577 19.172 1.00 13.59  ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.906  -35.121 22.025 1.00 14.24  ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.037  -35.012 23.519 1.00 14.95  ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.315  -35.848 24.354 1.00 16.12  ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.812  -34.013 24.108 1.00 15.75  ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.400  -35.736 25.735 1.00 17.69  ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.887  -33.886 25.491 1.00 17.10  ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.202  -34.774 26.292 1.00 18.40  ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.251  -34.610 27.672 1.00 20.26  ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.473  -37.408 19.592 1.00 12.82  ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.929  -37.463 18.218 1.00 13.78  ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.749  -36.484 18.110 1.00 14.81  ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.886  -36.463 19.020 1.00 16.39  ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.444  -38.927 18.100 1.00 14.77  ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.055  -39.303 19.532 1.00 15.44  ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.975  -38.513 20.453 1.00 14.60  ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.692  -35.705 17.034 1.00 13.58  ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.614  -34.728 16.857 1.00 14.37  ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.194  -34.639 15.404 1.00 12.89  ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 4.981  -34.856 14.490 1.00 14.58  ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.071  -33.321 17.295 1.00 16.05  ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.119  -33.191 18.842 1.00 17.48  ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.393  -32.869 16.625 1.00 17.49  ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 2.952  -34.166 15.208 1.00 12.91  ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.510  -33.617 13.944 1.00 12.76  ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.826  -32.099 13.972 1.00 13.06  ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.762  -31.455 15.051 1.00 13.45  ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 1.007  -33.806 13.759 1.00 16.50  ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.700  -35.182 13.684 1.00 20.50  ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.159  -31.511 12.825 1.00 12.05  ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.479  -30.087 12.806 1.00 12.13  ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.882  -29.449 11.549 1.00 12.34  ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.598  -30.141 10.564 1.00 13.00  ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.987  -29.806 13.002 1.00 12.28  ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.912  -30.520 12.036 1.00 11.70  ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.367  -31.813 12.295 1.00 12.30  ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.305  -29.911 10.848 1.00 12.24  ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.229  -32.466 11.388 1.00 13.54  ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.170  -30.557 9.959  1.00 12.76  ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.613  -31.837 10.221 1.00 12.59  ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.635  -28.131 11.599 1.00 12.29  ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.004  -27.423 10.479 1.00 12.94  ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.960  -27.112 9.329  1.00 14.15  ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.138  -27.483 9.351  1.00 14.77  ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.355  -26.145 11.032 1.00 14.81  ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.320  -25.193 11.492 1.00 15.64  ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.436  -26.496 8.298  1.00 13.57  ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.255  -26.087 7.149  1.00 13.72  ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.930  -24.762 7.487  1.00 14.03  ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.325  -23.925 8.180  1.00 17.24  ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.340  -25.918 5.915  1.00 15.64  ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.654  -27.221 5.565  1.00 18.86  ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 1.075  -27.159 4.146  1.00 27.76  ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.780  -28.551 3.625  1.00 36.71  ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 1.429  -28.828 2.279  1.00 43.09  ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.127  -24.475 6.956  1.00 14.12  ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.799  -23.201 7.291  1.00 15.25  ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 4.941  -21.990 6.947  1.00 16.27  ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.405  -21.886 5.846  1.00 18.03  ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.076  -23.215 6.465  1.00 16.31  ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.316  -24.666 6.133  1.00 18.27  ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.959  -25.341 6.094  1.00 13.96  ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.839  -21.061 7.893  1.00 15.15  ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 3.961  -19.907 7.686  1.00 17.22  ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.365  -18.745 8.567  1.00 15.53  ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.324  -18.833 9.363  1.00 15.01  ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.511  -20.318 7.932  1.00 21.81  ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.265  -20.503 9.320  1.00 24.85  ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.663  -17.612 8.389  1.00 15.84  ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.872  -16.385 9.135  1.00 16.63  ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 2.998  -16.487 10.381 1.00 17.35  ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.744  -16.544 10.248 1.00 19.02  ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.329  -15.230 8.291  1.00 19.23  ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.246  -14.240 7.601  1.00 25.04  ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.424  -12.976 7.276  1.00 27.32  ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.396  -13.797 8.407  1.00 25.88  ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.609  -16.460 11.579 1.00 16.18  ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.933  -16.625 12.868 1.00 17.51  ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.323  -15.503 13.809 1.00 18.47  ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.496  -15.166 13.908 1.00 17.31  ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.317  -17.998 13.454 1.00 19.87  ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.795  -19.115 12.506 1.00 22.85  ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.794  -18.152 14.913 1.00 22.08  ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 2.915  -20.485 12.910 1.00 26.19  ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.352  -14.923 14.523 1.00 19.19  ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.632  -13.854 15.467 1.00 20.01  ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.366  -14.378 16.698 1.00 19.30  ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 2.984  -15.399 17.267 1.00 20.94  ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.274  -13.216 15.907 1.00 23.29  ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.452  -12.139 16.958 1.00 25.52  ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.367  -12.445 18.311 1.00 28.35  ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 1.848  -10.871 16.604 1.00 27.67  ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.583  -11.464 19.279 1.00 29.78  ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.028  -9.876  17.579 1.00 29.92  ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 1.916  -10.197 18.903 1.00 29.94  ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.464  -13.699 17.067 1.00 18.68  ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.276  -14.047 18.239 1.00 18.59  ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.354  -12.803 19.136 1.00 19.41  ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.759  -11.725 18.709 1.00 18.88  ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.688  -14.473 17.777 1.00 16.70  ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.564  -14.834 18.996 1.00 16.98  ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.590  -15.665 16.815 1.00 16.42  ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.051  -13.010 20.450 1.00 21.14  ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.101  -11.929 21.414 1.00 22.55  ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.498  -11.362 21.574 1.00 21.43  ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.467  -12.074 21.356 1.00 20.55  ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.615  -12.446 22.778 1.00 27.17  ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.237  -13.074 22.767 1.00 31.37  ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.091  -12.116 23.015 1.00 37.87  ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 0.933  -12.585 22.980 1.00 37.97  ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.338  -10.898 23.189 1.00 41.13  ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.616  -10.126 22.038 1.00 21.18  ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.896  -9.477  22.257 1.00 21.23  ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.690  -10.244 23.308 1.00 19.60  ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.131  -10.880 24.205 1.00 20.73  ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.689  -8.029  22.757 1.00 22.83  ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 9.994  -10.191 23.147 1.00 17.31  ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 10.940 -10.755 24.108 1.00 16.39  ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.101 -9.765  24.222 1.00 17.35  ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.037 -8.705  23.594 1.00 18.66  ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.444 -12.136 23.636 1.00 17.13  ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.191 -11.973 22.445 1.00 16.73  ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.139 -10.104 24.988 1.00 17.62  ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.312 -9.217  25.062 1.00 17.91  ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.091 -9.254  23.748 1.00 18.87  ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 15.876 -8.337  23.501 1.00 19.33  ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.219 -9.661  26.198 1.00 22.50  ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.620 -11.125 26.136 1.00 28.27  ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 14.809 -12.153 26.923 1.00 36.37  ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.441 -12.885 27.726 1.00 40.33  ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.572 -12.268 26.716 1.00 32.80  ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 14.819 -10.236 22.854 1.00 18.58  ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.541 -10.413 21.622 1.00 18.94  ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.891 -9.761  20.441 1.00 18.70  ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.591 -9.467  19.469 1.00 21.28  ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.681 -11.924 21.354 1.00 18.12  ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.304 -12.695 22.491 1.00 17.83  ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.667 -12.604 22.765 1.00 21.27  ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.534 -13.502 23.311 1.00 18.46  ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.242 -13.316 23.820 1.00 22.68  ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.101 -14.232 24.357 1.00 20.83  ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.462 -14.169 24.579 1.00 23.93  ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.025 -14.883 25.620 1.00 27.86  ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.554 -9.646  20.436 1.00 17.66  ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.809 -9.132  19.303 1.00 19.17  ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.597 -8.377  19.763 1.00 21.87  ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 10.949 -8.724  20.770 1.00 21.01  ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.220 -10.287 18.434 1.00 18.07  ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.233 -11.201 17.815 1.00 16.69  ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.432 -12.481 18.310 1.00 15.73  ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 13.990 -10.801 16.713 1.00 16.53  ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.339 -13.346 17.738 1.00 15.93  ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 14.900 -11.665 16.125 1.00 16.47  ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.047 -12.950 16.613 1.00 16.34  ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 16.010 -13.758 16.057 1.00 15.40  ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.181 -7.370  18.972 1.00 25.15  ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.884  -6.789  19.223 1.00 24.89  ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.749  -7.780  18.879 1.00 23.67  ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 8.995  -8.766  18.148 1.00 22.14  ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.845  -5.606  18.220 1.00 26.74  ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.737 -6.001  17.165 1.00 27.68  ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.793 -6.873  17.720 1.00 26.30  ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.512  -7.526  19.277 1.00 23.92  ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.342  -8.337  18.874 1.00 24.41  ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.255  -8.254  17.323 1.00 23.72  ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.450  -7.174  16.760 1.00 25.19  ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.050  -7.795  19.484 1.00 26.11  ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.177  -9.408  16.651 1.00 21.59  ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.264  -9.414  15.195 1.00 21.20  ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.718  -10.703 14.643 1.00 20.72  ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.474  -11.636 15.390 1.00 21.17  ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.750  -9.270  14.804 1.00 21.18  ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.560  -10.590 15.042 1.00 17.65  ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 10.000 -10.400 15.274 1.00 17.79  ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.866 -11.492 14.824 1.00 16.91  ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 10.959 -12.696 15.399 1.00 17.74  ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.809 -13.597 14.921 1.00 16.25  ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.230 -12.988 16.485 1.00 17.42  ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.614  -10.778 13.304 1.00 20.63  ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.298  -12.056 12.686 1.00 20.85  ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.620  -12.694 12.306 1.00 18.05  ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.460  -12.073 11.636 1.00 18.56  ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.518  -11.846 11.393 1.00 22.98  ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.093  -11.472 11.650 1.00 27.26  ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.127  -12.442 11.853 1.00 29.45  ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.714  -10.143 11.748 1.00 31.58  ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.803  -12.101 12.091 1.00 33.42  ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.402  -9.791  12.026 1.00 33.57  ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.459  -10.776 12.227 1.00 35.87  ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.862 -10.444 12.409 1.00 40.28  ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.813  -13.942 12.761 1.00 15.64  ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 7.979  -14.719 12.362 1.00 14.65  ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.570  -15.593 11.191 1.00 13.88  ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.514  -16.243 11.227 1.00 15.42  ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.479  -15.541 13.554 1.00 15.22  ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.676  -16.447 13.163 1.00 14.64  ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.422 -16.958 14.383 1.00 14.23  ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.655 -16.240 15.360 1.00 15.06  ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.884 -18.227 14.309 1.00 13.23  ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.392  -15.590 10.134 1.00 13.58  ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.131  -16.350 8.934  1.00 13.09  ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.790  -17.734 8.966  1.00 12.75  ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.653  -18.003 9.816  1.00 13.67  ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.592  -15.600 7.683  1.00 15.59  ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.004 -15.450 7.757  1.00 17.55  ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.259  -18.651 8.093  1.00 13.78  ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.794  -20.006 7.920  1.00 13.28  ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.718  -20.792 9.253  1.00 13.72  ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.564  -21.629 9.517  1.00 13.08  ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.238 -19.958 7.385  1.00 13.85  ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.343 -19.293 6.027  1.00 14.54  ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.324 -20.036 4.852  1.00 16.90  ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.417 -17.975 5.708  1.00 16.27  ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.409 -19.157 3.851  1.00 17.07  ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.480 -17.901 4.315  1.00 17.92  ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.685  -20.535 10.054 1.00 13.61  ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.525  -21.160 11.377 1.00 13.45  ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.448  -22.253 11.286 1.00 14.33  ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.403  -22.058 10.631 1.00 14.68  ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.131  -20.069 12.424 1.00 14.43  ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.064  -20.481 13.896 1.00 15.59  ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.445  -20.873 14.393 1.00 15.92  ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.582  -19.318 14.771 1.00 20.11  ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.682  -23.381 11.972 1.00 13.60  ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.706  -24.494 11.997 1.00 12.80  ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.353  -24.785 13.432 1.00 13.46  ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.266  -24.805 14.280 1.00 14.74  ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.380  -25.747 11.435 1.00 13.12  ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.777  -25.511 9.981  1.00 14.84  ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.858  -26.795 9.355  1.00 15.95  ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.341  -26.629 10.420 1.00 15.24  ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.075  -24.983 13.744 1.00 12.89  ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.678  -25.257 15.130 1.00 12.21  ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.306  -26.712 15.351 1.00 12.19  ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.780  -27.386 14.455 1.00 12.89  ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.443  -24.413 15.550 1.00 14.78  ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.650  -22.914 15.461 1.00 15.00  ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.397  -22.177 15.950 1.00 16.98  ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.886  -22.439 16.217 1.00 16.90  ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.507  -27.165 16.600 1.00 12.57  ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.047  -28.502 17.046 1.00 12.08  ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.509  -28.336 18.454 1.00 12.42  ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.839  -27.370 19.171 1.00 13.65  ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.219  -29.491 17.089 1.00 13.13  ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.676  -29.287 18.887 1.00 12.39  ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.271  -29.370 20.285 1.00 12.85  ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.354  -30.105 21.059 1.00 14.71  ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.599  -31.310 20.827 1.00 15.91  ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.111 -30.069 20.398 1.00 14.64  ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.534 -30.123 21.859 1.00 14.96  ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.142 -29.278 19.580 1.00 16.31  ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 3.029  -29.371 21.932 1.00 14.31  ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 4.114  -29.980 22.696 1.00 16.01  ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.719  -29.036 23.681 1.00 16.44  ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.518  -27.815 23.609 1.00 16.81  ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.444  -29.631 24.658 1.00 14.97  ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.082  -28.818 25.659 1.00 15.03  ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.365  -28.150 25.138 1.00 14.88  ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.176  -28.754 24.436 1.00 13.99  ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.482  -29.715 26.862 1.00 15.85  ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.177  -28.946 27.927 1.00 16.39  ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.495  -27.991 28.669 1.00 19.31  ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.492  -28.941 28.298 1.00 17.72  ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.395  -27.475 29.502 1.00 20.06  ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.607  -28.010 29.304 1.00 19.64  ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.602  -26.932 25.613 1.00 14.67  ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.840  -26.215 25.394 1.00 14.98  ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.954  -25.080 26.413 1.00 15.56  ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.961  -24.551 26.930 1.00 16.19  ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.976  -25.716 23.953 1.00 14.97  ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 8.063  -24.651 23.734 1.00 16.05  ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.201 -24.698 26.663 1.00 15.98  ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.602 -23.561 27.499 1.00 16.83  ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.660 -22.786 26.664 1.00 16.21  ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.225 -23.315 25.688 1.00 15.69  ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.222 -24.078 28.803 1.00 18.91  ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 10.184 -24.857 29.587 1.00 20.57  ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.660 -25.505 30.875 1.00 24.32  ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.625 -24.992 31.481 1.00 28.63  ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 10.114 -26.574 31.221 1.00 23.66  ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.959 -21.508 27.007 1.00 16.85  ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.905 -20.729 26.185 1.00 16.47  ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.260 -21.412 25.917 1.00 15.69  ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.789 -21.360 24.790 1.00 15.44  ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.052 -19.424 26.978 1.00 17.64  ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.712 -19.260 27.670 1.00 18.62  ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.332 -20.685 28.060 1.00 17.68  ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.822 -22.105 26.921 1.00 15.82  ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.095 -22.802 26.774 1.00 16.27  ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 16.059 -24.011 25.852 1.00 15.78  ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.108 -24.590 25.529 1.00 15.90  ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.850 -24.412 25.429 1.00 14.30  ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.719 -25.509 24.450 1.00 13.78  ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 15.021 -25.080 23.030 1.00 12.65  ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.162 -25.950 22.153 1.00 13.33  ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.301 -26.117 24.509 1.00 13.11  ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 13.078 -26.909 25.798 1.00 17.01  ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 14.021 -27.548 26.268 1.00 16.64  ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.960 -26.880 26.325 1.00 15.98  ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.174 -23.745 22.772 1.00 12.30  ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.506 -23.286 21.422 1.00 12.67  ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.787 -23.934 20.948 1.00 14.30  ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.743 -24.049 21.725 1.00 14.29  ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.633 -21.763 21.410 1.00 12.94  ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.035 -20.899 21.442 1.00 15.22  ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.775 -24.405 19.716 1.00 13.37  ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.943 -25.064 19.140 1.00 14.03  ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.770 -26.563 19.039 1.00 13.43  ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.532 -27.236 18.337 1.00 14.09  ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.793 -27.116 19.776 1.00 12.58  ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.546 -28.559 19.688 1.00 12.80  ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.101 -28.940 18.275 1.00 12.72  ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.304 -28.221 17.658 1.00 13.14  ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.615 -30.055 17.756 1.00 12.65  ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.288 -30.424 16.376 1.00 12.99  ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 14.968 -31.130 16.236 1.00 12.53  ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.615 -31.981 17.070 1.00 13.19  ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.469 -31.272 15.822 1.00 16.63  ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.636 -30.322 15.429 1.00 19.44  ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.054 -32.097 14.569 1.00 18.94  ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 19.956 -31.111 14.948 1.00 22.17  ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.247 -30.800 15.156 1.00 11.63  ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.067 -31.530 14.680 1.00 11.49  ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.555 -32.327 13.460 1.00 11.83  ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.153 -31.761 12.530 1.00 12.59  ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 11.977 -30.523 14.253 1.00 11.90  ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.782 -31.132 13.533 1.00 12.27  ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 9.960  -32.082 14.471 1.00 14.18  ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.854  -30.012 13.013 1.00 14.00  ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.305 -33.660 13.454 1.00 12.26  ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.731 -34.547 12.364 1.00 12.99  ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.551 -35.325 11.868 1.00 13.55  ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.725 -35.779 12.654 1.00 14.70  ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.794 -35.559 12.920 1.00 16.26  ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.219 -35.071 12.989 1.00 25.13  ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.172 -36.168 13.541 1.00 29.68  ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.315 -37.287 12.609 1.00 32.86  ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.184 -37.305 11.590 1.00 34.57  ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 18.996 -36.293 11.392 1.00 31.97  ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.247 -38.353 10.776 1.00 36.24  ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.489 -35.557 10.569 1.00 12.87  ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.506 -36.487 9.974  1.00 13.80  ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.313 -37.677 9.425  1.00 15.78  ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.552 -37.756 9.538  1.00 16.21  ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.708 -35.794 8.856  1.00 12.73  ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.746 -35.304 7.451  1.00 12.85  ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.579 -38.577 8.705  1.00 16.34  ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.261 -39.720 8.106  1.00 18.49  ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.334 -39.325 7.055  1.00 18.83  ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.179 -40.148 6.689  1.00 20.51  ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.221 -40.672 7.492  1.00 21.78  ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.568 -40.097 6.233  1.00 24.22  ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.543  -41.039 5.649  1.00 32.81  ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.344  -40.819 5.794  1.00 34.73  ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 9.988  -42.074 4.941  1.00 35.11  ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.336 -38.069 6.556  1.00 15.88  ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.283 -37.603 5.541  1.00 15.85  ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.507 -36.888 6.084  1.00 16.86  ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.437 -36.638 5.328  1.00 18.81  ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.598 -36.705 4.515  1.00 15.92  ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.410 -37.354 3.883  1.00 14.81  ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.135 -36.967 4.206  1.00 12.94  ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.355 -38.318 2.930  1.00 18.36  ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.313 -37.734 3.500  1.00 16.31  ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.003 -38.592 2.726  1.00 18.94  ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.489 -36.506 7.363  1.00 14.20  ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.614 -35.751 7.937  1.00 14.30  ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.116 -34.599 8.808  1.00 13.10  ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 14.982 -34.604 9.300  1.00 13.04  ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 16.992 -33.635 9.005  1.00 13.36  ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.680 -32.448 9.815  1.00 13.03  ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.686 -31.516 9.136  1.00 12.93  ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 15.926 -31.103 7.972  1.00 13.82  ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 17.974 -31.682 10.148 1.00 14.00  ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.651 -30.398 10.913 1.00 15.43  ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 18.907 -32.570 10.978 1.00 15.33  ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.591 -31.167 9.817  1.00 12.12  ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.553 -30.276 9.319  1.00 12.30  ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.769 -28.857 9.775  1.00 12.65  ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.545 -27.924 9.004  1.00 12.65  ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.186 -30.789 9.792  1.00 11.90  ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.057 -29.821 9.436  1.00 13.33  ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 11.901 -32.182 9.249  1.00 12.68  ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.182 -28.694 11.040 1.00 12.58  ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.341 -27.371 11.596 1.00 13.98  ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.707 -27.427 13.059 1.00 11.78  ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.095 -28.486 13.565 1.00 12.74  ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.627 -26.271 13.717 1.00 12.44  ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.030 -26.176 15.129 1.00 11.89  ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.968 -25.467 15.945 1.00 12.55  ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.280 -24.566 15.438 1.00 12.10  ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.389 -25.463 15.330 1.00 13.11  ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.401 -24.085 14.624 1.00 14.39  ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.565 -26.358 14.918 1.00 14.77  ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.738 -23.282 14.975 1.00 15.48  ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.832 -25.820 17.240 1.00 10.47  ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.887 -25.108 18.120 1.00 10.71  ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.249 -23.617 18.141 1.00 11.38  ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.442 -23.258 18.291 1.00 11.73  ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.982 -25.665 19.559 1.00 11.38  ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.091 -24.848 20.499 1.00 13.18  ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.533 -27.136 19.587 1.00 13.61  ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.240 -22.769 17.979 1.00 11.63  ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.417 -21.333 17.983 1.00 11.57  ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.410 -20.575 18.838 1.00 13.47  ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.743 -19.467 19.293 1.00 13.09  ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.394 -20.858 16.531 1.00 12.21  ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.497 -19.436 16.390 1.00 13.01  ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.214 -21.089 19.044 1.00 13.49  ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.198  -20.388 19.863 1.00 13.31  ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.402  -21.371 20.694 1.00 13.35  ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.440  -22.563 20.420 1.00 13.01  ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.206  -19.604 18.951 1.00 13.99  ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.330  -20.512 18.256 1.00 15.47  ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 8.867  -18.696 17.934 1.00 16.06  ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.693  -20.878 21.681 1.00 13.87  ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.783  -21.729 22.429 1.00 16.22  ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.839  -20.943 23.294 1.00 16.67  ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.039  -19.766 23.511 1.00 17.10  ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.835  -21.612 23.838 1.00 16.91  ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.854  -20.976 24.712 1.00 18.97  ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.515  -21.687 24.599 1.00 19.28  ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.151  -22.204 23.549 1.00 19.81  ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.744  -21.644 25.698 1.00 20.31  ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.401  -22.225 25.742 1.00 21.69  ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.334  -23.702 25.289 1.00 20.45  ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.669 -24.100 24.703 1.00 21.68  ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.564 -21.376 24.910 1.00 24.78  ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.708 -19.989 25.432 1.00 29.97  ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.935 -19.776 26.611 1.00 31.22  ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.588 -19.032 24.549 1.00 34.31  ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.403  -24.484 25.485 1.00 18.67  ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.421  -25.884 25.049 1.00 17.74  ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.662  -26.098 23.571 1.00 16.24  ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.420  -27.194 23.067 1.00 15.97  ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.140  -25.057 22.873 1.00 15.22  ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.470  -25.107 21.460 1.00 15.50  ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 3.950  -24.869 21.338 1.00 16.03  ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.492  -24.068 22.116 1.00 18.35  ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.698  -24.007 20.694 1.00 17.44  ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.177  -24.171 20.725 1.00 21.06  ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.510 -22.850 20.408 1.00 24.09  ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.255 -25.265 19.799 1.00 21.15  ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.627  -25.562 20.457 1.00 12.94  ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.048  -25.369 20.204 1.00 13.07  ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.191  -25.003 18.741 1.00 13.42  ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.523  -25.600 17.872 1.00 12.95  ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.879  -26.600 20.581 1.00 13.94  ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.340  -27.917 20.007 1.00 16.83  ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.382  -26.399 20.323 1.00 14.27  ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.094  -24.072 18.464 1.00 12.48  ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.295  -23.618 17.087 1.00 12.47  ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.705  -23.918 16.640 1.00 11.88  ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.659  -23.744 17.398 1.00 12.75  ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.810  -24.341 15.382 1.00 11.59  ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.082 -24.732 14.776 1.00 11.71  ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.354 -23.868 13.577 1.00 12.12  ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.492  -23.703 12.700 1.00 12.29  ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.050 -26.209 14.296 1.00 13.00  ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.591  -27.188 15.373 1.00 12.06  ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.486 -27.696 16.297 1.00 12.58  ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.256  -27.590 15.455 1.00 13.44  ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.052 -28.593 17.268 1.00 12.90  ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.832  -28.488 16.443 1.00 13.87  ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.739  -28.997 17.320 1.00 13.69  ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.604 -23.380 13.501 1.00 12.01  ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.050 -22.619 12.334 1.00 11.45  ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.450 -23.604 11.260 1.00 11.55  ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.368 -24.428 11.455 1.00 11.97  ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.266 -21.775 12.739 1.00 11.91  ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.748 -23.607 10.137 1.00 11.62  ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.065 -24.514 9.034  1.00 11.52  ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.385 -24.198 8.370  1.00 11.46  ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.740 -23.005 8.206  1.00 12.47  ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.953 -24.349 7.963  1.00 13.05  ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.047 -25.360 6.841  1.00 16.72  ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.176 -26.543 7.136  1.00 16.57  ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.053 -24.947 5.661  1.00 19.28  ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.132 -25.248 7.957  1.00 12.19  ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.348 -25.037 7.172  1.00 13.09  ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.280 -25.794 5.827  1.00 13.04  ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.227 -25.714 5.046  1.00 13.89  ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.648 -25.420 7.908  1.00 13.71  ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.807 -24.591 9.198  1.00 13.69  ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.689 -26.927 8.207  1.00 14.76  ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.180 -26.506 5.528  1.00 12.26  ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.103 -27.360 4.347  1.00 11.91  ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.145 -26.594 3.046  1.00 12.20  ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.488 -27.191 2.009  1.00 13.91  ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.845 -28.234 4.385  1.00 12.77  ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.844 -29.234 5.573  1.00 13.22  ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.540 -29.968 5.546  1.00 12.06  ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.465 -29.057 5.974  1.00 12.07  ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.223  -29.438 6.228  1.00 12.20  ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.841  -30.689 5.984  1.00 12.41  ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.338  -28.557 6.698  1.00 12.99  ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.768 -25.318 3.041  1.00 12.56  ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.830 -24.530 1.788  1.00 13.49  ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.215 -23.972 1.525  1.00 14.34  ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.426 -23.447 0.427  1.00 14.80  ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.823 -23.376 1.880  1.00 15.48  ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.123 -22.379 2.984  1.00 18.02  ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.462 -22.819 4.098  1.00 17.71  ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.055 -21.120 2.707  1.00 19.43  ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.173 -24.066 2.472  1.00 14.17  ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.516 -23.474 2.299  1.00 14.09  ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.404 -24.434 1.558  1.00 14.51  ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.244 -25.154 2.112  1.00 14.77  ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.113 -23.111 3.680  1.00 14.30  ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.253 -22.147 4.515  1.00 15.49  ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.884 -21.996 5.909  1.00 16.85  ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.065 -20.802 3.835  1.00 16.49  ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.187 -24.485 0.237  1.00 14.82  ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.839 -25.534 -0.584 1.00 15.21  ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.341 -25.358 -0.624 1.00 16.11  ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.069 -26.348 -0.779 1.00 18.19  ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.277 -25.563 -2.004 1.00 15.03  ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.762 -25.603 -2.108 1.00 15.28  ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.355 -25.664 -3.597 1.00 17.31  ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.135 -26.730 -1.304 1.00 17.41  ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.823 -24.092 -0.494 1.00 15.73  ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.260 -23.816 -0.555 1.00 16.90  ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.039 -24.409 0.643  1.00 18.46  ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.271 -24.506 0.561  1.00 19.50  ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.443 -22.291 -0.640 1.00 17.13  ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.771 -21.523 0.463  1.00 16.89  ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.542 -20.919 0.425  1.00 17.54  ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.329 -21.225 1.756  1.00 17.23  ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.300 -20.265 1.626  1.00 17.45  ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.400 -20.426 2.441  1.00 17.34  ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.559 -21.525 2.376  1.00 18.73  ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.649 -19.946 3.735  1.00 18.84  ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.815 -21.018 3.647  1.00 19.98  ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.873 -20.234 4.304  1.00 19.09  ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.357 -24.873 1.708  1.00 17.52  ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.100 -25.485 2.843  1.00 19.34  ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 23.903 -26.714 2.391  1.00 23.41  ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 24.922 -27.023 3.009  1.00 24.79  ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.102 -25.912 3.965  1.00 17.79  ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.534 -24.780 4.784  1.00 16.95  ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.497 -25.316 5.773  1.00 16.62  ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.705 -24.036 5.553  1.00 17.67  ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.454 -27.371 1.304  1.00 26.02  ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.059 -28.570 0.735  1.00 30.22  ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.037 -28.396 -0.366 1.00 33.78  ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.463 -29.415 -0.919 1.00 35.66  ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 22.951 -29.475 0.216  1.00 33.78  ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 22.358 -30.241 1.344  1.00 36.99  ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 23.132 -30.676 2.237  1.00 38.88  ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 21.140 -30.370 1.379  1.00 39.38  ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.389 -27.171 -0.709 1.00 34.60  ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.359 -26.945 -1.780 1.00 37.85  ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.457 -25.977 -1.343 1.00 40.37  ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.252 -25.534 -2.185 1.00 42.07  ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.639 -26.432 -3.033 1.00 41.58  ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 24.892 -25.138 -2.805 1.00 47.86  ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 23.745 -24.907 -3.773 1.00 57.72  ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 23.385 -23.728 -4.002 1.00 58.39  ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.195 -25.908 -4.288 1.00 61.08  ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1B3W C 2 .   ? 23.665 13.676  14.949 1.00 13.66  ? 201 A1B3W A N1  1 
HETATM 2156 C  C4  . A1B3W C 2 .   ? 28.346 10.386  6.968  1.00 16.76  ? 201 A1B3W A C4  1 
HETATM 2157 C  C5  . A1B3W C 2 .   ? 27.648 11.431  7.531  1.00 16.70  ? 201 A1B3W A C5  1 
HETATM 2158 C  C6  . A1B3W C 2 .   ? 26.639 11.145  8.422  1.00 15.10  ? 201 A1B3W A C6  1 
HETATM 2159 C  C7  . A1B3W C 2 .   ? 26.088 12.568  10.192 1.00 14.13  ? 201 A1B3W A C7  1 
HETATM 2160 C  C8  . A1B3W C 2 .   ? 24.253 14.191  9.673  1.00 13.94  ? 201 A1B3W A C8  1 
HETATM 2161 C  C10 . A1B3W C 2 .   ? 22.905 14.773  11.738 1.00 15.05  ? 201 A1B3W A C10 1 
HETATM 2162 C  C13 . A1B3W C 2 .   ? 25.348 14.115  11.912 1.00 14.20  ? 201 A1B3W A C13 1 
HETATM 2163 O  O3  . A1B3W C 2 .   ? 24.507 15.653  14.256 1.00 14.49  ? 201 A1B3W A O3  1 
HETATM 2164 C  C12 . A1B3W C 2 .   ? 24.035 14.539  14.002 1.00 13.67  ? 201 A1B3W A C12 1 
HETATM 2165 C  C11 . A1B3W C 2 .   ? 23.967 14.033  12.573 1.00 13.80  ? 201 A1B3W A C11 1 
HETATM 2166 C  C9  . A1B3W C 2 .   ? 22.874 14.193  10.316 1.00 14.74  ? 201 A1B3W A C9  1 
HETATM 2167 N  N   . A1B3W C 2 .   ? 25.258 13.563  10.555 1.00 13.66  ? 201 A1B3W A N   1 
HETATM 2168 O  O2  . A1B3W C 2 .   ? 26.977 12.147  10.880 1.00 14.79  ? 201 A1B3W A O2  1 
HETATM 2169 O  O1  . A1B3W C 2 .   ? 25.838 12.175  8.914  1.00 15.22  ? 201 A1B3W A O1  1 
HETATM 2170 C  C1  . A1B3W C 2 .   ? 26.339 9.814   8.757  1.00 14.59  ? 201 A1B3W A C1  1 
HETATM 2171 O  O   . A1B3W C 2 .   ? 25.308 9.650   9.643  1.00 14.20  ? 201 A1B3W A O   1 
HETATM 2172 C  C   . A1B3W C 2 .   ? 24.951 8.305   10.017 1.00 15.39  ? 201 A1B3W A C   1 
HETATM 2173 CL CL  . A1B3W C 2 .   ? 29.593 10.742  5.812  1.00 20.90  ? 201 A1B3W A CL  1 
HETATM 2174 C  C3  . A1B3W C 2 .   ? 28.075 9.078   7.283  1.00 15.40  ? 201 A1B3W A C3  1 
HETATM 2175 C  C2  . A1B3W C 2 .   ? 27.067 8.785   8.187  1.00 15.09  ? 201 A1B3W A C2  1 
HETATM 2176 ZN ZN  . ZN    D 3 .   ? 23.165 -5.536  26.967 1.00 17.24  2 202 ZN    A ZN  1 
HETATM 2177 S  S   . DMS   E 4 .   ? 15.044 -0.385  12.185 1.00 36.73  ? 203 DMS   A S   1 
HETATM 2178 O  O   . DMS   E 4 .   ? 16.364 -0.690  12.813 1.00 28.04  ? 203 DMS   A O   1 
HETATM 2179 C  C1  . DMS   E 4 .   ? 15.121 0.291   10.513 1.00 36.50  ? 203 DMS   A C1  1 
HETATM 2180 C  C2  . DMS   E 4 .   ? 14.370 1.081   13.053 1.00 36.16  ? 203 DMS   A C2  1 
HETATM 2181 S  S   . DMS   F 4 .   ? 31.200 10.338  13.815 1.00 49.64  ? 204 DMS   A S   1 
HETATM 2182 O  O   . DMS   F 4 .   ? 30.353 9.120   14.026 1.00 49.68  ? 204 DMS   A O   1 
HETATM 2183 C  C1  . DMS   F 4 .   ? 32.894 9.846   14.125 1.00 49.72  ? 204 DMS   A C1  1 
HETATM 2184 C  C2  . DMS   F 4 .   ? 31.050 11.427  15.252 1.00 49.27  ? 204 DMS   A C2  1 
HETATM 2185 N  N1  . A1B3W G 2 .   ? 11.805 -16.781 17.972 1.00 13.61  ? 201 A1B3W C N1  1 
HETATM 2186 C  C4  . A1B3W G 2 .   ? 7.825  -20.042 26.334 1.00 17.26  ? 201 A1B3W C C4  1 
HETATM 2187 C  C5  . A1B3W G 2 .   ? 8.526  -19.011 25.737 1.00 16.37  ? 201 A1B3W C C5  1 
HETATM 2188 C  C6  . A1B3W G 2 .   ? 9.435  -19.315 24.744 1.00 15.21  ? 201 A1B3W C C6  1 
HETATM 2189 C  C7  . A1B3W G 2 .   ? 9.905  -17.869 22.962 1.00 14.58  ? 201 A1B3W C C7  1 
HETATM 2190 C  C8  . A1B3W G 2 .   ? 11.810 -16.275 23.311 1.00 14.48  ? 201 A1B3W C C8  1 
HETATM 2191 C  C10 . A1B3W G 2 .   ? 12.936 -15.698 21.125 1.00 13.94  ? 201 A1B3W C C10 1 
HETATM 2192 C  C13 . A1B3W G 2 .   ? 10.516 -16.333 21.197 1.00 13.28  ? 201 A1B3W C C13 1 
HETATM 2193 O  O3  . A1B3W G 2 .   ? 11.140 -14.776 18.777 1.00 13.19  ? 201 A1B3W C O3  1 
HETATM 2194 C  C12 . A1B3W G 2 .   ? 11.593 -15.915 18.969 1.00 12.84  ? 201 A1B3W C C12 1 
HETATM 2195 C  C11 . A1B3W G 2 .   ? 11.806 -16.443 20.377 1.00 12.99  ? 201 A1B3W C C11 1 
HETATM 2196 C  C9  . A1B3W G 2 .   ? 13.122 -16.289 22.529 1.00 14.48  ? 201 A1B3W C C9  1 
HETATM 2197 N  N   . A1B3W G 2 .   ? 10.729 -16.897 22.535 1.00 14.05  ? 201 A1B3W C N   1 
HETATM 2198 O  O2  . A1B3W G 2 .   ? 8.932  -18.263 22.372 1.00 14.16  ? 201 A1B3W C O2  1 
HETATM 2199 O  O1  . A1B3W G 2 .   ? 10.261 -18.304 24.209 1.00 15.07  ? 201 A1B3W C O1  1 
HETATM 2200 C  C1  . A1B3W G 2 .   ? 9.638  -20.645 24.347 1.00 15.61  ? 201 A1B3W C C1  1 
HETATM 2201 O  O   . A1B3W G 2 .   ? 10.581 -20.829 23.372 1.00 14.77  ? 201 A1B3W C O   1 
HETATM 2202 C  C   . A1B3W G 2 .   ? 10.822 -22.182 22.922 1.00 14.89  ? 201 A1B3W C C   1 
HETATM 2203 CL CL  . A1B3W G 2 .   ? 6.583  -19.654 27.505 1.00 20.70  ? 201 A1B3W C CL  1 
HETATM 2204 C  C3  . A1B3W G 2 .   ? 8.012  -21.354 25.965 1.00 16.57  ? 201 A1B3W C C3  1 
HETATM 2205 C  C2  . A1B3W G 2 .   ? 8.914  -21.660 24.957 1.00 16.63  ? 201 A1B3W C C2  1 
HETATM 2206 S  S   . DMS   H 4 .   ? 3.851  -20.339 19.325 1.00 40.81  ? 202 DMS   C S   1 
HETATM 2207 O  O   . DMS   H 4 .   ? 4.572  -19.093 18.804 1.00 40.84  ? 202 DMS   C O   1 
HETATM 2208 C  C1  . DMS   H 4 .   ? 3.294  -20.085 21.035 1.00 41.09  ? 202 DMS   C C1  1 
HETATM 2209 C  C2  . DMS   H 4 .   ? 4.980  -21.657 19.637 1.00 40.57  ? 202 DMS   C C2  1 
HETATM 2210 ZN ZN  . ZN    I 3 .   ? 10.475 -35.510 5.540  1.00 13.55  2 203 ZN    C ZN  1 
HETATM 2211 S  S   . DMS   J 4 .   ? 18.958 -31.360 19.189 1.00 35.84  ? 204 DMS   C S   1 
HETATM 2212 O  O   . DMS   J 4 .   ? 19.254 -30.862 20.605 1.00 38.89  ? 204 DMS   C O   1 
HETATM 2213 C  C1  . DMS   J 4 .   ? 19.576 -33.104 19.092 1.00 36.02  ? 204 DMS   C C1  1 
HETATM 2214 C  C2  . DMS   J 4 .   ? 20.465 -30.694 18.445 1.00 37.08  ? 204 DMS   C C2  1 
HETATM 2215 O  O   . HOH   K 5 .   ? 11.663 -1.807  28.008 1.00 26.91  ? 301 HOH   A O   1 
HETATM 2216 O  O   . HOH   K 5 .   ? 6.824  -1.909  24.149 1.00 35.82  ? 302 HOH   A O   1 
HETATM 2217 O  O   . HOH   K 5 .   ? 14.756 22.117  24.350 1.00 20.64  ? 303 HOH   A O   1 
HETATM 2218 O  O   . HOH   K 5 .   ? 13.040 13.219  16.689 1.00 131.09 ? 304 HOH   A O   1 
HETATM 2219 O  O   . HOH   K 5 .   ? 23.782 7.370   28.154 1.00 21.03  ? 305 HOH   A O   1 
HETATM 2220 O  O   . HOH   K 5 .   ? 11.012 21.156  24.496 1.00 28.20  ? 306 HOH   A O   1 
HETATM 2221 O  O   . HOH   K 5 .   ? 31.585 7.365   23.048 1.00 31.50  ? 307 HOH   A O   1 
HETATM 2222 O  O   . HOH   K 5 .   ? 23.762 24.020  10.179 1.00 50.17  ? 308 HOH   A O   1 
HETATM 2223 O  O   . HOH   K 5 .   ? 34.820 14.862  24.980 1.00 34.33  ? 309 HOH   A O   1 
HETATM 2224 O  O   . HOH   K 5 .   ? 16.108 -0.711  4.830  1.00 28.81  ? 310 HOH   A O   1 
HETATM 2225 O  O   . HOH   K 5 .   ? 30.526 19.969  7.818  1.00 39.34  ? 311 HOH   A O   1 
HETATM 2226 O  O   . HOH   K 5 .   ? 34.795 13.758  16.351 1.00 28.23  ? 312 HOH   A O   1 
HETATM 2227 O  O   . HOH   K 5 .   ? 28.436 -6.119  3.528  1.00 24.16  ? 313 HOH   A O   1 
HETATM 2228 O  O   . HOH   K 5 .   ? 17.020 20.612  22.817 1.00 21.66  ? 314 HOH   A O   1 
HETATM 2229 O  O   . HOH   K 5 .   ? 7.182  7.396   31.578 1.00 31.48  ? 315 HOH   A O   1 
HETATM 2230 O  O   . HOH   K 5 .   ? 14.976 8.561   13.320 1.00 13.97  ? 316 HOH   A O   1 
HETATM 2231 O  O   . HOH   K 5 .   ? 35.479 13.553  11.546 1.00 31.74  ? 317 HOH   A O   1 
HETATM 2232 O  O   . HOH   K 5 .   ? 20.950 10.328  32.246 1.00 41.90  ? 318 HOH   A O   1 
HETATM 2233 O  O   . HOH   K 5 .   ? 26.943 19.046  14.851 1.00 16.82  ? 319 HOH   A O   1 
HETATM 2234 O  O   . HOH   K 5 .   ? 25.402 17.730  12.682 1.00 15.74  ? 320 HOH   A O   1 
HETATM 2235 O  O   . HOH   K 5 .   ? 34.438 -0.768  16.631 1.00 14.54  ? 321 HOH   A O   1 
HETATM 2236 O  O   . HOH   K 5 .   ? 35.510 10.477  9.796  1.00 48.79  ? 322 HOH   A O   1 
HETATM 2237 O  O   . HOH   K 5 .   ? 31.011 12.650  9.033  1.00 33.96  ? 323 HOH   A O   1 
HETATM 2238 O  O   . HOH   K 5 .   ? 22.500 6.530   1.735  1.00 18.81  ? 324 HOH   A O   1 
HETATM 2239 O  O   . HOH   K 5 .   ? 3.938  20.052  15.016 1.00 43.95  ? 325 HOH   A O   1 
HETATM 2240 O  O   . HOH   K 5 .   ? 22.426 -5.973  0.550  1.00 39.79  ? 326 HOH   A O   1 
HETATM 2241 O  O   . HOH   K 5 .   ? 11.210 -0.266  15.793 1.00 26.04  ? 327 HOH   A O   1 
HETATM 2242 O  O   . HOH   K 5 .   ? 23.829 16.751  27.196 1.00 38.28  ? 328 HOH   A O   1 
HETATM 2243 O  O   . HOH   K 5 .   ? 3.875  19.726  21.394 1.00 31.23  ? 329 HOH   A O   1 
HETATM 2244 O  O   . HOH   K 5 .   ? 6.293  2.932   28.926 1.00 39.47  ? 330 HOH   A O   1 
HETATM 2245 O  O   . HOH   K 5 .   ? 17.772 -7.628  21.546 1.00 24.19  ? 331 HOH   A O   1 
HETATM 2246 O  O   . HOH   K 5 .   ? 6.762  15.326  29.029 1.00 40.41  ? 332 HOH   A O   1 
HETATM 2247 O  O   . HOH   K 5 .   ? 23.951 3.875   29.279 1.00 20.05  ? 333 HOH   A O   1 
HETATM 2248 O  O   . HOH   K 5 .   ? 23.655 1.761   -0.815 1.00 15.41  ? 334 HOH   A O   1 
HETATM 2249 O  O   . HOH   K 5 .   ? 5.001  10.820  12.465 1.00 36.16  ? 335 HOH   A O   1 
HETATM 2250 O  O   . HOH   K 5 .   ? 20.120 2.118   9.332  1.00 13.73  ? 336 HOH   A O   1 
HETATM 2251 O  O   . HOH   K 5 .   ? 32.211 2.724   5.043  1.00 30.07  ? 337 HOH   A O   1 
HETATM 2252 O  O   . HOH   K 5 .   ? 18.750 -11.620 27.382 1.00 32.28  ? 338 HOH   A O   1 
HETATM 2253 O  O   . HOH   K 5 .   ? 27.952 2.987   -0.232 1.00 22.30  ? 339 HOH   A O   1 
HETATM 2254 O  O   . HOH   K 5 .   ? 5.057  2.970   21.033 1.00 21.85  ? 340 HOH   A O   1 
HETATM 2255 O  O   . HOH   K 5 .   ? 20.047 11.817  8.559  1.00 17.00  ? 341 HOH   A O   1 
HETATM 2256 O  O   . HOH   K 5 .   ? 8.962  3.828   12.049 1.00 33.30  ? 342 HOH   A O   1 
HETATM 2257 O  O   . HOH   K 5 .   ? 4.107  9.806   17.963 1.00 30.66  ? 343 HOH   A O   1 
HETATM 2258 O  O   . HOH   K 5 .   ? 23.418 10.898  21.405 1.00 13.42  ? 344 HOH   A O   1 
HETATM 2259 O  O   . HOH   K 5 .   ? 29.449 7.216   4.202  1.00 22.82  ? 345 HOH   A O   1 
HETATM 2260 O  O   . HOH   K 5 .   ? 4.897  10.467  14.796 1.00 38.24  ? 346 HOH   A O   1 
HETATM 2261 O  O   . HOH   K 5 .   ? 29.623 25.766  15.899 1.00 34.93  ? 347 HOH   A O   1 
HETATM 2262 O  O   . HOH   K 5 .   ? 23.216 -11.006 30.908 1.00 46.80  ? 348 HOH   A O   1 
HETATM 2263 O  O   . HOH   K 5 .   ? 27.526 24.779  18.773 1.00 35.08  ? 349 HOH   A O   1 
HETATM 2264 O  O   . HOH   K 5 .   ? 17.202 2.068   9.302  1.00 18.86  ? 350 HOH   A O   1 
HETATM 2265 O  O   . HOH   K 5 .   ? 24.768 -8.660  24.818 1.00 33.22  ? 351 HOH   A O   1 
HETATM 2266 O  O   . HOH   K 5 .   ? -1.904 15.590  20.263 1.00 31.82  ? 352 HOH   A O   1 
HETATM 2267 O  O   . HOH   K 5 .   ? 24.550 14.214  30.390 1.00 55.13  ? 353 HOH   A O   1 
HETATM 2268 O  O   . HOH   K 5 .   ? 16.467 18.477  26.938 1.00 35.13  ? 354 HOH   A O   1 
HETATM 2269 O  O   . HOH   K 5 .   ? 13.406 18.579  14.665 1.00 27.89  ? 355 HOH   A O   1 
HETATM 2270 O  O   . HOH   K 5 .   ? 28.245 0.931   26.747 1.00 21.14  ? 356 HOH   A O   1 
HETATM 2271 O  O   . HOH   K 5 .   ? 25.464 1.567   29.849 1.00 22.02  ? 357 HOH   A O   1 
HETATM 2272 O  O   . HOH   K 5 .   ? 22.138 8.892   2.981  1.00 20.04  ? 358 HOH   A O   1 
HETATM 2273 O  O   . HOH   K 5 .   ? 17.770 20.096  13.493 1.00 21.15  ? 359 HOH   A O   1 
HETATM 2274 O  O   . HOH   K 5 .   ? 17.238 0.296   2.570  1.00 35.27  ? 360 HOH   A O   1 
HETATM 2275 O  O   . HOH   K 5 .   ? 16.338 8.904   6.786  1.00 19.52  ? 361 HOH   A O   1 
HETATM 2276 O  O   . HOH   K 5 .   ? 17.111 18.375  15.467 1.00 14.03  ? 362 HOH   A O   1 
HETATM 2277 O  O   . HOH   K 5 .   ? 12.480 17.748  13.127 1.00 34.61  ? 363 HOH   A O   1 
HETATM 2278 O  O   . HOH   K 5 .   ? 20.312 20.485  24.007 1.00 34.62  ? 364 HOH   A O   1 
HETATM 2279 O  O   . HOH   K 5 .   ? 12.028 -2.782  16.061 1.00 30.78  ? 365 HOH   A O   1 
HETATM 2280 O  O   . HOH   K 5 .   ? 34.850 -6.273  21.640 1.00 39.69  ? 366 HOH   A O   1 
HETATM 2281 O  O   . HOH   K 5 .   ? 4.239  4.109   28.109 1.00 36.86  ? 367 HOH   A O   1 
HETATM 2282 O  O   . HOH   K 5 .   ? 31.397 14.672  12.682 1.00 23.28  ? 368 HOH   A O   1 
HETATM 2283 O  O   . HOH   K 5 .   ? 17.609 16.482  28.438 1.00 42.79  ? 369 HOH   A O   1 
HETATM 2284 O  O   . HOH   K 5 .   ? 30.583 -3.087  12.059 1.00 23.09  ? 370 HOH   A O   1 
HETATM 2285 O  O   . HOH   K 5 .   ? 34.440 3.768   26.114 1.00 26.89  ? 371 HOH   A O   1 
HETATM 2286 O  O   . HOH   K 5 .   ? 21.538 9.869   23.341 1.00 13.34  ? 372 HOH   A O   1 
HETATM 2287 O  O   . HOH   K 5 .   ? 29.683 -2.294  8.226  1.00 18.33  ? 373 HOH   A O   1 
HETATM 2288 O  O   . HOH   K 5 .   ? 29.293 13.807  11.140 1.00 28.17  ? 374 HOH   A O   1 
HETATM 2289 O  O   . HOH   K 5 .   ? 3.370  17.980  23.502 1.00 33.00  ? 375 HOH   A O   1 
HETATM 2290 O  O   . HOH   K 5 .   ? 12.647 -6.262  22.152 1.00 23.09  ? 376 HOH   A O   1 
HETATM 2291 O  O   . HOH   K 5 .   ? 32.057 8.374   4.600  1.00 26.16  ? 377 HOH   A O   1 
HETATM 2292 O  O   . HOH   K 5 .   ? 30.767 5.379   7.696  1.00 21.82  ? 378 HOH   A O   1 
HETATM 2293 O  O   . HOH   K 5 .   ? 25.935 8.524   0.963  1.00 29.75  ? 379 HOH   A O   1 
HETATM 2294 O  O   . HOH   K 5 .   ? 32.939 -2.602  15.307 1.00 19.08  ? 380 HOH   A O   1 
HETATM 2295 O  O   . HOH   K 5 .   ? 26.809 19.172  24.496 1.00 40.88  ? 381 HOH   A O   1 
HETATM 2296 O  O   . HOH   K 5 .   ? 25.018 4.178   -1.217 1.00 17.97  ? 382 HOH   A O   1 
HETATM 2297 O  O   . HOH   K 5 .   ? 35.371 14.465  20.239 1.00 22.19  ? 383 HOH   A O   1 
HETATM 2298 O  O   . HOH   K 5 .   ? 30.283 -5.797  26.333 1.00 29.74  ? 384 HOH   A O   1 
HETATM 2299 O  O   . HOH   K 5 .   ? 27.893 16.101  10.514 1.00 26.61  ? 385 HOH   A O   1 
HETATM 2300 O  O   . HOH   K 5 .   ? 18.530 -3.754  14.623 1.00 32.49  ? 386 HOH   A O   1 
HETATM 2301 O  O   . HOH   K 5 .   ? 19.481 -6.051  32.767 1.00 39.32  ? 387 HOH   A O   1 
HETATM 2302 O  O   . HOH   K 5 .   ? 20.525 -7.624  1.901  1.00 43.21  ? 388 HOH   A O   1 
HETATM 2303 O  O   . HOH   K 5 .   ? 16.785 4.482   5.957  1.00 22.51  ? 389 HOH   A O   1 
HETATM 2304 O  O   . HOH   K 5 .   ? 19.879 -4.718  15.306 1.00 26.12  ? 390 HOH   A O   1 
HETATM 2305 O  O   . HOH   K 5 .   ? 29.858 6.390   29.919 1.00 29.69  ? 391 HOH   A O   1 
HETATM 2306 O  O   . HOH   K 5 .   ? 22.899 20.754  20.288 1.00 23.24  ? 392 HOH   A O   1 
HETATM 2307 O  O   . HOH   K 5 .   ? 6.611  16.081  8.906  1.00 29.70  ? 393 HOH   A O   1 
HETATM 2308 O  O   . HOH   K 5 .   ? 2.756  8.509   26.123 1.00 31.23  ? 394 HOH   A O   1 
HETATM 2309 O  O   . HOH   K 5 .   ? 29.234 25.531  13.142 1.00 24.27  ? 395 HOH   A O   1 
HETATM 2310 O  O   . HOH   K 5 .   ? 17.898 22.173  7.398  1.00 42.75  ? 396 HOH   A O   1 
HETATM 2311 O  O   . HOH   K 5 .   ? 32.650 12.263  27.590 1.00 29.92  ? 397 HOH   A O   1 
HETATM 2312 O  O   . HOH   K 5 .   ? 18.245 -5.294  30.471 1.00 26.20  ? 398 HOH   A O   1 
HETATM 2313 O  O   . HOH   K 5 .   ? 22.196 -8.358  19.355 1.00 31.15  ? 399 HOH   A O   1 
HETATM 2314 O  O   . HOH   K 5 .   ? 17.356 22.165  15.618 1.00 28.24  ? 400 HOH   A O   1 
HETATM 2315 O  O   . HOH   K 5 .   ? 16.405 -3.433  13.974 1.00 33.44  ? 401 HOH   A O   1 
HETATM 2316 O  O   . HOH   K 5 .   ? 29.214 1.171   25.333 1.00 62.88  ? 402 HOH   A O   1 
HETATM 2317 O  O   . HOH   K 5 .   ? 28.756 22.098  21.945 1.00 28.19  ? 403 HOH   A O   1 
HETATM 2318 O  O   . HOH   K 5 .   ? 3.407  2.305   19.043 1.00 30.32  ? 404 HOH   A O   1 
HETATM 2319 O  O   . HOH   K 5 .   ? 27.812 11.950  27.493 1.00 23.76  ? 405 HOH   A O   1 
HETATM 2320 O  O   . HOH   K 5 .   ? 22.385 14.505  4.915  1.00 40.79  ? 406 HOH   A O   1 
HETATM 2321 O  O   . HOH   K 5 .   ? 20.531 13.420  6.342  1.00 28.24  ? 407 HOH   A O   1 
HETATM 2322 O  O   . HOH   K 5 .   ? 20.086 13.832  29.121 1.00 29.75  ? 408 HOH   A O   1 
HETATM 2323 O  O   . HOH   K 5 .   ? 15.671 12.078  30.678 1.00 41.01  ? 409 HOH   A O   1 
HETATM 2324 O  O   . HOH   K 5 .   ? 20.087 23.333  14.993 1.00 41.52  ? 410 HOH   A O   1 
HETATM 2325 O  O   . HOH   K 5 .   ? -0.144 14.531  22.840 1.00 57.37  ? 411 HOH   A O   1 
HETATM 2326 O  O   . HOH   K 5 .   ? 12.102 18.368  26.329 1.00 24.92  ? 412 HOH   A O   1 
HETATM 2327 O  O   . HOH   K 5 .   ? 3.836  14.528  10.395 1.00 26.72  ? 413 HOH   A O   1 
HETATM 2328 O  O   . HOH   K 5 .   ? 30.233 -2.044  3.416  1.00 35.18  ? 414 HOH   A O   1 
HETATM 2329 O  O   . HOH   K 5 .   ? 15.099 23.128  16.817 1.00 20.58  ? 415 HOH   A O   1 
HETATM 2330 O  O   . HOH   K 5 .   ? 14.512 -3.982  16.102 1.00 32.84  ? 416 HOH   A O   1 
HETATM 2331 O  O   . HOH   K 5 .   ? 26.584 -6.504  29.777 1.00 35.36  ? 417 HOH   A O   1 
HETATM 2332 O  O   . HOH   K 5 .   ? 11.068 2.103   12.470 1.00 25.53  ? 418 HOH   A O   1 
HETATM 2333 O  O   . HOH   K 5 .   ? 13.216 8.515   11.053 1.00 19.05  ? 419 HOH   A O   1 
HETATM 2334 O  O   . HOH   K 5 .   ? 2.280  14.189  24.599 1.00 54.53  ? 420 HOH   A O   1 
HETATM 2335 O  O   . HOH   K 5 .   ? 35.616 -5.024  16.899 1.00 39.35  ? 421 HOH   A O   1 
HETATM 2336 O  O   . HOH   K 5 .   ? 32.783 5.367   4.562  1.00 38.46  ? 422 HOH   A O   1 
HETATM 2337 O  O   . HOH   K 5 .   ? 0.817  17.145  23.198 1.00 50.03  ? 423 HOH   A O   1 
HETATM 2338 O  O   . HOH   K 5 .   ? 15.875 8.464   33.777 1.00 34.47  ? 424 HOH   A O   1 
HETATM 2339 O  O   . HOH   K 5 .   ? 25.986 -8.485  22.819 1.00 47.83  ? 425 HOH   A O   1 
HETATM 2340 O  O   . HOH   K 5 .   ? 19.441 -9.838  20.530 1.00 29.86  ? 426 HOH   A O   1 
HETATM 2341 O  O   . HOH   K 5 .   ? 10.756 6.731   11.436 1.00 38.79  ? 427 HOH   A O   1 
HETATM 2342 O  O   . HOH   K 5 .   ? 8.758  -2.586  27.510 1.00 45.73  ? 428 HOH   A O   1 
HETATM 2343 O  O   . HOH   K 5 .   ? 31.521 -7.273  17.980 1.00 35.37  ? 429 HOH   A O   1 
HETATM 2344 O  O   . HOH   K 5 .   ? 16.319 7.026   4.681  1.00 30.79  ? 430 HOH   A O   1 
HETATM 2345 O  O   . HOH   K 5 .   ? 25.936 14.507  6.339  1.00 41.96  ? 431 HOH   A O   1 
HETATM 2346 O  O   . HOH   K 5 .   ? 35.769 22.820  19.896 1.00 44.16  ? 432 HOH   A O   1 
HETATM 2347 O  O   . HOH   K 5 .   ? 24.621 -5.246  32.991 1.00 36.70  ? 433 HOH   A O   1 
HETATM 2348 O  O   . HOH   K 5 .   ? 14.830 -6.791  15.786 1.00 52.92  ? 434 HOH   A O   1 
HETATM 2349 O  O   . HOH   K 5 .   ? 25.917 21.902  5.813  1.00 40.43  ? 435 HOH   A O   1 
HETATM 2350 O  O   . HOH   K 5 .   ? 6.652  -0.899  27.955 1.00 51.42  ? 436 HOH   A O   1 
HETATM 2351 O  O   . HOH   K 5 .   ? 19.496 11.517  4.354  1.00 39.39  ? 437 HOH   A O   1 
HETATM 2352 O  O   . HOH   K 5 .   ? 6.571  18.954  26.278 1.00 60.61  ? 438 HOH   A O   1 
HETATM 2353 O  O   . HOH   K 5 .   ? 18.133 10.886  6.699  1.00 22.27  ? 439 HOH   A O   1 
HETATM 2354 O  O   . HOH   K 5 .   ? 27.644 16.169  7.874  1.00 45.92  ? 440 HOH   A O   1 
HETATM 2355 O  O   . HOH   K 5 .   ? 13.696 21.546  14.878 1.00 24.90  ? 441 HOH   A O   1 
HETATM 2356 O  O   . HOH   K 5 .   ? 2.412  20.949  12.008 1.00 45.30  ? 442 HOH   A O   1 
HETATM 2357 O  O   . HOH   K 5 .   ? 2.111  21.380  8.292  1.00 54.18  ? 443 HOH   A O   1 
HETATM 2358 O  O   . HOH   K 5 .   ? 20.312 -6.648  -0.488 1.00 42.63  ? 444 HOH   A O   1 
HETATM 2359 O  O   . HOH   K 5 .   ? 23.162 22.805  18.490 1.00 28.51  ? 445 HOH   A O   1 
HETATM 2360 O  O   . HOH   K 5 .   ? 30.876 -2.915  5.767  1.00 32.20  ? 446 HOH   A O   1 
HETATM 2361 O  O   . HOH   K 5 .   ? 33.595 -2.261  9.244  1.00 24.00  ? 447 HOH   A O   1 
HETATM 2362 O  O   . HOH   K 5 .   ? 8.972  17.532  8.543  1.00 46.42  ? 448 HOH   A O   1 
HETATM 2363 O  O   . HOH   K 5 .   ? 28.130 1.696   29.344 1.00 28.84  ? 449 HOH   A O   1 
HETATM 2364 O  O   . HOH   K 5 .   ? 11.667 -4.501  29.773 1.00 50.37  ? 450 HOH   A O   1 
HETATM 2365 O  O   . HOH   K 5 .   ? 28.537 4.213   30.455 1.00 34.72  ? 451 HOH   A O   1 
HETATM 2366 O  O   . HOH   K 5 .   ? 31.349 -3.865  9.690  1.00 22.99  ? 452 HOH   A O   1 
HETATM 2367 O  O   . HOH   K 5 .   ? 27.709 9.132   2.893  1.00 28.87  ? 453 HOH   A O   1 
HETATM 2368 O  O   . HOH   K 5 .   ? 23.590 10.662  1.663  1.00 37.85  ? 454 HOH   A O   1 
HETATM 2369 O  O   . HOH   K 5 .   ? 35.194 11.577  15.771 1.00 41.90  ? 455 HOH   A O   1 
HETATM 2370 O  O   . HOH   K 5 .   ? -3.703 0.468   24.817 1.00 45.51  ? 456 HOH   A O   1 
HETATM 2371 O  O   . HOH   K 5 .   ? 2.884  3.777   16.884 1.00 39.67  ? 457 HOH   A O   1 
HETATM 2372 O  O   . HOH   K 5 .   ? 22.892 13.425  2.552  1.00 52.33  ? 458 HOH   A O   1 
HETATM 2373 O  O   . HOH   K 5 .   ? 29.526 21.282  24.891 1.00 58.58  ? 459 HOH   A O   1 
HETATM 2374 O  O   . HOH   K 5 .   ? 24.928 24.610  19.411 1.00 35.20  ? 460 HOH   A O   1 
HETATM 2375 O  O   . HOH   K 5 .   ? 27.627 13.811  4.459  1.00 46.93  ? 461 HOH   A O   1 
HETATM 2376 O  O   . HOH   K 5 .   ? 27.826 11.721  2.895  1.00 42.61  ? 462 HOH   A O   1 
HETATM 2377 O  O   . HOH   L 5 .   ? 5.827  -28.095 7.934  1.00 257.37 ? 301 HOH   C O   1 
HETATM 2378 O  O   . HOH   L 5 .   ? 13.760 -24.289 30.977 1.00 33.04  ? 302 HOH   C O   1 
HETATM 2379 O  O   . HOH   L 5 .   ? 20.192 -8.333  7.820  1.00 25.34  ? 303 HOH   C O   1 
HETATM 2380 O  O   . HOH   L 5 .   ? 10.274 -28.709 1.541  1.00 181.57 ? 304 HOH   C O   1 
HETATM 2381 O  O   . HOH   L 5 .   ? 15.682 -38.931 9.723  1.00 57.81  ? 305 HOH   C O   1 
HETATM 2382 O  O   . HOH   L 5 .   ? 12.773 -13.957 4.822  1.00 37.62  ? 306 HOH   C O   1 
HETATM 2383 O  O   . HOH   L 5 .   ? 2.671  -22.883 10.403 1.00 27.31  ? 307 HOH   C O   1 
HETATM 2384 O  O   . HOH   L 5 .   ? 35.505 -15.388 15.633 1.00 33.99  ? 308 HOH   C O   1 
HETATM 2385 O  O   . HOH   L 5 .   ? 10.723 -27.373 33.578 1.00 24.18  ? 309 HOH   C O   1 
HETATM 2386 O  O   . HOH   L 5 .   ? 31.071 -10.460 10.555 1.00 33.45  ? 310 HOH   C O   1 
HETATM 2387 O  O   . HOH   L 5 .   ? 22.064 -32.506 3.705  1.00 25.59  ? 311 HOH   C O   1 
HETATM 2388 O  O   . HOH   L 5 .   ? 10.114 -22.707 4.772  1.00 20.19  ? 312 HOH   C O   1 
HETATM 2389 O  O   . HOH   L 5 .   ? 23.691 -9.200  7.811  1.00 22.43  ? 313 HOH   C O   1 
HETATM 2390 O  O   . HOH   L 5 .   ? 12.545 -29.293 33.465 1.00 20.30  ? 314 HOH   C O   1 
HETATM 2391 O  O   . HOH   L 5 .   ? 25.942 -32.917 5.826  1.00 46.66  ? 315 HOH   C O   1 
HETATM 2392 O  O   . HOH   L 5 .   ? 5.415  -25.292 24.269 1.00 19.30  ? 316 HOH   C O   1 
HETATM 2393 O  O   . HOH   L 5 .   ? 17.072 -37.511 2.914  1.00 32.89  ? 317 HOH   C O   1 
HETATM 2394 O  O   . HOH   L 5 .   ? 26.365 -22.697 -0.334 1.00 34.49  ? 318 HOH   C O   1 
HETATM 2395 O  O   . HOH   L 5 .   ? 2.687  -31.184 3.834  1.00 34.01  ? 319 HOH   C O   1 
HETATM 2396 O  O   . HOH   L 5 .   ? 11.414 -20.423 0.749  1.00 39.01  ? 320 HOH   C O   1 
HETATM 2397 O  O   . HOH   L 5 .   ? 10.515 -12.751 20.534 1.00 15.41  ? 321 HOH   C O   1 
HETATM 2398 O  O   . HOH   L 5 .   ? 20.447 -22.255 18.619 1.00 15.49  ? 322 HOH   C O   1 
HETATM 2399 O  O   . HOH   L 5 .   ? 22.616 -35.925 12.154 1.00 34.47  ? 323 HOH   C O   1 
HETATM 2400 O  O   . HOH   L 5 .   ? 4.276  -35.865 21.548 1.00 26.09  ? 324 HOH   C O   1 
HETATM 2401 O  O   . HOH   L 5 .   ? 13.966 -19.591 0.711  1.00 31.01  ? 325 HOH   C O   1 
HETATM 2402 O  O   . HOH   L 5 .   ? 0.265  -15.162 22.705 1.00 36.82  ? 326 HOH   C O   1 
HETATM 2403 O  O   . HOH   L 5 .   ? 23.464 -31.102 15.022 1.00 25.07  ? 327 HOH   C O   1 
HETATM 2404 O  O   . HOH   L 5 .   ? 23.992 -12.594 19.052 1.00 29.22  ? 328 HOH   C O   1 
HETATM 2405 O  O   . HOH   L 5 .   ? 28.744 -10.107 18.607 1.00 37.50  ? 329 HOH   C O   1 
HETATM 2406 O  O   . HOH   L 5 .   ? 16.442 -14.008 4.022  1.00 41.54  ? 330 HOH   C O   1 
HETATM 2407 O  O   . HOH   L 5 .   ? 0.730  -16.683 18.044 1.00 29.17  ? 331 HOH   C O   1 
HETATM 2408 O  O   . HOH   L 5 .   ? 4.803  -30.865 -1.882 1.00 33.79  ? 332 HOH   C O   1 
HETATM 2409 O  O   . HOH   L 5 .   ? 8.722  -11.454 18.457 1.00 17.64  ? 333 HOH   C O   1 
HETATM 2410 O  O   . HOH   L 5 .   ? 9.819  -26.002 3.479  1.00 17.07  ? 334 HOH   C O   1 
HETATM 2411 O  O   . HOH   L 5 .   ? 29.322 -27.788 9.853  1.00 23.07  ? 335 HOH   C O   1 
HETATM 2412 O  O   . HOH   L 5 .   ? 8.511  -39.332 24.339 1.00 34.77  ? 336 HOH   C O   1 
HETATM 2413 O  O   . HOH   L 5 .   ? 27.485 -27.414 2.154  1.00 36.56  ? 337 HOH   C O   1 
HETATM 2414 O  O   . HOH   L 5 .   ? 3.579  -23.318 3.671  1.00 25.28  ? 338 HOH   C O   1 
HETATM 2415 O  O   . HOH   L 5 .   ? 7.073  -36.577 29.162 1.00 34.09  ? 339 HOH   C O   1 
HETATM 2416 O  O   . HOH   L 5 .   ? 20.800 -28.432 -2.532 1.00 34.69  ? 340 HOH   C O   1 
HETATM 2417 O  O   . HOH   L 5 .   ? 6.013  -32.385 29.658 1.00 37.74  ? 341 HOH   C O   1 
HETATM 2418 O  O   . HOH   L 5 .   ? 11.284 -19.445 11.480 1.00 13.77  ? 342 HOH   C O   1 
HETATM 2419 O  O   . HOH   L 5 .   ? 8.280  -28.231 2.994  1.00 17.07  ? 343 HOH   C O   1 
HETATM 2420 O  O   . HOH   L 5 .   ? 18.053 -11.709 5.486  1.00 36.02  ? 344 HOH   C O   1 
HETATM 2421 O  O   . HOH   L 5 .   ? 16.264 -34.156 17.418 1.00 41.66  ? 345 HOH   C O   1 
HETATM 2422 O  O   . HOH   L 5 .   ? 11.219 -35.736 -0.675 1.00 29.69  ? 346 HOH   C O   1 
HETATM 2423 O  O   . HOH   L 5 .   ? 34.604 -10.925 10.768 1.00 43.34  ? 347 HOH   C O   1 
HETATM 2424 O  O   . HOH   L 5 .   ? 15.971 -18.848 23.987 1.00 18.02  ? 348 HOH   C O   1 
HETATM 2425 O  O   . HOH   L 5 .   ? 0.932  -31.462 17.119 1.00 14.50  ? 349 HOH   C O   1 
HETATM 2426 O  O   . HOH   L 5 .   ? 30.738 -21.205 12.996 1.00 33.09  ? 350 HOH   C O   1 
HETATM 2427 O  O   . HOH   L 5 .   ? 21.246 -36.413 9.791  1.00 24.90  ? 351 HOH   C O   1 
HETATM 2428 O  O   . HOH   L 5 .   ? 6.938  -23.097 29.050 1.00 28.88  ? 352 HOH   C O   1 
HETATM 2429 O  O   . HOH   L 5 .   ? 29.634 -26.314 2.859  1.00 35.66  ? 353 HOH   C O   1 
HETATM 2430 O  O   . HOH   L 5 .   ? 11.220 -36.099 31.356 1.00 31.69  ? 354 HOH   C O   1 
HETATM 2431 O  O   . HOH   L 5 .   ? 18.282 -28.609 22.843 1.00 20.02  ? 355 HOH   C O   1 
HETATM 2432 O  O   . HOH   L 5 .   ? 30.495 -20.400 16.374 1.00 32.57  ? 356 HOH   C O   1 
HETATM 2433 O  O   . HOH   L 5 .   ? 15.446 -28.618 23.046 1.00 15.83  ? 357 HOH   C O   1 
HETATM 2434 O  O   . HOH   L 5 .   ? 22.044 -12.227 17.127 1.00 24.31  ? 358 HOH   C O   1 
HETATM 2435 O  O   . HOH   L 5 .   ? 14.419 -22.065 29.683 1.00 25.98  ? 359 HOH   C O   1 
HETATM 2436 O  O   . HOH   L 5 .   ? 26.230 -27.156 19.183 1.00 37.60  ? 360 HOH   C O   1 
HETATM 2437 O  O   . HOH   L 5 .   ? 17.736 -9.898  9.321  1.00 20.54  ? 361 HOH   C O   1 
HETATM 2438 O  O   . HOH   L 5 .   ? 10.663 -13.674 5.690  1.00 47.28  ? 362 HOH   C O   1 
HETATM 2439 O  O   . HOH   L 5 .   ? 5.349  -17.452 24.936 1.00 27.29  ? 363 HOH   C O   1 
HETATM 2440 O  O   . HOH   L 5 .   ? 1.305  -29.324 24.887 1.00 28.88  ? 364 HOH   C O   1 
HETATM 2441 O  O   . HOH   L 5 .   ? 30.414 -20.159 19.084 1.00 31.80  ? 365 HOH   C O   1 
HETATM 2442 O  O   . HOH   L 5 .   ? 18.330 -12.311 16.859 1.00 16.69  ? 366 HOH   C O   1 
HETATM 2443 O  O   . HOH   L 5 .   ? 19.880 -31.400 26.831 1.00 26.99  ? 367 HOH   C O   1 
HETATM 2444 O  O   . HOH   L 5 .   ? 4.089  -8.715  22.859 1.00 29.17  ? 368 HOH   C O   1 
HETATM 2445 O  O   . HOH   L 5 .   ? 6.771  -16.473 22.635 1.00 26.25  ? 369 HOH   C O   1 
HETATM 2446 O  O   . HOH   L 5 .   ? 27.623 -15.055 2.514  1.00 43.39  ? 370 HOH   C O   1 
HETATM 2447 O  O   . HOH   L 5 .   ? 12.975 -20.537 9.377  1.00 13.18  ? 371 HOH   C O   1 
HETATM 2448 O  O   . HOH   L 5 .   ? 6.473  -18.150 5.940  1.00 21.01  ? 372 HOH   C O   1 
HETATM 2449 O  O   . HOH   L 5 .   ? 0.902  -33.573 20.480 1.00 25.88  ? 373 HOH   C O   1 
HETATM 2450 O  O   . HOH   L 5 .   ? 19.735 -22.097 25.422 1.00 24.33  ? 374 HOH   C O   1 
HETATM 2451 O  O   . HOH   L 5 .   ? 31.200 -10.668 16.329 1.00 23.84  ? 375 HOH   C O   1 
HETATM 2452 O  O   . HOH   L 5 .   ? 5.523  -29.075 7.327  1.00 15.42  ? 376 HOH   C O   1 
HETATM 2453 O  O   . HOH   L 5 .   ? 3.620  -35.970 6.810  1.00 24.36  ? 377 HOH   C O   1 
HETATM 2454 O  O   . HOH   L 5 .   ? 9.654  -40.761 1.414  1.00 46.57  ? 378 HOH   C O   1 
HETATM 2455 O  O   . HOH   L 5 .   ? 8.215  -14.380 22.927 1.00 24.62  ? 379 HOH   C O   1 
HETATM 2456 O  O   . HOH   L 5 .   ? 7.579  -5.501  14.693 1.00 36.85  ? 380 HOH   C O   1 
HETATM 2457 O  O   . HOH   L 5 .   ? 4.150  -24.154 26.332 1.00 26.96  ? 381 HOH   C O   1 
HETATM 2458 O  O   . HOH   L 5 .   ? 20.826 -12.011 21.223 1.00 28.84  ? 382 HOH   C O   1 
HETATM 2459 O  O   . HOH   L 5 .   ? 19.360 -26.869 25.412 1.00 34.31  ? 383 HOH   C O   1 
HETATM 2460 O  O   . HOH   L 5 .   ? 16.676 -7.778  14.538 1.00 35.76  ? 384 HOH   C O   1 
HETATM 2461 O  O   . HOH   L 5 .   ? 32.652 -16.576 6.801  1.00 47.70  ? 385 HOH   C O   1 
HETATM 2462 O  O   . HOH   L 5 .   ? 36.243 -32.060 9.268  1.00 43.20  ? 386 HOH   C O   1 
HETATM 2463 O  O   . HOH   L 5 .   ? 2.756  -20.303 28.078 1.00 37.70  ? 387 HOH   C O   1 
HETATM 2464 O  O   . HOH   L 5 .   ? 18.156 -10.795 19.058 1.00 31.69  ? 388 HOH   C O   1 
HETATM 2465 O  O   . HOH   L 5 .   ? 5.706  -32.537 24.531 1.00 18.51  ? 389 HOH   C O   1 
HETATM 2466 O  O   . HOH   L 5 .   ? 28.521 -33.172 12.279 1.00 27.00  ? 390 HOH   C O   1 
HETATM 2467 O  O   . HOH   L 5 .   ? 14.810 -35.429 16.989 1.00 21.10  ? 391 HOH   C O   1 
HETATM 2468 O  O   . HOH   L 5 .   ? 13.903 -16.515 3.528  1.00 28.60  ? 392 HOH   C O   1 
HETATM 2469 O  O   . HOH   L 5 .   ? 15.182 -35.424 1.726  1.00 22.68  ? 393 HOH   C O   1 
HETATM 2470 O  O   . HOH   L 5 .   ? 7.927  -34.847 0.487  1.00 19.59  ? 394 HOH   C O   1 
HETATM 2471 O  O   . HOH   L 5 .   ? 4.641  -30.208 30.992 1.00 39.77  ? 395 HOH   C O   1 
HETATM 2472 O  O   . HOH   L 5 .   ? -2.281 -30.327 8.583  1.00 17.81  ? 396 HOH   C O   1 
HETATM 2473 O  O   . HOH   L 5 .   ? 22.767 -33.750 15.045 1.00 34.96  ? 397 HOH   C O   1 
HETATM 2474 O  O   . HOH   L 5 .   ? 5.990  -8.306  11.695 1.00 36.86  ? 398 HOH   C O   1 
HETATM 2475 O  O   . HOH   L 5 .   ? 19.506 -7.347  15.193 1.00 22.37  ? 399 HOH   C O   1 
HETATM 2476 O  O   . HOH   L 5 .   ? 18.166 -18.201 1.406  1.00 38.67  ? 400 HOH   C O   1 
HETATM 2477 O  O   . HOH   L 5 .   ? 8.659  -38.466 9.466  1.00 24.11  ? 401 HOH   C O   1 
HETATM 2478 O  O   . HOH   L 5 .   ? 32.053 -16.588 20.494 1.00 26.42  ? 402 HOH   C O   1 
HETATM 2479 O  O   . HOH   L 5 .   ? 9.543  -9.970  11.282 1.00 37.93  ? 403 HOH   C O   1 
HETATM 2480 O  O   . HOH   L 5 .   ? 21.808 -14.850 23.542 1.00 34.45  ? 404 HOH   C O   1 
HETATM 2481 O  O   . HOH   L 5 .   ? 16.690 -8.485  16.872 1.00 50.40  ? 405 HOH   C O   1 
HETATM 2482 O  O   . HOH   L 5 .   ? 4.165  -33.402 22.278 1.00 30.57  ? 406 HOH   C O   1 
HETATM 2483 O  O   . HOH   L 5 .   ? 29.051 -14.713 22.454 1.00 30.01  ? 407 HOH   C O   1 
HETATM 2484 O  O   . HOH   L 5 .   ? 1.820  -17.519 6.028  1.00 31.78  ? 408 HOH   C O   1 
HETATM 2485 O  O   . HOH   L 5 .   ? 31.182 -26.090 -2.483 1.00 54.50  ? 409 HOH   C O   1 
HETATM 2486 O  O   . HOH   L 5 .   ? 14.300 -10.063 8.577  1.00 34.51  ? 410 HOH   C O   1 
HETATM 2487 O  O   . HOH   L 5 .   ? 12.048 -9.733  12.672 1.00 27.08  ? 411 HOH   C O   1 
HETATM 2488 O  O   . HOH   L 5 .   ? 5.714  -10.696 26.007 1.00 45.79  ? 412 HOH   C O   1 
HETATM 2489 O  O   . HOH   L 5 .   ? 22.295 -12.108 5.650  1.00 25.92  ? 413 HOH   C O   1 
HETATM 2490 O  O   . HOH   L 5 .   ? 26.308 -32.841 13.761 1.00 26.46  ? 414 HOH   C O   1 
HETATM 2491 O  O   . HOH   L 5 .   ? 31.265 -21.925 4.733  1.00 38.51  ? 415 HOH   C O   1 
HETATM 2492 O  O   . HOH   L 5 .   ? 10.327 -22.288 31.959 1.00 44.89  ? 416 HOH   C O   1 
HETATM 2493 O  O   . HOH   L 5 .   ? 4.465  -15.881 21.261 1.00 27.52  ? 417 HOH   C O   1 
HETATM 2494 O  O   . HOH   L 5 .   ? -0.483 -15.920 14.029 1.00 27.79  ? 418 HOH   C O   1 
HETATM 2495 O  O   . HOH   L 5 .   ? 10.625 -14.993 3.408  1.00 42.42  ? 419 HOH   C O   1 
HETATM 2496 O  O   . HOH   L 5 .   ? 24.787 -23.896 19.834 1.00 32.85  ? 420 HOH   C O   1 
HETATM 2497 O  O   . HOH   L 5 .   ? 1.251  -34.163 17.745 1.00 18.68  ? 421 HOH   C O   1 
HETATM 2498 O  O   . HOH   L 5 .   ? 11.875 -38.838 12.873 1.00 29.80  ? 422 HOH   C O   1 
HETATM 2499 O  O   . HOH   L 5 .   ? 24.068 -28.854 18.866 1.00 26.36  ? 423 HOH   C O   1 
HETATM 2500 O  O   . HOH   L 5 .   ? -0.310 -18.612 21.477 1.00 40.72  ? 424 HOH   C O   1 
HETATM 2501 O  O   . HOH   L 5 .   ? 16.060 -17.257 26.129 1.00 28.06  ? 425 HOH   C O   1 
HETATM 2502 O  O   . HOH   L 5 .   ? 22.375 -22.371 20.618 1.00 20.29  ? 426 HOH   C O   1 
HETATM 2503 O  O   . HOH   L 5 .   ? 8.840  -13.664 25.503 1.00 43.00  ? 427 HOH   C O   1 
HETATM 2504 O  O   . HOH   L 5 .   ? 13.514 -42.104 4.301  1.00 49.38  ? 428 HOH   C O   1 
HETATM 2505 O  O   . HOH   L 5 .   ? 31.033 -28.669 11.815 1.00 28.08  ? 429 HOH   C O   1 
HETATM 2506 O  O   . HOH   L 5 .   ? 22.627 -12.947 19.282 1.00 37.85  ? 430 HOH   C O   1 
HETATM 2507 O  O   . HOH   L 5 .   ? 20.216 -8.775  17.496 1.00 34.65  ? 431 HOH   C O   1 
HETATM 2508 O  O   . HOH   L 5 .   ? 6.863  -36.271 2.867  1.00 23.13  ? 432 HOH   C O   1 
HETATM 2509 O  O   . HOH   L 5 .   ? 17.693 -38.667 24.249 1.00 34.89  ? 433 HOH   C O   1 
HETATM 2510 O  O   . HOH   L 5 .   ? 19.196 -21.834 -2.655 1.00 29.07  ? 434 HOH   C O   1 
HETATM 2511 O  O   . HOH   L 5 .   ? 17.452 -34.883 18.184 1.00 30.03  ? 435 HOH   C O   1 
HETATM 2512 O  O   . HOH   L 5 .   ? 17.294 -19.827 28.227 1.00 47.11  ? 436 HOH   C O   1 
HETATM 2513 O  O   . HOH   L 5 .   ? 18.023 -20.002 25.633 1.00 25.89  ? 437 HOH   C O   1 
HETATM 2514 O  O   . HOH   L 5 .   ? 24.284 -15.579 23.064 1.00 50.93  ? 438 HOH   C O   1 
HETATM 2515 O  O   . HOH   L 5 .   ? 5.567  -28.523 4.342  1.00 37.94  ? 439 HOH   C O   1 
HETATM 2516 O  O   . HOH   L 5 .   ? 30.439 -14.966 3.566  1.00 60.37  ? 440 HOH   C O   1 
HETATM 2517 O  O   . HOH   L 5 .   ? 10.788 -14.669 26.539 1.00 52.18  ? 441 HOH   C O   1 
HETATM 2518 O  O   . HOH   L 5 .   ? 8.706  -8.220  26.722 1.00 48.34  ? 442 HOH   C O   1 
HETATM 2519 O  O   . HOH   L 5 .   ? 29.221 -22.039 20.658 1.00 39.32  ? 443 HOH   C O   1 
HETATM 2520 O  O   . HOH   L 5 .   ? 30.484 -31.235 13.101 1.00 39.72  ? 444 HOH   C O   1 
HETATM 2521 O  O   . HOH   L 5 .   ? 17.292 -9.942  29.059 1.00 50.89  ? 445 HOH   C O   1 
HETATM 2522 O  O   . HOH   L 5 .   ? 12.232 -7.591  14.259 1.00 43.70  ? 446 HOH   C O   1 
HETATM 2523 O  O   . HOH   L 5 .   ? 4.351  -22.461 28.308 1.00 35.34  ? 447 HOH   C O   1 
HETATM 2524 O  O   . HOH   L 5 .   ? 12.701 -16.846 1.369  1.00 50.98  ? 448 HOH   C O   1 
HETATM 2525 O  O   . HOH   L 5 .   ? 33.041 -8.808  19.510 1.00 65.22  ? 449 HOH   C O   1 
HETATM 2526 O  O   . HOH   L 5 .   ? 2.366  -17.087 22.770 1.00 37.08  ? 450 HOH   C O   1 
HETATM 2527 O  O   . HOH   L 5 .   ? 2.564  -28.778 27.244 1.00 36.07  ? 451 HOH   C O   1 
HETATM 2528 O  O   . HOH   L 5 .   ? 15.976 -17.325 1.852  1.00 55.29  ? 452 HOH   C O   1 
HETATM 2529 O  O   . HOH   L 5 .   ? 8.449  -23.728 2.708  1.00 31.92  ? 453 HOH   C O   1 
HETATM 2530 O  O   . HOH   L 5 .   ? 17.913 -41.089 5.018  1.00 72.64  ? 454 HOH   C O   1 
HETATM 2531 O  O   . HOH   L 5 .   ? 9.448  -39.382 12.244 1.00 30.23  ? 455 HOH   C O   1 
HETATM 2532 O  O   . HOH   L 5 .   ? -1.405 -13.562 26.434 1.00 50.95  ? 456 HOH   C O   1 
HETATM 2533 O  O   . HOH   L 5 .   ? 32.945 -9.092  11.884 1.00 42.07  ? 457 HOH   C O   1 
HETATM 2534 O  O   . HOH   L 5 .   ? 38.099 -14.437 9.337  1.00 39.97  ? 458 HOH   C O   1 
HETATM 2535 O  O   . HOH   L 5 .   ? 32.167 -27.041 13.644 1.00 34.67  ? 459 HOH   C O   1 
HETATM 2536 O  O   . HOH   L 5 .   ? 29.785 -30.300 16.042 1.00 47.93  ? 460 HOH   C O   1 
HETATM 2537 O  O   . HOH   L 5 .   ? 31.770 -36.049 12.122 1.00 34.17  ? 461 HOH   C O   1 
HETATM 2538 O  O   . HOH   L 5 .   ? 8.563  -21.269 30.038 1.00 31.99  ? 462 HOH   C O   1 
HETATM 2539 O  O   . HOH   L 5 .   ? 29.698 -8.592  9.166  1.00 33.21  ? 463 HOH   C O   1 
HETATM 2540 O  O   . HOH   L 5 .   ? 35.392 -10.050 8.363  1.00 50.93  ? 464 HOH   C O   1 
HETATM 2541 O  O   . HOH   L 5 .   ? 5.472  -39.529 23.294 1.00 31.36  ? 465 HOH   C O   1 
HETATM 2542 O  O   . HOH   L 5 .   ? 20.767 -19.547 -3.062 1.00 33.35  ? 466 HOH   C O   1 
HETATM 2543 O  O   . HOH   L 5 .   ? 28.730 -9.322  6.652  1.00 42.33  ? 467 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   ? 0.2048 0.2179 0.2153 0.0031  -0.0092 0.0080  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.1981 0.2133 0.2165 0.0018  -0.0103 0.0068  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.1936 0.2079 0.2138 -0.0002 -0.0091 0.0041  7   SER   A C   
4    O  O   . SER   A 1   ? 0.2172 0.2296 0.2324 -0.0005 -0.0086 0.0028  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.2430 0.2602 0.2626 0.0028  -0.0148 0.0067  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.2795 0.2960 0.2946 0.0025  -0.0175 0.0041  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.1924 0.2078 0.2198 -0.0014 -0.0080 0.0035  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.1825 0.1963 0.2116 -0.0031 -0.0061 0.0014  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.1766 0.1899 0.2109 -0.0037 -0.0028 0.0017  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.1890 0.2028 0.2242 -0.0029 -0.0017 0.0031  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.1577 0.1698 0.1956 -0.0051 -0.0010 0.0002  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.1683 0.1791 0.2099 -0.0054 0.0027  0.0004  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.1781 0.1847 0.2176 -0.0063 0.0061  -0.0007 9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.1879 0.1932 0.2260 -0.0071 0.0054  -0.0019 9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.1822 0.1964 0.2340 -0.0060 0.0023  0.0004  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1625 0.1660 0.2010 -0.0058 0.0101  -0.0004 10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1750 0.1735 0.2114 -0.0061 0.0144  -0.0008 10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1664 0.1652 0.2116 -0.0072 0.0177  -0.0009 10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1780 0.1788 0.2271 -0.0067 0.0182  -0.0004 10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1788 0.1730 0.2065 -0.0041 0.0167  -0.0003 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.1748 0.1698 0.1957 -0.0027 0.0133  -0.0004 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.2050 0.1928 0.2286 -0.0037 0.0215  -0.0003 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.2056 0.1982 0.2200 -0.0006 0.0141  -0.0005 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1663 0.1632 0.2158 -0.0089 0.0203  -0.0018 11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.1860 0.1833 0.2458 -0.0102 0.0243  -0.0020 11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.1909 0.1807 0.2462 -0.0098 0.0312  -0.0014 11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2208 0.2069 0.2738 -0.0106 0.0328  -0.0018 11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.1880 0.1897 0.2588 -0.0126 0.0217  -0.0038 11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2051 0.2138 0.2799 -0.0123 0.0149  -0.0042 11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2167 0.2300 0.3003 -0.0119 0.0141  -0.0037 11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2279 0.2379 0.2966 -0.0119 0.0096  -0.0047 11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2270 0.2458 0.3126 -0.0109 0.0080  -0.0034 11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2385 0.2538 0.3088 -0.0110 0.0039  -0.0046 11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2381 0.2576 0.3167 -0.0104 0.0029  -0.0038 11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.2579 0.2818 0.3369 -0.0089 -0.0025 -0.0031 11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1985 0.1851 0.2507 -0.0082 0.0355  -0.0003 12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2136 0.1917 0.2586 -0.0070 0.0425  0.0007  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2222 0.1994 0.2741 -0.0072 0.0482  0.0011  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2205 0.2007 0.2743 -0.0063 0.0470  0.0010  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2451 0.2183 0.2743 -0.0038 0.0417  0.0014  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2480 0.2251 0.2759 -0.0025 0.0381  0.0010  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2712 0.2350 0.2915 -0.0017 0.0488  0.0027  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2336 0.2067 0.2907 -0.0084 0.0550  0.0014  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2352 0.2073 0.3003 -0.0086 0.0616  0.0018  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2266 0.2082 0.3069 -0.0102 0.0576  0.0005  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2305 0.2186 0.3198 -0.0123 0.0521  -0.0008 13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2292 0.2115 0.3109 -0.0087 0.0596  0.0009  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2283 0.2193 0.3235 -0.0095 0.0554  0.0001  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2069 0.2009 0.2951 -0.0078 0.0487  0.0003  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2132 0.2109 0.3075 -0.0071 0.0477  0.0003  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2687 0.2597 0.3744 -0.0094 0.0622  0.0003  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3686 0.3592 0.4868 -0.0118 0.0681  -0.0002 14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.4087 0.4063 0.5408 -0.0142 0.0642  -0.0016 14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3810 0.3630 0.4936 -0.0110 0.0774  0.0010  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.1878 0.1803 0.2643 -0.0073 0.0444  0.0003  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1781 0.1730 0.2485 -0.0059 0.0387  0.0005  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1720 0.1712 0.2419 -0.0068 0.0318  0.0002  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1718 0.1697 0.2399 -0.0079 0.0315  -0.0003 15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.1932 0.1815 0.2484 -0.0037 0.0402  0.0005  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2114 0.1942 0.2635 -0.0021 0.0466  0.0005  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2206 0.2057 0.2801 -0.0017 0.0479  0.0003  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2423 0.2169 0.2834 -0.0005 0.0517  0.0008  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2347 0.2141 0.2902 0.0000  0.0540  0.0000  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2558 0.2244 0.2920 0.0014  0.0577  0.0007  15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2644 0.2356 0.3082 0.0016  0.0590  0.0002  15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.3021 0.2669 0.3405 0.0037  0.0652  -0.0002 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1541 0.1579 0.2250 -0.0061 0.0267  0.0006  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1630 0.1701 0.2313 -0.0063 0.0206  0.0006  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1649 0.1706 0.2242 -0.0047 0.0190  0.0012  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1720 0.1781 0.2331 -0.0038 0.0197  0.0016  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1700 0.1838 0.2488 -0.0067 0.0163  0.0008  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.1940 0.2107 0.2688 -0.0060 0.0103  0.0014  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.2001 0.2226 0.2836 -0.0058 0.0057  0.0015  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2223 0.2466 0.3024 -0.0039 0.0019  0.0034  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2627 0.2883 0.3379 -0.0032 -0.0028 0.0037  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2681 0.2936 0.3406 -0.0044 -0.0047 0.0019  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2562 0.2825 0.3283 -0.0012 -0.0050 0.0059  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1607 0.1645 0.2110 -0.0044 0.0173  0.0009  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1547 0.1577 0.1981 -0.0031 0.0157  0.0010  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1550 0.1617 0.1984 -0.0032 0.0112  0.0017  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1586 0.1657 0.1998 -0.0038 0.0093  0.0015  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1760 0.1741 0.2093 -0.0021 0.0171  0.0002  17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1819 0.1800 0.2105 -0.0009 0.0153  -0.0004 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1893 0.1822 0.2203 -0.0017 0.0221  -0.0001 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1437 0.1524 0.1889 -0.0026 0.0098  0.0026  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.1486 0.1600 0.1930 -0.0023 0.0063  0.0038  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.1398 0.1504 0.1814 -0.0016 0.0065  0.0041  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.1435 0.1524 0.1855 -0.0013 0.0085  0.0031  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.1774 0.1921 0.2286 -0.0020 0.0044  0.0053  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2039 0.2204 0.2591 -0.0029 0.0031  0.0045  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.1830 0.1978 0.2401 -0.0014 0.0064  0.0059  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.1301 0.1420 0.1696 -0.0012 0.0046  0.0052  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.1335 0.1452 0.1732 -0.0008 0.0052  0.0057  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.1418 0.1539 0.1875 -0.0004 0.0062  0.0070  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.1452 0.1588 0.1938 0.0002  0.0049  0.0089  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.1416 0.1543 0.1784 -0.0003 0.0040  0.0073  19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.1494 0.1617 0.1806 -0.0003 0.0033  0.0061  19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.1602 0.1725 0.1887 -0.0004 0.0018  0.0060  19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.1625 0.1744 0.1926 -0.0003 0.0041  0.0048  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.1210 0.1317 0.1689 -0.0006 0.0081  0.0059  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.1285 0.1387 0.1823 -0.0002 0.0095  0.0070  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.1357 0.1468 0.1912 0.0008  0.0087  0.0104  20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.1493 0.1609 0.2089 0.0019  0.0085  0.0123  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.1471 0.1551 0.2022 -0.0006 0.0114  0.0047  20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.1417 0.1484 0.2029 -0.0001 0.0134  0.0052  20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.1569 0.1612 0.2194 -0.0008 0.0150  0.0024  20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.1562 0.1583 0.2241 -0.0004 0.0174  0.0021  20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.1660 0.1672 0.2392 -0.0002 0.0186  0.0042  20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.1647 0.1672 0.2381 0.0001  0.0178  0.0075  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.1781 0.1767 0.2562 0.0002  0.0211  0.0035  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.1212 0.1323 0.1732 0.0008  0.0084  0.0113  21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.1394 0.1500 0.1913 0.0022  0.0085  0.0148  21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.1557 0.1678 0.2048 0.0037  0.0055  0.0168  21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.1861 0.1974 0.2341 0.0055  0.0051  0.0201  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.1470 0.1566 0.1966 0.0018  0.0101  0.0152  21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.1412 0.1518 0.1846 0.0018  0.0086  0.0147  21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.1531 0.1647 0.1950 0.0006  0.0080  0.0114  21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.1502 0.1605 0.1883 0.0031  0.0079  0.0170  21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.1534 0.1654 0.1899 0.0011  0.0071  0.0119  21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.1542 0.1654 0.1880 0.0025  0.0071  0.0150  21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.1621 0.1760 0.2096 0.0030  0.0033  0.0149  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.1584 0.1742 0.2043 0.0041  -0.0002 0.0158  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.1672 0.1852 0.2201 0.0040  -0.0013 0.0149  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.1815 0.2018 0.2353 0.0045  -0.0046 0.0147  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.1555 0.1715 0.1952 0.0033  -0.0018 0.0140  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.1632 0.1774 0.1966 0.0037  -0.0006 0.0149  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.1848 0.1991 0.2127 0.0031  -0.0020 0.0129  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.1723 0.1854 0.2025 0.0061  -0.0010 0.0185  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.1602 0.1774 0.2184 0.0032  0.0017  0.0139  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.1685 0.1875 0.2340 0.0031  0.0018  0.0131  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.1698 0.1912 0.2400 0.0054  -0.0010 0.0156  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.1721 0.1920 0.2412 0.0072  -0.0009 0.0183  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.1656 0.1823 0.2346 0.0025  0.0059  0.0119  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.1751 0.1999 0.2512 0.0054  -0.0032 0.0146  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.1801 0.2080 0.2617 0.0079  -0.0069 0.0164  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.1883 0.2167 0.2794 0.0088  -0.0042 0.0172  24  THR   A C   
137  O  O   . THR   A 18  ? 0.1885 0.2148 0.2819 0.0073  0.0004  0.0157  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.2095 0.2417 0.2947 0.0073  -0.0111 0.0142  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.2009 0.2342 0.2942 0.0051  -0.0079 0.0117  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.2389 0.2703 0.3150 0.0062  -0.0134 0.0129  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.2078 0.2390 0.3046 0.0118  -0.0075 0.0192  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.2216 0.2538 0.3290 0.0130  -0.0052 0.0198  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.1815 0.2159 0.2974 0.0106  -0.0025 0.0165  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.1986 0.2311 0.3193 0.0101  0.0027  0.0159  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.2581 0.2941 0.3710 0.0168  -0.0103 0.0222  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.3618 0.3946 0.4664 0.0201  -0.0122 0.0263  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4017 0.4289 0.5029 0.0205  -0.0075 0.0286  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4009 0.4350 0.5004 0.0233  -0.0182 0.0283  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4191 0.4442 0.5134 0.0237  -0.0099 0.0324  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4229 0.4517 0.5148 0.0257  -0.0164 0.0324  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.1814 0.2194 0.2989 0.0090  -0.0055 0.0142  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.1836 0.2231 0.3092 0.0066  -0.0023 0.0114  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.1695 0.2036 0.2885 0.0043  0.0039  0.0100  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.1774 0.2102 0.3017 0.0034  0.0091  0.0088  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.2320 0.2758 0.3608 0.0053  -0.0066 0.0090  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.3880 0.4334 0.5270 0.0027  -0.0027 0.0063  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.4359 0.4850 0.5881 0.0034  -0.0016 0.0060  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.4358 0.4780 0.5690 -0.0001 0.0000  0.0044  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.1626 0.1930 0.2693 0.0035  0.0036  0.0102  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.1738 0.1992 0.2738 0.0019  0.0085  0.0088  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.1641 0.1865 0.2661 0.0029  0.0127  0.0093  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.1650 0.1844 0.2671 0.0021  0.0175  0.0076  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.1657 0.1886 0.2541 0.0015  0.0068  0.0091  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.1828 0.2068 0.2671 0.0002  0.0041  0.0079  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.2051 0.2294 0.2928 -0.0013 0.0057  0.0061  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.1875 0.2118 0.2655 0.0008  0.0007  0.0088  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.1559 0.1783 0.2587 0.0048  0.0113  0.0115  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.1658 0.1849 0.2708 0.0057  0.0153  0.0117  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.1809 0.2014 0.2967 0.0065  0.0183  0.0113  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.1935 0.2102 0.3097 0.0064  0.0233  0.0099  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.1630 0.1812 0.2668 0.0075  0.0135  0.0145  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.1679 0.1829 0.2623 0.0064  0.0134  0.0143  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.1980 0.2138 0.2862 0.0065  0.0101  0.0157  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.1675 0.1781 0.2584 0.0053  0.0169  0.0123  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.1943 0.2068 0.2766 0.0053  0.0118  0.0149  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.1855 0.1951 0.2695 0.0045  0.0154  0.0125  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.1839 0.1913 0.2767 0.0050  0.0209  0.0099  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.1877 0.1940 0.2686 0.0034  0.0174  0.0104  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.1868 0.1903 0.2747 0.0040  0.0225  0.0076  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.1938 0.1972 0.2766 0.0031  0.0206  0.0077  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.1749 0.2007 0.2994 0.0072  0.0155  0.0119  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.1811 0.2092 0.3181 0.0079  0.0185  0.0114  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2007 0.2271 0.3385 0.0057  0.0238  0.0087  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2224 0.2488 0.3689 0.0061  0.0286  0.0080  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.1897 0.2249 0.3367 0.0094  0.0131  0.0125  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.1820 0.2067 0.3110 0.0036  0.0233  0.0074  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.1933 0.2150 0.3207 0.0018  0.0284  0.0055  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.1780 0.1930 0.2907 0.0013  0.0307  0.0045  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.1754 0.1875 0.2818 0.0000  0.0326  0.0033  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.1984 0.2239 0.3294 0.0001  0.0257  0.0047  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2286 0.2610 0.3754 0.0005  0.0236  0.0047  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2557 0.2889 0.4130 0.0002  0.0285  0.0039  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2365 0.2740 0.3854 0.0015  0.0162  0.0056  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.1693 0.1816 0.2774 0.0025  0.0305  0.0048  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.1855 0.1926 0.2812 0.0022  0.0313  0.0035  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.1960 0.1973 0.2857 0.0021  0.0370  0.0014  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2150 0.2143 0.3093 0.0030  0.0419  0.0009  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.1823 0.1879 0.2774 0.0033  0.0306  0.0038  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.1978 0.1986 0.2822 0.0030  0.0309  0.0018  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.1957 0.1980 0.2733 0.0019  0.0266  0.0021  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2188 0.2178 0.3054 0.0038  0.0311  0.0017  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.1903 0.1886 0.2693 0.0015  0.0366  0.0004  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2095 0.2011 0.2796 0.0022  0.0414  -0.0014 32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2320 0.2199 0.2919 0.0031  0.0396  -0.0034 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2601 0.2430 0.3154 0.0044  0.0429  -0.0054 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2198 0.2101 0.2849 0.0014  0.0422  -0.0012 32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2344 0.2168 0.2872 0.0028  0.0466  -0.0026 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2285 0.2220 0.3053 0.0002  0.0447  0.0000  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2051 0.1956 0.2618 0.0024  0.0343  -0.0032 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2071 0.1951 0.2561 0.0029  0.0322  -0.0054 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.1792 0.1718 0.2302 0.0019  0.0271  -0.0042 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.1908 0.1868 0.2433 0.0011  0.0249  -0.0023 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2154 0.1986 0.2521 0.0040  0.0329  -0.0071 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2201 0.2021 0.2491 0.0046  0.0292  -0.0096 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2414 0.2199 0.2660 0.0057  0.0291  -0.0130 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2052 0.1897 0.2308 0.0042  0.0248  -0.0094 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2444 0.2240 0.2646 0.0058  0.0244  -0.0149 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2260 0.2091 0.2464 0.0050  0.0221  -0.0126 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2192 0.2071 0.2461 0.0032  0.0229  -0.0071 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2269 0.2122 0.2442 0.0051  0.0179  -0.0133 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2368 0.2262 0.2594 0.0033  0.0192  -0.0077 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2316 0.2200 0.2500 0.0043  0.0168  -0.0106 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.1777 0.1700 0.2286 0.0019  0.0254  -0.0056 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.1712 0.1669 0.2233 0.0010  0.0215  -0.0046 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.1685 0.1624 0.2175 0.0010  0.0202  -0.0078 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.1821 0.1725 0.2304 0.0015  0.0219  -0.0105 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.1772 0.1761 0.2379 0.0007  0.0209  -0.0015 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.1745 0.1718 0.2416 0.0013  0.0235  -0.0016 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2062 0.2012 0.2740 0.0010  0.0236  -0.0037 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2539 0.2455 0.3239 0.0015  0.0263  -0.0055 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.1916 0.1878 0.2586 0.0002  0.0214  -0.0037 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.1721 0.1685 0.2199 0.0004  0.0171  -0.0076 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.1681 0.1639 0.2150 0.0001  0.0153  -0.0108 35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.1657 0.1651 0.2170 -0.0010 0.0136  -0.0090 35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.1556 0.1573 0.2038 -0.0010 0.0117  -0.0079 35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.1960 0.1897 0.2336 0.0014  0.0138  -0.0139 35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.2641 0.2575 0.3009 0.0015  0.0111  -0.0183 35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.2962 0.2922 0.3405 0.0000  0.0103  -0.0186 35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.2749 0.2655 0.3037 0.0032  0.0099  -0.0214 35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.1699 0.1695 0.2282 -0.0018 0.0145  -0.0088 36  SER   A N   
241  C  CA  A SER   A 30  ? 0.1748 0.1766 0.2375 -0.0027 0.0142  -0.0068 36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.1700 0.1719 0.2326 -0.0027 0.0141  -0.0068 36  SER   A CA  
243  C  C   . SER   A 30  ? 0.1684 0.1721 0.2296 -0.0032 0.0118  -0.0096 36  SER   A C   
244  O  O   . SER   A 30  ? 0.1812 0.1874 0.2428 -0.0035 0.0112  -0.0076 36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2112 0.2113 0.2818 -0.0034 0.0166  -0.0064 36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.1930 0.1935 0.2636 -0.0034 0.0165  -0.0060 36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2685 0.2700 0.3434 -0.0042 0.0172  -0.0041 36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2305 0.2291 0.3040 -0.0043 0.0166  -0.0106 36  SER   A OG  
249  N  N   . SER   A 31  ? 0.1674 0.1698 0.2267 -0.0030 0.0103  -0.0144 37  SER   A N   
250  C  CA  . SER   A 31  ? 0.1723 0.1771 0.2313 -0.0031 0.0073  -0.0175 37  SER   A CA  
251  C  C   . SER   A 31  ? 0.1663 0.1727 0.2180 -0.0018 0.0055  -0.0161 37  SER   A C   
252  O  O   . SER   A 31  ? 0.1864 0.1954 0.2388 -0.0017 0.0033  -0.0175 37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2173 0.2205 0.2753 -0.0027 0.0051  -0.0234 37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3013 0.3015 0.3489 -0.0006 0.0041  -0.0246 37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1478 0.1524 0.1933 -0.0009 0.0064  -0.0137 38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1495 0.1547 0.1882 0.0002  0.0052  -0.0124 38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.1548 0.1617 0.1949 -0.0005 0.0064  -0.0080 38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.1500 0.1574 0.1854 0.0001  0.0055  -0.0068 38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1651 0.1665 0.1958 0.0018  0.0058  -0.0130 38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1814 0.1804 0.2071 0.0033  0.0040  -0.0175 38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.1787 0.1726 0.1949 0.0053  0.0055  -0.0177 38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.1745 0.1678 0.1844 0.0065  0.0053  -0.0157 38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.1913 0.1799 0.1912 0.0089  0.0059  -0.0162 38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2208 0.2049 0.2147 0.0107  0.0065  -0.0188 38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.1945 0.1823 0.1895 0.0098  0.0060  -0.0142 38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.1452 0.1526 0.1909 -0.0014 0.0081  -0.0056 39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.1369 0.1454 0.1827 -0.0014 0.0086  -0.0017 39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.1396 0.1472 0.1814 -0.0009 0.0086  -0.0009 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.1400 0.1487 0.1798 -0.0009 0.0077  0.0010  39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.1464 0.1571 0.1913 -0.0015 0.0078  -0.0002 39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.1360 0.1472 0.1799 -0.0012 0.0079  0.0034  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.1322 0.1429 0.1795 -0.0011 0.0089  0.0055  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.1389 0.1510 0.1786 -0.0008 0.0069  0.0041  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.1340 0.1392 0.1749 -0.0006 0.0098  -0.0025 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.1337 0.1379 0.1725 -0.0004 0.0108  -0.0017 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.1322 0.1358 0.1762 -0.0004 0.0130  -0.0009 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.1448 0.1469 0.1914 -0.0002 0.0144  -0.0020 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1446 0.1454 0.1760 0.0006  0.0114  -0.0039 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.1615 0.1626 0.1873 0.0012  0.0093  -0.0046 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1854 0.1821 0.2031 0.0029  0.0102  -0.0064 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.1746 0.1773 0.2004 0.0006  0.0087  -0.0024 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.1375 0.1421 0.1835 -0.0006 0.0134  0.0007  41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.1443 0.1487 0.1962 -0.0005 0.0157  0.0013  41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.1405 0.1446 0.1921 -0.0008 0.0170  0.0013  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.1433 0.1489 0.1932 -0.0014 0.0151  0.0018  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.1403 0.1480 0.1994 -0.0003 0.0143  0.0038  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.1508 0.1591 0.2178 0.0002  0.0163  0.0046  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.1704 0.1799 0.2427 0.0012  0.0155  0.0066  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.1657 0.1770 0.2367 -0.0001 0.0154  0.0053  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.1462 0.1479 0.1996 -0.0005 0.0208  0.0006  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.1502 0.1509 0.2051 -0.0010 0.0235  0.0006  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.1664 0.1692 0.2319 -0.0011 0.0256  0.0014  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.1791 0.1806 0.2470 -0.0002 0.0279  0.0011  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.1749 0.1694 0.2211 -0.0002 0.0274  -0.0008 42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.1908 0.1835 0.2396 -0.0008 0.0315  -0.0004 42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.1920 0.1848 0.2282 0.0004  0.0247  -0.0017 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.1704 0.1769 0.2431 -0.0021 0.0246  0.0021  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.1603 0.1699 0.2451 -0.0021 0.0261  0.0026  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.1770 0.1856 0.2659 -0.0033 0.0301  0.0019  43  SER   A C   
300  O  O   . SER   A 37  ? 0.1852 0.1913 0.2682 -0.0043 0.0306  0.0013  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.1697 0.1854 0.2613 -0.0020 0.0205  0.0039  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.1877 0.2056 0.2776 -0.0031 0.0167  0.0036  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.1793 0.1896 0.2793 -0.0033 0.0334  0.0019  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.1983 0.2077 0.3047 -0.0046 0.0383  0.0012  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2168 0.2328 0.3346 -0.0063 0.0341  0.0007  44  SER   A C   
306  O  O   . SER   A 38  ? 0.2216 0.2435 0.3456 -0.0057 0.0284  0.0011  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2327 0.2402 0.3457 -0.0037 0.0449  0.0012  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.2724 0.2860 0.3974 -0.0029 0.0423  0.0017  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.2274 0.2421 0.3481 -0.0082 0.0370  -0.0003 45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2432 0.2639 0.3755 -0.0102 0.0331  -0.0016 45  THR   A CA  
311  C  C   . THR   A 39  ? 0.2775 0.2988 0.4240 -0.0118 0.0395  -0.0026 45  THR   A C   
312  O  O   . THR   A 39  ? 0.2794 0.2943 0.4227 -0.0115 0.0477  -0.0020 45  THR   A O   
313  C  CB  . THR   A 39  ? 0.2539 0.2723 0.3772 -0.0116 0.0304  -0.0024 45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.2716 0.2826 0.3895 -0.0123 0.0378  -0.0023 45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.2520 0.2691 0.3612 -0.0101 0.0255  -0.0015 45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3033 0.3317 0.4652 -0.0133 0.0358  -0.0044 46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3287 0.3584 0.5066 -0.0153 0.0418  -0.0057 46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3474 0.3730 0.5235 -0.0182 0.0445  -0.0071 46  THR   A C   
319  O  O   . THR   A 40  ? 0.3752 0.3963 0.5562 -0.0196 0.0533  -0.0071 46  THR   A O   
320  C  CB  . THR   A 40  ? 0.3592 0.3993 0.5569 -0.0155 0.0365  -0.0074 46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.3806 0.4257 0.5766 -0.0157 0.0264  -0.0088 46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3750 0.4180 0.5761 -0.0125 0.0360  -0.0057 46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3289 0.3554 0.4979 -0.0189 0.0375  -0.0082 47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3222 0.3446 0.4892 -0.0214 0.0395  -0.0096 47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3166 0.3288 0.4641 -0.0202 0.0445  -0.0073 47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.3016 0.3119 0.4357 -0.0176 0.0424  -0.0055 47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3318 0.3593 0.4994 -0.0224 0.0298  -0.0120 47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3151 0.3208 0.4615 -0.0219 0.0507  -0.0075 48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3255 0.3212 0.4536 -0.0204 0.0553  -0.0053 48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3235 0.3192 0.4405 -0.0201 0.0480  -0.0059 48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3390 0.3385 0.4632 -0.0223 0.0436  -0.0084 48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.3826 0.3709 0.5144 -0.0222 0.0649  -0.0051 48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.4885 0.4660 0.6017 -0.0203 0.0692  -0.0028 48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.6007 0.5713 0.7003 -0.0167 0.0747  0.0000  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6287 0.6016 0.7333 -0.0158 0.0770  0.0004  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6261 0.5881 0.7081 -0.0143 0.0767  0.0019  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3001 0.2918 0.4004 -0.0173 0.0469  -0.0040 49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.3144 0.3064 0.4042 -0.0166 0.0403  -0.0044 49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.3458 0.3317 0.4282 -0.0172 0.0417  -0.0047 49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.3848 0.3628 0.4624 -0.0167 0.0489  -0.0033 49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.3140 0.3026 0.3925 -0.0174 0.0350  -0.0060 50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.3092 0.2926 0.3816 -0.0179 0.0354  -0.0066 50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.3167 0.2931 0.3723 -0.0148 0.0372  -0.0043 50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.3127 0.2833 0.3637 -0.0149 0.0395  -0.0043 50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.3017 0.2908 0.3770 -0.0192 0.0276  -0.0093 50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.3163 0.3110 0.3831 -0.0166 0.0199  -0.0084 50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.3014 0.2784 0.3485 -0.0120 0.0358  -0.0026 51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.2845 0.2566 0.3166 -0.0088 0.0355  -0.0011 51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.2838 0.2477 0.3065 -0.0060 0.0420  0.0011  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.3147 0.2775 0.3419 -0.0064 0.0466  0.0017  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.2808 0.2591 0.3101 -0.0075 0.0293  -0.0012 51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3063 0.2904 0.3394 -0.0089 0.0232  -0.0028 51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3081 0.2898 0.3370 -0.0090 0.0222  -0.0035 51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.2446 0.2354 0.2836 -0.0095 0.0192  -0.0032 51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2593 0.2175 0.2687 -0.0029 0.0420  0.0023  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.2847 0.2348 0.2809 0.0011  0.0459  0.0043  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.2621 0.2153 0.2502 0.0039  0.0400  0.0039  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2589 0.2162 0.2472 0.0036  0.0350  0.0030  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3376 0.2794 0.3259 0.0027  0.0488  0.0056  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.4064 0.3433 0.4009 0.0005  0.0556  0.0062  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.3643 0.2982 0.3361 0.0081  0.0503  0.0077  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.2407 0.1919 0.2222 0.0065  0.0408  0.0042  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.2257 0.1796 0.2006 0.0091  0.0354  0.0033  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.2329 0.1800 0.1942 0.0135  0.0356  0.0042  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.2568 0.1955 0.2098 0.0159  0.0408  0.0058  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.2210 0.1768 0.1967 0.0095  0.0354  0.0024  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.2316 0.1933 0.2207 0.0057  0.0360  0.0019  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.2259 0.1855 0.1973 0.0115  0.0294  0.0008  53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.2409 0.2110 0.2384 0.0033  0.0303  0.0010  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2172 0.1677 0.1761 0.0148  0.0301  0.0034  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2280 0.1732 0.1747 0.0196  0.0289  0.0040  54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2392 0.1824 0.1777 0.0229  0.0278  0.0031  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2317 0.1804 0.1748 0.0217  0.0251  0.0011  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.2261 0.1771 0.1746 0.0201  0.0229  0.0028  54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2534 0.1881 0.1787 0.0276  0.0298  0.0045  55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.2545 0.1864 0.1693 0.0318  0.0279  0.0031  55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.2797 0.2087 0.1839 0.0370  0.0237  0.0033  55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.3079 0.2275 0.2001 0.0411  0.0271  0.0058  55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.2761 0.1987 0.1830 0.0332  0.0352  0.0049  55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.2766 0.2019 0.1953 0.0282  0.0400  0.0049  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.2710 0.2046 0.1981 0.0258  0.0358  0.0019  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.2814 0.2168 0.2193 0.0218  0.0408  0.0024  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.2855 0.2282 0.2339 0.0188  0.0386  0.0007  55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.2559 0.2047 0.2061 0.0189  0.0320  -0.0017 55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.2976 0.2417 0.2560 0.0157  0.0430  0.0014  55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.2746 0.2118 0.1841 0.0370  0.0167  0.0009  56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.2759 0.2128 0.1798 0.0412  0.0122  0.0009  56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.2774 0.2239 0.1880 0.0412  0.0044  -0.0028 56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.2749 0.2280 0.1947 0.0375  0.0029  -0.0051 56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.2529 0.1893 0.1617 0.0394  0.0147  0.0032  56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.2576 0.2055 0.1841 0.0329  0.0125  0.0015  56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.2989 0.2464 0.2061 0.0452  -0.0003 -0.0033 57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.2995 0.2567 0.2152 0.0451  -0.0073 -0.0068 57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.2975 0.2598 0.2217 0.0439  -0.0083 -0.0061 57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.3065 0.2747 0.2351 0.0458  -0.0137 -0.0084 57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.3600 0.3158 0.2661 0.0514  -0.0133 -0.0092 57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.4489 0.3980 0.3434 0.0576  -0.0139 -0.0068 57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.4499 0.3942 0.3430 0.0571  -0.0088 -0.0030 57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5497 0.4981 0.4364 0.0633  -0.0197 -0.0088 57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.2634 0.2237 0.1909 0.0405  -0.0031 -0.0035 58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2450 0.2094 0.1799 0.0392  -0.0036 -0.0031 58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2372 0.2120 0.1844 0.0364  -0.0074 -0.0058 58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2303 0.2088 0.1830 0.0331  -0.0074 -0.0072 58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.2588 0.2200 0.1963 0.0353  0.0021  -0.0007 58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.2791 0.2280 0.2050 0.0383  0.0076  0.0029  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2251 0.2043 0.1769 0.0379  -0.0101 -0.0066 59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.2176 0.2059 0.1816 0.0352  -0.0122 -0.0086 59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.2070 0.1964 0.1755 0.0335  -0.0096 -0.0072 59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2045 0.2005 0.1818 0.0326  -0.0109 -0.0085 59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2453 0.2392 0.2131 0.0385  -0.0180 -0.0117 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.3015 0.2965 0.2680 0.0389  -0.0213 -0.0144 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3475 0.3494 0.3205 0.0416  -0.0276 -0.0182 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3643 0.3642 0.3300 0.0465  -0.0320 -0.0198 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.2737 0.2839 0.2608 0.0386  -0.0282 -0.0200 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.1939 0.1765 0.1563 0.0333  -0.0057 -0.0047 60  THR   A N   
416  C  CA  . THR   A 54  ? 0.2040 0.1866 0.1698 0.0310  -0.0029 -0.0037 60  THR   A CA  
417  C  C   . THR   A 54  ? 0.2041 0.1821 0.1679 0.0274  0.0011  -0.0023 60  THR   A C   
418  O  O   . THR   A 54  ? 0.2168 0.1896 0.1750 0.0277  0.0028  -0.0014 60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2241 0.2030 0.1858 0.0350  -0.0026 -0.0028 60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2738 0.2438 0.2256 0.0375  -0.0005 -0.0009 60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2370 0.2209 0.2018 0.0391  -0.0069 -0.0044 60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.1948 0.1746 0.1631 0.0241  0.0027  -0.0023 61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.1945 0.1713 0.1629 0.0205  0.0057  -0.0016 61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.1724 0.1521 0.1453 0.0178  0.0060  -0.0022 61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.1823 0.1643 0.1565 0.0192  0.0053  -0.0028 61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.1667 0.1457 0.1415 0.0143  0.0074  -0.0022 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.1652 0.1459 0.1425 0.0119  0.0074  -0.0030 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.1626 0.1474 0.1444 0.0091  0.0064  -0.0030 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.1748 0.1585 0.1578 0.0078  0.0071  -0.0026 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.1878 0.1625 0.1626 0.0110  0.0095  -0.0035 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2030 0.1793 0.1797 0.0085  0.0088  -0.0049 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.2190 0.1891 0.1891 0.0143  0.0107  -0.0032 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.1669 0.1559 0.1510 0.0082  0.0052  -0.0032 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.1546 0.1470 0.1426 0.0059  0.0042  -0.0029 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.1519 0.1444 0.1393 0.0045  0.0035  -0.0035 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.1583 0.1494 0.1423 0.0054  0.0039  -0.0042 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.1581 0.1553 0.1497 0.0064  0.0034  -0.0022 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.1501 0.1499 0.1422 0.0071  0.0035  -0.0020 63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.1632 0.1629 0.1542 0.0092  0.0042  -0.0025 63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.1609 0.1629 0.1544 0.0060  0.0034  -0.0011 63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.1573 0.1592 0.1495 0.0099  0.0052  -0.0023 63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.1665 0.1699 0.1598 0.0069  0.0045  -0.0006 63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.1607 0.1641 0.1537 0.0087  0.0057  -0.0012 63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.1754 0.1801 0.1689 0.0096  0.0078  -0.0007 63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.1515 0.1457 0.1419 0.0025  0.0024  -0.0034 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.1567 0.1516 0.1463 0.0016  0.0007  -0.0041 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.1617 0.1599 0.1510 0.0024  -0.0001 -0.0026 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.1606 0.1615 0.1537 0.0022  -0.0001 -0.0012 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.1559 0.1510 0.1495 -0.0006 -0.0007 -0.0051 64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.1754 0.1713 0.1674 -0.0011 -0.0036 -0.0063 64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.1901 0.1828 0.1774 -0.0009 -0.0040 -0.0084 64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.1783 0.1776 0.1728 -0.0013 -0.0061 -0.0055 64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.1950 0.1881 0.1795 -0.0009 -0.0071 -0.0101 64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.1898 0.1896 0.1812 -0.0010 -0.0093 -0.0066 64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.2081 0.2048 0.1943 -0.0008 -0.0100 -0.0091 64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.2499 0.2466 0.2319 -0.0002 -0.0137 -0.0107 64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.1681 0.1654 0.1526 0.0034  -0.0001 -0.0029 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.1595 0.1586 0.1423 0.0045  0.0002  -0.0012 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.1769 0.1754 0.1556 0.0045  -0.0024 -0.0016 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.1817 0.1773 0.1542 0.0052  -0.0028 -0.0032 65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.1695 0.1676 0.1492 0.0063  0.0028  -0.0011 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.1883 0.1873 0.1655 0.0079  0.0050  0.0013  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.1678 0.1685 0.1494 0.0040  -0.0043 -0.0004 66  SER   A N   
464  C  CA  . SER   A 60  ? 0.1767 0.1771 0.1546 0.0045  -0.0077 -0.0009 66  SER   A CA  
465  C  C   . SER   A 60  ? 0.1901 0.1884 0.1591 0.0069  -0.0070 0.0002  66  SER   A C   
466  O  O   . SER   A 60  ? 0.2080 0.2043 0.1706 0.0077  -0.0099 -0.0016 66  SER   A O   
467  C  CB  . SER   A 60  ? 0.2191 0.2227 0.2028 0.0040  -0.0098 0.0005  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.2983 0.3029 0.2830 0.0051  -0.0076 0.0037  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.1748 0.1730 0.1431 0.0081  -0.0030 0.0028  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.1778 0.1731 0.1374 0.0106  -0.0009 0.0043  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.1871 0.1790 0.1402 0.0115  0.0004  0.0019  67  SER   A C   
472  O  O   . SER   A 61  ? 0.2010 0.1899 0.1458 0.0137  0.0025  0.0028  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.1950 0.1912 0.1577 0.0114  0.0037  0.0076  67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.1938 0.1916 0.1628 0.0104  0.0066  0.0069  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.1789 0.1708 0.1352 0.0099  -0.0003 -0.0009 68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.1820 0.1703 0.1328 0.0105  0.0005  -0.0036 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.1989 0.1858 0.1495 0.0089  -0.0035 -0.0072 68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.2197 0.2030 0.1662 0.0091  -0.0030 -0.0099 68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.2022 0.1909 0.1574 0.0107  0.0044  -0.0033 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.1988 0.1889 0.1550 0.0123  0.0088  -0.0005 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.2225 0.2086 0.1694 0.0147  0.0115  -0.0005 68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.2402 0.2273 0.1893 0.0161  0.0168  0.0024  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.2247 0.2118 0.1722 0.0169  0.0184  0.0054  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.2267 0.2128 0.1694 0.0168  0.0147  0.0061  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.2283 0.2160 0.1791 0.0179  0.0239  0.0078  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.2075 0.1971 0.1640 0.0070  -0.0068 -0.0075 69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.2253 0.2142 0.1852 0.0048  -0.0099 -0.0110 69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.2325 0.2186 0.1941 0.0040  -0.0069 -0.0125 69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.2529 0.2355 0.2125 0.0032  -0.0078 -0.0159 69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.2739 0.2608 0.2272 0.0053  -0.0140 -0.0142 69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.3638 0.3536 0.3170 0.0060  -0.0181 -0.0131 69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.4082 0.3975 0.3603 0.0052  -0.0239 -0.0177 69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.4150 0.4062 0.3630 0.0074  -0.0283 -0.0165 69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.4022 0.3902 0.3376 0.0107  -0.0296 -0.0164 69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.4259 0.4089 0.3521 0.0118  -0.0270 -0.0180 69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.3542 0.3436 0.2854 0.0133  -0.0333 -0.0145 69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.2122 0.1994 0.1773 0.0044  -0.0035 -0.0101 70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.2157 0.1998 0.1811 0.0047  -0.0007 -0.0110 70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.2006 0.1867 0.1722 0.0044  0.0009  -0.0090 70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.1933 0.1831 0.1680 0.0045  0.0007  -0.0068 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.2580 0.2404 0.2179 0.0073  0.0022  -0.0105 70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.3859 0.3635 0.3384 0.0080  0.0020  -0.0135 70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.4830 0.4591 0.4315 0.0107  0.0058  -0.0127 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.5658 0.5362 0.5074 0.0116  0.0066  -0.0159 70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6287 0.5974 0.5616 0.0125  0.0052  -0.0171 70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.1932 0.1761 0.1655 0.0044  0.0025  -0.0097 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.1783 0.1620 0.1540 0.0051  0.0041  -0.0080 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.1972 0.1804 0.1707 0.0079  0.0060  -0.0073 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.2265 0.2065 0.1962 0.0090  0.0071  -0.0086 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.1866 0.1662 0.1638 0.0040  0.0051  -0.0088 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.1901 0.1705 0.1716 0.0012  0.0037  -0.0096 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.2443 0.2265 0.2303 0.0003  0.0042  -0.0082 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.1891 0.1686 0.1717 -0.0008 0.0020  -0.0120 71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.2121 0.1947 0.2026 -0.0022 0.0030  -0.0096 71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.2498 0.2313 0.2388 -0.0030 0.0013  -0.0120 71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.1778 0.1641 0.1543 0.0091  0.0063  -0.0057 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.1792 0.1663 0.1557 0.0119  0.0075  -0.0054 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.1837 0.1708 0.1619 0.0134  0.0072  -0.0047 72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.1800 0.1687 0.1605 0.0123  0.0062  -0.0041 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.1792 0.1715 0.1590 0.0123  0.0078  -0.0044 72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.1862 0.1781 0.1627 0.0119  0.0087  -0.0045 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.2098 0.1990 0.1824 0.0136  0.0106  -0.0055 72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.2006 0.1943 0.1772 0.0103  0.0077  -0.0037 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.2112 0.1991 0.1788 0.0137  0.0117  -0.0057 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.2138 0.2063 0.1856 0.0107  0.0085  -0.0035 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.2168 0.2063 0.1836 0.0123  0.0105  -0.0046 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.2514 0.2388 0.2116 0.0131  0.0114  -0.0046 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.1762 0.1613 0.1529 0.0163  0.0079  -0.0048 73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.1863 0.1714 0.1634 0.0186  0.0070  -0.0042 73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.1923 0.1841 0.1750 0.0195  0.0053  -0.0043 73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2172 0.2127 0.2036 0.0195  0.0060  -0.0046 73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.1974 0.1782 0.1711 0.0219  0.0082  -0.0043 73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2006 0.1824 0.1750 0.0216  0.0096  -0.0052 73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.1758 0.1582 0.1499 0.0179  0.0096  -0.0056 73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.1794 0.1723 0.1630 0.0203  0.0035  -0.0042 74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.1794 0.1786 0.1692 0.0209  0.0014  -0.0050 74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.1837 0.1825 0.1720 0.0241  -0.0012 -0.0056 74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.1928 0.1863 0.1746 0.0251  -0.0011 -0.0049 74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2064 0.2083 0.1996 0.0176  0.0012  -0.0048 74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2306 0.2347 0.2268 0.0154  0.0030  -0.0043 74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2118 0.2096 0.2007 0.0162  0.0015  -0.0041 74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.1854 0.1899 0.1801 0.0258  -0.0035 -0.0070 75  SER   A N   
543  C  CA  . SER   A 69  ? 0.1887 0.1949 0.1838 0.0286  -0.0073 -0.0085 75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1832 0.1944 0.1851 0.0258  -0.0085 -0.0099 75  SER   A C   
545  O  O   . SER   A 69  ? 0.1885 0.2043 0.1983 0.0236  -0.0071 -0.0102 75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2405 0.2507 0.2405 0.0322  -0.0094 -0.0099 75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3429 0.3479 0.3365 0.0353  -0.0083 -0.0085 75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1696 0.1789 0.1678 0.0258  -0.0102 -0.0106 76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1581 0.1712 0.1625 0.0229  -0.0108 -0.0119 76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1699 0.1845 0.1744 0.0252  -0.0152 -0.0148 76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.1834 0.1943 0.1797 0.0289  -0.0175 -0.0151 76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1655 0.1749 0.1663 0.0197  -0.0079 -0.0100 76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1607 0.1631 0.1514 0.0208  -0.0069 -0.0087 76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.1880 0.1859 0.1737 0.0210  -0.0044 -0.0067 76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.1752 0.1750 0.1616 0.0217  -0.0080 -0.0095 76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.2022 0.1934 0.1800 0.0217  -0.0026 -0.0054 76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.1895 0.1822 0.1668 0.0228  -0.0059 -0.0079 76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.2084 0.1970 0.1819 0.0228  -0.0031 -0.0058 76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1687 0.1883 0.1821 0.0231  -0.0163 -0.0170 77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1745 0.1958 0.1888 0.0248  -0.0210 -0.0206 77  SER   A CA  
561  C  C   . SER   A 71  ? 0.1879 0.2035 0.1930 0.0248  -0.0209 -0.0205 77  SER   A C   
562  O  O   . SER   A 71  ? 0.1986 0.2105 0.2003 0.0224  -0.0169 -0.0178 77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1874 0.2157 0.2157 0.0222  -0.0219 -0.0235 77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2219 0.2493 0.2529 0.0181  -0.0179 -0.0217 77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.1820 0.1968 0.1828 0.0278  -0.0252 -0.0235 78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.1931 0.2021 0.1847 0.0282  -0.0247 -0.0237 78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.1935 0.2046 0.1928 0.0237  -0.0226 -0.0245 78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2110 0.2282 0.2224 0.0213  -0.0235 -0.0264 78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2370 0.2450 0.2223 0.0328  -0.0305 -0.0274 78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.2720 0.2761 0.2471 0.0379  -0.0321 -0.0257 78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.3451 0.3474 0.3118 0.0433  -0.0384 -0.0293 78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4433 0.4393 0.3971 0.0486  -0.0384 -0.0264 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.5166 0.5103 0.4605 0.0548  -0.0449 -0.0294 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.1976 0.2034 0.1906 0.0226  -0.0196 -0.0232 79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.2029 0.2102 0.2032 0.0187  -0.0175 -0.0238 79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.2053 0.2167 0.2130 0.0184  -0.0215 -0.0288 79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.2186 0.2286 0.2206 0.0215  -0.0256 -0.0323 79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2356 0.2360 0.2264 0.0191  -0.0144 -0.0224 79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2695 0.2647 0.2494 0.0220  -0.0132 -0.0197 79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2257 0.2235 0.2051 0.0251  -0.0174 -0.0210 79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.1855 0.2017 0.2058 0.0148  -0.0201 -0.0291 80  SER   A N   
582  C  CA  . SER   A 74  ? 0.1900 0.2104 0.2199 0.0139  -0.0234 -0.0341 80  SER   A CA  
583  C  C   . SER   A 74  ? 0.1654 0.1875 0.2060 0.0096  -0.0196 -0.0334 80  SER   A C   
584  O  O   . SER   A 74  ? 0.1673 0.1876 0.2073 0.0077  -0.0150 -0.0289 80  SER   A O   
585  C  CB  . SER   A 74  ? 0.2581 0.2845 0.2950 0.0154  -0.0273 -0.0364 80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.3395 0.3696 0.3853 0.0130  -0.0237 -0.0334 80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.1673 0.1926 0.2180 0.0082  -0.0218 -0.0380 81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.1847 0.2110 0.2464 0.0043  -0.0182 -0.0378 81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.1851 0.2167 0.2585 0.0026  -0.0165 -0.0365 81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.2078 0.2445 0.2892 0.0032  -0.0200 -0.0405 81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.2108 0.2374 0.2774 0.0039  -0.0216 -0.0441 81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.2665 0.2914 0.3406 0.0006  -0.0182 -0.0447 81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.2666 0.2857 0.3324 0.0003  -0.0137 -0.0402 81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.3057 0.3303 0.3826 0.0008  -0.0226 -0.0521 81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.1811 0.2118 0.2560 0.0007  -0.0111 -0.0313 82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.1897 0.2242 0.2735 -0.0005 -0.0082 -0.0292 82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.1775 0.2110 0.2694 -0.0036 -0.0030 -0.0269 82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.1706 0.1998 0.2569 -0.0042 -0.0004 -0.0237 82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.2163 0.2496 0.2909 0.0012  -0.0068 -0.0246 82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.2623 0.2962 0.3295 0.0046  -0.0117 -0.0268 82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.2266 0.2621 0.3076 0.0001  -0.0026 -0.0215 82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.3089 0.3417 0.3685 0.0064  -0.0109 -0.0236 82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.1594 0.1964 0.2646 -0.0055 -0.0008 -0.0280 83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.1833 0.2184 0.2957 -0.0080 0.0050  -0.0251 83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.1950 0.2276 0.3005 -0.0075 0.0096  -0.0185 83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.2117 0.2463 0.3149 -0.0062 0.0098  -0.0170 83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.2045 0.2440 0.3336 -0.0101 0.0067  -0.0281 83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.2665 0.3033 0.4033 -0.0125 0.0139  -0.0246 83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.2958 0.3319 0.4327 -0.0124 0.0195  -0.0194 83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.2958 0.3295 0.4375 -0.0145 0.0153  -0.0258 83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.3152 0.3477 0.4574 -0.0140 0.0264  -0.0156 83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.3095 0.3397 0.4577 -0.0164 0.0223  -0.0220 83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.3080 0.3375 0.4559 -0.0160 0.0279  -0.0167 83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.1738 0.2018 0.2753 -0.0080 0.0127  -0.0146 84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.1638 0.1890 0.2580 -0.0072 0.0164  -0.0085 84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.1778 0.2003 0.2789 -0.0087 0.0221  -0.0055 84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.1829 0.2030 0.2877 -0.0099 0.0229  -0.0061 84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.1760 0.1982 0.2584 -0.0059 0.0141  -0.0067 84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.1886 0.2081 0.2638 -0.0049 0.0168  -0.0011 84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.1728 0.1965 0.2483 -0.0043 0.0093  -0.0095 84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.1900 0.2120 0.2914 -0.0083 0.0266  -0.0017 85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.1870 0.2054 0.2938 -0.0092 0.0331  0.0020  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.1976 0.2110 0.2966 -0.0082 0.0338  0.0061  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.1882 0.2011 0.2768 -0.0066 0.0302  0.0072  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.2637 0.2815 0.3687 -0.0082 0.0379  0.0058  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 0.4089 0.4318 0.5227 -0.0089 0.0381  0.0022  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 0.5705 0.5930 0.6761 -0.0068 0.0402  0.0054  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 0.5968 0.6146 0.6978 -0.0058 0.0459  0.0105  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 0.6107 0.6368 0.7135 -0.0057 0.0362  0.0028  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.2052 0.2146 0.3097 -0.0090 0.0389  0.0088  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 0.2076 0.2122 0.3059 -0.0075 0.0397  0.0130  86  ALA   A CA  
632  C  C   . ALA   A 80  ? 0.2078 0.2105 0.2931 -0.0046 0.0396  0.0180  86  ALA   A C   
633  O  O   . ALA   A 80  ? 0.2210 0.2238 0.3032 -0.0038 0.0420  0.0198  86  ALA   A O   
634  C  CB  . ALA   A 80  ? 0.2266 0.2265 0.3332 -0.0085 0.0462  0.0156  86  ALA   A CB  
635  N  N   . SER   A 81  ? 0.2026 0.2037 0.2805 -0.0030 0.0367  0.0200  87  SER   A N   
636  C  CA  . SER   A 81  ? 0.2066 0.2057 0.2725 -0.0001 0.0356  0.0243  87  SER   A CA  
637  C  C   . SER   A 81  ? 0.2170 0.2121 0.2814 0.0016  0.0363  0.0281  87  SER   A C   
638  O  O   . SER   A 81  ? 0.2300 0.2235 0.3027 0.0003  0.0383  0.0273  87  SER   A O   
639  C  CB  . SER   A 81  ? 0.2160 0.2188 0.2751 0.0003  0.0295  0.0216  87  SER   A CB  
640  O  OG  . SER   A 81  ? 0.2100 0.2138 0.2710 -0.0003 0.0261  0.0194  87  SER   A OG  
641  N  N   . GLU   A 82  ? 0.2306 0.2241 0.2849 0.0046  0.0343  0.0317  88  GLU   A N   
642  C  CA  . GLU   A 82  ? 0.2491 0.2394 0.3023 0.0067  0.0339  0.0351  88  GLU   A CA  
643  C  C   . GLU   A 82  ? 0.2429 0.2361 0.3006 0.0056  0.0299  0.0318  88  GLU   A C   
644  O  O   . GLU   A 82  ? 0.2623 0.2533 0.3223 0.0069  0.0301  0.0338  88  GLU   A O   
645  C  CB  . GLU   A 82  ? 0.3199 0.3084 0.3612 0.0105  0.0318  0.0394  88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 0.4086 0.4013 0.4434 0.0105  0.0261  0.0366  88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 0.5537 0.5467 0.5818 0.0107  0.0268  0.0362  88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 0.6156 0.6080 0.6336 0.0131  0.0239  0.0376  88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 0.5283 0.5223 0.5615 0.0084  0.0301  0.0341  88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 0.2165 0.2141 0.2752 0.0035  0.0265  0.0268  89  TYR   A N   
651  C  CA  . TYR   A 83  ? 0.2057 0.2056 0.2671 0.0027  0.0232  0.0237  89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.1944 0.1944 0.2642 0.0002  0.0246  0.0196  89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.2133 0.2132 0.2860 0.0000  0.0236  0.0179  89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.2060 0.2096 0.2619 0.0024  0.0189  0.0211  89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 0.2094 0.2130 0.2568 0.0046  0.0168  0.0240  89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 0.2336 0.2374 0.2755 0.0048  0.0173  0.0244  89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 0.2189 0.2226 0.2640 0.0066  0.0140  0.0261  89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 0.2508 0.2541 0.2841 0.0070  0.0151  0.0264  89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 0.2268 0.2307 0.2641 0.0088  0.0113  0.0281  89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 0.2435 0.2470 0.2743 0.0089  0.0117  0.0280  89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 0.2865 0.2896 0.3086 0.0111  0.0088  0.0295  89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.1837 0.1841 0.2578 -0.0016 0.0268  0.0175  90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.1910 0.1921 0.2730 -0.0039 0.0271  0.0126  90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.2038 0.2039 0.2936 -0.0055 0.0312  0.0123  90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.2047 0.2054 0.2929 -0.0052 0.0330  0.0143  90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.1801 0.1853 0.2599 -0.0049 0.0231  0.0076  90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.1627 0.1689 0.2353 -0.0038 0.0194  0.0071  90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.1669 0.1719 0.2407 -0.0038 0.0187  0.0052  90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.1593 0.1674 0.2246 -0.0028 0.0172  0.0082  90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.1594 0.1652 0.2278 -0.0029 0.0162  0.0047  90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.1438 0.1526 0.2040 -0.0021 0.0144  0.0074  90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.1477 0.1555 0.2097 -0.0023 0.0141  0.0057  90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.1508 0.1590 0.2090 -0.0017 0.0125  0.0052  90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.2205 0.2194 0.3195 -0.0075 0.0327  0.0089  91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.2248 0.2238 0.3338 -0.0097 0.0362  0.0071  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.2100 0.2144 0.3201 -0.0108 0.0328  0.0023  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.2104 0.2175 0.3137 -0.0100 0.0278  -0.0001 91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.2487 0.2451 0.3666 -0.0114 0.0375  0.0038  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.2609 0.2582 0.3729 -0.0105 0.0328  0.0012  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.2249 0.2226 0.3260 -0.0078 0.0311  0.0058  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.2044 0.2104 0.3238 -0.0126 0.0355  0.0007  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.2015 0.2130 0.3242 -0.0135 0.0321  -0.0043 92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.2040 0.2173 0.3280 -0.0142 0.0266  -0.0109 92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.2181 0.2287 0.3477 -0.0155 0.0275  -0.0131 92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.2060 0.2188 0.3419 -0.0156 0.0366  -0.0054 92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.1894 0.2060 0.3059 -0.0128 0.0213  -0.0133 93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.1864 0.2034 0.3008 -0.0126 0.0163  -0.0188 93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.1867 0.2076 0.2952 -0.0110 0.0111  -0.0217 93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.1981 0.2210 0.3034 -0.0101 0.0115  -0.0189 93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.1902 0.2029 0.2958 -0.0113 0.0165  -0.0162 93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.1893 0.2025 0.2827 -0.0091 0.0148  -0.0125 93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.1850 0.1949 0.2731 -0.0081 0.0167  -0.0080 93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.1852 0.1953 0.2633 -0.0064 0.0140  -0.0073 93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.1693 0.1810 0.2410 -0.0054 0.0128  -0.0051 93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.1783 0.1896 0.2423 -0.0042 0.0109  -0.0047 93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.1746 0.1880 0.2480 -0.0055 0.0141  -0.0033 93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.1807 0.2018 0.2864 -0.0104 0.0065  -0.0268 94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.1867 0.2100 0.2838 -0.0080 0.0016  -0.0287 94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.1794 0.1991 0.2635 -0.0062 0.0016  -0.0254 94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.2076 0.2237 0.2888 -0.0062 0.0022  -0.0259 94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.1957 0.2204 0.2943 -0.0074 -0.0038 -0.0359 94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.2144 0.2442 0.3270 -0.0090 -0.0050 -0.0401 94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.2250 0.2598 0.3395 -0.0077 -0.0079 -0.0412 94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.2305 0.2600 0.3558 -0.0119 -0.0030 -0.0429 94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.2551 0.2954 0.3846 -0.0093 -0.0088 -0.0452 94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2592 0.2938 0.3997 -0.0138 -0.0036 -0.0470 94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.2763 0.3164 0.4191 -0.0125 -0.0066 -0.0481 94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.3210 0.3667 0.4807 -0.0144 -0.0072 -0.0526 94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.1566 0.1772 0.2334 -0.0046 0.0011  -0.0223 95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.1504 0.1680 0.2158 -0.0030 0.0009  -0.0198 95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.1516 0.1691 0.2095 -0.0007 -0.0034 -0.0233 95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.1730 0.1936 0.2318 0.0003  -0.0060 -0.0249 95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.1445 0.1625 0.2064 -0.0027 0.0030  -0.0147 95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.1569 0.1721 0.2089 -0.0014 0.0028  -0.0125 95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.1412 0.1562 0.1910 -0.0016 0.0048  -0.0079 95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.1569 0.1720 0.2109 -0.0025 0.0072  -0.0051 95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.1490 0.1631 0.1911 -0.0004 0.0038  -0.0068 95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.1564 0.1700 0.2068 0.0005  -0.0039 -0.0242 96  SER   A N   
719  C  CA  . SER   A 90  ? 0.1491 0.1609 0.1900 0.0033  -0.0073 -0.0270 96  SER   A CA  
720  C  C   . SER   A 90  ? 0.1681 0.1778 0.1994 0.0049  -0.0063 -0.0233 96  SER   A C   
721  O  O   . SER   A 90  ? 0.1650 0.1743 0.1968 0.0037  -0.0032 -0.0192 96  SER   A O   
722  C  CB  . SER   A 90  ? 0.1744 0.1821 0.2114 0.0039  -0.0077 -0.0303 96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.2073 0.2115 0.2418 0.0033  -0.0036 -0.0269 96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.1610 0.1693 0.1841 0.0078  -0.0092 -0.0249 97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.1660 0.1711 0.1794 0.0097  -0.0082 -0.0220 97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.1647 0.1728 0.1815 0.0085  -0.0068 -0.0185 97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.1671 0.1726 0.1790 0.0086  -0.0045 -0.0154 97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.1826 0.1825 0.1904 0.0095  -0.0044 -0.0200 97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.2047 0.2006 0.2071 0.0111  -0.0051 -0.0234 97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.2380 0.2287 0.2281 0.0145  -0.0056 -0.0241 97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.2096 0.2055 0.2166 0.0099  -0.0051 -0.0262 97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.2467 0.2343 0.2335 0.0155  -0.0061 -0.0275 97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.2302 0.2209 0.2273 0.0127  -0.0060 -0.0291 97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.1557 0.1686 0.1806 0.0077  -0.0082 -0.0194 98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.1592 0.1744 0.1869 0.0068  -0.0065 -0.0163 98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.1658 0.1826 0.1912 0.0092  -0.0090 -0.0173 98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.1593 0.1784 0.1870 0.0108  -0.0125 -0.0209 98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.1691 0.1882 0.2079 0.0043  -0.0050 -0.0162 98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.1746 0.1954 0.2160 0.0034  -0.0025 -0.0129 98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.1821 0.1999 0.2174 0.0029  -0.0003 -0.0092 98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.1922 0.2157 0.2442 0.0013  -0.0001 -0.0126 98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.1540 0.1696 0.1752 0.0097  -0.0075 -0.0144 99  MET   A N   
743  C  CA  . MET   A 93  ? 0.1485 0.1648 0.1669 0.0122  -0.0091 -0.0147 99  MET   A CA  
744  C  C   . MET   A 93  ? 0.1552 0.1744 0.1788 0.0111  -0.0071 -0.0129 99  MET   A C   
745  O  O   . MET   A 93  ? 0.1685 0.1860 0.1904 0.0094  -0.0042 -0.0101 99  MET   A O   
746  C  CB  . MET   A 93  ? 0.1605 0.1711 0.1680 0.0140  -0.0083 -0.0128 99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.1960 0.2025 0.1966 0.0156  -0.0095 -0.0143 99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.2215 0.2203 0.2101 0.0174  -0.0069 -0.0117 99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.2626 0.2612 0.2552 0.0133  -0.0027 -0.0088 99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.1512 0.1747 0.1811 0.0121  -0.0084 -0.0145 100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.1608 0.1866 0.1954 0.0112  -0.0055 -0.0128 100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.1551 0.1800 0.1851 0.0137  -0.0057 -0.0121 100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.1632 0.1878 0.1902 0.0166  -0.0088 -0.0137 100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.2000 0.2315 0.2472 0.0103  -0.0054 -0.0149 100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.2602 0.2928 0.3144 0.0076  -0.0042 -0.0155 100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2720 0.3097 0.3398 0.0063  -0.0023 -0.0168 100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.2670 0.2959 0.3169 0.0056  -0.0008 -0.0119 100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.1527 0.1767 0.1818 0.0130  -0.0024 -0.0098 101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.1533 0.1760 0.1785 0.0152  -0.0018 -0.0091 101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.1449 0.1690 0.1737 0.0142  0.0020  -0.0077 101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.1550 0.1797 0.1868 0.0119  0.0044  -0.0064 101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.1841 0.2008 0.1987 0.0154  -0.0014 -0.0074 101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.1363 0.1607 0.1649 0.0164  0.0028  -0.0078 102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.1371 0.1613 0.1664 0.0161  0.0070  -0.0064 102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.1646 0.1831 0.1833 0.0157  0.0083  -0.0046 102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.1800 0.1950 0.1923 0.0170  0.0068  -0.0049 102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.1487 0.1759 0.1835 0.0188  0.0075  -0.0077 102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.1757 0.2018 0.2103 0.0189  0.0128  -0.0062 102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.1611 0.1949 0.2084 0.0191  0.0055  -0.0102 102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.1626 0.1798 0.1794 0.0138  0.0108  -0.0029 103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.1662 0.1785 0.1736 0.0132  0.0114  -0.0017 103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.1655 0.1774 0.1721 0.0116  0.0135  0.0002  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.1801 0.1948 0.1932 0.0106  0.0143  0.0009  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.1641 0.1723 0.1627 0.0118  0.0145  0.0011  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.1578 0.1648 0.1535 0.0111  0.0160  0.0031  104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.1500 0.1573 0.1462 0.0093  0.0132  0.0039  104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.1589 0.1652 0.1531 0.0086  0.0102  0.0027  104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.1805 0.1830 0.1662 0.0121  0.0168  0.0033  104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.1782 0.1789 0.1591 0.0122  0.0180  0.0056  104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 0.1870 0.1881 0.1702 0.0130  0.0225  0.0078  104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 0.1993 0.1980 0.1742 0.0118  0.0151  0.0060  104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 0.2015 0.1999 0.1782 0.0134  0.0224  0.0100  104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 0.2107 0.2080 0.1825 0.0128  0.0175  0.0088  104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.1636 0.1717 0.1624 0.0088  0.0149  0.0059  105 SER   A N   
785  C  CA  . SER   A 99  ? 0.1590 0.1670 0.1578 0.0076  0.0126  0.0070  105 SER   A CA  
786  C  C   . SER   A 99  ? 0.1599 0.1669 0.1582 0.0080  0.0154  0.0101  105 SER   A C   
787  O  O   . SER   A 99  ? 0.1709 0.1782 0.1725 0.0085  0.0195  0.0112  105 SER   A O   
788  C  CB  . SER   A 99  ? 0.1718 0.1824 0.1775 0.0062  0.0107  0.0058  105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.1647 0.1779 0.1785 0.0058  0.0128  0.0059  105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.1642 0.1698 0.1588 0.0080  0.0133  0.0114  106 GLU   A N   
791  C  CA  . GLU   A 100 ? 0.1721 0.1761 0.1652 0.0088  0.0150  0.0148  106 GLU   A CA  
792  C  C   . GLU   A 100 ? 0.1861 0.1916 0.1840 0.0076  0.0122  0.0150  106 GLU   A C   
793  O  O   . GLU   A 100 ? 0.1715 0.1787 0.1715 0.0064  0.0089  0.0127  106 GLU   A O   
794  C  CB  . GLU   A 100 ? 0.1960 0.1962 0.1774 0.0110  0.0141  0.0160  106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 0.1988 0.1968 0.1749 0.0123  0.0174  0.0155  106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 0.2325 0.2262 0.1957 0.0147  0.0167  0.0160  106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 0.2609 0.2523 0.2181 0.0163  0.0155  0.0183  106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 0.2316 0.2238 0.1903 0.0153  0.0172  0.0138  106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 0.1888 0.1934 0.1888 0.0080  0.0139  0.0179  107 PRO   A N   
800  C  CA  . PRO   A 101 ? 0.1854 0.1915 0.1910 0.0070  0.0118  0.0181  107 PRO   A CA  
801  C  C   . PRO   A 101 ? 0.1843 0.1912 0.1875 0.0069  0.0069  0.0167  107 PRO   A C   
802  O  O   . PRO   A 101 ? 0.1811 0.1900 0.1899 0.0054  0.0053  0.0150  107 PRO   A O   
803  C  CB  . PRO   A 101 ? 0.2046 0.2081 0.2100 0.0084  0.0147  0.0221  107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 0.2093 0.2112 0.2145 0.0089  0.0199  0.0233  107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 0.2015 0.2034 0.1998 0.0095  0.0189  0.0213  107 PRO   A CD  
806  N  N   . GLY   A 102 ? 0.1813 0.1865 0.1762 0.0085  0.0046  0.0172  108 GLY   A N   
807  C  CA  . GLY   A 102 ? 0.1782 0.1846 0.1722 0.0083  -0.0003 0.0155  108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.1753 0.1829 0.1711 0.0064  -0.0016 0.0119  108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.1848 0.1936 0.1823 0.0056  -0.0049 0.0102  108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.1685 0.1759 0.1648 0.0057  0.0010  0.0107  109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.1553 0.1631 0.1529 0.0044  0.0001  0.0078  109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.1520 0.1615 0.1567 0.0029  0.0001  0.0070  109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.1656 0.1747 0.1708 0.0020  -0.0005 0.0050  109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.1600 0.1670 0.1557 0.0048  0.0026  0.0069  109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.1808 0.1854 0.1686 0.0062  0.0027  0.0067  109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.1879 0.1914 0.1717 0.0062  -0.0001 0.0057  109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.1701 0.1740 0.1562 0.0073  0.0058  0.0075  109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.1434 0.1540 0.1529 0.0028  0.0010  0.0086  110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.1390 0.1506 0.1543 0.0017  0.0012  0.0076  110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.1473 0.1590 0.1635 0.0009  -0.0008 0.0065  110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.1582 0.1703 0.1736 0.0012  -0.0029 0.0071  110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.1404 0.1526 0.1606 0.0018  0.0025  0.0095  110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.1655 0.1779 0.1886 0.0018  0.0057  0.0097  110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.1327 0.1437 0.1503 0.0001  0.0000  0.0048  111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.1390 0.1496 0.1587 -0.0009 -0.0007 0.0037  111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.1503 0.1588 0.1661 -0.0013 -0.0008 0.0020  111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.1655 0.1728 0.1833 -0.0023 -0.0002 0.0009  111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.1457 0.1533 0.1563 -0.0005 -0.0010 0.0018  112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.1523 0.1573 0.1591 -0.0006 -0.0008 0.0002  112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.1537 0.1565 0.1603 -0.0004 0.0013  -0.0004 112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.1575 0.1608 0.1642 0.0005  0.0021  0.0000  112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.1488 0.1485 0.1546 -0.0010 0.0023  -0.0014 113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.1426 0.1390 0.1465 -0.0003 0.0047  -0.0015 113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.1526 0.1468 0.1508 0.0017  0.0050  -0.0018 113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.1630 0.1562 0.1587 0.0019  0.0045  -0.0023 113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.1686 0.1619 0.1747 -0.0018 0.0066  -0.0021 113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.1904 0.1861 0.2030 -0.0030 0.0070  -0.0017 113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.2032 0.1909 0.2046 -0.0005 0.0097  -0.0020 113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.2263 0.2199 0.2442 -0.0050 0.0094  -0.0025 113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.1442 0.1373 0.1403 0.0034  0.0057  -0.0016 114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.1600 0.1505 0.1508 0.0059  0.0059  -0.0019 114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.1683 0.1530 0.1551 0.0068  0.0084  -0.0015 114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.1765 0.1601 0.1640 0.0065  0.0098  -0.0012 114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.1683 0.1618 0.1598 0.0076  0.0043  -0.0023 114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.1619 0.1534 0.1485 0.0109  0.0036  -0.0028 114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.1884 0.1802 0.1741 0.0118  0.0033  -0.0029 114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.1876 0.1827 0.1764 0.0121  0.0013  -0.0041 114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.1668 0.1470 0.1495 0.0078  0.0097  -0.0014 115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.1781 0.1514 0.1563 0.0089  0.0130  -0.0006 115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.1826 0.1522 0.1538 0.0126  0.0129  -0.0001 115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.2025 0.1735 0.1734 0.0135  0.0113  -0.0006 115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.2269 0.1973 0.2082 0.0061  0.0154  -0.0009 115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.2857 0.2579 0.2741 0.0028  0.0166  -0.0012 115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.3058 0.2754 0.2988 0.0001  0.0185  -0.0022 115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.3170 0.2883 0.3180 -0.0026 0.0201  -0.0025 115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.2952 0.2616 0.2972 -0.0030 0.0249  -0.0017 115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.2639 0.2230 0.2580 -0.0004 0.0287  -0.0001 115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.3392 0.3079 0.3500 -0.0055 0.0264  -0.0021 115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.1961 0.1599 0.1609 0.0152  0.0150  0.0010  116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.2015 0.1599 0.1585 0.0194  0.0154  0.0020  116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.2197 0.1693 0.1733 0.0191  0.0208  0.0036  116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.2280 0.1769 0.1867 0.0155  0.0237  0.0035  116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.2233 0.1812 0.1740 0.0235  0.0133  0.0021  116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.2261 0.1786 0.1719 0.0237  0.0169  0.0031  116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.2327 0.1753 0.1782 0.0230  0.0225  0.0052  117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.2620 0.1948 0.2039 0.0231  0.0286  0.0071  117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.2734 0.2022 0.2135 0.0225  0.0328  0.0084  117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.2874 0.2093 0.2280 0.0210  0.0387  0.0097  117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.2873 0.2125 0.2195 0.0284  0.0297  0.0091  117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.3534 0.2761 0.2754 0.0338  0.0280  0.0104  117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.4858 0.4030 0.3987 0.0398  0.0272  0.0121  117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 0.5381 0.4607 0.4509 0.0426  0.0215  0.0109  117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 0.4838 0.3898 0.3892 0.0420  0.0330  0.0151  117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.2500 0.1827 0.1888 0.0233  0.0304  0.0078  118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.2580 0.1865 0.1943 0.0232  0.0348  0.0089  118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.2426 0.1767 0.1902 0.0180  0.0358  0.0075  118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.2580 0.1883 0.2058 0.0173  0.0406  0.0084  118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.2604 0.1886 0.1873 0.0277  0.0319  0.0088  118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.2925 0.2155 0.2080 0.0335  0.0301  0.0100  118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.3107 0.2399 0.2257 0.0360  0.0231  0.0082  118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 0.3413 0.2534 0.2458 0.0376  0.0346  0.0130  118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.3445 0.2670 0.2490 0.0415  0.0229  0.0100  118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 0.3648 0.2766 0.2621 0.0427  0.0297  0.0130  118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.2066 0.1496 0.1634 0.0149  0.0312  0.0055  119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.2182 0.1670 0.1855 0.0106  0.0312  0.0042  119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.1916 0.1496 0.1637 0.0096  0.0252  0.0025  119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.2027 0.1632 0.1721 0.0113  0.0213  0.0020  119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.1827 0.1453 0.1622 0.0070  0.0249  0.0018  120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.1730 0.1436 0.1574 0.0060  0.0202  0.0006  120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.1761 0.1475 0.1552 0.0088  0.0179  0.0002  120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.2002 0.1680 0.1752 0.0103  0.0202  0.0005  120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.1857 0.1604 0.1796 0.0028  0.0207  0.0003  120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.1948 0.1765 0.1927 0.0023  0.0165  -0.0004 120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.1970 0.1722 0.1975 -0.0001 0.0215  -0.0001 120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.1777 0.1538 0.1574 0.0095  0.0137  -0.0007 121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.1803 0.1583 0.1571 0.0118  0.0108  -0.0018 121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.1881 0.1720 0.1722 0.0098  0.0090  -0.0028 121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.1812 0.1653 0.1644 0.0108  0.0082  -0.0040 121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.1876 0.1671 0.1620 0.0140  0.0078  -0.0023 121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.2106 0.1938 0.1852 0.0159  0.0040  -0.0042 121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.2029 0.1758 0.1694 0.0168  0.0095  -0.0012 121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.1747 0.1629 0.1656 0.0072  0.0083  -0.0024 122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.1756 0.1687 0.1731 0.0056  0.0069  -0.0027 122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.1556 0.1522 0.1581 0.0035  0.0061  -0.0018 122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.1615 0.1566 0.1629 0.0029  0.0067  -0.0014 122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.1463 0.1468 0.1538 0.0026  0.0049  -0.0016 123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.1448 0.1482 0.1557 0.0013  0.0040  -0.0005 123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.1437 0.1500 0.1561 0.0017  0.0030  -0.0003 123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.1419 0.1493 0.1565 0.0021  0.0029  -0.0011 123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.1615 0.1662 0.1776 -0.0001 0.0043  0.0004  123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.1817 0.1871 0.2012 0.0000  0.0051  0.0002  123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.1860 0.1885 0.2026 -0.0010 0.0056  0.0002  123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.1854 0.1925 0.2110 -0.0010 0.0053  0.0015  123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.1349 0.1423 0.1466 0.0016  0.0024  0.0006  124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.1286 0.1384 0.1422 0.0019  0.0026  0.0013  124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.1276 0.1388 0.1464 0.0012  0.0031  0.0023  124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.1347 0.1459 0.1549 0.0006  0.0029  0.0034  124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.1383 0.1480 0.1488 0.0021  0.0024  0.0025  124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.1492 0.1604 0.1614 0.0026  0.0038  0.0037  124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.1566 0.1643 0.1622 0.0028  0.0023  0.0013  124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.1333 0.1460 0.1557 0.0013  0.0038  0.0017  125 SER   A N   
922  C  CA  . SER   A 119 ? 0.1286 0.1421 0.1566 0.0006  0.0048  0.0024  125 SER   A CA  
923  C  C   . SER   A 119 ? 0.1397 0.1547 0.1717 0.0005  0.0065  0.0031  125 SER   A C   
924  O  O   . SER   A 119 ? 0.1500 0.1648 0.1857 0.0001  0.0080  0.0049  125 SER   A O   
925  C  CB  . SER   A 119 ? 0.1339 0.1470 0.1640 0.0004  0.0043  0.0000  125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.1445 0.1579 0.1804 -0.0003 0.0054  0.0000  125 SER   A OG  
927  N  N   . THR   A 120 ? 0.1415 0.1577 0.1734 0.0011  0.0067  0.0021  126 THR   A N   
928  C  CA  . THR   A 120 ? 0.1448 0.1624 0.1820 0.0009  0.0093  0.0028  126 THR   A CA  
929  C  C   . THR   A 120 ? 0.1461 0.1642 0.1801 0.0020  0.0101  0.0032  126 THR   A C   
930  O  O   . THR   A 120 ? 0.1449 0.1621 0.1731 0.0029  0.0083  0.0024  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.1544 0.1744 0.1999 0.0002  0.0090  -0.0003 126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.1644 0.1862 0.2090 0.0013  0.0067  -0.0030 126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.1584 0.1776 0.2067 -0.0007 0.0080  -0.0016 126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.1495 0.1682 0.1871 0.0020  0.0133  0.0044  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.1591 0.1784 0.1951 0.0032  0.0147  0.0043  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.1851 0.2046 0.2259 0.0032  0.0195  0.0061  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.2074 0.2266 0.2537 0.0021  0.0218  0.0073  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.1850 0.2045 0.2237 0.0044  0.0216  0.0063  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.2130 0.2314 0.2539 0.0049  0.0274  0.0087  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.2023 0.2233 0.2475 0.0058  0.0292  0.0069  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.2255 0.2504 0.2765 0.0057  0.0258  0.0036  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.2039 0.2229 0.2470 0.0070  0.0344  0.0091  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.2006 0.2220 0.2491 0.0081  0.0373  0.0077  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.1926 0.2162 0.2394 0.0093  0.0328  0.0046  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.1974 0.2255 0.2537 0.0099  0.0328  0.0022  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.2633 0.2893 0.3283 0.0065  0.0404  0.0064  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.3633 0.3859 0.4301 0.0054  0.0463  0.0100  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 0.3846 0.4026 0.4444 0.0068  0.0518  0.0134  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.4018 0.4258 0.4769 0.0032  0.0454  0.0094  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.1845 0.2048 0.2194 0.0101  0.0295  0.0049  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.1821 0.2029 0.2140 0.0115  0.0258  0.0025  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.1631 0.1867 0.1987 0.0108  0.0203  0.0001  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.1809 0.2050 0.2151 0.0124  0.0175  -0.0018 130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.1464 0.1707 0.1850 0.0090  0.0189  0.0002  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.1400 0.1656 0.1795 0.0085  0.0140  -0.0019 131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.1463 0.1681 0.1776 0.0075  0.0124  -0.0004 131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.1584 0.1778 0.1861 0.0068  0.0145  0.0021  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.1545 0.1840 0.2052 0.0072  0.0135  -0.0036 131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.1927 0.2273 0.2544 0.0080  0.0140  -0.0060 131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.2231 0.2611 0.2974 0.0059  0.0150  -0.0075 131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.2028 0.2390 0.2630 0.0103  0.0088  -0.0089 131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.1347 0.1558 0.1631 0.0077  0.0087  -0.0019 132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.1378 0.1561 0.1609 0.0067  0.0072  -0.0010 132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.1387 0.1579 0.1642 0.0065  0.0044  -0.0031 132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.1530 0.1732 0.1790 0.0081  0.0024  -0.0051 132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.1455 0.1601 0.1596 0.0072  0.0066  -0.0003 132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.1707 0.1843 0.1819 0.0090  0.0053  -0.0019 132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.1601 0.1727 0.1713 0.0059  0.0053  0.0004  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.1307 0.1495 0.1578 0.0050  0.0043  -0.0026 133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.1294 0.1483 0.1578 0.0050  0.0020  -0.0047 133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.1372 0.1527 0.1600 0.0045  0.0016  -0.0038 133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.1505 0.1651 0.1724 0.0034  0.0029  -0.0017 133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.1412 0.1550 0.1605 0.0056  0.0000  -0.0055 134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.1466 0.1567 0.1609 0.0053  0.0004  -0.0047 134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.1444 0.1537 0.1596 0.0053  0.0000  -0.0063 134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.1446 0.1543 0.1594 0.0068  -0.0019 -0.0087 134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.1558 0.1627 0.1631 0.0070  0.0001  -0.0048 134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.1491 0.1563 0.1549 0.0074  0.0005  -0.0039 134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.1493 0.1552 0.1537 0.0061  0.0017  -0.0024 134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.1609 0.1696 0.1670 0.0094  -0.0005 -0.0050 134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.1541 0.1595 0.1561 0.0066  0.0021  -0.0021 134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.1667 0.1751 0.1712 0.0099  0.0004  -0.0043 134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.1577 0.1642 0.1597 0.0085  0.0018  -0.0029 134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.1405 0.1485 0.1567 0.0039  0.0014  -0.0051 135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.1450 0.1512 0.1611 0.0040  0.0017  -0.0065 135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.1476 0.1494 0.1558 0.0057  0.0023  -0.0068 135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.1654 0.1651 0.1716 0.0051  0.0040  -0.0050 135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.1444 0.1509 0.1650 0.0023  0.0035  -0.0049 135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.1466 0.1464 0.1503 0.0078  0.0009  -0.0090 136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.1569 0.1512 0.1515 0.0100  0.0021  -0.0089 136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.1591 0.1500 0.1530 0.0091  0.0054  -0.0081 136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.1705 0.1626 0.1688 0.0081  0.0058  -0.0091 136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.1850 0.1780 0.1742 0.0130  -0.0009 -0.0117 136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.2487 0.2352 0.2266 0.0162  0.0002  -0.0112 136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.2397 0.2240 0.2145 0.0166  0.0018  -0.0090 136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.3118 0.2947 0.2835 0.0183  -0.0001 -0.0130 136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.1578 0.1440 0.1465 0.0097  0.0085  -0.0064 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.1742 0.1568 0.1624 0.0093  0.0124  -0.0058 137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.1904 0.1655 0.1675 0.0123  0.0148  -0.0058 137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.2000 0.1709 0.1754 0.0124  0.0191  -0.0051 137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.1896 0.1733 0.1844 0.0066  0.0150  -0.0037 137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.1964 0.1865 0.2005 0.0042  0.0127  -0.0035 137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.2029 0.1843 0.1947 0.0067  0.0160  -0.0024 137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.1949 0.1681 0.1643 0.0152  0.0125  -0.0063 138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.1965 0.1616 0.1539 0.0187  0.0150  -0.0055 138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.2233 0.1840 0.1733 0.0212  0.0158  -0.0071 138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.2443 0.1970 0.1843 0.0238  0.0198  -0.0059 138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.2094 0.1737 0.1603 0.0219  0.0115  -0.0055 138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.2131 0.1797 0.1691 0.0200  0.0117  -0.0037 138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.2141 0.1801 0.1644 0.0235  0.0083  -0.0040 138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.2054 0.1784 0.1608 0.0236  0.0029  -0.0067 138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.2089 0.1846 0.1639 0.0259  -0.0010 -0.0076 138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.2335 0.2044 0.1811 0.0291  -0.0005 -0.0060 138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.2217 0.2045 0.1843 0.0251  -0.0052 -0.0101 138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.2072 0.1722 0.1615 0.0205  0.0125  -0.0100 139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.2234 0.1839 0.1704 0.0229  0.0131  -0.0123 139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.2421 0.2002 0.1927 0.0208  0.0190  -0.0114 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.2640 0.2171 0.2076 0.0229  0.0207  -0.0130 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.2357 0.2013 0.1864 0.0229  0.0071  -0.0165 139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.2613 0.2340 0.2266 0.0185  0.0067  -0.0167 139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.2609 0.2373 0.2335 0.0160  0.0076  -0.0141 139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.3053 0.2791 0.2740 0.0177  0.0058  -0.0195 139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.2243 0.1860 0.1857 0.0172  0.0216  -0.0091 140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.2158 0.1766 0.1832 0.0153  0.0268  -0.0083 140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.2246 0.1783 0.1862 0.0164  0.0334  -0.0059 140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.2161 0.1705 0.1840 0.0143  0.0364  -0.0036 140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.2061 0.1745 0.1879 0.0113  0.0258  -0.0071 140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.2153 0.1902 0.2033 0.0101  0.0203  -0.0089 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.2212 0.2023 0.2208 0.0069  0.0196  -0.0070 140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.2310 0.2050 0.2187 0.0108  0.0198  -0.0117 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.2381 0.1837 0.1864 0.0202  0.0357  -0.0066 141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.2567 0.1936 0.1969 0.0221  0.0427  -0.0040 141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.2670 0.2034 0.2166 0.0194  0.0499  -0.0023 141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.2810 0.2132 0.2309 0.0190  0.0557  0.0004  141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.2725 0.2002 0.1948 0.0273  0.0440  -0.0049 141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.2836 0.2125 0.1972 0.0305  0.0360  -0.0074 141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.3207 0.2393 0.2148 0.0364  0.0372  -0.0083 141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.2859 0.2171 0.2004 0.0304  0.0329  -0.0054 141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.2648 0.2054 0.2230 0.0176  0.0497  -0.0039 142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.2652 0.2061 0.2339 0.0154  0.0562  -0.0027 142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.2699 0.2174 0.2533 0.0115  0.0560  -0.0009 142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.2984 0.2459 0.2910 0.0098  0.0617  0.0003  142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.2568 0.2007 0.2309 0.0150  0.0553  -0.0050 142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.2450 0.1972 0.2262 0.0132  0.0475  -0.0067 142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.2550 0.2079 0.2300 0.0146  0.0417  -0.0094 142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.2426 0.2032 0.2389 0.0097  0.0450  -0.0057 142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.2585 0.2195 0.2444 0.0120  0.0367  -0.0099 142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.2495 0.2150 0.2476 0.0093  0.0386  -0.0075 142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.2553 0.2198 0.2639 0.0072  0.0475  -0.0037 142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.2436 0.2167 0.2536 0.0067  0.0352  -0.0067 142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.2350 0.2074 0.2553 0.0049  0.0432  -0.0034 142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.2358 0.2120 0.2560 0.0048  0.0375  -0.0046 142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.2612 0.2140 0.2470 0.0102  0.0498  -0.0009 143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.2609 0.2194 0.2594 0.0067  0.0491  0.0003  143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.3167 0.2699 0.3157 0.0062  0.0558  0.0022  143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.3234 0.2805 0.3351 0.0032  0.0572  0.0027  143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.2572 0.2206 0.2554 0.0060  0.0421  0.0000  143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.2450 0.2153 0.2476 0.0053  0.0360  -0.0014 143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.2563 0.2301 0.2573 0.0050  0.0303  -0.0015 143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.2386 0.2150 0.2553 0.0026  0.0360  -0.0010 143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.3730 0.3168 0.3581 0.0094  0.0600  0.0032  144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.4413 0.3779 0.4245 0.0095  0.0674  0.0054  144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.5037 0.4339 0.4868 0.0103  0.0766  0.0064  144 ASP   A C   
1064 O  O   . ASP   A 138 ? 0.5280 0.4506 0.5080 0.0108  0.0838  0.0085  144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 0.4997 0.4287 0.4665 0.0131  0.0669  0.0065  144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 0.6169 0.5504 0.5870 0.0115  0.0614  0.0064  144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 0.6503 0.5884 0.6338 0.0076  0.0619  0.0065  144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 0.6721 0.6049 0.6323 0.0142  0.0564  0.0060  144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 0.5318 0.4642 0.5184 0.0104  0.0774  0.0051  145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 0.5796 0.5058 0.5668 0.0113  0.0869  0.0060  145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 0.6061 0.5401 0.6111 0.0084  0.0875  0.0049  145 GLU   A C   
1072 O  O   . GLU   A 139 ? 0.6317 0.5619 0.6390 0.0091  0.0950  0.0052  145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 0.6302 0.5474 0.5985 0.0162  0.0890  0.0056  145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 0.7044 0.6267 0.6703 0.0171  0.0812  0.0026  145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 0.8038 0.7187 0.7493 0.0220  0.0791  0.0012  145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 0.8233 0.7394 0.7661 0.0231  0.0760  -0.0016 145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 0.8438 0.7517 0.7762 0.0248  0.0801  0.0029  145 GLU   A OE2 
1078 N  N   . SER   B 1   ? 0.2554 0.2436 0.2507 0.0010  -0.0193 -0.0088 7   SER   C N   
1079 C  CA  . SER   B 1   ? 0.2474 0.2393 0.2511 0.0010  -0.0203 -0.0094 7   SER   C CA  
1080 C  C   . SER   B 1   ? 0.2401 0.2347 0.2478 0.0015  -0.0189 -0.0085 7   SER   C C   
1081 O  O   . SER   B 1   ? 0.2551 0.2483 0.2591 0.0019  -0.0184 -0.0073 7   SER   C O   
1082 C  CB  . SER   B 1   ? 0.2826 0.2738 0.2881 0.0010  -0.0249 -0.0104 7   SER   C CB  
1083 O  OG  . SER   B 1   ? 0.3488 0.3380 0.3516 0.0019  -0.0277 -0.0094 7   SER   C OG  
1084 N  N   . GLY   B 2   ? 0.2155 0.2137 0.2303 0.0012  -0.0181 -0.0091 8   GLY   C N   
1085 C  CA  . GLY   B 2   ? 0.2076 0.2082 0.2263 0.0016  -0.0167 -0.0088 8   GLY   C CA  
1086 C  C   . GLY   B 2   ? 0.1891 0.1932 0.2129 0.0007  -0.0137 -0.0093 8   GLY   C C   
1087 O  O   . GLY   B 2   ? 0.2107 0.2147 0.2335 -0.0002 -0.0122 -0.0093 8   GLY   C O   
1088 N  N   . ALA   B 3   ? 0.1758 0.1825 0.2047 0.0008  -0.0128 -0.0099 9   ALA   C N   
1089 C  CA  . ALA   B 3   ? 0.1764 0.1860 0.2092 -0.0004 -0.0096 -0.0105 9   ALA   C CA  
1090 C  C   . ALA   B 3   ? 0.1841 0.1949 0.2182 -0.0001 -0.0076 -0.0108 9   ALA   C C   
1091 O  O   . ALA   B 3   ? 0.2085 0.2184 0.2426 0.0012  -0.0091 -0.0108 9   ALA   C O   
1092 C  CB  . ALA   B 3   ? 0.1910 0.2032 0.2311 -0.0010 -0.0104 -0.0121 9   ALA   C CB  
1093 N  N   . ILE   B 4   ? 0.1655 0.1780 0.2001 -0.0014 -0.0043 -0.0109 10  ILE   C N   
1094 C  CA  . ILE   B 4   ? 0.1632 0.1771 0.1994 -0.0016 -0.0018 -0.0118 10  ILE   C CA  
1095 C  C   . ILE   B 4   ? 0.1582 0.1753 0.2014 -0.0023 0.0000  -0.0137 10  ILE   C C   
1096 O  O   . ILE   B 4   ? 0.1738 0.1919 0.2183 -0.0038 0.0011  -0.0137 10  ILE   C O   
1097 C  CB  . ILE   B 4   ? 0.1649 0.1780 0.1955 -0.0028 0.0006  -0.0106 10  ILE   C CB  
1098 C  CG1 . ILE   B 4   ? 0.1828 0.1935 0.2078 -0.0022 -0.0009 -0.0089 10  ILE   C CG1 
1099 C  CG2 . ILE   B 4   ? 0.1846 0.1985 0.2158 -0.0032 0.0030  -0.0119 10  ILE   C CG2 
1100 C  CD1 . ILE   B 4   ? 0.2020 0.2123 0.2225 -0.0033 0.0007  -0.0076 10  ILE   C CD1 
1101 N  N   . TYR   B 5   ? 0.1622 0.1810 0.2106 -0.0013 0.0004  -0.0155 11  TYR   C N   
1102 C  CA  . TYR   B 5   ? 0.1783 0.2009 0.2347 -0.0019 0.0026  -0.0177 11  TYR   C CA  
1103 C  C   . TYR   B 5   ? 0.1941 0.2173 0.2498 -0.0026 0.0067  -0.0190 11  TYR   C C   
1104 O  O   . TYR   B 5   ? 0.2055 0.2277 0.2611 -0.0011 0.0063  -0.0198 11  TYR   C O   
1105 C  CB  . TYR   B 5   ? 0.1921 0.2165 0.2567 0.0002  -0.0006 -0.0192 11  TYR   C CB  
1106 C  CG  . TYR   B 5   ? 0.1816 0.2054 0.2466 0.0005  -0.0049 -0.0183 11  TYR   C CG  
1107 C  CD1 . TYR   B 5   ? 0.2031 0.2296 0.2732 -0.0010 -0.0047 -0.0191 11  TYR   C CD1 
1108 C  CD2 . TYR   B 5   ? 0.2034 0.2233 0.2628 0.0019  -0.0088 -0.0165 11  TYR   C CD2 
1109 C  CE1 . TYR   B 5   ? 0.2273 0.2527 0.2970 -0.0010 -0.0086 -0.0184 11  TYR   C CE1 
1110 C  CE2 . TYR   B 5   ? 0.2285 0.2473 0.2869 0.0019  -0.0125 -0.0159 11  TYR   C CE2 
1111 C  CZ  . TYR   B 5   ? 0.2467 0.2681 0.3103 0.0006  -0.0126 -0.0169 11  TYR   C CZ  
1112 O  OH  . TYR   B 5   ? 0.2814 0.3012 0.3432 0.0004  -0.0163 -0.0165 11  TYR   C OH  
1113 N  N   . VAL   B 6   ? 0.2029 0.2271 0.2569 -0.0050 0.0107  -0.0193 12  VAL   C N   
1114 C  CA  . VAL   B 6   ? 0.2156 0.2397 0.2669 -0.0061 0.0149  -0.0205 12  VAL   C CA  
1115 C  C   . VAL   B 6   ? 0.2196 0.2468 0.2753 -0.0084 0.0193  -0.0223 12  VAL   C C   
1116 O  O   . VAL   B 6   ? 0.2097 0.2370 0.2645 -0.0103 0.0199  -0.0210 12  VAL   C O   
1117 C  CB  . VAL   B 6   ? 0.2465 0.2670 0.2872 -0.0073 0.0151  -0.0183 12  VAL   C CB  
1118 C  CG1 . VAL   B 6   ? 0.2623 0.2816 0.2989 -0.0088 0.0144  -0.0158 12  VAL   C CG1 
1119 C  CG2 . VAL   B 6   ? 0.2612 0.2813 0.2982 -0.0088 0.0191  -0.0197 12  VAL   C CG2 
1120 N  N   . GLY   B 7   ? 0.2299 0.2597 0.2914 -0.0081 0.0226  -0.0254 13  GLY   C N   
1121 C  CA  . GLY   B 7   ? 0.2357 0.2690 0.3024 -0.0104 0.0275  -0.0274 13  GLY   C CA  
1122 C  C   . GLY   B 7   ? 0.2321 0.2686 0.3070 -0.0107 0.0259  -0.0273 13  GLY   C C   
1123 O  O   . GLY   B 7   ? 0.2393 0.2772 0.3205 -0.0082 0.0214  -0.0276 13  GLY   C O   
1124 N  N   . ASN   B 8   ? 0.2269 0.2639 0.3007 -0.0139 0.0287  -0.0266 14  ASN   C N   
1125 C  CA  . ASN   B 8   ? 0.2236 0.2632 0.3047 -0.0146 0.0269  -0.0264 14  ASN   C CA  
1126 C  C   . ASN   B 8   ? 0.2032 0.2385 0.2768 -0.0153 0.0234  -0.0230 14  ASN   C C   
1127 O  O   . ASN   B 8   ? 0.2166 0.2522 0.2922 -0.0174 0.0237  -0.0223 14  ASN   C O   
1128 C  CB  . ASN   B 8   ? 0.2532 0.2967 0.3410 -0.0178 0.0323  -0.0284 14  ASN   C CB  
1129 C  CG  . ASN   B 8   ? 0.3414 0.3905 0.4402 -0.0165 0.0351  -0.0324 14  ASN   C CG  
1130 O  OD1 . ASN   B 8   ? 0.3688 0.4215 0.4782 -0.0138 0.0315  -0.0341 14  ASN   C OD1 
1131 N  ND2 . ASN   B 8   ? 0.3722 0.4214 0.4683 -0.0182 0.0412  -0.0341 14  ASN   C ND2 
1132 N  N   . TYR   B 9   ? 0.1816 0.2130 0.2473 -0.0133 0.0201  -0.0210 15  TYR   C N   
1133 C  CA  . TYR   B 9   ? 0.1784 0.2058 0.2373 -0.0134 0.0170  -0.0181 15  TYR   C CA  
1134 C  C   . TYR   B 9   ? 0.1714 0.1977 0.2302 -0.0104 0.0116  -0.0175 15  TYR   C C   
1135 O  O   . TYR   B 9   ? 0.1832 0.2098 0.2429 -0.0082 0.0103  -0.0183 15  TYR   C O   
1136 C  CB  . TYR   B 9   ? 0.1918 0.2150 0.2397 -0.0143 0.0184  -0.0158 15  TYR   C CB  
1137 C  CG  . TYR   B 9   ? 0.2117 0.2344 0.2565 -0.0176 0.0234  -0.0157 15  TYR   C CG  
1138 C  CD1 . TYR   B 9   ? 0.2330 0.2558 0.2800 -0.0202 0.0251  -0.0152 15  TYR   C CD1 
1139 C  CD2 . TYR   B 9   ? 0.2320 0.2535 0.2708 -0.0183 0.0263  -0.0159 15  TYR   C CD2 
1140 C  CE1 . TYR   B 9   ? 0.2637 0.2851 0.3065 -0.0237 0.0299  -0.0146 15  TYR   C CE1 
1141 C  CE2 . TYR   B 9   ? 0.2499 0.2702 0.2842 -0.0217 0.0310  -0.0156 15  TYR   C CE2 
1142 C  CZ  . TYR   B 9   ? 0.2750 0.2951 0.3112 -0.0244 0.0328  -0.0148 15  TYR   C CZ  
1143 O  OH  . TYR   B 9   ? 0.3074 0.3254 0.3380 -0.0280 0.0375  -0.0141 15  TYR   C OH  
1144 N  N   . ARG   B 10  ? 0.1551 0.1792 0.2120 -0.0105 0.0086  -0.0160 16  ARG   C N   
1145 C  CA  . ARG   B 10  ? 0.1664 0.1885 0.2210 -0.0082 0.0040  -0.0152 16  ARG   C CA  
1146 C  C   . ARG   B 10  ? 0.1610 0.1789 0.2070 -0.0087 0.0037  -0.0127 16  ARG   C C   
1147 O  O   . ARG   B 10  ? 0.1737 0.1903 0.2187 -0.0105 0.0046  -0.0120 16  ARG   C O   
1148 C  CB  . ARG   B 10  ? 0.1769 0.2005 0.2380 -0.0080 0.0006  -0.0163 16  ARG   C CB  
1149 C  CG  . ARG   B 10  ? 0.1915 0.2119 0.2483 -0.0065 -0.0038 -0.0153 16  ARG   C CG  
1150 C  CD  . ARG   B 10  ? 0.1932 0.2152 0.2563 -0.0063 -0.0077 -0.0168 16  ARG   C CD  
1151 N  NE  . ARG   B 10  ? 0.2128 0.2311 0.2711 -0.0066 -0.0104 -0.0160 16  ARG   C NE  
1152 C  CZ  . ARG   B 10  ? 0.2683 0.2838 0.3221 -0.0050 -0.0143 -0.0156 16  ARG   C CZ  
1153 N  NH1 . ARG   B 10  ? 0.2458 0.2611 0.2984 -0.0029 -0.0161 -0.0153 16  ARG   C NH1 
1154 N  NH2 . ARG   B 10  ? 0.2476 0.2597 0.2971 -0.0055 -0.0161 -0.0155 16  ARG   C NH2 
1155 N  N   . VAL   B 11  ? 0.1612 0.1771 0.2015 -0.0071 0.0024  -0.0116 17  VAL   C N   
1156 C  CA  . VAL   B 11  ? 0.1596 0.1721 0.1929 -0.0070 0.0020  -0.0095 17  VAL   C CA  
1157 C  C   . VAL   B 11  ? 0.1626 0.1734 0.1943 -0.0054 -0.0014 -0.0092 17  VAL   C C   
1158 O  O   . VAL   B 11  ? 0.1776 0.1885 0.2092 -0.0038 -0.0031 -0.0096 17  VAL   C O   
1159 C  CB  . VAL   B 11  ? 0.1773 0.1891 0.2054 -0.0067 0.0033  -0.0085 17  VAL   C CB  
1160 C  CG1 . VAL   B 11  ? 0.1873 0.1965 0.2099 -0.0067 0.0029  -0.0064 17  VAL   C CG1 
1161 C  CG2 . VAL   B 11  ? 0.1859 0.1993 0.2148 -0.0082 0.0066  -0.0093 17  VAL   C CG2 
1162 N  N   . VAL   B 12  ? 0.1494 0.1579 0.1794 -0.0058 -0.0022 -0.0086 18  VAL   C N   
1163 C  CA  . VAL   B 12  ? 0.1580 0.1644 0.1855 -0.0044 -0.0050 -0.0087 18  VAL   C CA  
1164 C  C   . VAL   B 12  ? 0.1472 0.1506 0.1699 -0.0042 -0.0045 -0.0074 18  VAL   C C   
1165 O  O   . VAL   B 12  ? 0.1609 0.1636 0.1829 -0.0052 -0.0027 -0.0064 18  VAL   C O   
1166 C  CB  . VAL   B 12  ? 0.1904 0.1968 0.2219 -0.0050 -0.0071 -0.0102 18  VAL   C CB  
1167 C  CG1 . VAL   B 12  ? 0.2315 0.2410 0.2686 -0.0046 -0.0085 -0.0116 18  VAL   C CG1 
1168 C  CG2 . VAL   B 12  ? 0.1921 0.1981 0.2260 -0.0071 -0.0057 -0.0103 18  VAL   C CG2 
1169 N  N   . ASN   B 13  ? 0.1468 0.1482 0.1662 -0.0029 -0.0060 -0.0076 19  ASN   C N   
1170 C  CA  . ASN   B 13  ? 0.1541 0.1528 0.1703 -0.0024 -0.0056 -0.0070 19  ASN   C CA  
1171 C  C   . ASN   B 13  ? 0.1568 0.1536 0.1750 -0.0037 -0.0058 -0.0075 19  ASN   C C   
1172 O  O   . ASN   B 13  ? 0.1642 0.1609 0.1846 -0.0043 -0.0075 -0.0090 19  ASN   C O   
1173 C  CB  . ASN   B 13  ? 0.1706 0.1675 0.1832 -0.0011 -0.0068 -0.0076 19  ASN   C CB  
1174 C  CG  . ASN   B 13  ? 0.1741 0.1721 0.1844 -0.0002 -0.0064 -0.0070 19  ASN   C CG  
1175 O  OD1 . ASN   B 13  ? 0.1768 0.1754 0.1870 -0.0001 -0.0076 -0.0073 19  ASN   C OD1 
1176 N  ND2 . ASN   B 13  ? 0.1844 0.1828 0.1933 0.0004  -0.0049 -0.0060 19  ASN   C ND2 
1177 N  N   . ARG   B 14  ? 0.1619 0.1569 0.1792 -0.0040 -0.0045 -0.0063 20  ARG   C N   
1178 C  CA  . ARG   B 14  ? 0.1683 0.1607 0.1873 -0.0055 -0.0045 -0.0066 20  ARG   C CA  
1179 C  C   . ARG   B 14  ? 0.1705 0.1601 0.1886 -0.0051 -0.0064 -0.0085 20  ARG   C C   
1180 O  O   . ARG   B 14  ? 0.1696 0.1586 0.1905 -0.0066 -0.0074 -0.0097 20  ARG   C O   
1181 C  CB  . ARG   B 14  ? 0.1701 0.1598 0.1873 -0.0056 -0.0033 -0.0047 20  ARG   C CB  
1182 C  CG  . ARG   B 14  ? 0.1676 0.1540 0.1862 -0.0077 -0.0028 -0.0045 20  ARG   C CG  
1183 C  CD  . ARG   B 14  ? 0.1758 0.1584 0.1916 -0.0071 -0.0023 -0.0022 20  ARG   C CD  
1184 N  NE  . ARG   B 14  ? 0.1799 0.1582 0.1961 -0.0093 -0.0017 -0.0014 20  ARG   C NE  
1185 C  CZ  . ARG   B 14  ? 0.2181 0.1920 0.2346 -0.0092 -0.0027 -0.0023 20  ARG   C CZ  
1186 N  NH1 . ARG   B 14  ? 0.2226 0.1962 0.2391 -0.0074 -0.0041 -0.0046 20  ARG   C NH1 
1187 N  NH2 . ARG   B 14  ? 0.2339 0.2033 0.2505 -0.0114 -0.0021 -0.0012 20  ARG   C NH2 
1188 N  N   . HIS   B 15  ? 0.1653 0.1536 0.1798 -0.0031 -0.0069 -0.0089 21  HIS   C N   
1189 C  CA  . HIS   B 15  ? 0.1689 0.1541 0.1814 -0.0028 -0.0084 -0.0110 21  HIS   C CA  
1190 C  C   . HIS   B 15  ? 0.1803 0.1666 0.1932 -0.0035 -0.0108 -0.0125 21  HIS   C C   
1191 O  O   . HIS   B 15  ? 0.1971 0.1804 0.2082 -0.0038 -0.0125 -0.0144 21  HIS   C O   
1192 C  CB  . HIS   B 15  ? 0.1839 0.1672 0.1923 -0.0007 -0.0075 -0.0112 21  HIS   C CB  
1193 C  CG  . HIS   B 15  ? 0.1718 0.1573 0.1776 0.0003  -0.0073 -0.0111 21  HIS   C CG  
1194 N  ND1 . HIS   B 15  ? 0.1780 0.1668 0.1845 0.0009  -0.0060 -0.0094 21  HIS   C ND1 
1195 C  CD2 . HIS   B 15  ? 0.1806 0.1649 0.1824 0.0006  -0.0083 -0.0125 21  HIS   C CD2 
1196 C  CE1 . HIS   B 15  ? 0.1754 0.1648 0.1789 0.0015  -0.0061 -0.0097 21  HIS   C CE1 
1197 N  NE2 . HIS   B 15  ? 0.1869 0.1736 0.1872 0.0014  -0.0074 -0.0114 21  HIS   C NE2 
1198 N  N   . LEU   B 16  ? 0.1815 0.1716 0.1965 -0.0036 -0.0112 -0.0119 22  LEU   C N   
1199 C  CA  . LEU   B 16  ? 0.1952 0.1864 0.2114 -0.0040 -0.0141 -0.0132 22  LEU   C CA  
1200 C  C   . LEU   B 16  ? 0.1971 0.1914 0.2205 -0.0056 -0.0147 -0.0136 22  LEU   C C   
1201 O  O   . LEU   B 16  ? 0.2027 0.1989 0.2291 -0.0058 -0.0173 -0.0146 22  LEU   C O   
1202 C  CB  . LEU   B 16  ? 0.1903 0.1830 0.2041 -0.0026 -0.0145 -0.0124 22  LEU   C CB  
1203 C  CG  . LEU   B 16  ? 0.1955 0.1855 0.2025 -0.0013 -0.0136 -0.0122 22  LEU   C CG  
1204 C  CD1 . LEU   B 16  ? 0.2086 0.1998 0.2133 -0.0005 -0.0139 -0.0112 22  LEU   C CD1 
1205 C  CD2 . LEU   B 16  ? 0.2170 0.2027 0.2192 -0.0014 -0.0155 -0.0141 22  LEU   C CD2 
1206 N  N   . ALA   B 17  ? 0.1850 0.1800 0.2115 -0.0070 -0.0121 -0.0129 23  ALA   C N   
1207 C  CA  . ALA   B 17  ? 0.1836 0.1819 0.2172 -0.0089 -0.0117 -0.0134 23  ALA   C CA  
1208 C  C   . ALA   B 17  ? 0.1926 0.1904 0.2297 -0.0103 -0.0147 -0.0155 23  ALA   C C   
1209 O  O   . ALA   B 17  ? 0.2015 0.1953 0.2354 -0.0106 -0.0158 -0.0162 23  ALA   C O   
1210 C  CB  . ALA   B 17  ? 0.1838 0.1815 0.2182 -0.0105 -0.0083 -0.0120 23  ALA   C CB  
1211 N  N   . THR   B 18  ? 0.1950 0.1972 0.2391 -0.0111 -0.0160 -0.0166 24  THR   C N   
1212 C  CA  . THR   B 18  ? 0.2002 0.2029 0.2490 -0.0125 -0.0194 -0.0187 24  THR   C CA  
1213 C  C   . THR   B 18  ? 0.1973 0.2009 0.2522 -0.0156 -0.0173 -0.0193 24  THR   C C   
1214 O  O   . THR   B 18  ? 0.1900 0.1939 0.2453 -0.0167 -0.0132 -0.0178 24  THR   C O   
1215 C  CB  . THR   B 18  ? 0.2204 0.2280 0.2754 -0.0115 -0.0222 -0.0197 24  THR   C CB  
1216 O  OG1 . THR   B 18  ? 0.2337 0.2462 0.2960 -0.0124 -0.0189 -0.0195 24  THR   C OG1 
1217 C  CG2 . THR   B 18  ? 0.2309 0.2372 0.2799 -0.0087 -0.0242 -0.0188 24  THR   C CG2 
1218 N  N   . HIS   B 19  ? 0.2085 0.2124 0.2682 -0.0174 -0.0203 -0.0213 25  HIS   C N   
1219 C  CA  . HIS   B 19  ? 0.2022 0.2076 0.2691 -0.0209 -0.0184 -0.0220 25  HIS   C CA  
1220 C  C   . HIS   B 19  ? 0.1854 0.1970 0.2600 -0.0219 -0.0148 -0.0217 25  HIS   C C   
1221 O  O   . HIS   B 19  ? 0.2035 0.2151 0.2799 -0.0243 -0.0105 -0.0208 25  HIS   C O   
1222 C  CB  . HIS   B 19  ? 0.2500 0.2565 0.3228 -0.0227 -0.0229 -0.0248 25  HIS   C CB  
1223 C  CG  . HIS   B 19  ? 0.3728 0.3727 0.4382 -0.0226 -0.0261 -0.0257 25  HIS   C CG  
1224 N  ND1 . HIS   B 19  ? 0.4324 0.4260 0.4917 -0.0233 -0.0237 -0.0249 25  HIS   C ND1 
1225 C  CD2 . HIS   B 19  ? 0.4221 0.4209 0.4860 -0.0220 -0.0316 -0.0277 25  HIS   C CD2 
1226 C  CE1 . HIS   B 19  ? 0.4471 0.4361 0.5016 -0.0231 -0.0274 -0.0267 25  HIS   C CE1 
1227 N  NE2 . HIS   B 19  ? 0.4497 0.4415 0.5061 -0.0225 -0.0321 -0.0284 25  HIS   C NE2 
1228 N  N   . ASN   B 20  ? 0.1880 0.2046 0.2669 -0.0198 -0.0165 -0.0224 26  ASN   C N   
1229 C  CA  . ASN   B 20  ? 0.1923 0.2148 0.2788 -0.0203 -0.0130 -0.0227 26  ASN   C CA  
1230 C  C   . ASN   B 20  ? 0.1853 0.2060 0.2654 -0.0200 -0.0079 -0.0204 26  ASN   C C   
1231 O  O   . ASN   B 20  ? 0.1876 0.2107 0.2713 -0.0221 -0.0033 -0.0202 26  ASN   C O   
1232 C  CB  . ASN   B 20  ? 0.2235 0.2506 0.3153 -0.0177 -0.0162 -0.0239 26  ASN   C CB  
1233 C  CG  . ASN   B 20  ? 0.2977 0.3315 0.3994 -0.0181 -0.0127 -0.0249 26  ASN   C CG  
1234 O  OD1 . ASN   B 20  ? 0.3159 0.3542 0.4277 -0.0207 -0.0113 -0.0267 26  ASN   C OD1 
1235 N  ND2 . ASN   B 20  ? 0.3207 0.3550 0.4195 -0.0158 -0.0107 -0.0241 26  ASN   C ND2 
1236 N  N   . ASP   B 21  ? 0.1801 0.1965 0.2504 -0.0175 -0.0087 -0.0186 27  ASP   C N   
1237 C  CA  . ASP   B 21  ? 0.1851 0.1998 0.2494 -0.0173 -0.0045 -0.0165 27  ASP   C CA  
1238 C  C   . ASP   B 21  ? 0.1909 0.2023 0.2531 -0.0202 -0.0013 -0.0152 27  ASP   C C   
1239 O  O   . ASP   B 21  ? 0.1996 0.2117 0.2615 -0.0218 0.0028  -0.0141 27  ASP   C O   
1240 C  CB  . ASP   B 21  ? 0.1772 0.1879 0.2324 -0.0145 -0.0062 -0.0150 27  ASP   C CB  
1241 C  CG  . ASP   B 21  ? 0.1918 0.2046 0.2469 -0.0118 -0.0083 -0.0154 27  ASP   C CG  
1242 O  OD1 . ASP   B 21  ? 0.2050 0.2220 0.2652 -0.0116 -0.0068 -0.0160 27  ASP   C OD1 
1243 O  OD2 . ASP   B 21  ? 0.1968 0.2069 0.2468 -0.0099 -0.0113 -0.0152 27  ASP   C OD2 
1244 N  N   . TRP   B 22  ? 0.1881 0.1953 0.2484 -0.0211 -0.0033 -0.0153 28  TRP   C N   
1245 C  CA  . TRP   B 22  ? 0.1940 0.1970 0.2522 -0.0238 -0.0007 -0.0139 28  TRP   C CA  
1246 C  C   . TRP   B 22  ? 0.2120 0.2181 0.2780 -0.0278 0.0022  -0.0148 28  TRP   C C   
1247 O  O   . TRP   B 22  ? 0.2333 0.2370 0.2970 -0.0302 0.0060  -0.0130 28  TRP   C O   
1248 C  CB  . TRP   B 22  ? 0.1964 0.1936 0.2509 -0.0236 -0.0036 -0.0142 28  TRP   C CB  
1249 C  CG  . TRP   B 22  ? 0.1856 0.1783 0.2314 -0.0207 -0.0042 -0.0125 28  TRP   C CG  
1250 C  CD1 . TRP   B 22  ? 0.1951 0.1870 0.2372 -0.0177 -0.0071 -0.0133 28  TRP   C CD1 
1251 C  CD2 . TRP   B 22  ? 0.1884 0.1767 0.2284 -0.0206 -0.0019 -0.0099 28  TRP   C CD2 
1252 N  NE1 . TRP   B 22  ? 0.1993 0.1874 0.2347 -0.0158 -0.0063 -0.0115 28  TRP   C NE1 
1253 C  CE2 . TRP   B 22  ? 0.1991 0.1850 0.2334 -0.0173 -0.0034 -0.0094 28  TRP   C CE2 
1254 C  CE3 . TRP   B 22  ? 0.2137 0.1997 0.2526 -0.0230 0.0013  -0.0077 28  TRP   C CE3 
1255 C  CZ2 . TRP   B 22  ? 0.2150 0.1967 0.2438 -0.0161 -0.0024 -0.0070 28  TRP   C CZ2 
1256 C  CZ3 . TRP   B 22  ? 0.2299 0.2113 0.2622 -0.0218 0.0021  -0.0051 28  TRP   C CZ3 
1257 C  CH2 . TRP   B 22  ? 0.2295 0.2090 0.2574 -0.0182 0.0001  -0.0048 28  TRP   C CH2 
1258 N  N   . ALA   B 23  ? 0.1936 0.2053 0.2688 -0.0283 0.0006  -0.0174 29  ALA   C N   
1259 C  CA  . ALA   B 23  ? 0.2069 0.2228 0.2913 -0.0321 0.0037  -0.0186 29  ALA   C CA  
1260 C  C   . ALA   B 23  ? 0.2075 0.2278 0.2939 -0.0326 0.0088  -0.0183 29  ALA   C C   
1261 O  O   . ALA   B 23  ? 0.2310 0.2543 0.3234 -0.0360 0.0129  -0.0190 29  ALA   C O   
1262 C  CB  . ALA   B 23  ? 0.2015 0.2228 0.2965 -0.0323 -0.0002 -0.0218 29  ALA   C CB  
1263 N  N   . ASN   B 24  ? 0.1841 0.2052 0.2663 -0.0291 0.0084  -0.0178 30  ASN   C N   
1264 C  CA  . ASN   B 24  ? 0.1841 0.2085 0.2666 -0.0290 0.0127  -0.0177 30  ASN   C CA  
1265 C  C   . ASN   B 24  ? 0.1910 0.2104 0.2617 -0.0279 0.0142  -0.0149 30  ASN   C C   
1266 O  O   . ASN   B 24  ? 0.1919 0.2128 0.2602 -0.0259 0.0152  -0.0148 30  ASN   C O   
1267 C  CB  . ASN   B 24  ? 0.1824 0.2129 0.2721 -0.0261 0.0106  -0.0201 30  ASN   C CB  
1268 C  CG  . ASN   B 24  ? 0.2190 0.2554 0.3219 -0.0275 0.0094  -0.0230 30  ASN   C CG  
1269 O  OD1 . ASN   B 24  ? 0.2428 0.2837 0.3535 -0.0303 0.0139  -0.0245 30  ASN   C OD1 
1270 N  ND2 . ASN   B 24  ? 0.2074 0.2437 0.3129 -0.0261 0.0035  -0.0239 30  ASN   C ND2 
1271 N  N   . LEU   B 25  ? 0.1942 0.2074 0.2580 -0.0289 0.0139  -0.0126 31  LEU   C N   
1272 C  CA  . LEU   B 25  ? 0.2011 0.2093 0.2543 -0.0275 0.0142  -0.0097 31  LEU   C CA  
1273 C  C   . LEU   B 25  ? 0.2082 0.2164 0.2572 -0.0291 0.0189  -0.0085 31  LEU   C C   
1274 O  O   . LEU   B 25  ? 0.2345 0.2424 0.2845 -0.0327 0.0228  -0.0082 31  LEU   C O   
1275 C  CB  . LEU   B 25  ? 0.2064 0.2078 0.2546 -0.0285 0.0129  -0.0077 31  LEU   C CB  
1276 C  CG  . LEU   B 25  ? 0.2167 0.2127 0.2550 -0.0269 0.0126  -0.0047 31  LEU   C CG  
1277 C  CD1 . LEU   B 25  ? 0.2196 0.2166 0.2553 -0.0227 0.0094  -0.0050 31  LEU   C CD1 
1278 C  CD2 . LEU   B 25  ? 0.2341 0.2233 0.2689 -0.0279 0.0115  -0.0029 31  LEU   C CD2 
1279 N  N   . VAL   B 26  ? 0.1924 0.2003 0.2356 -0.0267 0.0186  -0.0076 32  VAL   C N   
1280 C  CA  . VAL   B 26  ? 0.2048 0.2116 0.2419 -0.0281 0.0223  -0.0063 32  VAL   C CA  
1281 C  C   . VAL   B 26  ? 0.2250 0.2254 0.2520 -0.0275 0.0208  -0.0029 32  VAL   C C   
1282 O  O   . VAL   B 26  ? 0.2601 0.2566 0.2811 -0.0301 0.0233  -0.0007 32  VAL   C O   
1283 C  CB  . VAL   B 26  ? 0.2134 0.2245 0.2517 -0.0260 0.0228  -0.0082 32  VAL   C CB  
1284 C  CG1 . VAL   B 26  ? 0.2406 0.2496 0.2706 -0.0271 0.0260  -0.0068 32  VAL   C CG1 
1285 C  CG2 . VAL   B 26  ? 0.2256 0.2431 0.2748 -0.0265 0.0246  -0.0116 32  VAL   C CG2 
1286 N  N   . TRP   B 27  ? 0.2048 0.2039 0.2298 -0.0241 0.0167  -0.0023 33  TRP   C N   
1287 C  CA  . TRP   B 27  ? 0.2224 0.2166 0.2396 -0.0229 0.0148  0.0005  33  TRP   C CA  
1288 C  C   . TRP   B 27  ? 0.2068 0.2005 0.2251 -0.0196 0.0107  0.0002  33  TRP   C C   
1289 O  O   . TRP   B 27  ? 0.2071 0.2046 0.2295 -0.0178 0.0093  -0.0019 33  TRP   C O   
1290 C  CB  . TRP   B 27  ? 0.2352 0.2299 0.2465 -0.0224 0.0158  0.0014  33  TRP   C CB  
1291 C  CG  . TRP   B 27  ? 0.2448 0.2359 0.2495 -0.0204 0.0130  0.0040  33  TRP   C CG  
1292 C  CD1 . TRP   B 27  ? 0.2795 0.2652 0.2775 -0.0214 0.0126  0.0071  33  TRP   C CD1 
1293 C  CD2 . TRP   B 27  ? 0.2317 0.2246 0.2364 -0.0171 0.0101  0.0036  33  TRP   C CD2 
1294 N  NE1 . TRP   B 27  ? 0.2920 0.2766 0.2869 -0.0186 0.0093  0.0085  33  TRP   C NE1 
1295 C  CE2 . TRP   B 27  ? 0.2593 0.2485 0.2583 -0.0162 0.0081  0.0063  33  TRP   C CE2 
1296 C  CE3 . TRP   B 27  ? 0.2252 0.2221 0.2342 -0.0150 0.0089  0.0013  33  TRP   C CE3 
1297 C  CZ2 . TRP   B 27  ? 0.2543 0.2447 0.2526 -0.0133 0.0054  0.0064  33  TRP   C CZ2 
1298 C  CZ3 . TRP   B 27  ? 0.2269 0.2243 0.2342 -0.0125 0.0065  0.0017  33  TRP   C CZ3 
1299 C  CH2 . TRP   B 27  ? 0.2312 0.2257 0.2337 -0.0117 0.0049  0.0041  33  TRP   C CH2 
1300 N  N   . GLU   B 28  ? 0.2120 0.2008 0.2264 -0.0187 0.0089  0.0022  34  GLU   C N   
1301 C  CA  . GLU   B 28  ? 0.2179 0.2061 0.2326 -0.0155 0.0057  0.0018  34  GLU   C CA  
1302 C  C   . GLU   B 28  ? 0.2106 0.1945 0.2200 -0.0141 0.0043  0.0044  34  GLU   C C   
1303 O  O   . GLU   B 28  ? 0.2142 0.1939 0.2199 -0.0158 0.0051  0.0067  34  GLU   C O   
1304 C  CB  . GLU   B 28  ? 0.2152 0.2025 0.2342 -0.0156 0.0043  0.0000  34  GLU   C CB  
1305 C  CG  . GLU   B 28  ? 0.2259 0.2086 0.2451 -0.0182 0.0052  0.0009  34  GLU   C CG  
1306 C  CD  . GLU   B 28  ? 0.2548 0.2310 0.2696 -0.0172 0.0039  0.0031  34  GLU   C CD  
1307 O  OE1 . GLU   B 28  ? 0.2914 0.2631 0.3044 -0.0196 0.0051  0.0050  34  GLU   C OE1 
1308 O  OE2 . GLU   B 28  ? 0.2229 0.1984 0.2365 -0.0141 0.0018  0.0030  34  GLU   C OE2 
1309 N  N   . ASP   B 29  ? 0.2096 0.1945 0.2188 -0.0111 0.0022  0.0040  35  ASP   C N   
1310 C  CA  . ASP   B 29  ? 0.1994 0.1811 0.2053 -0.0091 0.0005  0.0061  35  ASP   C CA  
1311 C  C   . ASP   B 29  ? 0.1936 0.1756 0.2016 -0.0062 -0.0012 0.0047  35  ASP   C C   
1312 O  O   . ASP   B 29  ? 0.1892 0.1749 0.1981 -0.0047 -0.0016 0.0034  35  ASP   C O   
1313 C  CB  . ASP   B 29  ? 0.2128 0.1963 0.2151 -0.0090 0.0005  0.0076  35  ASP   C CB  
1314 C  CG  . ASP   B 29  ? 0.2499 0.2307 0.2493 -0.0072 -0.0016 0.0100  35  ASP   C CG  
1315 O  OD1 . ASP   B 29  ? 0.3028 0.2817 0.3042 -0.0050 -0.0032 0.0099  35  ASP   C OD1 
1316 O  OD2 . ASP   B 29  ? 0.2635 0.2443 0.2589 -0.0079 -0.0019 0.0118  35  ASP   C OD2 
1317 N  N   . SER   B 30  ? 0.1899 0.1673 0.1983 -0.0055 -0.0021 0.0048  36  SER   C N   
1318 C  CA  A SER   B 30  ? 0.1888 0.1658 0.1987 -0.0029 -0.0032 0.0031  36  SER   C CA  
1319 C  CA  B SER   B 30  ? 0.1922 0.1694 0.2022 -0.0028 -0.0032 0.0031  36  SER   C CA  
1320 C  C   . SER   B 30  ? 0.1923 0.1714 0.2019 -0.0001 -0.0041 0.0038  36  SER   C C   
1321 O  O   . SER   B 30  ? 0.2014 0.1829 0.2122 0.0016  -0.0041 0.0020  36  SER   C O   
1322 C  CB  A SER   B 30  ? 0.2282 0.1991 0.2384 -0.0027 -0.0038 0.0033  36  SER   C CB  
1323 C  CB  B SER   B 30  ? 0.2394 0.2106 0.2497 -0.0024 -0.0039 0.0030  36  SER   C CB  
1324 O  OG  A SER   B 30  ? 0.2736 0.2436 0.2849 -0.0002 -0.0045 0.0012  36  SER   C OG  
1325 O  OG  B SER   B 30  ? 0.3003 0.2692 0.3115 -0.0051 -0.0033 0.0021  36  SER   C OG  
1326 N  N   . SER   B 31  ? 0.1810 0.1592 0.1887 0.0001  -0.0048 0.0065  37  SER   C N   
1327 C  CA  . SER   B 31  ? 0.1831 0.1639 0.1916 0.0025  -0.0060 0.0071  37  SER   C CA  
1328 C  C   . SER   B 31  ? 0.1839 0.1703 0.1926 0.0023  -0.0053 0.0059  37  SER   C C   
1329 O  O   . SER   B 31  ? 0.2033 0.1925 0.2138 0.0042  -0.0059 0.0056  37  SER   C O   
1330 C  CB  . SER   B 31  ? 0.2321 0.2103 0.2382 0.0026  -0.0077 0.0103  37  SER   C CB  
1331 O  OG  . SER   B 31  ? 0.3017 0.2815 0.3043 0.0002  -0.0073 0.0116  37  SER   C OG  
1332 N  N   . ARG   B 32  ? 0.1716 0.1598 0.1793 0.0000  -0.0041 0.0053  38  ARG   C N   
1333 C  CA  . ARG   B 32  ? 0.1672 0.1601 0.1753 -0.0002 -0.0035 0.0041  38  ARG   C CA  
1334 C  C   . ARG   B 32  ? 0.1616 0.1558 0.1713 -0.0001 -0.0028 0.0017  38  ARG   C C   
1335 O  O   . ARG   B 32  ? 0.1587 0.1560 0.1686 -0.0002 -0.0025 0.0008  38  ARG   C O   
1336 C  CB  . ARG   B 32  ? 0.1825 0.1763 0.1882 -0.0026 -0.0025 0.0049  38  ARG   C CB  
1337 C  CG  . ARG   B 32  ? 0.1833 0.1758 0.1858 -0.0029 -0.0036 0.0074  38  ARG   C CG  
1338 C  CD  . ARG   B 32  ? 0.1851 0.1779 0.1841 -0.0054 -0.0022 0.0079  38  ARG   C CD  
1339 N  NE  . ARG   B 32  ? 0.1709 0.1678 0.1707 -0.0056 -0.0016 0.0062  38  ARG   C NE  
1340 C  CZ  . ARG   B 32  ? 0.1795 0.1773 0.1761 -0.0071 -0.0010 0.0064  38  ARG   C CZ  
1341 N  NH1 . ARG   B 32  ? 0.2122 0.2071 0.2038 -0.0087 -0.0010 0.0083  38  ARG   C NH1 
1342 N  NH2 . ARG   B 32  ? 0.1900 0.1909 0.1876 -0.0070 -0.0006 0.0048  38  ARG   C NH2 
1343 N  N   . ASP   B 33  ? 0.1686 0.1601 0.1791 -0.0002 -0.0028 0.0007  39  ASP   C N   
1344 C  CA  . ASP   B 33  ? 0.1553 0.1475 0.1668 -0.0006 -0.0028 -0.0015 39  ASP   C CA  
1345 C  C   . ASP   B 33  ? 0.1492 0.1441 0.1617 -0.0023 -0.0023 -0.0020 39  ASP   C C   
1346 O  O   . ASP   B 33  ? 0.1580 0.1547 0.1711 -0.0020 -0.0027 -0.0033 39  ASP   C O   
1347 C  CB  . ASP   B 33  ? 0.1601 0.1537 0.1710 0.0012  -0.0030 -0.0028 39  ASP   C CB  
1348 C  CG  . ASP   B 33  ? 0.1596 0.1527 0.1701 0.0009  -0.0035 -0.0048 39  ASP   C CG  
1349 O  OD1 . ASP   B 33  ? 0.1787 0.1693 0.1897 0.0001  -0.0042 -0.0058 39  ASP   C OD1 
1350 O  OD2 . ASP   B 33  ? 0.1744 0.1692 0.1837 0.0014  -0.0036 -0.0054 39  ASP   C OD2 
1351 N  N   . LEU   B 34  ? 0.1451 0.1399 0.1577 -0.0041 -0.0013 -0.0008 40  LEU   C N   
1352 C  CA  . LEU   B 34  ? 0.1518 0.1493 0.1663 -0.0057 -0.0003 -0.0017 40  LEU   C CA  
1353 C  C   . LEU   B 34  ? 0.1751 0.1716 0.1919 -0.0078 0.0006  -0.0021 40  LEU   C C   
1354 O  O   . LEU   B 34  ? 0.1805 0.1739 0.1959 -0.0088 0.0011  -0.0008 40  LEU   C O   
1355 C  CB  . LEU   B 34  ? 0.1578 0.1570 0.1703 -0.0063 0.0009  -0.0007 40  LEU   C CB  
1356 C  CG  . LEU   B 34  ? 0.1712 0.1723 0.1823 -0.0047 0.0002  -0.0006 40  LEU   C CG  
1357 C  CD1 . LEU   B 34  ? 0.1879 0.1900 0.1965 -0.0058 0.0012  0.0003  40  LEU   C CD1 
1358 C  CD2 . LEU   B 34  ? 0.1914 0.1945 0.2046 -0.0040 -0.0004 -0.0024 40  LEU   C CD2 
1359 N  N   . LEU   B 35  ? 0.1655 0.1649 0.1862 -0.0086 0.0009  -0.0039 41  LEU   C N   
1360 C  CA  . LEU   B 35  ? 0.1629 0.1628 0.1874 -0.0110 0.0022  -0.0046 41  LEU   C CA  
1361 C  C   . LEU   B 35  ? 0.1536 0.1578 0.1818 -0.0115 0.0035  -0.0060 41  LEU   C C   
1362 O  O   . LEU   B 35  ? 0.1632 0.1695 0.1926 -0.0098 0.0021  -0.0070 41  LEU   C O   
1363 C  CB  . LEU   B 35  ? 0.1724 0.1710 0.1999 -0.0113 0.0004  -0.0060 41  LEU   C CB  
1364 C  CG  . LEU   B 35  ? 0.1779 0.1772 0.2104 -0.0141 0.0016  -0.0069 41  LEU   C CG  
1365 C  CD1 . LEU   B 35  ? 0.1874 0.1830 0.2204 -0.0148 0.0000  -0.0074 41  LEU   C CD1 
1366 C  CD2 . LEU   B 35  ? 0.1908 0.1953 0.2299 -0.0143 0.0011  -0.0092 41  LEU   C CD2 
1367 N  N   . VAL   B 36  ? 0.1537 0.1589 0.1836 -0.0139 0.0064  -0.0060 42  VAL   C N   
1368 C  CA  . VAL   B 36  ? 0.1592 0.1687 0.1935 -0.0145 0.0084  -0.0077 42  VAL   C CA  
1369 C  C   . VAL   B 36  ? 0.1647 0.1762 0.2058 -0.0169 0.0098  -0.0092 42  VAL   C C   
1370 O  O   . VAL   B 36  ? 0.1762 0.1853 0.2160 -0.0194 0.0117  -0.0081 42  VAL   C O   
1371 C  CB  . VAL   B 36  ? 0.1638 0.1731 0.1935 -0.0156 0.0115  -0.0068 42  VAL   C CB  
1372 C  CG1 . VAL   B 36  ? 0.1890 0.2025 0.2237 -0.0162 0.0142  -0.0092 42  VAL   C CG1 
1373 C  CG2 . VAL   B 36  ? 0.1719 0.1796 0.1957 -0.0135 0.0097  -0.0055 42  VAL   C CG2 
1374 N  N   . SER   B 37  ? 0.1704 0.1860 0.2189 -0.0161 0.0088  -0.0116 43  SER   C N   
1375 C  CA  . SER   B 37  ? 0.1628 0.1817 0.2198 -0.0182 0.0100  -0.0134 43  SER   C CA  
1376 C  C   . SER   B 37  ? 0.1795 0.2035 0.2426 -0.0183 0.0128  -0.0155 43  SER   C C   
1377 O  O   . SER   B 37  ? 0.1905 0.2152 0.2516 -0.0163 0.0128  -0.0158 43  SER   C O   
1378 C  CB  . SER   B 37  ? 0.1694 0.1889 0.2310 -0.0172 0.0055  -0.0147 43  SER   C CB  
1379 O  OG  . SER   B 37  ? 0.1873 0.2084 0.2500 -0.0141 0.0023  -0.0155 43  SER   C OG  
1380 N  N   . SER   B 38  ? 0.1817 0.2092 0.2527 -0.0208 0.0155  -0.0172 44  SER   C N   
1381 C  CA  . SER   B 38  ? 0.2052 0.2379 0.2832 -0.0209 0.0188  -0.0197 44  SER   C CA  
1382 C  C   . SER   B 38  ? 0.2263 0.2638 0.3148 -0.0185 0.0151  -0.0222 44  SER   C C   
1383 O  O   . SER   B 38  ? 0.2399 0.2776 0.3321 -0.0183 0.0110  -0.0225 44  SER   C O   
1384 C  CB  . SER   B 38  ? 0.2281 0.2626 0.3097 -0.0250 0.0242  -0.0204 44  SER   C CB  
1385 O  OG  . SER   B 38  ? 0.2567 0.2928 0.3455 -0.0269 0.0228  -0.0211 44  SER   C OG  
1386 N  N   . THR   B 39  ? 0.2379 0.2789 0.3310 -0.0167 0.0163  -0.0242 45  THR   C N   
1387 C  CA  . THR   B 39  ? 0.2604 0.3057 0.3638 -0.0140 0.0126  -0.0264 45  THR   C CA  
1388 C  C   . THR   B 39  ? 0.2922 0.3439 0.4071 -0.0147 0.0169  -0.0297 45  THR   C C   
1389 O  O   . THR   B 39  ? 0.2965 0.3485 0.4090 -0.0167 0.0230  -0.0302 45  THR   C O   
1390 C  CB  . THR   B 39  ? 0.2817 0.3243 0.3799 -0.0102 0.0094  -0.0257 45  THR   C CB  
1391 O  OG1 . THR   B 39  ? 0.3026 0.3454 0.3984 -0.0102 0.0140  -0.0264 45  THR   C OG1 
1392 C  CG2 . THR   B 39  ? 0.3012 0.3378 0.3878 -0.0095 0.0062  -0.0227 45  THR   C CG2 
1393 N  N   . THR   B 40  ? 0.3110 0.3678 0.4381 -0.0129 0.0137  -0.0320 46  THR   C N   
1394 C  CA  . THR   B 40  ? 0.3316 0.3951 0.4714 -0.0128 0.0175  -0.0356 46  THR   C CA  
1395 C  C   . THR   B 40  ? 0.3452 0.4084 0.4852 -0.0090 0.0171  -0.0367 46  THR   C C   
1396 O  O   . THR   B 40  ? 0.3726 0.4387 0.5168 -0.0092 0.0226  -0.0392 46  THR   C O   
1397 C  CB  . THR   B 40  ? 0.3644 0.4341 0.5191 -0.0128 0.0142  -0.0378 46  THR   C CB  
1398 O  OG1 . THR   B 40  ? 0.4146 0.4821 0.5684 -0.0097 0.0059  -0.0366 46  THR   C OG1 
1399 C  CG2 . THR   B 40  ? 0.3733 0.4439 0.5295 -0.0173 0.0161  -0.0374 46  THR   C CG2 
1400 N  N   . ALA   B 41  ? 0.3345 0.3937 0.4696 -0.0057 0.0109  -0.0350 47  ALA   C N   
1401 C  CA  . ALA   B 41  ? 0.3347 0.3925 0.4693 -0.0022 0.0099  -0.0356 47  ALA   C CA  
1402 C  C   . ALA   B 41  ? 0.3359 0.3885 0.4575 -0.0028 0.0136  -0.0342 47  ALA   C C   
1403 O  O   . ALA   B 41  ? 0.3412 0.3899 0.4521 -0.0049 0.0139  -0.0315 47  ALA   C O   
1404 C  CB  . ALA   B 41  ? 0.3453 0.4004 0.4792 0.0012  0.0019  -0.0341 47  ALA   C CB  
1405 N  N   . GLN   B 42  ? 0.3257 0.3783 0.4484 -0.0010 0.0159  -0.0360 48  GLN   C N   
1406 C  CA  . GLN   B 42  ? 0.3253 0.3732 0.4363 -0.0017 0.0190  -0.0350 48  GLN   C CA  
1407 C  C   . GLN   B 42  ? 0.3134 0.3555 0.4157 0.0005  0.0137  -0.0322 48  GLN   C C   
1408 O  O   . GLN   B 42  ? 0.3324 0.3739 0.4389 0.0036  0.0093  -0.0324 48  GLN   C O   
1409 C  CB  . GLN   B 42  ? 0.3610 0.4108 0.4771 -0.0007 0.0237  -0.0386 48  GLN   C CB  
1410 C  CG  . GLN   B 42  ? 0.4361 0.4808 0.5407 -0.0009 0.0260  -0.0382 48  GLN   C CG  
1411 C  CD  . GLN   B 42  ? 0.5292 0.5725 0.6243 -0.0049 0.0314  -0.0374 48  GLN   C CD  
1412 O  OE1 . GLN   B 42  ? 0.5633 0.6093 0.6606 -0.0077 0.0346  -0.0376 48  GLN   C OE1 
1413 N  NE2 . GLN   B 42  ? 0.5636 0.6021 0.6477 -0.0054 0.0323  -0.0365 48  GLN   C NE2 
1414 N  N   . GLY   B 43  ? 0.2551 0.2930 0.3453 -0.0013 0.0142  -0.0295 49  GLY   C N   
1415 C  CA  . GLY   B 43  ? 0.2364 0.2691 0.3177 0.0001  0.0102  -0.0268 49  GLY   C CA  
1416 C  C   . GLY   B 43  ? 0.2403 0.2703 0.3167 0.0007  0.0122  -0.0275 49  GLY   C C   
1417 O  O   . GLY   B 43  ? 0.2611 0.2915 0.3349 -0.0012 0.0171  -0.0288 49  GLY   C O   
1418 N  N   . CYS   B 44  ? 0.2197 0.2462 0.2935 0.0029  0.0083  -0.0264 50  CYS   C N   
1419 C  CA  . CYS   B 44  ? 0.2280 0.2515 0.2981 0.0036  0.0097  -0.0272 50  CYS   C CA  
1420 C  C   . CYS   B 44  ? 0.2313 0.2502 0.2906 0.0028  0.0082  -0.0245 50  CYS   C C   
1421 O  O   . CYS   B 44  ? 0.2537 0.2696 0.3101 0.0034  0.0084  -0.0250 50  CYS   C O   
1422 C  CB  . CYS   B 44  ? 0.2424 0.2655 0.3201 0.0068  0.0074  -0.0290 50  CYS   C CB  
1423 S  SG  . CYS   B 44  ? 0.2999 0.3293 0.3923 0.0080  0.0098  -0.0330 50  CYS   C SG  
1424 N  N   . ASP   B 45  ? 0.1867 0.2050 0.2406 0.0015  0.0069  -0.0218 51  ASP   C N   
1425 C  CA  . ASP   B 45  ? 0.1971 0.2119 0.2419 0.0007  0.0059  -0.0195 51  ASP   C CA  
1426 C  C   . ASP   B 45  ? 0.2175 0.2320 0.2571 -0.0014 0.0096  -0.0202 51  ASP   C C   
1427 O  O   . ASP   B 45  ? 0.2500 0.2666 0.2901 -0.0030 0.0129  -0.0212 51  ASP   C O   
1428 C  CB  . ASP   B 45  ? 0.1969 0.2112 0.2378 0.0001  0.0036  -0.0168 51  ASP   C CB  
1429 C  CG  . ASP   B 45  ? 0.2647 0.2782 0.3081 0.0018  -0.0005 -0.0159 51  ASP   C CG  
1430 O  OD1 . ASP   B 45  ? 0.2781 0.2901 0.3240 0.0036  -0.0025 -0.0164 51  ASP   C OD1 
1431 O  OD2 . ASP   B 45  ? 0.2536 0.2675 0.2961 0.0014  -0.0019 -0.0147 51  ASP   C OD2 
1432 N  N   . THR   B 46  ? 0.2123 0.2240 0.2466 -0.0016 0.0091  -0.0197 52  THR   C N   
1433 C  CA  . THR   B 46  ? 0.2257 0.2365 0.2538 -0.0037 0.0118  -0.0202 52  THR   C CA  
1434 C  C   . THR   B 46  ? 0.2028 0.2129 0.2247 -0.0049 0.0102  -0.0172 52  THR   C C   
1435 O  O   . THR   B 46  ? 0.2154 0.2242 0.2361 -0.0041 0.0074  -0.0155 52  THR   C O   
1436 C  CB  . THR   B 46  ? 0.2856 0.2936 0.3119 -0.0034 0.0117  -0.0215 52  THR   C CB  
1437 O  OG1 . THR   B 46  ? 0.3392 0.3477 0.3715 -0.0022 0.0137  -0.0248 52  THR   C OG1 
1438 C  CG2 . THR   B 46  ? 0.3132 0.3198 0.3318 -0.0058 0.0131  -0.0216 52  THR   C CG2 
1439 N  N   . ILE   B 47  ? 0.1833 0.1940 0.2013 -0.0068 0.0119  -0.0166 53  ILE   C N   
1440 C  CA  . ILE   B 47  ? 0.1772 0.1873 0.1899 -0.0077 0.0103  -0.0139 53  ILE   C CA  
1441 C  C   . ILE   B 47  ? 0.1884 0.1969 0.1954 -0.0089 0.0101  -0.0139 53  ILE   C C   
1442 O  O   . ILE   B 47  ? 0.1927 0.2004 0.1968 -0.0103 0.0123  -0.0157 53  ILE   C O   
1443 C  CB  . ILE   B 47  ? 0.1966 0.2073 0.2074 -0.0092 0.0118  -0.0128 53  ILE   C CB  
1444 C  CG1 . ILE   B 47  ? 0.2223 0.2349 0.2393 -0.0086 0.0125  -0.0133 53  ILE   C CG1 
1445 C  CG2 . ILE   B 47  ? 0.1980 0.2078 0.2043 -0.0095 0.0095  -0.0099 53  ILE   C CG2 
1446 C  CD1 . ILE   B 47  ? 0.2518 0.2645 0.2719 -0.0068 0.0092  -0.0121 53  ILE   C CD1 
1447 N  N   . ALA   B 48  ? 0.1659 0.1739 0.1713 -0.0086 0.0074  -0.0121 54  ALA   C N   
1448 C  CA  . ALA   B 48  ? 0.1666 0.1736 0.1673 -0.0099 0.0066  -0.0120 54  ALA   C CA  
1449 C  C   . ALA   B 48  ? 0.1650 0.1720 0.1605 -0.0116 0.0069  -0.0109 54  ALA   C C   
1450 O  O   . ALA   B 48  ? 0.1758 0.1834 0.1712 -0.0114 0.0065  -0.0090 54  ALA   C O   
1451 C  CB  . ALA   B 48  ? 0.1707 0.1780 0.1722 -0.0092 0.0041  -0.0102 54  ALA   C CB  
1452 N  N   . ARG   B 49  ? 0.1603 0.1660 0.1510 -0.0133 0.0073  -0.0120 55  ARG   C N   
1453 C  CA  . ARG   B 49  ? 0.1622 0.1671 0.1463 -0.0151 0.0068  -0.0108 55  ARG   C CA  
1454 C  C   . ARG   B 49  ? 0.1741 0.1788 0.1556 -0.0159 0.0040  -0.0106 55  ARG   C C   
1455 O  O   . ARG   B 49  ? 0.1840 0.1871 0.1623 -0.0173 0.0046  -0.0128 55  ARG   C O   
1456 C  CB  . ARG   B 49  ? 0.1672 0.1705 0.1473 -0.0168 0.0103  -0.0127 55  ARG   C CB  
1457 C  CG  . ARG   B 49  ? 0.1925 0.1969 0.1770 -0.0161 0.0133  -0.0134 55  ARG   C CG  
1458 C  CD  . ARG   B 49  ? 0.1898 0.1947 0.1749 -0.0159 0.0125  -0.0105 55  ARG   C CD  
1459 N  NE  . ARG   B 49  ? 0.2062 0.2121 0.1958 -0.0157 0.0155  -0.0116 55  ARG   C NE  
1460 C  CZ  . ARG   B 49  ? 0.2147 0.2213 0.2071 -0.0153 0.0151  -0.0098 55  ARG   C CZ  
1461 N  NH1 . ARG   B 49  ? 0.1890 0.1951 0.1802 -0.0146 0.0121  -0.0071 55  ARG   C NH1 
1462 N  NH2 . ARG   B 49  ? 0.2437 0.2518 0.2411 -0.0154 0.0178  -0.0112 55  ARG   C NH2 
1463 N  N   . CYS   B 50  ? 0.1568 0.1631 0.1402 -0.0151 0.0011  -0.0083 56  CYS   C N   
1464 C  CA  . CYS   B 50  ? 0.1647 0.1720 0.1484 -0.0157 -0.0015 -0.0082 56  CYS   C CA  
1465 C  C   . CYS   B 50  ? 0.1733 0.1829 0.1595 -0.0147 -0.0043 -0.0056 56  CYS   C C   
1466 O  O   . CYS   B 50  ? 0.1766 0.1867 0.1644 -0.0133 -0.0042 -0.0039 56  CYS   C O   
1467 C  CB  . CYS   B 50  ? 0.1665 0.1737 0.1546 -0.0151 -0.0008 -0.0097 56  CYS   C CB  
1468 S  SG  . CYS   B 50  ? 0.1612 0.1699 0.1556 -0.0126 -0.0006 -0.0082 56  CYS   C SG  
1469 N  N   . ASP   B 51  ? 0.1818 0.1931 0.1694 -0.0153 -0.0067 -0.0055 57  ASP   C N   
1470 C  CA  . ASP   B 51  ? 0.1816 0.1960 0.1735 -0.0142 -0.0090 -0.0036 57  ASP   C CA  
1471 C  C   . ASP   B 51  ? 0.1713 0.1877 0.1687 -0.0139 -0.0086 -0.0041 57  ASP   C C   
1472 O  O   . ASP   B 51  ? 0.1774 0.1968 0.1784 -0.0139 -0.0104 -0.0033 57  ASP   C O   
1473 C  CB  . ASP   B 51  ? 0.2155 0.2310 0.2051 -0.0152 -0.0126 -0.0025 57  ASP   C CB  
1474 C  CG  . ASP   B 51  ? 0.2515 0.2673 0.2398 -0.0175 -0.0142 -0.0042 57  ASP   C CG  
1475 O  OD1 . ASP   B 51  ? 0.2575 0.2721 0.2461 -0.0184 -0.0123 -0.0062 57  ASP   C OD1 
1476 O  OD2 . ASP   B 51  ? 0.3405 0.3574 0.3271 -0.0184 -0.0179 -0.0034 57  ASP   C OD2 
1477 N  N   . CYS   B 52  ? 0.1652 0.1799 0.1634 -0.0137 -0.0063 -0.0053 58  CYS   C N   
1478 C  CA  . CYS   B 52  ? 0.1574 0.1729 0.1596 -0.0136 -0.0057 -0.0054 58  CYS   C CA  
1479 C  C   . CYS   B 52  ? 0.1545 0.1727 0.1607 -0.0121 -0.0059 -0.0038 58  CYS   C C   
1480 O  O   . CYS   B 52  ? 0.1474 0.1657 0.1536 -0.0104 -0.0057 -0.0028 58  CYS   C O   
1481 C  CB  . CYS   B 52  ? 0.1572 0.1696 0.1592 -0.0129 -0.0036 -0.0064 58  CYS   C CB  
1482 S  SG  . CYS   B 52  ? 0.1795 0.1885 0.1787 -0.0146 -0.0028 -0.0090 58  CYS   C SG  
1483 N  N   . GLN   B 53  ? 0.1411 0.1612 0.1507 -0.0128 -0.0059 -0.0038 59  GLN   C N   
1484 C  CA  . GLN   B 53  ? 0.1423 0.1649 0.1559 -0.0116 -0.0052 -0.0028 59  GLN   C CA  
1485 C  C   . GLN   B 53  ? 0.1510 0.1721 0.1652 -0.0123 -0.0031 -0.0031 59  GLN   C C   
1486 O  O   . GLN   B 53  ? 0.1516 0.1749 0.1688 -0.0121 -0.0020 -0.0026 59  GLN   C O   
1487 C  CB  . GLN   B 53  ? 0.1464 0.1737 0.1644 -0.0120 -0.0070 -0.0024 59  GLN   C CB  
1488 C  CG  . GLN   B 53  ? 0.1705 0.1987 0.1878 -0.0106 -0.0092 -0.0014 59  GLN   C CG  
1489 C  CD  . GLN   B 53  ? 0.1866 0.2195 0.2092 -0.0105 -0.0115 -0.0009 59  GLN   C CD  
1490 O  OE1 . GLN   B 53  ? 0.2103 0.2444 0.2324 -0.0117 -0.0146 -0.0009 59  GLN   C OE1 
1491 N  NE2 . GLN   B 53  ? 0.1540 0.1900 0.1823 -0.0091 -0.0102 -0.0007 59  GLN   C NE2 
1492 N  N   . THR   B 54  ? 0.1667 0.1839 0.1780 -0.0130 -0.0024 -0.0038 60  THR   C N   
1493 C  CA  . THR   B 54  ? 0.1716 0.1861 0.1824 -0.0134 -0.0009 -0.0036 60  THR   C CA  
1494 C  C   . THR   B 54  ? 0.1686 0.1790 0.1765 -0.0120 -0.0006 -0.0039 60  THR   C C   
1495 O  O   . THR   B 54  ? 0.1759 0.1853 0.1825 -0.0118 -0.0012 -0.0049 60  THR   C O   
1496 C  CB  . THR   B 54  ? 0.2251 0.2387 0.2364 -0.0159 -0.0007 -0.0042 60  THR   C CB  
1497 O  OG1 . THR   B 54  ? 0.2664 0.2774 0.2756 -0.0167 -0.0016 -0.0055 60  THR   C OG1 
1498 C  CG2 . THR   B 54  ? 0.2554 0.2737 0.2707 -0.0175 -0.0011 -0.0042 60  THR   C CG2 
1499 N  N   . GLY   B 55  ? 0.1589 0.1670 0.1658 -0.0112 0.0002  -0.0032 61  GLY   C N   
1500 C  CA  . GLY   B 55  ? 0.1705 0.1752 0.1757 -0.0097 -0.0001 -0.0034 61  GLY   C CA  
1501 C  C   . GLY   B 55  ? 0.1480 0.1499 0.1513 -0.0091 0.0002  -0.0023 61  GLY   C C   
1502 O  O   . GLY   B 55  ? 0.1659 0.1677 0.1686 -0.0104 0.0012  -0.0015 61  GLY   C O   
1503 N  N   . VAL   B 56  ? 0.1430 0.1425 0.1454 -0.0075 -0.0007 -0.0024 62  VAL   C N   
1504 C  CA  . VAL   B 56  ? 0.1509 0.1467 0.1505 -0.0069 -0.0012 -0.0013 62  VAL   C CA  
1505 C  C   . VAL   B 56  ? 0.1526 0.1493 0.1524 -0.0051 -0.0020 -0.0015 62  VAL   C C   
1506 O  O   . VAL   B 56  ? 0.1603 0.1581 0.1625 -0.0041 -0.0027 -0.0025 62  VAL   C O   
1507 C  CB  . VAL   B 56  ? 0.1545 0.1454 0.1529 -0.0067 -0.0025 -0.0012 62  VAL   C CB  
1508 C  CG1 . VAL   B 56  ? 0.1793 0.1658 0.1740 -0.0060 -0.0038 0.0002  62  VAL   C CG1 
1509 C  CG2 . VAL   B 56  ? 0.1824 0.1718 0.1805 -0.0089 -0.0016 -0.0011 62  VAL   C CG2 
1510 N  N   . TYR   B 57  ? 0.1480 0.1438 0.1451 -0.0048 -0.0017 -0.0007 63  TYR   C N   
1511 C  CA  . TYR   B 57  ? 0.1478 0.1437 0.1448 -0.0033 -0.0028 -0.0011 63  TYR   C CA  
1512 C  C   . TYR   B 57  ? 0.1579 0.1494 0.1508 -0.0029 -0.0045 -0.0003 63  TYR   C C   
1513 O  O   . TYR   B 57  ? 0.1664 0.1547 0.1551 -0.0039 -0.0040 0.0008  63  TYR   C O   
1514 C  CB  . TYR   B 57  ? 0.1525 0.1515 0.1502 -0.0031 -0.0014 -0.0013 63  TYR   C CB  
1515 C  CG  . TYR   B 57  ? 0.1561 0.1541 0.1504 -0.0036 0.0001  -0.0009 63  TYR   C CG  
1516 C  CD1 . TYR   B 57  ? 0.1672 0.1664 0.1614 -0.0051 0.0021  -0.0004 63  TYR   C CD1 
1517 C  CD2 . TYR   B 57  ? 0.1660 0.1621 0.1573 -0.0028 -0.0003 -0.0012 63  TYR   C CD2 
1518 C  CE1 . TYR   B 57  ? 0.1877 0.1864 0.1792 -0.0058 0.0043  -0.0003 63  TYR   C CE1 
1519 C  CE2 . TYR   B 57  ? 0.1723 0.1674 0.1598 -0.0034 0.0017  -0.0011 63  TYR   C CE2 
1520 C  CZ  . TYR   B 57  ? 0.1815 0.1781 0.1694 -0.0049 0.0043  -0.0007 63  TYR   C CZ  
1521 O  OH  . TYR   B 57  ? 0.1958 0.1917 0.1805 -0.0056 0.0070  -0.0009 63  TYR   C OH  
1522 N  N   . TYR   B 58  ? 0.1554 0.1465 0.1493 -0.0015 -0.0065 -0.0009 64  TYR   C N   
1523 C  CA  . TYR   B 58  ? 0.1633 0.1502 0.1531 -0.0009 -0.0089 -0.0003 64  TYR   C CA  
1524 C  C   . TYR   B 58  ? 0.1690 0.1558 0.1551 -0.0011 -0.0081 -0.0005 64  TYR   C C   
1525 O  O   . TYR   B 58  ? 0.1700 0.1596 0.1588 -0.0006 -0.0077 -0.0016 64  TYR   C O   
1526 C  CB  . TYR   B 58  ? 0.1766 0.1634 0.1702 0.0006  -0.0119 -0.0010 64  TYR   C CB  
1527 C  CG  . TYR   B 58  ? 0.1780 0.1603 0.1672 0.0011  -0.0152 -0.0002 64  TYR   C CG  
1528 C  CD1 . TYR   B 58  ? 0.1947 0.1719 0.1789 0.0008  -0.0165 0.0014  64  TYR   C CD1 
1529 C  CD2 . TYR   B 58  ? 0.2086 0.1913 0.1980 0.0018  -0.0172 -0.0011 64  TYR   C CD2 
1530 C  CE1 . TYR   B 58  ? 0.2077 0.1800 0.1865 0.0012  -0.0201 0.0025  64  TYR   C CE1 
1531 C  CE2 . TYR   B 58  ? 0.2149 0.1932 0.1993 0.0022  -0.0208 -0.0004 64  TYR   C CE2 
1532 C  CZ  . TYR   B 58  ? 0.2230 0.1961 0.2019 0.0019  -0.0223 0.0015  64  TYR   C CZ  
1533 O  OH  . TYR   B 58  ? 0.2754 0.2433 0.2481 0.0022  -0.0263 0.0025  64  TYR   C OH  
1534 N  N   . CYS   B 59  ? 0.1761 0.1588 0.1554 -0.0019 -0.0080 0.0005  65  CYS   C N   
1535 C  CA  . CYS   B 59  ? 0.1772 0.1586 0.1515 -0.0022 -0.0070 0.0001  65  CYS   C CA  
1536 C  C   . CYS   B 59  ? 0.1942 0.1705 0.1628 -0.0019 -0.0107 0.0005  65  CYS   C C   
1537 O  O   . CYS   B 59  ? 0.2082 0.1795 0.1704 -0.0027 -0.0115 0.0020  65  CYS   C O   
1538 C  CB  . CYS   B 59  ? 0.1825 0.1634 0.1531 -0.0039 -0.0033 0.0007  65  CYS   C CB  
1539 S  SG  . CYS   B 59  ? 0.2155 0.1944 0.1793 -0.0044 -0.0011 -0.0002 65  CYS   C SG  
1540 N  N   . SER   B 60  ? 0.1923 0.1695 0.1629 -0.0008 -0.0129 -0.0008 66  SER   C N   
1541 C  CA  . SER   B 60  ? 0.2150 0.1879 0.1811 -0.0004 -0.0172 -0.0006 66  SER   C CA  
1542 C  C   . SER   B 60  ? 0.2272 0.1949 0.1826 -0.0017 -0.0166 -0.0002 66  SER   C C   
1543 O  O   . SER   B 60  ? 0.2461 0.2083 0.1950 -0.0019 -0.0200 0.0012  66  SER   C O   
1544 C  CB  . SER   B 60  ? 0.2611 0.2365 0.2325 0.0006  -0.0195 -0.0023 66  SER   C CB  
1545 O  OG  . SER   B 60  ? 0.3330 0.3096 0.3036 0.0002  -0.0173 -0.0039 66  SER   C OG  
1546 N  N   . SER   B 61  ? 0.2161 0.1849 0.1693 -0.0025 -0.0122 -0.0012 67  SER   C N   
1547 C  CA  . SER   B 61  ? 0.2280 0.1920 0.1707 -0.0039 -0.0107 -0.0012 67  SER   C CA  
1548 C  C   . SER   B 61  ? 0.2442 0.2042 0.1803 -0.0055 -0.0091 0.0011  67  SER   C C   
1549 O  O   . SER   B 61  ? 0.2566 0.2117 0.1826 -0.0071 -0.0077 0.0014  67  SER   C O   
1550 C  CB  . SER   B 61  ? 0.2255 0.1921 0.1689 -0.0040 -0.0063 -0.0033 67  SER   C CB  
1551 O  OG  . SER   B 61  ? 0.2306 0.2018 0.1796 -0.0042 -0.0021 -0.0031 67  SER   C OG  
1552 N  N   . ARG   B 62  ? 0.2217 0.1832 0.1627 -0.0055 -0.0092 0.0026  68  ARG   C N   
1553 C  CA  . ARG   B 62  ? 0.2286 0.1860 0.1644 -0.0072 -0.0083 0.0049  68  ARG   C CA  
1554 C  C   . ARG   B 62  ? 0.2350 0.1892 0.1719 -0.0062 -0.0132 0.0068  68  ARG   C C   
1555 O  O   . ARG   B 62  ? 0.2514 0.2011 0.1841 -0.0074 -0.0132 0.0090  68  ARG   C O   
1556 C  CB  . ARG   B 62  ? 0.2513 0.2131 0.1920 -0.0083 -0.0032 0.0049  68  ARG   C CB  
1557 C  CG  . ARG   B 62  ? 0.2462 0.2106 0.1857 -0.0093 0.0018  0.0032  68  ARG   C CG  
1558 C  CD  . ARG   B 62  ? 0.2750 0.2335 0.2030 -0.0116 0.0043  0.0041  68  ARG   C CD  
1559 N  NE  . ARG   B 62  ? 0.2827 0.2440 0.2100 -0.0124 0.0097  0.0020  68  ARG   C NE  
1560 C  CZ  . ARG   B 62  ? 0.3481 0.3085 0.2716 -0.0117 0.0102  0.0000  68  ARG   C CZ  
1561 N  NH1 . ARG   B 62  ? 0.3465 0.3034 0.2664 -0.0105 0.0053  -0.0003 68  ARG   C NH1 
1562 N  NH2 . ARG   B 62  ? 0.3681 0.3309 0.2916 -0.0123 0.0156  -0.0021 68  ARG   C NH2 
1563 N  N   . ARG   B 63  ? 0.2400 0.1969 0.1839 -0.0040 -0.0171 0.0057  69  ARG   C N   
1564 C  CA  . ARG   B 63  ? 0.2426 0.1980 0.1907 -0.0025 -0.0213 0.0068  69  ARG   C CA  
1565 C  C   . ARG   B 63  ? 0.2696 0.2254 0.2209 -0.0032 -0.0190 0.0079  69  ARG   C C   
1566 O  O   . ARG   B 63  ? 0.2983 0.2490 0.2470 -0.0032 -0.0212 0.0098  69  ARG   C O   
1567 C  CB  . ARG   B 63  ? 0.2828 0.2307 0.2229 -0.0022 -0.0266 0.0087  69  ARG   C CB  
1568 C  CG  . ARG   B 63  ? 0.3347 0.2822 0.2722 -0.0016 -0.0299 0.0074  69  ARG   C CG  
1569 C  CD  . ARG   B 63  ? 0.4383 0.3901 0.3858 0.0007  -0.0339 0.0058  69  ARG   C CD  
1570 N  NE  . ARG   B 63  ? 0.5136 0.4629 0.4568 0.0010  -0.0386 0.0052  69  ARG   C NE  
1571 C  CZ  . ARG   B 63  ? 0.5647 0.5162 0.5073 0.0005  -0.0376 0.0031  69  ARG   C CZ  
1572 N  NH1 . ARG   B 63  ? 0.5510 0.5074 0.4974 0.0000  -0.0322 0.0014  69  ARG   C NH1 
1573 N  NH2 . ARG   B 63  ? 0.5843 0.5330 0.5226 0.0006  -0.0423 0.0024  69  ARG   C NH2 
1574 N  N   . LYS   B 64  ? 0.2546 0.2160 0.2110 -0.0039 -0.0145 0.0066  70  LYS   C N   
1575 C  CA  . LYS   B 64  ? 0.2577 0.2196 0.2165 -0.0051 -0.0121 0.0074  70  LYS   C CA  
1576 C  C   . LYS   B 64  ? 0.2171 0.1863 0.1850 -0.0046 -0.0099 0.0054  70  LYS   C C   
1577 O  O   . LYS   B 64  ? 0.2070 0.1806 0.1775 -0.0040 -0.0087 0.0039  70  LYS   C O   
1578 C  CB  . LYS   B 64  ? 0.3214 0.2813 0.2735 -0.0079 -0.0078 0.0084  70  LYS   C CB  
1579 C  CG  . LYS   B 64  ? 0.4775 0.4291 0.4205 -0.0095 -0.0089 0.0112  70  LYS   C CG  
1580 C  CD  . LYS   B 64  ? 0.5637 0.5147 0.5019 -0.0127 -0.0037 0.0118  70  LYS   C CD  
1581 C  CE  . LYS   B 64  ? 0.6479 0.5907 0.5780 -0.0150 -0.0038 0.0148  70  LYS   C CE  
1582 N  NZ  . LYS   B 64  ? 0.6792 0.6144 0.5976 -0.0154 -0.0060 0.0165  70  LYS   C NZ  
1583 N  N   . HIS   B 65  ? 0.1886 0.1582 0.1602 -0.0050 -0.0093 0.0056  71  HIS   C N   
1584 C  CA  . HIS   B 65  ? 0.1810 0.1566 0.1594 -0.0052 -0.0069 0.0041  71  HIS   C CA  
1585 C  C   . HIS   B 65  ? 0.2196 0.1964 0.1966 -0.0076 -0.0033 0.0045  71  HIS   C C   
1586 O  O   . HIS   B 65  ? 0.2559 0.2281 0.2283 -0.0093 -0.0026 0.0061  71  HIS   C O   
1587 C  CB  . HIS   B 65  ? 0.1826 0.1580 0.1659 -0.0043 -0.0084 0.0035  71  HIS   C CB  
1588 C  CG  . HIS   B 65  ? 0.1886 0.1643 0.1755 -0.0019 -0.0115 0.0026  71  HIS   C CG  
1589 N  ND1 . HIS   B 65  ? 0.2245 0.2054 0.2175 -0.0008 -0.0111 0.0007  71  HIS   C ND1 
1590 C  CD2 . HIS   B 65  ? 0.1968 0.1681 0.1822 -0.0005 -0.0151 0.0034  71  HIS   C CD2 
1591 C  CE1 . HIS   B 65  ? 0.1956 0.1756 0.1914 0.0010  -0.0140 0.0002  71  HIS   C CE1 
1592 N  NE2 . HIS   B 65  ? 0.2442 0.2188 0.2360 0.0014  -0.0167 0.0017  71  HIS   C NE2 
1593 N  N   . TYR   B 66  ? 0.1781 0.1609 0.1596 -0.0078 -0.0010 0.0033  72  TYR   C N   
1594 C  CA  . TYR   B 66  ? 0.1819 0.1671 0.1641 -0.0100 0.0023  0.0034  72  TYR   C CA  
1595 C  C   . TYR   B 66  ? 0.1763 0.1662 0.1649 -0.0102 0.0026  0.0023  72  TYR   C C   
1596 O  O   . TYR   B 66  ? 0.1769 0.1703 0.1690 -0.0086 0.0017  0.0012  72  TYR   C O   
1597 C  CB  . TYR   B 66  ? 0.1905 0.1787 0.1720 -0.0100 0.0047  0.0028  72  TYR   C CB  
1598 C  CG  . TYR   B 66  ? 0.2036 0.1869 0.1775 -0.0104 0.0052  0.0037  72  TYR   C CG  
1599 C  CD1 . TYR   B 66  ? 0.2214 0.2011 0.1901 -0.0129 0.0073  0.0050  72  TYR   C CD1 
1600 C  CD2 . TYR   B 66  ? 0.2150 0.1972 0.1863 -0.0087 0.0037  0.0031  72  TYR   C CD2 
1601 C  CE1 . TYR   B 66  ? 0.2457 0.2204 0.2059 -0.0136 0.0080  0.0059  72  TYR   C CE1 
1602 C  CE2 . TYR   B 66  ? 0.2363 0.2138 0.1995 -0.0094 0.0040  0.0037  72  TYR   C CE2 
1603 C  CZ  . TYR   B 66  ? 0.2561 0.2296 0.2134 -0.0118 0.0061  0.0052  72  TYR   C CZ  
1604 O  OH  . TYR   B 66  ? 0.2846 0.2528 0.2324 -0.0126 0.0066  0.0058  72  TYR   C OH  
1605 N  N   . PRO   B 67  ? 0.1692 0.1590 0.1588 -0.0123 0.0037  0.0025  73  PRO   C N   
1606 C  CA  . PRO   B 67  ? 0.1781 0.1725 0.1731 -0.0128 0.0038  0.0013  73  PRO   C CA  
1607 C  C   . PRO   B 67  ? 0.1880 0.1883 0.1864 -0.0133 0.0058  0.0008  73  PRO   C C   
1608 O  O   . PRO   B 67  ? 0.2084 0.2089 0.2056 -0.0146 0.0082  0.0014  73  PRO   C O   
1609 C  CB  . PRO   B 67  ? 0.1919 0.1832 0.1862 -0.0153 0.0043  0.0018  73  PRO   C CB  
1610 C  CG  . PRO   B 67  ? 0.2034 0.1907 0.1927 -0.0168 0.0059  0.0035  73  PRO   C CG  
1611 C  CD  . PRO   B 67  ? 0.1948 0.1798 0.1801 -0.0146 0.0049  0.0040  73  PRO   C CD  
1612 N  N   . VAL   B 68  ? 0.1696 0.1744 0.1721 -0.0122 0.0049  -0.0001 74  VAL   C N   
1613 C  CA  . VAL   B 68  ? 0.1764 0.1866 0.1829 -0.0120 0.0061  -0.0006 74  VAL   C CA  
1614 C  C   . VAL   B 68  ? 0.1549 0.1691 0.1656 -0.0123 0.0046  -0.0013 74  VAL   C C   
1615 O  O   . VAL   B 68  ? 0.1770 0.1900 0.1869 -0.0118 0.0028  -0.0017 74  VAL   C O   
1616 C  CB  . VAL   B 68  ? 0.1977 0.2086 0.2036 -0.0097 0.0061  -0.0007 74  VAL   C CB  
1617 C  CG1 . VAL   B 68  ? 0.2183 0.2261 0.2198 -0.0097 0.0079  -0.0003 74  VAL   C CG1 
1618 C  CG2 . VAL   B 68  ? 0.2167 0.2262 0.2218 -0.0079 0.0038  -0.0010 74  VAL   C CG2 
1619 N  N   . SER   B 69  ? 0.1519 0.1712 0.1673 -0.0127 0.0053  -0.0015 75  SER   C N   
1620 C  CA  . SER   B 69  ? 0.1474 0.1708 0.1666 -0.0122 0.0033  -0.0019 75  SER   C CA  
1621 C  C   . SER   B 69  ? 0.1506 0.1751 0.1705 -0.0095 0.0029  -0.0018 75  SER   C C   
1622 O  O   . SER   B 69  ? 0.1557 0.1799 0.1753 -0.0084 0.0047  -0.0017 75  SER   C O   
1623 C  CB  . SER   B 69  ? 0.1911 0.2196 0.2161 -0.0138 0.0038  -0.0023 75  SER   C CB  
1624 O  OG  . SER   B 69  ? 0.2423 0.2695 0.2670 -0.0167 0.0041  -0.0025 75  SER   C OG  
1625 N  N   . PHE   B 70  ? 0.1376 0.1628 0.1576 -0.0086 0.0006  -0.0017 76  PHE   C N   
1626 C  CA  . PHE   B 70  ? 0.1383 0.1638 0.1587 -0.0062 0.0001  -0.0013 76  PHE   C CA  
1627 C  C   . PHE   B 70  ? 0.1391 0.1676 0.1623 -0.0058 -0.0024 -0.0009 76  PHE   C C   
1628 O  O   . PHE   B 70  ? 0.1472 0.1765 0.1702 -0.0073 -0.0041 -0.0010 76  PHE   C O   
1629 C  CB  . PHE   B 70  ? 0.1431 0.1643 0.1590 -0.0053 0.0001  -0.0012 76  PHE   C CB  
1630 C  CG  . PHE   B 70  ? 0.1374 0.1565 0.1506 -0.0062 -0.0011 -0.0014 76  PHE   C CG  
1631 C  CD1 . PHE   B 70  ? 0.1466 0.1632 0.1578 -0.0074 -0.0005 -0.0019 76  PHE   C CD1 
1632 C  CD2 . PHE   B 70  ? 0.1446 0.1637 0.1568 -0.0059 -0.0025 -0.0012 76  PHE   C CD2 
1633 C  CE1 . PHE   B 70  ? 0.1636 0.1783 0.1728 -0.0080 -0.0012 -0.0026 76  PHE   C CE1 
1634 C  CE2 . PHE   B 70  ? 0.1527 0.1699 0.1622 -0.0068 -0.0028 -0.0018 76  PHE   C CE2 
1635 C  CZ  . PHE   B 70  ? 0.1516 0.1669 0.1600 -0.0078 -0.0021 -0.0027 76  PHE   C CZ  
1636 N  N   . SER   B 71  ? 0.1373 0.1669 0.1627 -0.0037 -0.0029 -0.0004 77  SER   C N   
1637 C  CA  . SER   B 71  ? 0.1440 0.1758 0.1719 -0.0029 -0.0058 0.0004  77  SER   C CA  
1638 C  C   . SER   B 71  ? 0.1620 0.1906 0.1849 -0.0031 -0.0078 0.0012  77  SER   C C   
1639 O  O   . SER   B 71  ? 0.1725 0.1977 0.1908 -0.0038 -0.0067 0.0009  77  SER   C O   
1640 C  CB  . SER   B 71  ? 0.1654 0.1991 0.1980 -0.0004 -0.0055 0.0005  77  SER   C CB  
1641 O  OG  . SER   B 71  ? 0.1783 0.2081 0.2078 0.0012  -0.0047 0.0007  77  SER   C OG  
1642 N  N   . LYS   B 72  ? 0.1542 0.1838 0.1778 -0.0026 -0.0107 0.0023  78  LYS   C N   
1643 C  CA  . LYS   B 72  ? 0.1590 0.1852 0.1770 -0.0030 -0.0123 0.0033  78  LYS   C CA  
1644 C  C   . LYS   B 72  ? 0.1643 0.1876 0.1813 -0.0011 -0.0117 0.0042  78  LYS   C C   
1645 O  O   . LYS   B 72  ? 0.2030 0.2276 0.2245 0.0009  -0.0116 0.0044  78  LYS   C O   
1646 C  CB  . LYS   B 72  ? 0.1827 0.2106 0.2010 -0.0033 -0.0163 0.0044  78  LYS   C CB  
1647 C  CG  . LYS   B 72  ? 0.2222 0.2529 0.2417 -0.0055 -0.0172 0.0033  78  LYS   C CG  
1648 C  CD  . LYS   B 72  ? 0.3354 0.3664 0.3527 -0.0064 -0.0215 0.0043  78  LYS   C CD  
1649 C  CE  . LYS   B 72  ? 0.4486 0.4811 0.4651 -0.0091 -0.0224 0.0028  78  LYS   C CE  
1650 N  NZ  . LYS   B 72  ? 0.5337 0.5622 0.5414 -0.0111 -0.0239 0.0029  78  LYS   C NZ  
1651 N  N   . PRO   B 73  ? 0.1684 0.1878 0.1801 -0.0018 -0.0112 0.0047  79  PRO   C N   
1652 C  CA  . PRO   B 73  ? 0.1839 0.2003 0.1950 -0.0004 -0.0106 0.0055  79  PRO   C CA  
1653 C  C   . PRO   B 73  ? 0.1961 0.2124 0.2095 0.0015  -0.0131 0.0072  79  PRO   C C   
1654 O  O   . PRO   B 73  ? 0.2190 0.2353 0.2308 0.0011  -0.0160 0.0086  79  PRO   C O   
1655 C  CB  . PRO   B 73  ? 0.2005 0.2134 0.2058 -0.0021 -0.0098 0.0058  79  PRO   C CB  
1656 C  CG  . PRO   B 73  ? 0.2256 0.2396 0.2290 -0.0040 -0.0090 0.0044  79  PRO   C CG  
1657 C  CD  . PRO   B 73  ? 0.1688 0.1864 0.1752 -0.0040 -0.0107 0.0042  79  PRO   C CD  
1658 N  N   . SER   B 74  ? 0.1811 0.1968 0.1979 0.0036  -0.0122 0.0069  80  SER   C N   
1659 C  CA  . SER   B 74  ? 0.2062 0.2217 0.2264 0.0059  -0.0146 0.0083  80  SER   C CA  
1660 C  C   . SER   B 74  ? 0.1854 0.1979 0.2069 0.0077  -0.0132 0.0079  80  SER   C C   
1661 O  O   . SER   B 74  ? 0.1799 0.1907 0.1995 0.0070  -0.0106 0.0066  80  SER   C O   
1662 C  CB  . SER   B 74  ? 0.2603 0.2813 0.2872 0.0070  -0.0157 0.0076  80  SER   C CB  
1663 O  OG  . SER   B 74  ? 0.2966 0.3199 0.3277 0.0079  -0.0126 0.0055  80  SER   C OG  
1664 N  N   . LEU   B 75  ? 0.1885 0.1999 0.2132 0.0101  -0.0153 0.0091  81  LEU   C N   
1665 C  CA  . LEU   B 75  ? 0.1992 0.2072 0.2256 0.0121  -0.0143 0.0087  81  LEU   C CA  
1666 C  C   . LEU   B 75  ? 0.2048 0.2167 0.2377 0.0140  -0.0123 0.0063  81  LEU   C C   
1667 O  O   . LEU   B 75  ? 0.2226 0.2387 0.2615 0.0157  -0.0137 0.0062  81  LEU   C O   
1668 C  CB  . LEU   B 75  ? 0.2327 0.2377 0.2602 0.0140  -0.0179 0.0111  81  LEU   C CB  
1669 C  CG  . LEU   B 75  ? 0.3105 0.3085 0.3323 0.0133  -0.0190 0.0134  81  LEU   C CG  
1670 C  CD1 . LEU   B 75  ? 0.3392 0.3342 0.3644 0.0163  -0.0222 0.0152  81  LEU   C CD1 
1671 C  CD2 . LEU   B 75  ? 0.3231 0.3175 0.3427 0.0124  -0.0159 0.0121  81  LEU   C CD2 
1672 N  N   . ILE   B 76  ? 0.1907 0.2014 0.2226 0.0139  -0.0091 0.0042  82  ILE   C N   
1673 C  CA  . ILE   B 76  ? 0.2052 0.2189 0.2413 0.0151  -0.0063 0.0016  82  ILE   C CA  
1674 C  C   . ILE   B 76  ? 0.2188 0.2283 0.2546 0.0166  -0.0047 0.0001  82  ILE   C C   
1675 O  O   . ILE   B 76  ? 0.2073 0.2122 0.2382 0.0155  -0.0045 0.0002  82  ILE   C O   
1676 C  CB  . ILE   B 76  ? 0.2353 0.2512 0.2685 0.0127  -0.0040 0.0004  82  ILE   C CB  
1677 C  CG1 . ILE   B 76  ? 0.2714 0.2913 0.3054 0.0111  -0.0056 0.0016  82  ILE   C CG1 
1678 C  CG2 . ILE   B 76  ? 0.2619 0.2796 0.2973 0.0134  -0.0005 -0.0022 82  ILE   C CG2 
1679 C  CD1 . ILE   B 76  ? 0.3136 0.3358 0.3459 0.0090  -0.0039 0.0007  82  ILE   C CD1 
1680 N  N   . PHE   B 77  ? 0.2257 0.2366 0.2670 0.0192  -0.0033 -0.0016 83  PHE   C N   
1681 C  CA  . PHE   B 77  ? 0.2376 0.2442 0.2786 0.0208  -0.0016 -0.0036 83  PHE   C CA  
1682 C  C   . PHE   B 77  ? 0.2307 0.2361 0.2666 0.0190  0.0015  -0.0058 83  PHE   C C   
1683 O  O   . PHE   B 77  ? 0.2501 0.2594 0.2860 0.0179  0.0036  -0.0069 83  PHE   C O   
1684 C  CB  . PHE   B 77  ? 0.2756 0.2848 0.3246 0.0242  -0.0005 -0.0053 83  PHE   C CB  
1685 C  CG  . PHE   B 77  ? 0.3055 0.3100 0.3542 0.0259  0.0018  -0.0080 83  PHE   C CG  
1686 C  CD1 . PHE   B 77  ? 0.3415 0.3468 0.3887 0.0255  0.0059  -0.0112 83  PHE   C CD1 
1687 C  CD2 . PHE   B 77  ? 0.3349 0.3334 0.3833 0.0275  -0.0003 -0.0072 83  PHE   C CD2 
1688 C  CE1 . PHE   B 77  ? 0.3617 0.3622 0.4075 0.0269  0.0080  -0.0140 83  PHE   C CE1 
1689 C  CE2 . PHE   B 77  ? 0.3651 0.3588 0.4130 0.0289  0.0018  -0.0099 83  PHE   C CE2 
1690 C  CZ  . PHE   B 77  ? 0.3654 0.3602 0.4118 0.0286  0.0059  -0.0134 83  PHE   C CZ  
1691 N  N   . VAL   B 78  ? 0.2262 0.2260 0.2575 0.0184  0.0015  -0.0063 84  VAL   C N   
1692 C  CA  . VAL   B 78  ? 0.2275 0.2254 0.2535 0.0167  0.0035  -0.0084 84  VAL   C CA  
1693 C  C   . VAL   B 78  ? 0.2396 0.2327 0.2652 0.0183  0.0048  -0.0109 84  VAL   C C   
1694 O  O   . VAL   B 78  ? 0.2342 0.2230 0.2602 0.0191  0.0031  -0.0103 84  VAL   C O   
1695 C  CB  . VAL   B 78  ? 0.2059 0.2017 0.2270 0.0141  0.0018  -0.0069 84  VAL   C CB  
1696 C  CG1 . VAL   B 78  ? 0.2118 0.2057 0.2278 0.0126  0.0030  -0.0089 84  VAL   C CG1 
1697 C  CG2 . VAL   B 78  ? 0.2008 0.2009 0.2223 0.0127  0.0007  -0.0048 84  VAL   C CG2 
1698 N  N   . GLU   B 79  ? 0.2622 0.2554 0.2858 0.0184  0.0079  -0.0138 85  GLU   C N   
1699 C  CA  . GLU   B 79  ? 0.2820 0.2705 0.3043 0.0197  0.0094  -0.0167 85  GLU   C CA  
1700 C  C   . GLU   B 79  ? 0.2715 0.2542 0.2886 0.0181  0.0076  -0.0169 85  GLU   C C   
1701 O  O   . GLU   B 79  ? 0.2614 0.2444 0.2750 0.0157  0.0060  -0.0154 85  GLU   C O   
1702 C  CB  . GLU   B 79  ? 0.3412 0.3308 0.3605 0.0194  0.0133  -0.0197 85  GLU   C CB  
1703 C  CG  . GLU   B 79  ? 0.3905 0.3863 0.4152 0.0204  0.0159  -0.0200 85  GLU   C CG  
1704 C  CD  . GLU   B 79  ? 0.4703 0.4669 0.5017 0.0237  0.0184  -0.0225 85  GLU   C CD  
1705 O  OE1 . GLU   B 79  ? 0.4675 0.4700 0.5051 0.0247  0.0204  -0.0227 85  GLU   C OE1 
1706 O  OE2 . GLU   B 79  ? 0.5135 0.5048 0.5446 0.0253  0.0182  -0.0242 85  GLU   C OE2 
1707 N  N   . ALA   B 80  ? 0.2701 0.2475 0.2870 0.0194  0.0079  -0.0190 86  ALA   C N   
1708 C  CA  . ALA   B 80  ? 0.2741 0.2458 0.2867 0.0177  0.0061  -0.0196 86  ALA   C CA  
1709 C  C   . ALA   B 80  ? 0.2558 0.2271 0.2617 0.0152  0.0065  -0.0211 86  ALA   C C   
1710 O  O   . ALA   B 80  ? 0.2705 0.2436 0.2737 0.0153  0.0089  -0.0228 86  ALA   C O   
1711 C  CB  . ALA   B 80  ? 0.2961 0.2618 0.3097 0.0196  0.0069  -0.0223 86  ALA   C CB  
1712 N  N   . SER   B 81  ? 0.2284 0.1975 0.2318 0.0130  0.0039  -0.0204 87  SER   C N   
1713 C  CA  . SER   B 81  ? 0.2192 0.1870 0.2164 0.0107  0.0031  -0.0217 87  SER   C CA  
1714 C  C   . SER   B 81  ? 0.2335 0.1961 0.2296 0.0093  0.0008  -0.0228 87  SER   C C   
1715 O  O   . SER   B 81  ? 0.2498 0.2097 0.2495 0.0101  0.0005  -0.0224 87  SER   C O   
1716 C  CB  . SER   B 81  ? 0.2271 0.1996 0.2241 0.0090  0.0018  -0.0192 87  SER   C CB  
1717 O  OG  . SER   B 81  ? 0.2206 0.1938 0.2212 0.0081  -0.0003 -0.0168 87  SER   C OG  
1718 N  N   . GLU   B 82  ? 0.2389 0.2002 0.2305 0.0072  -0.0010 -0.0240 88  GLU   C N   
1719 C  CA  . GLU   B 82  ? 0.2439 0.2010 0.2354 0.0054  -0.0034 -0.0251 88  GLU   C CA  
1720 C  C   . GLU   B 82  ? 0.2536 0.2129 0.2503 0.0040  -0.0051 -0.0220 88  GLU   C C   
1721 O  O   . GLU   B 82  ? 0.2600 0.2160 0.2585 0.0026  -0.0064 -0.0224 88  GLU   C O   
1722 C  CB  . GLU   B 82  ? 0.3044 0.2601 0.2903 0.0034  -0.0055 -0.0270 88  GLU   C CB  
1723 C  CG  . GLU   B 82  ? 0.3762 0.3368 0.3612 0.0025  -0.0068 -0.0250 88  GLU   C CG  
1724 C  CD  . GLU   B 82  ? 0.4801 0.4421 0.4598 0.0033  -0.0051 -0.0252 88  GLU   C CD  
1725 O  OE1 . GLU   B 82  ? 0.5321 0.4935 0.5068 0.0020  -0.0072 -0.0256 88  GLU   C OE1 
1726 O  OE2 . GLU   B 82  ? 0.4339 0.3977 0.4148 0.0050  -0.0018 -0.0248 88  GLU   C OE2 
1727 N  N   . TYR   B 83  ? 0.2474 0.2120 0.2466 0.0043  -0.0046 -0.0192 89  TYR   C N   
1728 C  CA  . TYR   B 83  ? 0.2499 0.2168 0.2531 0.0029  -0.0056 -0.0165 89  TYR   C CA  
1729 C  C   . TYR   B 83  ? 0.2460 0.2121 0.2524 0.0039  -0.0047 -0.0143 89  TYR   C C   
1730 O  O   . TYR   B 83  ? 0.2781 0.2439 0.2867 0.0023  -0.0053 -0.0125 89  TYR   C O   
1731 C  CB  . TYR   B 83  ? 0.2377 0.2102 0.2408 0.0024  -0.0058 -0.0150 89  TYR   C CB  
1732 C  CG  . TYR   B 83  ? 0.2349 0.2079 0.2346 0.0015  -0.0073 -0.0166 89  TYR   C CG  
1733 C  CD1 . TYR   B 83  ? 0.2785 0.2508 0.2789 -0.0005 -0.0098 -0.0175 89  TYR   C CD1 
1734 C  CD2 . TYR   B 83  ? 0.2440 0.2178 0.2396 0.0026  -0.0063 -0.0172 89  TYR   C CD2 
1735 C  CE1 . TYR   B 83  ? 0.2974 0.2698 0.2944 -0.0011 -0.0119 -0.0188 89  TYR   C CE1 
1736 C  CE2 . TYR   B 83  ? 0.2756 0.2490 0.2668 0.0017  -0.0080 -0.0183 89  TYR   C CE2 
1737 C  CZ  . TYR   B 83  ? 0.3148 0.2875 0.3068 0.0000  -0.0111 -0.0190 89  TYR   C CZ  
1738 O  OH  . TYR   B 83  ? 0.3663 0.3382 0.3539 -0.0007 -0.0136 -0.0198 89  TYR   C OH  
1739 N  N   . TYR   B 84  ? 0.2326 0.1990 0.2394 0.0066  -0.0032 -0.0142 90  TYR   C N   
1740 C  CA  . TYR   B 84  ? 0.2508 0.2169 0.2608 0.0080  -0.0029 -0.0118 90  TYR   C CA  
1741 C  C   . TYR   B 84  ? 0.2853 0.2491 0.2965 0.0110  -0.0017 -0.0133 90  TYR   C C   
1742 O  O   . TYR   B 84  ? 0.2744 0.2395 0.2843 0.0123  -0.0001 -0.0156 90  TYR   C O   
1743 C  CB  . TYR   B 84  ? 0.2344 0.2063 0.2457 0.0084  -0.0027 -0.0093 90  TYR   C CB  
1744 C  CG  . TYR   B 84  ? 0.2161 0.1911 0.2269 0.0058  -0.0034 -0.0078 90  TYR   C CG  
1745 C  CD1 . TYR   B 84  ? 0.2031 0.1821 0.2125 0.0052  -0.0032 -0.0084 90  TYR   C CD1 
1746 C  CD2 . TYR   B 84  ? 0.2143 0.1878 0.2259 0.0040  -0.0041 -0.0057 90  TYR   C CD2 
1747 C  CE1 . TYR   B 84  ? 0.2046 0.1863 0.2143 0.0033  -0.0038 -0.0073 90  TYR   C CE1 
1748 C  CE2 . TYR   B 84  ? 0.2124 0.1892 0.2241 0.0018  -0.0042 -0.0048 90  TYR   C CE2 
1749 C  CZ  . TYR   B 84  ? 0.2095 0.1905 0.2207 0.0017  -0.0041 -0.0056 90  TYR   C CZ  
1750 O  OH  . TYR   B 84  ? 0.1965 0.1803 0.2085 -0.0003 -0.0041 -0.0051 90  TYR   C OH  
1751 N  N   . PRO   B 85  ? 0.3271 0.2875 0.3411 0.0124  -0.0023 -0.0117 91  PRO   C N   
1752 C  CA  . PRO   B 85  ? 0.3231 0.2825 0.3399 0.0159  -0.0013 -0.0128 91  PRO   C CA  
1753 C  C   . PRO   B 85  ? 0.3045 0.2707 0.3241 0.0176  -0.0005 -0.0116 91  PRO   C C   
1754 O  O   . PRO   B 85  ? 0.2839 0.2543 0.3029 0.0160  -0.0013 -0.0093 91  PRO   C O   
1755 C  CB  . PRO   B 85  ? 0.3475 0.3017 0.3667 0.0166  -0.0030 -0.0105 91  PRO   C CB  
1756 C  CG  . PRO   B 85  ? 0.3597 0.3148 0.3773 0.0137  -0.0044 -0.0072 91  PRO   C CG  
1757 C  CD  . PRO   B 85  ? 0.3422 0.3002 0.3569 0.0108  -0.0039 -0.0086 91  PRO   C CD  
1758 N  N   . ALA   B 86  ? 0.3061 0.2734 0.3292 0.0207  0.0010  -0.0132 92  ALA   C N   
1759 C  CA  . ALA   B 86  ? 0.3087 0.2826 0.3360 0.0223  0.0015  -0.0121 92  ALA   C CA  
1760 C  C   . ALA   B 86  ? 0.2992 0.2734 0.3286 0.0223  -0.0016 -0.0079 92  ALA   C C   
1761 O  O   . ALA   B 86  ? 0.3194 0.2882 0.3494 0.0230  -0.0034 -0.0065 92  ALA   C O   
1762 C  CB  . ALA   B 86  ? 0.3283 0.3029 0.3607 0.0258  0.0036  -0.0146 92  ALA   C CB  
1763 N  N   . ARG   B 87  ? 0.2705 0.2501 0.2996 0.0209  -0.0023 -0.0058 93  ARG   C N   
1764 C  CA  . ARG   B 87  ? 0.2656 0.2450 0.2947 0.0202  -0.0051 -0.0021 93  ARG   C CA  
1765 C  C   . ARG   B 87  ? 0.2570 0.2431 0.2870 0.0196  -0.0055 -0.0008 93  ARG   C C   
1766 O  O   . ARG   B 87  ? 0.2612 0.2516 0.2914 0.0191  -0.0034 -0.0026 93  ARG   C O   
1767 C  CB  . ARG   B 87  ? 0.2685 0.2439 0.2923 0.0170  -0.0058 -0.0008 93  ARG   C CB  
1768 C  CG  . ARG   B 87  ? 0.2235 0.2030 0.2441 0.0141  -0.0046 -0.0014 93  ARG   C CG  
1769 C  CD  . ARG   B 87  ? 0.2276 0.2038 0.2447 0.0115  -0.0044 -0.0019 93  ARG   C CD  
1770 N  NE  . ARG   B 87  ? 0.2161 0.1955 0.2310 0.0088  -0.0043 -0.0011 93  ARG   C NE  
1771 C  CZ  . ARG   B 87  ? 0.2254 0.2091 0.2396 0.0081  -0.0034 -0.0023 93  ARG   C CZ  
1772 N  NH1 . ARG   B 87  ? 0.2062 0.1921 0.2190 0.0059  -0.0035 -0.0016 93  ARG   C NH1 
1773 N  NH2 . ARG   B 87  ? 0.2207 0.2060 0.2354 0.0097  -0.0023 -0.0044 93  ARG   C NH2 
1774 N  N   . TYR   B 88  ? 0.2560 0.2422 0.2856 0.0191  -0.0082 0.0025  94  TYR   C N   
1775 C  CA  . TYR   B 88  ? 0.2570 0.2489 0.2864 0.0178  -0.0087 0.0036  94  TYR   C CA  
1776 C  C   . TYR   B 88  ? 0.2238 0.2147 0.2473 0.0143  -0.0083 0.0044  94  TYR   C C   
1777 O  O   . TYR   B 88  ? 0.2329 0.2192 0.2531 0.0129  -0.0092 0.0061  94  TYR   C O   
1778 C  CB  . TYR   B 88  ? 0.2833 0.2755 0.3144 0.0188  -0.0122 0.0066  94  TYR   C CB  
1779 C  CG  . TYR   B 88  ? 0.3339 0.3290 0.3726 0.0224  -0.0130 0.0058  94  TYR   C CG  
1780 C  CD1 . TYR   B 88  ? 0.3578 0.3600 0.4010 0.0228  -0.0124 0.0047  94  TYR   C CD1 
1781 C  CD2 . TYR   B 88  ? 0.3890 0.3798 0.4311 0.0254  -0.0141 0.0059  94  TYR   C CD2 
1782 C  CE1 . TYR   B 88  ? 0.4041 0.4099 0.4557 0.0261  -0.0129 0.0037  94  TYR   C CE1 
1783 C  CE2 . TYR   B 88  ? 0.4104 0.4043 0.4608 0.0290  -0.0147 0.0048  94  TYR   C CE2 
1784 C  CZ  . TYR   B 88  ? 0.4353 0.4371 0.4907 0.0293  -0.0138 0.0036  94  TYR   C CZ  
1785 O  OH  . TYR   B 88  ? 0.4866 0.4924 0.5515 0.0329  -0.0144 0.0024  94  TYR   C OH  
1786 N  N   . GLN   B 89  ? 0.1922 0.1872 0.2148 0.0128  -0.0067 0.0030  95  GLN   C N   
1787 C  CA  . GLN   B 89  ? 0.1811 0.1761 0.1993 0.0098  -0.0063 0.0035  95  GLN   C CA  
1788 C  C   . GLN   B 89  ? 0.1707 0.1687 0.1881 0.0089  -0.0077 0.0054  95  GLN   C C   
1789 O  O   . GLN   B 89  ? 0.1877 0.1900 0.2080 0.0098  -0.0080 0.0051  95  GLN   C O   
1790 C  CB  . GLN   B 89  ? 0.1881 0.1849 0.2055 0.0090  -0.0042 0.0011  95  GLN   C CB  
1791 C  CG  . GLN   B 89  ? 0.1815 0.1789 0.1957 0.0063  -0.0040 0.0014  95  GLN   C CG  
1792 C  CD  . GLN   B 89  ? 0.1767 0.1741 0.1898 0.0057  -0.0027 -0.0007 95  GLN   C CD  
1793 O  OE1 . GLN   B 89  ? 0.1882 0.1831 0.2011 0.0063  -0.0023 -0.0022 95  GLN   C OE1 
1794 N  NE2 . GLN   B 89  ? 0.1636 0.1634 0.1755 0.0043  -0.0024 -0.0009 95  GLN   C NE2 
1795 N  N   . SER   B 90  ? 0.1689 0.1648 0.1824 0.0068  -0.0083 0.0071  96  SER   C N   
1796 C  CA  . SER   B 90  ? 0.1628 0.1605 0.1740 0.0055  -0.0096 0.0087  96  SER   C CA  
1797 C  C   . SER   B 90  ? 0.1582 0.1587 0.1677 0.0034  -0.0080 0.0074  96  SER   C C   
1798 O  O   . SER   B 90  ? 0.1697 0.1702 0.1793 0.0028  -0.0061 0.0057  96  SER   C O   
1799 C  CB  . SER   B 90  ? 0.1974 0.1906 0.2043 0.0043  -0.0110 0.0113  96  SER   C CB  
1800 O  OG  . SER   B 90  ? 0.2240 0.2147 0.2283 0.0021  -0.0089 0.0108  96  SER   C OG  
1801 N  N   . HIS   B 91  ? 0.1707 0.1738 0.1790 0.0026  -0.0090 0.0080  97  HIS   C N   
1802 C  CA  . HIS   B 91  ? 0.1643 0.1696 0.1708 0.0006  -0.0077 0.0068  97  HIS   C CA  
1803 C  C   . HIS   B 91  ? 0.1679 0.1758 0.1774 0.0012  -0.0061 0.0047  97  HIS   C C   
1804 O  O   . HIS   B 91  ? 0.1601 0.1683 0.1685 0.0001  -0.0047 0.0035  97  HIS   C O   
1805 C  CB  . HIS   B 91  ? 0.1736 0.1762 0.1764 -0.0015 -0.0062 0.0069  97  HIS   C CB  
1806 C  CG  . HIS   B 91  ? 0.1849 0.1843 0.1831 -0.0027 -0.0072 0.0091  97  HIS   C CG  
1807 N  ND1 . HIS   B 91  ? 0.2161 0.2158 0.2100 -0.0045 -0.0075 0.0096  97  HIS   C ND1 
1808 C  CD2 . HIS   B 91  ? 0.2087 0.2041 0.2055 -0.0024 -0.0081 0.0110  97  HIS   C CD2 
1809 C  CE1 . HIS   B 91  ? 0.2212 0.2170 0.2105 -0.0054 -0.0085 0.0119  97  HIS   C CE1 
1810 N  NE2 . HIS   B 91  ? 0.2323 0.2253 0.2233 -0.0042 -0.0089 0.0130  97  HIS   C NE2 
1811 N  N   . LEU   B 92  ? 0.1648 0.1744 0.1780 0.0031  -0.0064 0.0043  98  LEU   C N   
1812 C  CA  . LEU   B 92  ? 0.1615 0.1729 0.1765 0.0035  -0.0046 0.0025  98  LEU   C CA  
1813 C  C   . LEU   B 92  ? 0.1707 0.1860 0.1877 0.0031  -0.0048 0.0022  98  LEU   C C   
1814 O  O   . LEU   B 92  ? 0.1736 0.1910 0.1931 0.0037  -0.0064 0.0031  98  LEU   C O   
1815 C  CB  . LEU   B 92  ? 0.1735 0.1838 0.1909 0.0055  -0.0040 0.0017  98  LEU   C CB  
1816 C  CG  . LEU   B 92  ? 0.1880 0.1988 0.2057 0.0058  -0.0019 -0.0001 98  LEU   C CG  
1817 C  CD1 . LEU   B 92  ? 0.1941 0.2026 0.2083 0.0045  -0.0013 -0.0008 98  LEU   C CD1 
1818 C  CD2 . LEU   B 92  ? 0.2450 0.2545 0.2647 0.0079  -0.0010 -0.0012 98  LEU   C CD2 
1819 N  N   . MET   B 93  ? 0.1615 0.1776 0.1777 0.0020  -0.0033 0.0011  99  MET   C N   
1820 C  CA  . MET   B 93  ? 0.1496 0.1690 0.1677 0.0012  -0.0031 0.0007  99  MET   C CA  
1821 C  C   . MET   B 93  ? 0.1575 0.1774 0.1766 0.0015  -0.0009 -0.0004 99  MET   C C   
1822 O  O   . MET   B 93  ? 0.1756 0.1928 0.1918 0.0014  0.0001  -0.0010 99  MET   C O   
1823 C  CB  . MET   B 93  ? 0.1549 0.1736 0.1700 -0.0008 -0.0032 0.0006  99  MET   C CB  
1824 C  CG  . MET   B 93  ? 0.1777 0.1955 0.1906 -0.0015 -0.0048 0.0015  99  MET   C CG  
1825 S  SD  . MET   B 93  ? 0.1935 0.2098 0.2027 -0.0035 -0.0042 0.0006  99  MET   C SD  
1826 C  CE  . MET   B 93  ? 0.1857 0.1993 0.1942 -0.0029 -0.0025 -0.0002 99  MET   C CE  
1827 N  N   . LEU   B 94  ? 0.1478 0.1712 0.1709 0.0017  -0.0001 -0.0008 100 LEU   C N   
1828 C  CA  . LEU   B 94  ? 0.1390 0.1627 0.1624 0.0016  0.0026  -0.0019 100 LEU   C CA  
1829 C  C   . LEU   B 94  ? 0.1384 0.1633 0.1612 -0.0006 0.0037  -0.0020 100 LEU   C C   
1830 O  O   . LEU   B 94  ? 0.1458 0.1732 0.1708 -0.0018 0.0024  -0.0016 100 LEU   C O   
1831 C  CB  . LEU   B 94  ? 0.1685 0.1955 0.1975 0.0033  0.0038  -0.0026 100 LEU   C CB  
1832 C  CG  . LEU   B 94  ? 0.1716 0.1968 0.2015 0.0057  0.0030  -0.0026 100 LEU   C CG  
1833 C  CD1 . LEU   B 94  ? 0.1934 0.2219 0.2297 0.0076  0.0045  -0.0038 100 LEU   C CD1 
1834 C  CD2 . LEU   B 94  ? 0.1991 0.2193 0.2236 0.0059  0.0037  -0.0032 100 LEU   C CD2 
1835 N  N   . ALA   B 95  ? 0.1450 0.1678 0.1647 -0.0013 0.0060  -0.0026 101 ALA   C N   
1836 C  CA  . ALA   B 95  ? 0.1390 0.1622 0.1579 -0.0036 0.0076  -0.0026 101 ALA   C CA  
1837 C  C   . ALA   B 95  ? 0.1437 0.1665 0.1615 -0.0037 0.0109  -0.0034 101 ALA   C C   
1838 O  O   . ALA   B 95  ? 0.1606 0.1815 0.1765 -0.0021 0.0117  -0.0041 101 ALA   C O   
1839 C  CB  . ALA   B 95  ? 0.1556 0.1743 0.1690 -0.0047 0.0065  -0.0020 101 ALA   C CB  
1840 N  N   . VAL   B 96  ? 0.1427 0.1669 0.1613 -0.0058 0.0131  -0.0034 102 VAL   C N   
1841 C  CA  . VAL   B 96  ? 0.1500 0.1728 0.1657 -0.0067 0.0169  -0.0040 102 VAL   C CA  
1842 C  C   . VAL   B 96  ? 0.1786 0.1949 0.1856 -0.0078 0.0165  -0.0031 102 VAL   C C   
1843 O  O   . VAL   B 96  ? 0.1951 0.2093 0.2000 -0.0096 0.0156  -0.0020 102 VAL   C O   
1844 C  CB  . VAL   B 96  ? 0.1694 0.1966 0.1901 -0.0089 0.0197  -0.0044 102 VAL   C CB  
1845 C  CG1 . VAL   B 96  ? 0.1754 0.2009 0.1922 -0.0101 0.0244  -0.0051 102 VAL   C CG1 
1846 C  CG2 . VAL   B 96  ? 0.1851 0.2193 0.2155 -0.0074 0.0192  -0.0053 102 VAL   C CG2 
1847 N  N   . GLY   B 97  ? 0.1764 0.1890 0.1783 -0.0065 0.0168  -0.0036 103 GLY   C N   
1848 C  CA  . GLY   B 97  ? 0.2028 0.2091 0.1965 -0.0073 0.0156  -0.0027 103 GLY   C CA  
1849 C  C   . GLY   B 97  ? 0.2110 0.2139 0.1997 -0.0060 0.0157  -0.0036 103 GLY   C C   
1850 O  O   . GLY   B 97  ? 0.2140 0.2189 0.2057 -0.0042 0.0163  -0.0050 103 GLY   C O   
1851 N  N   . HIS   B 98  ? 0.1971 0.1941 0.1775 -0.0070 0.0150  -0.0028 104 HIS   C N   
1852 C  CA  . HIS   B 98  ? 0.2012 0.1943 0.1756 -0.0062 0.0146  -0.0037 104 HIS   C CA  
1853 C  C   . HIS   B 98  ? 0.1992 0.1914 0.1750 -0.0042 0.0105  -0.0039 104 HIS   C C   
1854 O  O   . HIS   B 98  ? 0.1874 0.1794 0.1649 -0.0041 0.0075  -0.0029 104 HIS   C O   
1855 C  CB  . HIS   B 98  ? 0.2171 0.2036 0.1815 -0.0080 0.0145  -0.0024 104 HIS   C CB  
1856 C  CG  . HIS   B 98  ? 0.2279 0.2098 0.1851 -0.0074 0.0134  -0.0034 104 HIS   C CG  
1857 N  ND1 . HIS   B 98  ? 0.2656 0.2476 0.2205 -0.0073 0.0170  -0.0055 104 HIS   C ND1 
1858 C  CD2 . HIS   B 98  ? 0.2478 0.2252 0.2003 -0.0067 0.0091  -0.0029 104 HIS   C CD2 
1859 C  CE1 . HIS   B 98  ? 0.2791 0.2562 0.2270 -0.0069 0.0148  -0.0062 104 HIS   C CE1 
1860 N  NE2 . HIS   B 98  ? 0.2751 0.2495 0.2216 -0.0065 0.0098  -0.0046 104 HIS   C NE2 
1861 N  N   . SER   B 99  ? 0.1972 0.1884 0.1717 -0.0030 0.0106  -0.0055 105 SER   C N   
1862 C  CA  . SER   B 99  ? 0.2014 0.1912 0.1763 -0.0017 0.0071  -0.0060 105 SER   C CA  
1863 C  C   . SER   B 99  ? 0.2114 0.1982 0.1817 -0.0011 0.0078  -0.0079 105 SER   C C   
1864 O  O   . SER   B 99  ? 0.2194 0.2068 0.1890 -0.0011 0.0115  -0.0094 105 SER   C O   
1865 C  CB  . SER   B 99  ? 0.1972 0.1913 0.1803 -0.0004 0.0059  -0.0059 105 SER   C CB  
1866 O  OG  . SER   B 99  ? 0.2087 0.2055 0.1957 0.0007  0.0082  -0.0071 105 SER   C OG  
1867 N  N   . GLU   B 100 ? 0.2184 0.2022 0.1864 -0.0007 0.0043  -0.0083 106 GLU   C N   
1868 C  CA  . GLU   B 100 ? 0.2316 0.2121 0.1956 -0.0002 0.0038  -0.0103 106 GLU   C CA  
1869 C  C   . GLU   B 100 ? 0.2215 0.2032 0.1911 0.0008  0.0006  -0.0106 106 GLU   C C   
1870 O  O   . GLU   B 100 ? 0.2125 0.1967 0.1870 0.0009  -0.0014 -0.0092 106 GLU   C O   
1871 C  CB  . GLU   B 100 ? 0.2632 0.2380 0.2173 -0.0015 0.0019  -0.0102 106 GLU   C CB  
1872 C  CG  . GLU   B 100 ? 0.2868 0.2599 0.2347 -0.0030 0.0055  -0.0096 106 GLU   C CG  
1873 C  CD  . GLU   B 100 ? 0.3403 0.3068 0.2768 -0.0045 0.0038  -0.0088 106 GLU   C CD  
1874 O  OE1 . GLU   B 100 ? 0.3976 0.3604 0.3296 -0.0043 0.0003  -0.0098 106 GLU   C OE1 
1875 O  OE2 . GLU   B 100 ? 0.3339 0.2989 0.2661 -0.0060 0.0055  -0.0071 106 GLU   C OE2 
1876 N  N   . PRO   B 101 ? 0.2305 0.2103 0.1995 0.0014  0.0002  -0.0126 107 PRO   C N   
1877 C  CA  . PRO   B 101 ? 0.2234 0.2042 0.1980 0.0019  -0.0023 -0.0128 107 PRO   C CA  
1878 C  C   . PRO   B 101 ? 0.2131 0.1940 0.1890 0.0013  -0.0063 -0.0117 107 PRO   C C   
1879 O  O   . PRO   B 101 ? 0.2067 0.1907 0.1891 0.0015  -0.0073 -0.0110 107 PRO   C O   
1880 C  CB  . PRO   B 101 ? 0.2405 0.2176 0.2120 0.0022  -0.0023 -0.0154 107 PRO   C CB  
1881 C  CG  . PRO   B 101 ? 0.2543 0.2307 0.2223 0.0026  0.0019  -0.0166 107 PRO   C CG  
1882 C  CD  . PRO   B 101 ? 0.2437 0.2204 0.2075 0.0015  0.0028  -0.0150 107 PRO   C CD  
1883 N  N   . GLY   B 102 ? 0.2178 0.1955 0.1877 0.0006  -0.0087 -0.0116 108 GLY   C N   
1884 C  CA  . GLY   B 102 ? 0.2228 0.2008 0.1946 0.0003  -0.0128 -0.0107 108 GLY   C CA  
1885 C  C   . GLY   B 102 ? 0.2142 0.1952 0.1903 0.0005  -0.0126 -0.0087 108 GLY   C C   
1886 O  O   . GLY   B 102 ? 0.2142 0.1962 0.1938 0.0007  -0.0156 -0.0081 108 GLY   C O   
1887 N  N   . ASP   B 103 ? 0.1947 0.1775 0.1711 0.0005  -0.0091 -0.0078 109 ASP   C N   
1888 C  CA  . ASP   B 103 ? 0.1858 0.1715 0.1663 0.0005  -0.0086 -0.0062 109 ASP   C CA  
1889 C  C   . ASP   B 103 ? 0.1676 0.1574 0.1558 0.0010  -0.0082 -0.0063 109 ASP   C C   
1890 O  O   . ASP   B 103 ? 0.1743 0.1662 0.1659 0.0009  -0.0083 -0.0054 109 ASP   C O   
1891 C  CB  . ASP   B 103 ? 0.1779 0.1641 0.1562 0.0000  -0.0052 -0.0054 109 ASP   C CB  
1892 C  CG  . ASP   B 103 ? 0.2314 0.2132 0.2016 -0.0009 -0.0053 -0.0047 109 ASP   C CG  
1893 O  OD1 . ASP   B 103 ? 0.2287 0.2074 0.1961 -0.0010 -0.0087 -0.0040 109 ASP   C OD1 
1894 O  OD2 . ASP   B 103 ? 0.2198 0.2010 0.1864 -0.0016 -0.0021 -0.0049 109 ASP   C OD2 
1895 N  N   . CYS   B 104 ? 0.1621 0.1525 0.1526 0.0013  -0.0079 -0.0074 110 CYS   C N   
1896 C  CA  . CYS   B 104 ? 0.1638 0.1572 0.1604 0.0013  -0.0075 -0.0072 110 CYS   C CA  
1897 C  C   . CYS   B 104 ? 0.1829 0.1775 0.1831 0.0010  -0.0096 -0.0071 110 CYS   C C   
1898 O  O   . CYS   B 104 ? 0.1835 0.1765 0.1830 0.0010  -0.0123 -0.0078 110 CYS   C O   
1899 C  CB  . CYS   B 104 ? 0.1672 0.1597 0.1649 0.0015  -0.0073 -0.0083 110 CYS   C CB  
1900 S  SG  . CYS   B 104 ? 0.1964 0.1887 0.1930 0.0024  -0.0043 -0.0085 110 CYS   C SG  
1901 N  N   . GLY   B 105 ? 0.1689 0.1663 0.1729 0.0009  -0.0085 -0.0064 111 GLY   C N   
1902 C  CA  . GLY   B 105 ? 0.1753 0.1743 0.1835 0.0007  -0.0097 -0.0067 111 GLY   C CA  
1903 C  C   . GLY   B 105 ? 0.1678 0.1669 0.1755 0.0010  -0.0098 -0.0060 111 GLY   C C   
1904 O  O   . GLY   B 105 ? 0.1743 0.1751 0.1861 0.0010  -0.0101 -0.0063 111 GLY   C O   
1905 N  N   . GLY   B 106 ? 0.1594 0.1565 0.1623 0.0010  -0.0095 -0.0052 112 GLY   C N   
1906 C  CA  . GLY   B 106 ? 0.1627 0.1591 0.1647 0.0010  -0.0095 -0.0044 112 GLY   C CA  
1907 C  C   . GLY   B 106 ? 0.1597 0.1589 0.1647 0.0006  -0.0074 -0.0043 112 GLY   C C   
1908 O  O   . GLY   B 106 ? 0.1643 0.1654 0.1697 0.0002  -0.0056 -0.0042 112 GLY   C O   
1909 N  N   . ILE   B 107 ? 0.1580 0.1574 0.1653 0.0007  -0.0078 -0.0045 113 ILE   C N   
1910 C  CA  . ILE   B 107 ? 0.1608 0.1624 0.1703 0.0001  -0.0059 -0.0048 113 ILE   C CA  
1911 C  C   . ILE   B 107 ? 0.1561 0.1573 0.1629 -0.0007 -0.0047 -0.0039 113 ILE   C C   
1912 O  O   . ILE   B 107 ? 0.1662 0.1647 0.1703 -0.0008 -0.0053 -0.0032 113 ILE   C O   
1913 C  CB  . ILE   B 107 ? 0.2055 0.2074 0.2190 0.0006  -0.0065 -0.0059 113 ILE   C CB  
1914 C  CG1 . ILE   B 107 ? 0.2388 0.2430 0.2566 0.0007  -0.0065 -0.0070 113 ILE   C CG1 
1915 C  CG2 . ILE   B 107 ? 0.2343 0.2371 0.2484 -0.0002 -0.0046 -0.0064 113 ILE   C CG2 
1916 C  CD1 . ILE   B 107 ? 0.2711 0.2764 0.2947 0.0015  -0.0068 -0.0086 113 ILE   C CD1 
1917 N  N   . LEU   B 108 ? 0.1437 0.1472 0.1511 -0.0015 -0.0032 -0.0040 114 LEU   C N   
1918 C  CA  . LEU   B 108 ? 0.1421 0.1462 0.1485 -0.0025 -0.0022 -0.0035 114 LEU   C CA  
1919 C  C   . LEU   B 108 ? 0.1457 0.1502 0.1536 -0.0030 -0.0019 -0.0046 114 LEU   C C   
1920 O  O   . LEU   B 108 ? 0.1543 0.1603 0.1636 -0.0031 -0.0013 -0.0052 114 LEU   C O   
1921 C  CB  . LEU   B 108 ? 0.1464 0.1530 0.1528 -0.0029 -0.0014 -0.0030 114 LEU   C CB  
1922 C  CG  . LEU   B 108 ? 0.1505 0.1587 0.1570 -0.0041 -0.0008 -0.0028 114 LEU   C CG  
1923 C  CD1 . LEU   B 108 ? 0.1755 0.1826 0.1808 -0.0048 -0.0004 -0.0023 114 LEU   C CD1 
1924 C  CD2 . LEU   B 108 ? 0.1712 0.1821 0.1788 -0.0039 -0.0007 -0.0022 114 LEU   C CD2 
1925 N  N   . ARG   B 109 ? 0.1520 0.1547 0.1592 -0.0036 -0.0019 -0.0048 115 ARG   C N   
1926 C  CA  . ARG   B 109 ? 0.1610 0.1634 0.1693 -0.0041 -0.0014 -0.0062 115 ARG   C CA  
1927 C  C   . ARG   B 109 ? 0.1687 0.1709 0.1755 -0.0057 -0.0010 -0.0061 115 ARG   C C   
1928 O  O   . ARG   B 109 ? 0.1840 0.1850 0.1896 -0.0063 -0.0012 -0.0051 115 ARG   C O   
1929 C  CB  . ARG   B 109 ? 0.2028 0.2022 0.2127 -0.0029 -0.0024 -0.0068 115 ARG   C CB  
1930 C  CG  . ARG   B 109 ? 0.3138 0.3140 0.3271 -0.0014 -0.0028 -0.0078 115 ARG   C CG  
1931 C  CD  . ARG   B 109 ? 0.3716 0.3688 0.3873 0.0000  -0.0044 -0.0084 115 ARG   C CD  
1932 N  NE  . ARG   B 109 ? 0.4117 0.4078 0.4288 -0.0002 -0.0033 -0.0101 115 ARG   C NE  
1933 C  CZ  . ARG   B 109 ? 0.4316 0.4296 0.4523 0.0002  -0.0017 -0.0123 115 ARG   C CZ  
1934 N  NH1 . ARG   B 109 ? 0.3967 0.3978 0.4202 0.0005  -0.0010 -0.0129 115 ARG   C NH1 
1935 N  NH2 . ARG   B 109 ? 0.4531 0.4495 0.4743 -0.0001 -0.0004 -0.0142 115 ARG   C NH2 
1936 N  N   . CYS   B 110 ? 0.1598 0.1629 0.1664 -0.0067 -0.0003 -0.0073 116 CYS   C N   
1937 C  CA  . CYS   B 110 ? 0.1721 0.1747 0.1774 -0.0084 -0.0003 -0.0078 116 CYS   C CA  
1938 C  C   . CYS   B 110 ? 0.1980 0.1977 0.2036 -0.0085 0.0002  -0.0098 116 CYS   C C   
1939 O  O   . CYS   B 110 ? 0.2033 0.2019 0.2107 -0.0069 0.0006  -0.0107 116 CYS   C O   
1940 C  CB  . CYS   B 110 ? 0.1580 0.1635 0.1621 -0.0097 -0.0004 -0.0078 116 CYS   C CB  
1941 S  SG  . CYS   B 110 ? 0.1599 0.1658 0.1625 -0.0097 0.0007  -0.0092 116 CYS   C SG  
1942 N  N   . GLN   B 111 ? 0.2060 0.2046 0.2101 -0.0103 0.0003  -0.0108 117 GLN   C N   
1943 C  CA  . GLN   B 111 ? 0.2343 0.2298 0.2385 -0.0103 0.0010  -0.0131 117 GLN   C CA  
1944 C  C   . GLN   B 111 ? 0.2383 0.2347 0.2426 -0.0097 0.0026  -0.0152 117 GLN   C C   
1945 O  O   . GLN   B 111 ? 0.2599 0.2540 0.2655 -0.0091 0.0036  -0.0174 117 GLN   C O   
1946 C  CB  . GLN   B 111 ? 0.2771 0.2712 0.2794 -0.0127 0.0006  -0.0141 117 GLN   C CB  
1947 C  CG  . GLN   B 111 ? 0.3080 0.3048 0.3076 -0.0144 0.0005  -0.0147 117 GLN   C CG  
1948 C  CD  . GLN   B 111 ? 0.4177 0.4133 0.4157 -0.0170 -0.0003 -0.0158 117 GLN   C CD  
1949 O  OE1 . GLN   B 111 ? 0.4410 0.4390 0.4394 -0.0185 -0.0016 -0.0145 117 GLN   C OE1 
1950 N  NE2 . GLN   B 111 ? 0.4485 0.4405 0.4450 -0.0177 0.0005  -0.0185 117 GLN   C NE2 
1951 N  N   . HIS   B 112 ? 0.2002 0.1998 0.2033 -0.0099 0.0030  -0.0145 118 HIS   C N   
1952 C  CA  . HIS   B 112 ? 0.1997 0.2002 0.2022 -0.0099 0.0049  -0.0161 118 HIS   C CA  
1953 C  C   . HIS   B 112 ? 0.2108 0.2127 0.2172 -0.0081 0.0057  -0.0159 118 HIS   C C   
1954 O  O   . HIS   B 112 ? 0.2350 0.2376 0.2419 -0.0081 0.0079  -0.0176 118 HIS   C O   
1955 C  CB  . HIS   B 112 ? 0.2015 0.2038 0.1996 -0.0116 0.0049  -0.0154 118 HIS   C CB  
1956 C  CG  . HIS   B 112 ? 0.1889 0.1903 0.1835 -0.0136 0.0036  -0.0158 118 HIS   C CG  
1957 N  ND1 . HIS   B 112 ? 0.1646 0.1679 0.1591 -0.0143 0.0013  -0.0137 118 HIS   C ND1 
1958 C  CD2 . HIS   B 112 ? 0.2356 0.2347 0.2272 -0.0152 0.0043  -0.0183 118 HIS   C CD2 
1959 C  CE1 . HIS   B 112 ? 0.2085 0.2108 0.2004 -0.0163 0.0003  -0.0148 118 HIS   C CE1 
1960 N  NE2 . HIS   B 112 ? 0.2435 0.2430 0.2332 -0.0169 0.0020  -0.0176 118 HIS   C NE2 
1961 N  N   . GLY   B 113 ? 0.1762 0.1785 0.1850 -0.0067 0.0041  -0.0140 119 GLY   C N   
1962 C  CA  . GLY   B 113 ? 0.1758 0.1794 0.1882 -0.0052 0.0043  -0.0138 119 GLY   C CA  
1963 C  C   . GLY   B 113 ? 0.1603 0.1653 0.1721 -0.0049 0.0028  -0.0114 119 GLY   C C   
1964 O  O   . GLY   B 113 ? 0.1603 0.1650 0.1700 -0.0053 0.0016  -0.0098 119 GLY   C O   
1965 N  N   . VAL   B 114 ? 0.1623 0.1688 0.1765 -0.0042 0.0031  -0.0113 120 VAL   C N   
1966 C  CA  . VAL   B 114 ? 0.1580 0.1654 0.1718 -0.0038 0.0019  -0.0094 120 VAL   C CA  
1967 C  C   . VAL   B 114 ? 0.1575 0.1659 0.1679 -0.0050 0.0022  -0.0081 120 VAL   C C   
1968 O  O   . VAL   B 114 ? 0.1691 0.1781 0.1780 -0.0061 0.0037  -0.0085 120 VAL   C O   
1969 C  CB  . VAL   B 114 ? 0.1685 0.1771 0.1862 -0.0031 0.0021  -0.0099 120 VAL   C CB  
1970 C  CG1 . VAL   B 114 ? 0.1869 0.1957 0.2036 -0.0029 0.0009  -0.0083 120 VAL   C CG1 
1971 C  CG2 . VAL   B 114 ? 0.1844 0.1921 0.2061 -0.0015 0.0008  -0.0110 120 VAL   C CG2 
1972 N  N   . VAL   B 115 ? 0.1477 0.1561 0.1566 -0.0048 0.0010  -0.0065 121 VAL   C N   
1973 C  CA  . VAL   B 115 ? 0.1504 0.1599 0.1573 -0.0054 0.0006  -0.0052 121 VAL   C CA  
1974 C  C   . VAL   B 115 ? 0.1544 0.1642 0.1620 -0.0047 0.0004  -0.0042 121 VAL   C C   
1975 O  O   . VAL   B 115 ? 0.1548 0.1648 0.1610 -0.0052 0.0005  -0.0033 121 VAL   C O   
1976 C  CB  . VAL   B 115 ? 0.1454 0.1553 0.1516 -0.0056 -0.0003 -0.0044 121 VAL   C CB  
1977 C  CG1 . VAL   B 115 ? 0.1631 0.1746 0.1688 -0.0057 -0.0010 -0.0031 121 VAL   C CG1 
1978 C  CG2 . VAL   B 115 ? 0.1557 0.1649 0.1612 -0.0067 -0.0001 -0.0055 121 VAL   C CG2 
1979 N  N   . GLY   B 116 ? 0.1532 0.1623 0.1624 -0.0036 -0.0002 -0.0042 122 GLY   C N   
1980 C  CA  . GLY   B 116 ? 0.1709 0.1797 0.1805 -0.0029 -0.0006 -0.0036 122 GLY   C CA  
1981 C  C   . GLY   B 116 ? 0.1432 0.1509 0.1536 -0.0019 -0.0015 -0.0039 122 GLY   C C   
1982 O  O   . GLY   B 116 ? 0.1555 0.1624 0.1662 -0.0017 -0.0020 -0.0045 122 GLY   C O   
1983 N  N   . ILE   B 117 ? 0.1518 0.1588 0.1620 -0.0014 -0.0019 -0.0036 123 ILE   C N   
1984 C  CA  . ILE   B 117 ? 0.1456 0.1510 0.1553 -0.0006 -0.0030 -0.0041 123 ILE   C CA  
1985 C  C   . ILE   B 117 ? 0.1548 0.1594 0.1625 0.0000  -0.0028 -0.0037 123 ILE   C C   
1986 O  O   . ILE   B 117 ? 0.1488 0.1540 0.1568 0.0002  -0.0021 -0.0032 123 ILE   C O   
1987 C  CB  . ILE   B 117 ? 0.1604 0.1653 0.1723 -0.0006 -0.0038 -0.0049 123 ILE   C CB  
1988 C  CG1 . ILE   B 117 ? 0.1764 0.1814 0.1891 -0.0011 -0.0030 -0.0046 123 ILE   C CG1 
1989 C  CG2 . ILE   B 117 ? 0.1801 0.1860 0.1951 -0.0009 -0.0041 -0.0058 123 ILE   C CG2 
1990 C  CD1 . ILE   B 117 ? 0.1895 0.1940 0.2048 -0.0016 -0.0038 -0.0055 123 ILE   C CD1 
1991 N  N   . VAL   B 118 ? 0.1299 0.1328 0.1352 0.0004  -0.0033 -0.0039 124 VAL   C N   
1992 C  CA  . VAL   B 118 ? 0.1340 0.1360 0.1371 0.0009  -0.0025 -0.0040 124 VAL   C CA  
1993 C  C   . VAL   B 118 ? 0.1424 0.1435 0.1465 0.0014  -0.0027 -0.0046 124 VAL   C C   
1994 O  O   . VAL   B 118 ? 0.1471 0.1470 0.1517 0.0012  -0.0041 -0.0052 124 VAL   C O   
1995 C  CB  . VAL   B 118 ? 0.1448 0.1440 0.1437 0.0008  -0.0030 -0.0043 124 VAL   C CB  
1996 C  CG1 . VAL   B 118 ? 0.1687 0.1668 0.1651 0.0013  -0.0015 -0.0050 124 VAL   C CG1 
1997 C  CG2 . VAL   B 118 ? 0.1734 0.1727 0.1711 0.0001  -0.0026 -0.0035 124 VAL   C CG2 
1998 N  N   . SER   B 119 ? 0.1451 0.1468 0.1498 0.0021  -0.0016 -0.0045 125 SER   C N   
1999 C  CA  . SER   B 119 ? 0.1447 0.1448 0.1502 0.0027  -0.0017 -0.0050 125 SER   C CA  
2000 C  C   . SER   B 119 ? 0.1694 0.1684 0.1740 0.0038  -0.0005 -0.0059 125 SER   C C   
2001 O  O   . SER   B 119 ? 0.1657 0.1620 0.1697 0.0043  -0.0007 -0.0069 125 SER   C O   
2002 C  CB  . SER   B 119 ? 0.1514 0.1527 0.1596 0.0025  -0.0018 -0.0038 125 SER   C CB  
2003 O  OG  . SER   B 119 ? 0.1621 0.1612 0.1711 0.0030  -0.0020 -0.0038 125 SER   C OG  
2004 N  N   . THR   B 120 ? 0.1690 0.1699 0.1737 0.0042  0.0011  -0.0058 126 THR   C N   
2005 C  CA  . THR   B 120 ? 0.1668 0.1673 0.1715 0.0054  0.0030  -0.0070 126 THR   C CA  
2006 C  C   . THR   B 120 ? 0.1676 0.1692 0.1702 0.0049  0.0049  -0.0074 126 THR   C C   
2007 O  O   . THR   B 120 ? 0.1631 0.1661 0.1652 0.0037  0.0046  -0.0063 126 THR   C O   
2008 C  CB  . THR   B 120 ? 0.1731 0.1757 0.1827 0.0069  0.0033  -0.0064 126 THR   C CB  
2009 O  OG1 . THR   B 120 ? 0.1896 0.1963 0.2019 0.0065  0.0036  -0.0053 126 THR   C OG1 
2010 C  CG2 . THR   B 120 ? 0.1993 0.2004 0.2105 0.0071  0.0014  -0.0054 126 THR   C CG2 
2011 N  N   . GLY   B 121 ? 0.1750 0.1756 0.1762 0.0056  0.0072  -0.0089 127 GLY   C N   
2012 C  CA  . GLY   B 121 ? 0.2049 0.2069 0.2044 0.0048  0.0098  -0.0093 127 GLY   C CA  
2013 C  C   . GLY   B 121 ? 0.2107 0.2125 0.2104 0.0058  0.0131  -0.0114 127 GLY   C C   
2014 O  O   . GLY   B 121 ? 0.2167 0.2163 0.2166 0.0072  0.0130  -0.0128 127 GLY   C O   
2015 N  N   . GLY   B 122 ? 0.2130 0.2169 0.2126 0.0050  0.0162  -0.0118 128 GLY   C N   
2016 C  CA  . GLY   B 122 ? 0.2388 0.2431 0.2390 0.0058  0.0203  -0.0142 128 GLY   C CA  
2017 C  C   . GLY   B 122 ? 0.2393 0.2489 0.2445 0.0052  0.0234  -0.0141 128 GLY   C C   
2018 O  O   . GLY   B 122 ? 0.2426 0.2565 0.2536 0.0050  0.0219  -0.0125 128 GLY   C O   
2019 N  N   . ASN   B 123 ? 0.2530 0.2626 0.2562 0.0047  0.0280  -0.0161 129 ASN   C N   
2020 C  CA  . ASN   B 123 ? 0.2668 0.2818 0.2755 0.0038  0.0319  -0.0165 129 ASN   C CA  
2021 C  C   . ASN   B 123 ? 0.2506 0.2675 0.2590 0.0011  0.0309  -0.0140 129 ASN   C C   
2022 O  O   . ASN   B 123 ? 0.2615 0.2843 0.2779 0.0008  0.0320  -0.0138 129 ASN   C O   
2023 C  CB  . ASN   B 123 ? 0.3001 0.3210 0.3206 0.0065  0.0320  -0.0175 129 ASN   C CB  
2024 C  CG  . ASN   B 123 ? 0.3660 0.3851 0.3877 0.0092  0.0337  -0.0202 129 ASN   C CG  
2025 O  OD1 . ASN   B 123 ? 0.3841 0.4009 0.4011 0.0087  0.0380  -0.0227 129 ASN   C OD1 
2026 N  ND2 . ASN   B 123 ? 0.4189 0.4385 0.4463 0.0119  0.0305  -0.0199 129 ASN   C ND2 
2027 N  N   . GLY   B 124 ? 0.2324 0.2444 0.2327 -0.0006 0.0285  -0.0123 130 GLY   C N   
2028 C  CA  . GLY   B 124 ? 0.2204 0.2332 0.2203 -0.0029 0.0274  -0.0100 130 GLY   C CA  
2029 C  C   . GLY   B 124 ? 0.1984 0.2142 0.2043 -0.0022 0.0233  -0.0085 130 GLY   C C   
2030 O  O   . GLY   B 124 ? 0.1940 0.2115 0.2014 -0.0040 0.0228  -0.0072 130 GLY   C O   
2031 N  N   . LEU   B 125 ? 0.1844 0.2005 0.1933 0.0002  0.0206  -0.0088 131 LEU   C N   
2032 C  CA  . LEU   B 125 ? 0.1859 0.2040 0.1991 0.0009  0.0168  -0.0074 131 LEU   C CA  
2033 C  C   . LEU   B 125 ? 0.1958 0.2093 0.2040 0.0013  0.0137  -0.0067 131 LEU   C C   
2034 O  O   . LEU   B 125 ? 0.2276 0.2376 0.2320 0.0022  0.0140  -0.0078 131 LEU   C O   
2035 C  CB  . LEU   B 125 ? 0.2063 0.2286 0.2277 0.0032  0.0163  -0.0080 131 LEU   C CB  
2036 C  CG  . LEU   B 125 ? 0.2478 0.2760 0.2765 0.0031  0.0190  -0.0089 131 LEU   C CG  
2037 C  CD1 . LEU   B 125 ? 0.2828 0.3138 0.3188 0.0061  0.0189  -0.0100 131 LEU   C CD1 
2038 C  CD2 . LEU   B 125 ? 0.2465 0.2783 0.2786 0.0013  0.0175  -0.0075 131 LEU   C CD2 
2039 N  N   . VAL   B 126 ? 0.1568 0.1700 0.1648 0.0006  0.0110  -0.0053 132 VAL   C N   
2040 C  CA  . VAL   B 126 ? 0.1606 0.1705 0.1655 0.0009  0.0083  -0.0048 132 VAL   C CA  
2041 C  C   . VAL   B 126 ? 0.1629 0.1750 0.1721 0.0016  0.0061  -0.0040 132 VAL   C C   
2042 O  O   . VAL   B 126 ? 0.1547 0.1700 0.1672 0.0010  0.0058  -0.0033 132 VAL   C O   
2043 C  CB  . VAL   B 126 ? 0.1743 0.1810 0.1743 -0.0006 0.0073  -0.0040 132 VAL   C CB  
2044 C  CG1 . VAL   B 126 ? 0.2098 0.2185 0.2114 -0.0022 0.0075  -0.0030 132 VAL   C CG1 
2045 C  CG2 . VAL   B 126 ? 0.1799 0.1840 0.1782 -0.0001 0.0045  -0.0038 132 VAL   C CG2 
2046 N  N   . GLY   B 127 ? 0.1518 0.1618 0.1604 0.0026  0.0046  -0.0041 133 GLY   C N   
2047 C  CA  . GLY   B 127 ? 0.1503 0.1616 0.1618 0.0030  0.0027  -0.0032 133 GLY   C CA  
2048 C  C   . GLY   B 127 ? 0.1442 0.1534 0.1535 0.0022  0.0012  -0.0028 133 GLY   C C   
2049 O  O   . GLY   B 127 ? 0.1571 0.1636 0.1639 0.0022  0.0008  -0.0034 133 GLY   C O   
2050 N  N   . PHE   B 128 ? 0.1397 0.1504 0.1502 0.0015  0.0002  -0.0019 134 PHE   C N   
2051 C  CA  . PHE   B 128 ? 0.1421 0.1515 0.1514 0.0007  -0.0007 -0.0018 134 PHE   C CA  
2052 C  C   . PHE   B 128 ? 0.1470 0.1564 0.1570 0.0007  -0.0014 -0.0010 134 PHE   C C   
2053 O  O   . PHE   B 128 ? 0.1483 0.1593 0.1593 0.0007  -0.0020 -0.0001 134 PHE   C O   
2054 C  CB  . PHE   B 128 ? 0.1582 0.1687 0.1670 -0.0006 -0.0007 -0.0017 134 PHE   C CB  
2055 C  CG  . PHE   B 128 ? 0.1469 0.1569 0.1545 -0.0010 0.0000  -0.0020 134 PHE   C CG  
2056 C  CD1 . PHE   B 128 ? 0.1552 0.1625 0.1604 -0.0010 -0.0003 -0.0023 134 PHE   C CD1 
2057 C  CD2 . PHE   B 128 ? 0.1632 0.1753 0.1720 -0.0014 0.0010  -0.0017 134 PHE   C CD2 
2058 C  CE1 . PHE   B 128 ? 0.1604 0.1664 0.1634 -0.0016 0.0004  -0.0022 134 PHE   C CE1 
2059 C  CE2 . PHE   B 128 ? 0.1695 0.1809 0.1767 -0.0022 0.0021  -0.0018 134 PHE   C CE2 
2060 C  CZ  . PHE   B 128 ? 0.1696 0.1774 0.1733 -0.0024 0.0018  -0.0019 134 PHE   C CZ  
2061 N  N   . ALA   B 129 ? 0.1464 0.1539 0.1559 0.0004  -0.0016 -0.0013 135 ALA   C N   
2062 C  CA  . ALA   B 129 ? 0.1396 0.1464 0.1490 -0.0002 -0.0019 -0.0004 135 ALA   C CA  
2063 C  C   . ALA   B 129 ? 0.1409 0.1487 0.1493 -0.0016 -0.0016 -0.0004 135 ALA   C C   
2064 O  O   . ALA   B 129 ? 0.1460 0.1539 0.1548 -0.0022 -0.0011 -0.0014 135 ALA   C O   
2065 C  CB  . ALA   B 129 ? 0.1461 0.1507 0.1558 -0.0004 -0.0018 -0.0010 135 ALA   C CB  
2066 N  N   . ASP   B 130 ? 0.1419 0.1504 0.1492 -0.0021 -0.0020 0.0007  136 ASP   C N   
2067 C  CA  . ASP   B 130 ? 0.1411 0.1501 0.1465 -0.0037 -0.0016 0.0005  136 ASP   C CA  
2068 C  C   . ASP   B 130 ? 0.1411 0.1488 0.1455 -0.0049 -0.0003 0.0002  136 ASP   C C   
2069 O  O   . ASP   B 130 ? 0.1546 0.1605 0.1586 -0.0050 -0.0002 0.0011  136 ASP   C O   
2070 C  CB  . ASP   B 130 ? 0.1609 0.1704 0.1644 -0.0040 -0.0029 0.0018  136 ASP   C CB  
2071 C  CG  . ASP   B 130 ? 0.2083 0.2181 0.2089 -0.0057 -0.0027 0.0013  136 ASP   C CG  
2072 O  OD1 . ASP   B 130 ? 0.2058 0.2165 0.2072 -0.0061 -0.0020 -0.0001 136 ASP   C OD1 
2073 O  OD2 . ASP   B 130 ? 0.2424 0.2508 0.2394 -0.0068 -0.0031 0.0023  136 ASP   C OD2 
2074 N  N   . VAL   B 131 ? 0.1503 0.1585 0.1545 -0.0059 0.0010  -0.0012 137 VAL   C N   
2075 C  CA  . VAL   B 131 ? 0.1620 0.1696 0.1658 -0.0073 0.0029  -0.0018 137 VAL   C CA  
2076 C  C   . VAL   B 131 ? 0.1627 0.1701 0.1628 -0.0089 0.0040  -0.0023 137 VAL   C C   
2077 O  O   . VAL   B 131 ? 0.1739 0.1809 0.1730 -0.0104 0.0062  -0.0031 137 VAL   C O   
2078 C  CB  . VAL   B 131 ? 0.1681 0.1766 0.1762 -0.0070 0.0039  -0.0037 137 VAL   C CB  
2079 C  CG1 . VAL   B 131 ? 0.1671 0.1751 0.1778 -0.0058 0.0026  -0.0034 137 VAL   C CG1 
2080 C  CG2 . VAL   B 131 ? 0.1807 0.1902 0.1901 -0.0064 0.0038  -0.0052 137 VAL   C CG2 
2081 N  N   . ARG   B 132 ? 0.1533 0.1612 0.1513 -0.0089 0.0026  -0.0021 138 ARG   C N   
2082 C  CA  . ARG   B 132 ? 0.1503 0.1578 0.1445 -0.0105 0.0035  -0.0030 138 ARG   C CA  
2083 C  C   . ARG   B 132 ? 0.1564 0.1620 0.1450 -0.0123 0.0040  -0.0018 138 ARG   C C   
2084 O  O   . ARG   B 132 ? 0.1798 0.1844 0.1644 -0.0140 0.0056  -0.0030 138 ARG   C O   
2085 C  CB  . ARG   B 132 ? 0.1610 0.1694 0.1546 -0.0103 0.0014  -0.0030 138 ARG   C CB  
2086 C  CG  . ARG   B 132 ? 0.1650 0.1745 0.1629 -0.0091 0.0014  -0.0043 138 ARG   C CG  
2087 C  CD  . ARG   B 132 ? 0.1502 0.1605 0.1476 -0.0094 -0.0004 -0.0041 138 ARG   C CD  
2088 N  NE  . ARG   B 132 ? 0.1495 0.1612 0.1481 -0.0085 -0.0022 -0.0022 138 ARG   C NE  
2089 C  CZ  . ARG   B 132 ? 0.1499 0.1634 0.1501 -0.0085 -0.0038 -0.0018 138 ARG   C CZ  
2090 N  NH1 . ARG   B 132 ? 0.1527 0.1664 0.1525 -0.0097 -0.0039 -0.0030 138 ARG   C NH1 
2091 N  NH2 . ARG   B 132 ? 0.1587 0.1738 0.1612 -0.0073 -0.0050 -0.0004 138 ARG   C NH2 
2092 N  N   . ASP   B 133 ? 0.1618 0.1661 0.1493 -0.0119 0.0026  0.0006  139 ASP   C N   
2093 C  CA  . ASP   B 133 ? 0.1768 0.1781 0.1578 -0.0138 0.0028  0.0023  139 ASP   C CA  
2094 C  C   . ASP   B 133 ? 0.1881 0.1880 0.1688 -0.0153 0.0062  0.0018  139 ASP   C C   
2095 O  O   . ASP   B 133 ? 0.1970 0.1940 0.1715 -0.0174 0.0073  0.0030  139 ASP   C O   
2096 C  CB  . ASP   B 133 ? 0.2026 0.2025 0.1829 -0.0126 -0.0004 0.0052  139 ASP   C CB  
2097 C  CG  . ASP   B 133 ? 0.2332 0.2330 0.2185 -0.0110 -0.0004 0.0058  139 ASP   C CG  
2098 O  OD1 . ASP   B 133 ? 0.2268 0.2289 0.2173 -0.0098 0.0004  0.0041  139 ASP   C OD1 
2099 O  OD2 . ASP   B 133 ? 0.2528 0.2495 0.2361 -0.0111 -0.0013 0.0081  139 ASP   C OD2 
2100 N  N   . LEU   B 134 ? 0.1831 0.1850 0.1702 -0.0145 0.0079  0.0002  140 LEU   C N   
2101 C  CA  . LEU   B 134 ? 0.1819 0.1832 0.1704 -0.0160 0.0111  -0.0004 140 LEU   C CA  
2102 C  C   . LEU   B 134 ? 0.1869 0.1894 0.1749 -0.0176 0.0147  -0.0030 140 LEU   C C   
2103 O  O   . LEU   B 134 ? 0.1873 0.1925 0.1814 -0.0169 0.0162  -0.0055 140 LEU   C O   
2104 C  CB  . LEU   B 134 ? 0.1814 0.1846 0.1775 -0.0144 0.0107  -0.0011 140 LEU   C CB  
2105 C  CG  . LEU   B 134 ? 0.1966 0.1985 0.1933 -0.0127 0.0076  0.0009  140 LEU   C CG  
2106 C  CD1 . LEU   B 134 ? 0.2112 0.2146 0.2144 -0.0113 0.0071  -0.0004 140 LEU   C CD1 
2107 C  CD2 . LEU   B 134 ? 0.2120 0.2100 0.2044 -0.0139 0.0073  0.0035  140 LEU   C CD2 
2108 N  N   . LEU   B 135 ? 0.1943 0.1943 0.1745 -0.0198 0.0160  -0.0025 141 LEU   C N   
2109 C  CA  . LEU   B 135 ? 0.1996 0.2003 0.1781 -0.0213 0.0196  -0.0054 141 LEU   C CA  
2110 C  C   . LEU   B 135 ? 0.2089 0.2112 0.1920 -0.0226 0.0241  -0.0074 141 LEU   C C   
2111 O  O   . LEU   B 135 ? 0.2334 0.2379 0.2199 -0.0226 0.0271  -0.0106 141 LEU   C O   
2112 C  CB  . LEU   B 135 ? 0.2020 0.1992 0.1697 -0.0237 0.0199  -0.0045 141 LEU   C CB  
2113 C  CG  . LEU   B 135 ? 0.2072 0.2029 0.1704 -0.0228 0.0149  -0.0023 141 LEU   C CG  
2114 C  CD1 . LEU   B 135 ? 0.2380 0.2299 0.1899 -0.0255 0.0151  -0.0016 141 LEU   C CD1 
2115 C  CD2 . LEU   B 135 ? 0.2314 0.2301 0.1999 -0.0205 0.0127  -0.0040 141 LEU   C CD2 
2116 N  N   . TRP   B 136 ? 0.2041 0.2053 0.1881 -0.0237 0.0249  -0.0055 142 TRP   C N   
2117 C  CA  . TRP   B 136 ? 0.2166 0.2198 0.2059 -0.0253 0.0293  -0.0073 142 TRP   C CA  
2118 C  C   . TRP   B 136 ? 0.2307 0.2388 0.2317 -0.0230 0.0290  -0.0100 142 TRP   C C   
2119 O  O   . TRP   B 136 ? 0.2410 0.2518 0.2480 -0.0240 0.0327  -0.0124 142 TRP   C O   
2120 C  CB  . TRP   B 136 ? 0.2211 0.2215 0.2084 -0.0272 0.0295  -0.0044 142 TRP   C CB  
2121 C  CG  . TRP   B 136 ? 0.2173 0.2169 0.2073 -0.0249 0.0248  -0.0022 142 TRP   C CG  
2122 C  CD1 . TRP   B 136 ? 0.2287 0.2247 0.2130 -0.0240 0.0210  0.0010  142 TRP   C CD1 
2123 C  CD2 . TRP   B 136 ? 0.2177 0.2200 0.2169 -0.0233 0.0235  -0.0031 142 TRP   C CD2 
2124 N  NE1 . TRP   B 136 ? 0.2258 0.2221 0.2153 -0.0219 0.0180  0.0018  142 TRP   C NE1 
2125 C  CE2 . TRP   B 136 ? 0.2204 0.2202 0.2183 -0.0216 0.0195  -0.0006 142 TRP   C CE2 
2126 C  CE3 . TRP   B 136 ? 0.2322 0.2388 0.2407 -0.0232 0.0254  -0.0059 142 TRP   C CE3 
2127 C  CZ2 . TRP   B 136 ? 0.2368 0.2378 0.2413 -0.0200 0.0174  -0.0010 142 TRP   C CZ2 
2128 C  CZ3 . TRP   B 136 ? 0.2454 0.2532 0.2605 -0.0217 0.0227  -0.0060 142 TRP   C CZ3 
2129 C  CH2 . TRP   B 136 ? 0.2360 0.2408 0.2485 -0.0203 0.0190  -0.0036 142 TRP   C CH2 
2130 N  N   . LEU   B 137 ? 0.2175 0.2265 0.2215 -0.0199 0.0247  -0.0098 143 LEU   C N   
2131 C  CA  . LEU   B 137 ? 0.2360 0.2488 0.2499 -0.0177 0.0239  -0.0120 143 LEU   C CA  
2132 C  C   . LEU   B 137 ? 0.2854 0.3007 0.3032 -0.0176 0.0271  -0.0156 143 LEU   C C   
2133 O  O   . LEU   B 137 ? 0.2988 0.3174 0.3256 -0.0165 0.0277  -0.0177 143 LEU   C O   
2134 C  CB  . LEU   B 137 ? 0.2164 0.2289 0.2308 -0.0148 0.0191  -0.0110 143 LEU   C CB  
2135 C  CG  . LEU   B 137 ? 0.2064 0.2174 0.2202 -0.0141 0.0161  -0.0085 143 LEU   C CG  
2136 C  CD1 . LEU   B 137 ? 0.2023 0.2131 0.2159 -0.0116 0.0123  -0.0078 143 LEU   C CD1 
2137 C  CD2 . LEU   B 137 ? 0.2126 0.2253 0.2336 -0.0143 0.0163  -0.0092 143 LEU   C CD2 
2138 N  N   . ASP   B 138 ? 0.3214 0.3349 0.3324 -0.0187 0.0290  -0.0163 144 ASP   C N   
2139 C  CA  . ASP   B 138 ? 0.3734 0.3883 0.3865 -0.0186 0.0323  -0.0199 144 ASP   C CA  
2140 C  C   . ASP   B 138 ? 0.4184 0.4341 0.4310 -0.0214 0.0383  -0.0220 144 ASP   C C   
2141 O  O   . ASP   B 138 ? 0.4416 0.4580 0.4552 -0.0213 0.0414  -0.0254 144 ASP   C O   
2142 C  CB  . ASP   B 138 ? 0.4219 0.4340 0.4275 -0.0184 0.0309  -0.0200 144 ASP   C CB  
2143 C  CG  . ASP   B 138 ? 0.4611 0.4736 0.4707 -0.0154 0.0266  -0.0198 144 ASP   C CG  
2144 O  OD1 . ASP   B 138 ? 0.4813 0.4963 0.4997 -0.0133 0.0262  -0.0214 144 ASP   C OD1 
2145 O  OD2 . ASP   B 138 ? 0.4939 0.5043 0.4980 -0.0151 0.0235  -0.0180 144 ASP   C OD2 
2146 N  N   . GLU   B 139 ? 0.4296 0.4447 0.4404 -0.0239 0.0402  -0.0203 145 GLU   C N   
2147 C  CA  . GLU   B 139 ? 0.4707 0.4866 0.4809 -0.0271 0.0466  -0.0222 145 GLU   C CA  
2148 C  C   . GLU   B 139 ? 0.4987 0.5177 0.5173 -0.0282 0.0484  -0.0222 145 GLU   C C   
2149 O  O   . GLU   B 139 ? 0.5203 0.5397 0.5384 -0.0315 0.0540  -0.0232 145 GLU   C O   
2150 C  CB  . GLU   B 139 ? 0.5245 0.5350 0.5205 -0.0303 0.0482  -0.0200 145 GLU   C CB  
2151 C  CG  . GLU   B 139 ? 0.6070 0.6140 0.5975 -0.0310 0.0444  -0.0153 145 GLU   C CG  
2152 C  CD  . GLU   B 139 ? 0.7384 0.7397 0.7150 -0.0325 0.0427  -0.0126 145 GLU   C CD  
2153 O  OE1 . GLU   B 139 ? 0.7501 0.7476 0.7207 -0.0342 0.0415  -0.0089 145 GLU   C OE1 
2154 O  OE2 . GLU   B 139 ? 0.7827 0.7832 0.7548 -0.0320 0.0422  -0.0141 145 GLU   C OE2 
2155 N  N1  . A1B3W C .   ? 0.1519 0.1662 0.2008 -0.0018 0.0101  0.0031  201 A1B3W A N1  
2156 C  C4  . A1B3W C .   ? 0.2008 0.2103 0.2256 0.0053  0.0259  0.0161  201 A1B3W A C4  
2157 C  C5  . A1B3W C .   ? 0.1985 0.2081 0.2278 0.0042  0.0248  0.0166  201 A1B3W A C5  
2158 C  C6  . A1B3W C .   ? 0.1781 0.1890 0.2065 0.0035  0.0200  0.0147  201 A1B3W A C6  
2159 C  C7  . A1B3W C .   ? 0.1614 0.1743 0.2014 0.0011  0.0182  0.0122  201 A1B3W A C7  
2160 C  C8  . A1B3W C .   ? 0.1604 0.1695 0.1997 0.0018  0.0185  0.0168  201 A1B3W A C8  
2161 C  C10 . A1B3W C .   ? 0.1718 0.1824 0.2176 0.0001  0.0147  0.0130  201 A1B3W A C10 
2162 C  C13 . A1B3W C .   ? 0.1586 0.1721 0.2087 -0.0009 0.0168  0.0096  201 A1B3W A C13 
2163 O  O3  . A1B3W C .   ? 0.1591 0.1725 0.2188 -0.0030 0.0147  0.0048  201 A1B3W A O3  
2164 C  C12 . A1B3W C .   ? 0.1510 0.1647 0.2037 -0.0020 0.0128  0.0056  201 A1B3W A C12 
2165 C  C11 . A1B3W C .   ? 0.1548 0.1677 0.2020 -0.0008 0.0138  0.0092  201 A1B3W A C11 
2166 C  C9  . A1B3W C .   ? 0.1707 0.1802 0.2092 0.0018  0.0150  0.0161  201 A1B3W A C9  
2167 N  N   . A1B3W C .   ? 0.1547 0.1667 0.1977 0.0006  0.0179  0.0130  201 A1B3W A N   
2168 O  O2  . A1B3W C .   ? 0.1675 0.1829 0.2114 0.0005  0.0177  0.0093  201 A1B3W A O2  
2169 O  O1  . A1B3W C .   ? 0.1785 0.1891 0.2107 0.0027  0.0192  0.0152  201 A1B3W A O1  
2170 C  C1  . A1B3W C .   ? 0.1731 0.1849 0.1964 0.0038  0.0165  0.0124  201 A1B3W A C1  
2171 O  O   . A1B3W C .   ? 0.1680 0.1804 0.1911 0.0031  0.0128  0.0110  201 A1B3W A O   
2172 C  C   . A1B3W C .   ? 0.1847 0.1972 0.2029 0.0033  0.0100  0.0089  201 A1B3W A C   
2173 CL CL  . A1B3W C .   ? 0.2536 0.2610 0.2796 0.0063  0.0331  0.0188  201 A1B3W A CL  
2174 C  C3  . A1B3W C .   ? 0.1851 0.1955 0.2047 0.0057  0.0222  0.0138  201 A1B3W A C3  
2175 C  C2  . A1B3W C .   ? 0.1810 0.1924 0.1999 0.0049  0.0175  0.0120  201 A1B3W A C2  
2185 N  N1  . A1B3W G .   ? 0.1719 0.1647 0.1804 0.0055  -0.0014 -0.0062 201 A1B3W C N1  
2186 C  C4  . A1B3W G .   ? 0.2291 0.2172 0.2096 0.0045  0.0123  -0.0153 201 A1B3W C C4  
2187 C  C5  . A1B3W G .   ? 0.2170 0.2043 0.2008 0.0056  0.0099  -0.0156 201 A1B3W C C5  
2188 C  C6  . A1B3W G .   ? 0.2009 0.1893 0.1876 0.0052  0.0066  -0.0136 201 A1B3W C C6  
2189 C  C7  . A1B3W G .   ? 0.1895 0.1793 0.1852 0.0067  0.0042  -0.0127 201 A1B3W C C7  
2190 C  C8  . A1B3W G .   ? 0.1911 0.1744 0.1848 0.0060  0.0007  -0.0145 201 A1B3W C C8  
2191 C  C10 . A1B3W G .   ? 0.1812 0.1661 0.1824 0.0052  -0.0019 -0.0116 201 A1B3W C C10 
2192 C  C13 . A1B3W G .   ? 0.1709 0.1600 0.1735 0.0076  0.0019  -0.0113 201 A1B3W C C13 
2193 O  O3  . A1B3W G .   ? 0.1681 0.1559 0.1773 0.0077  -0.0007 -0.0082 201 A1B3W C O3  
2194 C  C12 . A1B3W G .   ? 0.1635 0.1534 0.1710 0.0065  -0.0009 -0.0080 201 A1B3W C C12 
2195 C  C11 . A1B3W G .   ? 0.1670 0.1560 0.1705 0.0061  -0.0005 -0.0099 201 A1B3W C C11 
2196 C  C9  . A1B3W G .   ? 0.1902 0.1738 0.1863 0.0047  -0.0020 -0.0133 201 A1B3W C C9  
2197 N  N   . A1B3W G .   ? 0.1831 0.1706 0.1803 0.0068  0.0024  -0.0129 201 A1B3W C N   
2198 O  O2  . A1B3W G .   ? 0.1819 0.1752 0.1811 0.0073  0.0056  -0.0117 201 A1B3W C O2  
2199 O  O1  . A1B3W G .   ? 0.1987 0.1857 0.1880 0.0057  0.0043  -0.0139 201 A1B3W C O1  
2200 C  C1  . A1B3W G .   ? 0.2053 0.1957 0.1919 0.0040  0.0056  -0.0116 201 A1B3W C C1  
2201 O  O   . A1B3W G .   ? 0.1933 0.1848 0.1831 0.0038  0.0028  -0.0103 201 A1B3W C O   
2202 C  C   . A1B3W G .   ? 0.1942 0.1874 0.1842 0.0028  0.0018  -0.0085 201 A1B3W C C   
2203 CL CL  . A1B3W G .   ? 0.2739 0.2612 0.2513 0.0047  0.0176  -0.0179 201 A1B3W C CL  
2204 C  C3  . A1B3W G .   ? 0.2198 0.2096 0.2000 0.0032  0.0111  -0.0130 201 A1B3W C C3  
2205 C  C2  . A1B3W G .   ? 0.2191 0.2101 0.2026 0.0031  0.0077  -0.0113 201 A1B3W C C2  
# 
