data_7I36
# 
_entry.id   7I36 
# 
_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   7I36         pdb_00007i36 10.2210/pdb7i36/pdb 
WWPDB D_1001408257 ?            ?                   
# 
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                        7I36 
_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 '1-[(3S)-3-hydroxypyrrolidin-1-yl]-2-(2-methoxyphenyl)ethan-1-one' 235.279   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                         65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                               78.133    2   ?         ? ? ? 
5 water       nat water                                                              18.015    380 ?         ? ? ? 
# 
_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 '1-[(3S)-3-hydroxypyrrolidin-1-yl]-2-(2-methoxyphenyl)ethan-1-one' A1B09 
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 
A1B09 non-polymer         . '1-[(3S)-3-hydroxypyrrolidin-1-yl]-2-(2-methoxyphenyl)ethan-1-one' ? 'C13 H17 N O3'   235.279 
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 140 146 146 GLU GLU 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 140 146 146 GLU GLU 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        A1B09 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B09 
_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 A1B09 1   201 201 A1B09 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 379 HOH   HOH A . 
H 5 HOH   2   302 381 HOH   HOH A . 
H 5 HOH   3   303 97  HOH   HOH A . 
H 5 HOH   4   304 386 HOH   HOH A . 
H 5 HOH   5   305 158 HOH   HOH A . 
H 5 HOH   6   306 344 HOH   HOH A . 
H 5 HOH   7   307 371 HOH   HOH A . 
H 5 HOH   8   308 260 HOH   HOH A . 
H 5 HOH   9   309 155 HOH   HOH A . 
H 5 HOH   10  310 135 HOH   HOH A . 
H 5 HOH   11  311 78  HOH   HOH A . 
H 5 HOH   12  312 148 HOH   HOH A . 
H 5 HOH   13  313 232 HOH   HOH A . 
H 5 HOH   14  314 132 HOH   HOH A . 
H 5 HOH   15  315 288 HOH   HOH A . 
H 5 HOH   16  316 121 HOH   HOH A . 
H 5 HOH   17  317 242 HOH   HOH A . 
H 5 HOH   18  318 152 HOH   HOH A . 
H 5 HOH   19  319 380 HOH   HOH A . 
H 5 HOH   20  320 246 HOH   HOH A . 
H 5 HOH   21  321 194 HOH   HOH A . 
H 5 HOH   22  322 353 HOH   HOH A . 
H 5 HOH   23  323 92  HOH   HOH A . 
H 5 HOH   24  324 362 HOH   HOH A . 
H 5 HOH   25  325 213 HOH   HOH A . 
H 5 HOH   26  326 146 HOH   HOH A . 
H 5 HOH   27  327 18  HOH   HOH A . 
H 5 HOH   28  328 338 HOH   HOH A . 
H 5 HOH   29  329 91  HOH   HOH A . 
H 5 HOH   30  330 103 HOH   HOH A . 
H 5 HOH   31  331 193 HOH   HOH A . 
H 5 HOH   32  332 302 HOH   HOH A . 
H 5 HOH   33  333 93  HOH   HOH A . 
H 5 HOH   34  334 111 HOH   HOH A . 
H 5 HOH   35  335 9   HOH   HOH A . 
H 5 HOH   36  336 67  HOH   HOH A . 
H 5 HOH   37  337 118 HOH   HOH A . 
H 5 HOH   38  338 358 HOH   HOH A . 
H 5 HOH   39  339 241 HOH   HOH A . 
H 5 HOH   40  340 332 HOH   HOH A . 
H 5 HOH   41  341 6   HOH   HOH A . 
H 5 HOH   42  342 320 HOH   HOH A . 
H 5 HOH   43  343 244 HOH   HOH A . 
H 5 HOH   44  344 261 HOH   HOH A . 
H 5 HOH   45  345 352 HOH   HOH A . 
H 5 HOH   46  346 240 HOH   HOH A . 
H 5 HOH   47  347 168 HOH   HOH A . 
H 5 HOH   48  348 42  HOH   HOH A . 
H 5 HOH   49  349 3   HOH   HOH A . 
H 5 HOH   50  350 144 HOH   HOH A . 
H 5 HOH   51  351 275 HOH   HOH A . 
H 5 HOH   52  352 2   HOH   HOH A . 
H 5 HOH   53  353 225 HOH   HOH A . 
H 5 HOH   54  354 55  HOH   HOH A . 
H 5 HOH   55  355 24  HOH   HOH A . 
H 5 HOH   56  356 173 HOH   HOH A . 
H 5 HOH   57  357 68  HOH   HOH A . 
H 5 HOH   58  358 175 HOH   HOH A . 
H 5 HOH   59  359 124 HOH   HOH A . 
H 5 HOH   60  360 267 HOH   HOH A . 
H 5 HOH   61  361 156 HOH   HOH A . 
H 5 HOH   62  362 298 HOH   HOH A . 
H 5 HOH   63  363 105 HOH   HOH A . 
H 5 HOH   64  364 187 HOH   HOH A . 
H 5 HOH   65  365 76  HOH   HOH A . 
H 5 HOH   66  366 25  HOH   HOH A . 
H 5 HOH   67  367 388 HOH   HOH A . 
H 5 HOH   68  368 5   HOH   HOH A . 
H 5 HOH   69  369 356 HOH   HOH A . 
H 5 HOH   70  370 273 HOH   HOH A . 
H 5 HOH   71  371 383 HOH   HOH A . 
H 5 HOH   72  372 53  HOH   HOH A . 
H 5 HOH   73  373 107 HOH   HOH A . 
H 5 HOH   74  374 227 HOH   HOH A . 
H 5 HOH   75  375 41  HOH   HOH A . 
H 5 HOH   76  376 48  HOH   HOH A . 
H 5 HOH   77  377 75  HOH   HOH A . 
H 5 HOH   78  378 255 HOH   HOH A . 
H 5 HOH   79  379 61  HOH   HOH A . 
H 5 HOH   80  380 206 HOH   HOH A . 
H 5 HOH   81  381 163 HOH   HOH A . 
H 5 HOH   82  382 39  HOH   HOH A . 
H 5 HOH   83  383 23  HOH   HOH A . 
H 5 HOH   84  384 112 HOH   HOH A . 
H 5 HOH   85  385 80  HOH   HOH A . 
H 5 HOH   86  386 177 HOH   HOH A . 
H 5 HOH   87  387 100 HOH   HOH A . 
H 5 HOH   88  388 233 HOH   HOH A . 
H 5 HOH   89  389 211 HOH   HOH A . 
H 5 HOH   90  390 12  HOH   HOH A . 
H 5 HOH   91  391 171 HOH   HOH A . 
H 5 HOH   92  392 239 HOH   HOH A . 
H 5 HOH   93  393 205 HOH   HOH A . 
H 5 HOH   94  394 363 HOH   HOH A . 
H 5 HOH   95  395 60  HOH   HOH A . 
H 5 HOH   96  396 179 HOH   HOH A . 
H 5 HOH   97  397 323 HOH   HOH A . 
H 5 HOH   98  398 96  HOH   HOH A . 
H 5 HOH   99  399 216 HOH   HOH A . 
H 5 HOH   100 400 34  HOH   HOH A . 
H 5 HOH   101 401 56  HOH   HOH A . 
H 5 HOH   102 402 185 HOH   HOH A . 
H 5 HOH   103 403 327 HOH   HOH A . 
H 5 HOH   104 404 188 HOH   HOH A . 
H 5 HOH   105 405 359 HOH   HOH A . 
H 5 HOH   106 406 130 HOH   HOH A . 
H 5 HOH   107 407 95  HOH   HOH A . 
H 5 HOH   108 408 322 HOH   HOH A . 
H 5 HOH   109 409 128 HOH   HOH A . 
H 5 HOH   110 410 291 HOH   HOH A . 
H 5 HOH   111 411 258 HOH   HOH A . 
H 5 HOH   112 412 186 HOH   HOH A . 
H 5 HOH   113 413 157 HOH   HOH A . 
H 5 HOH   114 414 30  HOH   HOH A . 
H 5 HOH   115 415 28  HOH   HOH A . 
H 5 HOH   116 416 223 HOH   HOH A . 
H 5 HOH   117 417 208 HOH   HOH A . 
H 5 HOH   118 418 305 HOH   HOH A . 
H 5 HOH   119 419 257 HOH   HOH A . 
H 5 HOH   120 420 101 HOH   HOH A . 
H 5 HOH   121 421 224 HOH   HOH A . 
H 5 HOH   122 422 337 HOH   HOH A . 
H 5 HOH   123 423 343 HOH   HOH A . 
H 5 HOH   124 424 212 HOH   HOH A . 
H 5 HOH   125 425 22  HOH   HOH A . 
H 5 HOH   126 426 77  HOH   HOH A . 
H 5 HOH   127 427 366 HOH   HOH A . 
H 5 HOH   128 428 294 HOH   HOH A . 
H 5 HOH   129 429 137 HOH   HOH A . 
H 5 HOH   130 430 7   HOH   HOH A . 
H 5 HOH   131 431 50  HOH   HOH A . 
H 5 HOH   132 432 150 HOH   HOH A . 
H 5 HOH   133 433 346 HOH   HOH A . 
H 5 HOH   134 434 248 HOH   HOH A . 
H 5 HOH   135 435 180 HOH   HOH A . 
H 5 HOH   136 436 335 HOH   HOH A . 
H 5 HOH   137 437 27  HOH   HOH A . 
H 5 HOH   138 438 330 HOH   HOH A . 
H 5 HOH   139 439 123 HOH   HOH A . 
H 5 HOH   140 440 172 HOH   HOH A . 
H 5 HOH   141 441 73  HOH   HOH A . 
H 5 HOH   142 442 11  HOH   HOH A . 
H 5 HOH   143 443 384 HOH   HOH A . 
H 5 HOH   144 444 230 HOH   HOH A . 
H 5 HOH   145 445 167 HOH   HOH A . 
H 5 HOH   146 446 8   HOH   HOH A . 
H 5 HOH   147 447 65  HOH   HOH A . 
H 5 HOH   148 448 321 HOH   HOH A . 
H 5 HOH   149 449 52  HOH   HOH A . 
H 5 HOH   150 450 170 HOH   HOH A . 
H 5 HOH   151 451 86  HOH   HOH A . 
H 5 HOH   152 452 203 HOH   HOH A . 
H 5 HOH   153 453 331 HOH   HOH A . 
H 5 HOH   154 454 293 HOH   HOH A . 
H 5 HOH   155 455 256 HOH   HOH A . 
H 5 HOH   156 456 263 HOH   HOH A . 
H 5 HOH   157 457 162 HOH   HOH A . 
H 5 HOH   158 458 354 HOH   HOH A . 
H 5 HOH   159 459 102 HOH   HOH A . 
H 5 HOH   160 460 350 HOH   HOH A . 
H 5 HOH   161 461 269 HOH   HOH A . 
H 5 HOH   162 462 238 HOH   HOH A . 
H 5 HOH   163 463 360 HOH   HOH A . 
H 5 HOH   164 464 315 HOH   HOH A . 
H 5 HOH   165 465 351 HOH   HOH A . 
H 5 HOH   166 466 389 HOH   HOH A . 
H 5 HOH   167 467 316 HOH   HOH A . 
H 5 HOH   168 468 374 HOH   HOH A . 
H 5 HOH   169 469 309 HOH   HOH A . 
H 5 HOH   170 470 306 HOH   HOH A . 
H 5 HOH   171 471 285 HOH   HOH A . 
H 5 HOH   172 472 382 HOH   HOH A . 
H 5 HOH   173 473 226 HOH   HOH A . 
H 5 HOH   174 474 378 HOH   HOH A . 
H 5 HOH   175 475 190 HOH   HOH A . 
H 5 HOH   176 476 301 HOH   HOH A . 
H 5 HOH   177 477 182 HOH   HOH A . 
H 5 HOH   178 478 387 HOH   HOH A . 
H 5 HOH   179 479 375 HOH   HOH A . 
H 5 HOH   180 480 296 HOH   HOH A . 
H 5 HOH   181 481 222 HOH   HOH A . 
H 5 HOH   182 482 272 HOH   HOH A . 
H 5 HOH   183 483 195 HOH   HOH A . 
H 5 HOH   184 484 280 HOH   HOH A . 
H 5 HOH   185 485 231 HOH   HOH A . 
H 5 HOH   186 486 120 HOH   HOH A . 
H 5 HOH   187 487 372 HOH   HOH A . 
H 5 HOH   188 488 115 HOH   HOH A . 
H 5 HOH   189 489 313 HOH   HOH A . 
H 5 HOH   190 490 318 HOH   HOH A . 
H 5 HOH   191 491 283 HOH   HOH A . 
H 5 HOH   192 492 390 HOH   HOH A . 
H 5 HOH   193 493 251 HOH   HOH A . 
H 5 HOH   194 494 268 HOH   HOH A . 
H 5 HOH   195 495 207 HOH   HOH A . 
I 5 HOH   1   301 292 HOH   HOH C . 
I 5 HOH   2   302 287 HOH   HOH C . 
I 5 HOH   3   303 370 HOH   HOH C . 
I 5 HOH   4   304 122 HOH   HOH C . 
I 5 HOH   5   305 85  HOH   HOH C . 
I 5 HOH   6   306 126 HOH   HOH C . 
I 5 HOH   7   307 311 HOH   HOH C . 
I 5 HOH   8   308 70  HOH   HOH C . 
I 5 HOH   9   309 334 HOH   HOH C . 
I 5 HOH   10  310 284 HOH   HOH C . 
I 5 HOH   11  311 36  HOH   HOH C . 
I 5 HOH   12  312 4   HOH   HOH C . 
I 5 HOH   13  313 43  HOH   HOH C . 
I 5 HOH   14  314 342 HOH   HOH C . 
I 5 HOH   15  315 253 HOH   HOH C . 
I 5 HOH   16  316 234 HOH   HOH C . 
I 5 HOH   17  317 310 HOH   HOH C . 
I 5 HOH   18  318 202 HOH   HOH C . 
I 5 HOH   19  319 218 HOH   HOH C . 
I 5 HOH   20  320 131 HOH   HOH C . 
I 5 HOH   21  321 46  HOH   HOH C . 
I 5 HOH   22  322 299 HOH   HOH C . 
I 5 HOH   23  323 117 HOH   HOH C . 
I 5 HOH   24  324 184 HOH   HOH C . 
I 5 HOH   25  325 72  HOH   HOH C . 
I 5 HOH   26  326 151 HOH   HOH C . 
I 5 HOH   27  327 136 HOH   HOH C . 
I 5 HOH   28  328 141 HOH   HOH C . 
I 5 HOH   29  329 339 HOH   HOH C . 
I 5 HOH   30  330 196 HOH   HOH C . 
I 5 HOH   31  331 17  HOH   HOH C . 
I 5 HOH   32  332 198 HOH   HOH C . 
I 5 HOH   33  333 110 HOH   HOH C . 
I 5 HOH   34  334 54  HOH   HOH C . 
I 5 HOH   35  335 35  HOH   HOH C . 
I 5 HOH   36  336 10  HOH   HOH C . 
I 5 HOH   37  337 1   HOH   HOH C . 
I 5 HOH   38  338 279 HOH   HOH C . 
I 5 HOH   39  339 143 HOH   HOH C . 
I 5 HOH   40  340 307 HOH   HOH C . 
I 5 HOH   41  341 271 HOH   HOH C . 
I 5 HOH   42  342 181 HOH   HOH C . 
I 5 HOH   43  343 164 HOH   HOH C . 
I 5 HOH   44  344 183 HOH   HOH C . 
I 5 HOH   45  345 348 HOH   HOH C . 
I 5 HOH   46  346 13  HOH   HOH C . 
I 5 HOH   47  347 51  HOH   HOH C . 
I 5 HOH   48  348 87  HOH   HOH C . 
I 5 HOH   49  349 345 HOH   HOH C . 
I 5 HOH   50  350 88  HOH   HOH C . 
I 5 HOH   51  351 45  HOH   HOH C . 
I 5 HOH   52  352 220 HOH   HOH C . 
I 5 HOH   53  353 64  HOH   HOH C . 
I 5 HOH   54  354 108 HOH   HOH C . 
I 5 HOH   55  355 125 HOH   HOH C . 
I 5 HOH   56  356 169 HOH   HOH C . 
I 5 HOH   57  357 74  HOH   HOH C . 
I 5 HOH   58  358 217 HOH   HOH C . 
I 5 HOH   59  359 58  HOH   HOH C . 
I 5 HOH   60  360 139 HOH   HOH C . 
I 5 HOH   61  361 89  HOH   HOH C . 
I 5 HOH   62  362 106 HOH   HOH C . 
I 5 HOH   63  363 145 HOH   HOH C . 
I 5 HOH   64  364 277 HOH   HOH C . 
I 5 HOH   65  365 249 HOH   HOH C . 
I 5 HOH   66  366 79  HOH   HOH C . 
I 5 HOH   67  367 98  HOH   HOH C . 
I 5 HOH   68  368 361 HOH   HOH C . 
I 5 HOH   69  369 154 HOH   HOH C . 
I 5 HOH   70  370 221 HOH   HOH C . 
I 5 HOH   71  371 176 HOH   HOH C . 
I 5 HOH   72  372 57  HOH   HOH C . 
I 5 HOH   73  373 133 HOH   HOH C . 
I 5 HOH   74  374 219 HOH   HOH C . 
I 5 HOH   75  375 347 HOH   HOH C . 
I 5 HOH   76  376 40  HOH   HOH C . 
I 5 HOH   77  377 129 HOH   HOH C . 
I 5 HOH   78  378 153 HOH   HOH C . 
I 5 HOH   79  379 326 HOH   HOH C . 
I 5 HOH   80  380 14  HOH   HOH C . 
I 5 HOH   81  381 59  HOH   HOH C . 
I 5 HOH   82  382 355 HOH   HOH C . 
I 5 HOH   83  383 165 HOH   HOH C . 
I 5 HOH   84  384 243 HOH   HOH C . 
I 5 HOH   85  385 62  HOH   HOH C . 
I 5 HOH   86  386 15  HOH   HOH C . 
I 5 HOH   87  387 340 HOH   HOH C . 
I 5 HOH   88  388 200 HOH   HOH C . 
I 5 HOH   89  389 209 HOH   HOH C . 
I 5 HOH   90  390 114 HOH   HOH C . 
I 5 HOH   91  391 29  HOH   HOH C . 
I 5 HOH   92  392 32  HOH   HOH C . 
I 5 HOH   93  393 159 HOH   HOH C . 
I 5 HOH   94  394 16  HOH   HOH C . 
I 5 HOH   95  395 328 HOH   HOH C . 
I 5 HOH   96  396 94  HOH   HOH C . 
I 5 HOH   97  397 47  HOH   HOH C . 
I 5 HOH   98  398 38  HOH   HOH C . 
I 5 HOH   99  399 336 HOH   HOH C . 
I 5 HOH   100 400 31  HOH   HOH C . 
I 5 HOH   101 401 49  HOH   HOH C . 
I 5 HOH   102 402 26  HOH   HOH C . 
I 5 HOH   103 403 197 HOH   HOH C . 
I 5 HOH   104 404 229 HOH   HOH C . 
I 5 HOH   105 405 266 HOH   HOH C . 
I 5 HOH   106 406 116 HOH   HOH C . 
I 5 HOH   107 407 333 HOH   HOH C . 
I 5 HOH   108 408 178 HOH   HOH C . 
I 5 HOH   109 409 215 HOH   HOH C . 
I 5 HOH   110 410 81  HOH   HOH C . 
I 5 HOH   111 411 71  HOH   HOH C . 
I 5 HOH   112 412 99  HOH   HOH C . 
I 5 HOH   113 413 289 HOH   HOH C . 
I 5 HOH   114 414 274 HOH   HOH C . 
I 5 HOH   115 415 161 HOH   HOH C . 
I 5 HOH   116 416 140 HOH   HOH C . 
I 5 HOH   117 417 245 HOH   HOH C . 
I 5 HOH   118 418 66  HOH   HOH C . 
I 5 HOH   119 419 341 HOH   HOH C . 
I 5 HOH   120 420 69  HOH   HOH C . 
I 5 HOH   121 421 237 HOH   HOH C . 
I 5 HOH   122 422 33  HOH   HOH C . 
I 5 HOH   123 423 19  HOH   HOH C . 
I 5 HOH   124 424 235 HOH   HOH C . 
I 5 HOH   125 425 138 HOH   HOH C . 
I 5 HOH   126 426 37  HOH   HOH C . 
I 5 HOH   127 427 281 HOH   HOH C . 
I 5 HOH   128 428 297 HOH   HOH C . 
I 5 HOH   129 429 365 HOH   HOH C . 
I 5 HOH   130 430 127 HOH   HOH C . 
I 5 HOH   131 431 367 HOH   HOH C . 
I 5 HOH   132 432 236 HOH   HOH C . 
I 5 HOH   133 433 290 HOH   HOH C . 
I 5 HOH   134 434 113 HOH   HOH C . 
I 5 HOH   135 435 369 HOH   HOH C . 
I 5 HOH   136 436 204 HOH   HOH C . 
I 5 HOH   137 437 174 HOH   HOH C . 
I 5 HOH   138 438 63  HOH   HOH C . 
I 5 HOH   139 439 44  HOH   HOH C . 
I 5 HOH   140 440 324 HOH   HOH C . 
I 5 HOH   141 441 20  HOH   HOH C . 
I 5 HOH   142 442 282 HOH   HOH C . 
I 5 HOH   143 443 160 HOH   HOH C . 
I 5 HOH   144 444 147 HOH   HOH C . 
I 5 HOH   145 445 349 HOH   HOH C . 
I 5 HOH   146 446 192 HOH   HOH C . 
I 5 HOH   147 447 134 HOH   HOH C . 
I 5 HOH   148 448 21  HOH   HOH C . 
I 5 HOH   149 449 325 HOH   HOH C . 
I 5 HOH   150 450 82  HOH   HOH C . 
I 5 HOH   151 451 250 HOH   HOH C . 
I 5 HOH   152 452 317 HOH   HOH C . 
I 5 HOH   153 453 300 HOH   HOH C . 
I 5 HOH   154 454 319 HOH   HOH C . 
I 5 HOH   155 455 149 HOH   HOH C . 
I 5 HOH   156 456 391 HOH   HOH C . 
I 5 HOH   157 457 376 HOH   HOH C . 
I 5 HOH   158 458 119 HOH   HOH C . 
I 5 HOH   159 459 109 HOH   HOH C . 
I 5 HOH   160 460 84  HOH   HOH C . 
I 5 HOH   161 461 286 HOH   HOH C . 
I 5 HOH   162 462 104 HOH   HOH C . 
I 5 HOH   163 463 189 HOH   HOH C . 
I 5 HOH   164 464 262 HOH   HOH C . 
I 5 HOH   165 465 276 HOH   HOH C . 
I 5 HOH   166 466 210 HOH   HOH C . 
I 5 HOH   167 467 199 HOH   HOH C . 
I 5 HOH   168 468 373 HOH   HOH C . 
I 5 HOH   169 469 228 HOH   HOH C . 
I 5 HOH   170 470 142 HOH   HOH C . 
I 5 HOH   171 471 385 HOH   HOH C . 
I 5 HOH   172 472 214 HOH   HOH C . 
I 5 HOH   173 473 191 HOH   HOH C . 
I 5 HOH   174 474 304 HOH   HOH C . 
I 5 HOH   175 475 83  HOH   HOH C . 
I 5 HOH   176 476 254 HOH   HOH C . 
I 5 HOH   177 477 270 HOH   HOH C . 
I 5 HOH   178 478 295 HOH   HOH C . 
I 5 HOH   179 479 201 HOH   HOH C . 
I 5 HOH   180 480 166 HOH   HOH C . 
I 5 HOH   181 481 252 HOH   HOH C . 
I 5 HOH   182 482 264 HOH   HOH C . 
I 5 HOH   183 483 278 HOH   HOH C . 
I 5 HOH   184 484 265 HOH   HOH C . 
I 5 HOH   185 485 303 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           7I36 
_cell.length_a           86.763 
_cell.length_b           57.039 
_cell.length_c           64.885 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.78 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I36 
_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          7I36 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.13 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_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                     7I36 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.21 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   85913 
_reflns.percent_possible_obs         76.9 
_reflns.pdbx_Rmerge_I_obs            0.036 
_reflns.pdbx_netI_over_sigmaI        27.7 
_reflns.pdbx_redundancy              5.2 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     449790 
_reflns.pdbx_chi_squared             1.05 
_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                  1.15 
_reflns_shell.d_res_low                   1.17 
_reflns_shell.number_measured_all         323 
_reflns_shell.number_unique_obs           322 
_reflns_shell.Rmerge_I_obs                0.342 
_reflns_shell.pdbx_chi_squared            0.00 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        5.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             0.647 
_reflns_shell.pdbx_Rpim_I_all             0.342 
_reflns_shell.pdbx_CC_half                0.760 
_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                                 7I36 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     85873 
_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                             16.55 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    76.8 
_refine.ls_R_factor_obs                          0.1819 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1811 
_refine.ls_R_factor_R_free                       0.1972 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_number_reflns_R_free                  4307 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.B_iso_mean                               19.77 
_refine.aniso_B[1][1]                            -0.95560 
_refine.aniso_B[2][2]                            0.28910 
_refine.aniso_B[3][3]                            0.66650 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.43780 
_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             0.042 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.043 
_refine.pdbx_overall_SU_R_Blow_DPI               0.045 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.045 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I36 
_refine_analyze.Luzzati_coordinate_error_obs    0.15 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             380 
_refine_hist.number_atoms_total               2573 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.55 
# 
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                  0.014 ? 2.00  2264 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.14  ? 2.00  3085 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  758  '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  404  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2264 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.10  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.39 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  2086 '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                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1628 
_refine_ls_shell.R_factor_R_work                  0.3024 
_refine_ls_shell.percent_reflns_obs               12.44 
_refine_ls_shell.R_factor_R_free                  0.2946 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.24 
_refine_ls_shell.number_reflns_R_free             90 
_refine_ls_shell.number_reflns_all                1718 
_refine_ls_shell.R_factor_all                     0.3020 
# 
_struct.entry_id                  7I36 
_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-0032509-001 (A71EV2A-x3621)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I36 
_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 3 ? 
G N N 4 ? 
H N N 5 ? 
I 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 7I36 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I36 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,H 
2 1 B,F,G,I   
# 
_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 ? ? ? ? ? ? ? 2.390 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
# 
_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_555 108.6 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.4 ? 
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_555 117.6 ? 
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_555 103.5 ? 
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_555 102.7 ? 
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_555 117.9 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.3 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.9 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.4 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.6 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.3 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O 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                   7I36 
_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   A HOH 311 ? ? O A HOH 394 ? ? 1.40 
2 1 O   A HOH 369 ? ? O A HOH 442 ? ? 1.62 
3 1 O   C HOH 377 ? ? O C HOH 435 ? ? 1.73 
4 1 O   C HOH 329 ? ? O C HOH 373 ? ? 1.80 
5 1 O   C HOH 367 ? ? O C HOH 382 ? ? 1.96 
6 1 OE1 A GLN 95  ? ? O A HOH 301 ? ? 1.99 
7 1 O   A HOH 337 ? ? O A HOH 436 ? ? 2.12 
8 1 O   C HOH 309 ? ? O C HOH 408 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 125 ? ? -131.93 -30.34 
2 1 SER C 125 ? ? -134.24 -30.12 
# 
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 15.0003 8.1925   14.4312 -0.0218 -0.0141 0.0032 0.0119 0.0015  0.0095 1.7024 0.9411 0.8085 1.1560  
-0.8005 -0.5369 0.0103  0.0844 0.1444 0.0616 0.0666 0.0431 -0.0334 -0.0827 -0.0769 
'X-RAY DIFFRACTION' 2 ? refined 25.8072 -20.1798 17.7553 -0.0244 -0.0095 0.0174 0.0106 -0.0009 0.0210 0.7373 0.9827 0.1891 -0.3281 
-0.1732 -0.0690 -0.0029 0.0172 0.1333 0.0368 0.0503 0.0079 0.0422  -0.0009 -0.0474 
# 
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 ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 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 
A1B09 C4   C  Y N 1   
A1B09 C5   C  Y N 2   
A1B09 C6   C  Y N 3   
A1B09 C7   C  N N 4   
A1B09 C8   C  N N 5   
A1B09 C10  C  N N 6   
A1B09 O1   O  N N 7   
A1B09 N    N  N N 8   
A1B09 C12  C  N N 9   
A1B09 C11  C  N R 10  
A1B09 O2   O  N N 11  
A1B09 C9   C  N N 12  
A1B09 C1   C  Y N 13  
A1B09 O    O  N N 14  
A1B09 C    C  N N 15  
A1B09 C3   C  Y N 16  
A1B09 C2   C  Y N 17  
A1B09 H6   H  N N 18  
A1B09 H7   H  N N 19  
A1B09 H8   H  N N 20  
A1B09 H9   H  N N 21  
A1B09 H12  H  N N 22  
A1B09 H13  H  N N 23  
A1B09 H15  H  N N 24  
A1B09 H16  H  N N 25  
A1B09 H    H  N N 26  
A1B09 H14  H  N N 27  
A1B09 H10  H  N N 28  
A1B09 H11  H  N N 29  
A1B09 H2   H  N N 30  
A1B09 H1   H  N N 31  
A1B09 H3   H  N N 32  
A1B09 H5   H  N N 33  
A1B09 H4   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
DMS   S    S  N N 122 
DMS   O    O  N N 123 
DMS   C1   C  N N 124 
DMS   C2   C  N N 125 
DMS   H11  H  N N 126 
DMS   H12  H  N N 127 
DMS   H13  H  N N 128 
DMS   H21  H  N N 129 
DMS   H22  H  N N 130 
DMS   H23  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
HIS   N    N  N N 181 
HIS   CA   C  N S 182 
HIS   C    C  N N 183 
HIS   O    O  N N 184 
HIS   CB   C  N N 185 
HIS   CG   C  Y N 186 
HIS   ND1  N  Y N 187 
HIS   CD2  C  Y N 188 
HIS   CE1  C  Y N 189 
HIS   NE2  N  Y N 190 
HIS   OXT  O  N N 191 
HIS   H    H  N N 192 
HIS   H2   H  N N 193 
HIS   HA   H  N N 194 
HIS   HB2  H  N N 195 
HIS   HB3  H  N N 196 
HIS   HD1  H  N N 197 
HIS   HD2  H  N N 198 
HIS   HE1  H  N N 199 
HIS   HE2  H  N N 200 
HIS   HXT  H  N N 201 
HOH   O    O  N N 202 
HOH   H1   H  N N 203 
HOH   H2   H  N N 204 
ILE   N    N  N N 205 
ILE   CA   C  N S 206 
ILE   C    C  N N 207 
ILE   O    O  N N 208 
ILE   CB   C  N S 209 
ILE   CG1  C  N N 210 
ILE   CG2  C  N N 211 
ILE   CD1  C  N N 212 
ILE   OXT  O  N N 213 
ILE   H    H  N N 214 
ILE   H2   H  N N 215 
ILE   HA   H  N N 216 
ILE   HB   H  N N 217 
ILE   HG12 H  N N 218 
ILE   HG13 H  N N 219 
ILE   HG21 H  N N 220 
ILE   HG22 H  N N 221 
ILE   HG23 H  N N 222 
ILE   HD11 H  N N 223 
ILE   HD12 H  N N 224 
ILE   HD13 H  N N 225 
ILE   HXT  H  N N 226 
LEU   N    N  N N 227 
LEU   CA   C  N S 228 
LEU   C    C  N N 229 
LEU   O    O  N N 230 
LEU   CB   C  N N 231 
LEU   CG   C  N N 232 
LEU   CD1  C  N N 233 
LEU   CD2  C  N N 234 
LEU   OXT  O  N N 235 
LEU   H    H  N N 236 
LEU   H2   H  N N 237 
LEU   HA   H  N N 238 
LEU   HB2  H  N N 239 
LEU   HB3  H  N N 240 
LEU   HG   H  N N 241 
LEU   HD11 H  N N 242 
LEU   HD12 H  N N 243 
LEU   HD13 H  N N 244 
LEU   HD21 H  N N 245 
LEU   HD22 H  N N 246 
LEU   HD23 H  N N 247 
LEU   HXT  H  N N 248 
LYS   N    N  N N 249 
LYS   CA   C  N S 250 
LYS   C    C  N N 251 
LYS   O    O  N N 252 
LYS   CB   C  N N 253 
LYS   CG   C  N N 254 
LYS   CD   C  N N 255 
LYS   CE   C  N N 256 
LYS   NZ   N  N N 257 
LYS   OXT  O  N N 258 
LYS   H    H  N N 259 
LYS   H2   H  N N 260 
LYS   HA   H  N N 261 
LYS   HB2  H  N N 262 
LYS   HB3  H  N N 263 
LYS   HG2  H  N N 264 
LYS   HG3  H  N N 265 
LYS   HD2  H  N N 266 
LYS   HD3  H  N N 267 
LYS   HE2  H  N N 268 
LYS   HE3  H  N N 269 
LYS   HZ1  H  N N 270 
LYS   HZ2  H  N N 271 
LYS   HZ3  H  N N 272 
LYS   HXT  H  N N 273 
MET   N    N  N N 274 
MET   CA   C  N S 275 
MET   C    C  N N 276 
MET   O    O  N N 277 
MET   CB   C  N N 278 
MET   CG   C  N N 279 
MET   SD   S  N N 280 
MET   CE   C  N N 281 
MET   OXT  O  N N 282 
MET   H    H  N N 283 
MET   H2   H  N N 284 
MET   HA   H  N N 285 
MET   HB2  H  N N 286 
MET   HB3  H  N N 287 
MET   HG2  H  N N 288 
MET   HG3  H  N N 289 
MET   HE1  H  N N 290 
MET   HE2  H  N N 291 
MET   HE3  H  N N 292 
MET   HXT  H  N N 293 
PHE   N    N  N N 294 
PHE   CA   C  N S 295 
PHE   C    C  N N 296 
PHE   O    O  N N 297 
PHE   CB   C  N N 298 
PHE   CG   C  Y N 299 
PHE   CD1  C  Y N 300 
PHE   CD2  C  Y N 301 
PHE   CE1  C  Y N 302 
PHE   CE2  C  Y N 303 
PHE   CZ   C  Y N 304 
PHE   OXT  O  N N 305 
PHE   H    H  N N 306 
PHE   H2   H  N N 307 
PHE   HA   H  N N 308 
PHE   HB2  H  N N 309 
PHE   HB3  H  N N 310 
PHE   HD1  H  N N 311 
PHE   HD2  H  N N 312 
PHE   HE1  H  N N 313 
PHE   HE2  H  N N 314 
PHE   HZ   H  N N 315 
PHE   HXT  H  N N 316 
PRO   N    N  N N 317 
PRO   CA   C  N S 318 
PRO   C    C  N N 319 
PRO   O    O  N N 320 
PRO   CB   C  N N 321 
PRO   CG   C  N N 322 
PRO   CD   C  N N 323 
PRO   OXT  O  N N 324 
PRO   H    H  N N 325 
PRO   HA   H  N N 326 
PRO   HB2  H  N N 327 
PRO   HB3  H  N N 328 
PRO   HG2  H  N N 329 
PRO   HG3  H  N N 330 
PRO   HD2  H  N N 331 
PRO   HD3  H  N N 332 
PRO   HXT  H  N N 333 
SER   N    N  N N 334 
SER   CA   C  N S 335 
SER   C    C  N N 336 
SER   O    O  N N 337 
SER   CB   C  N N 338 
SER   OG   O  N N 339 
SER   OXT  O  N N 340 
SER   H    H  N N 341 
SER   H2   H  N N 342 
SER   HA   H  N N 343 
SER   HB2  H  N N 344 
SER   HB3  H  N N 345 
SER   HG   H  N N 346 
SER   HXT  H  N N 347 
THR   N    N  N N 348 
THR   CA   C  N S 349 
THR   C    C  N N 350 
THR   O    O  N N 351 
THR   CB   C  N R 352 
THR   OG1  O  N N 353 
THR   CG2  C  N N 354 
THR   OXT  O  N N 355 
THR   H    H  N N 356 
THR   H2   H  N N 357 
THR   HA   H  N N 358 
THR   HB   H  N N 359 
THR   HG1  H  N N 360 
THR   HG21 H  N N 361 
THR   HG22 H  N N 362 
THR   HG23 H  N N 363 
THR   HXT  H  N N 364 
TRP   N    N  N N 365 
TRP   CA   C  N S 366 
TRP   C    C  N N 367 
TRP   O    O  N N 368 
TRP   CB   C  N N 369 
TRP   CG   C  Y N 370 
TRP   CD1  C  Y N 371 
TRP   CD2  C  Y N 372 
TRP   NE1  N  Y N 373 
TRP   CE2  C  Y N 374 
TRP   CE3  C  Y N 375 
TRP   CZ2  C  Y N 376 
TRP   CZ3  C  Y N 377 
TRP   CH2  C  Y N 378 
TRP   OXT  O  N N 379 
TRP   H    H  N N 380 
TRP   H2   H  N N 381 
TRP   HA   H  N N 382 
TRP   HB2  H  N N 383 
TRP   HB3  H  N N 384 
TRP   HD1  H  N N 385 
TRP   HE1  H  N N 386 
TRP   HE3  H  N N 387 
TRP   HZ2  H  N N 388 
TRP   HZ3  H  N N 389 
TRP   HH2  H  N N 390 
TRP   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
ZN    ZN   ZN N N 435 
# 
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 
A1B09 C   O    sing N N 1   
A1B09 O   C1   sing N N 2   
A1B09 C1  C2   doub Y N 3   
A1B09 C2  C3   sing Y N 4   
A1B09 C3  C4   doub Y N 5   
A1B09 C4  C5   sing Y N 6   
A1B09 C5  C6   doub Y N 7   
A1B09 C1  C6   sing Y N 8   
A1B09 C6  C7   sing N N 9   
A1B09 C7  C8   sing N N 10  
A1B09 C8  O1   doub N N 11  
A1B09 N   C8   sing N N 12  
A1B09 N   C9   sing N N 13  
A1B09 C9  C10  sing N N 14  
A1B09 C10 C11  sing N N 15  
A1B09 O2  C11  sing N N 16  
A1B09 C11 C12  sing N N 17  
A1B09 C12 N    sing N N 18  
A1B09 C4  H6   sing N N 19  
A1B09 C5  H7   sing N N 20  
A1B09 C7  H8   sing N N 21  
A1B09 C7  H9   sing N N 22  
A1B09 C10 H12  sing N N 23  
A1B09 C10 H13  sing N N 24  
A1B09 C12 H15  sing N N 25  
A1B09 C12 H16  sing N N 26  
A1B09 C11 H    sing N N 27  
A1B09 O2  H14  sing N N 28  
A1B09 C9  H10  sing N N 29  
A1B09 C9  H11  sing N N 30  
A1B09 C   H2   sing N N 31  
A1B09 C   H1   sing N N 32  
A1B09 C   H3   sing N N 33  
A1B09 C3  H5   sing N N 34  
A1B09 C2  H4   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_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                    7I36 
_atom_sites.fract_transf_matrix[1][1]   0.011526 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000964 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017532 
_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]   0.015466 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.707 8.078   24.822 1.00 16.44 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.964 8.168   24.047 1.00 15.83 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.097 6.970   23.114 1.00 15.80 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.365 5.980   23.288 1.00 15.92 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.144 8.201   25.024 1.00 18.28 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.236 6.969   25.711 1.00 21.50 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.020 7.036   22.156 1.00 14.47 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.271 5.929   21.235 1.00 13.49 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.670 6.400   19.858 1.00 12.09 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.356 7.517   19.468 1.00 13.58 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.345 5.561   19.142 1.00 11.19 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.826 5.896   17.798 1.00 11.63 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.795 4.686   16.896 1.00 11.48 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.701 3.538   17.371 1.00 12.48 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.275 6.414   17.917 1.00 13.05 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.868 4.922   15.593 1.00 10.80 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.091 3.874   14.582 1.00 10.47 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.555 3.965   14.176 1.00 11.83 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.053 5.069   13.892 1.00 11.98 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.223 4.081   13.328 1.00 10.80 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.733 4.240   13.678 1.00 12.31 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.416 2.888   12.347 1.00 12.53 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.937 4.816   12.471 1.00 13.19 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.264 2.835   14.150 1.00 11.35 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.674 2.800   13.752 1.00 12.48 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.786 1.973   12.480 1.00 13.09 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.778 0.728   12.544 1.00 14.02 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.551 2.211   14.885 1.00 13.75 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.595 3.101   16.100 1.00 13.10 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.477 4.181   16.172 1.00 14.71 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.764 2.872   17.186 1.00 15.36 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.467 5.060   17.269 1.00 14.97 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.776 3.720   18.307 1.00 15.64 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.600 4.838   18.314 1.00 15.81 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.630 5.708   19.407 1.00 18.57 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.822 2.626   11.328 1.00 12.69 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.903 1.988   10.017 1.00 13.32 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.134 2.490   9.304  1.00 14.83 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.377 3.710   9.251  1.00 13.81 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.602 2.256   9.187  1.00 14.71 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.261 3.755   9.098  1.00 15.54 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.745 1.647   7.801  1.00 16.52 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.992 1.579   8.808  1.00 15.82 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.240 2.006   8.165  1.00 16.19 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.065 2.883   9.096  1.00 15.13 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.182 2.584   10.296 1.00 15.66 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.539 4.039   8.575  1.00 14.66 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.236 5.023   9.422  1.00 14.32 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.327 6.206   9.727  1.00 13.56 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.820 7.343   9.856  1.00 13.86 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.598 5.466   8.847  1.00 16.16 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.657 4.406   8.964  1.00 19.72 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.399 4.323   9.951  1.00 21.99 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.690 3.527   8.005  1.00 18.94 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.052 5.927   9.975  1.00 12.85 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.089 6.960   10.330 1.00 12.15 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.429 6.629   11.680 1.00 11.86 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.147 5.444   12.002 1.00 12.36 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.975 7.038   9.254  1.00 13.04 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.477 7.442   7.890  1.00 13.85 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.143 8.653   7.693  1.00 15.07 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.281 6.616   6.798  1.00 16.06 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.606 9.024   6.429  1.00 15.77 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.701 6.998   5.524  1.00 17.12 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.347 8.204   5.344  1.00 17.60 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.803 8.582   4.085  1.00 22.06 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.082 7.688   12.422 1.00 11.20 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.287 7.615   13.652 1.00 11.16 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.068 8.491   13.413 1.00 10.87 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.219 9.702   13.124 1.00 11.57 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.112 8.168   14.854 1.00 12.09 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.338 8.488   16.111 1.00 12.98 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.268 8.871   17.283 1.00 14.35 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.716 9.937   18.125 1.00 14.97 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.039 9.745   19.250 1.00 15.89 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.749 8.505   19.659 1.00 17.38 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.593 10.784  19.947 1.00 16.19 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.871 7.889   13.467 1.00 10.31 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.601 8.609   13.243 1.00 10.05 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.925 8.821   14.576 1.00 11.07 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.619 7.827   15.272 1.00 11.80 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.669 7.821   12.298 1.00 10.52 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.449 8.680   11.948 1.00 11.32 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.369 7.331   11.021 1.00 11.97 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.679 10.082  14.936 1.00 9.92  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.059 10.413  16.234 0.50 10.48 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.107 10.387  16.244 0.50 12.30 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.970 11.411  16.056 1.00 10.73 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.821 12.047  14.976 1.00 12.12 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.087 11.020  17.250 0.50 10.45 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.285 10.982  17.112 0.50 16.05 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.999 9.943   17.793 0.50 11.60 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.868 11.333  18.524 0.50 16.44 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.828 12.263  16.664 0.50 7.15  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.459 10.040  17.177 0.50 18.47 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.133 11.583  17.097 1.00 10.85 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.139 12.667  17.062 1.00 11.48 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.947 13.993  17.062 1.00 12.04 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.882 14.164  17.869 1.00 12.17 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.266 12.672  18.332 1.00 11.72 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.404 11.435  18.425 1.00 12.14 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.815 10.431  19.042 1.00 12.80 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.237 11.478  17.810 1.00 12.97 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.553 14.930  16.174 1.00 11.94 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.310 16.216  16.119 1.00 12.42 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.266 16.897  17.488 1.00 14.43 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.287 17.452  17.918 1.00 14.99 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.700 17.100  15.054 1.00 13.08 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.482 18.422  14.809 1.00 13.28 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.723 19.282  13.814 1.00 15.38 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.465 20.485  13.381 1.00 16.57 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.450 21.643  14.030 1.00 17.64 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.845 21.746  15.209 1.00 18.40 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.060 22.718  13.507 1.00 19.29 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.115 16.779  18.202 1.00 13.77 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.013 17.486  19.480 1.00 16.05 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.883 16.902  20.599 1.00 15.86 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.983 17.513  21.675 1.00 18.65 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.539 17.643  19.934 1.00 17.60 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.877 16.384  20.429 1.00 16.03 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.237 15.516  19.568 1.00 15.62 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.691 15.941  21.699 1.00 17.56 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.698 14.548  20.328 1.00 16.43 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.936 14.770  21.617 1.00 17.29 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.409 15.671  20.410 1.00 15.98 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.285 14.984  21.370 1.00 15.09 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.755 14.930  20.914 1.00 16.19 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.585 14.325  21.567 1.00 16.90 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.765 13.582  21.687 1.00 15.24 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.369 13.589  22.297 1.00 15.61 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.926 12.129  22.560 1.00 16.70 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.336 14.397  23.652 1.00 17.67 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.089 15.578  19.774 1.00 15.15 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.471 15.544  19.267 1.00 15.01 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.445 16.192  20.229 1.00 16.27 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.129 17.230  20.832 1.00 16.57 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.540 16.265  17.913 1.00 14.92 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.610 15.577  20.372 1.00 15.25 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.666 16.098  21.279 1.00 15.36 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.602 17.092  20.561 1.00 16.41 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.560 17.238  19.323 1.00 14.96 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.530 14.909  21.769 1.00 17.16 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.270 14.377  20.653 1.00 17.65 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.700 13.811  22.464 1.00 18.34 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.530 17.750  21.307 1.00 16.17 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.521 18.588  20.667 1.00 16.39 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.357 17.782  19.689 1.00 15.40 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.649 18.253  18.597 1.00 15.72 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.454 19.241  21.719 1.00 18.16 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.716 19.876  21.110 1.00 24.68 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.663 21.055  20.370 1.00 28.58 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.978 19.365  20.991 1.00 28.66 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.907 21.333  20.011 1.00 29.78 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.737 20.312  20.291 1.00 30.91 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.738 16.525  20.064 1.00 15.28 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.535 15.722  19.148 1.00 15.54 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.764 15.445  17.841 1.00 13.78 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.352 15.489  16.761 1.00 14.91 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.984 14.386  19.764 1.00 17.22 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.945 13.665  18.841 1.00 24.43 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.100 14.100  18.653 1.00 28.17 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.476 12.590  18.192 1.00 25.80 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.427 15.210  17.942 1.00 13.50 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.635 15.041  16.715 1.00 13.14 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.692 16.298  15.814 1.00 12.50 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.912 16.189  14.599 1.00 12.67 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.171 14.761  17.056 1.00 13.25 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.907 13.400  17.652 1.00 14.24 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.555 12.414  17.202 1.00 14.83 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.073 13.319  18.586 1.00 14.62 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.491 17.479  16.411 1.00 12.84 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.531 18.734  15.626 1.00 13.19 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.937 18.997  15.055 1.00 12.61 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.029 19.554  13.955 1.00 13.28 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.072 19.913  16.521 1.00 13.62 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.570 19.973  16.653 1.00 13.54 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.830 19.691  17.761 1.00 15.41 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.637 20.425  15.653 1.00 14.00 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.488 19.916  17.513 1.00 15.18 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.340 20.349  16.213 1.00 14.73 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.782 20.874  14.331 1.00 15.57 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.192 20.751  15.496 1.00 16.16 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.658 21.183  13.608 1.00 16.12 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.401 21.193  14.195 1.00 17.09 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.001 18.572  15.761 1.00 12.64 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.359 18.797  15.282 1.00 13.52 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.781 17.791  14.202 1.00 14.38 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.821 17.952  13.575 1.00 15.86 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.319 18.745  16.469 1.00 15.98 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.976 16.719  13.991 1.00 13.83 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.269 15.673  12.980 1.00 14.21 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.999 15.505  12.126 1.00 13.49 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.608 14.373  11.783 1.00 13.68 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.666 14.346  13.678 1.00 15.82 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.010 14.530  14.341 1.00 16.64 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.044 14.468  13.667 1.00 19.93 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.029 14.820  15.652 1.00 16.72 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.352 16.598  11.788 1.00 12.99 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.041 16.553  11.144 1.00 12.24 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.097 16.101  9.698  1.00 13.28 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.959 16.550  8.917  1.00 15.13 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.468 17.988  11.191 1.00 13.10 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.070 18.125  10.596 1.00 13.96 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.048 17.352  11.444 1.00 14.07 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.644 19.606  10.526 1.00 16.36 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.180 15.219  9.296  1.00 12.20 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.016 14.815  7.903  1.00 13.02 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.771 15.519  7.323  1.00 13.08 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.807 16.077  6.216  1.00 14.90 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.900 13.279  7.801  1.00 12.48 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.529 12.874  6.347  1.00 15.02 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.199 12.598  8.265  1.00 14.55 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.626 15.481  8.043  1.00 13.09 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.359 16.029  7.534  1.00 12.83 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.408 16.230  8.691  1.00 13.37 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.442 15.445  9.660  1.00 12.68 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.754 15.015  6.504  1.00 14.12 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.339 15.286  6.061  1.00 15.12 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.923 16.140  5.071  1.00 17.37 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.148 14.678  6.587  1.00 14.91 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.550 16.081  4.945  1.00 18.80 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.053 15.181  5.851  1.00 16.93 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.903 13.741  7.594  1.00 15.67 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.728 14.739  6.080  1.00 18.03 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.608 13.287  7.792  1.00 16.71 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.539 13.806  7.072  1.00 18.37 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.567 17.265  8.633  1.00 14.20 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.561 17.461  9.667  1.00 14.30 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.334 18.099  9.053  1.00 15.45 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.457 18.904  8.098  1.00 16.08 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.084 18.286  10.837 1.00 16.29 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.681 19.652  10.472 1.00 17.23 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.719 20.828  10.282 1.00 17.81 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.077 21.800  9.555  1.00 18.91 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.613 20.808  10.872 1.00 17.11 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.162 17.806  9.614  1.00 14.50 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.916 18.368  9.116  1.00 14.78 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.952 18.533  10.291 1.00 14.68 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.413 17.554  10.849 1.00 14.69 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.312 17.452  8.018  1.00 16.45 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.051 17.948  7.366  1.00 19.36 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.203 18.484  8.075  1.00 22.78 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.879 17.708  6.160  1.00 25.67 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.725 19.794  10.683 1.00 15.67 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.870 20.134  11.805 0.50 16.26 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.881 20.074  11.831 0.50 17.45 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.422 19.692  11.582 1.00 17.23 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.786 19.170  12.511 1.00 18.24 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.929 21.639  12.051 0.50 16.61 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.030 21.529  12.261 0.50 21.34 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.001 22.004  13.055 0.50 16.52 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.716 22.373  11.171 0.50 27.61 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.919 19.823  10.348 1.00 17.79 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.537 19.407  10.054 1.00 18.61 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.286 17.918  10.229 1.00 16.94 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.149 17.513  10.476 1.00 18.30 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.108 19.813  8.648  1.00 20.97 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.650 19.007  7.622  1.00 26.29 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.342 17.096  10.163 1.00 15.14 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.270 15.633  10.355 1.00 15.53 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.738 15.181  11.751 1.00 14.68 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.658 13.982  12.056 1.00 14.15 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.139 14.927  9.294  1.00 15.62 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.592 15.099  7.870  1.00 17.86 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.473 14.437  6.825  1.00 17.59 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.380 12.971  6.957  1.00 14.99 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.545 12.119  5.955  1.00 16.35 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.798 12.565  4.722  1.00 18.76 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.385 10.808  6.152  1.00 16.40 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.296 16.089  12.577 1.00 13.86 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.934 15.770  13.848 1.00 13.41 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.100 14.767  13.684 1.00 12.56 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.314 13.925  14.565 1.00 12.73 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.933 15.266  14.903 1.00 15.13 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.542 15.045  16.286 1.00 14.36 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.389 15.882  16.739 1.00 15.38 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.155 14.044  16.969 1.00 15.42 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.896 14.885  12.600 1.00 12.43 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.991 13.928  12.380 1.00 11.48 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.340 14.656  12.259 1.00 11.46 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.427 15.770  11.675 1.00 12.36 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.749 13.130  11.100 1.00 11.52 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.676 12.015  11.153 1.00 13.05 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.589 11.302  9.818  1.00 14.45 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.941 11.001  12.290 1.00 14.10 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.379 13.997  12.726 1.00 11.06 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.762 14.448  12.518 1.00 10.98 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.600 13.217  12.377 1.00 10.75 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.416 12.198  13.076 1.00 10.86 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.218 15.307  13.730 1.00 11.74 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.650 15.882  13.633 1.00 12.02 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.755 17.236  14.331 1.00 13.97 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.686 14.940  14.267 1.00 11.87 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.565 13.298  11.442 1.00 10.90 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.511 12.207  11.173 1.00 10.61 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.920 12.721  11.341 1.00 11.00 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.252 13.773  10.751 1.00 11.84 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.284 11.622  9.754  1.00 10.66 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.312 10.527  9.468  1.00 12.20 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.839 11.097  9.612  1.00 12.03 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.731 12.024  12.111 1.00 10.35 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.151 12.361  12.292 1.00 11.04 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.012 11.198  11.834 1.00 12.07 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.536 10.054  11.608 1.00 12.31 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.424 12.733  13.745 1.00 12.48 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.095 11.668  14.622 1.00 12.99 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.300 11.468  11.640 1.00 13.07 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.239 10.432  11.191 1.00 14.31 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.860 9.699   12.385 1.00 15.79 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.045 10.305  13.464 1.00 18.16 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.329 11.036  10.299 1.00 16.80 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.038 11.999  11.070 1.00 19.40 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.208 8.398   12.203 1.00 16.27 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.792 7.605   13.273 1.00 17.87 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.130 7.024   12.832 1.00 19.91 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.350 6.776   11.638 1.00 18.78 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.852 6.422   13.664 1.00 18.67 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.724 5.512   12.576 1.00 19.16 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.451 6.885   14.069 1.00 18.83 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.989 6.747   13.813 1.00 21.22 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.267 6.110   13.520 1.00 22.54 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.062 4.597   13.308 1.00 22.56 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.583 4.040   12.335 1.00 25.24 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.278 6.427   14.647 1.00 26.42 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.769 5.917   15.871 1.00 31.57 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.512 7.901   14.792 1.00 26.82 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.243 3.966   14.163 1.00 22.78 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.971 2.528   14.049 1.00 23.39 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.754 2.234   13.133 1.00 22.17 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.797 3.004   13.140 1.00 21.12 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.673 1.964   15.430 1.00 26.28 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.730 1.098   12.443 1.00 21.04 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.595 0.688   11.599 1.00 21.44 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.497 0.078   12.451 1.00 20.82 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.775 -0.665  13.393 1.00 22.13 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.030 -0.336  10.542 1.00 24.51 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.890 0.286   9.427  1.00 30.09 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.294 -0.750  8.417  1.00 37.44 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.158 -1.602  8.681  1.00 37.64 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.635 -0.727  7.260  1.00 38.58 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.244 0.419   12.139 1.00 17.76 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.076 -0.073  12.858 1.00 17.87 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.496 -1.339  12.267 1.00 17.06 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.785 -1.704  11.125 1.00 17.89 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.542 -1.941  13.033 1.00 15.87 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.936 -3.235  12.676 1.00 16.13 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.489 -3.166  12.238 1.00 15.81 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.942 -4.209  11.838 1.00 16.63 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.085 -4.231  13.825 1.00 17.81 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.786 -4.646  14.213 1.00 21.76 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.831 -2.016  12.380 1.00 14.28 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.441 -1.916  11.958 1.00 13.79 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.369 -1.859  10.433 1.00 15.19 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.266 -1.295  9.790  1.00 16.72 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.812 -0.656  12.571 1.00 12.81 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.703 -0.714  14.083 1.00 14.38 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.336 -1.826  14.626 1.00 14.61 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.905 0.348   14.744 1.00 14.82 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.329 -2.388  9.869  1.00 16.20 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.027 -2.301  8.424  1.00 17.33 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.685 -1.567  8.256  1.00 15.80 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.791 -1.697  9.101  1.00 16.50 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.988 -3.656  7.776  1.00 21.70 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 20.963 -4.395  8.387  1.00 26.41 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.335 -4.380  7.933  1.00 23.23 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.571 -0.731  7.230  1.00 15.50 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.357 0.026   6.999  1.00 13.87 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.375 -0.746  6.123  1.00 15.14 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.750 -1.293  5.058  1.00 16.26 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.665 1.391   6.372  1.00 14.21 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.774 2.167   7.140  1.00 14.55 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.394 2.259   6.224  1.00 14.18 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.431 2.456   8.639  1.00 15.56 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.113 -0.777  6.504  1.00 13.48 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.051 -1.381  5.702  1.00 14.15 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.782 -0.532  4.441  1.00 14.69 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.781 0.719   4.473  1.00 15.20 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.769 -1.410  6.530  1.00 13.99 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.542 -1.230  3.305  1.00 16.59 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.223 -0.554  2.045  1.00 18.15 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.937 -1.239  1.588  1.00 20.93 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.006 -2.235  0.829  1.00 22.85 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.399 -0.691  1.027  1.00 19.58 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.722 -0.116  1.552  1.00 19.19 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.738 1.404   1.840  1.00 18.73 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.068 1.878   2.294  1.00 16.92 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.276 3.028   2.927  1.00 16.82 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.282 3.891   3.098  1.00 17.46 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.492 3.341   3.376  1.00 18.22 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.778 -0.664  2.008  1.00 20.68 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.452 -1.287  1.890  1.00 20.44 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.342 -0.279  2.203  1.00 20.84 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.540 0.858   2.609  1.00 23.42 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.416 -2.426  2.897  1.00 18.96 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.349 -1.842  4.614  1.00 18.77 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.044  -0.784  2.108  1.00 24.17 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.886  0.012   2.496  1.00 27.11 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.077  -0.714  3.596  1.00 25.92 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.845  -0.565  3.682  1.00 27.55 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.973  0.442   1.326  1.00 34.14 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.104  1.643   1.685  1.00 43.81 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 5.155  1.928   0.926  1.00 47.32 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 6.382  2.310   2.755  1.00 44.27 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.765  -1.464  4.502  1.00 21.92 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.075  -2.107  5.648  1.00 19.79 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.340  -1.058  6.472  1.00 20.50 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.801  0.087   6.649  1.00 19.94 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.067  -2.859  6.536  1.00 20.73 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.801  -4.380  5.835  1.00 21.17 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.215  -1.483  7.010  1.00 18.08 ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.420  -0.731  7.964  1.00 17.98 ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.197  -1.504  9.260  1.00 15.23 ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.347  -1.135  10.034 1.00 15.63 ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.071  -0.255  7.394  1.00 21.11 ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.164  0.887   6.393  1.00 24.46 ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.755  1.390   6.043  1.00 29.67 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.254  1.211   4.916  1.00 32.34 ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.079  2.060   6.974  1.00 25.78 ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.939  -2.613  9.461  1.00 14.03 ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.968  -3.315  10.724 1.00 13.97 ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.425  -3.576  11.126 1.00 13.07 ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.286  -3.774  10.258 1.00 14.57 ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.191  -4.606  10.736 1.00 16.73 ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.802  -5.535  9.893  1.00 23.25 ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.749  -4.448  10.322 1.00 16.60 ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.685  -3.527  12.411 1.00 12.34 ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.065  -3.713  12.877 1.00 11.56 ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.070  -3.763  14.392 1.00 10.97 ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.034  -4.005  15.018 1.00 11.22 ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.252  -3.560  14.991 1.00 10.33 ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.407  -3.639  16.438 1.00 9.28  ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.269 -2.464  16.878 1.00 9.17  ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.261 -2.159  16.183 1.00 10.24 ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.132 -4.979  16.772 1.00 11.57 ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.511 -5.068  18.229 1.00 13.50 ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.244  -6.180  16.396 1.00 12.10 ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.915  -1.794  17.977 1.00 9.18  ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.774 -0.716  18.475 1.00 9.50  ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.215 -0.920  19.906 1.00 9.59  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.528 -1.580  20.681 1.00 10.48 ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.096 0.691   18.329 1.00 10.32 ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.120  1.085   19.424 1.00 9.79  ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.831  0.560   19.455 1.00 10.99 ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.478  1.982   20.425 1.00 10.70 ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.932  0.908   20.463 1.00 12.33 ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.566  2.357   21.421 1.00 11.87 ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.304  1.825   21.415 1.00 12.82 ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.368  2.141   22.393 1.00 15.25 ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.355 -0.319  20.273 1.00 9.33  ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.824 -0.390  21.648 1.00 9.90  ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.372 0.834   22.446 1.00 10.11 ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.594 1.986   22.055 1.00 10.44 ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.376 -0.458  21.686 1.00 11.16 ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.845 -0.603  23.113 1.00 11.35 ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.524 -1.718  23.854 1.00 11.37 ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.600 0.400   23.735 1.00 12.27 ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.905 -1.826  25.188 1.00 13.33 ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.981 0.301   25.064 1.00 13.50 ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.666 -0.834  25.769 1.00 13.54 ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.032 -0.962  27.120 1.00 16.75 ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.767 0.529   23.595 1.00 9.88  ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.235 1.521   24.547 1.00 10.62 ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.053 1.506   25.849 1.00 10.98 ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.859 0.590   26.690 1.00 11.33 ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.773  1.214   24.839 1.00 10.95 ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.023  2.350   26.060 1.00 12.47 ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.985 2.450   26.028 1.00 11.69 ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.867 2.430   27.209 1.00 12.86 ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.111 2.626   28.521 1.00 12.39 ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.507 2.019   29.522 1.00 14.46 ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.973 3.472   27.069 1.00 14.54 ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.526 4.813   27.182 1.00 16.57 ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.964 3.373   28.502 1.00 11.68 ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.165 3.583   29.706 1.00 12.40 ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.340 2.376   30.135 1.00 12.22 ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.702  2.411   31.181 1.00 12.97 ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.283 4.822   29.556 1.00 13.27 ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.280  4.622   28.589 1.00 13.68 ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.449 1.271   29.381 1.00 12.58 ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.864  -0.019  29.763 1.00 12.73 ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.909 -1.161  29.724 1.00 14.19 ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.552 -2.326  29.988 1.00 14.30 ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.685  -0.354  28.826 1.00 13.36 ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.524  0.608   28.946 1.00 13.86 ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.760  0.322   30.234 1.00 14.45 ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.607  1.225   30.390 1.00 16.05 ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.628  2.366   31.057 1.00 15.05 ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.767  2.815   31.595 1.00 16.57 ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.506  3.092   31.193 1.00 17.06 ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.139 -0.897  29.239 1.00 14.93 ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.131 -1.958  28.961 1.00 15.65 ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.518 -3.071  28.090 1.00 17.02 ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.700 -4.279  28.363 1.00 19.38 ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.732 -2.570  30.236 1.00 18.39 ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.689 -1.652  30.829 1.00 18.47 ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.510 -2.465  31.841 1.00 20.55 ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.270 -1.520  32.641 1.00 23.07 ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.946 -1.136  33.873 1.00 20.57 ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.865 -1.633  34.471 1.00 21.27 ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.696 -0.250  34.516 1.00 22.55 ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.770 -2.693  27.066 1.00 14.07 ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.065 -3.688  26.267 1.00 14.71 ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.055 -3.283  24.821 1.00 13.04 ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.975 -2.086  24.476 1.00 13.10 ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.605  -3.796  26.783 1.00 17.44 ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.465  -4.737  27.996 1.00 25.74 ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 8.032  -5.115  28.270 1.00 34.89 ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.940  -5.860  29.586 1.00 40.29 ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.457  -5.043  30.725 1.00 44.03 ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.999 -4.296  23.956 1.00 12.45 ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.775 -4.134  22.519 1.00 11.73 ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.312  -4.457  22.251 1.00 13.71 ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.811  -5.516  22.693 1.00 16.78 ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.680 -5.097  21.718 1.00 11.53 ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.143 -4.775  21.831 1.00 12.54 ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.858 -4.117  20.848 1.00 15.84 ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.989 -5.103  22.836 1.00 12.89 ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.136 -4.071  21.270 1.00 14.11 ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.239 -4.628  22.458 1.00 16.15 ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.617  -3.590  21.505 1.00 11.53 ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.190  -3.797  21.240 1.00 11.66 ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.961  -3.910  19.742 1.00 10.63 ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.459  -3.067  18.975 1.00 10.84 ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.377  -2.551  21.714 1.00 12.15 ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.321  -2.396  23.220 1.00 12.77 ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.488  -3.206  23.995 1.00 14.55 ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.068  -1.420  23.862 1.00 13.00 ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.397  -3.050  25.375 1.00 14.87 ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.971  -1.231  25.243 1.00 14.86 ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.131  -2.047  25.994 1.00 15.07 ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.053  -1.858  27.375 1.00 17.45 ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.120  -4.874  19.337 1.00 10.97 ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.695  -4.924  17.927 1.00 11.52 ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.668  -3.828  17.651 1.00 12.05 ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.740  -3.644  18.480 1.00 14.26 ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.045  -6.320  17.757 1.00 14.27 ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.681  -6.726  19.170 1.00 16.13 ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.571  -5.974  20.152 1.00 11.94 ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.788  -3.163  16.547 1.00 10.71 ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.874  -2.038  16.194 1.00 12.78 ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.557  -2.035  14.731 1.00 12.11 ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.353  -2.406  13.883 1.00 12.75 ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.463  -0.660  16.572 1.00 15.80 ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.431  -0.458  18.083 1.00 17.40 ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.857  -0.468  16.003 1.00 16.36 ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.358  -1.508  14.407 1.00 12.33 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.960  -1.062  13.077 1.00 12.90 ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.196  0.454   12.983 1.00 12.45 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.846  1.146   13.969 1.00 13.37 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.474  -1.284  12.870 1.00 17.03 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.259  -2.679  12.908 1.00 24.43 ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.776  0.973   11.923 1.00 13.53 ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.079  2.391   11.858 1.00 13.62 ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.692  2.966   10.523 1.00 14.66 ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.618  2.257   9.516  1.00 16.22 ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.584  2.649   12.203 1.00 13.52 ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.613  1.846   11.403 1.00 12.70 ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.026  0.583   11.829 1.00 12.42 ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.182  2.362   10.248 1.00 13.43 ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.960  -0.134  11.105 1.00 13.33 ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.130  1.624   9.525  1.00 14.40 ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.482  0.374   9.952  1.00 14.00 ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.404  4.260   10.494 1.00 15.35 ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.990  4.939   9.272  1.00 16.34 ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.168  5.169   8.319  1.00 16.13 ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.350  5.072   8.701  1.00 15.69 ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.296  6.259   9.638  1.00 18.41 ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.139  7.178   10.319 1.00 19.87 ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.866  5.522   7.077  1.00 16.82 ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.930  5.844   6.119  1.00 17.25 ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.565  7.187   6.454  1.00 18.04 ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.888  8.061   7.002  1.00 19.59 ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.356  5.830   4.702  1.00 19.91 ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.916  4.450   4.306  1.00 22.28 ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.582  4.382   2.797  1.00 30.36 ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.280  2.959   2.385  1.00 36.37 ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.386  2.772   0.904  1.00 41.01 ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.825  7.422   6.094  1.00 17.31 ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.471  8.698   6.442  1.00 17.58 ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.687  9.882   5.881  1.00 19.69 ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.342  9.885   4.704  1.00 21.95 ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.877  8.573   5.830  1.00 19.77 ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.095  7.136   5.605  1.00 22.79 ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.766  6.471   5.445  1.00 18.85 ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.399  10.847  6.731  1.00 18.94 ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.507  11.956  6.343  1.00 20.74 ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.916  13.236  7.079  1.00 19.67 ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.740  13.233  7.996  1.00 18.96 ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.030  11.632  6.684  1.00 25.44 ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.665  10.277  6.502  1.00 34.63 ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.196  14.342  6.739  1.00 21.55 ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.385  15.648  7.349  1.00 23.52 ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.278  15.756  8.417  1.00 24.45 ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.076  15.804  8.085  1.00 26.47 ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.203  16.741  6.264  1.00 25.06 ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.496  18.150  6.699  1.00 29.05 ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 5.959  18.338  6.982  1.00 30.04 ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.083  19.153  5.601  1.00 30.52 ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.650  15.719  9.684  1.00 22.89 ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.748  15.687  10.841 1.00 23.96 ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.016  16.841  11.786 1.00 25.07 ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.186  17.184  12.054 1.00 24.20 ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.023  14.376  11.603 1.00 25.30 ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.889  13.138  10.648 1.00 27.11 ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.204  14.277  12.921 1.00 26.84 ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 2.695  11.966  11.174 1.00 26.54 ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.956  17.458  12.317 1.00 26.34 ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.094  18.528  13.285 1.00 26.14 ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.424  17.910  14.636 1.00 28.13 ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.765  16.978  15.096 1.00 30.92 ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.770  19.331  13.398 1.00 27.54 ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 0.985  20.623  14.128 1.00 31.00 ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.700  21.652  13.543 1.00 33.38 ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.567  20.766  15.438 1.00 34.09 ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.920  22.836  14.227 1.00 35.66 ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.766  21.957  16.115 1.00 34.93 ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.432  22.987  15.501 1.00 35.64 ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.542  18.359  15.227 1.00 25.50 ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 3.991  17.863  16.515 1.00 24.54 ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.895  19.009  17.526 1.00 24.69 ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.434  20.074  17.241 1.00 25.42 ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.450  17.324  16.395 1.00 22.82 ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 5.910  16.765  17.746 1.00 23.88 ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.520  16.241  15.290 1.00 22.96 ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.366  18.730  18.721 1.00 24.30 ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.220  19.752  19.767 1.00 25.92 ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.582  20.184  20.283 1.00 26.10 ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.562  19.446  20.187 1.00 26.04 ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.370  19.220  20.933 1.00 30.38 ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 0.898  19.015  20.584 1.00 36.27 ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.212  20.243  20.009 1.00 47.25 ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.431  21.364  20.526 1.00 49.07 ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.536 20.083  19.018 1.00 52.43 ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.612  21.370  20.914 1.00 26.51 ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.837  21.910  21.496 1.00 27.57 ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.407  20.972  22.533 1.00 29.04 ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.675  20.267  23.255 1.00 30.23 ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.541  23.242  22.162 1.00 29.01 ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.733  20.885  22.547 1.00 28.67 ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.440  20.071  23.537 1.00 28.66 ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.549  20.993  24.126 1.00 29.14 ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.590  22.165  23.768 1.00 28.93 ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 9.077  18.855  22.872 1.00 28.76 ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 10.103 19.314  21.996 1.00 27.32 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.524 20.441  24.922 1.00 29.80 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.585 21.369  25.375 1.00 30.35 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.623 21.646  24.251 1.00 26.61 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.391 22.609  24.356 1.00 27.51 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.225 20.976  26.704 1.00 36.62 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 13.295 19.937  26.617 1.00 42.51 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 14.027 19.721  27.925 1.00 51.83 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 13.458 19.047  28.816 1.00 52.21 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 15.169 20.222  28.056 1.00 54.71 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.539 20.892  23.119 1.00 23.96 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.518 21.011  22.027 1.00 21.82 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.048 21.741  20.781 1.00 21.81 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 13.872 22.227  20.018 1.00 21.74 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.956 19.604  21.646 1.00 22.15 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.558 18.882  22.826 1.00 22.49 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.843 19.171  23.254 1.00 24.70 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.799 18.009  23.595 1.00 25.17 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.424 18.476  24.305 1.00 26.78 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.358 17.324  24.665 1.00 26.70 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.655 17.599  25.050 1.00 28.19 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.231 16.901  26.091 1.00 31.37 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.728 21.743  20.517 1.00 23.12 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.196 22.414  19.334 1.00 22.38 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 9.860  23.056  19.717 1.00 24.32 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.089  22.449  20.489 1.00 25.59 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 10.876 21.373  18.218 1.00 21.43 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.065 20.592  17.677 1.00 18.97 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 12.975 21.178  16.802 1.00 18.83 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.271 19.273  18.037 1.00 18.28 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.039 20.454  16.276 1.00 17.20 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.352 18.545  17.544 1.00 17.87 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.223 19.138  16.649 1.00 16.82 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.307 18.443  16.166 1.00 16.69 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.547  24.173  19.061 1.00 26.14 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.189  24.720  19.206 1.00 27.23 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.227  23.757  18.488 1.00 28.71 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.671  22.849  17.735 1.00 27.45 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.292  26.074  18.460 1.00 29.00 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.308  25.841  17.395 1.00 29.93 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.339 24.935  18.056 1.00 26.92 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 5.919  23.978  18.615 1.00 29.92 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 4.930  23.193  17.870 1.00 30.18 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.185  23.518  16.364 1.00 29.88 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.440  24.671  16.018 1.00 31.86 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.518  23.637  18.282 1.00 30.75 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.308  22.491  15.523 1.00 28.88 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.691  22.675  14.133 1.00 27.68 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.346  21.404  13.357 1.00 27.60 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.979  20.383  13.941 1.00 28.24 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.228  22.918  14.052 1.00 28.39 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.095  21.596  14.004 1.00 29.89 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.365  21.704  14.750 1.00 29.05 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.330 20.675  14.337 1.00 28.25 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.404 19.440  14.793 1.00 29.94 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 11.390 18.639  14.388 1.00 23.16 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 9.499  18.986  15.674 1.00 28.94 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.514  21.465  12.045 1.00 27.26 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.381  20.313  11.202 1.00 27.72 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.736  19.617  11.100 1.00 24.57 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.742  20.238  10.727 1.00 25.34 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.932  20.742  9.817  1.00 28.84 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.448  21.041  9.774  1.00 29.61 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.516  20.018  9.714  1.00 30.31 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.970  22.336  9.933  1.00 30.91 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.156  20.273  9.734  1.00 32.20 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.605  22.603  9.944  1.00 32.07 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.702  21.563  9.863  1.00 33.19 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.654 21.763  9.868  1.00 37.17 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.749  18.292  11.372 1.00 21.93 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.940  17.443  11.260 1.00 19.84 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.733  16.577  10.024 1.00 19.26 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.655  15.998  9.820  1.00 19.97 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.136  16.611  12.527 1.00 20.17 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.393  15.771  12.447 1.00 19.81 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.924  15.275  13.792 1.00 21.05 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 9.833  15.935  14.832 1.00 24.91 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.532 14.093  13.797 1.00 16.53 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.758  16.471  9.176  1.00 17.48 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.665  15.706  7.958  1.00 17.66 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.250  14.289  8.167  1.00 15.95 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.037 14.048  9.098  1.00 16.18 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.380  16.445  6.832  1.00 20.34 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.759 16.549  7.153  1.00 22.55 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.849  13.381  7.260  1.00 16.76 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.345  11.999  7.218  1.00 15.80 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.078  11.292  8.562  1.00 14.65 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.904  10.446  8.988  1.00 15.39 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.871 11.964  6.844  1.00 17.32 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.169 12.549  5.471  1.00 18.72 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.262 11.742  4.357  1.00 21.56 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.310 13.838  5.095  1.00 22.03 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.516 12.563  3.330  1.00 22.03 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.558 13.830  3.729  1.00 23.04 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.955  11.577  9.190  1.00 14.29 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.631  11.031  10.509 1.00 14.67 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.574  9.937   10.333 1.00 14.14 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.632  10.100  9.549  1.00 15.33 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.053  12.157  11.402 1.00 16.01 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.782  11.751  12.883 1.00 18.88 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.058  11.447  13.606 1.00 18.64 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.046  12.892  13.647 1.00 21.62 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.695  8.857   11.114 1.00 13.97 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.731  7.728   11.098 1.00 13.59 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.150  7.590   12.493 1.00 13.93 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.914  7.641   13.469 1.00 14.44 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.504  6.465   10.739 1.00 14.13 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.132  6.563   9.338  1.00 15.29 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.244  5.177   8.904  1.00 18.57 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.569  5.443   10.170 1.00 22.97 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.828  7.393   12.629 1.00 13.47 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.242  7.274   13.951 1.00 14.30 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.752  5.858   14.236 1.00 13.30 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.292  5.147   13.316 1.00 15.09 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 2.019  8.223   14.093 1.00 17.01 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.280  9.705   14.062 1.00 21.91 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.991  10.505  14.435 1.00 24.21 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.309  10.134  15.088 1.00 24.53 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.783  5.471   15.509 1.00 13.40 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.233  4.179   15.960 1.00 12.98 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.630  4.382   17.348 1.00 12.83 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.924  5.373   18.047 1.00 13.19 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.362  3.113   16.069 1.00 14.13 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.808  3.410   17.770 1.00 12.26 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.298  3.394   19.107 1.00 11.92 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.336  2.647   19.996 1.00 13.88 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.671  1.497   19.739 1.00 15.18 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.064 2.690   19.127 1.00 12.71 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.554 2.519   20.571 1.00 14.65 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.068 3.487   18.282 1.00 12.99 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.833  3.365   21.001 1.00 13.79 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.847  2.777   21.892 1.00 14.54 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.307  3.800   22.887 1.00 16.07 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 3.022  4.982   22.793 1.00 17.80 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.954  3.296   23.964 1.00 18.04 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.454  4.132   25.020 1.00 19.35 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.736  4.816   24.647 1.00 18.02 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.658  4.175   24.078 1.00 17.57 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.651  3.277   26.311 1.00 19.30 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 5.046  4.136   27.457 1.00 20.28 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.142  5.004   28.035 1.00 20.35 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.249  4.294   28.063 1.00 21.18 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.831  5.664   28.961 1.00 20.81 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 6.100  5.238   29.016 1.00 21.28 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.858  6.079   24.914 1.00 18.99 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 7.037  6.789   24.786 1.00 19.52 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 7.019  7.864   25.855 1.00 20.97 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.931  8.272   26.296 1.00 24.32 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.237  7.277   23.359 1.00 20.38 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.116  8.013   22.930 1.00 24.47 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.216  8.264   26.263 1.00 16.99 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.605  9.389   27.131 1.00 17.61 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.786  10.111  26.471 1.00 18.53 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.413 9.558   25.554 1.00 17.16 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 9.014  8.867   28.506 1.00 18.62 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.836  8.189   29.200 1.00 20.68 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.050  7.578   30.581 1.00 23.81 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.918  8.076   31.335 1.00 28.62 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.358  6.586   30.895 1.00 23.09 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 10.084 11.379  26.817 1.00 18.98 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 11.148 12.110  26.080 1.00 19.13 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.468 11.385  25.930 1.00 18.32 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 13.014 11.321  24.814 1.00 17.57 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 11.302 13.426  26.881 1.00 21.58 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.944  13.643  27.406 1.00 22.37 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.389  12.271  27.773 1.00 19.30 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.963 10.764  26.994 1.00 16.93 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.208 10.015  26.979 1.00 16.07 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.166 8.718   26.180 1.00 14.36 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.198 8.074   26.014 1.00 14.47 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.995 8.302   25.680 1.00 12.98 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.920 7.156   24.750 1.00 12.24 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.435 7.504   23.345 1.00 12.24 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.687 6.595   22.523 1.00 11.69 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.472 6.622   24.638 1.00 12.11 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.083 5.882   25.908 1.00 12.79 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.962 5.197   26.478 1.00 13.50 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.887  5.980   26.323 1.00 13.75 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.607 8.818   23.051 1.00 11.99 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.172 9.189   21.732 1.00 12.41 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.493 8.486   21.494 1.00 12.34 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.331 8.394   22.381 1.00 12.74 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.347 10.701  21.660 1.00 13.29 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.772 11.591  21.382 1.00 15.25 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.677 7.963   20.278 1.00 11.02 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.885 7.260   19.907 1.00 11.34 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.692 5.752   19.818 1.00 11.28 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.547 5.059   19.251 1.00 11.84 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.612 5.228   20.425 1.00 10.69 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.345 3.801   20.324 1.00 10.43 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.101 3.385   18.867 1.00 9.40  ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.416 4.106   18.121 1.00 9.91  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.593 2.224   18.465 1.00 9.92  ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.442 1.816   17.060 1.00 9.58  ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.106 1.168   16.781 1.00 9.19  ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.639 0.333   17.587 1.00 9.64  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.598 0.841   16.718 1.00 10.09 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.888 1.683   16.451 1.00 11.83 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.297 -0.055  15.500 1.00 10.86 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.154 0.850   16.307 1.00 15.29 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.526 1.503   15.630 1.00 8.84  ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.417 0.786   15.008 1.00 8.89  ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.026 -0.069  13.889 1.00 8.77  ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.804 0.469   13.060 1.00 9.83  ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.429 1.816   14.404 1.00 9.72  ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.315 1.183   13.519 1.00 10.46 ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.323  0.369   14.371 1.00 11.90 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.546  2.298   12.754 1.00 12.48 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.706 -1.345  13.833 1.00 9.55  ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.285 -2.252  12.795 1.00 10.16 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.212 -3.142  12.249 1.00 11.02 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.210 -3.457  12.899 1.00 11.17 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.450 -3.079  13.404 1.00 11.65 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 13.980 -4.064  14.486 1.00 11.70 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.204 -4.803  15.048 1.00 13.27 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 15.987 -3.928  15.905 1.00 14.21 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.287 -3.722  15.796 1.00 14.38 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 17.953 -4.146  14.715 1.00 15.63 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.927 -3.001  16.704 1.00 15.65 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.473 -3.653  11.046 1.00 13.59 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.553 -4.601  10.360 1.00 17.24 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.408 -5.766  9.937  1.00 19.90 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.595 -5.887  10.280 1.00 18.78 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.874 -3.919  9.170  1.00 16.55 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.023 -3.545  7.809  1.00 16.30 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.779 -6.699  9.158  1.00 22.35 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.514 -7.847  8.661  1.00 24.74 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.739 -7.489  7.782  1.00 25.57 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.674 -8.274  7.709  1.00 28.38 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.579 -8.837  7.905  1.00 29.28 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.065 -8.268  6.600  1.00 33.82 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.155 -9.219  5.858  1.00 40.04 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.925  -9.165  5.989  1.00 42.54 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.743 -10.080 5.036  1.00 38.48 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.783 -6.283  7.213  1.00 21.42 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.872 -5.860  6.297  1.00 20.26 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.028 -5.118  6.996  1.00 20.10 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.063 -4.849  6.373  1.00 22.75 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.258 -4.974  5.203  1.00 20.65 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.143 -5.684  4.465  1.00 23.42 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.819 -5.310  4.585  1.00 23.01 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.224 -6.649  3.502  1.00 26.45 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.122 -6.144  3.814  1.00 26.67 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.933 -6.957  3.135  1.00 29.25 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.814 -4.657  8.250  1.00 17.51 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.850 -3.902  8.939  1.00 16.20 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.243 -2.742  9.725  1.00 13.94 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.051 -2.732  10.071 1.00 13.60 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.105 -1.734  10.006 1.00 12.47 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.669 -0.536  10.758 1.00 12.33 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.823 0.387   9.907  1.00 10.93 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.225 0.746   8.776  1.00 11.83 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.882 0.233   11.333 1.00 11.70 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.446 1.558   11.998 1.00 13.11 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.666 -0.656  12.304 1.00 13.00 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.670 0.793   10.393 1.00 10.23 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.715 1.644   9.723  1.00 10.73 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.862 3.085   10.143 1.00 10.52 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.714 4.018   9.344  1.00 12.08 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.265 1.152   10.002 1.00 12.45 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.193 2.129   9.479  1.00 15.13 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.026 -0.234  9.453  1.00 14.08 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.056 3.324   11.453 1.00 10.66 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.162 4.713   11.955 1.00 11.02 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.374 4.734   13.456 1.00 10.21 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.709 3.668   14.029 1.00 10.34 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.277 5.919   14.074 1.00 10.10 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.489 6.033   15.527 1.00 9.61  ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.356 6.806   16.152 1.00 9.88  ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.743 7.687   15.491 1.00 11.21 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.844 6.730   15.877 1.00 10.78 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.997 8.068   15.148 1.00 12.30 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.993 5.776   15.653 1.00 12.33 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.274 8.865   15.666 1.00 13.42 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.050 6.535   17.414 1.00 9.87  ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 12.010 7.263   18.140 1.00 10.27 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.385 8.751   18.161 1.00 10.80 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.552 9.109   18.463 1.00 10.89 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.903 6.763   19.592 1.00 11.06 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.921 7.622   20.418 1.00 11.74 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.448 5.276   19.650 1.00 11.55 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.427 9.626   17.841 1.00 11.44 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.622 11.085  17.786 1.00 12.51 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.535 11.839  18.521 1.00 13.68 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.821 12.967  19.007 1.00 16.14 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.760 11.495  16.331 1.00 13.06 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.801 12.906  16.124 1.00 15.84 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.280  11.316  18.592 1.00 13.96 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.194  12.107  19.234 1.00 15.27 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.364  11.166  20.111 1.00 17.12 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.446  9.922   19.974 1.00 15.37 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.277  12.806  18.157 1.00 17.22 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.463  11.810  17.502 1.00 17.61 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 8.036  13.613  17.153 1.00 17.81 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.524  11.741  20.967 1.00 19.29 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.622  10.927  21.757 1.00 21.54 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.543  11.697  22.491 1.00 23.02 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.566  12.917  22.475 1.00 24.90 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.742  10.922  23.226 1.00 24.30 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.688  11.405  24.125 1.00 24.47 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.369  10.695  23.920 1.00 27.09 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.033  10.311  22.787 1.00 27.81 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.602  10.542  25.022 1.00 26.22 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.765 10.017  25.018 1.00 27.56 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -0.943 8.751   24.243 1.00 25.51 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.007 8.526   23.626 1.00 26.08 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.709 11.093  24.512 1.00 30.30 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.791 12.266  25.447 1.00 34.76 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -2.069 12.092  26.639 1.00 38.29 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.523 13.464  24.911 1.00 34.56 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.030 7.829   24.461 1.00 21.98 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.145 6.526   23.885 1.00 20.66 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.235  6.524   22.431 1.00 16.08 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? 0.064  5.482   21.878 1.00 17.63 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.892  7.573   21.891 1.00 16.02 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.465  7.499   20.528 1.00 15.68 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 3.006  7.581   20.610 1.00 16.68 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.588  8.187   21.554 1.00 19.30 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.964  8.638   19.673 1.00 17.37 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.559 8.612   19.484 1.00 18.39 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.094 9.997   19.096 1.00 21.43 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.991 7.481   18.499 1.00 18.81 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.654  6.996   19.619 1.00 13.10 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.117  7.116   19.462 1.00 13.06 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.350  7.490   17.987 1.00 13.21 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.741  6.892   17.107 1.00 13.61 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.823  5.815   19.916 1.00 12.93 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.265  4.563   19.233 1.00 13.77 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.356  5.945   19.752 1.00 12.96 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.252  8.437   17.732 1.00 13.18 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.595  8.831   16.365 1.00 13.05 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.053  8.508   16.089 1.00 12.10 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.926  8.683   16.965 1.00 13.70 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.299  8.022   14.878 1.00 11.40 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.659  7.606   14.455 1.00 11.39 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.114 8.401   13.249 1.00 12.14 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.339  8.570   12.292 1.00 12.67 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.621  6.110   14.029 1.00 11.81 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 9.005  5.180   15.066 1.00 10.87 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.755  4.701   16.139 1.00 10.54 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.665  4.796   14.961 1.00 12.17 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.178  3.841   17.083 1.00 10.94 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.107  3.926   15.896 1.00 12.46 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.878  3.449   16.939 1.00 11.17 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.370 8.882   13.319 1.00 11.18 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.995 9.552   12.165 1.00 12.18 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.473 8.478   11.198 1.00 11.63 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.355 7.662   11.568 1.00 11.75 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.145 10.413  12.670 1.00 12.47 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.935 8.423   9.980  1.00 12.13 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.349 7.432   8.989  1.00 12.43 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.754 7.725   8.493  1.00 12.72 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.154 8.897   8.347  1.00 14.02 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.393 7.506   7.784  1.00 14.94 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.663 6.511   6.716  1.00 19.43 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.762 5.300   7.026  1.00 17.91 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.887 6.955   5.544  1.00 24.60 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.497 6.651   8.203  1.00 11.84 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.823 6.783   7.554  1.00 11.78 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.935 5.961   6.269  1.00 12.35 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.006 5.968   5.632  1.00 12.38 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 16.995 6.443   8.507  1.00 11.78 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.042 7.358   9.741  1.00 12.54 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.020 4.981   8.922  1.00 13.06 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.868 5.288   5.844  1.00 13.04 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.950 4.362   4.711  1.00 13.60 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.199 5.051   3.375  1.00 15.33 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.687 4.397   2.416  1.00 15.93 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.694 3.503   4.603  1.00 14.12 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.564 2.556   5.824  1.00 13.11 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.260 1.783   5.680  1.00 15.13 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.119 2.686   5.924  1.00 14.65 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.843  2.317   5.999  1.00 17.09 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.495  1.067   5.723  1.00 17.20 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.908  3.214   6.320  1.00 17.93 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.880 6.367   3.267  1.00 14.82 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.148 7.073   2.018  1.00 15.87 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.596 7.593   1.925  1.00 15.55 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.001 8.095   0.858  1.00 17.23 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.170 8.269   1.887  1.00 17.79 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.403 9.330   2.965  1.00 21.48 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.532 8.963   4.173  1.00 19.87 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.434 10.526  2.636  1.00 24.49 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.391 7.531   3.011  1.00 14.04 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.763 8.080   3.032  1.00 13.66 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.716 7.030   2.483  1.00 14.15 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.421 6.331   3.233  1.00 14.00 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.118 8.490   4.479  1.00 13.33 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.159 9.522   5.127  1.00 14.90 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.533 9.763   6.593  1.00 15.72 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.177 10.828  4.372  1.00 17.78 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.734 6.891   1.139  1.00 14.32 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.485 5.795   0.515  1.00 14.57 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 21.975 5.895   0.696  1.00 14.44 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.683 4.864   0.747  1.00 16.37 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.120 5.667   -1.010 1.00 16.54 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.609 5.666   -1.298 1.00 18.65 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.368 5.343   -2.801 1.00 21.40 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.833 4.630   -0.461 1.00 20.10 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.469 7.137   0.865  1.00 13.55 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.884 7.395   1.031  1.00 14.37 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.422 6.805   2.336  1.00 14.68 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.644 6.682   2.468  1.00 15.64 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.178 8.911   0.899  1.00 14.89 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.359 9.739   1.860  1.00 14.20 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.213 10.420  1.570  1.00 14.89 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.698 10.066  3.228  1.00 14.35 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.768 11.094  2.702  1.00 15.93 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.690 10.920  3.710  1.00 14.65 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.777 9.756   4.061  1.00 15.00 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.712 11.431  5.026  1.00 15.95 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.808 10.288  5.353  1.00 16.49 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.799 11.127  5.800  1.00 16.11 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.565 6.463   3.331  1.00 13.51 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.079 5.806   4.549  1.00 15.11 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.767 4.481   4.239  1.00 16.77 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.625 4.021   5.028  1.00 18.56 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.944 5.546   5.538  1.00 14.86 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.387 6.790   6.218  1.00 14.12 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.131 6.436   7.005  1.00 15.27 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.468 7.436   7.168  1.00 15.37 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.448 3.856   3.065  1.00 19.03 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.024 2.544   2.687  1.00 21.61 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.372 2.642   1.973  1.00 25.76 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.931 1.602   1.598  1.00 27.66 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.061 1.775   1.730  1.00 22.21 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.699 1.463   2.289  1.00 24.83 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.528 1.559   3.527  1.00 27.30 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.780 1.122   1.499  1.00 31.21 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.880 3.863   1.690  1.00 26.47 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.145 4.059   0.929  1.00 29.35 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.151 4.895   1.725  1.00 30.90 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.754 5.633   2.616  1.00 30.89 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.874 4.785   -0.415 1.00 33.02 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 26.515 4.561   -1.064 1.00 41.21 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 25.930 5.783   -1.757 1.00 50.41 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.481 6.897   -1.598 1.00 52.24 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 24.897 5.625   -2.447 1.00 53.62 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.439 4.866   1.331  1.00 32.84 ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.528 5.634   1.961  1.00 35.49 ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 31.318 7.133   1.789  1.00 36.91 ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 31.648 7.911   2.699  1.00 37.53 ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 32.882 5.234   1.345  1.00 39.22 ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 34.078 5.640   2.185  1.00 48.62 ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 35.435 5.308   1.585  1.00 58.67 ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 35.480 4.586   0.561  1.00 61.26 ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 36.456 5.775   2.143  1.00 61.03 ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.923 -21.268 7.645  1.00 17.82 ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.778 -21.040 8.570  1.00 17.08 ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.751 -22.168 9.640  1.00 16.89 ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.415 -23.218 9.485  1.00 18.78 ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.467 -21.074 7.781  1.00 20.55 ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.311 -22.361 7.210  1.00 25.95 ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.973 -21.964 10.708 1.00 16.93 ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.779 -22.963 11.750 1.00 16.19 ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.519 -22.347 13.103 1.00 14.96 ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.936 -21.221 13.361 1.00 15.05 ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.860 -23.075 13.983 1.00 14.09 ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.533 -22.595 15.323 1.00 14.09 ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.659 -23.717 16.347 1.00 12.88 ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.719 -24.904 15.961 1.00 14.41 ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.085 -22.073 15.323 1.00 16.15 ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.656 -23.351 17.624 1.00 12.67 ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.578 -24.284 18.755 1.00 13.14 ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.181 -24.095 19.353 1.00 13.06 ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.749 -22.940 19.553 1.00 13.85 ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.620 -23.965 19.828 1.00 12.53 ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.052 -23.832 19.234 1.00 14.09 ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.569 -25.062 20.919 1.00 14.34 ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.013 -23.222 20.259 1.00 14.76 ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.477 -25.189 19.657 1.00 13.12 ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.128 -25.143 20.228 1.00 13.73 ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.182 -25.819 21.595 1.00 14.52 ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.249 -27.058 21.671 1.00 16.00 ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.079 -25.851 19.311 1.00 14.81 ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.888 -25.096 18.006 1.00 15.09 ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.049 -23.983 17.935 1.00 15.23 ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.603 -25.439 16.871 1.00 15.96 ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.941 -23.243 16.762 1.00 16.91 ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.495 -24.715 15.691 1.00 18.11 ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.656 -23.623 15.640 1.00 17.60 ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.583 -22.874 14.487 1.00 19.62 ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.243 -25.063 22.682 1.00 15.03 ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.324 -25.595 24.056 1.00 16.13 ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.185 -24.977 24.883 1.00 16.73 ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 13.996 -23.764 24.871 1.00 15.54 ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.722 -25.311 24.659 1.00 17.10 ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.092 -23.817 24.567 1.00 17.34 ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.765 -25.794 26.089 1.00 18.19 ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.356 -25.806 25.570 1.00 17.69 ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.240 -25.269 26.334 1.00 17.59 ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.311 -24.433 25.460 1.00 18.10 ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.042 -24.834 24.320 1.00 19.21 ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 10.978 -23.238 25.902 1.00 17.59 ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.186 -22.332 25.065 1.00 17.66 ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.062 -21.224 24.488 1.00 16.67 ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.598 -20.096 24.320 1.00 16.85 ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.938  -21.757 25.792 1.00 19.72 ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.853  -22.812 25.931 1.00 26.16 ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 6.987  -22.963 25.062 1.00 29.15 ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 7.962  -23.617 26.964 1.00 28.32 ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.276 -21.593 24.087 1.00 14.65 ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.247 -20.640 23.507 1.00 14.12 ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.710 -21.110 22.136 1.00 14.31 ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.901 -22.326 21.919 1.00 14.88 ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.489 -20.482 24.426 1.00 15.60 ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.162 -19.959 25.819 1.00 16.45 ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.593 -18.701 25.996 1.00 18.31 ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.461 -20.707 26.953 1.00 18.34 ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.294 -18.222 27.273 1.00 21.22 ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.205 -20.213 28.235 1.00 21.55 ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.647 -18.964 28.381 1.00 24.41 ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.358 -18.468 29.641 1.00 29.97 ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 13.965 -20.154 21.246 1.00 13.56 ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.589 -20.382 19.929 1.00 12.96 ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.853 -19.514 19.931 1.00 12.64 ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.768 -18.294 20.122 1.00 13.48 ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.627 -19.924 18.791 1.00 13.98 ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.259 -19.775 17.402 1.00 14.81 ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.181 -19.463 16.358 1.00 14.98 ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.614 -18.525 15.319 1.00 15.94 ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.156 -18.837 14.136 1.00 17.06 ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.414 -20.119 13.821 1.00 18.59 ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.521 -17.869 13.288 1.00 17.97 ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.020 -20.107 19.684 1.00 12.31 ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.317 -19.400 19.662 1.00 11.68 ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.796 -19.340 18.248 1.00 12.19 ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.961 -20.405 17.606 1.00 13.02 ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.381 -20.133 20.534 1.00 12.23 ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.638 -19.269 20.613 1.00 13.91 ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.841 -20.473 21.941 1.00 14.74 ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.049 -18.130 17.717 1.00 11.52 ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.499 -17.962 16.326 0.50 11.56 ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.450 -17.988 16.325 0.50 13.28 ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.627 -16.959 16.253 1.00 12.08 ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.886 -16.197 17.217 1.00 12.78 ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.347 -17.441 15.401 0.50 11.86 ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.167 -17.460 15.573 0.50 17.30 ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.375 -18.567 15.101 0.50 12.95 ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.405 -17.256 14.097 0.50 17.85 ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.696 -16.130 15.932 0.50 8.55  ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 16.993 -18.406 15.760 0.50 20.62 ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.329 -16.918 15.109 1.00 11.67 ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.314 -15.862 14.905 1.00 11.37 ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.507 -14.515 14.849 1.00 12.23 ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.491 -14.417 14.153 1.00 12.16 ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.020 -15.999 13.539 1.00 12.40 ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.890 -17.264 13.470 1.00 11.52 ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.427 -18.318 13.044 1.00 13.27 ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.127 -17.141 13.924 1.00 13.07 ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.011 -13.491 15.562 1.00 12.28 ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.284 -12.188 15.575 1.00 12.12 ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.137 -11.647 14.143 1.00 13.54 ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.057 -11.125 13.800 1.00 13.52 ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.030 -11.196 16.449 1.00 12.47 ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.231 -9.854  16.657 1.00 12.70 ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.090 -8.894  17.460 1.00 13.16 ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.405 -7.629  17.890 1.00 13.98 ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.302 -6.542  17.149 1.00 14.74 ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.678 -6.559  15.886 1.00 15.55 ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.803 -5.430  17.665 1.00 15.49 ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.160 -11.847 13.281 1.00 13.11 ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.065 -11.305 11.918 1.00 13.70 ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.054 -12.028 11.020 1.00 14.69 ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.778 -11.507 9.938  1.00 16.43 ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.455 -11.206 11.242 1.00 14.77 ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.044 -12.532 10.819 1.00 13.63 ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.781 -13.341 11.693 1.00 14.08 ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.047 -13.107 9.587  1.00 14.41 ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.183 -14.396 10.962 1.00 14.79 ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.775 -14.278 9.686  1.00 14.10 ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.538 -13.197 11.442 1.00 13.25 ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.524 -13.959 10.695 1.00 14.24 ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.130 -13.894 11.367 1.00 14.85 ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.206 -14.624 10.947 1.00 15.60 ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.990 -15.415 10.517 1.00 14.38 ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.282 -15.556 9.720  1.00 14.86 ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.722 -17.018 9.647  1.00 15.35 ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.177 -14.940 8.308  1.00 15.82 ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 17.971 -13.117 12.480 1.00 14.85 ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.684 -13.059 13.188 1.00 14.31 ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.591 -12.516 12.295 1.00 15.80 ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.819 -11.584 11.506 1.00 16.53 ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.827 -12.187 14.441 1.00 15.45 ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.402 -13.077 12.458 1.00 16.58 ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.246 -12.658 11.667 1.00 16.82 ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.421 -11.598 12.432 1.00 16.26 ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.634 -11.305 13.608 1.00 16.45 ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.327 -13.891 11.413 1.00 18.14 ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.779 -14.310 12.648 1.00 18.16 ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.053 -15.064 10.707 1.00 19.94 ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.404 -10.992 11.740 1.00 17.63 ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.469 -10.084 12.425 1.00 18.59 ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.779  -10.835 13.563 1.00 15.90 ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.682  -10.267 14.652 1.00 17.93 ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.353  -9.598  11.470 1.00 20.34 ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.224  -8.875  12.176 1.00 21.60 ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.391  -7.614  12.732 1.00 24.62 ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.014  -9.342  12.535 1.00 23.96 ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.208  -7.280  13.240 1.00 24.36 ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.358  -8.306  13.189 1.00 24.11 ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.366  -12.100 13.359 1.00 16.32 ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.729  -12.837 14.448 1.00 18.03 ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.646  -12.999 15.648 1.00 16.55 ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.221  -12.900 16.793 1.00 16.12 ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.193  -14.205 14.004 1.00 19.96 ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.389  -14.896 15.103 1.00 25.83 ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.271  -14.460 15.439 1.00 28.62 ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.964  -15.925 15.748 1.00 27.56 ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 10.972 -13.210 15.394 1.00 16.12 ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.915 -13.296 16.498 1.00 15.66 ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 11.964 -11.989 17.304 1.00 14.89 ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.889 -11.999 18.531 1.00 16.15 ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.326 -13.617 15.994 1.00 14.96 ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.539 -15.029 15.507 1.00 15.19 ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.958 -15.954 16.114 1.00 17.19 ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.240 -15.202 14.477 1.00 15.69 ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.051 -10.840 16.594 1.00 15.45 ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.095 -9.546  17.269 1.00 15.69 ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.746 -9.213  17.987 1.00 15.40 ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.767 -8.597  19.061 1.00 16.44 ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.472 -8.433  16.297 1.00 15.90 ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 13.957 -8.389  16.036 1.00 15.89 ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.610 -8.852  14.938 1.00 16.82 ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 14.963 -7.811  16.892 1.00 14.11 ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 15.971 -8.583  15.042 1.00 16.22 ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.205 -7.935  16.230 1.00 15.22 ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 14.923 -7.124  18.113 1.00 17.36 ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.375 -7.409  16.741 1.00 15.52 ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.104 -6.617  18.624 1.00 18.13 ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.308 -6.774  17.937 1.00 17.70 ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.632  -9.683  17.434 1.00 15.94 ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.305  -9.451  18.039 1.00 17.12 ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.059  -10.332 19.278 1.00 18.49 ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.082  -10.122 20.012 1.00 18.45 ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.214  -9.701  17.009 1.00 18.27 ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 8.909  -11.373 19.494 1.00 18.29 ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.813  -12.282 20.640 1.00 16.82 ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.191 -12.330 21.327 1.00 16.51 ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.622 -13.406 21.743 1.00 16.24 ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.361  -13.668 20.123 1.00 18.23 ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.947  -13.619 19.634 1.00 19.35 ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 5.988  -13.636 20.454 1.00 21.81 ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.756  -13.488 18.332 1.00 20.04 ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 10.897 -11.201 21.408 1.00 17.25 ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.272 -11.192 21.901 1.00 16.48 ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.397 -11.511 23.374 1.00 18.21 ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.618 -11.028 24.192 1.00 19.51 ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.819 -9.779  21.653 1.00 16.99 ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.282 -9.617  22.020 1.00 17.43 ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.189 -10.487 21.121 1.00 17.19 ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.708 -8.173  21.906 1.00 19.15 ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.380 -12.334 23.719 1.00 16.67 ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.722 -12.606 25.110 1.00 17.22 ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.051 -11.892 25.442 1.00 17.42 ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.172 -11.220 26.473 1.00 18.31 ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.855 -14.128 25.350 1.00 17.61 ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.413 -14.420 26.753 1.00 19.09 ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.520 -14.841 25.143 1.00 17.97 ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.081 -12.039 24.570 1.00 15.42 ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.397 -11.462 24.852 1.00 15.79 ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.186 -11.407 23.537 1.00 15.93 ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.000 -12.287 22.669 1.00 15.35 ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.130 -12.362 25.900 1.00 17.15 ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.603 -12.099 26.093 1.00 17.19 ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.180 -11.148 26.895 1.00 19.56 ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.685 -12.789 25.450 1.00 16.08 ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.562 -11.239 26.826 1.00 20.38 ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 21.895 -12.244 25.948 1.00 17.73 ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.751 -13.832 24.506 1.00 15.98 ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.157 -12.737 25.559 1.00 17.27 ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.004 -14.329 24.151 1.00 17.51 ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.175 -13.742 24.628 1.00 17.59 ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.046 -10.423 23.390 1.00 15.14 ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.906 -10.322 22.208 1.00 16.07 ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.189 -9.640  22.556 1.00 15.83 ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.197 -8.751  23.460 1.00 16.47 ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.214 -9.653  21.028 1.00 17.40 ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.655 -8.269  21.302 1.00 18.17 ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.633 -7.104  21.250 1.00 19.50 ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.356 -6.073  21.911 1.00 22.24 ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.655 -7.175  20.516 1.00 18.27 ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.282 -10.002 21.856 1.00 14.95 ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.572 -9.362  22.093 1.00 15.17 ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.340 -9.329  20.765 1.00 15.06 ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.784 -10.374 20.263 1.00 14.41 ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.300 -10.136 23.204 1.00 16.38 ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.640 -9.590  23.597 1.00 19.48 ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.376 -9.136  22.712 1.00 20.38 ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 25.996 -9.703  24.788 1.00 24.17 ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.510 -8.118  20.193 1.00 15.13 ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.214 -7.931  18.936 0.50 14.84 ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.192 -7.995  18.924 0.50 15.46 ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.679 -8.395  19.029 1.00 15.13 ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.182 -9.022  18.085 1.00 14.88 ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.163 -6.473  18.484 0.50 15.40 ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.012 -6.607  18.331 0.50 17.72 ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.071 -6.249  17.412 0.50 15.63 ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.465 -5.650  19.264 0.50 20.49 ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.351 -8.116  20.154 1.00 15.56 ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.762 -8.518  20.270 1.00 16.17 ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 28.942 -10.038 20.233 1.00 14.78 ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.027 -10.484 19.863 1.00 15.62 ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.380 -7.983  21.550 1.00 19.55 ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.995 -8.686  22.715 1.00 24.44 ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.895 -10.828 20.565 1.00 13.91 ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 27.962 -12.295 20.515 1.00 13.68 ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.325 -12.880 19.236 1.00 12.94 ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.363 -14.096 19.024 1.00 12.55 ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.209 -12.881 21.740 1.00 15.91 ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 27.892 -12.539 23.054 1.00 16.30 ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.137 -13.089 24.254 1.00 14.58 ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.197 -14.577 24.286 1.00 14.13 ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.164 -15.322 25.398 1.00 13.98 ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.050 -14.752 26.590 1.00 15.66 ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.330 -16.646 25.326 1.00 14.55 ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.666 -12.038 18.417 1.00 12.42 ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.886 -12.496 17.276 1.00 12.50 ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.772 -13.465 17.712 1.00 11.69 ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.473 -14.399 16.944 1.00 12.29 ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.732 -13.096 16.150 1.00 12.41 ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.944 -13.437 14.879 1.00 13.62 ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.047 -12.646 14.489 1.00 14.18 ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.265 -14.447 14.227 1.00 13.01 ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.102 -13.226 18.865 1.00 11.55 ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.020 -14.129 19.300 1.00 11.85 ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.714 -13.378 19.546 1.00 12.24 ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.736 -12.208 20.025 1.00 13.21 ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.416 -14.836 20.607 1.00 12.86 ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.483 -15.954 20.513 1.00 12.78 ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.739 -16.538 21.927 1.00 14.71 ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.048 -17.079 19.562 1.00 13.12 ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.615 -14.060 19.318 1.00 11.63 ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.300 -13.549 19.684 1.00 12.59 ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.456 -14.766 20.068 1.00 12.28 ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.551 -15.842 19.443 1.00 12.82 ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.662 -12.807 18.469 1.00 13.43 ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.257 -12.224 18.722 1.00 12.91 ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.057 -10.928 17.933 1.00 15.71 ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.168 -13.239 18.346 1.00 13.99 ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.665 -14.595 21.131 1.00 12.83 ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.751 -15.606 21.646 1.00 12.78 ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.330 -15.067 21.640 1.00 12.89 ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.106 -13.935 22.116 1.00 14.65 ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.164 -16.046 23.065 1.00 13.57 ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.194 -17.094 23.610 1.00 15.88 ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.612 -16.609 23.066 1.00 14.74 ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.416 -15.832 21.076 1.00 12.84 ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 12.999 -15.483 21.044 1.00 13.28 ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.187 -16.579 21.734 1.00 14.25 ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.669 -17.693 22.008 1.00 15.00 ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.527 -15.260 19.613 1.00 14.67 ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.686 -16.423 18.817 1.00 15.46 ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.961 -16.251 22.122 1.00 15.11 ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.069 -17.216 22.776 1.00 16.35 ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.255  -18.016 21.750 1.00 18.41 ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 8.945  -17.517 20.670 1.00 19.74 ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.164  -16.498 23.774 1.00 18.56 ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.316  -15.614 23.068 1.00 22.39 ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.896  -19.257 22.084 1.00 18.71 ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.153  -20.143 21.185 1.00 19.60 ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.849  -20.588 21.878 1.00 21.87 ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.776  -20.700 23.102 1.00 21.46 ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 8.999  -21.395 20.822 1.00 20.26 ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.249  -22.167 21.986 1.00 21.52 ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.368 -21.043 20.167 1.00 20.40 ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.868  -20.963 21.063 1.00 23.96 ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.613  -21.517 21.601 1.00 26.12 ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.827  -22.986 21.968 1.00 26.44 ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.437  -23.429 23.056 1.00 29.06 ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.476  -21.277 20.605 1.00 30.98 ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.798  -21.941 19.389 1.00 35.20 ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.301  -19.807 20.286 1.00 30.48 ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.505  -23.739 21.083 1.00 23.94 ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.752  -25.155 21.324 1.00 24.15 ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.076  -25.403 22.071 1.00 22.52 ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.022  -24.653 21.879 1.00 22.43 ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.789  -25.893 19.993 1.00 26.14 ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.173  -26.458 22.871 1.00 22.36 ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.400  -26.809 23.571 1.00 23.03 ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.376  -27.485 22.599 1.00 22.13 ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 8.960  -28.293 21.761 1.00 23.77 ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.095  -27.732 24.768 1.00 28.50 ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.473  -26.981 25.943 1.00 37.83 ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.309  -27.927 27.105 1.00 49.67 ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.391  -28.760 27.137 1.00 53.43 ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.200  -27.839 28.087 1.00 52.23 ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.660 -27.133 22.711 1.00 19.50 ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.749 -27.715 21.931 1.00 19.27 ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.406 -28.840 22.706 1.00 19.14 ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.176 -29.006 23.913 1.00 21.34 ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.242 -29.570 22.043 1.00 17.91 ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.832 -30.775 22.615 1.00 18.70 ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.323 -30.800 22.657 1.00 18.45 ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.873 -31.843 23.064 1.00 20.98 ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.294 -31.995 21.869 1.00 18.69 ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.492 -32.105 21.917 1.00 25.92 ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.018 -29.752 22.225 1.00 15.69 ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.478 -29.753 22.246 1.00 15.68 ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.902 -29.554 23.708 1.00 16.26 ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.208 -28.882 24.507 1.00 18.36 ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.027 -28.588 21.402 1.00 16.34 ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.861 -28.771 19.912 1.00 20.67 ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.893 -29.928 19.445 1.00 22.54 ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.714 -27.735 19.188 1.00 17.72 ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.012 -30.182 24.061 1.00 14.93 ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.626 -30.024 25.375 1.00 15.29 ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.890 -29.171 25.218 1.00 14.42 ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.719 -29.474 24.319 1.00 15.46 ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.033 -31.389 25.936 1.00 18.02 ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.832 -32.179 26.132 1.00 20.29 ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.819 -31.265 27.263 1.00 19.69 ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.065 -28.124 26.037 1.00 15.06 ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.265 -27.303 25.990 1.00 14.69 ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.364 -27.988 26.827 1.00 13.77 ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.132 -28.444 27.956 1.00 14.84 ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.019 -25.925 26.582 1.00 15.44 ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.795 -25.242 25.948 1.00 16.02 ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.286 -25.069 26.482 1.00 16.66 ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 20.983 -25.099 24.397 1.00 18.01 ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.571 -28.072 26.285 1.00 12.46 ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.709 -28.633 27.038 1.00 12.36 ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.069 -27.693 28.211 1.00 11.93 ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.030 -26.451 28.056 1.00 12.72 ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.908 -28.734 26.107 1.00 12.48 ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.434 -28.302 29.368 1.00 12.61 ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.884 -27.550 30.539 1.00 12.64 ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.196 -28.203 30.916 1.00 12.70 ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.228 -29.227 31.611 1.00 14.79 ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.854 -27.606 31.682 1.00 13.71 ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.489 -27.037 31.237 1.00 13.67 ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.495 -25.544 30.874 1.00 15.41 ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.133 -25.112 30.522 1.00 15.03 ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.872 -23.998 29.828 1.00 15.22 ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.853 -23.170 29.488 1.00 14.56 ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.610 -23.695 29.473 1.00 16.87 ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.300 -27.619 30.402 1.00 12.26 ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.639 -28.249 30.431 1.00 12.77 ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.681 -27.272 29.903 1.00 12.80 ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.364 -26.160 29.461 1.00 13.39 ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.588 -29.477 29.506 1.00 11.94 ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.438 -29.041 27.729 1.00 12.56 ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 32.976 -27.722 29.963 1.00 14.12 ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.101 -27.005 29.371 1.00 15.02 ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.766 -27.865 28.276 1.00 14.24 ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.969 -27.722 28.036 1.00 15.62 ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.114 -26.532 30.424 1.00 17.79 ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.820 -27.614 31.147 1.00 22.34 ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.507 -28.799 30.902 1.00 20.37 ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.772 -27.287 31.918 1.00 27.05 ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 33.994 -28.740 27.572 1.00 13.30 ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.572 -29.500 26.438 1.00 12.60 ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.228 -28.599 25.423 1.00 12.48 ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.797 -27.461 25.185 1.00 12.89 ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.499 -30.326 25.720 1.00 13.17 ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.872 -31.749 26.651 1.00 13.60 ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.281 -29.123 24.824 1.00 12.22 ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.974 -28.517 23.694 1.00 13.14 ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.051 -29.447 22.513 1.00 12.35 ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.819 -29.210 21.558 1.00 12.46 ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.391 -28.043 24.069 1.00 13.35 ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.397 -26.776 24.958 1.00 18.02 ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.772 -26.185 25.154 1.00 20.11 ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.311 -26.238 26.276 1.00 21.63 ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.373 -25.667 24.064 1.00 18.10 ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.249 -30.537 22.509 1.00 11.54 ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.152 -31.391 21.327 1.00 12.73 ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.664 -31.655 21.068 1.00 12.70 ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.865 -31.772 22.012 1.00 12.88 ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.887 -32.687 21.406 1.00 16.16 ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.329 -33.456 22.403 1.00 20.01 ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.354 -32.495 21.699 1.00 15.82 ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.283 -31.716 19.792 1.00 11.00 ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.865 -31.937 19.461 1.00 10.92 ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.740 -32.134 17.964 1.00 9.95  ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.738 -32.442 17.291 1.00 11.18 ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.512 -32.027 17.473 1.00 9.85  ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.230 -32.241 16.037 1.00 9.68  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.316 -31.121 15.596 1.00 9.55  ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.371 -30.794 16.307 1.00 10.67 ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.472 -33.597 15.873 1.00 10.29 ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.986 -33.795 14.438 1.00 11.81 ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.375 -34.786 16.288 1.00 11.47 ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.584 -30.516 14.425 1.00 9.93  ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.694 -29.448 13.911 1.00 8.98  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.126 -29.798 12.542 1.00 10.05 ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.798 -30.485 11.768 1.00 10.77 ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.364 -28.040 13.903 1.00 10.26 ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.241 -27.716 12.696 1.00 10.35 ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.524 -28.225 12.588 1.00 11.09 ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.775 -26.889 11.671 1.00 10.71 ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.332 -27.926 11.496 1.00 11.49 ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.592 -26.562 10.590 1.00 11.49 ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.865 -27.078 10.510 1.00 11.31 ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.734 -26.787 9.451  1.00 14.10 ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.967 -29.239 12.245 1.00 9.77  ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.365 -29.411 10.914 1.00 10.10 ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.742 -28.257 10.002 1.00 10.69 ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.505 -27.067 10.307 1.00 11.05 ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.834 -29.507 10.992 1.00 11.61 ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.251 -29.792 9.618  1.00 12.60 ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.592 -30.953 8.927  1.00 13.13 ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.375 -28.904 9.018  1.00 13.31 ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.092 -31.212 7.642  1.00 13.52 ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.864 -29.164 7.727  1.00 13.49 ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.232 -30.325 7.076  1.00 13.72 ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.774 -30.604 5.780  1.00 16.68 ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.261 -28.622 8.825  1.00 10.34 ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.676 -27.685 7.764  1.00 11.21 ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.741 -27.872 6.543  1.00 11.94 ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.913 -28.821 5.758  1.00 12.50 ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.121 -27.952 7.385  1.00 10.81 ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.714 -26.899 6.031  1.00 13.52 ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.739 -26.990 6.407  1.00 12.99 ? 66  SER   C N   1 
ATOM   1558 C  CA  A SER   B 1 60  ? 25.764 -27.162 5.336  0.50 14.50 ? 66  SER   C CA  1 
ATOM   1559 C  CA  B SER   B 1 60  ? 25.765 -27.136 5.335  0.50 13.63 ? 66  SER   C CA  1 
ATOM   1560 C  C   . SER   B 1 60  ? 26.391 -27.065 3.942  1.00 14.22 ? 66  SER   C C   1 
ATOM   1561 O  O   . SER   B 1 60  ? 25.980 -27.813 3.063  1.00 15.91 ? 66  SER   C O   1 
ATOM   1562 C  CB  A SER   B 1 60  ? 24.600 -26.199 5.487  0.50 17.35 ? 66  SER   C CB  1 
ATOM   1563 C  CB  B SER   B 1 60  ? 24.677 -26.086 5.445  0.50 13.84 ? 66  SER   C CB  1 
ATOM   1564 O  OG  A SER   B 1 60  ? 25.053 -24.858 5.468  0.50 20.23 ? 66  SER   C OG  1 
ATOM   1565 O  OG  B SER   B 1 60  ? 23.727 -26.334 4.423  0.50 12.44 ? 66  SER   C OG  1 
ATOM   1566 N  N   . SER   B 1 61  ? 27.404 -26.212 3.765  1.00 13.13 ? 67  SER   C N   1 
ATOM   1567 C  CA  . SER   B 1 61  ? 28.052 -26.067 2.441  1.00 13.83 ? 67  SER   C CA  1 
ATOM   1568 C  C   . SER   B 1 61  ? 28.871 -27.278 2.028  1.00 15.20 ? 67  SER   C C   1 
ATOM   1569 O  O   . SER   B 1 61  ? 29.286 -27.351 0.849  1.00 17.40 ? 67  SER   C O   1 
ATOM   1570 C  CB  . SER   B 1 61  ? 28.894 -24.815 2.415  1.00 15.27 ? 67  SER   C CB  1 
ATOM   1571 O  OG  . SER   B 1 61  ? 30.007 -24.924 3.278  1.00 15.60 ? 67  SER   C OG  1 
ATOM   1572 N  N   . ARG   B 1 62  ? 29.078 -28.269 2.900  1.00 13.54 ? 68  ARG   C N   1 
ATOM   1573 C  CA  . ARG   B 1 62  ? 29.708 -29.536 2.533  1.00 14.05 ? 68  ARG   C CA  1 
ATOM   1574 C  C   . ARG   B 1 62  ? 28.764 -30.733 2.744  1.00 14.85 ? 68  ARG   C C   1 
ATOM   1575 O  O   . ARG   B 1 62  ? 29.179 -31.875 2.579  1.00 16.11 ? 68  ARG   C O   1 
ATOM   1576 C  CB  . ARG   B 1 62  ? 30.980 -29.746 3.357  1.00 14.21 ? 68  ARG   C CB  1 
ATOM   1577 C  CG  . ARG   B 1 62  ? 32.033 -28.646 3.163  1.00 19.18 ? 68  ARG   C CG  1 
ATOM   1578 C  CD  . ARG   B 1 62  ? 32.687 -28.850 1.834  1.00 17.95 ? 68  ARG   C CD  1 
ATOM   1579 N  NE  . ARG   B 1 62  ? 33.727 -27.822 1.536  1.00 20.19 ? 68  ARG   C NE  1 
ATOM   1580 C  CZ  . ARG   B 1 62  ? 33.512 -26.643 0.966  1.00 21.65 ? 68  ARG   C CZ  1 
ATOM   1581 N  NH1 . ARG   B 1 62  ? 32.310 -26.333 0.493  1.00 23.46 ? 68  ARG   C NH1 1 
ATOM   1582 N  NH2 . ARG   B 1 62  ? 34.541 -25.836 0.674  1.00 25.10 ? 68  ARG   C NH2 1 
ATOM   1583 N  N   . ARG   B 1 63  ? 27.554 -30.480 3.285  1.00 15.04 ? 69  ARG   C N   1 
ATOM   1584 C  CA  . ARG   B 1 63  ? 26.622 -31.552 3.708  1.00 16.37 ? 69  ARG   C CA  1 
ATOM   1585 C  C   . ARG   B 1 63  ? 27.317 -32.581 4.599  1.00 17.13 ? 69  ARG   C C   1 
ATOM   1586 O  O   . ARG   B 1 63  ? 27.193 -33.804 4.403  1.00 19.53 ? 69  ARG   C O   1 
ATOM   1587 C  CB  . ARG   B 1 63  ? 26.001 -32.267 2.477  1.00 17.92 ? 69  ARG   C CB  1 
ATOM   1588 C  CG  . ARG   B 1 63  ? 25.154 -31.379 1.611  1.00 21.19 ? 69  ARG   C CG  1 
ATOM   1589 C  CD  . ARG   B 1 63  ? 23.904 -30.957 2.293  1.00 25.59 ? 69  ARG   C CD  1 
ATOM   1590 N  NE  . ARG   B 1 63  ? 22.914 -30.496 1.328  1.00 28.17 ? 69  ARG   C NE  1 
ATOM   1591 C  CZ  . ARG   B 1 63  ? 22.685 -29.226 1.032  1.00 28.07 ? 69  ARG   C CZ  1 
ATOM   1592 N  NH1 . ARG   B 1 63  ? 23.437 -28.263 1.560  1.00 25.95 ? 69  ARG   C NH1 1 
ATOM   1593 N  NH2 . ARG   B 1 63  ? 21.731 -28.905 0.171  1.00 28.56 ? 69  ARG   C NH2 1 
ATOM   1594 N  N   . LYS   B 1 64  ? 28.127 -32.079 5.565  1.00 14.16 ? 70  LYS   C N   1 
ATOM   1595 C  CA  . LYS   B 1 64  ? 28.925 -32.986 6.375  1.00 14.74 ? 70  LYS   C CA  1 
ATOM   1596 C  C   . LYS   B 1 64  ? 28.995 -32.502 7.802  1.00 13.10 ? 70  LYS   C C   1 
ATOM   1597 O  O   . LYS   B 1 64  ? 29.002 -31.279 8.056  1.00 13.96 ? 70  LYS   C O   1 
ATOM   1598 C  CB  . LYS   B 1 64  ? 30.346 -33.031 5.789  1.00 19.21 ? 70  LYS   C CB  1 
ATOM   1599 C  CG  . LYS   B 1 64  ? 30.474 -34.064 4.653  1.00 29.71 ? 70  LYS   C CG  1 
ATOM   1600 C  CD  . LYS   B 1 64  ? 31.919 -34.412 4.332  1.00 38.92 ? 70  LYS   C CD  1 
ATOM   1601 C  CE  . LYS   B 1 64  ? 31.997 -35.234 3.071  1.00 44.57 ? 70  LYS   C CE  1 
ATOM   1602 N  NZ  . LYS   B 1 64  ? 31.415 -34.507 1.909  1.00 48.53 ? 70  LYS   C NZ  1 
ATOM   1603 N  N   . HIS   B 1 65  ? 29.116 -33.459 8.710  1.00 12.17 ? 71  HIS   C N   1 
ATOM   1604 C  CA  . HIS   B 1 65  ? 29.404 -33.189 10.117 1.00 12.35 ? 71  HIS   C CA  1 
ATOM   1605 C  C   . HIS   B 1 65  ? 30.872 -33.469 10.320 1.00 14.21 ? 71  HIS   C C   1 
ATOM   1606 O  O   . HIS   B 1 65  ? 31.360 -34.577 9.998  1.00 17.52 ? 71  HIS   C O   1 
ATOM   1607 C  CB  . HIS   B 1 65  ? 28.572 -34.091 11.037 1.00 13.40 ? 71  HIS   C CB  1 
ATOM   1608 C  CG  . HIS   B 1 65  ? 27.100 -33.814 10.990 1.00 11.99 ? 71  HIS   C CG  1 
ATOM   1609 N  ND1 . HIS   B 1 65  ? 26.440 -33.060 11.948 1.00 14.79 ? 71  HIS   C ND1 1 
ATOM   1610 C  CD2 . HIS   B 1 65  ? 26.192 -34.235 10.078 1.00 11.86 ? 71  HIS   C CD2 1 
ATOM   1611 C  CE1 . HIS   B 1 65  ? 25.143 -33.060 11.601 1.00 12.84 ? 71  HIS   C CE1 1 
ATOM   1612 N  NE2 . HIS   B 1 65  ? 24.941 -33.777 10.512 1.00 15.50 ? 71  HIS   C NE2 1 
ATOM   1613 N  N   . TYR   B 1 66  ? 31.618 -32.507 10.891 1.00 11.95 ? 72  TYR   C N   1 
ATOM   1614 C  CA  . TYR   B 1 66  ? 33.071 -32.685 11.062 1.00 11.45 ? 72  TYR   C CA  1 
ATOM   1615 C  C   . TYR   B 1 66  ? 33.429 -32.729 12.555 1.00 10.64 ? 72  TYR   C C   1 
ATOM   1616 O  O   . TYR   B 1 66  ? 32.991 -31.852 13.311 1.00 10.88 ? 72  TYR   C O   1 
ATOM   1617 C  CB  . TYR   B 1 66  ? 33.798 -31.450 10.506 1.00 11.82 ? 72  TYR   C CB  1 
ATOM   1618 C  CG  . TYR   B 1 66  ? 33.772 -31.357 8.984  1.00 12.30 ? 72  TYR   C CG  1 
ATOM   1619 C  CD1 . TYR   B 1 66  ? 34.606 -32.147 8.205  1.00 15.12 ? 72  TYR   C CD1 1 
ATOM   1620 C  CD2 . TYR   B 1 66  ? 32.959 -30.441 8.331  1.00 13.58 ? 72  TYR   C CD2 1 
ATOM   1621 C  CE1 . TYR   B 1 66  ? 34.636 -32.021 6.812  1.00 15.68 ? 72  TYR   C CE1 1 
ATOM   1622 C  CE2 . TYR   B 1 66  ? 32.967 -30.316 6.943  1.00 14.86 ? 72  TYR   C CE2 1 
ATOM   1623 C  CZ  . TYR   B 1 66  ? 33.810 -31.108 6.194  1.00 15.02 ? 72  TYR   C CZ  1 
ATOM   1624 O  OH  . TYR   B 1 66  ? 33.783 -30.924 4.810  1.00 17.34 ? 72  TYR   C OH  1 
ATOM   1625 N  N   . PRO   B 1 67  ? 34.240 -33.698 12.968 1.00 10.74 ? 73  PRO   C N   1 
ATOM   1626 C  CA  . PRO   B 1 67  ? 34.767 -33.671 14.344 1.00 11.40 ? 73  PRO   C CA  1 
ATOM   1627 C  C   . PRO   B 1 67  ? 35.882 -32.613 14.444 1.00 11.78 ? 73  PRO   C C   1 
ATOM   1628 O  O   . PRO   B 1 67  ? 36.759 -32.540 13.563 1.00 14.06 ? 73  PRO   C O   1 
ATOM   1629 C  CB  . PRO   B 1 67  ? 35.382 -35.080 14.525 1.00 13.54 ? 73  PRO   C CB  1 
ATOM   1630 C  CG  . PRO   B 1 67  ? 35.646 -35.590 13.147 1.00 16.10 ? 73  PRO   C CG  1 
ATOM   1631 C  CD  . PRO   B 1 67  ? 34.741 -34.869 12.178 1.00 12.43 ? 73  PRO   C CD  1 
ATOM   1632 N  N   . VAL   B 1 68  ? 35.848 -31.796 15.482 1.00 10.66 ? 74  VAL   C N   1 
ATOM   1633 C  CA  . VAL   B 1 68  ? 36.815 -30.694 15.638 1.00 11.50 ? 74  VAL   C CA  1 
ATOM   1634 C  C   . VAL   B 1 68  ? 37.202 -30.526 17.079 1.00 11.39 ? 74  VAL   C C   1 
ATOM   1635 O  O   . VAL   B 1 68  ? 36.470 -30.819 18.014 1.00 11.35 ? 74  VAL   C O   1 
ATOM   1636 C  CB  . VAL   B 1 68  ? 36.215 -29.325 15.153 1.00 13.44 ? 74  VAL   C CB  1 
ATOM   1637 C  CG1 . VAL   B 1 68  ? 36.117 -29.247 13.611 1.00 15.27 ? 74  VAL   C CG1 1 
ATOM   1638 C  CG2 . VAL   B 1 68  ? 34.862 -29.039 15.825 1.00 13.40 ? 74  VAL   C CG2 1 
ATOM   1639 N  N   . SER   B 1 69  ? 38.429 -29.977 17.268 1.00 11.27 ? 75  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 69  ? 38.880 -29.350 18.506 1.00 11.28 ? 75  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 69  ? 38.593 -27.855 18.419 1.00 10.86 ? 75  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 69  ? 38.747 -27.255 17.327 1.00 11.63 ? 75  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 69  ? 40.383 -29.519 18.688 1.00 13.63 ? 75  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 69  ? 40.652 -30.901 18.765 1.00 19.64 ? 75  SER   C OG  1 
ATOM   1645 N  N   . PHE   B 1 70  ? 38.124 -27.243 19.477 1.00 10.56 ? 76  PHE   C N   1 
ATOM   1646 C  CA  . PHE   B 1 70  ? 37.766 -25.824 19.443 1.00 10.85 ? 76  PHE   C CA  1 
ATOM   1647 C  C   . PHE   B 1 70  ? 38.246 -25.091 20.683 1.00 11.28 ? 76  PHE   C C   1 
ATOM   1648 O  O   . PHE   B 1 70  ? 38.403 -25.702 21.748 1.00 11.95 ? 76  PHE   C O   1 
ATOM   1649 C  CB  . PHE   B 1 70  ? 36.251 -25.603 19.187 1.00 11.28 ? 76  PHE   C CB  1 
ATOM   1650 C  CG  . PHE   B 1 70  ? 35.330 -26.305 20.181 1.00 10.57 ? 76  PHE   C CG  1 
ATOM   1651 C  CD1 . PHE   B 1 70  ? 34.905 -27.609 19.957 1.00 11.25 ? 76  PHE   C CD1 1 
ATOM   1652 C  CD2 . PHE   B 1 70  ? 34.901 -25.655 21.328 1.00 11.62 ? 76  PHE   C CD2 1 
ATOM   1653 C  CE1 . PHE   B 1 70  ? 34.074 -28.246 20.874 1.00 10.69 ? 76  PHE   C CE1 1 
ATOM   1654 C  CE2 . PHE   B 1 70  ? 34.028 -26.303 22.229 1.00 11.58 ? 76  PHE   C CE2 1 
ATOM   1655 C  CZ  . PHE   B 1 70  ? 33.660 -27.601 22.006 1.00 11.56 ? 76  PHE   C CZ  1 
ATOM   1656 N  N   . SER   B 1 71  ? 38.515 -23.814 20.540 1.00 11.45 ? 77  SER   C N   1 
ATOM   1657 C  CA  . SER   B 1 71  ? 39.106 -23.032 21.616 1.00 12.47 ? 77  SER   C CA  1 
ATOM   1658 C  C   . SER   B 1 71  ? 38.109 -22.661 22.691 1.00 13.29 ? 77  SER   C C   1 
ATOM   1659 O  O   . SER   B 1 71  ? 36.893 -22.854 22.570 1.00 14.03 ? 77  SER   C O   1 
ATOM   1660 C  CB  . SER   B 1 71  ? 39.815 -21.810 21.021 1.00 13.34 ? 77  SER   C CB  1 
ATOM   1661 O  OG  . SER   B 1 71  ? 38.925 -20.910 20.365 1.00 15.10 ? 77  SER   C OG  1 
ATOM   1662 N  N   . LYS   B 1 72  ? 38.596 -22.054 23.773 1.00 16.15 ? 78  LYS   C N   1 
ATOM   1663 C  CA  . LYS   B 1 72  ? 37.713 -21.620 24.863 1.00 15.82 ? 78  LYS   C CA  1 
ATOM   1664 C  C   . LYS   B 1 72  ? 37.004 -20.306 24.460 1.00 15.09 ? 78  LYS   C C   1 
ATOM   1665 O  O   . LYS   B 1 72  ? 37.603 -19.492 23.750 1.00 16.77 ? 78  LYS   C O   1 
ATOM   1666 C  CB  . LYS   B 1 72  ? 38.544 -21.395 26.145 1.00 20.72 ? 78  LYS   C CB  1 
ATOM   1667 C  CG  . LYS   B 1 72  ? 39.276 -22.651 26.570 1.00 24.14 ? 78  LYS   C CG  1 
ATOM   1668 C  CD  . LYS   B 1 72  ? 39.518 -22.701 28.103 1.00 36.87 ? 78  LYS   C CD  1 
ATOM   1669 C  CE  . LYS   B 1 72  ? 39.624 -24.133 28.631 1.00 43.77 ? 78  LYS   C CE  1 
ATOM   1670 N  NZ  . LYS   B 1 72  ? 39.615 -24.195 30.127 1.00 47.69 ? 78  LYS   C NZ  1 
ATOM   1671 N  N   . PRO   B 1 73  ? 35.756 -20.061 24.916 1.00 14.49 ? 79  PRO   C N   1 
ATOM   1672 C  CA  . PRO   B 1 73  ? 35.032 -18.823 24.488 1.00 14.69 ? 79  PRO   C CA  1 
ATOM   1673 C  C   . PRO   B 1 73  ? 35.789 -17.566 24.868 1.00 15.40 ? 79  PRO   C C   1 
ATOM   1674 O  O   . PRO   B 1 73  ? 36.233 -17.425 26.022 1.00 18.15 ? 79  PRO   C O   1 
ATOM   1675 C  CB  . PRO   B 1 73  ? 33.715 -18.859 25.257 1.00 16.74 ? 79  PRO   C CB  1 
ATOM   1676 C  CG  . PRO   B 1 73  ? 33.554 -20.281 25.700 1.00 19.65 ? 79  PRO   C CG  1 
ATOM   1677 C  CD  . PRO   B 1 73  ? 34.939 -20.917 25.808 1.00 16.08 ? 79  PRO   C CD  1 
ATOM   1678 N  N   . SER   B 1 74  ? 36.042 -16.685 23.896 1.00 14.88 ? 80  SER   C N   1 
ATOM   1679 C  CA  . SER   B 1 74  ? 36.918 -15.527 24.120 1.00 16.14 ? 80  SER   C CA  1 
ATOM   1680 C  C   . SER   B 1 74  ? 36.509 -14.359 23.214 1.00 16.03 ? 80  SER   C C   1 
ATOM   1681 O  O   . SER   B 1 74  ? 35.631 -14.506 22.362 1.00 15.28 ? 80  SER   C O   1 
ATOM   1682 C  CB  . SER   B 1 74  ? 38.365 -15.893 23.761 1.00 19.32 ? 80  SER   C CB  1 
ATOM   1683 O  OG  . SER   B 1 74  ? 38.779 -17.105 24.370 1.00 27.06 ? 80  SER   C OG  1 
ATOM   1684 N  N   . LEU   B 1 75  ? 37.175 -13.216 23.397 1.00 16.74 ? 81  LEU   C N   1 
ATOM   1685 C  CA  . LEU   B 1 75  ? 36.987 -12.000 22.593 1.00 17.80 ? 81  LEU   C CA  1 
ATOM   1686 C  C   . LEU   B 1 75  ? 38.013 -12.049 21.449 1.00 18.94 ? 81  LEU   C C   1 
ATOM   1687 O  O   . LEU   B 1 75  ? 39.249 -11.992 21.702 1.00 21.24 ? 81  LEU   C O   1 
ATOM   1688 C  CB  . LEU   B 1 75  ? 37.220 -10.750 23.481 1.00 19.85 ? 81  LEU   C CB  1 
ATOM   1689 C  CG  . LEU   B 1 75  ? 36.961 -9.407  22.844 1.00 22.91 ? 81  LEU   C CG  1 
ATOM   1690 C  CD1 . LEU   B 1 75  ? 35.477 -9.212  22.591 1.00 22.38 ? 81  LEU   C CD1 1 
ATOM   1691 C  CD2 . LEU   B 1 75  ? 37.517 -8.276  23.747 1.00 25.47 ? 81  LEU   C CD2 1 
ATOM   1692 N  N   . ILE   B 1 76  ? 37.555 -12.262 20.225 1.00 19.60 ? 82  ILE   C N   1 
ATOM   1693 C  CA  . ILE   B 1 76  ? 38.397 -12.496 19.052 1.00 21.34 ? 82  ILE   C CA  1 
ATOM   1694 C  C   . ILE   B 1 76  ? 38.120 -11.454 17.983 1.00 20.24 ? 82  ILE   C C   1 
ATOM   1695 O  O   . ILE   B 1 76  ? 36.942 -11.139 17.724 1.00 18.57 ? 82  ILE   C O   1 
ATOM   1696 C  CB  . ILE   B 1 76  ? 38.017 -13.890 18.487 1.00 23.40 ? 82  ILE   C CB  1 
ATOM   1697 C  CG1 . ILE   B 1 76  ? 38.190 -15.022 19.552 1.00 25.92 ? 82  ILE   C CG1 1 
ATOM   1698 C  CG2 . ILE   B 1 76  ? 38.715 -14.215 17.148 1.00 25.42 ? 82  ILE   C CG2 1 
ATOM   1699 C  CD1 . ILE   B 1 76  ? 39.439 -15.898 19.532 1.00 28.26 ? 82  ILE   C CD1 1 
ATOM   1700 N  N   . PHE   B 1 77  ? 39.180 -10.928 17.329 1.00 20.08 ? 83  PHE   C N   1 
ATOM   1701 C  CA  . PHE   B 1 77  ? 38.990 -10.002 16.221 1.00 19.92 ? 83  PHE   C CA  1 
ATOM   1702 C  C   . PHE   B 1 77  ? 38.615 -10.865 14.990 1.00 21.52 ? 83  PHE   C C   1 
ATOM   1703 O  O   . PHE   B 1 77  ? 39.304 -11.840 14.641 1.00 23.85 ? 83  PHE   C O   1 
ATOM   1704 C  CB  . PHE   B 1 77  ? 40.288 -9.204  15.929 1.00 20.40 ? 83  PHE   C CB  1 
ATOM   1705 C  CG  . PHE   B 1 77  ? 40.016 -8.058  14.978 1.00 21.87 ? 83  PHE   C CG  1 
ATOM   1706 C  CD1 . PHE   B 1 77  ? 39.304 -6.950  15.392 1.00 23.56 ? 83  PHE   C CD1 1 
ATOM   1707 C  CD2 . PHE   B 1 77  ? 40.383 -8.141  13.632 1.00 24.10 ? 83  PHE   C CD2 1 
ATOM   1708 C  CE1 . PHE   B 1 77  ? 38.993 -5.919  14.502 1.00 25.18 ? 83  PHE   C CE1 1 
ATOM   1709 C  CE2 . PHE   B 1 77  ? 40.077 -7.103  12.752 1.00 24.44 ? 83  PHE   C CE2 1 
ATOM   1710 C  CZ  . PHE   B 1 77  ? 39.417 -5.994  13.200 1.00 24.60 ? 83  PHE   C CZ  1 
ATOM   1711 N  N   . VAL   B 1 78  ? 37.493 -10.517 14.356 1.00 18.23 ? 84  VAL   C N   1 
ATOM   1712 C  CA  . VAL   B 1 78  ? 36.983 -11.248 13.208 1.00 18.10 ? 84  VAL   C CA  1 
ATOM   1713 C  C   . VAL   B 1 78  ? 37.087 -10.316 11.993 1.00 17.27 ? 84  VAL   C C   1 
ATOM   1714 O  O   . VAL   B 1 78  ? 36.586 -9.184  12.078 1.00 17.92 ? 84  VAL   C O   1 
ATOM   1715 C  CB  . VAL   B 1 78  ? 35.495 -11.653 13.494 1.00 18.14 ? 84  VAL   C CB  1 
ATOM   1716 C  CG1 . VAL   B 1 78  ? 34.948 -12.449 12.322 1.00 18.14 ? 84  VAL   C CG1 1 
ATOM   1717 C  CG2 . VAL   B 1 78  ? 35.376 -12.466 14.798 1.00 18.91 ? 84  VAL   C CG2 1 
ATOM   1718 N  N   . GLU   B 1 79  ? 37.594 -10.798 10.840 1.00 17.10 ? 85  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 79  ? 37.637 -9.972  9.628  1.00 17.48 ? 85  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 79  ? 36.225 -9.735  9.084  1.00 17.00 ? 85  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 79  ? 35.268 -10.426 9.455  1.00 16.45 ? 85  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 79  ? 38.507 -10.643 8.546  1.00 20.29 ? 85  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 79  ? 39.995 -10.698 8.902  1.00 23.21 ? 85  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 79  ? 40.616 -9.324  9.145  1.00 28.91 ? 85  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 79  ? 40.250 -8.343  8.448  1.00 32.22 ? 85  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 79  ? 41.463 -9.212  10.062 1.00 33.19 ? 85  GLU   C OE2 1 
ATOM   1727 N  N   . ALA   B 1 80  ? 36.077 -8.734  8.226  1.00 17.38 ? 86  ALA   C N   1 
ATOM   1728 C  CA  . ALA   B 1 80  ? 34.789 -8.405  7.640  1.00 18.75 ? 86  ALA   C CA  1 
ATOM   1729 C  C   . ALA   B 1 80  ? 34.178 -9.602  6.920  1.00 18.94 ? 86  ALA   C C   1 
ATOM   1730 O  O   . ALA   B 1 80  ? 34.910 -10.399 6.320  1.00 20.68 ? 86  ALA   C O   1 
ATOM   1731 C  CB  . ALA   B 1 80  ? 34.970 -7.257  6.641  1.00 20.69 ? 86  ALA   C CB  1 
ATOM   1732 N  N   . SER   B 1 81  ? 32.883 -9.768  7.072  1.00 17.78 ? 87  SER   C N   1 
ATOM   1733 C  CA  . SER   B 1 81  ? 32.170 -10.801 6.376  1.00 19.15 ? 87  SER   C CA  1 
ATOM   1734 C  C   . SER   B 1 81  ? 31.068 -10.131 5.569  1.00 19.68 ? 87  SER   C C   1 
ATOM   1735 O  O   . SER   B 1 81  ? 30.913 -8.886  5.594  1.00 20.23 ? 87  SER   C O   1 
ATOM   1736 C  CB  . SER   B 1 81  ? 31.561 -11.770 7.392  1.00 17.71 ? 87  SER   C CB  1 
ATOM   1737 O  OG  . SER   B 1 81  ? 30.518 -11.105 8.104  1.00 17.14 ? 87  SER   C OG  1 
ATOM   1738 N  N   . GLU   B 1 82  ? 30.240 -10.938 4.920  1.00 20.21 ? 88  GLU   C N   1 
ATOM   1739 C  CA  . GLU   B 1 82  ? 29.133 -10.322 4.182  1.00 21.74 ? 88  GLU   C CA  1 
ATOM   1740 C  C   . GLU   B 1 82  ? 28.074 -9.685  5.100  1.00 21.65 ? 88  GLU   C C   1 
ATOM   1741 O  O   . GLU   B 1 82  ? 27.320 -8.813  4.641  1.00 23.59 ? 88  GLU   C O   1 
ATOM   1742 C  CB  . GLU   B 1 82  ? 28.534 -11.308 3.188  1.00 27.19 ? 88  GLU   C CB  1 
ATOM   1743 C  CG  . GLU   B 1 82  ? 27.665 -12.401 3.741  1.00 35.22 ? 88  GLU   C CG  1 
ATOM   1744 C  CD  . GLU   B 1 82  ? 27.041 -13.208 2.617  1.00 40.62 ? 88  GLU   C CD  1 
ATOM   1745 O  OE1 . GLU   B 1 82  ? 27.738 -13.443 1.601  1.00 40.89 ? 88  GLU   C OE1 1 
ATOM   1746 O  OE2 . GLU   B 1 82  ? 25.857 -13.601 2.752  1.00 42.53 ? 88  GLU   C OE2 1 
ATOM   1747 N  N   . TYR   B 1 83  ? 28.085 -10.006 6.395  1.00 18.29 ? 89  TYR   C N   1 
ATOM   1748 C  CA  . TYR   B 1 83  ? 27.055 -9.532  7.303  1.00 17.87 ? 89  TYR   C CA  1 
ATOM   1749 C  C   . TYR   B 1 83  ? 27.555 -8.704  8.497  1.00 18.93 ? 89  TYR   C C   1 
ATOM   1750 O  O   . TYR   B 1 83  ? 26.707 -8.134  9.197  1.00 19.25 ? 89  TYR   C O   1 
ATOM   1751 C  CB  . TYR   B 1 83  ? 26.190 -10.724 7.782  1.00 17.07 ? 89  TYR   C CB  1 
ATOM   1752 C  CG  . TYR   B 1 83  ? 27.014 -11.922 8.257  1.00 16.66 ? 89  TYR   C CG  1 
ATOM   1753 C  CD1 . TYR   B 1 83  ? 27.443 -12.907 7.367  1.00 16.96 ? 89  TYR   C CD1 1 
ATOM   1754 C  CD2 . TYR   B 1 83  ? 27.376 -12.061 9.589  1.00 15.85 ? 89  TYR   C CD2 1 
ATOM   1755 C  CE1 . TYR   B 1 83  ? 28.211 -14.001 7.795  1.00 16.53 ? 89  TYR   C CE1 1 
ATOM   1756 C  CE2 . TYR   B 1 83  ? 28.162 -13.130 10.027 1.00 16.20 ? 89  TYR   C CE2 1 
ATOM   1757 C  CZ  . TYR   B 1 83  ? 28.579 -14.108 9.126  1.00 15.78 ? 89  TYR   C CZ  1 
ATOM   1758 O  OH  . TYR   B 1 83  ? 29.383 -15.158 9.536  1.00 16.83 ? 89  TYR   C OH  1 
ATOM   1759 N  N   . TYR   B 1 84  ? 28.854 -8.577  8.737  1.00 16.89 ? 90  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 84  ? 29.377 -7.657  9.772  1.00 16.90 ? 90  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 84  ? 30.693 -7.029  9.260  1.00 16.86 ? 90  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 84  ? 31.427 -7.662  8.498  1.00 16.92 ? 90  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 84  ? 29.749 -8.402  11.099 1.00 15.75 ? 90  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 84  ? 28.567 -8.824  11.951 1.00 14.80 ? 90  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 84  ? 27.624 -7.894  12.402 1.00 15.21 ? 90  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 84  ? 28.382 -10.148 12.296 1.00 14.40 ? 90  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 84  ? 26.558 -8.287  13.222 1.00 15.68 ? 90  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 84  ? 27.322 -10.550 13.095 1.00 13.95 ? 90  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 84  ? 26.404 -9.627  13.539 1.00 14.51 ? 90  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 84  ? 25.346 -10.024 14.325 1.00 14.59 ? 90  TYR   C OH  1 
ATOM   1771 N  N   . PRO   B 1 85  ? 31.066 -5.827  9.735  1.00 17.72 ? 91  PRO   C N   1 
ATOM   1772 C  CA  . PRO   B 1 85  ? 32.422 -5.311  9.438  1.00 17.59 ? 91  PRO   C CA  1 
ATOM   1773 C  C   . PRO   B 1 85  ? 33.457 -6.079  10.272 1.00 17.78 ? 91  PRO   C C   1 
ATOM   1774 O  O   . PRO   B 1 85  ? 33.097 -6.887  11.184 1.00 16.88 ? 91  PRO   C O   1 
ATOM   1775 C  CB  . PRO   B 1 85  ? 32.297 -3.844  9.900  1.00 18.76 ? 91  PRO   C CB  1 
ATOM   1776 C  CG  . PRO   B 1 85  ? 31.399 -3.934  11.065 1.00 19.01 ? 91  PRO   C CG  1 
ATOM   1777 C  CD  . PRO   B 1 85  ? 30.326 -4.981  10.706 1.00 18.30 ? 91  PRO   C CD  1 
ATOM   1778 N  N   . ALA   B 1 86  ? 34.760 -5.808  10.040 1.00 17.00 ? 92  ALA   C N   1 
ATOM   1779 C  CA  . ALA   B 1 86  ? 35.806 -6.352  10.897 1.00 19.00 ? 92  ALA   C CA  1 
ATOM   1780 C  C   . ALA   B 1 86  ? 35.595 -5.781  12.312 1.00 20.14 ? 92  ALA   C C   1 
ATOM   1781 O  O   . ALA   B 1 86  ? 35.289 -4.577  12.454 1.00 22.16 ? 92  ALA   C O   1 
ATOM   1782 C  CB  . ALA   B 1 86  ? 37.176 -5.933  10.363 1.00 19.52 ? 92  ALA   C CB  1 
ATOM   1783 N  N   . ARG   B 1 87  ? 35.615 -6.665  13.326 1.00 19.45 ? 93  ARG   C N   1 
ATOM   1784 C  CA  . ARG   B 1 87  ? 35.293 -6.220  14.675 1.00 19.54 ? 93  ARG   C CA  1 
ATOM   1785 C  C   . ARG   B 1 87  ? 35.678 -7.293  15.687 1.00 18.63 ? 93  ARG   C C   1 
ATOM   1786 O  O   . ARG   B 1 87  ? 35.930 -8.435  15.322 1.00 18.33 ? 93  ARG   C O   1 
ATOM   1787 C  CB  . ARG   B 1 87  ? 33.764 -5.948  14.822 1.00 19.96 ? 93  ARG   C CB  1 
ATOM   1788 C  CG  . ARG   B 1 87  ? 32.950 -7.253  14.674 1.00 18.72 ? 93  ARG   C CG  1 
ATOM   1789 C  CD  . ARG   B 1 87  ? 31.468 -6.988  14.826 1.00 18.57 ? 93  ARG   C CD  1 
ATOM   1790 N  NE  . ARG   B 1 87  ? 30.759 -8.267  15.075 1.00 17.67 ? 93  ARG   C NE  1 
ATOM   1791 C  CZ  . ARG   B 1 87  ? 29.671 -8.435  15.805 1.00 18.05 ? 93  ARG   C CZ  1 
ATOM   1792 N  NH1 . ARG   B 1 87  ? 29.047 -7.382  16.339 1.00 18.12 ? 93  ARG   C NH1 1 
ATOM   1793 N  NH2 . ARG   B 1 87  ? 29.199 -9.659  16.019 1.00 18.46 ? 93  ARG   C NH2 1 
ATOM   1794 N  N   . TYR   B 1 88  ? 35.606 -6.930  16.995 1.00 20.10 ? 94  TYR   C N   1 
ATOM   1795 C  CA  . TYR   B 1 88  ? 35.762 -7.929  18.046 1.00 21.41 ? 94  TYR   C CA  1 
ATOM   1796 C  C   . TYR   B 1 88  ? 34.387 -8.585  18.314 1.00 19.11 ? 94  TYR   C C   1 
ATOM   1797 O  O   . TYR   B 1 88  ? 33.377 -7.904  18.452 1.00 20.04 ? 94  TYR   C O   1 
ATOM   1798 C  CB  . TYR   B 1 88  ? 36.237 -7.276  19.362 1.00 23.79 ? 94  TYR   C CB  1 
ATOM   1799 C  CG  . TYR   B 1 88  ? 37.703 -6.946  19.292 1.00 26.64 ? 94  TYR   C CG  1 
ATOM   1800 C  CD1 . TYR   B 1 88  ? 38.658 -7.926  19.483 1.00 28.05 ? 94  TYR   C CD1 1 
ATOM   1801 C  CD2 . TYR   B 1 88  ? 38.129 -5.672  18.911 1.00 27.76 ? 94  TYR   C CD2 1 
ATOM   1802 C  CE1 . TYR   B 1 88  ? 40.014 -7.641  19.353 1.00 29.45 ? 94  TYR   C CE1 1 
ATOM   1803 C  CE2 . TYR   B 1 88  ? 39.470 -5.374  18.780 1.00 28.83 ? 94  TYR   C CE2 1 
ATOM   1804 C  CZ  . TYR   B 1 88  ? 40.412 -6.356  19.011 1.00 29.86 ? 94  TYR   C CZ  1 
ATOM   1805 O  OH  . TYR   B 1 88  ? 41.742 -6.013  18.880 1.00 33.26 ? 94  TYR   C OH  1 
ATOM   1806 N  N   . GLN   B 1 89  ? 34.361 -9.913  18.372 1.00 16.90 ? 95  GLN   C N   1 
ATOM   1807 C  CA  . GLN   B 1 89  ? 33.156 -10.659 18.732 1.00 15.26 ? 95  GLN   C CA  1 
ATOM   1808 C  C   . GLN   B 1 89  ? 33.476 -11.389 20.033 1.00 14.89 ? 95  GLN   C C   1 
ATOM   1809 O  O   . GLN   B 1 89  ? 34.574 -11.982 20.177 1.00 16.06 ? 95  GLN   C O   1 
ATOM   1810 C  CB  . GLN   B 1 89  ? 32.793 -11.609 17.582 1.00 16.42 ? 95  GLN   C CB  1 
ATOM   1811 C  CG  . GLN   B 1 89  ? 31.536 -12.420 17.879 1.00 16.36 ? 95  GLN   C CG  1 
ATOM   1812 C  CD  . GLN   B 1 89  ? 30.843 -12.984 16.662 1.00 15.61 ? 95  GLN   C CD  1 
ATOM   1813 O  OE1 . GLN   B 1 89  ? 30.816 -12.397 15.559 1.00 16.44 ? 95  GLN   C OE1 1 
ATOM   1814 N  NE2 . GLN   B 1 89  ? 30.249 -14.139 16.871 1.00 14.48 ? 95  GLN   C NE2 1 
ATOM   1815 N  N   . SER   B 1 90  ? 32.557 -11.375 20.965 1.00 14.52 ? 96  SER   C N   1 
ATOM   1816 C  CA  . SER   B 1 90  ? 32.739 -11.986 22.265 1.00 14.62 ? 96  SER   C CA  1 
ATOM   1817 C  C   . SER   B 1 90  ? 32.149 -13.397 22.328 1.00 14.03 ? 96  SER   C C   1 
ATOM   1818 O  O   . SER   B 1 90  ? 31.299 -13.774 21.522 1.00 13.52 ? 96  SER   C O   1 
ATOM   1819 C  CB  . SER   B 1 90  ? 32.176 -11.096 23.385 1.00 16.25 ? 96  SER   C CB  1 
ATOM   1820 O  OG  . SER   B 1 90  ? 30.780 -11.071 23.255 1.00 16.96 ? 96  SER   C OG  1 
ATOM   1821 N  N   . HIS   B 1 91  ? 32.608 -14.177 23.324 1.00 13.89 ? 97  HIS   C N   1 
ATOM   1822 C  CA  . HIS   B 1 91  ? 32.117 -15.539 23.594 1.00 13.58 ? 97  HIS   C CA  1 
ATOM   1823 C  C   . HIS   B 1 91  ? 32.223 -16.415 22.324 1.00 13.16 ? 97  HIS   C C   1 
ATOM   1824 O  O   . HIS   B 1 91  ? 31.317 -17.227 22.077 1.00 13.66 ? 97  HIS   C O   1 
ATOM   1825 C  CB  . HIS   B 1 91  ? 30.660 -15.511 24.152 1.00 14.10 ? 97  HIS   C CB  1 
ATOM   1826 C  CG  . HIS   B 1 91  ? 30.524 -14.759 25.457 1.00 15.48 ? 97  HIS   C CG  1 
ATOM   1827 N  ND1 . HIS   B 1 91  ? 30.536 -15.406 26.667 1.00 17.81 ? 97  HIS   C ND1 1 
ATOM   1828 C  CD2 . HIS   B 1 91  ? 30.439 -13.423 25.683 1.00 16.45 ? 97  HIS   C CD2 1 
ATOM   1829 C  CE1 . HIS   B 1 91  ? 30.405 -14.476 27.600 1.00 18.95 ? 97  HIS   C CE1 1 
ATOM   1830 N  NE2 . HIS   B 1 91  ? 30.336 -13.262 27.054 1.00 18.61 ? 97  HIS   C NE2 1 
ATOM   1831 N  N   . LEU   B 1 92  ? 33.307 -16.262 21.581 1.00 12.36 ? 98  LEU   C N   1 
ATOM   1832 C  CA  . LEU   B 1 92  ? 33.485 -16.955 20.324 1.00 12.54 ? 98  LEU   C CA  1 
ATOM   1833 C  C   . LEU   B 1 92  ? 34.572 -18.023 20.514 1.00 12.64 ? 98  LEU   C C   1 
ATOM   1834 O  O   . LEU   B 1 92  ? 35.545 -17.811 21.228 1.00 13.23 ? 98  LEU   C O   1 
ATOM   1835 C  CB  . LEU   B 1 92  ? 33.983 -15.948 19.227 1.00 13.53 ? 98  LEU   C CB  1 
ATOM   1836 C  CG  . LEU   B 1 92  ? 34.074 -16.526 17.816 1.00 14.68 ? 98  LEU   C CG  1 
ATOM   1837 C  CD1 . LEU   B 1 92  ? 32.720 -16.862 17.273 1.00 15.29 ? 98  LEU   C CD1 1 
ATOM   1838 C  CD2 . LEU   B 1 92  ? 34.765 -15.514 16.847 1.00 16.89 ? 98  LEU   C CD2 1 
ATOM   1839 N  N   . MET   B 1 93  ? 34.405 -19.171 19.855 1.00 12.15 ? 99  MET   C N   1 
ATOM   1840 C  CA  . MET   B 1 93  ? 35.344 -20.308 19.916 1.00 11.13 ? 99  MET   C CA  1 
ATOM   1841 C  C   . MET   B 1 93  ? 35.753 -20.615 18.480 1.00 12.31 ? 99  MET   C C   1 
ATOM   1842 O  O   . MET   B 1 93  ? 34.882 -20.650 17.608 1.00 12.79 ? 99  MET   C O   1 
ATOM   1843 C  CB  . MET   B 1 93  ? 34.613 -21.516 20.490 1.00 12.69 ? 99  MET   C CB  1 
ATOM   1844 C  CG  . MET   B 1 93  ? 34.127 -21.254 21.918 1.00 14.94 ? 99  MET   C CG  1 
ATOM   1845 S  SD  . MET   B 1 93  ? 33.108 -22.590 22.551 1.00 15.36 ? 99  MET   C SD  1 
ATOM   1846 C  CE  . MET   B 1 93  ? 31.611 -22.437 21.436 1.00 16.72 ? 99  MET   C CE  1 
ATOM   1847 N  N   . LEU   B 1 94  ? 37.027 -20.900 18.213 1.00 11.81 ? 100 LEU   C N   1 
ATOM   1848 C  CA  . LEU   B 1 94  ? 37.472 -21.177 16.852 1.00 12.10 ? 100 LEU   C CA  1 
ATOM   1849 C  C   . LEU   B 1 94  ? 37.921 -22.626 16.712 1.00 11.25 ? 100 LEU   C C   1 
ATOM   1850 O  O   . LEU   B 1 94  ? 38.456 -23.219 17.669 1.00 12.95 ? 100 LEU   C O   1 
ATOM   1851 C  CB  . LEU   B 1 94  ? 38.721 -20.316 16.465 1.00 12.91 ? 100 LEU   C CB  1 
ATOM   1852 C  CG  . LEU   B 1 94  ? 38.545 -18.810 16.414 1.00 15.12 ? 100 LEU   C CG  1 
ATOM   1853 C  CD1 . LEU   B 1 94  ? 39.860 -18.143 15.979 1.00 19.23 ? 100 LEU   C CD1 1 
ATOM   1854 C  CD2 . LEU   B 1 94  ? 37.401 -18.399 15.488 1.00 15.84 ? 100 LEU   C CD2 1 
ATOM   1855 N  N   . ALA   B 1 95  ? 37.773 -23.145 15.502 1.00 12.05 ? 101 ALA   C N   1 
ATOM   1856 C  CA  . ALA   B 1 95  ? 38.340 -24.438 15.112 1.00 12.09 ? 101 ALA   C CA  1 
ATOM   1857 C  C   . ALA   B 1 95  ? 38.892 -24.299 13.678 1.00 12.26 ? 101 ALA   C C   1 
ATOM   1858 O  O   . ALA   B 1 95  ? 38.507 -23.391 12.937 1.00 11.79 ? 101 ALA   C O   1 
ATOM   1859 C  CB  . ALA   B 1 95  ? 37.250 -25.537 15.148 1.00 12.09 ? 101 ALA   C CB  1 
ATOM   1860 N  N   . VAL   B 1 96  ? 39.757 -25.227 13.289 1.00 12.04 ? 102 VAL   C N   1 
ATOM   1861 C  CA  . VAL   B 1 96  ? 40.212 -25.315 11.905 1.00 13.30 ? 102 VAL   C CA  1 
ATOM   1862 C  C   . VAL   B 1 96  ? 39.136 -26.062 11.091 1.00 13.26 ? 102 VAL   C C   1 
ATOM   1863 O  O   . VAL   B 1 96  ? 38.810 -27.230 11.405 1.00 14.38 ? 102 VAL   C O   1 
ATOM   1864 C  CB  . VAL   B 1 96  ? 41.587 -26.035 11.881 1.00 14.61 ? 102 VAL   C CB  1 
ATOM   1865 C  CG1 . VAL   B 1 96  ? 42.048 -26.208 10.437 1.00 16.90 ? 102 VAL   C CG1 1 
ATOM   1866 C  CG2 . VAL   B 1 96  ? 42.607 -25.231 12.692 1.00 15.37 ? 102 VAL   C CG2 1 
ATOM   1867 N  N   . GLY   B 1 97  ? 38.543 -25.387 10.131 1.00 14.13 ? 103 GLY   C N   1 
ATOM   1868 C  CA  . GLY   B 1 97  ? 37.504 -26.014 9.333  1.00 15.20 ? 103 GLY   C CA  1 
ATOM   1869 C  C   . GLY   B 1 97  ? 36.822 -25.040 8.431  1.00 14.36 ? 103 GLY   C C   1 
ATOM   1870 O  O   . GLY   B 1 97  ? 37.106 -23.831 8.453  1.00 17.37 ? 103 GLY   C O   1 
ATOM   1871 N  N   . HIS   B 1 98  ? 35.943 -25.572 7.595  1.00 14.40 ? 104 HIS   C N   1 
ATOM   1872 C  CA  . HIS   B 1 98  ? 35.245 -24.778 6.615  1.00 14.63 ? 104 HIS   C CA  1 
ATOM   1873 C  C   . HIS   B 1 98  ? 33.982 -24.089 7.130  1.00 13.71 ? 104 HIS   C C   1 
ATOM   1874 O  O   . HIS   B 1 98  ? 33.163 -24.708 7.830  1.00 13.27 ? 104 HIS   C O   1 
ATOM   1875 C  CB  . HIS   B 1 98  ? 34.939 -25.635 5.418  1.00 18.19 ? 104 HIS   C CB  1 
ATOM   1876 C  CG  . HIS   B 1 98  ? 34.437 -24.823 4.303  1.00 20.13 ? 104 HIS   C CG  1 
ATOM   1877 N  ND1 . HIS   B 1 98  ? 35.228 -23.856 3.667  1.00 21.31 ? 104 HIS   C ND1 1 
ATOM   1878 C  CD2 . HIS   B 1 98  ? 33.184 -24.767 3.814  1.00 21.82 ? 104 HIS   C CD2 1 
ATOM   1879 C  CE1 . HIS   B 1 98  ? 34.412 -23.250 2.817  1.00 23.62 ? 104 HIS   C CE1 1 
ATOM   1880 N  NE2 . HIS   B 1 98  ? 33.188 -23.786 2.843  1.00 23.78 ? 104 HIS   C NE2 1 
ATOM   1881 N  N   . SER   B 1 99  ? 33.770 -22.823 6.732  1.00 14.08 ? 105 SER   C N   1 
ATOM   1882 C  CA  . SER   B 1 99  ? 32.545 -22.086 7.139  1.00 14.57 ? 105 SER   C CA  1 
ATOM   1883 C  C   . SER   B 1 99  ? 32.300 -20.944 6.122  1.00 16.08 ? 105 SER   C C   1 
ATOM   1884 O  O   . SER   B 1 99  ? 33.168 -20.055 6.023  1.00 18.24 ? 105 SER   C O   1 
ATOM   1885 C  CB  . SER   B 1 99  ? 32.802 -21.483 8.523  1.00 15.53 ? 105 SER   C CB  1 
ATOM   1886 O  OG  . SER   B 1 99  ? 31.692 -20.660 8.883  1.00 16.39 ? 105 SER   C OG  1 
ATOM   1887 N  N   . GLU   B 1 100 ? 31.199 -21.003 5.391  1.00 16.15 ? 106 GLU   C N   1 
ATOM   1888 C  CA  . GLU   B 1 100 ? 30.717 -19.990 4.403  1.00 17.32 ? 106 GLU   C CA  1 
ATOM   1889 C  C   . GLU   B 1 100 ? 29.594 -19.236 5.151  1.00 15.25 ? 106 GLU   C C   1 
ATOM   1890 O  O   . GLU   B 1 100 ? 29.037 -19.728 6.137  1.00 14.87 ? 106 GLU   C O   1 
ATOM   1891 C  CB  . GLU   B 1 100 ? 29.994 -20.679 3.202  1.00 20.12 ? 106 GLU   C CB  1 
ATOM   1892 C  CG  . GLU   B 1 100 ? 30.642 -21.783 2.434  1.00 27.74 ? 106 GLU   C CG  1 
ATOM   1893 C  CD  . GLU   B 1 100 ? 31.490 -21.340 1.286  1.00 28.96 ? 106 GLU   C CD  1 
ATOM   1894 O  OE1 . GLU   B 1 100 ? 32.139 -22.225 0.696  1.00 29.33 ? 106 GLU   C OE1 1 
ATOM   1895 O  OE2 . GLU   B 1 100 ? 31.579 -20.115 1.026  1.00 29.66 ? 106 GLU   C OE2 1 
ATOM   1896 N  N   . PRO   B 1 101 ? 29.170 -18.041 4.673  1.00 16.45 ? 107 PRO   C N   1 
ATOM   1897 C  CA  . PRO   B 1 101 ? 28.072 -17.331 5.370  1.00 15.60 ? 107 PRO   C CA  1 
ATOM   1898 C  C   . PRO   B 1 101 ? 26.813 -18.192 5.526  1.00 15.65 ? 107 PRO   C C   1 
ATOM   1899 O  O   . PRO   B 1 101 ? 26.204 -18.129 6.593  1.00 15.68 ? 107 PRO   C O   1 
ATOM   1900 C  CB  . PRO   B 1 101 ? 27.780 -16.113 4.435  1.00 18.04 ? 107 PRO   C CB  1 
ATOM   1901 C  CG  . PRO   B 1 101 ? 29.009 -15.939 3.692  1.00 21.58 ? 107 PRO   C CG  1 
ATOM   1902 C  CD  . PRO   B 1 101 ? 29.769 -17.222 3.589  1.00 18.66 ? 107 PRO   C CD  1 
ATOM   1903 N  N   . GLY   B 1 102 ? 26.483 -19.032 4.544  1.00 15.08 ? 108 GLY   C N   1 
ATOM   1904 C  CA  . GLY   B 1 102 ? 25.269 -19.848 4.637  1.00 15.39 ? 108 GLY   C CA  1 
ATOM   1905 C  C   . GLY   B 1 102 ? 25.367 -20.944 5.694  1.00 14.32 ? 108 GLY   C C   1 
ATOM   1906 O  O   . GLY   B 1 102 ? 24.367 -21.606 6.009  1.00 15.15 ? 108 GLY   C O   1 
ATOM   1907 N  N   . ASP   B 1 103 ? 26.574 -21.215 6.217  1.00 13.27 ? 109 ASP   C N   1 
ATOM   1908 C  CA  . ASP   B 1 103 ? 26.739 -22.233 7.258  1.00 12.13 ? 109 ASP   C CA  1 
ATOM   1909 C  C   . ASP   B 1 103 ? 26.359 -21.752 8.641  1.00 11.78 ? 109 ASP   C C   1 
ATOM   1910 O  O   . ASP   B 1 103 ? 26.255 -22.537 9.595  1.00 12.02 ? 109 ASP   C O   1 
ATOM   1911 C  CB  . ASP   B 1 103 ? 28.218 -22.696 7.269  1.00 14.28 ? 109 ASP   C CB  1 
ATOM   1912 C  CG  . ASP   B 1 103 ? 28.525 -23.503 6.042  1.00 14.32 ? 109 ASP   C CG  1 
ATOM   1913 O  OD1 . ASP   B 1 103 ? 27.669 -24.272 5.612  1.00 15.07 ? 109 ASP   C OD1 1 
ATOM   1914 O  OD2 . ASP   B 1 103 ? 29.666 -23.375 5.512  1.00 16.29 ? 109 ASP   C OD2 1 
ATOM   1915 N  N   . CYS   B 1 104 ? 26.166 -20.407 8.825  1.00 11.77 ? 110 CYS   C N   1 
ATOM   1916 C  CA  . CYS   B 1 104 ? 25.753 -19.874 10.124 1.00 11.20 ? 110 CYS   C CA  1 
ATOM   1917 C  C   . CYS   B 1 104 ? 24.507 -20.581 10.614 1.00 11.49 ? 110 CYS   C C   1 
ATOM   1918 O  O   . CYS   B 1 104 ? 23.564 -20.789 9.851  1.00 13.33 ? 110 CYS   C O   1 
ATOM   1919 C  CB  . CYS   B 1 104 ? 25.518 -18.357 10.053 1.00 11.96 ? 110 CYS   C CB  1 
ATOM   1920 S  SG  . CYS   B 1 104 ? 27.048 -17.391 9.956  1.00 14.15 ? 110 CYS   C SG  1 
ATOM   1921 N  N   . GLY   B 1 105 ? 24.493 -20.916 11.893 1.00 10.19 ? 111 GLY   C N   1 
ATOM   1922 C  CA  . GLY   B 1 105 ? 23.344 -21.592 12.513 1.00 11.47 ? 111 GLY   C CA  1 
ATOM   1923 C  C   . GLY   B 1 105 ? 23.558 -23.095 12.665 1.00 11.36 ? 111 GLY   C C   1 
ATOM   1924 O  O   . GLY   B 1 105 ? 22.793 -23.748 13.390 1.00 12.39 ? 111 GLY   C O   1 
ATOM   1925 N  N   . GLY   B 1 106 ? 24.585 -23.655 12.007 1.00 11.45 ? 112 GLY   C N   1 
ATOM   1926 C  CA  . GLY   B 1 106 ? 24.898 -25.095 12.171 1.00 12.00 ? 112 GLY   C CA  1 
ATOM   1927 C  C   . GLY   B 1 106 ? 25.289 -25.393 13.621 1.00 10.97 ? 112 GLY   C C   1 
ATOM   1928 O  O   . GLY   B 1 106 ? 26.018 -24.597 14.246 1.00 11.11 ? 112 GLY   C O   1 
ATOM   1929 N  N   . ILE   B 1 107 ? 24.849 -26.535 14.136 1.00 10.53 ? 113 ILE   C N   1 
ATOM   1930 C  CA  . ILE   B 1 107 ? 25.106 -26.846 15.544 1.00 10.35 ? 113 ILE   C CA  1 
ATOM   1931 C  C   . ILE   B 1 107 ? 26.479 -27.473 15.736 1.00 10.00 ? 113 ILE   C C   1 
ATOM   1932 O  O   . ILE   B 1 107 ? 26.903 -28.326 14.948 1.00 10.34 ? 113 ILE   C O   1 
ATOM   1933 C  CB  . ILE   B 1 107 ? 23.985 -27.829 16.036 1.00 12.76 ? 113 ILE   C CB  1 
ATOM   1934 C  CG1 . ILE   B 1 107 ? 22.736 -26.898 16.426 1.00 16.31 ? 113 ILE   C CG1 1 
ATOM   1935 C  CG2 . ILE   B 1 107 ? 24.409 -28.655 17.255 1.00 12.81 ? 113 ILE   C CG2 1 
ATOM   1936 C  CD1 . ILE   B 1 107 ? 21.402 -27.616 16.830 1.00 20.45 ? 113 ILE   C CD1 1 
ATOM   1937 N  N   . LEU   B 1 108 ? 27.155 -27.035 16.828 1.00 9.77  ? 114 LEU   C N   1 
ATOM   1938 C  CA  . LEU   B 1 108 ? 28.344 -27.712 17.381 1.00 9.40  ? 114 LEU   C CA  1 
ATOM   1939 C  C   . LEU   B 1 108 ? 27.823 -28.470 18.635 1.00 9.58  ? 114 LEU   C C   1 
ATOM   1940 O  O   . LEU   B 1 108 ? 27.180 -27.862 19.497 1.00 9.72  ? 114 LEU   C O   1 
ATOM   1941 C  CB  . LEU   B 1 108 ? 29.367 -26.640 17.798 1.00 9.72  ? 114 LEU   C CB  1 
ATOM   1942 C  CG  . LEU   B 1 108 ? 30.577 -27.151 18.597 1.00 10.41 ? 114 LEU   C CG  1 
ATOM   1943 C  CD1 . LEU   B 1 108 ? 31.475 -28.062 17.739 1.00 11.83 ? 114 LEU   C CD1 1 
ATOM   1944 C  CD2 . LEU   B 1 108 ? 31.391 -25.971 19.117 1.00 12.04 ? 114 LEU   C CD2 1 
ATOM   1945 N  N   . ARG   B 1 109 ? 28.114 -29.773 18.714 1.00 9.58  ? 115 ARG   C N   1 
ATOM   1946 C  CA  . ARG   B 1 109 ? 27.635 -30.587 19.863 1.00 9.99  ? 115 ARG   C CA  1 
ATOM   1947 C  C   . ARG   B 1 109 ? 28.776 -31.413 20.408 1.00 10.27 ? 115 ARG   C C   1 
ATOM   1948 O  O   . ARG   B 1 109 ? 29.695 -31.835 19.692 1.00 11.25 ? 115 ARG   C O   1 
ATOM   1949 C  CB  . ARG   B 1 109 ? 26.485 -31.495 19.395 1.00 12.83 ? 115 ARG   C CB  1 
ATOM   1950 C  CG  . ARG   B 1 109 ? 26.915 -32.517 18.359 1.00 16.33 ? 115 ARG   C CG  1 
ATOM   1951 C  CD  . ARG   B 1 109 ? 25.775 -33.422 17.888 1.00 20.40 ? 115 ARG   C CD  1 
ATOM   1952 N  NE  . ARG   B 1 109 ? 24.913 -32.692 16.958 1.00 25.62 ? 115 ARG   C NE  1 
ATOM   1953 C  CZ  . ARG   B 1 109 ? 23.609 -32.516 17.135 1.00 34.56 ? 115 ARG   C CZ  1 
ATOM   1954 N  NH1 . ARG   B 1 109 ? 23.013 -32.975 18.227 1.00 37.43 ? 115 ARG   C NH1 1 
ATOM   1955 N  NH2 . ARG   B 1 109 ? 22.896 -31.841 16.238 1.00 37.07 ? 115 ARG   C NH2 1 
ATOM   1956 N  N   . CYS   B 1 110 ? 28.678 -31.653 21.708 1.00 10.68 ? 116 CYS   C N   1 
ATOM   1957 C  CA  . CYS   B 1 110 ? 29.643 -32.544 22.420 1.00 11.81 ? 116 CYS   C CA  1 
ATOM   1958 C  C   . CYS   B 1 110 ? 28.774 -33.637 23.097 1.00 12.91 ? 116 CYS   C C   1 
ATOM   1959 O  O   . CYS   B 1 110 ? 27.544 -33.741 22.914 1.00 12.83 ? 116 CYS   C O   1 
ATOM   1960 C  CB  . CYS   B 1 110 ? 30.449 -31.760 23.457 1.00 11.41 ? 116 CYS   C CB  1 
ATOM   1961 S  SG  . CYS   B 1 110 ? 29.424 -31.104 24.817 1.00 11.65 ? 116 CYS   C SG  1 
ATOM   1962 N  N   . GLN   B 1 111 ? 29.411 -34.491 23.946 1.00 13.63 ? 117 GLN   C N   1 
ATOM   1963 C  CA  . GLN   B 1 111 ? 28.656 -35.540 24.639 1.00 15.15 ? 117 GLN   C CA  1 
ATOM   1964 C  C   . GLN   B 1 111 ? 27.590 -34.981 25.576 1.00 15.66 ? 117 GLN   C C   1 
ATOM   1965 O  O   . GLN   B 1 111 ? 26.616 -35.696 25.910 1.00 17.76 ? 117 GLN   C O   1 
ATOM   1966 C  CB  . GLN   B 1 111 ? 29.594 -36.484 25.449 1.00 17.26 ? 117 GLN   C CB  1 
ATOM   1967 C  CG  . GLN   B 1 111 ? 30.292 -35.778 26.608 1.00 19.14 ? 117 GLN   C CG  1 
ATOM   1968 C  CD  . GLN   B 1 111 ? 31.217 -36.674 27.396 1.00 31.15 ? 117 GLN   C CD  1 
ATOM   1969 O  OE1 . GLN   B 1 111 ? 32.423 -36.732 27.130 1.00 34.58 ? 117 GLN   C OE1 1 
ATOM   1970 N  NE2 . GLN   B 1 111 ? 30.667 -37.346 28.388 1.00 31.45 ? 117 GLN   C NE2 1 
ATOM   1971 N  N   . HIS   B 1 112 ? 27.679 -33.683 25.969 1.00 13.60 ? 118 HIS   C N   1 
ATOM   1972 C  CA  . HIS   B 1 112 ? 26.712 -33.125 26.915 1.00 14.36 ? 118 HIS   C CA  1 
ATOM   1973 C  C   . HIS   B 1 112 ? 25.520 -32.435 26.239 1.00 14.86 ? 118 HIS   C C   1 
ATOM   1974 O  O   . HIS   B 1 112 ? 24.579 -32.042 26.931 1.00 16.22 ? 118 HIS   C O   1 
ATOM   1975 C  CB  . HIS   B 1 112 ? 27.429 -32.140 27.846 1.00 15.23 ? 118 HIS   C CB  1 
ATOM   1976 C  CG  . HIS   B 1 112 ? 28.607 -32.766 28.545 1.00 13.11 ? 118 HIS   C CG  1 
ATOM   1977 N  ND1 . HIS   B 1 112 ? 29.918 -32.491 28.185 1.00 12.85 ? 118 HIS   C ND1 1 
ATOM   1978 C  CD2 . HIS   B 1 112 ? 28.616 -33.576 29.642 1.00 16.31 ? 118 HIS   C CD2 1 
ATOM   1979 C  CE1 . HIS   B 1 112 ? 30.674 -33.221 28.992 1.00 15.08 ? 118 HIS   C CE1 1 
ATOM   1980 N  NE2 . HIS   B 1 112 ? 29.927 -33.858 29.897 1.00 17.14 ? 118 HIS   C NE2 1 
ATOM   1981 N  N   . GLY   B 1 113 ? 25.593 -32.193 24.913 1.00 13.50 ? 119 GLY   C N   1 
ATOM   1982 C  CA  . GLY   B 1 113 ? 24.525 -31.488 24.218 1.00 13.31 ? 119 GLY   C CA  1 
ATOM   1983 C  C   . GLY   B 1 113 ? 25.078 -30.437 23.278 1.00 11.83 ? 119 GLY   C C   1 
ATOM   1984 O  O   . GLY   B 1 113 ? 26.206 -30.533 22.769 1.00 11.65 ? 119 GLY   C O   1 
ATOM   1985 N  N   . VAL   B 1 114 ? 24.223 -29.434 22.998 1.00 11.86 ? 120 VAL   C N   1 
ATOM   1986 C  CA  . VAL   B 1 114 ? 24.554 -28.358 22.064 1.00 11.46 ? 120 VAL   C CA  1 
ATOM   1987 C  C   . VAL   B 1 114 ? 25.484 -27.358 22.740 1.00 11.31 ? 120 VAL   C C   1 
ATOM   1988 O  O   . VAL   B 1 114 ? 25.178 -26.796 23.801 1.00 11.84 ? 120 VAL   C O   1 
ATOM   1989 C  CB  . VAL   B 1 114 ? 23.268 -27.663 21.568 1.00 12.53 ? 120 VAL   C CB  1 
ATOM   1990 C  CG1 . VAL   B 1 114 ? 23.627 -26.453 20.691 1.00 13.82 ? 120 VAL   C CG1 1 
ATOM   1991 C  CG2 . VAL   B 1 114 ? 22.347 -28.648 20.824 1.00 14.33 ? 120 VAL   C CG2 1 
ATOM   1992 N  N   . VAL   B 1 115 ? 26.646 -27.109 22.148 1.00 9.81  ? 121 VAL   C N   1 
ATOM   1993 C  CA  . VAL   B 1 115 ? 27.663 -26.170 22.641 1.00 10.48 ? 121 VAL   C CA  1 
ATOM   1994 C  C   . VAL   B 1 115 ? 27.435 -24.766 22.119 1.00 11.18 ? 121 VAL   C C   1 
ATOM   1995 O  O   . VAL   B 1 115 ? 27.669 -23.780 22.832 1.00 11.69 ? 121 VAL   C O   1 
ATOM   1996 C  CB  . VAL   B 1 115 ? 29.061 -26.703 22.238 1.00 10.77 ? 121 VAL   C CB  1 
ATOM   1997 C  CG1 . VAL   B 1 115 ? 30.142 -25.705 22.604 1.00 11.92 ? 121 VAL   C CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 115 ? 29.344 -28.076 22.846 1.00 12.00 ? 121 VAL   C CG2 1 
ATOM   1999 N  N   . GLY   B 1 116 ? 27.069 -24.655 20.835 1.00 10.55 ? 122 GLY   C N   1 
ATOM   2000 C  CA  . GLY   B 1 116 ? 26.856 -23.340 20.230 1.00 11.85 ? 122 GLY   C CA  1 
ATOM   2001 C  C   . GLY   B 1 116 ? 26.542 -23.518 18.756 1.00 10.57 ? 122 GLY   C C   1 
ATOM   2002 O  O   . GLY   B 1 116 ? 26.226 -24.638 18.317 1.00 10.93 ? 122 GLY   C O   1 
ATOM   2003 N  N   . ILE   B 1 117 ? 26.521 -22.362 18.018 1.00 10.34 ? 123 ILE   C N   1 
ATOM   2004 C  CA  . ILE   B 1 117 ? 26.170 -22.407 16.601 1.00 10.39 ? 123 ILE   C CA  1 
ATOM   2005 C  C   . ILE   B 1 117 ? 27.235 -21.668 15.797 1.00 10.15 ? 123 ILE   C C   1 
ATOM   2006 O  O   . ILE   B 1 117 ? 27.875 -20.713 16.270 1.00 11.10 ? 123 ILE   C O   1 
ATOM   2007 C  CB  . ILE   B 1 117 ? 24.760 -21.776 16.330 1.00 11.03 ? 123 ILE   C CB  1 
ATOM   2008 C  CG1 . ILE   B 1 117 ? 24.660 -20.372 16.968 1.00 12.75 ? 123 ILE   C CG1 1 
ATOM   2009 C  CG2 . ILE   B 1 117 ? 23.640 -22.703 16.753 1.00 12.76 ? 123 ILE   C CG2 1 
ATOM   2010 C  CD1 . ILE   B 1 117 ? 23.297 -19.602 16.533 1.00 13.33 ? 123 ILE   C CD1 1 
ATOM   2011 N  N   . VAL   B 1 118 ? 27.413 -22.082 14.539 1.00 9.94  ? 124 VAL   C N   1 
ATOM   2012 C  CA  . VAL   B 1 118 ? 28.349 -21.413 13.634 1.00 10.02 ? 124 VAL   C CA  1 
ATOM   2013 C  C   . VAL   B 1 118 ? 27.966 -19.930 13.507 1.00 10.58 ? 124 VAL   C C   1 
ATOM   2014 O  O   . VAL   B 1 118 ? 26.775 -19.591 13.293 1.00 10.42 ? 124 VAL   C O   1 
ATOM   2015 C  CB  . VAL   B 1 118 ? 28.338 -22.069 12.243 1.00 10.65 ? 124 VAL   C CB  1 
ATOM   2016 C  CG1 . VAL   B 1 118 ? 29.202 -21.328 11.223 1.00 11.04 ? 124 VAL   C CG1 1 
ATOM   2017 C  CG2 . VAL   B 1 118 ? 28.793 -23.538 12.309 1.00 11.30 ? 124 VAL   C CG2 1 
ATOM   2018 N  N   . SER   B 1 119 ? 28.979 -19.053 13.601 1.00 10.91 ? 125 SER   C N   1 
ATOM   2019 C  CA  . SER   B 1 119 ? 28.777 -17.593 13.494 1.00 11.21 ? 125 SER   C CA  1 
ATOM   2020 C  C   . SER   B 1 119 ? 29.786 -16.923 12.591 1.00 11.90 ? 125 SER   C C   1 
ATOM   2021 O  O   . SER   B 1 119 ? 29.459 -15.852 12.040 1.00 11.99 ? 125 SER   C O   1 
ATOM   2022 C  CB  . SER   B 1 119 ? 28.792 -17.004 14.896 1.00 12.19 ? 125 SER   C CB  1 
ATOM   2023 O  OG  . SER   B 1 119 ? 28.700 -15.569 14.880 1.00 13.28 ? 125 SER   C OG  1 
ATOM   2024 N  N   . THR   B 1 120 ? 31.046 -17.452 12.475 1.00 12.10 ? 126 THR   C N   1 
ATOM   2025 C  CA  . THR   B 1 120 ? 32.075 -16.765 11.668 1.00 12.05 ? 126 THR   C CA  1 
ATOM   2026 C  C   . THR   B 1 120 ? 32.767 -17.777 10.762 1.00 11.50 ? 126 THR   C C   1 
ATOM   2027 O  O   . THR   B 1 120 ? 32.705 -19.011 10.990 1.00 11.52 ? 126 THR   C O   1 
ATOM   2028 C  CB  . THR   B 1 120 ? 33.147 -16.034 12.541 1.00 12.29 ? 126 THR   C CB  1 
ATOM   2029 O  OG1 . THR   B 1 120 ? 33.978 -17.001 13.198 1.00 13.00 ? 126 THR   C OG1 1 
ATOM   2030 C  CG2 . THR   B 1 120 ? 32.542 -15.100 13.561 1.00 13.97 ? 126 THR   C CG2 1 
ATOM   2031 N  N   . GLY   B 1 121 ? 33.469 -17.280 9.773  1.00 12.43 ? 127 GLY   C N   1 
ATOM   2032 C  CA  . GLY   B 1 121 ? 34.246 -18.129 8.879  1.00 14.58 ? 127 GLY   C CA  1 
ATOM   2033 C  C   . GLY   B 1 121 ? 35.278 -17.313 8.124  1.00 17.53 ? 127 GLY   C C   1 
ATOM   2034 O  O   . GLY   B 1 121 ? 35.055 -16.145 7.808  1.00 20.58 ? 127 GLY   C O   1 
ATOM   2035 N  N   . GLY   B 1 122 ? 36.308 -17.948 7.665  1.00 21.16 ? 128 GLY   C N   1 
ATOM   2036 C  CA  . GLY   B 1 122 ? 37.366 -17.275 6.914  1.00 23.46 ? 128 GLY   C CA  1 
ATOM   2037 C  C   . GLY   B 1 122 ? 38.736 -17.744 7.325  1.00 22.68 ? 128 GLY   C C   1 
ATOM   2038 O  O   . GLY   B 1 122 ? 38.959 -18.196 8.439  1.00 22.29 ? 128 GLY   C O   1 
ATOM   2039 N  N   . ASN   B 1 123 ? 39.698 -17.612 6.404  1.00 21.33 ? 129 ASN   C N   1 
ATOM   2040 C  CA  . ASN   B 1 123 ? 41.092 -18.004 6.616  1.00 21.74 ? 129 ASN   C CA  1 
ATOM   2041 C  C   . ASN   B 1 123 ? 41.197 -19.461 7.064  1.00 19.80 ? 129 ASN   C C   1 
ATOM   2042 O  O   . ASN   B 1 123 ? 42.148 -19.796 7.767  1.00 22.62 ? 129 ASN   C O   1 
ATOM   2043 C  CB  . ASN   B 1 123 ? 41.843 -17.068 7.631  1.00 26.77 ? 129 ASN   C CB  1 
ATOM   2044 C  CG  . ASN   B 1 123 ? 42.681 -15.961 7.019  1.00 34.94 ? 129 ASN   C CG  1 
ATOM   2045 O  OD1 . ASN   B 1 123 ? 43.066 -15.997 5.847  1.00 35.82 ? 129 ASN   C OD1 1 
ATOM   2046 N  ND2 . ASN   B 1 123 ? 43.007 -14.933 7.799  1.00 37.95 ? 129 ASN   C ND2 1 
ATOM   2047 N  N   . GLY   B 1 124 ? 40.279 -20.339 6.634  1.00 18.13 ? 130 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 124 ? 40.319 -21.762 7.042  1.00 17.70 ? 130 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 124 ? 39.912 -22.041 8.484  1.00 15.86 ? 130 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 124 ? 40.191 -23.127 9.008  1.00 15.87 ? 130 GLY   C O   1 
ATOM   2051 N  N   . LEU   B 1 125 ? 39.280 -21.057 9.117  1.00 14.16 ? 131 LEU   C N   1 
ATOM   2052 C  CA  . LEU   B 1 125 ? 38.795 -21.199 10.489 1.00 14.18 ? 131 LEU   C CA  1 
ATOM   2053 C  C   . LEU   B 1 125 ? 37.266 -21.098 10.511 1.00 14.28 ? 131 LEU   C C   1 
ATOM   2054 O  O   . LEU   B 1 125 ? 36.661 -20.411 9.661  1.00 16.51 ? 131 LEU   C O   1 
ATOM   2055 C  CB  . LEU   B 1 125 ? 39.395 -20.113 11.409 1.00 16.04 ? 131 LEU   C CB  1 
ATOM   2056 C  CG  . LEU   B 1 125 ? 40.950 -20.145 11.486 1.00 18.79 ? 131 LEU   C CG  1 
ATOM   2057 C  CD1 . LEU   B 1 125 ? 41.559 -18.795 11.862 1.00 23.48 ? 131 LEU   C CD1 1 
ATOM   2058 C  CD2 . LEU   B 1 125 ? 41.458 -21.287 12.303 1.00 19.08 ? 131 LEU   C CD2 1 
ATOM   2059 N  N   . VAL   B 1 126 ? 36.652 -21.761 11.454 1.00 11.97 ? 132 VAL   C N   1 
ATOM   2060 C  CA  . VAL   B 1 126 ? 35.215 -21.666 11.702 1.00 11.10 ? 132 VAL   C CA  1 
ATOM   2061 C  C   . VAL   B 1 126 ? 35.056 -21.183 13.148 1.00 10.54 ? 132 VAL   C C   1 
ATOM   2062 O  O   . VAL   B 1 126 ? 35.714 -21.708 14.056 1.00 11.33 ? 132 VAL   C O   1 
ATOM   2063 C  CB  . VAL   B 1 126 ? 34.489 -22.999 11.460 1.00 11.24 ? 132 VAL   C CB  1 
ATOM   2064 C  CG1 . VAL   B 1 126 ? 35.123 -24.171 12.161 1.00 13.12 ? 132 VAL   C CG1 1 
ATOM   2065 C  CG2 . VAL   B 1 126 ? 32.983 -22.888 11.773 1.00 11.86 ? 132 VAL   C CG2 1 
ATOM   2066 N  N   . GLY   B 1 127 ? 34.162 -20.229 13.349 1.00 10.71 ? 133 GLY   C N   1 
ATOM   2067 C  CA  . GLY   B 1 127 ? 33.925 -19.704 14.698 1.00 10.59 ? 133 GLY   C CA  1 
ATOM   2068 C  C   . GLY   B 1 127 ? 32.499 -20.036 15.126 1.00 11.06 ? 133 GLY   C C   1 
ATOM   2069 O  O   . GLY   B 1 127 ? 31.543 -19.890 14.328 1.00 11.24 ? 133 GLY   C O   1 
ATOM   2070 N  N   . PHE   B 1 128 ? 32.365 -20.394 16.398 1.00 10.36 ? 134 PHE   C N   1 
ATOM   2071 C  CA  . PHE   B 1 128 ? 31.071 -20.768 17.025 1.00 10.07 ? 134 PHE   C CA  1 
ATOM   2072 C  C   . PHE   B 1 128 ? 30.726 -19.831 18.158 1.00 10.28 ? 134 PHE   C C   1 
ATOM   2073 O  O   . PHE   B 1 128 ? 31.586 -19.563 19.009 1.00 11.21 ? 134 PHE   C O   1 
ATOM   2074 C  CB  . PHE   B 1 128 ? 31.141 -22.210 17.604 1.00 10.42 ? 134 PHE   C CB  1 
ATOM   2075 C  CG  . PHE   B 1 128 ? 31.678 -23.215 16.591 1.00 10.61 ? 134 PHE   C CG  1 
ATOM   2076 C  CD1 . PHE   B 1 128 ? 30.832 -23.818 15.656 1.00 10.50 ? 134 PHE   C CD1 1 
ATOM   2077 C  CD2 . PHE   B 1 128 ? 33.019 -23.602 16.611 1.00 11.09 ? 134 PHE   C CD2 1 
ATOM   2078 C  CE1 . PHE   B 1 128 ? 31.324 -24.773 14.766 1.00 11.05 ? 134 PHE   C CE1 1 
ATOM   2079 C  CE2 . PHE   B 1 128 ? 33.512 -24.555 15.697 1.00 11.42 ? 134 PHE   C CE2 1 
ATOM   2080 C  CZ  . PHE   B 1 128 ? 32.672 -25.144 14.807 1.00 11.12 ? 134 PHE   C CZ  1 
ATOM   2081 N  N   . ALA   B 1 129 ? 29.474 -19.339 18.167 1.00 10.90 ? 135 ALA   C N   1 
ATOM   2082 C  CA  . ALA   B 1 129 ? 28.980 -18.534 19.285 1.00 10.88 ? 135 ALA   C CA  1 
ATOM   2083 C  C   . ALA   B 1 129 ? 28.592 -19.523 20.421 1.00 11.21 ? 135 ALA   C C   1 
ATOM   2084 O  O   . ALA   B 1 129 ? 27.685 -20.364 20.248 1.00 11.56 ? 135 ALA   C O   1 
ATOM   2085 C  CB  . ALA   B 1 129 ? 27.751 -17.732 18.839 1.00 12.00 ? 135 ALA   C CB  1 
ATOM   2086 N  N   . ASP   B 1 130 ? 29.271 -19.431 21.565 1.00 11.45 ? 136 ASP   C N   1 
ATOM   2087 C  CA  . ASP   B 1 130 ? 28.979 -20.326 22.699 1.00 11.68 ? 136 ASP   C CA  1 
ATOM   2088 C  C   . ASP   B 1 130 ? 27.635 -19.992 23.305 1.00 12.24 ? 136 ASP   C C   1 
ATOM   2089 O  O   . ASP   B 1 130 ? 27.233 -18.805 23.365 1.00 12.55 ? 136 ASP   C O   1 
ATOM   2090 C  CB  . ASP   B 1 130 ? 30.044 -20.091 23.782 1.00 13.02 ? 136 ASP   C CB  1 
ATOM   2091 C  CG  . ASP   B 1 130 ? 29.932 -21.007 24.978 1.00 15.46 ? 136 ASP   C CG  1 
ATOM   2092 O  OD1 . ASP   B 1 130 ? 29.807 -22.229 24.788 1.00 15.00 ? 136 ASP   C OD1 1 
ATOM   2093 O  OD2 . ASP   B 1 130 ? 29.880 -20.477 26.117 1.00 18.72 ? 136 ASP   C OD2 1 
ATOM   2094 N  N   . VAL   B 1 131 ? 26.925 -21.006 23.783 1.00 12.04 ? 137 VAL   C N   1 
ATOM   2095 C  CA  . VAL   B 1 131 ? 25.689 -20.815 24.555 1.00 11.94 ? 137 VAL   C CA  1 
ATOM   2096 C  C   . VAL   B 1 131 ? 25.741 -21.493 25.930 1.00 12.81 ? 137 VAL   C C   1 
ATOM   2097 O  O   . VAL   B 1 131 ? 24.757 -21.426 26.691 1.00 13.34 ? 137 VAL   C O   1 
ATOM   2098 C  CB  . VAL   B 1 131 ? 24.412 -21.268 23.802 1.00 12.63 ? 137 VAL   C CB  1 
ATOM   2099 C  CG1 . VAL   B 1 131 ? 24.231 -20.455 22.505 1.00 12.89 ? 137 VAL   C CG1 1 
ATOM   2100 C  CG2 . VAL   B 1 131 ? 24.442 -22.742 23.494 1.00 13.21 ? 137 VAL   C CG2 1 
ATOM   2101 N  N   . ARG   B 1 132 ? 26.864 -22.136 26.278 1.00 12.35 ? 138 ARG   C N   1 
ATOM   2102 C  CA  . ARG   B 1 132 ? 26.936 -22.920 27.525 1.00 12.65 ? 138 ARG   C CA  1 
ATOM   2103 C  C   . ARG   B 1 132 ? 26.870 -22.087 28.779 1.00 12.95 ? 138 ARG   C C   1 
ATOM   2104 O  O   . ARG   B 1 132 ? 26.542 -22.656 29.837 1.00 15.03 ? 138 ARG   C O   1 
ATOM   2105 C  CB  . ARG   B 1 132 ? 28.188 -23.770 27.524 1.00 12.28 ? 138 ARG   C CB  1 
ATOM   2106 C  CG  . ARG   B 1 132 ? 28.195 -24.834 26.384 1.00 12.29 ? 138 ARG   C CG  1 
ATOM   2107 C  CD  . ARG   B 1 132 ? 29.506 -25.598 26.438 1.00 11.90 ? 138 ARG   C CD  1 
ATOM   2108 N  NE  . ARG   B 1 132 ? 30.603 -24.710 26.038 1.00 12.15 ? 138 ARG   C NE  1 
ATOM   2109 C  CZ  . ARG   B 1 132 ? 31.853 -25.082 25.888 1.00 12.77 ? 138 ARG   C CZ  1 
ATOM   2110 N  NH1 . ARG   B 1 132 ? 32.238 -26.319 26.225 1.00 13.13 ? 138 ARG   C NH1 1 
ATOM   2111 N  NH2 . ARG   B 1 132 ? 32.743 -24.228 25.406 1.00 13.11 ? 138 ARG   C NH2 1 
ATOM   2112 N  N   . ASP   B 1 133 ? 27.188 -20.794 28.719 1.00 12.79 ? 139 ASP   C N   1 
ATOM   2113 C  CA  . ASP   B 1 133 ? 27.113 -19.926 29.895 1.00 14.08 ? 139 ASP   C CA  1 
ATOM   2114 C  C   . ASP   B 1 133 ? 25.689 -19.365 30.115 1.00 15.23 ? 139 ASP   C C   1 
ATOM   2115 O  O   . ASP   B 1 133 ? 25.462 -18.751 31.171 1.00 16.45 ? 139 ASP   C O   1 
ATOM   2116 C  CB  . ASP   B 1 133 ? 28.080 -18.736 29.752 1.00 15.96 ? 139 ASP   C CB  1 
ATOM   2117 C  CG  . ASP   B 1 133 ? 27.717 -17.807 28.608 1.00 16.94 ? 139 ASP   C CG  1 
ATOM   2118 O  OD1 . ASP   B 1 133 ? 27.375 -18.308 27.511 1.00 16.36 ? 139 ASP   C OD1 1 
ATOM   2119 O  OD2 . ASP   B 1 133 ? 27.748 -16.550 28.812 1.00 19.42 ? 139 ASP   C OD2 1 
ATOM   2120 N  N   . LEU   B 1 134 ? 24.743 -19.573 29.168 1.00 13.93 ? 140 LEU   C N   1 
ATOM   2121 C  CA  . LEU   B 1 134 ? 23.382 -18.998 29.270 1.00 14.16 ? 140 LEU   C CA  1 
ATOM   2122 C  C   . LEU   B 1 134 ? 22.519 -19.978 30.043 1.00 14.27 ? 140 LEU   C C   1 
ATOM   2123 O  O   . LEU   B 1 134 ? 21.711 -20.711 29.480 1.00 14.32 ? 140 LEU   C O   1 
ATOM   2124 C  CB  . LEU   B 1 134 ? 22.840 -18.755 27.850 1.00 14.10 ? 140 LEU   C CB  1 
ATOM   2125 C  CG  . LEU   B 1 134 ? 23.697 -17.794 26.988 1.00 14.12 ? 140 LEU   C CG  1 
ATOM   2126 C  CD1 . LEU   B 1 134 ? 23.137 -17.724 25.526 1.00 15.30 ? 140 LEU   C CD1 1 
ATOM   2127 C  CD2 . LEU   B 1 134 ? 23.796 -16.390 27.634 1.00 15.93 ? 140 LEU   C CD2 1 
ATOM   2128 N  N   . LEU   B 1 135 ? 22.716 -20.025 31.391 1.00 15.21 ? 141 LEU   C N   1 
ATOM   2129 C  CA  . LEU   B 1 135 ? 22.080 -21.057 32.214 1.00 15.99 ? 141 LEU   C CA  1 
ATOM   2130 C  C   . LEU   B 1 135 ? 20.562 -20.962 32.259 1.00 16.07 ? 141 LEU   C C   1 
ATOM   2131 O  O   . LEU   B 1 135 ? 19.873 -21.972 32.429 1.00 17.10 ? 141 LEU   C O   1 
ATOM   2132 C  CB  . LEU   B 1 135 ? 22.650 -21.073 33.656 1.00 16.35 ? 141 LEU   C CB  1 
ATOM   2133 C  CG  . LEU   B 1 135 ? 24.199 -21.089 33.737 1.00 16.55 ? 141 LEU   C CG  1 
ATOM   2134 C  CD1 . LEU   B 1 135 ? 24.719 -21.116 35.220 1.00 18.06 ? 141 LEU   C CD1 1 
ATOM   2135 C  CD2 . LEU   B 1 135 ? 24.832 -22.233 32.920 1.00 17.55 ? 141 LEU   C CD2 1 
ATOM   2136 N  N   . TRP   B 1 136 ? 20.050 -19.740 32.042 1.00 15.76 ? 142 TRP   C N   1 
ATOM   2137 C  CA  . TRP   B 1 136 ? 18.603 -19.469 32.077 1.00 16.70 ? 142 TRP   C CA  1 
ATOM   2138 C  C   . TRP   B 1 136 ? 17.876 -20.169 30.932 1.00 17.99 ? 142 TRP   C C   1 
ATOM   2139 O  O   . TRP   B 1 136 ? 16.653 -20.299 30.970 1.00 18.96 ? 142 TRP   C O   1 
ATOM   2140 C  CB  . TRP   B 1 136 ? 18.328 -17.959 32.065 1.00 17.06 ? 142 TRP   C CB  1 
ATOM   2141 C  CG  . TRP   B 1 136 ? 19.035 -17.230 30.958 1.00 16.74 ? 142 TRP   C CG  1 
ATOM   2142 C  CD1 . TRP   B 1 136 ? 20.209 -16.537 31.045 1.00 17.85 ? 142 TRP   C CD1 1 
ATOM   2143 C  CD2 . TRP   B 1 136 ? 18.522 -16.987 29.626 1.00 16.71 ? 142 TRP   C CD2 1 
ATOM   2144 N  NE1 . TRP   B 1 136 ? 20.503 -15.946 29.821 1.00 18.56 ? 142 TRP   C NE1 1 
ATOM   2145 C  CE2 . TRP   B 1 136 ? 19.466 -16.196 28.946 1.00 17.77 ? 142 TRP   C CE2 1 
ATOM   2146 C  CE3 . TRP   B 1 136 ? 17.376 -17.385 28.960 1.00 16.84 ? 142 TRP   C CE3 1 
ATOM   2147 C  CZ2 . TRP   B 1 136 ? 19.296 -15.820 27.595 1.00 17.14 ? 142 TRP   C CZ2 1 
ATOM   2148 C  CZ3 . TRP   B 1 136 ? 17.169 -16.947 27.662 1.00 16.73 ? 142 TRP   C CZ3 1 
ATOM   2149 C  CH2 . TRP   B 1 136 ? 18.139 -16.204 26.986 1.00 17.09 ? 142 TRP   C CH2 1 
ATOM   2150 N  N   . LEU   B 1 137 ? 18.573 -20.627 29.881 1.00 16.67 ? 143 LEU   C N   1 
ATOM   2151 C  CA  . LEU   B 1 137 ? 17.905 -21.396 28.812 1.00 16.72 ? 143 LEU   C CA  1 
ATOM   2152 C  C   . LEU   B 1 137 ? 17.280 -22.687 29.376 1.00 20.10 ? 143 LEU   C C   1 
ATOM   2153 O  O   . LEU   B 1 137 ? 16.355 -23.229 28.758 1.00 21.84 ? 143 LEU   C O   1 
ATOM   2154 C  CB  . LEU   B 1 137 ? 18.866 -21.755 27.667 1.00 16.17 ? 143 LEU   C CB  1 
ATOM   2155 C  CG  . LEU   B 1 137 ? 19.321 -20.568 26.813 1.00 14.96 ? 143 LEU   C CG  1 
ATOM   2156 C  CD1 . LEU   B 1 137 ? 20.478 -20.969 25.882 1.00 15.96 ? 143 LEU   C CD1 1 
ATOM   2157 C  CD2 . LEU   B 1 137 ? 18.165 -20.013 25.948 1.00 16.67 ? 143 LEU   C CD2 1 
ATOM   2158 N  N   . ASP   B 1 138 ? 17.819 -23.207 30.516 1.00 18.88 ? 144 ASP   C N   1 
ATOM   2159 C  CA  . ASP   B 1 138 ? 17.360 -24.481 31.097 1.00 20.61 ? 144 ASP   C CA  1 
ATOM   2160 C  C   . ASP   B 1 138 ? 16.115 -24.332 31.981 1.00 23.15 ? 144 ASP   C C   1 
ATOM   2161 O  O   . ASP   B 1 138 ? 15.681 -25.350 32.546 1.00 24.76 ? 144 ASP   C O   1 
ATOM   2162 C  CB  . ASP   B 1 138 ? 18.457 -25.137 31.966 1.00 20.79 ? 144 ASP   C CB  1 
ATOM   2163 C  CG  . ASP   B 1 138 ? 19.706 -25.544 31.206 1.00 20.81 ? 144 ASP   C CG  1 
ATOM   2164 O  OD1 . ASP   B 1 138 ? 19.669 -25.566 29.952 1.00 21.28 ? 144 ASP   C OD1 1 
ATOM   2165 O  OD2 . ASP   B 1 138 ? 20.733 -25.834 31.871 1.00 25.51 ? 144 ASP   C OD2 1 
ATOM   2166 N  N   . GLU   B 1 139 ? 15.529 -23.135 32.093 1.00 23.36 ? 145 GLU   C N   1 
ATOM   2167 C  CA  . GLU   B 1 139 ? 14.388 -22.942 32.995 1.00 27.51 ? 145 GLU   C CA  1 
ATOM   2168 C  C   . GLU   B 1 139 ? 13.427 -21.834 32.542 1.00 31.59 ? 145 GLU   C C   1 
ATOM   2169 O  O   . GLU   B 1 139 ? 13.682 -21.160 31.554 1.00 32.10 ? 145 GLU   C O   1 
ATOM   2170 C  CB  . GLU   B 1 139 ? 14.978 -22.586 34.389 1.00 31.91 ? 145 GLU   C CB  1 
ATOM   2171 C  CG  . GLU   B 1 139 ? 15.673 -21.233 34.365 1.00 39.49 ? 145 GLU   C CG  1 
ATOM   2172 C  CD  . GLU   B 1 139 ? 16.577 -20.838 35.519 1.00 49.35 ? 145 GLU   C CD  1 
ATOM   2173 O  OE1 . GLU   B 1 139 ? 17.081 -19.689 35.494 1.00 52.19 ? 145 GLU   C OE1 1 
ATOM   2174 O  OE2 . GLU   B 1 139 ? 16.780 -21.660 36.443 1.00 51.00 ? 145 GLU   C OE2 1 
ATOM   2175 N  N   . GLU   B 1 140 ? 12.352 -21.596 33.333 1.00 34.54 ? 146 GLU   C N   1 
ATOM   2176 C  CA  . GLU   B 1 140 ? 11.394 -20.482 33.219 1.00 37.07 ? 146 GLU   C CA  1 
ATOM   2177 C  C   . GLU   B 1 140 ? 10.738 -20.432 31.859 1.00 38.93 ? 146 GLU   C C   1 
ATOM   2178 O  O   . GLU   B 1 140 ? 10.485 -19.366 31.299 1.00 39.84 ? 146 GLU   C O   1 
ATOM   2179 C  CB  . GLU   B 1 140 ? 12.091 -19.159 33.628 1.00 39.19 ? 146 GLU   C CB  1 
ATOM   2180 C  CG  . GLU   B 1 140 ? 11.647 -17.837 32.994 1.00 46.69 ? 146 GLU   C CG  1 
ATOM   2181 C  CD  . GLU   B 1 140 ? 10.383 -17.155 33.489 1.00 54.61 ? 146 GLU   C CD  1 
ATOM   2182 O  OE1 . GLU   B 1 140 ? 10.294 -15.915 33.337 1.00 58.14 ? 146 GLU   C OE1 1 
ATOM   2183 O  OE2 . GLU   B 1 140 ? 9.475  -17.851 33.997 1.00 56.55 ? 146 GLU   C OE2 1 
HETATM 2184 C  C4  . A1B09 C 2 .   ? 6.215  12.841  25.408 1.00 30.74 ? 201 A1B09 A C4  1 
HETATM 2185 C  C5  . A1B09 C 2 .   ? 7.060  13.691  24.718 1.00 30.35 ? 201 A1B09 A C5  1 
HETATM 2186 C  C6  . A1B09 C 2 .   ? 8.050  13.188  23.877 1.00 29.77 ? 201 A1B09 A C6  1 
HETATM 2187 C  C7  . A1B09 C 2 .   ? 9.106  14.075  23.263 1.00 27.91 ? 201 A1B09 A C7  1 
HETATM 2188 C  C8  . A1B09 C 2 .   ? 8.715  14.635  21.908 1.00 27.74 ? 201 A1B09 A C8  1 
HETATM 2189 C  C10 . A1B09 C 2 .   ? 11.545 16.632  20.873 1.00 27.35 ? 201 A1B09 A C10 1 
HETATM 2190 O  O1  . A1B09 C 2 .   ? 7.580  14.570  21.472 1.00 25.17 ? 201 A1B09 A O1  1 
HETATM 2191 N  N   . A1B09 C 2 .   ? 9.693  15.276  21.242 1.00 28.15 ? 201 A1B09 A N   1 
HETATM 2192 C  C12 . A1B09 C 2 .   ? 9.424  15.973  19.978 1.00 27.88 ? 201 A1B09 A C12 1 
HETATM 2193 C  C11 . A1B09 C 2 .   ? 10.794 16.497  19.559 1.00 28.46 ? 201 A1B09 A C11 1 
HETATM 2194 O  O2  . A1B09 C 2 .   ? 11.429 15.581  18.646 1.00 28.63 ? 201 A1B09 A O2  1 
HETATM 2195 C  C9  . A1B09 C 2 .   ? 11.099 15.407  21.652 1.00 28.43 ? 201 A1B09 A C9  1 
HETATM 2196 C  C1  . A1B09 C 2 .   ? 8.137  11.810  23.707 1.00 30.10 ? 201 A1B09 A C1  1 
HETATM 2197 O  O   . A1B09 C 2 .   ? 9.115  11.410  22.831 1.00 30.00 ? 201 A1B09 A O   1 
HETATM 2198 C  C   . A1B09 C 2 .   ? 9.420  10.030  22.744 1.00 29.64 ? 201 A1B09 A C   1 
HETATM 2199 C  C3  . A1B09 C 2 .   ? 6.329  11.485  25.254 1.00 30.70 ? 201 A1B09 A C3  1 
HETATM 2200 C  C2  . A1B09 C 2 .   ? 7.275  10.958  24.387 1.00 30.11 ? 201 A1B09 A C2  1 
HETATM 2201 ZN ZN  . ZN    D 3 .   ? 11.031 -3.874  5.831  1.00 20.92 2 202 ZN    A ZN  1 
HETATM 2202 S  S   . DMS   E 4 .   ? 19.387 -1.901  24.208 1.00 85.98 ? 203 DMS   A S   1 
HETATM 2203 O  O   . DMS   E 4 .   ? 18.328 -2.281  23.217 1.00 85.82 ? 203 DMS   A O   1 
HETATM 2204 C  C1  . DMS   E 4 .   ? 19.531 -3.260  25.402 1.00 85.96 ? 203 DMS   A C1  1 
HETATM 2205 C  C2  . DMS   E 4 .   ? 21.005 -2.176  23.429 1.00 86.00 ? 203 DMS   A C2  1 
HETATM 2206 ZN ZN  . ZN    F 3 .   ? 30.628 -31.153 26.758 1.00 12.66 2 201 ZN    C ZN  1 
HETATM 2207 S  S   . DMS   G 4 .   ? 20.827 -31.996 9.352  1.00 87.20 ? 202 DMS   C S   1 
HETATM 2208 O  O   . DMS   G 4 .   ? 21.955 -32.419 8.474  1.00 87.37 ? 202 DMS   C O   1 
HETATM 2209 C  C1  . DMS   G 4 .   ? 21.326 -32.249 11.060 1.00 87.13 ? 202 DMS   C C1  1 
HETATM 2210 C  C2  . DMS   G 4 .   ? 20.778 -30.189 9.417  1.00 87.11 ? 202 DMS   C C2  1 
HETATM 2211 O  O   . HOH   H 5 .   ? 10.834 16.583  16.419 1.00 35.05 ? 301 HOH   A O   1 
HETATM 2212 O  O   . HOH   H 5 .   ? 11.250 8.844   4.303  1.00 23.95 ? 302 HOH   A O   1 
HETATM 2213 O  O   . HOH   H 5 .   ? 35.368 -3.832  7.885  1.00 23.57 ? 303 HOH   A O   1 
HETATM 2214 O  O   . HOH   H 5 .   ? 2.066  22.853  21.400 1.00 30.07 ? 304 HOH   A O   1 
HETATM 2215 O  O   . HOH   H 5 .   ? 8.520  -2.899  31.818 1.00 23.81 ? 305 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 23.329 3.660   -2.253 1.00 42.48 ? 306 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 35.508 8.052   9.787  1.00 58.89 ? 307 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 37.526 15.052  13.926 1.00 42.56 ? 308 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 13.916 2.950   1.225  1.00 21.78 ? 309 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 3.014  9.526   8.973  1.00 26.85 ? 310 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 6.085  2.289   5.449  1.00 25.17 ? 311 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 28.071 3.092   4.921  1.00 31.40 ? 312 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 29.516 22.244  19.448 1.00 26.02 ? 313 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 17.441 0.923   28.288 1.00 25.17 ? 314 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 4.260  9.452   27.956 1.00 38.28 ? 315 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 7.434  20.234  17.475 1.00 24.81 ? 316 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 5.521  17.758  24.058 1.00 48.60 ? 317 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 30.446 10.424  15.574 1.00 28.26 ? 318 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 0.429  -0.828  19.440 1.00 21.60 ? 319 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 21.833 2.356   -0.849 1.00 31.01 ? 320 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 33.884 -2.273  13.581 1.00 31.47 ? 321 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 12.349 22.163  12.927 1.00 37.01 ? 322 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 10.594 10.140  31.452 1.00 22.55 ? 323 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 16.054 -6.798  10.747 1.00 37.93 ? 324 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 33.845 14.125  9.678  1.00 29.90 ? 325 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 2.643  -2.825  20.775 1.00 23.23 ? 326 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 19.393 10.074  19.670 1.00 12.99 ? 327 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 12.528 -5.871  30.510 1.00 43.07 ? 328 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 4.672  -3.584  28.897 1.00 25.21 ? 329 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 10.802 5.714   3.418  1.00 24.65 ? 330 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 27.823 8.016   1.620  1.00 32.05 ? 331 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? -2.515 23.701  9.680  1.00 69.18 ? 332 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 23.496 21.645  7.266  1.00 22.39 ? 333 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 24.974 5.076   21.445 1.00 30.07 ? 334 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 22.655 0.852   17.392 1.00 15.39 ? 335 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 14.026 13.760  23.963 1.00 22.26 ? 336 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 20.005 19.854  5.589  1.00 40.89 ? 337 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 28.355 11.047  3.016  1.00 54.83 ? 338 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 3.744  -8.044  9.969  1.00 48.28 ? 339 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 15.809 24.011  14.711 1.00 36.64 ? 340 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? -0.068 1.345   15.910 1.00 12.55 ? 341 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 29.955 11.551  18.439 1.00 26.76 ? 342 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 32.314 2.260   5.996  1.00 37.51 ? 343 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 21.833 4.962   24.721 1.00 38.37 ? 344 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 36.807 2.541   10.040 1.00 44.97 ? 345 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 23.412 11.732  21.969 1.00 30.27 ? 346 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 12.131 16.807  27.919 1.00 35.46 ? 347 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 20.925 -4.150  14.187 1.00 16.16 ? 348 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 13.780 3.988   23.532 1.00 12.47 ? 349 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 15.152 14.368  26.287 1.00 33.15 ? 350 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 31.461 -2.583  15.357 1.00 49.91 ? 351 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 28.940 3.378   12.637 1.00 16.43 ? 352 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 30.103 -1.436  8.702  1.00 30.68 ? 353 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 16.641 3.846   23.701 1.00 16.71 ? 354 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 11.371 12.704  11.127 1.00 16.49 ? 355 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 26.867 -1.209  8.823  1.00 23.93 ? 356 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 31.631 19.913  11.716 1.00 20.76 ? 357 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 35.332 10.839  12.129 1.00 48.23 ? 358 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 33.763 11.072  15.517 1.00 38.20 ? 359 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 15.107 11.324  0.053  1.00 34.45 ? 360 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 4.004  12.925  18.194 1.00 28.60 ? 361 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 16.910 -3.522  27.804 1.00 32.90 ? 362 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 6.649  -6.922  23.767 1.00 22.38 ? 363 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 8.404  24.693  23.883 1.00 28.82 ? 364 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 18.411 21.881  9.515  1.00 19.14 ? 365 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 13.256 11.412  9.191  1.00 14.37 ? 366 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 20.675 -0.937  3.046  1.00 30.04 ? 367 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 29.438 11.905  21.286 1.00 32.76 ? 368 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 15.001 21.788  8.520  1.00 29.57 ? 369 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 3.228  20.793  24.543 1.00 43.92 ? 370 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 31.780 7.043   5.377  1.00 29.52 ? 371 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 20.777 -2.558  16.859 1.00 14.85 ? 372 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 1.504  5.336   27.093 1.00 32.83 ? 373 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 35.885 15.136  11.053 1.00 39.57 ? 374 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 17.581 19.963  17.001 1.00 17.11 ? 375 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 30.523 2.938   14.826 1.00 23.34 ? 376 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 12.258 11.126  29.717 1.00 20.62 ? 377 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 2.540  16.065  19.235 1.00 32.49 ? 378 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 30.335 4.530   5.787  1.00 23.31 ? 379 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 36.536 17.931  14.403 1.00 28.19 ? 380 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 5.713  16.714  21.587 1.00 31.76 ? 381 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 19.458 2.954   19.372 1.00 17.55 ? 382 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 9.621  4.008   33.538 1.00 14.57 ? 383 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 28.926 15.833  4.323  1.00 28.50 ? 384 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 11.488 -7.003  24.735 1.00 26.64 ? 385 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 25.330 18.004  4.706  1.00 30.54 ? 386 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 5.497  5.408   32.719 1.00 21.52 ? 387 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 24.138 -3.483  16.105 1.00 31.77 ? 388 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 25.486 19.588  21.718 1.00 25.84 ? 389 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 27.255 -1.296  15.807 1.00 25.54 ? 390 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 0.200  6.071   6.174  1.00 24.99 ? 391 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 18.070 17.815  4.312  1.00 34.75 ? 392 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 31.025 15.597  22.767 1.00 26.05 ? 393 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 6.045  3.156   6.546  1.00 28.68 ? 394 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 22.828 -0.648  5.342  1.00 21.91 ? 395 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 23.275 -6.550  11.970 1.00 28.41 ? 396 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 3.201  0.407   29.028 1.00 36.04 ? 397 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 17.829 10.604  26.207 1.00 22.90 ? 398 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 1.414  11.876  27.450 1.00 42.57 ? 399 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 14.460 -2.414  17.967 1.00 17.50 ? 400 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 3.856  -3.839  6.023  1.00 27.71 ? 401 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 17.116 6.092   26.952 1.00 29.15 ? 402 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 14.918 -4.973  0.548  1.00 44.03 ? 403 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 32.839 16.584  9.268  1.00 29.63 ? 404 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 4.737  -5.622  14.288 1.00 37.67 ? 405 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 16.279 9.386   -1.648 1.00 22.49 ? 406 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 15.242 15.093  3.344  1.00 32.64 ? 407 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 8.473  19.033  19.593 1.00 24.27 ? 408 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 32.012 8.746   7.593  1.00 22.68 ? 409 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 16.450 21.222  19.090 1.00 26.95 ? 410 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 8.480  -6.370  9.657  1.00 28.71 ? 411 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 0.549  -1.251  9.198  1.00 35.02 ? 412 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 28.015 17.561  24.179 1.00 23.98 ? 413 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 4.212  0.373   24.057 1.00 17.89 ? 414 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 34.017 18.659  10.730 1.00 25.64 ? 415 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 17.091 -5.353  12.176 1.00 31.90 ? 416 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 36.260 -0.390  12.712 1.00 36.25 ? 417 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 13.863 25.012  26.003 1.00 43.14 ? 418 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 11.615 17.919  4.681  1.00 41.17 ? 419 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 3.270  7.784   24.471 1.00 25.47 ? 420 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 5.180  26.425  20.117 1.00 29.73 ? 421 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 4.986  8.118   2.348  1.00 32.72 ? 422 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 7.183  26.437  14.392 1.00 38.55 ? 423 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 6.018  -3.537  31.501 1.00 27.33 ? 424 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 17.500 0.719   20.190 1.00 18.39 ? 425 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 7.291  13.865  4.762  1.00 23.53 ? 426 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 3.559  26.984  16.156 1.00 52.83 ? 427 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 6.210  23.969  10.563 1.00 38.38 ? 428 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 22.390 19.506  19.617 1.00 29.28 ? 429 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 0.510  -1.227  16.764 1.00 17.47 ? 430 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 8.328  6.519   33.844 1.00 20.07 ? 431 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 3.415  -0.235  21.483 1.00 21.84 ? 432 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 19.346 -0.445  33.076 1.00 38.36 ? 433 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 34.126 7.760   16.537 1.00 35.66 ? 434 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 33.928 5.180   16.633 1.00 34.39 ? 435 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 19.431 21.465  6.837  1.00 34.59 ? 436 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 23.253 19.110  6.311  1.00 18.90 ? 437 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 25.102 10.642  22.953 1.00 37.94 ? 438 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 19.760 13.339  2.188  1.00 29.53 ? 439 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 1.188  -5.002  17.483 1.00 34.31 ? 440 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 22.745 3.416   20.830 1.00 20.64 ? 441 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 15.850 21.362  7.203  1.00 24.11 ? 442 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 17.828 24.473  10.388 1.00 31.68 ? 443 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 14.209 24.426  17.880 1.00 39.47 ? 444 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 16.874 -3.985  2.898  1.00 28.17 ? 445 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 21.065 9.934   21.926 1.00 17.01 ? 446 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 17.145 -2.453  19.644 1.00 19.84 ? 447 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 19.634 9.232   -0.884 1.00 30.05 ? 448 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 23.427 8.307   21.704 1.00 25.51 ? 449 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 2.164  14.479  16.888 1.00 32.23 ? 450 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 21.003 -4.799  11.482 1.00 30.41 ? 451 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 31.104 19.455  9.078  1.00 42.28 ? 452 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 36.636 16.169  16.755 1.00 37.62 ? 453 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 19.355 16.667  26.329 1.00 44.07 ? 454 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 7.726  11.681  3.643  1.00 40.50 ? 455 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 9.219  3.774   3.040  1.00 31.99 ? 456 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? -1.342 -2.942  15.685 1.00 28.34 ? 457 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 17.048 23.659  17.074 1.00 53.48 ? 458 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 8.243  11.228  31.618 1.00 39.08 ? 459 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 6.169  5.482   1.652  1.00 30.38 ? 460 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 0.704  7.757   27.755 1.00 45.14 ? 461 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 10.661 17.143  25.648 1.00 31.68 ? 462 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 7.309  -4.368  2.711  1.00 35.76 ? 463 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 13.591 -6.480  25.654 1.00 39.71 ? 464 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 27.676 10.054  22.864 1.00 44.31 ? 465 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 0.926  3.471   26.033 1.00 34.93 ? 466 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 2.151  -5.389  14.611 1.00 42.26 ? 467 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 11.639 24.277  14.564 1.00 36.04 ? 468 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 2.697  -0.196  26.420 1.00 32.94 ? 469 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 30.862 12.934  23.148 1.00 44.92 ? 470 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 21.725 19.707  4.183  1.00 37.20 ? 471 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 16.804 -5.004  34.371 1.00 29.23 ? 472 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 29.697 0.601   16.447 1.00 31.74 ? 473 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 36.749 20.475  17.809 1.00 38.95 ? 474 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 18.558 2.086   22.680 1.00 35.99 ? 475 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 18.602 3.215   26.101 1.00 41.54 ? 476 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 23.819 0.981   19.769 1.00 29.47 ? 477 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 0.026  0.139   23.236 1.00 29.84 ? 478 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 4.814  28.295  18.164 1.00 41.33 ? 479 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 21.369 2.951   23.186 1.00 33.87 ? 480 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 30.392 7.077   17.777 1.00 36.41 ? 481 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 37.834 -4.468  6.775  1.00 32.98 ? 482 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? -0.434 13.789  17.097 1.00 35.25 ? 483 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 2.224  8.357   2.058  1.00 47.35 ? 484 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 21.212 11.369  24.493 1.00 37.04 ? 485 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 31.310 4.521   16.985 1.00 25.78 ? 486 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 12.446 -5.063  33.115 1.00 31.70 ? 487 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 21.394 -1.092  18.895 1.00 29.33 ? 488 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 2.351  -4.988  22.635 1.00 33.26 ? 489 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 39.330 -2.661  10.699 1.00 40.63 ? 490 HOH   A O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 28.831 1.478   19.009 1.00 48.70 ? 491 HOH   A O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 9.740  25.889  13.889 1.00 43.06 ? 492 HOH   A O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 3.985  -6.591  23.490 1.00 41.49 ? 493 HOH   A O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 38.087 19.733  15.520 1.00 34.14 ? 494 HOH   A O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 26.505 0.316   19.849 1.00 46.94 ? 495 HOH   A O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 17.475 -33.264 24.102 1.00 40.96 ? 301 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 31.667 -17.931 -0.108 1.00 42.78 ? 302 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 10.155 -20.038 28.918 1.00 33.16 ? 303 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 38.565 -18.569 21.570 1.00 26.67 ? 304 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 38.346 -7.353  7.023  1.00 22.25 ? 305 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 19.706 -4.103  20.188 1.00 21.45 ? 306 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 17.849 -6.032  24.082 1.00 25.39 ? 307 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 30.755 -18.118 26.936 1.00 18.82 ? 308 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 16.460 -17.162 11.037 1.00 37.06 ? 309 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 24.637 -5.906  15.213 1.00 28.76 ? 310 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 17.913 -27.540 16.540 1.00 18.11 ? 311 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 20.755 -18.731 12.853 1.00 13.92 ? 312 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 22.927 -5.908  21.121 1.00 19.98 ? 313 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 21.463 -24.956 4.076  1.00 38.20 ? 314 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 14.755 -18.635 31.923 1.00 39.06 ? 315 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 42.661 -11.297 11.248 1.00 29.62 ? 316 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 18.735 -32.423 19.951 1.00 38.67 ? 317 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 24.410 -9.294  26.922 1.00 44.06 ? 318 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 18.589 -8.862  13.794 1.00 28.03 ? 319 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 10.266 -17.556 18.314 1.00 25.97 ? 320 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 32.469 -23.705 29.158 1.00 16.63 ? 321 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 36.392 -2.477  11.133 1.00 33.78 ? 322 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 31.130 -23.775 -1.292 1.00 21.46 ? 323 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 37.266 -18.697 28.191 1.00 26.81 ? 324 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 40.121 -29.552 11.965 1.00 23.39 ? 325 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 36.143 -26.128 34.306 1.00 32.90 ? 326 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 26.369 -15.244 30.782 1.00 29.60 ? 327 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 14.845 -23.958 12.313 1.00 28.95 ? 328 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 36.131 -17.649 11.633 1.00 24.91 ? 329 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 21.695 -26.135 34.423 1.00 26.24 ? 330 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 30.934 -21.495 28.438 1.00 16.59 ? 331 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 7.226  -30.401 22.051 1.00 32.32 ? 332 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 22.088 -28.671 4.797  1.00 25.06 ? 333 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 24.819 -15.739 7.360  1.00 18.49 ? 334 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 37.445 -31.847 10.993 1.00 21.89 ? 335 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 26.080 -25.257 8.803  1.00 13.35 ? 336 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 40.583 -27.206 15.271 1.00 12.11 ? 337 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 37.322 -10.495 4.985  1.00 38.12 ? 338 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 41.307 -25.015 7.329  1.00 30.65 ? 339 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 16.806 -9.262  27.539 1.00 34.88 ? 340 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 13.843 -24.232 29.329 1.00 33.74 ? 341 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 35.279 -32.754 3.372  1.00 34.68 ? 342 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 27.902 -4.339  18.221 1.00 45.76 ? 343 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 26.585 -5.470  9.976  1.00 21.14 ? 344 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 38.719 -27.675 28.453 1.00 50.02 ? 345 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 29.897 -15.259 19.633 1.00 15.41 ? 346 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 11.928 -24.281 21.698 1.00 18.31 ? 347 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 9.164  -7.999  21.261 1.00 26.17 ? 348 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 22.779 -7.505  25.388 1.00 41.78 ? 349 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 9.870  -8.874  23.884 1.00 28.22 ? 350 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 35.245 -13.129 8.758  1.00 19.26 ? 351 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 17.579 -23.989 8.681  1.00 36.15 ? 352 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 23.924 -8.171  9.480  1.00 22.28 ? 353 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 10.481 -16.946 15.078 1.00 31.14 ? 354 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 36.358 -21.234 7.000  1.00 22.44 ? 355 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 13.212 -11.139 28.475 1.00 38.00 ? 356 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 20.781 -25.640 13.883 1.00 19.42 ? 357 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 11.151 -21.720 13.684 1.00 38.69 ? 358 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 29.805 -13.069 13.025 1.00 15.16 ? 359 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 6.939  -9.275  22.688 1.00 32.35 ? 360 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 22.870 -33.244 5.441  1.00 27.17 ? 361 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 25.826 -37.844 24.271 1.00 31.28 ? 362 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 27.107 -35.554 20.800 1.00 24.82 ? 363 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 29.901 -15.912 30.526 1.00 31.11 ? 364 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 34.138 -33.669 24.176 1.00 30.40 ? 365 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 32.062 -10.443 13.818 1.00 19.09 ? 366 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 37.702 -31.335 25.887 1.00 26.40 ? 367 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 20.147 -33.130 6.404  1.00 44.65 ? 368 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 10.700 -16.918 12.341 1.00 32.32 ? 369 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 14.587 -28.772 25.593 1.00 34.08 ? 370 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 23.571 -33.639 29.058 1.00 28.89 ? 371 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 19.205 -27.730 28.165 1.00 19.60 ? 372 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 36.613 -16.162 12.524 1.00 29.03 ? 373 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 32.104 -34.668 24.853 1.00 27.25 ? 374 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 39.402 -33.490 14.032 1.00 40.66 ? 375 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 22.946 -8.510  14.051 1.00 16.01 ? 376 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 34.730 -34.974 18.158 1.00 25.58 ? 377 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 13.212 -29.597 19.188 1.00 31.24 ? 378 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 36.125 -28.484 2.938  1.00 37.04 ? 379 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 28.977 -36.194 7.880  1.00 19.38 ? 380 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 4.262  -10.427 19.562 1.00 28.87 ? 381 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 36.288 -32.420 25.083 1.00 37.52 ? 382 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 31.778 -34.852 31.859 1.00 38.43 ? 383 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 31.261 -6.050  5.937  1.00 39.14 ? 384 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 23.252 -25.369 8.952  1.00 20.10 ? 385 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 28.101 -16.344 22.127 1.00 13.45 ? 386 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 22.332 -23.694 6.131  1.00 36.39 ? 387 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 22.251 -13.686 29.389 1.00 35.12 ? 388 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 23.674 -3.387  19.085 1.00 36.00 ? 389 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 8.802  -13.325 10.800 1.00 22.96 ? 390 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 34.330 -13.444 25.530 1.00 19.97 ? 391 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 33.002 -9.818  11.152 1.00 15.03 ? 392 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 11.484 -22.535 28.674 1.00 28.55 ? 393 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 22.986 -28.172 12.623 1.00 19.93 ? 394 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 10.982 -6.394  13.229 1.00 24.41 ? 395 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 31.570 -13.458 4.340  1.00 33.15 ? 396 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 26.033 -31.003 30.896 1.00 18.03 ? 397 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 31.302 -12.160 10.704 1.00 14.48 ? 398 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 33.675 -32.948 0.922  1.00 37.50 ? 399 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 26.585 -6.037  22.054 1.00 27.66 ? 400 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 10.065 -24.878 19.799 1.00 21.40 ? 401 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 30.364 -18.089 8.461  1.00 24.56 ? 402 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 38.975 -16.649 3.739  1.00 39.42 ? 403 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 29.985 -10.473 27.866 1.00 43.06 ? 404 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 37.999 -23.642 4.588  1.00 34.98 ? 405 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 26.705 -12.036 27.654 1.00 28.75 ? 406 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 38.751 -14.537 13.614 1.00 31.77 ? 407 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 14.755 -18.384 10.397 1.00 35.55 ? 408 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 20.391 -23.681 34.774 1.00 29.50 ? 409 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 26.404 -31.231 14.866 1.00 18.91 ? 410 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 43.301 -25.462 23.774 1.00 26.24 ? 411 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 36.988 -29.205 10.187 1.00 20.41 ? 412 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 37.823 -20.280 4.991  1.00 38.94 ? 413 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 4.641  -27.929 23.284 1.00 36.46 ? 414 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 21.759 -18.876 5.913  1.00 28.12 ? 415 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 3.860  -8.206  14.774 1.00 26.83 ? 416 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 5.797  -16.985 22.305 1.00 44.99 ? 417 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 35.821 -28.534 7.812  1.00 17.86 ? 418 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 10.836 -11.925 8.974  1.00 31.41 ? 419 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 35.621 -24.640 24.717 1.00 18.99 ? 420 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 38.870 -12.996 25.842 1.00 26.99 ? 421 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 33.047 -30.292 31.724 1.00 18.55 ? 422 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 17.203 -25.250 12.761 1.00 25.19 ? 423 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 6.635  -17.284 18.078 1.00 47.18 ? 424 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 34.646 -23.187 -0.747 1.00 35.49 ? 425 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 32.852 -14.350 9.471  1.00 15.22 ? 426 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 10.387 -30.956 25.347 1.00 33.27 ? 427 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 16.995 -31.589 28.448 1.00 47.16 ? 428 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 42.248 -12.111 14.042 1.00 35.85 ? 429 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 20.298 -32.220 22.242 1.00 30.28 ? 430 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 9.630  -24.462 29.345 1.00 45.56 ? 431 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 34.899 -4.072  17.719 1.00 28.95 ? 432 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 18.741 -11.537 7.692  1.00 46.67 ? 433 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 35.213 -13.656 6.075  1.00 32.70 ? 434 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 36.192 -34.060 18.061 1.00 31.73 ? 435 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 4.061  -12.736 17.142 1.00 38.99 ? 436 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 33.811 -35.932 8.813  1.00 34.30 ? 437 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 16.406 -20.513 11.557 1.00 23.35 ? 438 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 18.608 -8.308  25.537 1.00 20.57 ? 439 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 9.757  -18.431 26.728 1.00 30.73 ? 440 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 40.067 -29.893 14.692 1.00 16.80 ? 441 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 24.521 -13.774 5.509  1.00 37.99 ? 442 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 6.513  -22.935 18.287 1.00 34.82 ? 443 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 34.007 -15.597 27.123 1.00 31.40 ? 444 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 8.775  -12.974 24.602 1.00 54.09 ? 445 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 15.138 -30.075 18.050 1.00 44.44 ? 446 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 41.730 -12.509 18.080 1.00 26.21 ? 447 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 18.838 -19.083 10.877 1.00 19.14 ? 448 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 23.445 -31.150 13.225 1.00 31.65 ? 449 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 23.265 -17.600 33.311 1.00 20.94 ? 450 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 20.176 -19.636 36.086 1.00 30.88 ? 451 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 6.608  -20.048 18.105 1.00 33.51 ? 452 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 36.607 -24.568 27.276 1.00 35.91 ? 453 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 24.277 -16.530 3.288  1.00 37.08 ? 454 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 37.485 -14.034 9.883  1.00 31.14 ? 455 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 34.596 -30.245 33.886 1.00 35.30 ? 456 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 38.978 -33.647 17.411 1.00 43.10 ? 457 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 34.192 -31.817 29.601 1.00 23.27 ? 458 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 26.219 -35.325 7.454  1.00 25.54 ? 459 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 23.680 -15.693 31.491 1.00 28.79 ? 460 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 8.876  -19.208 16.860 1.00 36.12 ? 461 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 21.070 -17.459 34.640 1.00 27.63 ? 462 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 21.552 -26.838 10.316 1.00 30.78 ? 463 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 22.942 -16.711 5.390  1.00 40.23 ? 464 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 28.346 -12.584 30.198 1.00 48.61 ? 465 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 16.418 -27.523 14.172 1.00 29.65 ? 466 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 18.585 -26.105 10.256 1.00 36.23 ? 467 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 41.587 -15.197 13.960 1.00 33.97 ? 468 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 40.474 -28.647 7.858  1.00 46.62 ? 469 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 32.548 -19.353 29.132 1.00 30.26 ? 470 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 10.047 -21.355 16.280 1.00 32.85 ? 471 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 43.469 -20.633 3.809  1.00 50.38 ? 472 HOH   C O   1 
HETATM 2578 O  O   . HOH   I 5 .   ? 18.154 -17.961 8.371  1.00 32.86 ? 473 HOH   C O   1 
HETATM 2579 O  O   . HOH   I 5 .   ? 17.034 -28.959 28.874 1.00 40.35 ? 474 HOH   C O   1 
HETATM 2580 O  O   . HOH   I 5 .   ? 22.808 -11.855 6.000  1.00 37.86 ? 475 HOH   C O   1 
HETATM 2581 O  O   . HOH   I 5 .   ? 35.362 -20.227 29.408 1.00 41.50 ? 476 HOH   C O   1 
HETATM 2582 O  O   . HOH   I 5 .   ? 18.210 -16.404 38.334 1.00 36.59 ? 477 HOH   C O   1 
HETATM 2583 O  O   . HOH   I 5 .   ? 9.055  -23.524 17.642 1.00 31.74 ? 478 HOH   C O   1 
HETATM 2584 O  O   . HOH   I 5 .   ? 35.202 -23.006 28.981 1.00 27.61 ? 479 HOH   C O   1 
HETATM 2585 O  O   . HOH   I 5 .   ? 3.173  -8.595  22.095 1.00 42.02 ? 480 HOH   C O   1 
HETATM 2586 O  O   . HOH   I 5 .   ? 19.341 -17.642 5.851  1.00 36.71 ? 481 HOH   C O   1 
HETATM 2587 O  O   . HOH   I 5 .   ? 3.241  -9.442  17.093 1.00 31.92 ? 482 HOH   C O   1 
HETATM 2588 O  O   . HOH   I 5 .   ? 19.552 -15.097 34.678 1.00 35.65 ? 483 HOH   C O   1 
HETATM 2589 O  O   . HOH   I 5 .   ? 5.894  -24.321 15.216 1.00 54.33 ? 484 HOH   C O   1 
HETATM 2590 O  O   . HOH   I 5 .   ? 36.337 -35.637 8.503  1.00 49.81 ? 485 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   ? 0.2223 0.2103 0.1921 -0.0219 -0.0021 -0.0118 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2112 0.2025 0.1876 -0.0197 -0.0065 -0.0085 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2065 0.2015 0.1924 -0.0122 -0.0109 -0.0024 7   SER   A C   
4    O O   . SER   A 1   ? 0.2075 0.2036 0.1935 -0.0104 -0.0118 -0.0002 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2422 0.2401 0.2120 -0.0291 -0.0116 -0.0066 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2808 0.2864 0.2496 -0.0313 -0.0178 0.0002  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1865 0.1832 0.1803 -0.0088 -0.0128 -0.0004 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1701 0.1693 0.1732 -0.0032 -0.0149 0.0039  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1506 0.1485 0.1604 0.0008  -0.0130 0.0026  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1711 0.1655 0.1793 0.0011  -0.0097 -0.0007 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1356 0.1360 0.1536 0.0035  -0.0142 0.0055  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1394 0.1394 0.1630 0.0059  -0.0122 0.0041  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1352 0.1355 0.1655 0.0084  -0.0102 0.0049  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1468 0.1474 0.1800 0.0089  -0.0106 0.0075  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1551 0.1581 0.1826 0.0041  -0.0147 0.0056  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1259 0.1261 0.1585 0.0090  -0.0073 0.0026  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1198 0.1198 0.1583 0.0092  -0.0035 0.0014  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1336 0.1350 0.1808 0.0095  -0.0030 0.0020  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1356 0.1384 0.1814 0.0088  -0.0043 0.0013  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1252 0.1261 0.1591 0.0071  -0.0004 -0.0015 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1465 0.1480 0.1733 0.0070  -0.0012 -0.0008 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1460 0.1461 0.1838 0.0048  0.0052  -0.0045 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1571 0.1633 0.1809 0.0044  0.0002  -0.0007 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1242 0.1251 0.1819 0.0107  -0.0004 0.0036  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1340 0.1369 0.2032 0.0115  0.0012  0.0048  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1410 0.1405 0.2159 0.0104  0.0097  0.0000  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1510 0.1471 0.2344 0.0114  0.0147  0.0004  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1450 0.1515 0.2259 0.0137  -0.0021 0.0126  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1377 0.1489 0.2110 0.0119  -0.0100 0.0164  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1570 0.1724 0.2296 0.0100  -0.0132 0.0169  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1687 0.1800 0.2348 0.0108  -0.0134 0.0187  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1622 0.1810 0.2255 0.0061  -0.0190 0.0185  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1740 0.1892 0.2311 0.0070  -0.0192 0.0206  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1757 0.1941 0.2308 0.0042  -0.0215 0.0199  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2131 0.2345 0.2579 -0.0016 -0.0257 0.0202  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1374 0.1375 0.2071 0.0072  0.0122  -0.0049 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1455 0.1433 0.2172 0.0032  0.0210  -0.0110 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1618 0.1616 0.2401 0.0024  0.0233  -0.0125 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1492 0.1529 0.2225 0.0022  0.0180  -0.0111 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1677 0.1669 0.2245 -0.0024 0.0216  -0.0149 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1792 0.1836 0.2275 -0.0027 0.0148  -0.0124 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1911 0.1893 0.2473 -0.0095 0.0308  -0.0220 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1710 0.1679 0.2624 0.0022  0.0320  -0.0150 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1721 0.1712 0.2717 0.0015  0.0351  -0.0163 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1551 0.1598 0.2599 0.0061  0.0262  -0.0089 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1591 0.1653 0.2705 0.0104  0.0213  -0.0020 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1497 0.1580 0.2493 0.0039  0.0235  -0.0102 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1432 0.1566 0.2444 0.0062  0.0153  -0.0044 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1390 0.1525 0.2238 0.0047  0.0084  -0.0043 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1429 0.1589 0.2247 0.0038  0.0043  -0.0031 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1620 0.1793 0.2726 0.0054  0.0175  -0.0046 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1996 0.2182 0.3316 0.0087  0.0232  -0.0015 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2223 0.2469 0.3661 0.0120  0.0184  0.0068  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1892 0.2030 0.3276 0.0072  0.0341  -0.0074 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1339 0.1444 0.2099 0.0047  0.0076  -0.0050 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1293 0.1394 0.1930 0.0041  0.0027  -0.0043 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1269 0.1356 0.1880 0.0064  -0.0012 -0.0012 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1323 0.1398 0.1975 0.0078  0.0006  -0.0004 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1435 0.1534 0.1987 0.0008  0.0055  -0.0072 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1530 0.1655 0.2078 -0.0035 0.0089  -0.0099 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1679 0.1822 0.2226 -0.0040 0.0064  -0.0085 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1811 0.1944 0.2348 -0.0084 0.0151  -0.0142 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1759 0.1934 0.2299 -0.0086 0.0093  -0.0105 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1941 0.2110 0.2455 -0.0143 0.0184  -0.0169 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1992 0.2185 0.2509 -0.0140 0.0151  -0.0145 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2551 0.2785 0.3045 -0.0204 0.0182  -0.0168 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1211 0.1294 0.1749 0.0060  -0.0054 -0.0001 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1230 0.1297 0.1713 0.0064  -0.0082 0.0015  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1231 0.1268 0.1630 0.0061  -0.0072 -0.0003 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1330 0.1357 0.1710 0.0051  -0.0070 -0.0009 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1341 0.1434 0.1820 0.0044  -0.0126 0.0040  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1489 0.1563 0.1879 0.0023  -0.0147 0.0040  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1652 0.1774 0.2027 -0.0026 -0.0191 0.0065  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1783 0.1865 0.2042 -0.0073 -0.0184 0.0028  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1925 0.2002 0.2109 -0.0105 -0.0192 0.0026  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2094 0.2206 0.2305 -0.0088 -0.0216 0.0069  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2013 0.2040 0.2097 -0.0156 -0.0163 -0.0023 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1175 0.1201 0.1541 0.0070  -0.0062 -0.0003 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1162 0.1178 0.1480 0.0072  -0.0049 -0.0002 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1316 0.1299 0.1590 0.0077  -0.0057 -0.0002 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1413 0.1397 0.1672 0.0079  -0.0068 0.0002  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1214 0.1259 0.1524 0.0065  -0.0030 0.0001  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1315 0.1380 0.1608 0.0067  -0.0024 0.0029  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1379 0.1453 0.1717 0.0039  -0.0008 -0.0015 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1188 0.1138 0.1444 0.0073  -0.0042 -0.0008 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1288 0.1198 0.1495 0.0061  -0.0030 -0.0024 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1518 0.1429 0.1725 0.0061  -0.0031 -0.0024 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1325 0.1202 0.1551 0.0078  0.0018  -0.0020 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1477 0.1369 0.1760 0.0096  0.0032  0.0009  18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1305 0.1194 0.1472 0.0017  -0.0039 -0.0049 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2009 0.1905 0.2184 0.0018  -0.0044 -0.0046 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1433 0.1375 0.1599 -0.0002 -0.0090 -0.0029 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2096 0.1955 0.2196 -0.0025 -0.0026 -0.0077 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0886 0.0753 0.1080 0.0007  -0.0020 -0.0060 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2288 0.2241 0.2489 0.0008  -0.0093 -0.0024 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1364 0.1200 0.1557 0.0071  0.0048  -0.0040 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1442 0.1234 0.1686 0.0090  0.0113  -0.0034 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1526 0.1259 0.1789 0.0071  0.0150  -0.0057 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1576 0.1280 0.1768 0.0020  0.0143  -0.0105 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1502 0.1247 0.1704 0.0073  0.0157  -0.0070 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1545 0.1340 0.1727 0.0089  0.0127  -0.0048 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1646 0.1462 0.1756 0.0063  0.0083  -0.0062 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1615 0.1442 0.1870 0.0128  0.0150  -0.0004 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1482 0.1207 0.1846 0.0104  0.0188  -0.0015 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1557 0.1215 0.1949 0.0086  0.0231  -0.0036 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1863 0.1416 0.2203 0.0039  0.0305  -0.0113 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1968 0.1476 0.2250 -0.0016 0.0316  -0.0165 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1591 0.1257 0.2120 0.0132  0.0268  0.0039  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1625 0.1221 0.2201 0.0119  0.0315  0.0031  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1830 0.1444 0.2571 0.0169  0.0354  0.0130  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1979 0.1535 0.2781 0.0160  0.0393  0.0140  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2141 0.1565 0.2998 0.0152  0.0499  0.0100  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2273 0.1606 0.3112 0.0139  0.0577  0.0032  20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2343 0.1717 0.3270 0.0147  0.0535  0.0122  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1787 0.1308 0.2135 0.0048  0.0357  -0.0127 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2130 0.1544 0.2423 -0.0013 0.0449  -0.0214 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2158 0.1586 0.2281 -0.0104 0.0403  -0.0281 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2564 0.1914 0.2608 -0.0186 0.0475  -0.0363 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2318 0.1686 0.2682 0.0018  0.0537  -0.0214 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2121 0.1556 0.2416 0.0019  0.0486  -0.0210 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2015 0.1550 0.2370 0.0083  0.0420  -0.0127 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2362 0.1774 0.2536 -0.0046 0.0502  -0.0278 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2136 0.1697 0.2411 0.0065  0.0398  -0.0148 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2303 0.1795 0.2472 -0.0010 0.0444  -0.0233 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2156 0.1689 0.2227 -0.0099 0.0291  -0.0243 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2069 0.1651 0.2013 -0.0178 0.0229  -0.0269 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2190 0.1832 0.2130 -0.0197 0.0159  -0.0247 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2281 0.1991 0.2151 -0.0256 0.0096  -0.0240 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2075 0.1728 0.1990 -0.0160 0.0168  -0.0234 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2140 0.1746 0.2046 -0.0155 0.0235  -0.0260 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2264 0.1944 0.2139 -0.0139 0.0169  -0.0221 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2461 0.1991 0.2262 -0.0260 0.0317  -0.0350 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2035 0.1660 0.2062 -0.0151 0.0170  -0.0225 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1997 0.1678 0.2030 -0.0166 0.0110  -0.0205 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2190 0.1860 0.2132 -0.0271 0.0118  -0.0256 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2274 0.1850 0.2172 -0.0325 0.0203  -0.0321 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1959 0.1617 0.2092 -0.0110 0.0133  -0.0177 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2035 0.1804 0.1957 -0.0305 0.0037  -0.0224 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2068 0.1869 0.1900 -0.0422 0.0025  -0.0255 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2196 0.1974 0.2064 -0.0434 0.0042  -0.0268 24  THR   A C   
141  O O   . THR   A 18  ? 0.1987 0.1743 0.1954 -0.0348 0.0048  -0.0242 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2248 0.2198 0.2075 -0.0452 -0.0079 -0.0185 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2249 0.2259 0.2199 -0.0375 -0.0128 -0.0124 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2395 0.2379 0.2196 -0.0442 -0.0105 -0.0157 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2189 0.1987 0.1969 -0.0552 0.0043  -0.0305 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2208 0.1999 0.2019 -0.0569 0.0050  -0.0313 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2009 0.1910 0.1931 -0.0495 -0.0035 -0.0231 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2036 0.1905 0.2031 -0.0444 -0.0018 -0.0225 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2462 0.2289 0.2149 -0.0728 0.0051  -0.0359 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3265 0.3127 0.2985 -0.0755 0.0032  -0.0350 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3790 0.3523 0.3544 -0.0734 0.0115  -0.0399 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3705 0.3722 0.3464 -0.0778 -0.0063 -0.0282 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3912 0.3718 0.3684 -0.0772 0.0073  -0.0378 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3992 0.3973 0.3779 -0.0791 -0.0035 -0.0305 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1944 0.1973 0.1889 -0.0491 -0.0119 -0.0164 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1905 0.2025 0.1977 -0.0421 -0.0176 -0.0093 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1675 0.1729 0.1831 -0.0305 -0.0144 -0.0090 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1786 0.1856 0.2021 -0.0265 -0.0146 -0.0073 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2055 0.2313 0.2175 -0.0426 -0.0255 -0.0010 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2888 0.3230 0.3163 -0.0362 -0.0290 0.0056  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3328 0.3734 0.3641 -0.0399 -0.0311 0.0074  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3034 0.3366 0.3402 -0.0269 -0.0286 0.0085  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1672 0.1657 0.1802 -0.0265 -0.0110 -0.0107 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1618 0.1559 0.1815 -0.0177 -0.0082 -0.0098 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1551 0.1427 0.1771 -0.0169 -0.0034 -0.0119 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1542 0.1442 0.1829 -0.0126 -0.0039 -0.0093 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1660 0.1548 0.1827 -0.0147 -0.0052 -0.0109 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1767 0.1713 0.1928 -0.0136 -0.0095 -0.0079 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1796 0.1813 0.2027 -0.0109 -0.0136 -0.0036 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1847 0.1764 0.1943 -0.0158 -0.0080 -0.0098 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1640 0.1433 0.1807 -0.0217 0.0020  -0.0165 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1696 0.1416 0.1901 -0.0209 0.0075  -0.0175 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1597 0.1371 0.1824 -0.0236 0.0042  -0.0166 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1667 0.1423 0.1954 -0.0206 0.0060  -0.0146 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1806 0.1408 0.1960 -0.0265 0.0161  -0.0237 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1810 0.1340 0.1995 -0.0215 0.0221  -0.0236 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2078 0.1577 0.2200 -0.0243 0.0249  -0.0274 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1842 0.1335 0.2141 -0.0138 0.0264  -0.0186 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2044 0.1483 0.2242 -0.0180 0.0312  -0.0256 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1946 0.1389 0.2260 -0.0113 0.0317  -0.0192 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2005 0.1516 0.2397 -0.0094 0.0259  -0.0126 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2095 0.1512 0.2534 -0.0041 0.0365  -0.0132 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2042 0.1542 0.2543 -0.0030 0.0294  -0.0060 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2169 0.1621 0.2704 -0.0003 0.0349  -0.0060 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1587 0.1440 0.1776 -0.0295 -0.0010 -0.0169 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1665 0.1583 0.1888 -0.0323 -0.0041 -0.0156 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1714 0.1715 0.2034 -0.0257 -0.0082 -0.0105 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1869 0.1920 0.2238 -0.0266 -0.0096 -0.0093 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1973 0.1967 0.2133 -0.0420 -0.0082 -0.0162 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1629 0.1645 0.1979 -0.0197 -0.0092 -0.0082 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1628 0.1707 0.2065 -0.0146 -0.0109 -0.0050 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1553 0.1586 0.1989 -0.0097 -0.0077 -0.0049 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1556 0.1619 0.2023 -0.0064 -0.0082 -0.0035 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1789 0.1949 0.2272 -0.0139 -0.0150 -0.0015 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1857 0.2100 0.2366 -0.0194 -0.0189 0.0009  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2226 0.2524 0.2820 -0.0190 -0.0193 0.0026  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.1886 0.2147 0.2318 -0.0258 -0.0216 0.0010  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1519 0.1486 0.1932 -0.0097 -0.0042 -0.0056 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1428 0.1372 0.1848 -0.0059 -0.0019 -0.0034 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1529 0.1531 0.1987 -0.0049 -0.0022 -0.0010 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1748 0.1774 0.2229 -0.0069 -0.0020 -0.0008 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1564 0.1428 0.1985 -0.0063 0.0027  -0.0030 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1662 0.1519 0.2122 -0.0024 0.0051  0.0016  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1690 0.1536 0.2121 -0.0002 0.0051  0.0007  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1976 0.1754 0.2485 -0.0020 0.0108  0.0039  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1383 0.1414 0.1839 -0.0029 -0.0022 0.0005  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1462 0.1553 0.1930 -0.0043 -0.0016 0.0023  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1466 0.1568 0.1936 -0.0040 -0.0007 0.0079  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1676 0.1823 0.2161 -0.0067 -0.0004 0.0118  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1384 0.1508 0.1848 -0.0042 -0.0014 0.0000  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1691 0.1877 0.2140 -0.0083 0.0006  0.0007  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1631 0.1759 0.2140 -0.0039 -0.0016 -0.0030 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1478 0.1551 0.1945 -0.0010 -0.0002 0.0096  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1423 0.1526 0.1925 -0.0001 0.0007  0.0167  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1508 0.1548 0.2025 0.0039  0.0027  0.0168  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1447 0.1454 0.1917 0.0047  0.0021  0.0116  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1562 0.1768 0.2036 -0.0034 -0.0010 0.0192  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1653 0.1927 0.2165 -0.0033 -0.0014 0.0280  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1893 0.2247 0.2461 -0.0055 -0.0021 0.0377  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1624 0.1910 0.2132 -0.0012 -0.0015 0.0293  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2036 0.2462 0.2647 -0.0049 -0.0028 0.0458  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1826 0.2210 0.2397 -0.0023 -0.0023 0.0402  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1750 0.1986 0.2216 0.0011  -0.0011 0.0233  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.1942 0.2378 0.2532 -0.0012 -0.0027 0.0446  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1868 0.2142 0.2338 0.0020  -0.0013 0.0267  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2025 0.2396 0.2559 0.0011  -0.0019 0.0369  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1594 0.1616 0.2186 0.0062  0.0057  0.0230  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1618 0.1578 0.2238 0.0097  0.0094  0.0229  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1708 0.1719 0.2444 0.0123  0.0116  0.0336  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1748 0.1802 0.2559 0.0116  0.0116  0.0412  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1915 0.1749 0.2525 0.0097  0.0142  0.0163  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2031 0.1812 0.2704 0.0089  0.0181  0.0181  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2071 0.1811 0.2886 0.0125  0.0250  0.0258  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2187 0.1920 0.3080 0.0124  0.0269  0.0311  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1974 0.1687 0.2839 0.0157  0.0292  0.0271  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1576 0.1588 0.2343 0.0152  0.0135  0.0354  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1544 0.1621 0.2451 0.0181  0.0157  0.0474  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1541 0.1538 0.2501 0.0224  0.0221  0.0454  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1559 0.1572 0.2451 0.0223  0.0204  0.0415  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1706 0.1954 0.2591 0.0148  0.0091  0.0548  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.1984 0.2350 0.3020 0.0164  0.0093  0.0699  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2395 0.2710 0.3549 0.0218  0.0150  0.0732  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2733 0.3254 0.3766 0.0112  0.0039  0.0785  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1655 0.1556 0.2744 0.0258  0.0306  0.0476  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1739 0.1543 0.2895 0.0291  0.0395  0.0446  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.1892 0.1697 0.3039 0.0290  0.0392  0.0442  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1793 0.1706 0.3049 0.0326  0.0388  0.0543  36  SER   A C   
248  O O   . SER   A 30  ? 0.1945 0.1822 0.3164 0.0333  0.0416  0.0488  36  SER   A O   
249  C CB  A SER   A 30  ? 0.1777 0.1455 0.3079 0.0315  0.0506  0.0459  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2393 0.2054 0.3662 0.0308  0.0507  0.0431  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.1768 0.1350 0.3158 0.0345  0.0613  0.0432  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3103 0.2830 0.4559 0.0342  0.0516  0.0576  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1774 0.1840 0.3146 0.0334  0.0344  0.0691  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1798 0.2001 0.3273 0.0355  0.0328  0.0802  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1620 0.1891 0.2925 0.0318  0.0258  0.0741  37  SER   A C   
256  O O   . SER   A 31  ? 0.1752 0.2087 0.3113 0.0336  0.0266  0.0785  37  SER   A O   
257  C CB  . SER   A 31  ? 0.1987 0.2373 0.3606 0.0349  0.0279  0.0988  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2666 0.3184 0.4137 0.0275  0.0175  0.0994  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1464 0.1715 0.2575 0.0269  0.0200  0.0638  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1552 0.1843 0.2505 0.0232  0.0146  0.0569  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1532 0.1678 0.2369 0.0238  0.0173  0.0430  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1496 0.1660 0.2221 0.0215  0.0137  0.0378  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1575 0.1946 0.2413 0.0169  0.0074  0.0556  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1776 0.2327 0.2684 0.0130  0.0032  0.0692  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1760 0.2380 0.2542 0.0051  -0.0020 0.0661  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1472 0.2106 0.2118 0.0008  -0.0040 0.0579  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1644 0.2377 0.2193 -0.0079 -0.0072 0.0569  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1908 0.2754 0.2465 -0.0141 -0.0096 0.0639  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1687 0.2412 0.2131 -0.0114 -0.0072 0.0493  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1468 0.1477 0.2322 0.0254  0.0235  0.0371  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1490 0.1384 0.2220 0.0234  0.0252  0.0248  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1423 0.1339 0.2011 0.0194  0.0177  0.0190  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1487 0.1374 0.1975 0.0175  0.0160  0.0125  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1724 0.1591 0.2434 0.0243  0.0286  0.0215  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1704 0.1467 0.2285 0.0205  0.0305  0.0100  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1872 0.1543 0.2431 0.0180  0.0345  0.0045  39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1862 0.1639 0.2360 0.0190  0.0283  0.0067  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1388 0.1355 0.1981 0.0179  0.0138  0.0219  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1294 0.1281 0.1786 0.0146  0.0083  0.0169  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1310 0.1251 0.1794 0.0130  0.0084  0.0139  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1401 0.1335 0.1960 0.0137  0.0109  0.0181  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1263 0.1365 0.1748 0.0124  0.0041  0.0215  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1447 0.1608 0.1903 0.0118  0.0028  0.0227  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1596 0.1869 0.2026 0.0069  -0.0003 0.0258  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1629 0.1726 0.2004 0.0119  0.0022  0.0151  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1290 0.1213 0.1699 0.0107  0.0056  0.0079  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1289 0.1195 0.1688 0.0084  0.0045  0.0054  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1258 0.1209 0.1619 0.0069  0.0002  0.0031  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1282 0.1235 0.1608 0.0070  -0.0013 0.0013  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1424 0.1241 0.1795 0.0065  0.0077  0.0005  41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1468 0.1272 0.1827 0.0032  0.0067  -0.0020 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1747 0.1456 0.2104 0.0006  0.0127  -0.0054 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1454 0.1296 0.1759 0.0003  0.0018  -0.0050 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1259 0.1244 0.1639 0.0053  -0.0010 0.0034  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1211 0.1231 0.1589 0.0041  -0.0031 0.0012  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1258 0.1270 0.1652 0.0024  -0.0040 -0.0005 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1362 0.1367 0.1771 0.0013  -0.0029 0.0003  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1193 0.1275 0.1581 0.0023  -0.0023 0.0025  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1376 0.1475 0.1785 0.0010  -0.0017 -0.0008 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1365 0.1473 0.1731 0.0026  -0.0019 0.0048  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1169 0.1191 0.1571 0.0020  -0.0061 -0.0018 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1240 0.1283 0.1672 -0.0002 -0.0077 -0.0022 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1328 0.1422 0.1836 0.0006  -0.0079 -0.0015 43  SER   A C   
304  O O   . SER   A 37  ? 0.1349 0.1448 0.1879 0.0024  -0.0065 -0.0014 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1441 0.1471 0.1831 -0.0030 -0.0099 -0.0027 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1501 0.1552 0.1885 -0.0023 -0.0121 -0.0011 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1426 0.1554 0.1986 -0.0009 -0.0086 -0.0012 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1531 0.1706 0.2199 0.0002  -0.0071 -0.0002 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1680 0.1902 0.2418 0.0009  -0.0106 0.0044  44  SER   A C   
310  O O   . SER   A 38  ? 0.1988 0.2230 0.2679 -0.0019 -0.0151 0.0064  44  SER   A O   
311  C CB  . SER   A 38  ? 0.1823 0.2025 0.2535 -0.0017 -0.0056 -0.0013 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2152 0.2372 0.2847 -0.0043 -0.0094 0.0002  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1693 0.1939 0.2551 0.0037  -0.0081 0.0066  45  THR   A N   
314  C CA  . THR   A 39  ? 0.1841 0.2149 0.2801 0.0048  -0.0114 0.0137  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2016 0.2384 0.3163 0.0066  -0.0086 0.0175  45  THR   A C   
316  O O   . THR   A 39  ? 0.1866 0.2202 0.3066 0.0077  -0.0017 0.0129  45  THR   A O   
317  C CB  . THR   A 39  ? 0.1950 0.2225 0.2920 0.0077  -0.0100 0.0151  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2002 0.2233 0.3047 0.0101  -0.0022 0.0115  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2043 0.2263 0.2847 0.0064  -0.0118 0.0116  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2114 0.2578 0.3370 0.0063  -0.0135 0.0265  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2183 0.2720 0.3662 0.0089  -0.0107 0.0325  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2142 0.2645 0.3783 0.0144  -0.0037 0.0349  46  THR   A C   
323  O O   . THR   A 40  ? 0.2445 0.2919 0.4226 0.0171  0.0053  0.0323  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2602 0.3284 0.4152 0.0055  -0.0193 0.0432  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3248 0.3972 0.4777 0.0045  -0.0250 0.0504  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2700 0.3400 0.4090 -0.0011 -0.0241 0.0392  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2185 0.2675 0.3794 0.0154  -0.0065 0.0387  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2229 0.2674 0.3986 0.0202  0.0004  0.0411  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2163 0.2472 0.3789 0.0201  0.0080  0.0292  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2113 0.2385 0.3526 0.0170  0.0042  0.0233  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2564 0.3070 0.4350 0.0205  -0.0067 0.0519  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.1999 0.2241 0.3756 0.0228  0.0188  0.0265  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2128 0.2258 0.3761 0.0207  0.0262  0.0158  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2081 0.2182 0.3648 0.0216  0.0230  0.0185  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2188 0.2324 0.3898 0.0251  0.0209  0.0284  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2487 0.2547 0.4279 0.0212  0.0409  0.0104  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3183 0.3254 0.4995 0.0184  0.0461  0.0042  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4089 0.4081 0.6053 0.0175  0.0626  -0.0025 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4026 0.4021 0.6256 0.0226  0.0693  0.0038  48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4308 0.4234 0.6115 0.0103  0.0700  -0.0150 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1779 0.1830 0.3139 0.0182  0.0220  0.0110  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1831 0.1853 0.3106 0.0184  0.0193  0.0123  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1743 0.1678 0.3062 0.0179  0.0297  0.0073  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1850 0.1735 0.3214 0.0155  0.0400  0.0001  49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1616 0.1527 0.2888 0.0186  0.0274  0.0099  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1663 0.1487 0.2978 0.0178  0.0372  0.0060  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1702 0.1491 0.2812 0.0126  0.0376  -0.0019 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1828 0.1544 0.2949 0.0100  0.0464  -0.0066 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1824 0.1648 0.3294 0.0225  0.0361  0.0165  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2204 0.2082 0.3984 0.0285  0.0380  0.0284  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1549 0.1390 0.2486 0.0108  0.0289  -0.0026 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1546 0.1377 0.2314 0.0061  0.0289  -0.0081 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1746 0.1569 0.2458 -0.0007 0.0364  -0.0168 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.1921 0.1764 0.2668 -0.0014 0.0378  -0.0185 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1446 0.1336 0.2086 0.0069  0.0186  -0.0052 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1636 0.1539 0.2290 0.0108  0.0119  0.0019  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1661 0.1532 0.2359 0.0117  0.0140  0.0041  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1691 0.1638 0.2302 0.0117  0.0049  0.0049  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1912 0.1717 0.2527 -0.0067 0.0407  -0.0220 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2081 0.1905 0.2598 -0.0163 0.0467  -0.0299 52  THR   A CA  
361  C C   . THR   A 46  ? 0.1914 0.1820 0.2269 -0.0203 0.0395  -0.0283 52  THR   A C   
362  O O   . THR   A 46  ? 0.2013 0.1923 0.2334 -0.0174 0.0348  -0.0246 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2650 0.2395 0.3199 -0.0227 0.0599  -0.0378 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3268 0.2985 0.3779 -0.0227 0.0595  -0.0368 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.2803 0.2465 0.3558 -0.0177 0.0686  -0.0380 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1878 0.1860 0.2150 -0.0264 0.0382  -0.0297 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1678 0.1757 0.1835 -0.0299 0.0316  -0.0258 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1860 0.1979 0.1913 -0.0415 0.0367  -0.0303 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2016 0.2127 0.2036 -0.0513 0.0452  -0.0377 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1702 0.1861 0.1837 -0.0308 0.0267  -0.0222 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1727 0.1846 0.1956 -0.0213 0.0228  -0.0191 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1685 0.1954 0.1748 -0.0328 0.0197  -0.0153 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1855 0.1944 0.2114 -0.0123 0.0165  -0.0138 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1653 0.1821 0.1646 -0.0421 0.0322  -0.0264 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1752 0.1991 0.1635 -0.0543 0.0353  -0.0291 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1797 0.2185 0.1598 -0.0644 0.0325  -0.0263 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1828 0.2289 0.1657 -0.0595 0.0248  -0.0182 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1727 0.2004 0.1586 -0.0509 0.0295  -0.0234 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2057 0.2492 0.1753 -0.0799 0.0394  -0.0329 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2230 0.2833 0.1832 -0.0925 0.0366  -0.0294 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2588 0.3296 0.2070 -0.1060 0.0374  -0.0296 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2871 0.3557 0.2256 -0.1204 0.0474  -0.0402 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2432 0.3001 0.2008 -0.1011 0.0450  -0.0383 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2373 0.2837 0.2080 -0.0875 0.0445  -0.0382 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2271 0.2814 0.2030 -0.0783 0.0331  -0.0263 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2039 0.2483 0.1907 -0.0677 0.0335  -0.0275 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2000 0.2452 0.1939 -0.0570 0.0256  -0.0196 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2053 0.2600 0.1983 -0.0549 0.0176  -0.0096 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2175 0.2542 0.2205 -0.0488 0.0263  -0.0213 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2512 0.3341 0.2006 -0.1023 0.0278  -0.0180 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2475 0.3406 0.1884 -0.1119 0.0270  -0.0161 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2452 0.3548 0.1919 -0.1066 0.0156  -0.0002 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2738 0.3846 0.2314 -0.0947 0.0095  0.0086  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2338 0.3094 0.1772 -0.1055 0.0331  -0.0242 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2296 0.2957 0.1879 -0.0829 0.0258  -0.0166 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2853 0.4072 0.2257 -0.1153 0.0138  0.0035  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3147 0.4518 0.2634 -0.1097 0.0046  0.0187  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3016 0.4312 0.2520 -0.1033 0.0055  0.0168  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3164 0.4613 0.2689 -0.1054 0.0005  0.0266  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3959 0.5616 0.3397 -0.1252 -0.0014 0.0310  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5080 0.6886 0.4679 -0.1153 -0.0107 0.0497  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5441 0.7500 0.5038 -0.1264 -0.0164 0.0627  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5138 0.6807 0.4875 -0.0967 -0.0115 0.0515  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2583 0.3652 0.2096 -0.0946 0.0116  0.0055  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2332 0.3321 0.1867 -0.0877 0.0122  0.0043  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2359 0.3416 0.2014 -0.0755 0.0047  0.0165  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2257 0.3311 0.2007 -0.0662 0.0012  0.0223  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2521 0.3273 0.2084 -0.0788 0.0185  -0.0063 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2651 0.3275 0.2118 -0.0914 0.0312  -0.0218 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2038 0.3141 0.1689 -0.0757 0.0036  0.0194  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.1976 0.3114 0.1743 -0.0644 -0.0008 0.0286  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1678 0.2670 0.1438 -0.0574 0.0020  0.0225  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1694 0.2721 0.1524 -0.0510 -0.0002 0.0285  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2276 0.3659 0.2086 -0.0707 -0.0060 0.0421  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2622 0.4171 0.2501 -0.0735 -0.0106 0.0535  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.3166 0.4969 0.3139 -0.0775 -0.0161 0.0701  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3453 0.5469 0.3366 -0.0926 -0.0194 0.0768  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.2621 0.4422 0.2751 -0.0649 -0.0169 0.0779  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1603 0.2437 0.1289 -0.0594 0.0074  0.0111  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1644 0.2329 0.1336 -0.0522 0.0098  0.0063  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1583 0.2089 0.1295 -0.0461 0.0132  -0.0008 60  THR   A C   
422  O O   . THR   A 54  ? 0.1789 0.2268 0.1478 -0.0513 0.0167  -0.0056 60  THR   A O   
423  C CB  . THR   A 54  ? 0.2022 0.2705 0.1631 -0.0608 0.0134  0.0020  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.2893 0.3517 0.2424 -0.0709 0.0199  -0.0069 60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.1947 0.2825 0.1536 -0.0682 0.0099  0.0095  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1508 0.1910 0.1269 -0.0361 0.0122  -0.0006 61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1443 0.1706 0.1245 -0.0302 0.0142  -0.0048 61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1383 0.1568 0.1217 -0.0219 0.0122  -0.0031 61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1414 0.1625 0.1224 -0.0220 0.0112  -0.0012 61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1314 0.1413 0.1199 -0.0158 0.0115  -0.0036 62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1195 0.1233 0.1098 -0.0100 0.0092  -0.0016 62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1171 0.1202 0.1113 -0.0046 0.0058  0.0003  62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1298 0.1319 0.1275 -0.0042 0.0064  -0.0008 62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1506 0.1447 0.1442 -0.0103 0.0127  -0.0034 62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.1756 0.1655 0.1718 -0.0055 0.0094  0.0006  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1592 0.1521 0.1485 -0.0165 0.0175  -0.0063 62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1174 0.1209 0.1105 -0.0014 0.0032  0.0025  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1213 0.1231 0.1167 0.0020  0.0010  0.0032  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1244 0.1220 0.1181 0.0029  -0.0011 0.0043  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1370 0.1340 0.1271 0.0015  -0.0012 0.0050  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1297 0.1363 0.1261 0.0036  0.0012  0.0043  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1237 0.1304 0.1179 0.0044  0.0022  0.0047  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1379 0.1488 0.1307 0.0029  0.0035  0.0058  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1369 0.1396 0.1302 0.0055  0.0027  0.0034  63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1554 0.1661 0.1469 0.0034  0.0055  0.0058  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1526 0.1546 0.1437 0.0050  0.0055  0.0024  63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1634 0.1694 0.1544 0.0045  0.0070  0.0037  63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.1948 0.2002 0.1843 0.0038  0.0107  0.0024  63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1209 0.1169 0.1167 0.0040  -0.0033 0.0049  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1293 0.1242 0.1224 0.0026  -0.0061 0.0070  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1339 0.1292 0.1211 0.0011  -0.0055 0.0046  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1377 0.1327 0.1263 0.0022  -0.0040 0.0026  64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1435 0.1383 0.1424 0.0031  -0.0089 0.0098  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1461 0.1430 0.1421 -0.0002 -0.0130 0.0139  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1464 0.1438 0.1420 -0.0018 -0.0143 0.0181  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1581 0.1574 0.1508 -0.0031 -0.0155 0.0139  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.1710 0.1726 0.1629 -0.0065 -0.0188 0.0232  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.1739 0.1774 0.1616 -0.0087 -0.0196 0.0179  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.1737 0.1792 0.1615 -0.0104 -0.0217 0.0233  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2140 0.2261 0.1963 -0.0176 -0.0266 0.0288  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1331 0.1285 0.1140 -0.0020 -0.0057 0.0049  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1449 0.1395 0.1192 -0.0051 -0.0030 0.0014  65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.1514 0.1471 0.1187 -0.0114 -0.0064 0.0026  65  CYS   A C   
464  O O   . CYS   A 59  ? 0.1566 0.1545 0.1196 -0.0150 -0.0090 0.0059  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1498 0.1448 0.1213 -0.0054 0.0003  0.0002  65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.1722 0.1648 0.1369 -0.0099 0.0065  -0.0053 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.1609 0.1564 0.1269 -0.0139 -0.0069 0.0010  66  SER   A N   
468  C CA  . SER   A 60  ? 0.1767 0.1762 0.1356 -0.0220 -0.0111 0.0034  66  SER   A CA  
469  C C   . SER   A 60  ? 0.1748 0.1745 0.1215 -0.0302 -0.0084 -0.0001 66  SER   A C   
470  O O   . SER   A 60  ? 0.2011 0.2068 0.1416 -0.0373 -0.0134 0.0046  66  SER   A O   
471  C CB  . SER   A 60  ? 0.1978 0.1976 0.1570 -0.0241 -0.0116 0.0016  66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2270 0.2211 0.1817 -0.0263 -0.0044 -0.0065 66  SER   A OG  
473  N N   . SER   A 61  ? 0.1683 0.1625 0.1130 -0.0292 -0.0003 -0.0074 67  SER   A N   
474  C CA  . SER   A 61  ? 0.1814 0.1747 0.1151 -0.0372 0.0045  -0.0122 67  SER   A CA  
475  C C   . SER   A 61  ? 0.1789 0.1752 0.1101 -0.0376 0.0022  -0.0084 67  SER   A C   
476  O O   . SER   A 61  ? 0.1917 0.1882 0.1131 -0.0451 0.0055  -0.0118 67  SER   A O   
477  C CB  . SER   A 61  ? 0.1942 0.1799 0.1300 -0.0357 0.0156  -0.0207 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.1962 0.1808 0.1430 -0.0260 0.0181  -0.0190 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.1800 0.1785 0.1194 -0.0308 -0.0032 -0.0016 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.1815 0.1826 0.1194 -0.0314 -0.0061 0.0032  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.1968 0.2023 0.1402 -0.0308 -0.0141 0.0130  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.1973 0.2043 0.1417 -0.0309 -0.0164 0.0183  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.1882 0.1865 0.1328 -0.0240 -0.0021 0.0016  68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.1959 0.1916 0.1389 -0.0240 0.0061  -0.0053 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.2065 0.2032 0.1392 -0.0314 0.0084  -0.0073 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2274 0.2212 0.1611 -0.0311 0.0180  -0.0141 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2176 0.2075 0.1468 -0.0363 0.0252  -0.0211 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2396 0.2290 0.1611 -0.0432 0.0230  -0.0226 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.2427 0.2293 0.1761 -0.0353 0.0356  -0.0266 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.2035 0.2105 0.1534 -0.0288 -0.0174 0.0159  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.2079 0.2182 0.1686 -0.0260 -0.0231 0.0255  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2239 0.2297 0.1931 -0.0190 -0.0207 0.0268  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2514 0.2585 0.2264 -0.0189 -0.0232 0.0345  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2407 0.2597 0.1983 -0.0339 -0.0297 0.0351  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2415 0.2668 0.1935 -0.0412 -0.0330 0.0357  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.2632 0.3005 0.2173 -0.0483 -0.0414 0.0494  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.2957 0.3414 0.2396 -0.0593 -0.0448 0.0493  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.2678 0.3192 0.1945 -0.0727 -0.0455 0.0472  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.2799 0.3297 0.1985 -0.0758 -0.0434 0.0457  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.2937 0.3527 0.2103 -0.0843 -0.0478 0.0461  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.1879 0.1887 0.1581 -0.0142 -0.0156 0.0198  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.1954 0.1928 0.1706 -0.0102 -0.0128 0.0197  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.1733 0.1683 0.1539 -0.0055 -0.0094 0.0152  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.1745 0.1700 0.1532 -0.0046 -0.0080 0.0110  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2329 0.2303 0.1996 -0.0128 -0.0102 0.0166  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3386 0.3381 0.3012 -0.0176 -0.0132 0.0223  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4569 0.4558 0.4131 -0.0194 -0.0101 0.0194  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5261 0.5279 0.4767 -0.0254 -0.0134 0.0253  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.5748 0.5814 0.5167 -0.0323 -0.0163 0.0257  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.1646 0.1568 0.1515 -0.0034 -0.0071 0.0158  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.1549 0.1460 0.1447 -0.0014 -0.0033 0.0115  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.1812 0.1737 0.1660 -0.0032 -0.0005 0.0088  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2213 0.2118 0.2046 -0.0051 0.0003  0.0103  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1506 0.1376 0.1500 -0.0002 -0.0009 0.0126  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.1606 0.1479 0.1678 0.0020  -0.0034 0.0160  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2011 0.1885 0.2121 0.0036  -0.0022 0.0132  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.1629 0.1517 0.1751 0.0020  -0.0073 0.0231  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.1763 0.1647 0.1950 0.0051  -0.0050 0.0181  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.2012 0.1913 0.2210 0.0040  -0.0084 0.0246  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1528 0.1493 0.1360 -0.0029 0.0010  0.0060  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1542 0.1549 0.1339 -0.0049 0.0031  0.0050  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1393 0.1438 0.1209 -0.0069 0.0052  0.0036  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1401 0.1471 0.1249 -0.0056 0.0048  0.0034  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1593 0.1645 0.1379 -0.0035 0.0034  0.0050  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.1697 0.1721 0.1435 -0.0043 0.0028  0.0048  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.1938 0.1963 0.1628 -0.0070 0.0033  0.0053  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.1735 0.1738 0.1466 -0.0038 0.0021  0.0038  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2003 0.2014 0.1634 -0.0095 0.0030  0.0050  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.1997 0.1986 0.1662 -0.0071 0.0023  0.0029  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2039 0.2035 0.1652 -0.0101 0.0027  0.0035  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2368 0.2359 0.1902 -0.0151 0.0029  0.0023  72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1439 0.1502 0.1226 -0.0112 0.0075  0.0027  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1490 0.1620 0.1269 -0.0160 0.0094  0.0014  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1513 0.1760 0.1305 -0.0156 0.0076  0.0051  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.1785 0.2059 0.1575 -0.0141 0.0073  0.0071  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.1860 0.1972 0.1592 -0.0223 0.0129  -0.0010 73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.2114 0.2181 0.1834 -0.0195 0.0117  0.0008  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1586 0.1612 0.1338 -0.0132 0.0085  0.0028  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1311 0.1631 0.1129 -0.0172 0.0071  0.0067  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1514 0.1959 0.1385 -0.0161 0.0054  0.0128  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1389 0.1959 0.1254 -0.0234 0.0048  0.0156  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1489 0.2037 0.1316 -0.0280 0.0058  0.0120  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.1881 0.2299 0.1824 -0.0089 0.0047  0.0148  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.2112 0.2445 0.2052 -0.0040 0.0057  0.0128  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.1970 0.2334 0.1912 -0.0084 0.0040  0.0121  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1350 0.2069 0.1265 -0.0250 0.0032  0.0232  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1358 0.2245 0.1299 -0.0315 0.0010  0.0301  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1246 0.2172 0.1312 -0.0241 -0.0005 0.0372  75  SER   A C   
549  O O   . SER   A 69  ? 0.1347 0.2233 0.1499 -0.0157 0.0010  0.0394  75  SER   A O   
550  C CB  . SER   A 69  ? 0.1819 0.2872 0.1779 -0.0369 -0.0003 0.0371  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.2811 0.3823 0.2649 -0.0447 0.0017  0.0300  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1358 0.2344 0.1437 -0.0272 -0.0023 0.0401  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1323 0.2326 0.1527 -0.0201 -0.0030 0.0468  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1369 0.2570 0.1630 -0.0264 -0.0066 0.0579  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1566 0.2868 0.1731 -0.0379 -0.0085 0.0576  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1378 0.2210 0.1551 -0.0150 -0.0016 0.0385  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1324 0.2115 0.1387 -0.0220 -0.0016 0.0312  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1358 0.2035 0.1327 -0.0242 0.0009  0.0218  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1390 0.2251 0.1460 -0.0263 -0.0031 0.0341  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1511 0.2141 0.1411 -0.0302 0.0031  0.0151  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1560 0.2375 0.1535 -0.0332 -0.0013 0.0263  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1574 0.2272 0.1472 -0.0350 0.0023  0.0167  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1381 0.2648 0.1805 -0.0198 -0.0070 0.0685  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1405 0.2883 0.1920 -0.0251 -0.0110 0.0826  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1404 0.2871 0.1853 -0.0298 -0.0128 0.0802  77  SER   A C   
566  O O   . SER   A 71  ? 0.1434 0.2718 0.1812 -0.0261 -0.0103 0.0687  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1570 0.3106 0.2320 -0.0152 -0.0093 0.0956  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1792 0.3149 0.2607 -0.0049 -0.0048 0.0909  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1411 0.3086 0.1892 -0.0385 -0.0172 0.0919  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1483 0.3164 0.1908 -0.0437 -0.0188 0.0907  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1564 0.3153 0.2136 -0.0318 -0.0173 0.0947  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1693 0.3302 0.2447 -0.0226 -0.0159 0.1043  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1735 0.3688 0.2141 -0.0585 -0.0244 0.1032  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2073 0.4094 0.2297 -0.0729 -0.0245 0.0961  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.3030 0.5320 0.3185 -0.0915 -0.0297 0.1059  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3848 0.6178 0.3794 -0.1081 -0.0278 0.0957  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4412 0.6944 0.4224 -0.1290 -0.0305 0.0988  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1524 0.3019 0.2034 -0.0323 -0.0167 0.0880  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1549 0.2945 0.2188 -0.0218 -0.0147 0.0908  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1688 0.3261 0.2532 -0.0200 -0.0170 0.1104  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.1903 0.3689 0.2746 -0.0302 -0.0222 0.1216  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.1890 0.3212 0.2410 -0.0264 -0.0149 0.0818  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2340 0.3641 0.2677 -0.0357 -0.0144 0.0702  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1797 0.3247 0.2117 -0.0424 -0.0164 0.0759  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1562 0.3052 0.2584 -0.0079 -0.0124 0.1148  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1652 0.3302 0.2924 -0.0042 -0.0127 0.1350  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1518 0.2998 0.2958 0.0083  -0.0053 0.1351  80  SER   A C   
588  O O   . SER   A 74  ? 0.1532 0.2786 0.2885 0.0134  -0.0004 0.1196  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2169 0.3949 0.3547 -0.0034 -0.0125 0.1440  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.3370 0.5227 0.4560 -0.0136 -0.0167 0.1379  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1627 0.3228 0.3334 0.0130  -0.0037 0.1541  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.1857 0.3311 0.3769 0.0243  0.0053  0.1565  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.1938 0.3345 0.4005 0.0324  0.0133  0.1577  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2069 0.3673 0.4316 0.0326  0.0119  0.1743  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.1919 0.3544 0.4058 0.0244  0.0031  0.1786  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2401 0.3873 0.4764 0.0350  0.0130  0.1820  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2659 0.3909 0.4846 0.0350  0.0153  0.1645  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2429 0.4107 0.5062 0.0353  0.0105  0.2080  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.1846 0.3014 0.3837 0.0378  0.0214  0.1404  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.1978 0.3068 0.4060 0.0438  0.0300  0.1367  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2144 0.3017 0.4366 0.0523  0.0436  0.1308  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2130 0.2832 0.4235 0.0518  0.0457  0.1188  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2272 0.3266 0.4073 0.0392  0.0273  0.1183  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2495 0.3676 0.4130 0.0292  0.0153  0.1211  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2485 0.3377 0.4337 0.0442  0.0364  0.1116  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.2491 0.3642 0.3952 0.0255  0.0133  0.1106  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2222 0.3092 0.4696 0.0593  0.0540  0.1383  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2224 0.2872 0.4836 0.0661  0.0697  0.1311  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2620 0.3074 0.4995 0.0635  0.0744  0.1086  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2986 0.3489 0.5272 0.0615  0.0720  0.1048  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2254 0.2970 0.5240 0.0743  0.0809  0.1471  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2707 0.3196 0.5878 0.0808  0.0989  0.1418  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.2986 0.3424 0.6274 0.0830  0.1014  0.1479  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3150 0.3459 0.6343 0.0831  0.1138  0.1283  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3295 0.3506 0.6746 0.0879  0.1194  0.1416  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3276 0.3365 0.6630 0.0873  0.1323  0.1217  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3340 0.3377 0.6826 0.0898  0.1353  0.1284  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2398 0.2646 0.4646 0.0621  0.0796  0.0937  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2410 0.2486 0.4428 0.0579  0.0835  0.0734  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2452 0.2327 0.4602 0.0607  0.1021  0.0655  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2533 0.2325 0.4799 0.0629  0.1083  0.0675  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2302 0.2327 0.4040 0.0514  0.0734  0.0622  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2563 0.2441 0.4071 0.0462  0.0761  0.0438  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2292 0.2506 0.3924 0.0481  0.0576  0.0698  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.2452 0.2235 0.4546 0.0590  0.1106  0.0544  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.2690 0.2271 0.4887 0.0595  0.1304  0.0444  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.2838 0.2243 0.4838 0.0526  0.1330  0.0289  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.2905 0.2337 0.4650 0.0469  0.1198  0.0230  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.3289 0.2826 0.5429 0.0569  0.1380  0.0349  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.3902 0.3594 0.6287 0.0640  0.1396  0.0499  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.5152 0.4861 0.7938 0.0734  0.1519  0.0655  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.5405 0.4923 0.8315 0.0745  0.1693  0.0585  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.5672 0.5593 0.8655 0.0791  0.1441  0.0854  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.2909 0.2130 0.5032 0.0525  0.1517  0.0216  86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.3161 0.2209 0.5106 0.0444  0.1567  0.0062  86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.3471 0.2488 0.5074 0.0334  0.1505  -0.0099 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.3636 0.2677 0.5171 0.0313  0.1516  -0.0141 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.3349 0.2193 0.5482 0.0444  0.1808  -0.0008 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.3505 0.2492 0.4896 0.0265  0.1423  -0.0171 87  SER   A N   
640  C CA  . SER   A 81  ? 0.3614 0.2583 0.4691 0.0153  0.1359  -0.0306 87  SER   A CA  
641  C C   . SER   A 81  ? 0.3763 0.2578 0.4730 0.0056  0.1444  -0.0435 87  SER   A C   
642  O O   . SER   A 81  ? 0.3711 0.2425 0.4854 0.0088  0.1560  -0.0421 87  SER   A O   
643  C CB  . SER   A 81  ? 0.3625 0.2751 0.4551 0.0158  0.1146  -0.0244 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.3435 0.2569 0.4376 0.0171  0.1087  -0.0204 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.3942 0.2756 0.4625 -0.0064 0.1372  -0.0542 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.4086 0.2774 0.4670 -0.0164 0.1447  -0.0651 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3585 0.2319 0.4207 -0.0121 0.1346  -0.0574 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.3741 0.2367 0.4346 -0.0178 0.1421  -0.0639 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.4983 0.3652 0.5278 -0.0329 0.1439  -0.0791 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5748 0.4557 0.5848 -0.0371 0.1238  -0.0759 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.7017 0.5824 0.6851 -0.0548 0.1232  -0.0875 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.7091 0.5926 0.6821 -0.0604 0.1239  -0.0913 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.7423 0.6213 0.7150 -0.0638 0.1217  -0.0922 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3176 0.2060 0.3867 -0.0020 0.1195  -0.0436 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.2879 0.1823 0.3588 0.0012  0.1090  -0.0365 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.2786 0.1747 0.3754 0.0122  0.1120  -0.0235 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.2767 0.1730 0.3762 0.0132  0.1084  -0.0199 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.2913 0.2016 0.3488 0.0019  0.0903  -0.0315 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3033 0.2140 0.3372 -0.0091 0.0859  -0.0414 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3370 0.2449 0.3567 -0.0186 0.0838  -0.0484 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3385 0.2528 0.3650 -0.0110 0.0849  -0.0435 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.3687 0.2807 0.3680 -0.0294 0.0782  -0.0547 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3640 0.2808 0.3697 -0.0216 0.0799  -0.0505 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.3876 0.3035 0.3801 -0.0312 0.0769  -0.0558 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4325 0.3540 0.4056 -0.0424 0.0707  -0.0601 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.2877 0.1873 0.4036 0.0204  0.1170  -0.0149 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2677 0.1722 0.4106 0.0304  0.1190  0.0005  90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.2865 0.1843 0.4532 0.0359  0.1355  0.0036  90  TYR   A C   
669  O O   . TYR   A 84  ? 0.3039 0.2025 0.4660 0.0346  0.1382  -0.0010 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2482 0.1739 0.3923 0.0358  0.1022  0.0144  90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2209 0.1549 0.3451 0.0317  0.0863  0.0130  90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2180 0.1526 0.3451 0.0320  0.0829  0.0172  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2164 0.1574 0.3207 0.0278  0.0758  0.0080  90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2000 0.1424 0.3110 0.0285  0.0697  0.0160  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2138 0.1618 0.3033 0.0247  0.0631  0.0071  90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.1990 0.1478 0.2922 0.0251  0.0603  0.0110  90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.1995 0.1548 0.2797 0.0220  0.0493  0.0097  90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.3016 0.1956 0.4958 0.0427  0.1450  0.0139  91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.3065 0.1980 0.5301 0.0503  0.1597  0.0216  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.3150 0.2293 0.5464 0.0567  0.1467  0.0373  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.2989 0.2290 0.5151 0.0554  0.1281  0.0425  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3216 0.2067 0.5736 0.0563  0.1697  0.0323  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3333 0.2297 0.5741 0.0553  0.1524  0.0391  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.3085 0.2028 0.5115 0.0449  0.1421  0.0219  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.3210 0.2381 0.5777 0.0634  0.1568  0.0459  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.3130 0.2533 0.5803 0.0690  0.1454  0.0627  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.2992 0.2553 0.5809 0.0733  0.1346  0.0822  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3203 0.2685 0.6219 0.0769  0.1436  0.0883  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.3104 0.2498 0.6081 0.0759  0.1610  0.0698  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.2846 0.2608 0.5519 0.0709  0.1155  0.0895  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2620 0.2537 0.5360 0.0717  0.1042  0.1052  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2573 0.2728 0.5186 0.0683  0.0866  0.1132  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2700 0.2874 0.5155 0.0655  0.0832  0.1049  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2819 0.2615 0.5351 0.0664  0.1008  0.0934  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.3109 0.2959 0.5287 0.0585  0.0851  0.0821  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3135 0.2806 0.5096 0.0530  0.0874  0.0636  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3093 0.2840 0.4800 0.0471  0.0725  0.0584  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3365 0.3143 0.4867 0.0432  0.0651  0.0501  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.2554 0.2381 0.3865 0.0384  0.0539  0.0457  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.3246 0.3006 0.4743 0.0439  0.0696  0.0461  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2452 0.2784 0.5121 0.0673  0.0760  0.1287  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2489 0.3037 0.5007 0.0614  0.0601  0.1344  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2218 0.2701 0.4415 0.0541  0.0513  0.1191  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2346 0.2762 0.4519 0.0531  0.0511  0.1173  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2483 0.3266 0.5207 0.0615  0.0533  0.1586  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2431 0.3359 0.5463 0.0673  0.0580  0.1771  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2477 0.3578 0.5460 0.0641  0.0511  0.1813  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2496 0.3367 0.5879 0.0764  0.0713  0.1891  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2574 0.3815 0.5847 0.0694  0.0555  0.1983  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2493 0.3500 0.6192 0.0825  0.0766  0.2068  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.2591 0.3788 0.6231 0.0790  0.0684  0.2113  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.2939 0.4292 0.6890 0.0845  0.0729  0.2294  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.1951 0.2466 0.3916 0.0489  0.0439  0.1091  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1793 0.2268 0.3478 0.0423  0.0356  0.0960  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1670 0.2363 0.3286 0.0359  0.0237  0.1051  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1698 0.2535 0.3355 0.0346  0.0207  0.1130  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1942 0.2282 0.3439 0.0409  0.0376  0.0786  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1991 0.2291 0.3244 0.0351  0.0300  0.0670  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.2254 0.2399 0.3345 0.0338  0.0329  0.0508  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2774 0.2787 0.3903 0.0359  0.0420  0.0447  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1738 0.1897 0.2645 0.0292  0.0255  0.0436  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1472 0.2194 0.2975 0.0306  0.0173  0.1037  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1458 0.2375 0.2876 0.0222  0.0076  0.1106  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1342 0.2214 0.2504 0.0162  0.0033  0.0951  96  SER   A C   
725  O O   . SER   A 90  ? 0.1465 0.2162 0.2520 0.0185  0.0063  0.0807  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1761 0.2748 0.3220 0.0191  0.0043  0.1189  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2140 0.2957 0.3471 0.0192  0.0059  0.1048  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1416 0.2458 0.2494 0.0076  -0.0033 0.0994  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1376 0.2391 0.2236 0.0006  -0.0063 0.0866  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1294 0.2177 0.2096 0.0052  -0.0028 0.0756  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1475 0.2245 0.2129 0.0036  -0.0028 0.0625  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1637 0.2562 0.2383 -0.0023 -0.0070 0.0770  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1758 0.2821 0.2535 -0.0086 -0.0107 0.0869  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2114 0.3310 0.2768 -0.0206 -0.0148 0.0868  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2120 0.3210 0.3039 -0.0053 -0.0102 0.0974  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2118 0.3426 0.2828 -0.0248 -0.0174 0.0971  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2210 0.3459 0.3086 -0.0153 -0.0151 0.1044  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1202 0.2106 0.2123 0.0103  0.0002  0.0815  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1306 0.2089 0.2178 0.0142  0.0040  0.0720  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1214 0.2121 0.2037 0.0091  0.0009  0.0746  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1273 0.2362 0.2191 0.0061  -0.0017 0.0877  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1442 0.2151 0.2489 0.0228  0.0117  0.0756  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1871 0.2443 0.2860 0.0259  0.0169  0.0648  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.1946 0.2358 0.2777 0.0249  0.0170  0.0506  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2175 0.2686 0.3355 0.0331  0.0267  0.0686  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1269 0.2083 0.1954 0.0080  0.0013  0.0631  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1213 0.2115 0.1836 0.0030  -0.0007 0.0635  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1283 0.2086 0.1922 0.0087  0.0038  0.0587  99  MET   A C   
749  O O   . MET   A 93  ? 0.1421 0.2061 0.2005 0.0124  0.0067  0.0490  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1354 0.2219 0.1796 -0.0044 -0.0032 0.0535  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1481 0.2438 0.1889 -0.0117 -0.0063 0.0565  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.1985 0.2862 0.2208 -0.0199 -0.0059 0.0429  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2616 0.3270 0.2842 -0.0098 -0.0031 0.0331  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1168 0.2075 0.1876 0.0085  0.0044  0.0654  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1298 0.2115 0.2020 0.0132  0.0094  0.0606  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1209 0.2043 0.1799 0.0079  0.0071  0.0554  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1405 0.2377 0.1953 0.0007  0.0028  0.0599  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1540 0.2445 0.2479 0.0185  0.0141  0.0721  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2116 0.2979 0.3231 0.0252  0.0194  0.0776  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2306 0.3230 0.3661 0.0314  0.0267  0.0880  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2544 0.3189 0.3588 0.0286  0.0249  0.0645  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1288 0.1992 0.1813 0.0105  0.0105  0.0466  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1269 0.1976 0.1686 0.0063  0.0093  0.0422  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1267 0.1896 0.1713 0.0106  0.0148  0.0389  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1322 0.1859 0.1829 0.0156  0.0199  0.0366  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1504 0.2104 0.1759 0.0026  0.0067  0.0324  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1203 0.1862 0.1591 0.0076  0.0145  0.0376  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1188 0.1772 0.1569 0.0098  0.0195  0.0331  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1538 0.1977 0.1757 0.0078  0.0180  0.0228  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.1740 0.2173 0.1856 0.0036  0.0138  0.0205  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1246 0.1940 0.1644 0.0071  0.0194  0.0373  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1530 0.2140 0.1895 0.0081  0.0247  0.0313  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1161 0.2025 0.1749 0.0090  0.0204  0.0499  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1565 0.1895 0.1778 0.0101  0.0222  0.0177  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1743 0.1964 0.1817 0.0074  0.0201  0.0103  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.1968 0.2097 0.2041 0.0081  0.0254  0.0053  103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2152 0.2276 0.2334 0.0113  0.0313  0.0065  103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2283 0.2341 0.2230 0.0039  0.0239  -0.0002 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2490 0.2468 0.2395 0.0013  0.0285  -0.0060 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2332 0.2272 0.2241 0.0019  0.0267  -0.0070 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2281 0.2236 0.2161 0.0021  0.0195  -0.0048 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2540 0.2491 0.2301 -0.0053 0.0264  -0.0096 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2709 0.2595 0.2403 -0.0109 0.0319  -0.0162 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2717 0.2567 0.2447 -0.0119 0.0425  -0.0209 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2865 0.2719 0.2464 -0.0166 0.0289  -0.0189 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2826 0.2613 0.2466 -0.0191 0.0463  -0.0277 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2911 0.2711 0.2463 -0.0225 0.0375  -0.0261 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2459 0.2345 0.2412 0.0021  0.0337  -0.0104 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2545 0.2385 0.2486 0.0012  0.0329  -0.0126 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2765 0.2521 0.2679 -0.0034 0.0426  -0.0201 105 SER   A C   
791  O O   . SER   A 99  ? 0.3179 0.2913 0.3147 -0.0030 0.0516  -0.0223 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2602 0.2478 0.2664 0.0074  0.0313  -0.0069 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.3063 0.2964 0.3269 0.0121  0.0381  -0.0032 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2304 0.2017 0.2135 -0.0086 0.0412  -0.0243 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.2428 0.2053 0.2210 -0.0155 0.0500  -0.0326 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2541 0.2145 0.2352 -0.0144 0.0478  -0.0321 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.2340 0.2002 0.2178 -0.0099 0.0384  -0.0259 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2617 0.2246 0.2214 -0.0271 0.0479  -0.0377 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2883 0.2531 0.2445 -0.0289 0.0507  -0.0386 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3333 0.3003 0.2710 -0.0411 0.0483  -0.0422 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3988 0.3639 0.3249 -0.0516 0.0493  -0.0473 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3238 0.2954 0.2583 -0.0412 0.0451  -0.0392 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2627 0.2141 0.2446 -0.0183 0.0574  -0.0388 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2638 0.2132 0.2499 -0.0166 0.0556  -0.0378 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.2543 0.2105 0.2311 -0.0195 0.0429  -0.0347 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.2411 0.2008 0.2255 -0.0132 0.0370  -0.0290 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2997 0.2372 0.2830 -0.0243 0.0688  -0.0479 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.3093 0.2420 0.2985 -0.0235 0.0805  -0.0513 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2701 0.2119 0.2515 -0.0239 0.0723  -0.0479 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2407 0.2001 0.2025 -0.0288 0.0383  -0.0371 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2292 0.1966 0.1849 -0.0317 0.0266  -0.0323 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.2030 0.1779 0.1649 -0.0237 0.0172  -0.0237 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2025 0.1834 0.1638 -0.0243 0.0087  -0.0188 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.1832 0.1581 0.1520 -0.0168 0.0193  -0.0215 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1698 0.1506 0.1446 -0.0101 0.0123  -0.0146 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1662 0.1479 0.1510 -0.0039 0.0107  -0.0116 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1565 0.1426 0.1450 -0.0003 0.0054  -0.0072 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1668 0.1487 0.1447 -0.0065 0.0150  -0.0134 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.1785 0.1614 0.1461 -0.0126 0.0143  -0.0148 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.1886 0.1748 0.1495 -0.0173 0.0078  -0.0125 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1912 0.1726 0.1587 -0.0128 0.0201  -0.0172 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1631 0.1401 0.1522 -0.0032 0.0161  -0.0143 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1650 0.1436 0.1627 0.0017  0.0141  -0.0109 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1638 0.1463 0.1589 0.0003  0.0065  -0.0089 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1710 0.1537 0.1593 -0.0052 0.0039  -0.0104 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1769 0.1491 0.1790 0.0014  0.0210  -0.0140 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.1986 0.1676 0.2134 0.0066  0.0312  -0.0125 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1436 0.1302 0.1449 0.0046  0.0033  -0.0050 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1462 0.1360 0.1485 0.0043  -0.0020 -0.0031 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1444 0.1373 0.1471 0.0052  -0.0050 -0.0004 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1493 0.1442 0.1563 0.0061  -0.0075 0.0015  111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1381 0.1308 0.1371 0.0047  -0.0040 -0.0005 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1340 0.1286 0.1336 0.0053  -0.0058 0.0019  112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1187 0.1152 0.1233 0.0076  -0.0045 0.0023  112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1241 0.1224 0.1301 0.0086  -0.0023 0.0022  112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1242 0.1207 0.1319 0.0075  -0.0050 0.0033  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1185 0.1166 0.1290 0.0072  -0.0025 0.0022  113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1140 0.1142 0.1211 0.0055  -0.0006 0.0019  113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1210 0.1193 0.1258 0.0051  -0.0008 0.0024  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1236 0.1193 0.1404 0.0072  -0.0015 0.0022  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1439 0.1402 0.1652 0.0083  -0.0028 0.0024  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1331 0.1287 0.1509 0.0045  0.0032  -0.0006 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1851 0.1798 0.2159 0.0091  -0.0016 0.0037  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1079 0.1131 0.1147 0.0036  0.0008  0.0018  114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1081 0.1178 0.1117 -0.0002 0.0027  0.0017  114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1068 0.1159 0.1106 -0.0048 0.0059  -0.0016 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1190 0.1295 0.1249 -0.0057 0.0063  -0.0023 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1155 0.1342 0.1198 -0.0009 0.0019  0.0056  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1229 0.1504 0.1239 -0.0070 0.0029  0.0070  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1426 0.1690 0.1404 -0.0072 0.0034  0.0067  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1431 0.1826 0.1484 -0.0079 0.0013  0.0138  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1183 0.1245 0.1199 -0.0082 0.0093  -0.0042 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1269 0.1303 0.1290 -0.0138 0.0152  -0.0092 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1390 0.1453 0.1344 -0.0215 0.0188  -0.0118 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1415 0.1492 0.1338 -0.0212 0.0172  -0.0099 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1463 0.1394 0.1568 -0.0099 0.0181  -0.0104 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1483 0.1364 0.1598 -0.0080 0.0184  -0.0087 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1668 0.1471 0.1902 -0.0039 0.0208  -0.0068 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.1767 0.1593 0.2040 0.0016  0.0142  -0.0017 115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1760 0.1576 0.2126 0.0042  0.0144  -0.0002 115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.1909 0.1693 0.2338 0.0023  0.0214  -0.0043 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.1904 0.1751 0.2292 0.0076  0.0081  0.0049  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1722 0.1790 0.1650 -0.0296 0.0247  -0.0171 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2204 0.2300 0.2049 -0.0402 0.0298  -0.0213 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2569 0.2547 0.2445 -0.0444 0.0401  -0.0294 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2423 0.2310 0.2403 -0.0378 0.0425  -0.0300 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2092 0.2340 0.1856 -0.0495 0.0274  -0.0195 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2057 0.2321 0.1814 -0.0560 0.0315  -0.0241 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.2906 0.2888 0.2700 -0.0564 0.0474  -0.0358 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3238 0.3094 0.3067 -0.0619 0.0602  -0.0450 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3337 0.3173 0.3208 -0.0638 0.0651  -0.0493 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3702 0.3409 0.3673 -0.0628 0.0753  -0.0549 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3850 0.3716 0.3559 -0.0772 0.0683  -0.0526 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.4420 0.4443 0.3988 -0.0913 0.0669  -0.0544 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.5243 0.5296 0.4676 -0.1087 0.0746  -0.0619 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.5547 0.5717 0.4897 -0.1131 0.0684  -0.0572 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.5087 0.5039 0.4495 -0.1199 0.0890  -0.0740 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2786 0.2745 0.2608 -0.0650 0.0579  -0.0457 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2633 0.2590 0.2476 -0.0681 0.0620  -0.0497 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2582 0.2497 0.2560 -0.0542 0.0571  -0.0444 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2908 0.2806 0.2930 -0.0552 0.0611  -0.0476 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2667 0.2798 0.2380 -0.0789 0.0568  -0.0476 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.3041 0.3244 0.2611 -0.0949 0.0610  -0.0521 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.2967 0.3314 0.2463 -0.0977 0.0523  -0.0443 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3466 0.3631 0.2952 -0.1105 0.0736  -0.0635 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3457 0.3850 0.2828 -0.1142 0.0587  -0.0507 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3827 0.4108 0.3178 -0.1231 0.0720  -0.0630 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2236 0.2153 0.2264 -0.0426 0.0479  -0.0362 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2042 0.1937 0.2175 -0.0317 0.0427  -0.0311 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1741 0.1713 0.1843 -0.0253 0.0312  -0.0230 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1704 0.1723 0.1742 -0.0263 0.0276  -0.0204 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1533 0.1515 0.1690 -0.0189 0.0264  -0.0195 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1504 0.1538 0.1644 -0.0133 0.0177  -0.0130 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1314 0.1454 0.1385 -0.0179 0.0148  -0.0106 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1418 0.1605 0.1473 -0.0233 0.0165  -0.0121 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1409 0.1415 0.1623 -0.0066 0.0144  -0.0106 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1582 0.1628 0.1772 -0.0025 0.0078  -0.0058 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1568 0.1501 0.1871 -0.0020 0.0158  -0.0097 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1218 0.1408 0.1260 -0.0164 0.0107  -0.0060 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1251 0.1560 0.1266 -0.0198 0.0076  -0.0007 121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1202 0.1523 0.1272 -0.0131 0.0035  0.0048  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1366 0.1771 0.1453 -0.0150 0.0017  0.0097  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1464 0.1826 0.1439 -0.0222 0.0069  0.0018  121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1751 0.2257 0.1740 -0.0242 0.0030  0.0104  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1695 0.2049 0.1604 -0.0310 0.0119  -0.0041 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1236 0.1479 0.1337 -0.0057 0.0022  0.0047  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1268 0.1504 0.1417 -0.0004 0.0002  0.0084  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1193 0.1343 0.1343 0.0045  -0.0002 0.0065  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1233 0.1336 0.1361 0.0043  0.0001  0.0034  122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1175 0.1305 0.1356 0.0080  -0.0002 0.0082  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1144 0.1202 0.1304 0.0101  -0.0001 0.0057  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1172 0.1228 0.1352 0.0120  0.0026  0.0074  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1304 0.1403 0.1551 0.0134  0.0044  0.0118  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1307 0.1316 0.1473 0.0106  -0.0009 0.0036  123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1478 0.1499 0.1695 0.0116  0.0006  0.0055  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1505 0.1510 0.1671 0.0094  -0.0029 0.0021  123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1640 0.1607 0.1853 0.0112  0.0004  0.0027  123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1201 0.1212 0.1338 0.0118  0.0034  0.0048  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1250 0.1244 0.1409 0.0131  0.0079  0.0050  124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1314 0.1263 0.1528 0.0145  0.0119  0.0045  124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1352 0.1254 0.1531 0.0127  0.0109  0.0010  124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1393 0.1339 0.1472 0.0107  0.0083  0.0009  124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1482 0.1394 0.1583 0.0110  0.0151  -0.0009 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1457 0.1437 0.1493 0.0095  0.0052  0.0019  124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1355 0.1322 0.1669 0.0174  0.0167  0.0085  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1478 0.1395 0.1879 0.0193  0.0224  0.0090  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1614 0.1486 0.2096 0.0213  0.0314  0.0088  125 SER   A C   
928  O O   . SER   A 119 ? 0.1945 0.1724 0.2465 0.0211  0.0387  0.0051  125 SER   A O   
929  C CB  . SER   A 119 ? 0.1493 0.1485 0.1983 0.0213  0.0199  0.0166  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1821 0.1773 0.2426 0.0239  0.0257  0.0195  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1617 0.1548 0.2138 0.0229  0.0323  0.0126  126 THR   A N   
932  C CA  . THR   A 120 ? 0.1759 0.1651 0.2394 0.0255  0.0425  0.0130  126 THR   A CA  
933  C C   . THR   A 120 ? 0.2013 0.1916 0.2574 0.0235  0.0428  0.0098  126 THR   A C   
934  O O   . THR   A 120 ? 0.1808 0.1769 0.2264 0.0212  0.0347  0.0098  126 THR   A O   
935  C CB  . THR   A 120 ? 0.1903 0.1889 0.2751 0.0312  0.0450  0.0257  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.1904 0.2033 0.2755 0.0310  0.0382  0.0329  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1948 0.1948 0.2869 0.0327  0.0433  0.0309  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2285 0.2131 0.2913 0.0242  0.0530  0.0071  127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2583 0.2447 0.3156 0.0223  0.0541  0.0046  127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2746 0.2559 0.3442 0.0241  0.0673  0.0030  127 GLY   A C   
941  O O   . GLY   A 121 ? 0.2963 0.2706 0.3790 0.0266  0.0770  0.0029  127 GLY   A O   
942  N N   . GLY   A 122 ? 0.2921 0.2755 0.3557 0.0218  0.0681  0.0005  128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.2931 0.2714 0.3653 0.0219  0.0811  -0.0030 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.3197 0.3097 0.3999 0.0249  0.0797  0.0043  128 GLY   A C   
945  O O   . GLY   A 122 ? 0.3216 0.3250 0.4100 0.0288  0.0717  0.0154  128 GLY   A O   
946  N N   . ASN   A 123 ? 0.3111 0.2968 0.3885 0.0218  0.0879  -0.0021 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3215 0.3172 0.4084 0.0243  0.0895  0.0038  129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.2932 0.3030 0.3731 0.0242  0.0753  0.0113  129 ASN   A C   
949  O O   . ASN   A 123 ? 0.2914 0.3145 0.3852 0.0278  0.0741  0.0215  129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3447 0.3444 0.4622 0.0324  0.1001  0.0133  129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.4034 0.3874 0.5300 0.0319  0.1182  0.0043  129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4544 0.4300 0.5705 0.0260  0.1262  -0.0068 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.3960 0.3754 0.5417 0.0372  0.1253  0.0087  129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.2567 0.2637 0.3147 0.0188  0.0658  0.0058  130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2395 0.2565 0.2888 0.0172  0.0545  0.0103  130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.1764 0.2026 0.2320 0.0200  0.0467  0.0189  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.1955 0.2299 0.2446 0.0177  0.0390  0.0221  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1737 0.1968 0.2381 0.0232  0.0486  0.0209  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1660 0.1973 0.2323 0.0239  0.0404  0.0278  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.1863 0.2071 0.2402 0.0219  0.0370  0.0207  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2251 0.2337 0.2747 0.0210  0.0424  0.0128  131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1773 0.2166 0.2662 0.0292  0.0442  0.0388  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.1802 0.2331 0.2855 0.0315  0.0471  0.0488  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.2081 0.2652 0.3408 0.0382  0.0550  0.0595  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.1819 0.2518 0.2811 0.0269  0.0366  0.0559  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1411 0.1674 0.1894 0.0202  0.0286  0.0233  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1457 0.1646 0.1858 0.0190  0.0252  0.0187  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1419 0.1699 0.1902 0.0201  0.0215  0.0265  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1424 0.1825 0.1923 0.0182  0.0175  0.0327  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1508 0.1659 0.1746 0.0147  0.0196  0.0127  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1596 0.1835 0.1798 0.0122  0.0148  0.0159  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1551 0.1642 0.1733 0.0137  0.0162  0.0092  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1420 0.1648 0.1940 0.0218  0.0227  0.0259  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1354 0.1666 0.1940 0.0220  0.0191  0.0331  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1289 0.1545 0.1764 0.0194  0.0146  0.0273  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1551 0.1694 0.1961 0.0193  0.0161  0.0198  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1177 0.1524 0.1632 0.0162  0.0095  0.0310  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1219 0.1524 0.1586 0.0135  0.0060  0.0258  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1273 0.1639 0.1702 0.0128  0.0047  0.0314  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1275 0.1771 0.1767 0.0108  0.0032  0.0401  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1290 0.1636 0.1561 0.0083  0.0028  0.0233  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1202 0.1510 0.1418 0.0082  0.0036  0.0196  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1217 0.1419 0.1368 0.0090  0.0036  0.0132  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1332 0.1725 0.1565 0.0067  0.0039  0.0238  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1294 0.1470 0.1393 0.0083  0.0040  0.0109  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1400 0.1757 0.1577 0.0062  0.0047  0.0205  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1296 0.1542 0.1405 0.0070  0.0048  0.0140  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1184 0.1471 0.1595 0.0136  0.0048  0.0270  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1281 0.1617 0.1732 0.0122  0.0032  0.0312  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1220 0.1614 0.1585 0.0060  -0.0003 0.0290  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1285 0.1605 0.1575 0.0051  -0.0005 0.0212  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1352 0.1578 0.1810 0.0148  0.0052  0.0266  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1234 0.1762 0.1612 0.0009  -0.0023 0.0358  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1286 0.1867 0.1572 -0.0073 -0.0037 0.0323  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1343 0.1876 0.1612 -0.0083 -0.0035 0.0282  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1488 0.2016 0.1823 -0.0052 -0.0038 0.0323  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1538 0.2301 0.1838 -0.0147 -0.0062 0.0419  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2123 0.2950 0.2310 -0.0259 -0.0063 0.0376  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.1979 0.2740 0.2084 -0.0284 -0.0038 0.0288  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.2743 0.3679 0.2925 -0.0328 -0.0080 0.0426  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1271 0.1766 0.1461 -0.0128 -0.0020 0.0202  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1277 0.1744 0.1456 -0.0152 -0.0010 0.0161  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1349 0.1888 0.1454 -0.0260 0.0012  0.0130  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1364 0.1884 0.1456 -0.0292 0.0033  0.0088  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1318 0.1651 0.1507 -0.0097 0.0006  0.0088  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1420 0.1686 0.1657 -0.0018 -0.0009 0.0107  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1510 0.1790 0.1664 -0.0109 0.0033  0.0028  137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1426 0.2052 0.1477 -0.0330 0.0013  0.0146  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1509 0.2191 0.1466 -0.0456 0.0050  0.0093  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1696 0.2502 0.1626 -0.0546 0.0036  0.0136  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1794 0.2619 0.1641 -0.0657 0.0083  0.0067  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1572 0.2328 0.1465 -0.0526 0.0053  0.0101  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1485 0.2108 0.1387 -0.0458 0.0080  0.0041  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1735 0.2440 0.1573 -0.0532 0.0082  0.0053  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1616 0.2441 0.1508 -0.0497 0.0019  0.0172  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.1900 0.2820 0.1772 -0.0535 0.0002  0.0216  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.1948 0.2867 0.1720 -0.0631 0.0041  0.0149  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.1945 0.2961 0.1908 -0.0483 -0.0045 0.0330  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1578 0.2469 0.1582 -0.0508 -0.0019 0.0251  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1675 0.2693 0.1663 -0.0593 -0.0039 0.0310  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1658 0.2579 0.1671 -0.0556 -0.0019 0.0259  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1849 0.2861 0.1837 -0.0634 -0.0027 0.0290  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1837 0.2997 0.1927 -0.0567 -0.0102 0.0476  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2297 0.3341 0.2521 -0.0414 -0.0108 0.0510  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2139 0.3035 0.2375 -0.0326 -0.0085 0.0436  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2629 0.3728 0.2947 -0.0390 -0.0132 0.0611  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1506 0.2260 0.1569 -0.0446 0.0002  0.0191  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1472 0.2145 0.1573 -0.0406 0.0016  0.0153  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1570 0.2195 0.1611 -0.0474 0.0080  0.0040  140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1581 0.2083 0.1654 -0.0418 0.0117  -0.0035 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1447 0.1990 0.1626 -0.0276 0.0006  0.0143  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1616 0.2178 0.1866 -0.0208 -0.0030 0.0237  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.1751 0.2179 0.2044 -0.0111 -0.0025 0.0201  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.1936 0.2576 0.2242 -0.0220 -0.0053 0.0329  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1583 0.2313 0.1546 -0.0604 0.0100  0.0033  141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1650 0.2333 0.1554 -0.0690 0.0187  -0.0087 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1646 0.2222 0.1619 -0.0635 0.0227  -0.0150 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.1915 0.2397 0.1908 -0.0644 0.0310  -0.0249 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.1891 0.2725 0.1670 -0.0873 0.0206  -0.0087 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2129 0.3115 0.1844 -0.0946 0.0153  0.0002  141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2473 0.3616 0.2042 -0.1158 0.0181  -0.0014 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2337 0.3255 0.2045 -0.0912 0.0174  -0.0039 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1511 0.2096 0.1543 -0.0571 0.0173  -0.0086 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1617 0.2123 0.1718 -0.0522 0.0199  -0.0130 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1669 0.2048 0.1860 -0.0412 0.0214  -0.0168 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.1786 0.2108 0.2049 -0.0383 0.0248  -0.0210 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1658 0.2208 0.1792 -0.0491 0.0138  -0.0048 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1558 0.2100 0.1738 -0.0400 0.0072  0.0039  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1615 0.2254 0.1788 -0.0418 0.0026  0.0139  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1588 0.2024 0.1840 -0.0286 0.0053  0.0037  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1743 0.2323 0.1988 -0.0314 -0.0005 0.0188  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1610 0.2067 0.1888 -0.0242 0.0011  0.0120  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1685 0.2027 0.1989 -0.0228 0.0071  -0.0019 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1787 0.2154 0.2117 -0.0152 -0.0004 0.0126  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.1881 0.2157 0.2228 -0.0146 0.0039  0.0002  142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.1829 0.2112 0.2178 -0.0115 0.0008  0.0063  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1528 0.1876 0.1727 -0.0354 0.0185  -0.0143 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.1738 0.1984 0.2018 -0.0267 0.0197  -0.0169 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.1953 0.2143 0.2276 -0.0298 0.0289  -0.0249 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2166 0.2288 0.2597 -0.0230 0.0306  -0.0258 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1717 0.1948 0.1980 -0.0221 0.0160  -0.0135 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1616 0.1867 0.1880 -0.0166 0.0089  -0.0062 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.1772 0.2019 0.2012 -0.0140 0.0069  -0.0037 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1772 0.1963 0.2104 -0.0095 0.0066  -0.0057 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2253 0.2475 0.2501 -0.0409 0.0357  -0.0307 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.2589 0.2738 0.2882 -0.0452 0.0475  -0.0399 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3098 0.3232 0.3457 -0.0478 0.0543  -0.0449 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3341 0.3406 0.3762 -0.0514 0.0661  -0.0530 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.2697 0.2881 0.2862 -0.0587 0.0537  -0.0458 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3042 0.3247 0.3144 -0.0580 0.0490  -0.0420 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3346 0.3508 0.3516 -0.0465 0.0430  -0.0366 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.3869 0.4142 0.3848 -0.0700 0.0511  -0.0444 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3172 0.3365 0.3521 -0.0470 0.0484  -0.0408 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.3520 0.3712 0.3921 -0.0504 0.0545  -0.0454 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.3682 0.3863 0.4196 -0.0398 0.0483  -0.0397 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.3679 0.3872 0.4185 -0.0327 0.0386  -0.0323 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.3997 0.4292 0.4257 -0.0630 0.0538  -0.0459 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5059 0.5433 0.5165 -0.0740 0.0528  -0.0455 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6212 0.6725 0.6216 -0.0802 0.0439  -0.0370 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6422 0.6951 0.6474 -0.0743 0.0379  -0.0310 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.6626 0.7237 0.6508 -0.0914 0.0430  -0.0354 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.3900 0.4066 0.4511 -0.0401 0.0544  -0.0433 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.4198 0.4370 0.4917 -0.0321 0.0493  -0.0383 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.4389 0.4625 0.5011 -0.0331 0.0398  -0.0329 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.4454 0.4689 0.5117 -0.0259 0.0323  -0.0270 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.4634 0.4790 0.5479 -0.0340 0.0595  -0.0439 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.5769 0.5937 0.6765 -0.0253 0.0553  -0.0382 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.6993 0.7156 0.8145 -0.0263 0.0656  -0.0424 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.7330 0.7453 0.8493 -0.0331 0.0784  -0.0512 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.7242 0.7441 0.8507 -0.0209 0.0615  -0.0372 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2079 0.2373 0.2317 0.0069  -0.0135 0.0446  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.1951 0.2260 0.2279 0.0051  -0.0142 0.0446  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.1942 0.2217 0.2257 0.0036  -0.0142 0.0402  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2218 0.2463 0.2454 0.0036  -0.0147 0.0373  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2376 0.2714 0.2717 0.0045  -0.0187 0.0470  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3094 0.3414 0.3352 0.0036  -0.0227 0.0441  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.1922 0.2199 0.2312 0.0026  -0.0131 0.0401  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.1842 0.2087 0.2224 0.0015  -0.0124 0.0370  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1667 0.1905 0.2114 0.0018  -0.0089 0.0369  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1662 0.1911 0.2147 0.0030  -0.0067 0.0378  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1560 0.1775 0.2020 0.0011  -0.0081 0.0357  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1550 0.1751 0.2055 0.0018  -0.0043 0.0355  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1427 0.1583 0.1883 0.0022  -0.0026 0.0331  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1641 0.1781 0.2054 0.0013  -0.0044 0.0320  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1768 0.1996 0.2373 0.0008  -0.0040 0.0386  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1408 0.1540 0.1868 0.0038  0.0010  0.0323  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1497 0.1583 0.1913 0.0049  0.0036  0.0310  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1461 0.1546 0.1954 0.0046  0.0067  0.0334  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1536 0.1639 0.2088 0.0050  0.0083  0.0346  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1450 0.1507 0.1803 0.0077  0.0054  0.0283  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1659 0.1727 0.1968 0.0081  0.0026  0.0261  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1717 0.1724 0.2007 0.0093  0.0079  0.0275  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1761 0.1811 0.2037 0.0106  0.0034  0.0231  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1474 0.1535 0.1976 0.0039  0.0081  0.0343  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1524 0.1581 0.2111 0.0037  0.0118  0.0370  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1663 0.1662 0.2192 0.0063  0.0169  0.0367  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.1870 0.1841 0.2369 0.0060  0.0172  0.0366  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1622 0.1706 0.2300 0.0006  0.0091  0.0389  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1620 0.1762 0.2350 -0.0013 0.0041  0.0398  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1593 0.1771 0.2420 -0.0014 0.0049  0.0425  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1745 0.1902 0.2419 -0.0023 -0.0011 0.0381  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1776 0.2005 0.2641 -0.0025 0.0004  0.0438  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.1991 0.2196 0.2693 -0.0032 -0.0053 0.0393  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.1883 0.2125 0.2680 -0.0033 -0.0047 0.0423  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2116 0.2404 0.2935 -0.0036 -0.0087 0.0441  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1745 0.1720 0.2244 0.0091  0.0210  0.0364  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.1930 0.1846 0.2352 0.0125  0.0261  0.0362  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.1991 0.1893 0.2473 0.0140  0.0321  0.0387  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1819 0.1743 0.2342 0.0142  0.0324  0.0384  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2102 0.1994 0.2399 0.0155  0.0247  0.0324  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2118 0.2037 0.2434 0.0158  0.0231  0.0304  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2293 0.2122 0.2496 0.0196  0.0296  0.0325  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2119 0.1984 0.2619 0.0150  0.0376  0.0416  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2089 0.1938 0.2654 0.0166  0.0442  0.0444  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.2084 0.1992 0.2801 0.0135  0.0426  0.0463  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2182 0.2136 0.2982 0.0097  0.0377  0.0471  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.2010 0.1920 0.2754 0.0151  0.0456  0.0464  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.1951 0.1920 0.2839 0.0125  0.0438  0.0483  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1824 0.1825 0.2684 0.0121  0.0389  0.0455  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1811 0.1838 0.2753 0.0119  0.0398  0.0465  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2184 0.2140 0.3170 0.0140  0.0513  0.0516  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.2970 0.2919 0.4052 0.0131  0.0552  0.0556  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3281 0.3281 0.4514 0.0098  0.0526  0.0583  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3294 0.3178 0.4288 0.0160  0.0609  0.0560  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1601 0.1602 0.2362 0.0117  0.0339  0.0424  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1533 0.1563 0.2271 0.0113  0.0294  0.0398  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1540 0.1613 0.2285 0.0083  0.0229  0.0399  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1631 0.1691 0.2332 0.0074  0.0211  0.0396  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1779 0.1764 0.2383 0.0144  0.0298  0.0353  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.1916 0.1851 0.2483 0.0180  0.0359  0.0342  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2124 0.2066 0.2767 0.0186  0.0387  0.0346  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2216 0.2091 0.2662 0.0213  0.0389  0.0328  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2525 0.2414 0.3122 0.0222  0.0445  0.0331  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2659 0.2482 0.3048 0.0253  0.0445  0.0315  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.2995 0.2824 0.3457 0.0257  0.0472  0.0313  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3738 0.3510 0.4138 0.0299  0.0530  0.0297  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1415 0.1531 0.2206 0.0072  0.0196  0.0402  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1332 0.1484 0.2108 0.0052  0.0138  0.0401  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1308 0.1459 0.2036 0.0065  0.0129  0.0374  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1393 0.1553 0.2175 0.0073  0.0146  0.0377  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1405 0.1614 0.2294 0.0031  0.0111  0.0440  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1503 0.1750 0.2373 0.0020  0.0057  0.0444  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1474 0.1774 0.2444 0.0004  0.0027  0.0483  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1581 0.1917 0.2559 0.0007  0.0000  0.0501  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.1736 0.2091 0.2656 0.0002  -0.0045 0.0503  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.1960 0.2299 0.2805 -0.0008 -0.0074 0.0480  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.1837 0.2222 0.2768 0.0011  -0.0057 0.0527  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1298 0.1439 0.1940 0.0067  0.0102  0.0349  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1230 0.1371 0.1838 0.0078  0.0091  0.0322  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1278 0.1457 0.1897 0.0063  0.0055  0.0337  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1400 0.1579 0.1969 0.0053  0.0030  0.0338  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1349 0.1448 0.1852 0.0096  0.0090  0.0282  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1561 0.1664 0.2059 0.0107  0.0079  0.0252  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1694 0.1747 0.2158 0.0116  0.0128  0.0272  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1164 0.1371 0.1843 0.0064  0.0055  0.0350  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1156 0.1396 0.1840 0.0056  0.0029  0.0372  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1373 0.1614 0.2058 0.0056  0.0029  0.0372  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1211 0.1457 0.1921 0.0067  0.0038  0.0361  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1294 0.1523 0.2037 0.0077  0.0060  0.0336  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1154 0.1436 0.1916 0.0047  0.0020  0.0420  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1843 0.2122 0.2611 0.0046  0.0023  0.0420  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1296 0.1582 0.2041 0.0032  -0.0004 0.0430  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.1901 0.2215 0.2666 0.0044  -0.0005 0.0450  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0697 0.0988 0.1562 0.0053  0.0051  0.0436  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2261 0.2538 0.3034 0.0034  0.0015  0.0427  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1157 0.1423 0.1853 0.0066  0.0024  0.0378  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1099 0.1373 0.1847 0.0076  0.0039  0.0377  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1165 0.1460 0.2021 0.0077  0.0060  0.0410  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1139 0.1460 0.2020 0.0072  0.0053  0.0452  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1234 0.1526 0.1953 0.0078  0.0030  0.0404  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1161 0.1433 0.1783 0.0079  0.0014  0.0375  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1408 0.1675 0.1959 0.0072  -0.0007 0.0378  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1360 0.1618 0.1989 0.0087  0.0023  0.0345  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1152 0.1436 0.2078 0.0084  0.0084  0.0387  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1089 0.1388 0.2126 0.0086  0.0109  0.0415  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1242 0.1578 0.2324 0.0088  0.0110  0.0478  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1213 0.1571 0.2353 0.0088  0.0115  0.0520  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1118 0.1396 0.2223 0.0094  0.0131  0.0374  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1106 0.1390 0.2331 0.0097  0.0162  0.0395  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1149 0.1408 0.2444 0.0103  0.0179  0.0346  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1218 0.1470 0.2625 0.0108  0.0212  0.0350  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1267 0.1542 0.2793 0.0109  0.0237  0.0395  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1355 0.1661 0.2892 0.0108  0.0233  0.0448  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1332 0.1593 0.2961 0.0114  0.0269  0.0389  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1197 0.1541 0.2244 0.0093  0.0105  0.0488  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1252 0.1626 0.2327 0.0101  0.0111  0.0552  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1393 0.1789 0.2399 0.0100  0.0078  0.0589  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1598 0.2021 0.2622 0.0111  0.0079  0.0645  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1392 0.1764 0.2457 0.0112  0.0127  0.0557  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1293 0.1654 0.2232 0.0111  0.0103  0.0539  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1374 0.1709 0.2267 0.0104  0.0092  0.0480  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1417 0.1788 0.2271 0.0120  0.0090  0.0574  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1499 0.1830 0.2290 0.0107  0.0076  0.0482  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1416 0.1766 0.2177 0.0116  0.0075  0.0536  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1239 0.1624 0.2171 0.0087  0.0049  0.0559  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1375 0.1780 0.2256 0.0081  0.0010  0.0584  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1426 0.1841 0.2374 0.0070  0.0005  0.0588  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1524 0.1954 0.2449 0.0062  -0.0031 0.0599  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1440 0.1824 0.2201 0.0074  -0.0018 0.0549  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1525 0.1901 0.2220 0.0087  -0.0011 0.0551  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1633 0.1984 0.2216 0.0081  -0.0034 0.0513  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1639 0.2043 0.2328 0.0105  -0.0013 0.0610  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1404 0.1804 0.2433 0.0071  0.0041  0.0572  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1313 0.1717 0.2407 0.0064  0.0047  0.0577  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1462 0.1912 0.2631 0.0066  0.0032  0.0636  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1533 0.2005 0.2743 0.0079  0.0038  0.0677  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1445 0.1822 0.2604 0.0070  0.0093  0.0549  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1547 0.2009 0.2744 0.0056  0.0013  0.0644  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1534 0.2044 0.2813 0.0058  -0.0011 0.0698  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1417 0.1931 0.2830 0.0063  0.0032  0.0718  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1447 0.1924 0.2880 0.0064  0.0079  0.0685  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1702 0.2227 0.2962 0.0041  -0.0059 0.0694  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1700 0.2199 0.2999 0.0030  -0.0029 0.0667  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.1980 0.2494 0.3105 0.0035  -0.0102 0.0667  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1542 0.2103 0.3052 0.0069  0.0015  0.0775  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1615 0.2184 0.3266 0.0074  0.0057  0.0797  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1277 0.1820 0.2945 0.0061  0.0077  0.0763  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1528 0.2039 0.3245 0.0067  0.0134  0.0746  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1782 0.2411 0.3535 0.0081  0.0023  0.0864  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.1887 0.2525 0.3793 0.0085  0.0063  0.0887  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2250 0.2869 0.4236 0.0099  0.0125  0.0896  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2153 0.2809 0.4143 0.0075  0.0057  0.0896  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2169 0.2801 0.4284 0.0101  0.0150  0.0918  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2127 0.2781 0.4252 0.0086  0.0114  0.0919  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1341 0.1893 0.2966 0.0045  0.0035  0.0752  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1559 0.2083 0.3207 0.0035  0.0064  0.0726  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1423 0.1883 0.2982 0.0041  0.0113  0.0673  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1368 0.1795 0.2961 0.0047  0.0166  0.0659  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1806 0.2346 0.3432 0.0015  0.0012  0.0721  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2540 0.3055 0.4220 0.0007  0.0050  0.0707  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.2841 0.3375 0.4657 0.0009  0.0077  0.0738  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2809 0.3277 0.4387 0.0001  0.0063  0.0665  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1415 0.1855 0.2855 0.0042  0.0097  0.0642  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1402 0.1786 0.2761 0.0051  0.0134  0.0590  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1290 0.1653 0.2714 0.0067  0.0188  0.0584  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1470 0.1789 0.2878 0.0077  0.0231  0.0552  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1354 0.1728 0.2601 0.0050  0.0106  0.0564  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1414 0.1788 0.2569 0.0037  0.0064  0.0551  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1677 0.2032 0.2821 0.0030  0.0069  0.0538  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1491 0.1881 0.2590 0.0036  0.0028  0.0556  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1326 0.1719 0.2826 0.0073  0.0187  0.0616  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1337 0.1709 0.2913 0.0088  0.0237  0.0609  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1268 0.1637 0.2946 0.0093  0.0280  0.0628  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1409 0.1734 0.3104 0.0107  0.0331  0.0597  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1331 0.1735 0.2975 0.0093  0.0231  0.0646  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1360 0.1749 0.2929 0.0094  0.0219  0.0616  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1491 0.1903 0.2996 0.0090  0.0180  0.0634  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1152 0.1497 0.2711 0.0102  0.0248  0.0563  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1435 0.1823 0.2903 0.0094  0.0188  0.0601  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1309 0.1659 0.2816 0.0100  0.0225  0.0555  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1565 0.1868 0.3162 0.0111  0.0290  0.0520  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1356 0.1676 0.2865 0.0104  0.0240  0.0508  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1678 0.1948 0.3262 0.0117  0.0299  0.0468  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1632 0.1913 0.3180 0.0112  0.0272  0.0463  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1302 0.1712 0.3042 0.0084  0.0258  0.0672  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1413 0.1825 0.3266 0.0089  0.0300  0.0696  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1624 0.1984 0.3417 0.0092  0.0338  0.0659  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1597 0.1944 0.3471 0.0101  0.0390  0.0672  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1505 0.1982 0.3457 0.0078  0.0257  0.0756  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1655 0.1987 0.3309 0.0086  0.0316  0.0618  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1511 0.1791 0.3090 0.0093  0.0351  0.0586  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1537 0.1765 0.2972 0.0106  0.0355  0.0526  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1549 0.1747 0.2876 0.0106  0.0347  0.0500  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1686 0.1989 0.3253 0.0072  0.0312  0.0603  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.1759 0.2111 0.3482 0.0061  0.0309  0.0656  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2052 0.2386 0.3850 0.0070  0.0366  0.0670  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.1808 0.2221 0.3585 0.0046  0.0246  0.0688  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1632 0.1850 0.3074 0.0116  0.0363  0.0505  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1586 0.1765 0.2912 0.0125  0.0353  0.0447  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1858 0.1970 0.3089 0.0149  0.0394  0.0400  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.2020 0.2103 0.3290 0.0167  0.0449  0.0400  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1625 0.1811 0.3019 0.0130  0.0358  0.0439  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1719 0.1876 0.3029 0.0137  0.0340  0.0380  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1702 0.1886 0.2942 0.0121  0.0285  0.0383  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.1905 0.2063 0.3308 0.0142  0.0354  0.0370  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1715 0.1801 0.2816 0.0154  0.0369  0.0360  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.1846 0.1865 0.2832 0.0182  0.0398  0.0311  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.1894 0.1893 0.2830 0.0193  0.0375  0.0251  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2033 0.1985 0.2940 0.0219  0.0404  0.0207  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.1937 0.1939 0.2814 0.0183  0.0386  0.0312  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2195 0.2128 0.2930 0.0219  0.0408  0.0261  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.1956 0.1973 0.2898 0.0173  0.0413  0.0365  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1632 0.1664 0.2562 0.0175  0.0321  0.0246  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1694 0.1711 0.2594 0.0184  0.0296  0.0189  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1678 0.1747 0.2629 0.0159  0.0253  0.0210  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1598 0.1699 0.2534 0.0142  0.0232  0.0250  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.1933 0.1903 0.2680 0.0207  0.0281  0.0139  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.1952 0.1915 0.2663 0.0213  0.0238  0.0081  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2261 0.2193 0.2976 0.0231  0.0236  0.0020  33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.1814 0.1803 0.2493 0.0200  0.0191  0.0078  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2370 0.2310 0.3063 0.0230  0.0185  -0.0021 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2030 0.2005 0.2701 0.0212  0.0160  0.0016  33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.1797 0.1818 0.2457 0.0181  0.0170  0.0119  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.1974 0.1967 0.2623 0.0206  0.0114  -0.0002 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.1999 0.2032 0.2622 0.0177  0.0128  0.0099  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2010 0.2033 0.2638 0.0189  0.0103  0.0044  33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1557 0.1630 0.2565 0.0159  0.0242  0.0183  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1645 0.1761 0.2699 0.0141  0.0211  0.0203  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1612 0.1714 0.2689 0.0147  0.0194  0.0148  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1693 0.1762 0.2802 0.0161  0.0212  0.0103  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1760 0.1921 0.2929 0.0126  0.0224  0.0268  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1821 0.1975 0.3108 0.0133  0.0262  0.0272  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.1961 0.2112 0.3335 0.0134  0.0264  0.0243  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2293 0.2418 0.3739 0.0144  0.0294  0.0218  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.1795 0.1967 0.3178 0.0126  0.0240  0.0248  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1495 0.1621 0.2565 0.0138  0.0163  0.0148  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1508 0.1628 0.2626 0.0141  0.0145  0.0098  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1460 0.1622 0.2639 0.0127  0.0136  0.0138  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1398 0.1573 0.2503 0.0123  0.0114  0.0152  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1713 0.1798 0.2714 0.0158  0.0113  0.0033  35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2092 0.2170 0.3140 0.0163  0.0084  -0.0028 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2161 0.2272 0.3312 0.0149  0.0080  -0.0011 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2721 0.2762 0.3699 0.0183  0.0061  -0.0093 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1418 0.1597 0.2734 0.0121  0.0157  0.0158  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1347 0.1561 0.2729 0.0112  0.0161  0.0202  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1428 0.1643 0.2804 0.0112  0.0160  0.0203  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1391 0.1604 0.2756 0.0114  0.0132  0.0161  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1361 0.1596 0.2697 0.0110  0.0127  0.0196  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1361 0.1586 0.2903 0.0110  0.0196  0.0228  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1658 0.1887 0.3187 0.0110  0.0196  0.0240  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1359 0.1611 0.2968 0.0107  0.0204  0.0265  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.1988 0.2190 0.3605 0.0113  0.0201  0.0179  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1448 0.1635 0.2829 0.0120  0.0112  0.0086  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1523 0.1714 0.2907 0.0122  0.0080  0.0047  37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1397 0.1588 0.2632 0.0126  0.0053  0.0051  37  SER   C C   
1346 O O   . SER   B 31  ? 0.1495 0.1700 0.2739 0.0126  0.0037  0.0046  37  SER   C O   
1347 C CB  . SER   B 31  ? 0.1950 0.2112 0.3368 0.0131  0.0051  -0.0040 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2627 0.2756 0.3904 0.0147  0.0025  -0.0086 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1332 0.1507 0.2445 0.0130  0.0053  0.0063  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1349 0.1521 0.2329 0.0134  0.0032  0.0070  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1257 0.1453 0.2206 0.0122  0.0049  0.0140  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1242 0.1435 0.2093 0.0122  0.0035  0.0149  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1682 0.1816 0.2548 0.0148  0.0025  0.0040  38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1745 0.1849 0.2599 0.0167  -0.0001 -0.0035 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1584 0.1645 0.2311 0.0188  0.0000  -0.0059 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1570 0.1624 0.2174 0.0195  -0.0014 -0.0043 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.1605 0.1621 0.2086 0.0220  -0.0026 -0.0073 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.1841 0.1821 0.2289 0.0244  -0.0029 -0.0122 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1710 0.1721 0.2099 0.0226  -0.0036 -0.0055 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1157 0.1375 0.2187 0.0113  0.0077  0.0189  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1172 0.1411 0.2168 0.0105  0.0085  0.0251  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1106 0.1330 0.2004 0.0103  0.0076  0.0254  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1200 0.1435 0.2033 0.0097  0.0065  0.0283  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1164 0.1421 0.2131 0.0104  0.0079  0.0277  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1322 0.1601 0.2252 0.0099  0.0083  0.0339  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1368 0.1663 0.2356 0.0098  0.0099  0.0378  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1273 0.1552 0.2119 0.0099  0.0070  0.0348  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1099 0.1298 0.1993 0.0109  0.0084  0.0226  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1167 0.1351 0.1984 0.0109  0.0085  0.0234  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1195 0.1380 0.2075 0.0108  0.0113  0.0257  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1295 0.1473 0.2252 0.0114  0.0133  0.0240  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1340 0.1483 0.2065 0.0124  0.0075  0.0181  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1359 0.1496 0.2001 0.0128  0.0047  0.0162  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1649 0.1743 0.2199 0.0150  0.0038  0.0115  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1414 0.1564 0.2007 0.0114  0.0040  0.0202  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1123 0.1315 0.1979 0.0101  0.0116  0.0290  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1226 0.1417 0.2141 0.0101  0.0145  0.0312  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1213 0.1389 0.2064 0.0099  0.0146  0.0319  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1296 0.1482 0.2094 0.0088  0.0120  0.0331  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1284 0.1521 0.2299 0.0090  0.0146  0.0370  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1187 0.1431 0.2287 0.0091  0.0174  0.0400  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1491 0.1769 0.2708 0.0091  0.0185  0.0440  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1323 0.1584 0.2407 0.0079  0.0161  0.0433  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1291 0.1437 0.2149 0.0112  0.0181  0.0311  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1304 0.1429 0.2122 0.0113  0.0198  0.0322  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1278 0.1418 0.2200 0.0110  0.0231  0.0362  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1484 0.1616 0.2465 0.0121  0.0262  0.0355  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1458 0.1526 0.2172 0.0139  0.0219  0.0278  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1769 0.1812 0.2451 0.0144  0.0247  0.0298  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1641 0.1699 0.2263 0.0144  0.0180  0.0240  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1253 0.1418 0.2209 0.0093  0.0222  0.0399  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1265 0.1448 0.2333 0.0089  0.0250  0.0440  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1402 0.1558 0.2453 0.0091  0.0278  0.0448  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1539 0.1668 0.2494 0.0092  0.0268  0.0429  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1390 0.1636 0.2546 0.0068  0.0209  0.0484  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1502 0.1765 0.2608 0.0050  0.0162  0.0488  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1478 0.1636 0.2627 0.0095  0.0321  0.0477  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1640 0.1773 0.2800 0.0098  0.0359  0.0493  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.1855 0.2036 0.3105 0.0067  0.0320  0.0530  44  SER   C C   
1400 O O   . SER   B 38  ? 0.1976 0.2213 0.3311 0.0050  0.0277  0.0553  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.1908 0.2013 0.3132 0.0121  0.0433  0.0506  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2325 0.2482 0.3699 0.0108  0.0429  0.0544  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.1905 0.2063 0.3139 0.0063  0.0332  0.0534  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.1976 0.2174 0.3298 0.0033  0.0291  0.0558  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2230 0.2415 0.3665 0.0034  0.0350  0.0590  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2212 0.2340 0.3602 0.0061  0.0423  0.0588  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2101 0.2282 0.3315 0.0021  0.0249  0.0531  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2310 0.2427 0.3441 0.0041  0.0302  0.0518  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2153 0.2344 0.3256 0.0021  0.0199  0.0500  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2432 0.2666 0.4006 0.0007  0.0315  0.0618  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2664 0.2891 0.4372 0.0004  0.0367  0.0651  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2737 0.2920 0.4388 -0.0001 0.0379  0.0638  46  THR   C C   
1413 O O   . THR   B 40  ? 0.3084 0.3217 0.4741 0.0018  0.0458  0.0653  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3190 0.3492 0.5088 -0.0023 0.0320  0.0684  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3719 0.4057 0.5596 -0.0052 0.0226  0.0667  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3096 0.3437 0.5048 -0.0013 0.0315  0.0702  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2438 0.2634 0.4023 -0.0023 0.0305  0.0611  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2495 0.2650 0.4033 -0.0030 0.0311  0.0598  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2374 0.2468 0.3714 -0.0002 0.0335  0.0567  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2395 0.2495 0.3632 0.0009  0.0309  0.0544  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2723 0.2919 0.4291 -0.0066 0.0219  0.0580  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2389 0.2426 0.3682 0.0011  0.0383  0.0569  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2552 0.2533 0.3664 0.0040  0.0400  0.0543  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2459 0.2453 0.3495 0.0018  0.0323  0.0508  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2634 0.2650 0.3749 -0.0014 0.0283  0.0508  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3274 0.3188 0.4365 0.0065  0.0483  0.0565  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4463 0.4346 0.5565 0.0102  0.0570  0.0592  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.6002 0.5812 0.7058 0.0134  0.0654  0.0617  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6437 0.6242 0.7623 0.0121  0.0692  0.0652  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6405 0.6159 0.7281 0.0179  0.0685  0.0601  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2180 0.2160 0.3070 0.0037  0.0304  0.0478  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2179 0.2162 0.2980 0.0025  0.0244  0.0445  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2216 0.2139 0.2917 0.0046  0.0274  0.0437  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2520 0.2396 0.3193 0.0076  0.0340  0.0455  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2081 0.2002 0.2721 0.0035  0.0228  0.0412  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2225 0.2091 0.2787 0.0051  0.0251  0.0407  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2245 0.2097 0.2669 0.0071  0.0225  0.0376  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2601 0.2410 0.2960 0.0085  0.0239  0.0373  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2198 0.2063 0.2842 0.0018  0.0231  0.0408  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.3044 0.2926 0.3880 -0.0005 0.0263  0.0446  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.1896 0.1783 0.2283 0.0072  0.0189  0.0355  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.1935 0.1812 0.2210 0.0089  0.0163  0.0326  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2051 0.1886 0.2240 0.0133  0.0205  0.0325  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2314 0.2140 0.2522 0.0150  0.0245  0.0340  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2000 0.1927 0.2281 0.0079  0.0120  0.0308  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2520 0.2485 0.2849 0.0045  0.0073  0.0306  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2765 0.2713 0.3085 0.0032  0.0059  0.0300  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2118 0.2127 0.2489 0.0033  0.0050  0.0310  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.1925 0.1731 0.2017 0.0156  0.0196  0.0308  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2018 0.1785 0.2008 0.0202  0.0219  0.0300  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.1914 0.1707 0.1857 0.0211  0.0174  0.0263  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2038 0.1854 0.1981 0.0194  0.0133  0.0247  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2403 0.2121 0.2323 0.0225  0.0238  0.0311  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2680 0.2370 0.2660 0.0218  0.0288  0.0349  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2670 0.2349 0.2465 0.0280  0.0251  0.0301  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.2008 0.1797 0.1917 0.0236  0.0180  0.0247  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1963 0.1775 0.1844 0.0245  0.0138  0.0208  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1895 0.1672 0.1666 0.0284  0.0124  0.0190  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2072 0.1802 0.1764 0.0321  0.0156  0.0200  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.2052 0.1869 0.1945 0.0258  0.0147  0.0191  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2079 0.1925 0.2081 0.0227  0.0168  0.0216  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2201 0.2042 0.2088 0.0264  0.0100  0.0148  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2286 0.2186 0.2370 0.0186  0.0130  0.0221  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1723 0.1523 0.1490 0.0280  0.0080  0.0166  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1748 0.1524 0.1426 0.0317  0.0058  0.0147  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1717 0.1481 0.1337 0.0355  0.0046  0.0115  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1790 0.1581 0.1464 0.0343  0.0034  0.0092  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1739 0.1551 0.1451 0.0301  0.0014  0.0128  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1855 0.1574 0.1362 0.0403  0.0049  0.0112  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1892 0.1593 0.1320 0.0446  0.0028  0.0075  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.1922 0.1619 0.1285 0.0478  -0.0019 0.0056  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2232 0.1887 0.1500 0.0514  -0.0003 0.0080  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.2076 0.1721 0.1414 0.0483  0.0083  0.0095  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.2039 0.1692 0.1464 0.0449  0.0134  0.0120  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2219 0.1910 0.1726 0.0426  0.0112  0.0083  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2142 0.1838 0.1729 0.0400  0.0163  0.0114  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.2118 0.1854 0.1811 0.0367  0.0155  0.0103  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.2011 0.1781 0.1742 0.0357  0.0104  0.0061  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2297 0.2041 0.2071 0.0344  0.0199  0.0136  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.1830 0.1572 0.1258 0.0463  -0.0075 0.0018  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.1896 0.1650 0.1307 0.0482  -0.0123 0.0003  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.1849 0.1655 0.1359 0.0463  -0.0177 -0.0042 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.1888 0.1720 0.1479 0.0434  -0.0173 -0.0058 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.1780 0.1535 0.1221 0.0458  -0.0099 0.0045  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.1792 0.1600 0.1379 0.0391  -0.0093 0.0051  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.2010 0.1832 0.1523 0.0481  -0.0225 -0.0060 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2068 0.1943 0.1696 0.0463  -0.0272 -0.0096 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.1940 0.1838 0.1631 0.0441  -0.0267 -0.0070 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2080 0.2012 0.1843 0.0444  -0.0307 -0.0093 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2425 0.2304 0.2028 0.0503  -0.0339 -0.0150 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.3039 0.2898 0.2551 0.0549  -0.0369 -0.0144 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.2813 0.2650 0.2277 0.0552  -0.0332 -0.0096 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3635 0.3506 0.3136 0.0583  -0.0436 -0.0190 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.1832 0.1712 0.1507 0.0420  -0.0217 -0.0024 58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1719 0.1617 0.1451 0.0399  -0.0209 -0.0004 58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1646 0.1594 0.1501 0.0368  -0.0222 -0.0021 58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1674 0.1642 0.1583 0.0347  -0.0217 -0.0031 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1807 0.1680 0.1517 0.0373  -0.0158 0.0037  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.1921 0.1733 0.1513 0.0406  -0.0129 0.0070  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1592 0.1558 0.1494 0.0369  -0.0232 -0.0019 59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1655 0.1662 0.1674 0.0343  -0.0230 -0.0023 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1556 0.1557 0.1579 0.0326  -0.0195 0.0007  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1533 0.1562 0.1639 0.0314  -0.0187 0.0009  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1643 0.1684 0.1745 0.0362  -0.0277 -0.0057 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2219 0.2275 0.2352 0.0370  -0.0314 -0.0099 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2432 0.2528 0.2680 0.0381  -0.0363 -0.0136 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.2635 0.2728 0.2853 0.0415  -0.0418 -0.0171 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2121 0.2253 0.2503 0.0356  -0.0344 -0.0129 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1496 0.1458 0.1433 0.0326  -0.0170 0.0031  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1651 0.1601 0.1586 0.0306  -0.0137 0.0054  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1673 0.1597 0.1557 0.0283  -0.0109 0.0074  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1721 0.1621 0.1551 0.0294  -0.0107 0.0079  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2102 0.2028 0.2008 0.0328  -0.0136 0.0060  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2631 0.2518 0.2455 0.0349  -0.0135 0.0070  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2029 0.1984 0.1998 0.0353  -0.0167 0.0042  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1450 0.1379 0.1352 0.0255  -0.0087 0.0086  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1456 0.1366 0.1327 0.0231  -0.0069 0.0102  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1327 0.1243 0.1210 0.0206  -0.0055 0.0109  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1479 0.1397 0.1372 0.0212  -0.0050 0.0104  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1318 0.1232 0.1194 0.0181  -0.0048 0.0121  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1297 0.1212 0.1167 0.0160  -0.0042 0.0125  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1259 0.1206 0.1161 0.0140  -0.0047 0.0138  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1396 0.1345 0.1311 0.0134  -0.0049 0.0145  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1403 0.1276 0.1231 0.0149  -0.0036 0.0124  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1601 0.1473 0.1413 0.0127  -0.0040 0.0121  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1575 0.1411 0.1373 0.0170  -0.0027 0.0115  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1296 0.1267 0.1211 0.0133  -0.0044 0.0145  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1154 0.1156 0.1101 0.0117  -0.0049 0.0163  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1304 0.1303 0.1213 0.0103  -0.0055 0.0170  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1416 0.1396 0.1279 0.0110  -0.0048 0.0161  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1282 0.1322 0.1293 0.0126  -0.0042 0.0171  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1288 0.1340 0.1303 0.0133  -0.0026 0.0182  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1388 0.1429 0.1399 0.0149  -0.0014 0.0171  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1322 0.1398 0.1349 0.0126  -0.0021 0.0208  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1433 0.1483 0.1452 0.0159  0.0011  0.0185  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1418 0.1502 0.1444 0.0138  0.0002  0.0224  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1402 0.1472 0.1425 0.0154  0.0021  0.0213  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.1753 0.1827 0.1778 0.0170  0.0054  0.0232  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1255 0.1274 0.1183 0.0087  -0.0067 0.0186  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1308 0.1330 0.1199 0.0076  -0.0083 0.0192  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1369 0.1423 0.1270 0.0086  -0.0074 0.0217  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1383 0.1469 0.1347 0.0086  -0.0069 0.0238  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1489 0.1518 0.1405 0.0054  -0.0107 0.0198  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1629 0.1660 0.1499 0.0046  -0.0135 0.0197  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1732 0.1726 0.1530 0.0047  -0.0143 0.0170  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1698 0.1766 0.1596 0.0039  -0.0155 0.0222  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.1800 0.1793 0.1543 0.0042  -0.0174 0.0163  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1737 0.1807 0.1582 0.0036  -0.0189 0.0220  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.1806 0.1837 0.1569 0.0038  -0.0200 0.0187  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2204 0.2233 0.1898 0.0038  -0.0238 0.0177  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1351 0.1392 0.1186 0.0096  -0.0070 0.0216  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1457 0.1520 0.1282 0.0112  -0.0054 0.0245  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1574 0.1636 0.1328 0.0108  -0.0083 0.0252  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.1685 0.1715 0.1350 0.0114  -0.0091 0.0231  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1422 0.1466 0.1220 0.0134  -0.0019 0.0240  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.1764 0.1826 0.1545 0.0159  0.0016  0.0282  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.1682 0.1779 0.1476 0.0100  -0.0103 0.0279  66  SER   C N   
1558 C CA  A SER   B 60  ? 0.1891 0.1993 0.1626 0.0097  -0.0142 0.0284  66  SER   C CA  
1559 C CA  B SER   B 60  ? 0.1780 0.1883 0.1516 0.0098  -0.0142 0.0284  66  SER   C CA  
1560 C C   . SER   B 60  ? 0.1893 0.1983 0.1527 0.0125  -0.0130 0.0298  66  SER   C C   
1561 O O   . SER   B 60  ? 0.2144 0.2214 0.1685 0.0127  -0.0163 0.0278  66  SER   C O   
1562 C CB  A SER   B 60  ? 0.2213 0.2358 0.2021 0.0086  -0.0165 0.0314  66  SER   C CB  
1563 C CB  B SER   B 60  ? 0.1767 0.1914 0.1577 0.0089  -0.0161 0.0318  66  SER   C CB  
1564 O OG  A SER   B 60  ? 0.2550 0.2724 0.2412 0.0102  -0.0131 0.0355  66  SER   C OG  
1565 O OG  B SER   B 60  ? 0.1607 0.1761 0.1361 0.0087  -0.0209 0.0320  66  SER   C OG  
1566 N N   . SER   B 61  ? 0.1746 0.1845 0.1398 0.0148  -0.0081 0.0329  67  SER   C N   
1567 C CA  . SER   B 61  ? 0.1872 0.1956 0.1427 0.0181  -0.0056 0.0351  67  SER   C CA  
1568 C C   . SER   B 61  ? 0.2094 0.2128 0.1553 0.0192  -0.0041 0.0314  67  SER   C C   
1569 O O   . SER   B 61  ? 0.2416 0.2429 0.1769 0.0222  -0.0023 0.0325  67  SER   C O   
1570 C CB  . SER   B 61  ? 0.2024 0.2131 0.1649 0.0201  -0.0001 0.0398  67  SER   C CB  
1571 O OG  . SER   B 61  ? 0.2044 0.2143 0.1741 0.0199  0.0037  0.0382  67  SER   C OG  
1572 N N   . ARG   B 62  ? 0.1883 0.1895 0.1366 0.0173  -0.0048 0.0271  68  ARG   C N   
1573 C CA  . ARG   B 62  ? 0.1994 0.1954 0.1389 0.0182  -0.0038 0.0232  68  ARG   C CA  
1574 C C   . ARG   B 62  ? 0.2114 0.2049 0.1479 0.0156  -0.0090 0.0184  68  ARG   C C   
1575 O O   . ARG   B 62  ? 0.2308 0.2197 0.1615 0.0158  -0.0086 0.0146  68  ARG   C O   
1576 C CB  . ARG   B 62  ? 0.1997 0.1947 0.1456 0.0188  0.0008  0.0225  68  ARG   C CB  
1577 C CG  . ARG   B 62  ? 0.2602 0.2574 0.2113 0.0212  0.0063  0.0268  68  ARG   C CG  
1578 C CD  . ARG   B 62  ? 0.2491 0.2432 0.1896 0.0245  0.0100  0.0278  68  ARG   C CD  
1579 N NE  . ARG   B 62  ? 0.2751 0.2710 0.2212 0.0272  0.0163  0.0325  68  ARG   C NE  
1580 C CZ  . ARG   B 62  ? 0.2921 0.2907 0.2397 0.0286  0.0180  0.0375  68  ARG   C CZ  
1581 N NH1 . ARG   B 62  ? 0.3165 0.3164 0.2584 0.0281  0.0136  0.0386  68  ARG   C NH1 
1582 N NH2 . ARG   B 62  ? 0.3335 0.3331 0.2872 0.0311  0.0245  0.0416  68  ARG   C NH2 
1583 N N   . ARG   B 63  ? 0.2107 0.2072 0.1537 0.0129  -0.0133 0.0187  69  ARG   C N   
1584 C CA  . ARG   B 63  ? 0.2277 0.2223 0.1719 0.0100  -0.0177 0.0147  69  ARG   C CA  
1585 C C   . ARG   B 63  ? 0.2379 0.2288 0.1843 0.0095  -0.0151 0.0117  69  ARG   C C   
1586 O O   . ARG   B 63  ? 0.2712 0.2577 0.2132 0.0087  -0.0166 0.0077  69  ARG   C O   
1587 C CB  . ARG   B 63  ? 0.2517 0.2437 0.1854 0.0101  -0.0223 0.0116  69  ARG   C CB  
1588 C CG  . ARG   B 63  ? 0.2927 0.2885 0.2238 0.0108  -0.0261 0.0143  69  ARG   C CG  
1589 C CD  . ARG   B 63  ? 0.3433 0.3433 0.2855 0.0080  -0.0299 0.0156  69  ARG   C CD  
1590 N NE  . ARG   B 63  ? 0.3762 0.3791 0.3151 0.0083  -0.0355 0.0169  69  ARG   C NE  
1591 C CZ  . ARG   B 63  ? 0.3728 0.3801 0.3137 0.0099  -0.0352 0.0221  69  ARG   C CZ  
1592 N NH1 . ARG   B 63  ? 0.3435 0.3527 0.2897 0.0111  -0.0294 0.0262  69  ARG   C NH1 
1593 N NH2 . ARG   B 63  ? 0.3790 0.3890 0.3169 0.0104  -0.0410 0.0231  69  ARG   C NH2 
1594 N N   . LYS   B 64  ? 0.1975 0.1899 0.1507 0.0102  -0.0113 0.0137  70  LYS   C N   
1595 C CA  . LYS   B 64  ? 0.2055 0.1946 0.1601 0.0104  -0.0088 0.0115  70  LYS   C CA  
1596 C C   . LYS   B 64  ? 0.1807 0.1722 0.1448 0.0099  -0.0078 0.0130  70  LYS   C C   
1597 O O   . LYS   B 64  ? 0.1885 0.1840 0.1578 0.0102  -0.0071 0.0158  70  LYS   C O   
1598 C CB  . LYS   B 64  ? 0.2642 0.2514 0.2142 0.0133  -0.0046 0.0117  70  LYS   C CB  
1599 C CG  . LYS   B 64  ? 0.4024 0.3847 0.3415 0.0142  -0.0048 0.0085  70  LYS   C CG  
1600 C CD  . LYS   B 64  ? 0.5211 0.5006 0.4568 0.0171  0.0002  0.0083  70  LYS   C CD  
1601 C CE  . LYS   B 64  ? 0.5985 0.5730 0.5220 0.0184  0.0004  0.0053  70  LYS   C CE  
1602 N NZ  . LYS   B 64  ? 0.6507 0.6266 0.5664 0.0194  -0.0015 0.0068  70  LYS   C NZ  
1603 N N   . HIS   B 65  ? 0.1694 0.1579 0.1350 0.0094  -0.0074 0.0110  71  HIS   C N   
1604 C CA  . HIS   B 65  ? 0.1692 0.1589 0.1413 0.0098  -0.0061 0.0119  71  HIS   C CA  
1605 C C   . HIS   B 65  ? 0.1934 0.1817 0.1650 0.0122  -0.0033 0.0114  71  HIS   C C   
1606 O O   . HIS   B 65  ? 0.2380 0.2224 0.2053 0.0129  -0.0023 0.0094  71  HIS   C O   
1607 C CB  . HIS   B 65  ? 0.1826 0.1697 0.1566 0.0084  -0.0071 0.0108  71  HIS   C CB  
1608 C CG  . HIS   B 65  ? 0.1633 0.1520 0.1404 0.0060  -0.0096 0.0116  71  HIS   C CG  
1609 N ND1 . HIS   B 65  ? 0.1958 0.1872 0.1790 0.0054  -0.0095 0.0136  71  HIS   C ND1 
1610 C CD2 . HIS   B 65  ? 0.1624 0.1505 0.1377 0.0041  -0.0125 0.0104  71  HIS   C CD2 
1611 C CE1 . HIS   B 65  ? 0.1698 0.1622 0.1557 0.0032  -0.0119 0.0140  71  HIS   C CE1 
1612 N NE2 . HIS   B 65  ? 0.2055 0.1961 0.1872 0.0022  -0.0141 0.0119  71  HIS   C NE2 
1613 N N   . TYR   B 66  ? 0.1619 0.1534 0.1390 0.0135  -0.0021 0.0129  72  TYR   C N   
1614 C CA  . TYR   B 66  ? 0.1552 0.1462 0.1339 0.0158  0.0002  0.0124  72  TYR   C CA  
1615 C C   . TYR   B 66  ? 0.1432 0.1346 0.1265 0.0168  -0.0006 0.0119  72  TYR   C C   
1616 O O   . TYR   B 66  ? 0.1440 0.1381 0.1314 0.0163  -0.0018 0.0127  72  TYR   C O   
1617 C CB  . TYR   B 66  ? 0.1572 0.1519 0.1403 0.0169  0.0020  0.0144  72  TYR   C CB  
1618 C CG  . TYR   B 66  ? 0.1653 0.1593 0.1426 0.0172  0.0037  0.0155  72  TYR   C CG  
1619 C CD1 . TYR   B 66  ? 0.2037 0.1946 0.1761 0.0189  0.0064  0.0146  72  TYR   C CD1 
1620 C CD2 . TYR   B 66  ? 0.1809 0.1774 0.1576 0.0164  0.0029  0.0176  72  TYR   C CD2 
1621 C CE1 . TYR   B 66  ? 0.2135 0.2032 0.1790 0.0199  0.0083  0.0156  72  TYR   C CE1 
1622 C CE2 . TYR   B 66  ? 0.1996 0.1953 0.1696 0.0174  0.0043  0.0190  72  TYR   C CE2 
1623 C CZ  . TYR   B 66  ? 0.2049 0.1971 0.1688 0.0192  0.0071  0.0178  72  TYR   C CZ  
1624 O OH  . TYR   B 66  ? 0.2374 0.2285 0.1931 0.0208  0.0088  0.0193  72  TYR   C OH  
1625 N N   . PRO   B 67  ? 0.1456 0.1343 0.1279 0.0184  0.0002  0.0107  73  PRO   C N   
1626 C CA  . PRO   B 67  ? 0.1526 0.1419 0.1385 0.0201  -0.0009 0.0104  73  PRO   C CA  
1627 C C   . PRO   B 67  ? 0.1536 0.1471 0.1469 0.0216  -0.0008 0.0106  73  PRO   C C   
1628 O O   . PRO   B 67  ? 0.1816 0.1757 0.1770 0.0224  0.0014  0.0110  73  PRO   C O   
1629 C CB  . PRO   B 67  ? 0.1821 0.1673 0.1650 0.0218  0.0001  0.0095  73  PRO   C CB  
1630 C CG  . PRO   B 67  ? 0.2163 0.1995 0.1959 0.0214  0.0024  0.0090  73  PRO   C CG  
1631 C CD  . PRO   B 67  ? 0.1700 0.1548 0.1476 0.0192  0.0021  0.0095  73  PRO   C CD  
1632 N N   . VAL   B 68  ? 0.1371 0.1331 0.1347 0.0220  -0.0029 0.0103  74  VAL   C N   
1633 C CA  . VAL   B 68  ? 0.1435 0.1435 0.1500 0.0230  -0.0034 0.0100  74  VAL   C CA  
1634 C C   . VAL   B 68  ? 0.1410 0.1418 0.1499 0.0248  -0.0066 0.0082  74  VAL   C C   
1635 O O   . VAL   B 68  ? 0.1429 0.1418 0.1467 0.0251  -0.0081 0.0078  74  VAL   C O   
1636 C CB  . VAL   B 68  ? 0.1656 0.1687 0.1762 0.0212  -0.0029 0.0112  74  VAL   C CB  
1637 C CG1 . VAL   B 68  ? 0.1894 0.1925 0.1984 0.0202  0.0002  0.0134  74  VAL   C CG1 
1638 C CG2 . VAL   B 68  ? 0.1664 0.1690 0.1737 0.0198  -0.0045 0.0113  74  VAL   C CG2 
1639 N N   . SER   B 69  ? 0.1355 0.1394 0.1532 0.0263  -0.0076 0.0071  75  SER   C N   
1640 C CA  . SER   B 69  ? 0.1334 0.1393 0.1558 0.0279  -0.0116 0.0047  75  SER   C CA  
1641 C C   . SER   B 69  ? 0.1246 0.1337 0.1543 0.0263  -0.0118 0.0043  75  SER   C C   
1642 O O   . SER   B 69  ? 0.1318 0.1428 0.1673 0.0249  -0.0088 0.0061  75  SER   C O   
1643 C CB  . SER   B 69  ? 0.1598 0.1677 0.1902 0.0301  -0.0131 0.0034  75  SER   C CB  
1644 O OG  . SER   B 69  ? 0.2391 0.2439 0.2633 0.0318  -0.0126 0.0041  75  SER   C OG  
1645 N N   . PHE   B 70  ? 0.1209 0.1303 0.1499 0.0266  -0.0147 0.0023  76  PHE   C N   
1646 C CA  . PHE   B 70  ? 0.1215 0.1333 0.1575 0.0251  -0.0147 0.0017  76  PHE   C CA  
1647 C C   . PHE   B 70  ? 0.1250 0.1381 0.1657 0.0268  -0.0192 -0.0024 76  PHE   C C   
1648 O O   . PHE   B 70  ? 0.1362 0.1475 0.1704 0.0292  -0.0225 -0.0045 76  PHE   C O   
1649 C CB  . PHE   B 70  ? 0.1295 0.1398 0.1594 0.0231  -0.0125 0.0038  76  PHE   C CB  
1650 C CG  . PHE   B 70  ? 0.1252 0.1320 0.1444 0.0240  -0.0136 0.0033  76  PHE   C CG  
1651 C CD1 . PHE   B 70  ? 0.1377 0.1413 0.1484 0.0240  -0.0122 0.0051  76  PHE   C CD1 
1652 C CD2 . PHE   B 70  ? 0.1391 0.1453 0.1571 0.0250  -0.0156 0.0011  76  PHE   C CD2 
1653 C CE1 . PHE   B 70  ? 0.1345 0.1347 0.1368 0.0250  -0.0124 0.0053  76  PHE   C CE1 
1654 C CE2 . PHE   B 70  ? 0.1431 0.1456 0.1510 0.0263  -0.0155 0.0013  76  PHE   C CE2 
1655 C CZ  . PHE   B 70  ? 0.1463 0.1460 0.1470 0.0263  -0.0138 0.0036  76  PHE   C CZ  
1656 N N   . SER   B 71  ? 0.1223 0.1384 0.1743 0.0257  -0.0194 -0.0036 77  SER   C N   
1657 C CA  . SER   B 71  ? 0.1326 0.1501 0.1911 0.0271  -0.0241 -0.0084 77  SER   C CA  
1658 C C   . SER   B 71  ? 0.1464 0.1615 0.1968 0.0278  -0.0260 -0.0107 77  SER   C C   
1659 O O   . SER   B 71  ? 0.1595 0.1722 0.2013 0.0268  -0.0231 -0.0082 77  SER   C O   
1660 C CB  . SER   B 71  ? 0.1367 0.1580 0.2121 0.0256  -0.0232 -0.0090 77  SER   C CB  
1661 O OG  . SER   B 71  ? 0.1580 0.1796 0.2361 0.0233  -0.0193 -0.0065 77  SER   C OG  
1662 N N   . LYS   B 72  ? 0.1815 0.1970 0.2350 0.0295  -0.0309 -0.0158 78  LYS   C N   
1663 C CA  . LYS   B 72  ? 0.1810 0.1937 0.2263 0.0307  -0.0325 -0.0185 78  LYS   C CA  
1664 C C   . LYS   B 72  ? 0.1689 0.1825 0.2221 0.0281  -0.0296 -0.0183 78  LYS   C C   
1665 O O   . LYS   B 72  ? 0.1842 0.2011 0.2518 0.0263  -0.0288 -0.0183 78  LYS   C O   
1666 C CB  . LYS   B 72  ? 0.2431 0.2558 0.2883 0.0339  -0.0394 -0.0247 78  LYS   C CB  
1667 C CG  . LYS   B 72  ? 0.2892 0.3012 0.3271 0.0370  -0.0426 -0.0246 78  LYS   C CG  
1668 C CD  . LYS   B 72  ? 0.4542 0.4639 0.4828 0.0413  -0.0490 -0.0297 78  LYS   C CD  
1669 C CE  . LYS   B 72  ? 0.5470 0.5541 0.5620 0.0449  -0.0501 -0.0275 78  LYS   C CE  
1670 N NZ  . LYS   B 72  ? 0.6018 0.6058 0.6043 0.0497  -0.0554 -0.0316 78  LYS   C NZ  
1671 N N   . PRO   B 73  ? 0.1649 0.1756 0.2100 0.0281  -0.0276 -0.0179 79  PRO   C N   
1672 C CA  . PRO   B 73  ? 0.1645 0.1760 0.2178 0.0257  -0.0245 -0.0171 79  PRO   C CA  
1673 C C   . PRO   B 73  ? 0.1685 0.1818 0.2347 0.0257  -0.0276 -0.0223 79  PRO   C C   
1674 O O   . PRO   B 73  ? 0.2047 0.2167 0.2681 0.0281  -0.0325 -0.0281 79  PRO   C O   
1675 C CB  . PRO   B 73  ? 0.1955 0.2031 0.2374 0.0266  -0.0227 -0.0169 79  PRO   C CB  
1676 C CG  . PRO   B 73  ? 0.2380 0.2429 0.2659 0.0288  -0.0231 -0.0154 79  PRO   C CG  
1677 C CD  . PRO   B 73  ? 0.1919 0.1983 0.2209 0.0304  -0.0274 -0.0174 79  PRO   C CD  
1678 N N   . SER   B 74  ? 0.1560 0.1724 0.2369 0.0231  -0.0249 -0.0204 80  SER   C N   
1679 C CA  . SER   B 74  ? 0.1660 0.1845 0.2627 0.0228  -0.0276 -0.0252 80  SER   C CA  
1680 C C   . SER   B 74  ? 0.1598 0.1799 0.2694 0.0201  -0.0226 -0.0220 80  SER   C C   
1681 O O   . SER   B 74  ? 0.1515 0.1717 0.2575 0.0188  -0.0178 -0.0160 80  SER   C O   
1682 C CB  . SER   B 74  ? 0.2021 0.2239 0.3082 0.0230  -0.0301 -0.0259 80  SER   C CB  
1683 O OG  . SER   B 74  ? 0.3043 0.3250 0.3988 0.0255  -0.0340 -0.0273 80  SER   C OG  
1684 N N   . LEU   B 75  ? 0.1629 0.1845 0.2884 0.0195  -0.0242 -0.0261 81  LEU   C N   
1685 C CA  . LEU   B 75  ? 0.1707 0.1939 0.3116 0.0173  -0.0195 -0.0233 81  LEU   C CA  
1686 C C   . LEU   B 75  ? 0.1797 0.2065 0.3334 0.0162  -0.0170 -0.0193 81  LEU   C C   
1687 O O   . LEU   B 75  ? 0.2046 0.2333 0.3691 0.0167  -0.0205 -0.0232 81  LEU   C O   
1688 C CB  . LEU   B 75  ? 0.1932 0.2155 0.3456 0.0173  -0.0226 -0.0305 81  LEU   C CB  
1689 C CG  . LEU   B 75  ? 0.2261 0.2493 0.3950 0.0153  -0.0178 -0.0283 81  LEU   C CG  
1690 C CD1 . LEU   B 75  ? 0.2230 0.2441 0.3832 0.0148  -0.0130 -0.0236 81  LEU   C CD1 
1691 C CD2 . LEU   B 75  ? 0.2542 0.2765 0.4369 0.0153  -0.0219 -0.0368 81  LEU   C CD2 
1692 N N   . ILE   B 76  ? 0.1884 0.2161 0.3400 0.0153  -0.0112 -0.0117 82  ILE   C N   
1693 C CA  . ILE   B 76  ? 0.2069 0.2373 0.3665 0.0149  -0.0076 -0.0068 82  ILE   C CA  
1694 C C   . ILE   B 76  ? 0.1888 0.2204 0.3599 0.0137  -0.0012 -0.0011 82  ILE   C C   
1695 O O   . ILE   B 76  ? 0.1700 0.2004 0.3351 0.0131  0.0014  0.0022  82  ILE   C O   
1696 C CB  . ILE   B 76  ? 0.2391 0.2686 0.3814 0.0156  -0.0064 -0.0025 82  ILE   C CB  
1697 C CG1 . ILE   B 76  ? 0.2759 0.3037 0.4054 0.0171  -0.0121 -0.0072 82  ILE   C CG1 
1698 C CG2 . ILE   B 76  ? 0.2625 0.2938 0.4094 0.0156  -0.0017 0.0032  82  ILE   C CG2 
1699 C CD1 . ILE   B 76  ? 0.3045 0.3336 0.4357 0.0184  -0.0143 -0.0084 82  ILE   C CD1 
1700 N N   . PHE   B 77  ? 0.1803 0.2142 0.3684 0.0134  0.0017  0.0007  83  PHE   C N   
1701 C CA  . PHE   B 77  ? 0.1745 0.2094 0.3731 0.0128  0.0086  0.0073  83  PHE   C CA  
1702 C C   . PHE   B 77  ? 0.1993 0.2340 0.3844 0.0136  0.0130  0.0149  83  PHE   C C   
1703 O O   . PHE   B 77  ? 0.2303 0.2654 0.4104 0.0145  0.0130  0.0157  83  PHE   C O   
1704 C CB  . PHE   B 77  ? 0.1720 0.2091 0.3939 0.0125  0.0111  0.0070  83  PHE   C CB  
1705 C CG  . PHE   B 77  ? 0.1865 0.2239 0.4207 0.0121  0.0184  0.0136  83  PHE   C CG  
1706 C CD1 . PHE   B 77  ? 0.2058 0.2422 0.4471 0.0111  0.0186  0.0121  83  PHE   C CD1 
1707 C CD2 . PHE   B 77  ? 0.2135 0.2519 0.4503 0.0132  0.0255  0.0217  83  PHE   C CD2 
1708 C CE1 . PHE   B 77  ? 0.2226 0.2593 0.4747 0.0111  0.0255  0.0188  83  PHE   C CE1 
1709 C CE2 . PHE   B 77  ? 0.2146 0.2530 0.4611 0.0134  0.0325  0.0285  83  PHE   C CE2 
1710 C CZ  . PHE   B 77  ? 0.2140 0.2518 0.4690 0.0123  0.0324  0.0271  83  PHE   C CZ  
1711 N N   . VAL   B 78  ? 0.1598 0.1939 0.3389 0.0134  0.0164  0.0202  84  VAL   C N   
1712 C CA  . VAL   B 78  ? 0.1628 0.1966 0.3283 0.0143  0.0197  0.0268  84  VAL   C CA  
1713 C C   . VAL   B 78  ? 0.1486 0.1834 0.3242 0.0150  0.0267  0.0342  84  VAL   C C   
1714 O O   . VAL   B 78  ? 0.1536 0.1886 0.3388 0.0144  0.0284  0.0355  84  VAL   C O   
1715 C CB  . VAL   B 78  ? 0.1691 0.2014 0.3188 0.0137  0.0171  0.0269  84  VAL   C CB  
1716 C CG1 . VAL   B 78  ? 0.1739 0.2059 0.3096 0.0145  0.0193  0.0328  84  VAL   C CG1 
1717 C CG2 . VAL   B 78  ? 0.1823 0.2131 0.3231 0.0134  0.0109  0.0199  84  VAL   C CG2 
1718 N N   . GLU   B 79  ? 0.1476 0.1826 0.3194 0.0165  0.0311  0.0396  85  GLU   C N   
1719 C CA  . GLU   B 79  ? 0.1500 0.1854 0.3287 0.0180  0.0384  0.0476  85  GLU   C CA  
1720 C C   . GLU   B 79  ? 0.1477 0.1827 0.3155 0.0183  0.0389  0.0525  85  GLU   C C   
1721 O O   . GLU   B 79  ? 0.1457 0.1800 0.2993 0.0175  0.0342  0.0502  85  GLU   C O   
1722 C CB  . GLU   B 79  ? 0.1871 0.2222 0.3617 0.0201  0.0432  0.0521  85  GLU   C CB  
1723 C CG  . GLU   B 79  ? 0.2187 0.2547 0.4083 0.0201  0.0441  0.0488  85  GLU   C CG  
1724 C CD  . GLU   B 79  ? 0.2822 0.3197 0.4967 0.0194  0.0472  0.0490  85  GLU   C CD  
1725 O OE1 . GLU   B 79  ? 0.3219 0.3594 0.5429 0.0202  0.0529  0.0552  85  GLU   C OE1 
1726 O OE2 . GLU   B 79  ? 0.3314 0.3702 0.5596 0.0182  0.0438  0.0426  85  GLU   C OE2 
1727 N N   . ALA   B 80  ? 0.1498 0.1852 0.3255 0.0196  0.0448  0.0594  86  ALA   C N   
1728 C CA  . ALA   B 80  ? 0.1699 0.2054 0.3372 0.0203  0.0453  0.0647  86  ALA   C CA  
1729 C C   . ALA   B 80  ? 0.1798 0.2146 0.3251 0.0214  0.0431  0.0667  86  ALA   C C   
1730 O O   . ALA   B 80  ? 0.2046 0.2385 0.3427 0.0229  0.0448  0.0676  86  ALA   C O   
1731 C CB  . ALA   B 80  ? 0.1906 0.2266 0.3691 0.0225  0.0529  0.0731  86  ALA   C CB  
1732 N N   . SER   B 81  ? 0.1682 0.2032 0.3039 0.0207  0.0391  0.0666  87  SER   C N   
1733 C CA  . SER   B 81  ? 0.1922 0.2267 0.3088 0.0215  0.0365  0.0684  87  SER   C CA  
1734 C C   . SER   B 81  ? 0.1994 0.2350 0.3134 0.0229  0.0375  0.0751  87  SER   C C   
1735 O O   . SER   B 81  ? 0.2015 0.2382 0.3289 0.0232  0.0408  0.0786  87  SER   C O   
1736 C CB  . SER   B 81  ? 0.1770 0.2109 0.2850 0.0191  0.0298  0.0615  87  SER   C CB  
1737 O OG  . SER   B 81  ? 0.1676 0.2025 0.2809 0.0177  0.0277  0.0606  87  SER   C OG  
1738 N N   . GLU   B 82  ? 0.2116 0.2471 0.3093 0.0236  0.0343  0.0767  88  GLU   C N   
1739 C CA  . GLU   B 82  ? 0.2311 0.2683 0.3265 0.0251  0.0341  0.0830  88  GLU   C CA  
1740 C C   . GLU   B 82  ? 0.2265 0.2653 0.3306 0.0229  0.0313  0.0813  88  GLU   C C   
1741 O O   . GLU   B 82  ? 0.2492 0.2896 0.3575 0.0242  0.0325  0.0870  88  GLU   C O   
1742 C CB  . GLU   B 82  ? 0.3067 0.3434 0.3830 0.0267  0.0307  0.0848  88  GLU   C CB  
1743 C CG  . GLU   B 82  ? 0.4116 0.4483 0.4784 0.0242  0.0236  0.0792  88  GLU   C CG  
1744 C CD  . GLU   B 82  ? 0.4858 0.5221 0.5355 0.0259  0.0202  0.0814  88  GLU   C CD  
1745 O OE1 . GLU   B 82  ? 0.4926 0.5273 0.5337 0.0289  0.0233  0.0843  88  GLU   C OE1 
1746 O OE2 . GLU   B 82  ? 0.5110 0.5487 0.5564 0.0245  0.0145  0.0801  88  GLU   C OE2 
1747 N N   . TYR   B 83  ? 0.1829 0.2211 0.2908 0.0201  0.0283  0.0741  89  TYR   C N   
1748 C CA  . TYR   B 83  ? 0.1753 0.2143 0.2895 0.0183  0.0259  0.0721  89  TYR   C CA  
1749 C C   . TYR   B 83  ? 0.1839 0.2221 0.3132 0.0168  0.0277  0.0675  89  TYR   C C   
1750 O O   . TYR   B 83  ? 0.1858 0.2243 0.3212 0.0158  0.0268  0.0664  89  TYR   C O   
1751 C CB  . TYR   B 83  ? 0.1692 0.2079 0.2716 0.0166  0.0201  0.0678  89  TYR   C CB  
1752 C CG  . TYR   B 83  ? 0.1673 0.2039 0.2618 0.0156  0.0181  0.0618  89  TYR   C CG  
1753 C CD1 . TYR   B 83  ? 0.1755 0.2111 0.2577 0.0167  0.0175  0.0627  89  TYR   C CD1 
1754 C CD2 . TYR   B 83  ? 0.1561 0.1912 0.2549 0.0140  0.0170  0.0553  89  TYR   C CD2 
1755 C CE1 . TYR   B 83  ? 0.1729 0.2064 0.2487 0.0160  0.0161  0.0575  89  TYR   C CE1 
1756 C CE2 . TYR   B 83  ? 0.1635 0.1967 0.2555 0.0135  0.0152  0.0504  89  TYR   C CE2 
1757 C CZ  . TYR   B 83  ? 0.1620 0.1945 0.2431 0.0145  0.0149  0.0516  89  TYR   C CZ  
1758 O OH  . TYR   B 83  ? 0.1778 0.2084 0.2531 0.0142  0.0135  0.0471  89  TYR   C OH  
1759 N N   . TYR   B 84  ? 0.1562 0.1934 0.2922 0.0168  0.0300  0.0649  90  TYR   C N   
1760 C CA  . TYR   B 84  ? 0.1513 0.1878 0.3032 0.0157  0.0314  0.0605  90  TYR   C CA  
1761 C C   . TYR   B 84  ? 0.1467 0.1832 0.3107 0.0168  0.0364  0.0628  90  TYR   C C   
1762 O O   . TYR   B 84  ? 0.1495 0.1860 0.3073 0.0180  0.0379  0.0649  90  TYR   C O   
1763 C CB  . TYR   B 84  ? 0.1383 0.1732 0.2869 0.0139  0.0269  0.0514  90  TYR   C CB  
1764 C CG  . TYR   B 84  ? 0.1291 0.1633 0.2700 0.0128  0.0229  0.0482  90  TYR   C CG  
1765 C CD1 . TYR   B 84  ? 0.1318 0.1660 0.2802 0.0124  0.0238  0.0487  90  TYR   C CD1 
1766 C CD2 . TYR   B 84  ? 0.1290 0.1622 0.2560 0.0122  0.0190  0.0448  90  TYR   C CD2 
1767 C CE1 . TYR   B 84  ? 0.1401 0.1734 0.2821 0.0116  0.0210  0.0459  90  TYR   C CE1 
1768 C CE2 . TYR   B 84  ? 0.1256 0.1579 0.2465 0.0114  0.0162  0.0422  90  TYR   C CE2 
1769 C CZ  . TYR   B 84  ? 0.1302 0.1625 0.2585 0.0111  0.0173  0.0429  90  TYR   C CZ  
1770 O OH  . TYR   B 84  ? 0.1334 0.1646 0.2563 0.0105  0.0154  0.0408  90  TYR   C OH  
1771 N N   . PRO   B 85  ? 0.1517 0.1881 0.3337 0.0163  0.0392  0.0617  91  PRO   C N   
1772 C CA  . PRO   B 85  ? 0.1453 0.1817 0.3413 0.0169  0.0437  0.0626  91  PRO   C CA  
1773 C C   . PRO   B 85  ? 0.1480 0.1838 0.3437 0.0156  0.0401  0.0546  91  PRO   C C   
1774 O O   . PRO   B 85  ? 0.1404 0.1754 0.3257 0.0144  0.0342  0.0483  91  PRO   C O   
1775 C CB  . PRO   B 85  ? 0.1537 0.1898 0.3692 0.0162  0.0465  0.0623  91  PRO   C CB  
1776 C CG  . PRO   B 85  ? 0.1587 0.1939 0.3699 0.0145  0.0413  0.0560  91  PRO   C CG  
1777 C CD  . PRO   B 85  ? 0.1562 0.1920 0.3470 0.0149  0.0381  0.0583  91  PRO   C CD  
1778 N N   . ALA   B 86  ? 0.1338 0.1698 0.3422 0.0161  0.0435  0.0547  92  ALA   C N   
1779 C CA  . ALA   B 86  ? 0.1580 0.1940 0.3700 0.0150  0.0397  0.0470  92  ALA   C CA  
1780 C C   . ALA   B 86  ? 0.1699 0.2051 0.3902 0.0131  0.0351  0.0388  92  ALA   C C   
1781 O O   . ALA   B 86  ? 0.1911 0.2260 0.4249 0.0126  0.0375  0.0396  92  ALA   C O   
1782 C CB  . ALA   B 86  ? 0.1588 0.1955 0.3873 0.0158  0.0449  0.0493  92  ALA   C CB  
1783 N N   . ARG   B 87  ? 0.1649 0.1993 0.3750 0.0123  0.0286  0.0315  93  ARG   C N   
1784 C CA  . ARG   B 87  ? 0.1653 0.1983 0.3789 0.0111  0.0240  0.0237  93  ARG   C CA  
1785 C C   . ARG   B 87  ? 0.1576 0.1898 0.3605 0.0111  0.0174  0.0162  93  ARG   C C   
1786 O O   . ARG   B 87  ? 0.1576 0.1903 0.3486 0.0117  0.0164  0.0177  93  ARG   C O   
1787 C CB  . ARG   B 87  ? 0.1738 0.2056 0.3790 0.0110  0.0242  0.0256  93  ARG   C CB  
1788 C CG  . ARG   B 87  ? 0.1654 0.1970 0.3489 0.0114  0.0216  0.0273  93  ARG   C CG  
1789 C CD  . ARG   B 87  ? 0.1658 0.1966 0.3433 0.0112  0.0218  0.0292  93  ARG   C CD  
1790 N NE  . ARG   B 87  ? 0.1608 0.1909 0.3197 0.0112  0.0183  0.0283  93  ARG   C NE  
1791 C CZ  . ARG   B 87  ? 0.1685 0.1972 0.3202 0.0109  0.0164  0.0263  93  ARG   C CZ  
1792 N NH1 . ARG   B 87  ? 0.1669 0.1946 0.3270 0.0107  0.0178  0.0252  93  ARG   C NH1 
1793 N NH2 . ARG   B 87  ? 0.1790 0.2068 0.3155 0.0110  0.0136  0.0255  93  ARG   C NH2 
1794 N N   . TYR   B 88  ? 0.1759 0.2065 0.3814 0.0106  0.0128  0.0082  94  TYR   C N   
1795 C CA  . TYR   B 88  ? 0.1972 0.2266 0.3899 0.0111  0.0064  0.0016  94  TYR   C CA  
1796 C C   . TYR   B 88  ? 0.1750 0.2024 0.3487 0.0115  0.0056  0.0029  94  TYR   C C   
1797 O O   . TYR   B 88  ? 0.1869 0.2132 0.3614 0.0111  0.0075  0.0040  94  TYR   C O   
1798 C CB  . TYR   B 88  ? 0.2247 0.2527 0.4263 0.0110  0.0016  -0.0078 94  TYR   C CB  
1799 C CG  . TYR   B 88  ? 0.2543 0.2844 0.4734 0.0107  0.0004  -0.0106 94  TYR   C CG  
1800 C CD1 . TYR   B 88  ? 0.2730 0.3044 0.4883 0.0115  -0.0035 -0.0130 94  TYR   C CD1 
1801 C CD2 . TYR   B 88  ? 0.2609 0.2920 0.5019 0.0096  0.0041  -0.0098 94  TYR   C CD2 
1802 C CE1 . TYR   B 88  ? 0.2840 0.3179 0.5173 0.0112  -0.0043 -0.0151 94  TYR   C CE1 
1803 C CE2 . TYR   B 88  ? 0.2676 0.3009 0.5270 0.0092  0.0036  -0.0118 94  TYR   C CE2 
1804 C CZ  . TYR   B 88  ? 0.2813 0.3162 0.5371 0.0100  -0.0007 -0.0146 94  TYR   C CZ  
1805 O OH  . TYR   B 88  ? 0.3166 0.3540 0.5930 0.0095  -0.0010 -0.0165 94  TYR   C OH  
1806 N N   . GLN   B 89  ? 0.1523 0.1794 0.3106 0.0122  0.0032  0.0031  95  GLN   C N   
1807 C CA  . GLN   B 89  ? 0.1377 0.1628 0.2792 0.0125  0.0022  0.0037  95  GLN   C CA  
1808 C C   . GLN   B 89  ? 0.1369 0.1598 0.2692 0.0137  -0.0032 -0.0033 95  GLN   C C   
1809 O O   . GLN   B 89  ? 0.1513 0.1750 0.2838 0.0144  -0.0061 -0.0058 95  GLN   C O   
1810 C CB  . GLN   B 89  ? 0.1553 0.1816 0.2869 0.0124  0.0044  0.0104  95  GLN   C CB  
1811 C CG  . GLN   B 89  ? 0.1603 0.1847 0.2767 0.0124  0.0035  0.0114  95  GLN   C CG  
1812 C CD  . GLN   B 89  ? 0.1528 0.1784 0.2622 0.0120  0.0058  0.0181  95  GLN   C CD  
1813 O OE1 . GLN   B 89  ? 0.1605 0.1881 0.2762 0.0117  0.0091  0.0233  95  GLN   C OE1 
1814 N NE2 . GLN   B 89  ? 0.1433 0.1675 0.2394 0.0120  0.0039  0.0179  95  GLN   C NE2 
1815 N N   . SER   B 90  ? 0.1358 0.1560 0.2598 0.0143  -0.0044 -0.0060 96  SER   C N   
1816 C CA  . SER   B 90  ? 0.1415 0.1589 0.2551 0.0162  -0.0090 -0.0122 96  SER   C CA  
1817 C C   . SER   B 90  ? 0.1401 0.1561 0.2367 0.0170  -0.0093 -0.0097 96  SER   C C   
1818 O O   . SER   B 90  ? 0.1349 0.1515 0.2273 0.0159  -0.0061 -0.0039 96  SER   C O   
1819 C CB  . SER   B 90  ? 0.1629 0.1773 0.2773 0.0170  -0.0098 -0.0175 96  SER   C CB  
1820 O OG  . SER   B 90  ? 0.1744 0.1874 0.2827 0.0167  -0.0060 -0.0134 96  SER   C OG  
1821 N N   . HIS   B 91  ? 0.1422 0.1562 0.2292 0.0190  -0.0134 -0.0142 97  HIS   C N   
1822 C CA  . HIS   B 91  ? 0.1444 0.1562 0.2154 0.0202  -0.0137 -0.0124 97  HIS   C CA  
1823 C C   . HIS   B 91  ? 0.1387 0.1528 0.2085 0.0188  -0.0117 -0.0066 97  HIS   C C   
1824 O O   . HIS   B 91  ? 0.1485 0.1614 0.2091 0.0185  -0.0098 -0.0030 97  HIS   C O   
1825 C CB  . HIS   B 91  ? 0.1548 0.1635 0.2174 0.0207  -0.0111 -0.0112 97  HIS   C CB  
1826 C CG  . HIS   B 91  ? 0.1739 0.1794 0.2349 0.0228  -0.0126 -0.0172 97  HIS   C CG  
1827 N ND1 . HIS   B 91  ? 0.2091 0.2109 0.2569 0.0259  -0.0151 -0.0208 97  HIS   C ND1 
1828 C CD2 . HIS   B 91  ? 0.1828 0.1882 0.2538 0.0223  -0.0121 -0.0202 97  HIS   C CD2 
1829 C CE1 . HIS   B 91  ? 0.2242 0.2233 0.2727 0.0275  -0.0160 -0.0261 97  HIS   C CE1 
1830 N NE2 . HIS   B 91  ? 0.2143 0.2155 0.2771 0.0252  -0.0143 -0.0261 97  HIS   C NE2 
1831 N N   . LEU   B 92  ? 0.1245 0.1414 0.2036 0.0181  -0.0120 -0.0061 98  LEU   C N   
1832 C CA  . LEU   B 92  ? 0.1265 0.1451 0.2047 0.0171  -0.0096 -0.0010 98  LEU   C CA  
1833 C C   . LEU   B 92  ? 0.1292 0.1477 0.2033 0.0185  -0.0124 -0.0028 98  LEU   C C   
1834 O O   . LEU   B 92  ? 0.1349 0.1539 0.2140 0.0198  -0.0159 -0.0074 98  LEU   C O   
1835 C CB  . LEU   B 92  ? 0.1332 0.1550 0.2258 0.0157  -0.0066 0.0019  98  LEU   C CB  
1836 C CG  . LEU   B 92  ? 0.1480 0.1712 0.2386 0.0150  -0.0034 0.0076  98  LEU   C CG  
1837 C CD1 . LEU   B 92  ? 0.1590 0.1814 0.2406 0.0141  -0.0015 0.0119  98  LEU   C CD1 
1838 C CD2 . LEU   B 92  ? 0.1703 0.1962 0.2754 0.0145  0.0000  0.0105  98  LEU   C CD2 
1839 N N   . MET   B 93  ? 0.1260 0.1439 0.1916 0.0183  -0.0110 0.0006  99  MET   C N   
1840 C CA  . MET   B 93  ? 0.1147 0.1322 0.1759 0.0197  -0.0129 -0.0003 99  MET   C CA  
1841 C C   . MET   B 93  ? 0.1282 0.1472 0.1923 0.0187  -0.0095 0.0039  99  MET   C C   
1842 O O   . MET   B 93  ? 0.1355 0.1544 0.1960 0.0174  -0.0066 0.0078  99  MET   C O   
1843 C CB  . MET   B 93  ? 0.1404 0.1544 0.1872 0.0207  -0.0137 -0.0001 99  MET   C CB  
1844 C CG  . MET   B 93  ? 0.1714 0.1831 0.2131 0.0223  -0.0161 -0.0037 99  MET   C CG  
1845 S SD  . MET   B 93  ? 0.1834 0.1907 0.2093 0.0236  -0.0154 -0.0022 99  MET   C SD  
1846 C CE  . MET   B 93  ? 0.2004 0.2081 0.2267 0.0203  -0.0108 0.0030  99  MET   C CE  
1847 N N   . LEU   B 94  ? 0.1195 0.1399 0.1893 0.0197  -0.0099 0.0032  100 LEU   C N   
1848 C CA  . LEU   B 94  ? 0.1221 0.1435 0.1940 0.0192  -0.0059 0.0073  100 LEU   C CA  
1849 C C   . LEU   B 94  ? 0.1149 0.1344 0.1783 0.0204  -0.0062 0.0074  100 LEU   C C   
1850 O O   . LEU   B 94  ? 0.1372 0.1560 0.1987 0.0220  -0.0098 0.0042  100 LEU   C O   
1851 C CB  . LEU   B 94  ? 0.1259 0.1505 0.2141 0.0195  -0.0044 0.0072  100 LEU   C CB  
1852 C CG  . LEU   B 94  ? 0.1492 0.1757 0.2495 0.0184  -0.0031 0.0074  100 LEU   C CG  
1853 C CD1 . LEU   B 94  ? 0.1946 0.2239 0.3121 0.0187  -0.0011 0.0078  100 LEU   C CD1 
1854 C CD2 . LEU   B 94  ? 0.1600 0.1861 0.2560 0.0171  0.0008  0.0123  100 LEU   C CD2 
1855 N N   . ALA   B 95  ? 0.1268 0.1455 0.1855 0.0200  -0.0025 0.0110  101 ALA   C N   
1856 C CA  . ALA   B 95  ? 0.1300 0.1468 0.1825 0.0212  -0.0017 0.0114  101 ALA   C CA  
1857 C C   . ALA   B 95  ? 0.1308 0.1483 0.1867 0.0214  0.0033  0.0150  101 ALA   C C   
1858 O O   . ALA   B 95  ? 0.1233 0.1421 0.1825 0.0206  0.0060  0.0178  101 ALA   C O   
1859 C CB  . ALA   B 95  ? 0.1359 0.1492 0.1742 0.0206  -0.0024 0.0118  101 ALA   C CB  
1860 N N   . VAL   B 96  ? 0.1289 0.1452 0.1833 0.0228  0.0049  0.0151  102 VAL   C N   
1861 C CA  . VAL   B 96  ? 0.1451 0.1608 0.1993 0.0236  0.0103  0.0185  102 VAL   C CA  
1862 C C   . VAL   B 96  ? 0.1508 0.1631 0.1898 0.0229  0.0112  0.0200  102 VAL   C C   
1863 O O   . VAL   B 96  ? 0.1690 0.1784 0.1989 0.0228  0.0092  0.0181  102 VAL   C O   
1864 C CB  . VAL   B 96  ? 0.1602 0.1757 0.2194 0.0256  0.0117  0.0177  102 VAL   C CB  
1865 C CG1 . VAL   B 96  ? 0.1902 0.2043 0.2476 0.0268  0.0181  0.0212  102 VAL   C CG1 
1866 C CG2 . VAL   B 96  ? 0.1629 0.1823 0.2388 0.0261  0.0098  0.0158  102 VAL   C CG2 
1867 N N   . GLY   B 97  ? 0.1624 0.1752 0.1994 0.0224  0.0138  0.0232  103 GLY   C N   
1868 C CA  . GLY   B 97  ? 0.1813 0.1914 0.2048 0.0218  0.0137  0.0242  103 GLY   C CA  
1869 C C   . GLY   B 97  ? 0.1705 0.1820 0.1932 0.0215  0.0156  0.0279  103 GLY   C C   
1870 O O   . GLY   B 97  ? 0.2041 0.2185 0.2373 0.0217  0.0174  0.0300  103 GLY   C O   
1871 N N   . HIS   B 98  ? 0.1758 0.1850 0.1863 0.0213  0.0151  0.0288  104 HIS   C N   
1872 C CA  . HIS   B 98  ? 0.1793 0.1897 0.1870 0.0215  0.0164  0.0326  104 HIS   C CA  
1873 C C   . HIS   B 98  ? 0.1661 0.1787 0.1761 0.0194  0.0127  0.0331  104 HIS   C C   
1874 O O   . HIS   B 98  ? 0.1619 0.1737 0.1684 0.0176  0.0087  0.0303  104 HIS   C O   
1875 C CB  . HIS   B 98  ? 0.2303 0.2372 0.2237 0.0227  0.0170  0.0330  104 HIS   C CB  
1876 C CG  . HIS   B 98  ? 0.2559 0.2638 0.2453 0.0239  0.0186  0.0375  104 HIS   C CG  
1877 N ND1 . HIS   B 98  ? 0.2684 0.2775 0.2636 0.0263  0.0243  0.0420  104 HIS   C ND1 
1878 C CD2 . HIS   B 98  ? 0.2797 0.2878 0.2615 0.0232  0.0151  0.0384  104 HIS   C CD2 
1879 C CE1 . HIS   B 98  ? 0.2993 0.3092 0.2889 0.0271  0.0241  0.0457  104 HIS   C CE1 
1880 N NE2 . HIS   B 98  ? 0.3042 0.3137 0.2855 0.0254  0.0184  0.0435  104 HIS   C NE2 
1881 N N   . SER   B 99  ? 0.1680 0.1833 0.1839 0.0198  0.0146  0.0370  105 SER   C N   
1882 C CA  . SER   B 99  ? 0.1723 0.1899 0.1913 0.0181  0.0117  0.0379  105 SER   C CA  
1883 C C   . SER   B 99  ? 0.1901 0.2096 0.2113 0.0195  0.0146  0.0435  105 SER   C C   
1884 O O   . SER   B 99  ? 0.2138 0.2346 0.2447 0.0207  0.0189  0.0459  105 SER   C O   
1885 C CB  . SER   B 99  ? 0.1800 0.1993 0.2109 0.0169  0.0108  0.0354  105 SER   C CB  
1886 O OG  . SER   B 99  ? 0.1889 0.2102 0.2237 0.0156  0.0090  0.0366  105 SER   C OG  
1887 N N   . GLU   B 100 ? 0.1936 0.2133 0.2066 0.0195  0.0124  0.0456  106 GLU   C N   
1888 C CA  . GLU   B 100 ? 0.2078 0.2293 0.2208 0.0211  0.0142  0.0514  106 GLU   C CA  
1889 C C   . GLU   B 100 ? 0.1780 0.2024 0.1989 0.0190  0.0112  0.0517  106 GLU   C C   
1890 O O   . GLU   B 100 ? 0.1729 0.1971 0.1948 0.0167  0.0076  0.0478  106 GLU   C O   
1891 C CB  . GLU   B 100 ? 0.2490 0.2690 0.2466 0.0223  0.0116  0.0525  106 GLU   C CB  
1892 C CG  . GLU   B 100 ? 0.3510 0.3671 0.3360 0.0241  0.0127  0.0507  106 GLU   C CG  
1893 C CD  . GLU   B 100 ? 0.3681 0.3831 0.3490 0.0279  0.0186  0.0554  106 GLU   C CD  
1894 O OE1 . GLU   B 100 ? 0.3773 0.3887 0.3483 0.0296  0.0205  0.0538  106 GLU   C OE1 
1895 O OE2 . GLU   B 100 ? 0.3737 0.3910 0.3622 0.0293  0.0222  0.0607  106 GLU   C OE2 
1896 N N   . PRO   B 101 ? 0.1906 0.2174 0.2170 0.0200  0.0129  0.0569  107 PRO   C N   
1897 C CA  . PRO   B 101 ? 0.1763 0.2057 0.2107 0.0182  0.0104  0.0573  107 PRO   C CA  
1898 C C   . PRO   B 101 ? 0.1794 0.2087 0.2065 0.0164  0.0046  0.0550  107 PRO   C C   
1899 O O   . PRO   B 101 ? 0.1775 0.2075 0.2107 0.0143  0.0028  0.0525  107 PRO   C O   
1900 C CB  . PRO   B 101 ? 0.2053 0.2368 0.2433 0.0204  0.0132  0.0643  107 PRO   C CB  
1901 C CG  . PRO   B 101 ? 0.2509 0.2811 0.2880 0.0230  0.0186  0.0670  107 PRO   C CG  
1902 C CD  . PRO   B 101 ? 0.2182 0.2454 0.2455 0.0232  0.0182  0.0629  107 PRO   C CD  
1903 N N   . GLY   B 102 ? 0.1768 0.2049 0.1914 0.0172  0.0020  0.0552  108 GLY   C N   
1904 C CA  . GLY   B 102 ? 0.1823 0.2106 0.1919 0.0153  -0.0037 0.0529  108 GLY   C CA  
1905 C C   . GLY   B 102 ? 0.1697 0.1956 0.1788 0.0130  -0.0053 0.0470  108 GLY   C C   
1906 O O   . GLY   B 102 ? 0.1806 0.2064 0.1885 0.0110  -0.0093 0.0449  108 GLY   C O   
1907 N N   . ASP   B 103 ? 0.1569 0.1806 0.1669 0.0133  -0.0022 0.0445  109 ASP   C N   
1908 C CA  . ASP   B 103 ? 0.1434 0.1648 0.1526 0.0117  -0.0035 0.0395  109 ASP   C CA  
1909 C C   . ASP   B 103 ? 0.1355 0.1579 0.1542 0.0102  -0.0035 0.0382  109 ASP   C C   
1910 O O   . ASP   B 103 ? 0.1395 0.1599 0.1573 0.0091  -0.0046 0.0347  109 ASP   C O   
1911 C CB  . ASP   B 103 ? 0.1723 0.1912 0.1791 0.0131  -0.0004 0.0376  109 ASP   C CB  
1912 C CG  . ASP   B 103 ? 0.1774 0.1940 0.1727 0.0145  -0.0004 0.0377  109 ASP   C CG  
1913 O OD1 . ASP   B 103 ? 0.1897 0.2052 0.1777 0.0137  -0.0041 0.0365  109 ASP   C OD1 
1914 O OD2 . ASP   B 103 ? 0.2031 0.2188 0.1972 0.0166  0.0035  0.0389  109 ASP   C OD2 
1915 N N   . CYS   B 104 ? 0.1314 0.1565 0.1593 0.0105  -0.0017 0.0410  110 CYS   C N   
1916 C CA  . CYS   B 104 ? 0.1212 0.1468 0.1575 0.0094  -0.0015 0.0395  110 CYS   C CA  
1917 C C   . CYS   B 104 ? 0.1257 0.1508 0.1599 0.0077  -0.0044 0.0382  110 CYS   C C   
1918 O O   . CYS   B 104 ? 0.1494 0.1758 0.1813 0.0071  -0.0068 0.0403  110 CYS   C O   
1919 C CB  . CYS   B 104 ? 0.1266 0.1550 0.1729 0.0099  0.0006  0.0430  110 CYS   C CB  
1920 S SG  . CYS   B 104 ? 0.1517 0.1805 0.2055 0.0115  0.0049  0.0436  110 CYS   C SG  
1921 N N   . GLY   B 105 ? 0.1094 0.1326 0.1450 0.0072  -0.0041 0.0349  111 GLY   C N   
1922 C CA  . GLY   B 105 ? 0.1263 0.1483 0.1612 0.0058  -0.0057 0.0340  111 GLY   C CA  
1923 C C   . GLY   B 105 ? 0.1286 0.1475 0.1557 0.0053  -0.0070 0.0311  111 GLY   C C   
1924 O O   . GLY   B 105 ? 0.1421 0.1593 0.1692 0.0044  -0.0073 0.0301  111 GLY   C O   
1925 N N   . GLY   B 106 ? 0.1322 0.1498 0.1531 0.0062  -0.0071 0.0301  112 GLY   C N   
1926 C CA  . GLY   B 106 ? 0.1427 0.1567 0.1565 0.0060  -0.0079 0.0272  112 GLY   C CA  
1927 C C   . GLY   B 106 ? 0.1302 0.1418 0.1447 0.0067  -0.0066 0.0248  112 GLY   C C   
1928 O O   . GLY   B 106 ? 0.1306 0.1429 0.1486 0.0079  -0.0052 0.0242  112 GLY   C O   
1929 N N   . ILE   B 107 ? 0.1267 0.1353 0.1379 0.0061  -0.0070 0.0234  113 ILE   C N   
1930 C CA  . ILE   B 107 ? 0.1256 0.1316 0.1361 0.0073  -0.0056 0.0217  113 ILE   C CA  
1931 C C   . ILE   B 107 ? 0.1234 0.1273 0.1292 0.0090  -0.0054 0.0195  113 ILE   C C   
1932 O O   . ILE   B 107 ? 0.1296 0.1322 0.1312 0.0088  -0.0060 0.0189  113 ILE   C O   
1933 C CB  . ILE   B 107 ? 0.1572 0.1606 0.1671 0.0063  -0.0053 0.0219  113 ILE   C CB  
1934 C CG1 . ILE   B 107 ? 0.1991 0.2046 0.2159 0.0054  -0.0045 0.0241  113 ILE   C CG1 
1935 C CG2 . ILE   B 107 ? 0.1606 0.1599 0.1662 0.0081  -0.0037 0.0204  113 ILE   C CG2 
1936 C CD1 . ILE   B 107 ? 0.2511 0.2550 0.2708 0.0041  -0.0036 0.0252  113 ILE   C CD1 
1937 N N   . LEU   B 108 ? 0.1203 0.1238 0.1270 0.0109  -0.0048 0.0181  114 LEU   C N   
1938 C CA  . LEU   B 108 ? 0.1176 0.1190 0.1205 0.0130  -0.0050 0.0159  114 LEU   C CA  
1939 C C   . LEU   B 108 ? 0.1225 0.1202 0.1213 0.0141  -0.0043 0.0155  114 LEU   C C   
1940 O O   . LEU   B 108 ? 0.1239 0.1215 0.1240 0.0147  -0.0035 0.0157  114 LEU   C O   
1941 C CB  . LEU   B 108 ? 0.1194 0.1231 0.1269 0.0145  -0.0055 0.0145  114 LEU   C CB  
1942 C CG  . LEU   B 108 ? 0.1295 0.1315 0.1345 0.0170  -0.0066 0.0120  114 LEU   C CG  
1943 C CD1 . LEU   B 108 ? 0.1484 0.1498 0.1514 0.0172  -0.0064 0.0121  114 LEU   C CD1 
1944 C CD2 . LEU   B 108 ? 0.1472 0.1517 0.1585 0.0182  -0.0078 0.0100  114 LEU   C CD2 
1945 N N   . ARG   B 109 ? 0.1253 0.1198 0.1191 0.0148  -0.0041 0.0151  115 ARG   C N   
1946 C CA  . ARG   B 109 ? 0.1331 0.1236 0.1228 0.0163  -0.0027 0.0155  115 ARG   C CA  
1947 C C   . ARG   B 109 ? 0.1391 0.1272 0.1241 0.0191  -0.0032 0.0143  115 ARG   C C   
1948 O O   . ARG   B 109 ? 0.1514 0.1399 0.1362 0.0191  -0.0040 0.0134  115 ARG   C O   
1949 C CB  . ARG   B 109 ? 0.1696 0.1581 0.1598 0.0141  -0.0014 0.0171  115 ARG   C CB  
1950 C CG  . ARG   B 109 ? 0.2149 0.2022 0.2034 0.0130  -0.0022 0.0164  115 ARG   C CG  
1951 C CD  . ARG   B 109 ? 0.2666 0.2518 0.2566 0.0105  -0.0017 0.0172  115 ARG   C CD  
1952 N NE  . ARG   B 109 ? 0.3301 0.3188 0.3246 0.0079  -0.0033 0.0178  115 ARG   C NE  
1953 C CZ  . ARG   B 109 ? 0.4414 0.4308 0.4409 0.0062  -0.0029 0.0193  115 ARG   C CZ  
1954 N NH1 . ARG   B 109 ? 0.4783 0.4647 0.4789 0.0070  -0.0001 0.0206  115 ARG   C NH1 
1955 N NH2 . ARG   B 109 ? 0.4706 0.4636 0.4743 0.0041  -0.0049 0.0200  115 ARG   C NH2 
1956 N N   . CYS   B 110 ? 0.1465 0.1319 0.1273 0.0218  -0.0023 0.0145  116 CYS   C N   
1957 C CA  . CYS   B 110 ? 0.1636 0.1461 0.1390 0.0251  -0.0028 0.0139  116 CYS   C CA  
1958 C C   . CYS   B 110 ? 0.1806 0.1582 0.1517 0.0261  0.0003  0.0164  116 CYS   C C   
1959 O O   . CYS   B 110 ? 0.1791 0.1558 0.1526 0.0240  0.0027  0.0181  116 CYS   C O   
1960 C CB  . CYS   B 110 ? 0.1588 0.1424 0.1322 0.0284  -0.0052 0.0118  116 CYS   C CB  
1961 S SG  . CYS   B 110 ? 0.1640 0.1455 0.1331 0.0304  -0.0035 0.0123  116 CYS   C SG  
1962 N N   . GLN   B 111 ? 0.1928 0.1671 0.1581 0.0298  0.0006  0.0169  117 GLN   C N   
1963 C CA  . GLN   B 111 ? 0.2150 0.1842 0.1765 0.0313  0.0044  0.0198  117 GLN   C CA  
1964 C C   . GLN   B 111 ? 0.2226 0.1903 0.1821 0.0324  0.0071  0.0214  117 GLN   C C   
1965 O O   . GLN   B 111 ? 0.2504 0.2144 0.2098 0.0324  0.0113  0.0245  117 GLN   C O   
1966 C CB  . GLN   B 111 ? 0.2451 0.2108 0.2000 0.0357  0.0042  0.0206  117 GLN   C CB  
1967 C CG  . GLN   B 111 ? 0.2707 0.2371 0.2193 0.0402  0.0016  0.0193  117 GLN   C CG  
1968 C CD  . GLN   B 111 ? 0.4259 0.3895 0.3681 0.0450  0.0007  0.0203  117 GLN   C CD  
1969 O OE1 . GLN   B 111 ? 0.4681 0.4340 0.4118 0.0459  -0.0030 0.0183  117 GLN   C OE1 
1970 N NE2 . GLN   B 111 ? 0.4337 0.3923 0.3689 0.0484  0.0042  0.0236  117 GLN   C NE2 
1971 N N   . HIS   B 112 ? 0.1958 0.1662 0.1547 0.0331  0.0052  0.0195  118 HIS   C N   
1972 C CA  . HIS   B 112 ? 0.2069 0.1755 0.1632 0.0347  0.0082  0.0207  118 HIS   C CA  
1973 C C   . HIS   B 112 ? 0.2097 0.1807 0.1743 0.0306  0.0099  0.0215  118 HIS   C C   
1974 O O   . HIS   B 112 ? 0.2277 0.1970 0.1916 0.0316  0.0133  0.0231  118 HIS   C O   
1975 C CB  . HIS   B 112 ? 0.2196 0.1890 0.1702 0.0383  0.0053  0.0178  118 HIS   C CB  
1976 C CG  . HIS   B 112 ? 0.1959 0.1634 0.1386 0.0427  0.0027  0.0169  118 HIS   C CG  
1977 N ND1 . HIS   B 112 ? 0.1907 0.1618 0.1357 0.0428  -0.0026 0.0136  118 HIS   C ND1 
1978 C CD2 . HIS   B 112 ? 0.2415 0.2040 0.1744 0.0475  0.0048  0.0192  118 HIS   C CD2 
1979 C CE1 . HIS   B 112 ? 0.2224 0.1908 0.1597 0.0473  -0.0040 0.0140  118 HIS   C CE1 
1980 N NE2 . HIS   B 112 ? 0.2529 0.2161 0.1821 0.0504  0.0002  0.0173  118 HIS   C NE2 
1981 N N   . GLY   B 113 ? 0.1887 0.1638 0.1607 0.0264  0.0075  0.0205  119 GLY   C N   
1982 C CA  . GLY   B 113 ? 0.1826 0.1606 0.1626 0.0228  0.0083  0.0213  119 GLY   C CA  
1983 C C   . GLY   B 113 ? 0.1606 0.1437 0.1452 0.0207  0.0047  0.0191  119 GLY   C C   
1984 O O   . GLY   B 113 ? 0.1581 0.1427 0.1418 0.0208  0.0019  0.0173  119 GLY   C O   
1985 N N   . VAL   B 114 ? 0.1581 0.1439 0.1488 0.0188  0.0052  0.0198  120 VAL   C N   
1986 C CA  . VAL   B 114 ? 0.1495 0.1401 0.1457 0.0168  0.0026  0.0186  120 VAL   C CA  
1987 C C   . VAL   B 114 ? 0.1478 0.1393 0.1425 0.0191  0.0012  0.0159  120 VAL   C C   
1988 O O   . VAL   B 114 ? 0.1557 0.1456 0.1484 0.0212  0.0026  0.0152  120 VAL   C O   
1989 C CB  . VAL   B 114 ? 0.1598 0.1529 0.1635 0.0142  0.0038  0.0208  120 VAL   C CB  
1990 C CG1 . VAL   B 114 ? 0.1727 0.1704 0.1819 0.0128  0.0016  0.0202  120 VAL   C CG1 
1991 C CG2 . VAL   B 114 ? 0.1818 0.1744 0.1884 0.0116  0.0042  0.0229  120 VAL   C CG2 
1992 N N   . VAL   B 115 ? 0.1276 0.1216 0.1237 0.0190  -0.0016 0.0141  121 VAL   C N   
1993 C CA  . VAL   B 115 ? 0.1352 0.1306 0.1325 0.0208  -0.0037 0.0110  121 VAL   C CA  
1994 C C   . VAL   B 115 ? 0.1400 0.1391 0.1457 0.0190  -0.0037 0.0110  121 VAL   C C   
1995 O O   . VAL   B 115 ? 0.1457 0.1450 0.1533 0.0203  -0.0043 0.0086  121 VAL   C O   
1996 C CB  . VAL   B 115 ? 0.1388 0.1350 0.1353 0.0215  -0.0062 0.0096  121 VAL   C CB  
1997 C CG1 . VAL   B 115 ? 0.1513 0.1497 0.1519 0.0229  -0.0088 0.0063  121 VAL   C CG1 
1998 C CG2 . VAL   B 115 ? 0.1583 0.1507 0.1468 0.0237  -0.0061 0.0098  121 VAL   C CG2 
1999 N N   . GLY   B 116 ? 0.1295 0.1312 0.1400 0.0162  -0.0033 0.0134  122 GLY   C N   
2000 C CA  . GLY   B 116 ? 0.1421 0.1474 0.1610 0.0148  -0.0030 0.0142  122 GLY   C CA  
2001 C C   . GLY   B 116 ? 0.1242 0.1319 0.1455 0.0124  -0.0030 0.0173  122 GLY   C C   
2002 O O   . GLY   B 116 ? 0.1308 0.1371 0.1475 0.0116  -0.0032 0.0183  122 GLY   C O   
2003 N N   . ILE   B 117 ? 0.1177 0.1287 0.1463 0.0114  -0.0027 0.0188  123 ILE   C N   
2004 C CA  . ILE   B 117 ? 0.1172 0.1305 0.1470 0.0098  -0.0028 0.0219  123 ILE   C CA  
2005 C C   . ILE   B 117 ? 0.1120 0.1277 0.1461 0.0102  -0.0025 0.0225  123 ILE   C C   
2006 O O   . ILE   B 117 ? 0.1216 0.1383 0.1620 0.0110  -0.0019 0.0211  123 ILE   C O   
2007 C CB  . ILE   B 117 ? 0.1231 0.1383 0.1577 0.0084  -0.0022 0.0249  123 ILE   C CB  
2008 C CG1 . ILE   B 117 ? 0.1419 0.1583 0.1842 0.0090  -0.0007 0.0247  123 ILE   C CG1 
2009 C CG2 . ILE   B 117 ? 0.1467 0.1599 0.1781 0.0076  -0.0022 0.0253  123 ILE   C CG2 
2010 C CD1 . ILE   B 117 ? 0.1463 0.1651 0.1952 0.0078  0.0002  0.0284  123 ILE   C CD1 
2011 N N   . VAL   B 118 ? 0.1100 0.1265 0.1413 0.0098  -0.0026 0.0246  124 VAL   C N   
2012 C CA  . VAL   B 118 ? 0.1090 0.1276 0.1442 0.0104  -0.0012 0.0261  124 VAL   C CA  
2013 C C   . VAL   B 118 ? 0.1120 0.1333 0.1565 0.0103  0.0002  0.0285  124 VAL   C C   
2014 O O   . VAL   B 118 ? 0.1093 0.1317 0.1548 0.0094  -0.0001 0.0310  124 VAL   C O   
2015 C CB  . VAL   B 118 ? 0.1192 0.1376 0.1478 0.0104  -0.0013 0.0284  124 VAL   C CB  
2016 C CG1 . VAL   B 118 ? 0.1224 0.1427 0.1545 0.0116  0.0012  0.0311  124 VAL   C CG1 
2017 C CG2 . VAL   B 118 ? 0.1312 0.1466 0.1516 0.0106  -0.0023 0.0258  124 VAL   C CG2 
2018 N N   . SER   B 119 ? 0.1133 0.1357 0.1655 0.0111  0.0018  0.0280  125 SER   C N   
2019 C CA  . SER   B 119 ? 0.1129 0.1375 0.1756 0.0111  0.0037  0.0302  125 SER   C CA  
2020 C C   . SER   B 119 ? 0.1189 0.1452 0.1881 0.0120  0.0065  0.0327  125 SER   C C   
2021 O O   . SER   B 119 ? 0.1170 0.1451 0.1933 0.0121  0.0088  0.0365  125 SER   C O   
2022 C CB  . SER   B 119 ? 0.1236 0.1474 0.1920 0.0111  0.0031  0.0261  125 SER   C CB  
2023 O OG  . SER   B 119 ? 0.1331 0.1585 0.2129 0.0111  0.0051  0.0275  125 SER   C OG  
2024 N N   . THR   B 120 ? 0.1219 0.1475 0.1904 0.0129  0.0070  0.0310  126 THR   C N   
2025 C CA  . THR   B 120 ? 0.1181 0.1451 0.1948 0.0140  0.0106  0.0337  126 THR   C CA  
2026 C C   . THR   B 120 ? 0.1142 0.1401 0.1828 0.0151  0.0118  0.0349  126 THR   C C   
2027 O O   . THR   B 120 ? 0.1184 0.1423 0.1770 0.0149  0.0094  0.0324  126 THR   C O   
2028 C CB  . THR   B 120 ? 0.1165 0.1442 0.2063 0.0141  0.0108  0.0301  126 THR   C CB  
2029 O OG1 . THR   B 120 ? 0.1271 0.1535 0.2133 0.0145  0.0083  0.0257  126 THR   C OG1 
2030 C CG2 . THR   B 120 ? 0.1353 0.1632 0.2322 0.0132  0.0094  0.0276  126 THR   C CG2 
2031 N N   . GLY   B 121 ? 0.1242 0.1509 0.1973 0.0165  0.0160  0.0388  127 GLY   C N   
2032 C CA  . GLY   B 121 ? 0.1542 0.1795 0.2204 0.0180  0.0182  0.0401  127 GLY   C CA  
2033 C C   . GLY   B 121 ? 0.1878 0.2142 0.2641 0.0197  0.0239  0.0439  127 GLY   C C   
2034 O O   . GLY   B 121 ? 0.2231 0.2511 0.3077 0.0200  0.0266  0.0477  127 GLY   C O   
2035 N N   . GLY   B 122 ? 0.2347 0.2599 0.3094 0.0212  0.0265  0.0440  128 GLY   C N   
2036 C CA  . GLY   B 122 ? 0.2603 0.2862 0.3451 0.0232  0.0329  0.0480  128 GLY   C CA  
2037 C C   . GLY   B 122 ? 0.2478 0.2736 0.3403 0.0237  0.0338  0.0450  128 GLY   C C   
2038 O O   . GLY   B 122 ? 0.2420 0.2681 0.3368 0.0224  0.0291  0.0395  128 GLY   C O   
2039 N N   . ASN   B 123 ? 0.2293 0.2547 0.3264 0.0260  0.0404  0.0490  129 ASN   C N   
2040 C CA  . ASN   B 123 ? 0.2313 0.2570 0.3379 0.0269  0.0424  0.0471  129 ASN   C CA  
2041 C C   . ASN   B 123 ? 0.2111 0.2349 0.3062 0.0267  0.0381  0.0424  129 ASN   C C   
2042 O O   . ASN   B 123 ? 0.2436 0.2683 0.3477 0.0266  0.0367  0.0390  129 ASN   C O   
2043 C CB  . ASN   B 123 ? 0.2864 0.3154 0.4152 0.0255  0.0410  0.0442  129 ASN   C CB  
2044 C CG  . ASN   B 123 ? 0.3834 0.4139 0.5301 0.0267  0.0482  0.0490  129 ASN   C CG  
2045 O OD1 . ASN   B 123 ? 0.3959 0.4250 0.5402 0.0292  0.0555  0.0547  129 ASN   C OD1 
2046 N ND2 . ASN   B 123 ? 0.4143 0.4475 0.5801 0.0251  0.0468  0.0467  129 ASN   C ND2 
2047 N N   . GLY   B 124 ? 0.1972 0.2182 0.2735 0.0267  0.0362  0.0424  130 GLY   C N   
2048 C CA  . GLY   B 124 ? 0.1960 0.2147 0.2617 0.0265  0.0326  0.0381  130 GLY   C CA  
2049 C C   . GLY   B 124 ? 0.1721 0.1917 0.2389 0.0243  0.0255  0.0327  130 GLY   C C   
2050 O O   . GLY   B 124 ? 0.1743 0.1923 0.2363 0.0244  0.0228  0.0293  130 GLY   C O   
2051 N N   . LEU   B 125 ? 0.1476 0.1694 0.2209 0.0227  0.0230  0.0323  131 LEU   C N   
2052 C CA  . LEU   B 125 ? 0.1478 0.1700 0.2210 0.0210  0.0168  0.0275  131 LEU   C CA  
2053 C C   . LEU   B 125 ? 0.1525 0.1740 0.2162 0.0195  0.0145  0.0282  131 LEU   C C   
2054 O O   . LEU   B 125 ? 0.1807 0.2028 0.2437 0.0195  0.0170  0.0322  131 LEU   C O   
2055 C CB  . LEU   B 125 ? 0.1647 0.1899 0.2548 0.0205  0.0154  0.0252  131 LEU   C CB  
2056 C CG  . LEU   B 125 ? 0.1948 0.2214 0.2977 0.0218  0.0170  0.0241  131 LEU   C CG  
2057 C CD1 . LEU   B 125 ? 0.2466 0.2764 0.3692 0.0214  0.0176  0.0235  131 LEU   C CD1 
2058 C CD2 . LEU   B 125 ? 0.2002 0.2259 0.2989 0.0225  0.0128  0.0199  131 LEU   C CD2 
2059 N N   . VAL   B 126 ? 0.1257 0.1460 0.1829 0.0186  0.0100  0.0247  132 VAL   C N   
2060 C CA  . VAL   B 126 ? 0.1171 0.1368 0.1677 0.0171  0.0077  0.0249  132 VAL   C CA  
2061 C C   . VAL   B 126 ? 0.1079 0.1284 0.1644 0.0164  0.0043  0.0212  132 VAL   C C   
2062 O O   . VAL   B 126 ? 0.1180 0.1378 0.1749 0.0171  0.0019  0.0175  132 VAL   C O   
2063 C CB  . VAL   B 126 ? 0.1246 0.1414 0.1612 0.0167  0.0060  0.0244  132 VAL   C CB  
2064 C CG1 . VAL   B 126 ? 0.1503 0.1650 0.1832 0.0174  0.0043  0.0209  132 VAL   C CG1 
2065 C CG2 . VAL   B 126 ? 0.1339 0.1506 0.1662 0.0150  0.0036  0.0247  132 VAL   C CG2 
2066 N N   . GLY   B 127 ? 0.1084 0.1300 0.1683 0.0154  0.0041  0.0221  133 GLY   C N   
2067 C CA  . GLY   B 127 ? 0.1054 0.1271 0.1697 0.0150  0.0014  0.0184  133 GLY   C CA  
2068 C C   . GLY   B 127 ? 0.1147 0.1349 0.1705 0.0141  -0.0001 0.0185  133 GLY   C C   
2069 O O   . GLY   B 127 ? 0.1178 0.1385 0.1710 0.0132  0.0012  0.0221  133 GLY   C O   
2070 N N   . PHE   B 128 ? 0.1075 0.1259 0.1601 0.0146  -0.0028 0.0147  134 PHE   C N   
2071 C CA  . PHE   B 128 ? 0.1069 0.1234 0.1522 0.0141  -0.0036 0.0146  134 PHE   C CA  
2072 C C   . PHE   B 128 ? 0.1082 0.1244 0.1579 0.0145  -0.0043 0.0120  134 PHE   C C   
2073 O O   . PHE   B 128 ? 0.1192 0.1350 0.1719 0.0158  -0.0062 0.0081  134 PHE   C O   
2074 C CB  . PHE   B 128 ? 0.1157 0.1291 0.1509 0.0150  -0.0052 0.0129  134 PHE   C CB  
2075 C CG  . PHE   B 128 ? 0.1197 0.1327 0.1506 0.0149  -0.0046 0.0144  134 PHE   C CG  
2076 C CD1 . PHE   B 128 ? 0.1205 0.1328 0.1458 0.0136  -0.0037 0.0171  134 PHE   C CD1 
2077 C CD2 . PHE   B 128 ? 0.1253 0.1384 0.1577 0.0163  -0.0051 0.0127  134 PHE   C CD2 
2078 C CE1 . PHE   B 128 ? 0.1295 0.1407 0.1498 0.0138  -0.0032 0.0177  134 PHE   C CE1 
2079 C CE2 . PHE   B 128 ? 0.1312 0.1434 0.1594 0.0165  -0.0039 0.0140  134 PHE   C CE2 
2080 C CZ  . PHE   B 128 ? 0.1300 0.1409 0.1515 0.0153  -0.0029 0.0162  134 PHE   C CZ  
2081 N N   . ALA   B 129 ? 0.1159 0.1321 0.1660 0.0135  -0.0030 0.0140  135 ALA   C N   
2082 C CA  . ALA   B 129 ? 0.1152 0.1303 0.1680 0.0141  -0.0031 0.0114  135 ALA   C CA  
2083 C C   . ALA   B 129 ? 0.1241 0.1355 0.1663 0.0155  -0.0042 0.0092  135 ALA   C C   
2084 O O   . ALA   B 129 ? 0.1309 0.1411 0.1671 0.0148  -0.0032 0.0117  135 ALA   C O   
2085 C CB  . ALA   B 129 ? 0.1274 0.1437 0.1849 0.0127  -0.0007 0.0150  135 ALA   C CB  
2086 N N   . ASP   B 130 ? 0.1284 0.1380 0.1687 0.0176  -0.0062 0.0046  136 ASP   C N   
2087 C CA  . ASP   B 130 ? 0.1362 0.1420 0.1656 0.0197  -0.0069 0.0029  136 ASP   C CA  
2088 C C   . ASP   B 130 ? 0.1448 0.1484 0.1720 0.0199  -0.0043 0.0039  136 ASP   C C   
2089 O O   . ASP   B 130 ? 0.1460 0.1505 0.1802 0.0193  -0.0030 0.0034  136 ASP   C O   
2090 C CB  . ASP   B 130 ? 0.1540 0.1586 0.1820 0.0223  -0.0104 -0.0025 136 ASP   C CB  
2091 C CG  . ASP   B 130 ? 0.1904 0.1909 0.2059 0.0254  -0.0114 -0.0041 136 ASP   C CG  
2092 O OD1 . ASP   B 130 ? 0.1873 0.1864 0.1961 0.0256  -0.0106 -0.0016 136 ASP   C OD1 
2093 O OD2 . ASP   B 130 ? 0.2337 0.2318 0.2458 0.0278  -0.0125 -0.0079 136 ASP   C OD2 
2094 N N   . VAL   B 131 ? 0.1462 0.1468 0.1646 0.0208  -0.0028 0.0054  137 VAL   C N   
2095 C CA  . VAL   B 131 ? 0.1467 0.1445 0.1624 0.0217  0.0004  0.0063  137 VAL   C CA  
2096 C C   . VAL   B 131 ? 0.1632 0.1562 0.1673 0.0254  0.0006  0.0042  137 VAL   C C   
2097 O O   . VAL   B 131 ? 0.1722 0.1620 0.1726 0.0268  0.0041  0.0051  137 VAL   C O   
2098 C CB  . VAL   B 131 ? 0.1543 0.1530 0.1725 0.0192  0.0033  0.0113  137 VAL   C CB  
2099 C CG1 . VAL   B 131 ? 0.1526 0.1560 0.1812 0.0163  0.0030  0.0137  137 VAL   C CG1 
2100 C CG2 . VAL   B 131 ? 0.1641 0.1616 0.1764 0.0189  0.0029  0.0132  137 VAL   C CG2 
2101 N N   . ARG   B 132 ? 0.1597 0.1518 0.1579 0.0273  -0.0027 0.0018  138 ARG   C N   
2102 C CA  . ARG   B 132 ? 0.1692 0.1565 0.1550 0.0313  -0.0025 0.0007  138 ARG   C CA  
2103 C C   . ARG   B 132 ? 0.1757 0.1599 0.1564 0.0347  -0.0027 -0.0033 138 ARG   C C   
2104 O O   . ARG   B 132 ? 0.2075 0.1869 0.1768 0.0384  -0.0009 -0.0031 138 ARG   C O   
2105 C CB  . ARG   B 132 ? 0.1658 0.1533 0.1474 0.0327  -0.0064 -0.0007 138 ARG   C CB  
2106 C CG  . ARG   B 132 ? 0.1646 0.1538 0.1487 0.0300  -0.0056 0.0032  138 ARG   C CG  
2107 C CD  . ARG   B 132 ? 0.1607 0.1500 0.1416 0.0318  -0.0092 0.0016  138 ARG   C CD  
2108 N NE  . ARG   B 132 ? 0.1597 0.1530 0.1489 0.0310  -0.0129 -0.0017 138 ARG   C NE  
2109 C CZ  . ARG   B 132 ? 0.1665 0.1614 0.1571 0.0319  -0.0163 -0.0033 138 ARG   C CZ  
2110 N NH1 . ARG   B 132 ? 0.1744 0.1670 0.1575 0.0341  -0.0169 -0.0023 138 ARG   C NH1 
2111 N NH2 . ARG   B 132 ? 0.1662 0.1649 0.1668 0.0307  -0.0187 -0.0057 138 ARG   C NH2 
2112 N N   . ASP   B 133 ? 0.1705 0.1568 0.1588 0.0339  -0.0045 -0.0069 139 ASP   C N   
2113 C CA  . ASP   B 133 ? 0.1893 0.1724 0.1731 0.0370  -0.0049 -0.0116 139 ASP   C CA  
2114 C C   . ASP   B 133 ? 0.2043 0.1852 0.1893 0.0368  0.0010  -0.0094 139 ASP   C C   
2115 O O   . ASP   B 133 ? 0.2231 0.2000 0.2021 0.0399  0.0019  -0.0130 139 ASP   C O   
2116 C CB  . ASP   B 133 ? 0.2090 0.1950 0.2024 0.0361  -0.0094 -0.0170 139 ASP   C CB  
2117 C CG  . ASP   B 133 ? 0.2150 0.2051 0.2235 0.0318  -0.0073 -0.0148 139 ASP   C CG  
2118 O OD1 . ASP   B 133 ? 0.2052 0.1981 0.2182 0.0289  -0.0053 -0.0095 139 ASP   C OD1 
2119 O OD2 . ASP   B 133 ? 0.2439 0.2342 0.2597 0.0316  -0.0076 -0.0184 139 ASP   C OD2 
2120 N N   . LEU   B 134 ? 0.1847 0.1678 0.1768 0.0333  0.0049  -0.0038 140 LEU   C N   
2121 C CA  . LEU   B 134 ? 0.1867 0.1686 0.1828 0.0328  0.0104  -0.0012 140 LEU   C CA  
2122 C C   . LEU   B 134 ? 0.1930 0.1702 0.1790 0.0354  0.0150  0.0019  140 LEU   C C   
2123 O O   . LEU   B 134 ? 0.1922 0.1703 0.1815 0.0334  0.0180  0.0070  140 LEU   C O   
2124 C CB  . LEU   B 134 ? 0.1797 0.1668 0.1891 0.0281  0.0113  0.0032  140 LEU   C CB  
2125 C CG  . LEU   B 134 ? 0.1749 0.1666 0.1949 0.0257  0.0077  0.0012  140 LEU   C CG  
2126 C CD1 . LEU   B 134 ? 0.1848 0.1813 0.2154 0.0217  0.0086  0.0065  140 LEU   C CD1 
2127 C CD2 . LEU   B 134 ? 0.1969 0.1873 0.2211 0.0270  0.0079  -0.0033 140 LEU   C CD2 
2128 N N   . LEU   B 135 ? 0.2111 0.1828 0.1842 0.0404  0.0156  -0.0014 141 LEU   C N   
2129 C CA  . LEU   B 135 ? 0.2264 0.1928 0.1882 0.0438  0.0202  0.0019  141 LEU   C CA  
2130 C C   . LEU   B 135 ? 0.2264 0.1913 0.1930 0.0432  0.0278  0.0065  141 LEU   C C   
2131 O O   . LEU   B 135 ? 0.2413 0.2038 0.2048 0.0439  0.0322  0.0113  141 LEU   C O   
2132 C CB  . LEU   B 135 ? 0.2384 0.1991 0.1838 0.0499  0.0191  -0.0026 141 LEU   C CB  
2133 C CG  . LEU   B 135 ? 0.2417 0.2041 0.1832 0.0510  0.0108  -0.0079 141 LEU   C CG  
2134 C CD1 . LEU   B 135 ? 0.2685 0.2251 0.1926 0.0577  0.0089  -0.0125 141 LEU   C CD1 
2135 C CD2 . LEU   B 135 ? 0.2524 0.2181 0.1963 0.0487  0.0080  -0.0048 141 LEU   C CD2 
2136 N N   . TRP   B 136 ? 0.2188 0.1854 0.1947 0.0416  0.0292  0.0054  142 TRP   C N   
2137 C CA  . TRP   B 136 ? 0.2288 0.1943 0.2113 0.0410  0.0363  0.0096  142 TRP   C CA  
2138 C C   . TRP   B 136 ? 0.2399 0.2099 0.2339 0.0365  0.0374  0.0157  142 TRP   C C   
2139 O O   . TRP   B 136 ? 0.2505 0.2197 0.2502 0.0361  0.0431  0.0200  142 TRP   C O   
2140 C CB  . TRP   B 136 ? 0.2303 0.1968 0.2211 0.0404  0.0371  0.0068  142 TRP   C CB  
2141 C CG  . TRP   B 136 ? 0.2204 0.1931 0.2226 0.0363  0.0314  0.0050  142 TRP   C CG  
2142 C CD1 . TRP   B 136 ? 0.2345 0.2079 0.2358 0.0367  0.0260  -0.0009 142 TRP   C CD1 
2143 C CD2 . TRP   B 136 ? 0.2130 0.1917 0.2303 0.0315  0.0311  0.0093  142 TRP   C CD2 
2144 N NE1 . TRP   B 136 ? 0.2369 0.2163 0.2518 0.0324  0.0230  0.0000  142 TRP   C NE1 
2145 C CE2 . TRP   B 136 ? 0.2229 0.2055 0.2467 0.0295  0.0260  0.0063  142 TRP   C CE2 
2146 C CE3 . TRP   B 136 ? 0.2109 0.1921 0.2368 0.0291  0.0343  0.0153  142 TRP   C CE3 
2147 C CZ2 . TRP   B 136 ? 0.2085 0.1971 0.2456 0.0254  0.0246  0.0097  142 TRP   C CZ2 
2148 C CZ3 . TRP   B 136 ? 0.2031 0.1904 0.2421 0.0250  0.0321  0.0181  142 TRP   C CZ3 
2149 C CH2 . TRP   B 136 ? 0.2051 0.1958 0.2486 0.0234  0.0274  0.0155  142 TRP   C CH2 
2150 N N   . LEU   B 137 ? 0.2202 0.1949 0.2183 0.0331  0.0319  0.0160  143 LEU   C N   
2151 C CA  . LEU   B 137 ? 0.2167 0.1949 0.2239 0.0292  0.0322  0.0210  143 LEU   C CA  
2152 C C   . LEU   B 137 ? 0.2626 0.2367 0.2644 0.0309  0.0368  0.0246  143 LEU   C C   
2153 O O   . LEU   B 137 ? 0.2810 0.2570 0.2919 0.0282  0.0387  0.0289  143 LEU   C O   
2154 C CB  . LEU   B 137 ? 0.2073 0.1902 0.2170 0.0261  0.0258  0.0202  143 LEU   C CB  
2155 C CG  . LEU   B 137 ? 0.1875 0.1752 0.2058 0.0237  0.0222  0.0183  143 LEU   C CG  
2156 C CD1 . LEU   B 137 ? 0.1992 0.1902 0.2172 0.0218  0.0166  0.0171  143 LEU   C CD1 
2157 C CD2 . LEU   B 137 ? 0.2034 0.1951 0.2350 0.0206  0.0240  0.0223  143 LEU   C CD2 
2158 N N   . ASP   B 138 ? 0.2538 0.2224 0.2413 0.0356  0.0380  0.0230  144 ASP   C N   
2159 C CA  . ASP   B 138 ? 0.2792 0.2432 0.2607 0.0378  0.0428  0.0269  144 ASP   C CA  
2160 C C   . ASP   B 138 ? 0.3127 0.2723 0.2945 0.0405  0.0514  0.0301  144 ASP   C C   
2161 O O   . ASP   B 138 ? 0.3360 0.2912 0.3134 0.0428  0.0565  0.0339  144 ASP   C O   
2162 C CB  . ASP   B 138 ? 0.2884 0.2480 0.2537 0.0423  0.0408  0.0245  144 ASP   C CB  
2163 C CG  . ASP   B 138 ? 0.2876 0.2508 0.2523 0.0402  0.0334  0.0220  144 ASP   C CG  
2164 O OD1 . ASP   B 138 ? 0.2881 0.2565 0.2639 0.0353  0.0304  0.0228  144 ASP   C OD1 
2165 O OD2 . ASP   B 138 ? 0.3519 0.3126 0.3049 0.0438  0.0305  0.0193  144 ASP   C OD2 
2166 N N   . GLU   B 139 ? 0.3132 0.2736 0.3008 0.0404  0.0536  0.0292  145 GLU   C N   
2167 C CA  . GLU   B 139 ? 0.3673 0.3230 0.3549 0.0435  0.0625  0.0322  145 GLU   C CA  
2168 C C   . GLU   B 139 ? 0.4130 0.3720 0.4151 0.0410  0.0649  0.0332  145 GLU   C C   
2169 O O   . GLU   B 139 ? 0.4144 0.3793 0.4260 0.0370  0.0594  0.0316  145 GLU   C O   
2170 C CB  . GLU   B 139 ? 0.4316 0.3803 0.4005 0.0501  0.0644  0.0284  145 GLU   C CB  
2171 C CG  . GLU   B 139 ? 0.5276 0.4779 0.4951 0.0502  0.0595  0.0219  145 GLU   C CG  
2172 C CD  . GLU   B 139 ? 0.6604 0.6053 0.6096 0.0558  0.0574  0.0161  145 GLU   C CD  
2173 O OE1 . GLU   B 139 ? 0.6956 0.6418 0.6454 0.0556  0.0530  0.0103  145 GLU   C OE1 
2174 O OE2 . GLU   B 139 ? 0.6880 0.6273 0.6226 0.0606  0.0599  0.0173  145 GLU   C OE2 
2175 N N   . GLU   B 140 ? 0.4513 0.4062 0.4548 0.0438  0.0735  0.0361  146 GLU   C N   
2176 C CA  . GLU   B 140 ? 0.4788 0.4353 0.4945 0.0430  0.0775  0.0371  146 GLU   C CA  
2177 C C   . GLU   B 140 ? 0.4930 0.4572 0.5288 0.0370  0.0749  0.0407  146 GLU   C C   
2178 O O   . GLU   B 140 ? 0.4996 0.4682 0.5458 0.0346  0.0727  0.0399  146 GLU   C O   
2179 C CB  . GLU   B 140 ? 0.5081 0.4635 0.5176 0.0448  0.0748  0.0307  146 GLU   C CB  
2180 C CG  . GLU   B 140 ? 0.5966 0.5565 0.6211 0.0420  0.0743  0.0302  146 GLU   C CG  
2181 C CD  . GLU   B 140 ? 0.6955 0.6526 0.7270 0.0440  0.0832  0.0327  146 GLU   C CD  
2182 O OE1 . GLU   B 140 ? 0.7375 0.6959 0.7755 0.0436  0.0829  0.0302  146 GLU   C OE1 
2183 O OE2 . GLU   B 140 ? 0.7211 0.6748 0.7528 0.0461  0.0907  0.0374  146 GLU   C OE2 
2184 C C4  . A1B09 C .   ? 0.3934 0.3430 0.4315 0.0055  0.0839  -0.0272 201 A1B09 A C4  
2185 C C5  . A1B09 C .   ? 0.3876 0.3336 0.4319 0.0076  0.0841  -0.0256 201 A1B09 A C5  
2186 C C6  . A1B09 C .   ? 0.3800 0.3327 0.4185 0.0088  0.0710  -0.0208 201 A1B09 A C6  
2187 C C7  . A1B09 C .   ? 0.3566 0.3051 0.3987 0.0094  0.0709  -0.0205 201 A1B09 A C7  
2188 C C8  . A1B09 C .   ? 0.3458 0.2998 0.4084 0.0185  0.0709  -0.0093 201 A1B09 A C8  
2189 C C10 . A1B09 C .   ? 0.3451 0.2864 0.4076 0.0154  0.0706  -0.0127 201 A1B09 A C10 
2190 O O1  . A1B09 C .   ? 0.3062 0.2669 0.3832 0.0242  0.0730  -0.0014 201 A1B09 A O1  
2191 N N   . A1B09 C .   ? 0.3510 0.3029 0.4158 0.0190  0.0689  -0.0079 201 A1B09 A N   
2192 C C12 . A1B09 C .   ? 0.3393 0.2963 0.4238 0.0262  0.0695  0.0033  201 A1B09 A C12 
2193 C C11 . A1B09 C .   ? 0.3497 0.3027 0.4290 0.0239  0.0663  0.0010  201 A1B09 A C11 
2194 O O2  . A1B09 C .   ? 0.3507 0.3148 0.4223 0.0239  0.0527  0.0057  201 A1B09 A O2  
2195 C C9  . A1B09 C .   ? 0.3616 0.3074 0.4111 0.0121  0.0659  -0.0159 201 A1B09 A C9  
2196 C C1  . A1B09 C .   ? 0.3843 0.3466 0.4126 0.0083  0.0588  -0.0174 201 A1B09 A C1  
2197 O O   . A1B09 C .   ? 0.3823 0.3498 0.4078 0.0097  0.0485  -0.0132 201 A1B09 A O   
2198 C C   . A1B09 C .   ? 0.3790 0.3533 0.3937 0.0080  0.0378  -0.0115 201 A1B09 A C   
2199 C C3  . A1B09 C .   ? 0.3934 0.3527 0.4202 0.0048  0.0708  -0.0234 201 A1B09 A C3  
2200 C C2  . A1B09 C .   ? 0.3854 0.3507 0.4081 0.0065  0.0587  -0.0185 201 A1B09 A C2  
# 
