data_7HVW
# 
_entry.id   7HVW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HVW         pdb_00007hvw 10.2210/pdb7hvw/pdb 
WWPDB D_1001407996 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HVW 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                    15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-N~1~-[(2-methylphenyl)methyl]piperidine-1,3-dicarboxamide' 275.346   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                       65.409    2   ?         ? ? ? 
4 water       nat water                                                            18.015    399 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-N~1~-[(2-methylphenyl)methyl]piperidine-1,3-dicarboxamide' A1BO1 
3 'ZINC ION'                                                       ZN    
4 water                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BO1 non-polymer         . '(3S)-N~1~-[(2-methylphenyl)methyl]piperidine-1,3-dicarboxamide' ? 'C15 H21 N3 O2'  275.346 
ALA   'L-peptide linking' y ALANINE                                                          ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                         ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                       ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                  ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                         ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                        ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                  ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                          ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                        ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                            ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                          ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                           ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                       ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                    ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                          ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                           ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                        ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                       ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                         ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                           ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                       ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BO1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BO1 
_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 A1BO1 1   201 201 A1BO1 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 2 A1BO1 1   201 201 A1BO1 LIG C . 
F 3 ZN    1   202 1   ZN    ZN  C . 
G 4 HOH   1   301 459 HOH   HOH A . 
G 4 HOH   2   302 580 HOH   HOH A . 
G 4 HOH   3   303 239 HOH   HOH A . 
G 4 HOH   4   304 504 HOH   HOH A . 
G 4 HOH   5   305 168 HOH   HOH A . 
G 4 HOH   6   306 433 HOH   HOH A . 
G 4 HOH   7   307 229 HOH   HOH A . 
G 4 HOH   8   308 134 HOH   HOH A . 
G 4 HOH   9   309 87  HOH   HOH A . 
G 4 HOH   10  310 534 HOH   HOH A . 
G 4 HOH   11  311 565 HOH   HOH A . 
G 4 HOH   12  312 47  HOH   HOH A . 
G 4 HOH   13  313 53  HOH   HOH A . 
G 4 HOH   14  314 583 HOH   HOH A . 
G 4 HOH   15  315 557 HOH   HOH A . 
G 4 HOH   16  316 496 HOH   HOH A . 
G 4 HOH   17  317 22  HOH   HOH A . 
G 4 HOH   18  318 76  HOH   HOH A . 
G 4 HOH   19  319 325 HOH   HOH A . 
G 4 HOH   20  320 195 HOH   HOH A . 
G 4 HOH   21  321 485 HOH   HOH A . 
G 4 HOH   22  322 2   HOH   HOH A . 
G 4 HOH   23  323 29  HOH   HOH A . 
G 4 HOH   24  324 586 HOH   HOH A . 
G 4 HOH   25  325 488 HOH   HOH A . 
G 4 HOH   26  326 184 HOH   HOH A . 
G 4 HOH   27  327 57  HOH   HOH A . 
G 4 HOH   28  328 212 HOH   HOH A . 
G 4 HOH   29  329 78  HOH   HOH A . 
G 4 HOH   30  330 89  HOH   HOH A . 
G 4 HOH   31  331 426 HOH   HOH A . 
G 4 HOH   32  332 128 HOH   HOH A . 
G 4 HOH   33  333 108 HOH   HOH A . 
G 4 HOH   34  334 27  HOH   HOH A . 
G 4 HOH   35  335 55  HOH   HOH A . 
G 4 HOH   36  336 94  HOH   HOH A . 
G 4 HOH   37  337 12  HOH   HOH A . 
G 4 HOH   38  338 40  HOH   HOH A . 
G 4 HOH   39  339 336 HOH   HOH A . 
G 4 HOH   40  340 563 HOH   HOH A . 
G 4 HOH   41  341 10  HOH   HOH A . 
G 4 HOH   42  342 13  HOH   HOH A . 
G 4 HOH   43  343 487 HOH   HOH A . 
G 4 HOH   44  344 532 HOH   HOH A . 
G 4 HOH   45  345 116 HOH   HOH A . 
G 4 HOH   46  346 52  HOH   HOH A . 
G 4 HOH   47  347 468 HOH   HOH A . 
G 4 HOH   48  348 424 HOH   HOH A . 
G 4 HOH   49  349 96  HOH   HOH A . 
G 4 HOH   50  350 526 HOH   HOH A . 
G 4 HOH   51  351 508 HOH   HOH A . 
G 4 HOH   52  352 140 HOH   HOH A . 
G 4 HOH   53  353 579 HOH   HOH A . 
G 4 HOH   54  354 54  HOH   HOH A . 
G 4 HOH   55  355 185 HOH   HOH A . 
G 4 HOH   56  356 576 HOH   HOH A . 
G 4 HOH   57  357 139 HOH   HOH A . 
G 4 HOH   58  358 581 HOH   HOH A . 
G 4 HOH   59  359 432 HOH   HOH A . 
G 4 HOH   60  360 444 HOH   HOH A . 
G 4 HOH   61  361 492 HOH   HOH A . 
G 4 HOH   62  362 63  HOH   HOH A . 
G 4 HOH   63  363 458 HOH   HOH A . 
G 4 HOH   64  364 17  HOH   HOH A . 
G 4 HOH   65  365 60  HOH   HOH A . 
G 4 HOH   66  366 162 HOH   HOH A . 
G 4 HOH   67  367 171 HOH   HOH A . 
G 4 HOH   68  368 41  HOH   HOH A . 
G 4 HOH   69  369 548 HOH   HOH A . 
G 4 HOH   70  370 423 HOH   HOH A . 
G 4 HOH   71  371 166 HOH   HOH A . 
G 4 HOH   72  372 48  HOH   HOH A . 
G 4 HOH   73  373 234 HOH   HOH A . 
G 4 HOH   74  374 582 HOH   HOH A . 
G 4 HOH   75  375 438 HOH   HOH A . 
G 4 HOH   76  376 479 HOH   HOH A . 
G 4 HOH   77  377 495 HOH   HOH A . 
G 4 HOH   78  378 31  HOH   HOH A . 
G 4 HOH   79  379 81  HOH   HOH A . 
G 4 HOH   80  380 9   HOH   HOH A . 
G 4 HOH   81  381 118 HOH   HOH A . 
G 4 HOH   82  382 601 HOH   HOH A . 
G 4 HOH   83  383 1   HOH   HOH A . 
G 4 HOH   84  384 502 HOH   HOH A . 
G 4 HOH   85  385 578 HOH   HOH A . 
G 4 HOH   86  386 5   HOH   HOH A . 
G 4 HOH   87  387 69  HOH   HOH A . 
G 4 HOH   88  388 170 HOH   HOH A . 
G 4 HOH   89  389 84  HOH   HOH A . 
G 4 HOH   90  390 14  HOH   HOH A . 
G 4 HOH   91  391 566 HOH   HOH A . 
G 4 HOH   92  392 549 HOH   HOH A . 
G 4 HOH   93  393 272 HOH   HOH A . 
G 4 HOH   94  394 107 HOH   HOH A . 
G 4 HOH   95  395 596 HOH   HOH A . 
G 4 HOH   96  396 24  HOH   HOH A . 
G 4 HOH   97  397 91  HOH   HOH A . 
G 4 HOH   98  398 136 HOH   HOH A . 
G 4 HOH   99  399 486 HOH   HOH A . 
G 4 HOH   100 400 515 HOH   HOH A . 
G 4 HOH   101 401 431 HOH   HOH A . 
G 4 HOH   102 402 538 HOH   HOH A . 
G 4 HOH   103 403 120 HOH   HOH A . 
G 4 HOH   104 404 450 HOH   HOH A . 
G 4 HOH   105 405 62  HOH   HOH A . 
G 4 HOH   106 406 491 HOH   HOH A . 
G 4 HOH   107 407 436 HOH   HOH A . 
G 4 HOH   108 408 261 HOH   HOH A . 
G 4 HOH   109 409 109 HOH   HOH A . 
G 4 HOH   110 410 448 HOH   HOH A . 
G 4 HOH   111 411 18  HOH   HOH A . 
G 4 HOH   112 412 26  HOH   HOH A . 
G 4 HOH   113 413 44  HOH   HOH A . 
G 4 HOH   114 414 177 HOH   HOH A . 
G 4 HOH   115 415 474 HOH   HOH A . 
G 4 HOH   116 416 555 HOH   HOH A . 
G 4 HOH   117 417 65  HOH   HOH A . 
G 4 HOH   118 418 148 HOH   HOH A . 
G 4 HOH   119 419 585 HOH   HOH A . 
G 4 HOH   120 420 86  HOH   HOH A . 
G 4 HOH   121 421 59  HOH   HOH A . 
G 4 HOH   122 422 262 HOH   HOH A . 
G 4 HOH   123 423 51  HOH   HOH A . 
G 4 HOH   124 424 598 HOH   HOH A . 
G 4 HOH   125 425 183 HOH   HOH A . 
G 4 HOH   126 426 521 HOH   HOH A . 
G 4 HOH   127 427 537 HOH   HOH A . 
G 4 HOH   128 428 465 HOH   HOH A . 
G 4 HOH   129 429 535 HOH   HOH A . 
G 4 HOH   130 430 395 HOH   HOH A . 
G 4 HOH   131 431 552 HOH   HOH A . 
G 4 HOH   132 432 188 HOH   HOH A . 
G 4 HOH   133 433 453 HOH   HOH A . 
G 4 HOH   134 434 435 HOH   HOH A . 
G 4 HOH   135 435 428 HOH   HOH A . 
G 4 HOH   136 436 125 HOH   HOH A . 
G 4 HOH   137 437 441 HOH   HOH A . 
G 4 HOH   138 438 99  HOH   HOH A . 
G 4 HOH   139 439 501 HOH   HOH A . 
G 4 HOH   140 440 38  HOH   HOH A . 
G 4 HOH   141 441 6   HOH   HOH A . 
G 4 HOH   142 442 513 HOH   HOH A . 
G 4 HOH   143 443 467 HOH   HOH A . 
G 4 HOH   144 444 445 HOH   HOH A . 
G 4 HOH   145 445 597 HOH   HOH A . 
G 4 HOH   146 446 462 HOH   HOH A . 
G 4 HOH   147 447 477 HOH   HOH A . 
G 4 HOH   148 448 173 HOH   HOH A . 
G 4 HOH   149 449 593 HOH   HOH A . 
G 4 HOH   150 450 516 HOH   HOH A . 
G 4 HOH   151 451 528 HOH   HOH A . 
G 4 HOH   152 452 466 HOH   HOH A . 
G 4 HOH   153 453 570 HOH   HOH A . 
G 4 HOH   154 454 564 HOH   HOH A . 
G 4 HOH   155 455 594 HOH   HOH A . 
G 4 HOH   156 456 196 HOH   HOH A . 
G 4 HOH   157 457 97  HOH   HOH A . 
G 4 HOH   158 458 533 HOH   HOH A . 
G 4 HOH   159 459 377 HOH   HOH A . 
G 4 HOH   160 460 277 HOH   HOH A . 
G 4 HOH   161 461 590 HOH   HOH A . 
G 4 HOH   162 462 484 HOH   HOH A . 
G 4 HOH   163 463 122 HOH   HOH A . 
G 4 HOH   164 464 605 HOH   HOH A . 
G 4 HOH   165 465 104 HOH   HOH A . 
G 4 HOH   166 466 606 HOH   HOH A . 
G 4 HOH   167 467 595 HOH   HOH A . 
G 4 HOH   168 468 572 HOH   HOH A . 
G 4 HOH   169 469 238 HOH   HOH A . 
G 4 HOH   170 470 146 HOH   HOH A . 
G 4 HOH   171 471 256 HOH   HOH A . 
G 4 HOH   172 472 464 HOH   HOH A . 
G 4 HOH   173 473 602 HOH   HOH A . 
G 4 HOH   174 474 369 HOH   HOH A . 
G 4 HOH   175 475 609 HOH   HOH A . 
G 4 HOH   176 476 152 HOH   HOH A . 
G 4 HOH   177 477 527 HOH   HOH A . 
G 4 HOH   178 478 202 HOH   HOH A . 
G 4 HOH   179 479 200 HOH   HOH A . 
G 4 HOH   180 480 470 HOH   HOH A . 
G 4 HOH   181 481 603 HOH   HOH A . 
G 4 HOH   182 482 545 HOH   HOH A . 
G 4 HOH   183 483 551 HOH   HOH A . 
G 4 HOH   184 484 610 HOH   HOH A . 
G 4 HOH   185 485 204 HOH   HOH A . 
G 4 HOH   186 486 418 HOH   HOH A . 
G 4 HOH   187 487 573 HOH   HOH A . 
G 4 HOH   188 488 391 HOH   HOH A . 
G 4 HOH   189 489 483 HOH   HOH A . 
G 4 HOH   190 490 271 HOH   HOH A . 
G 4 HOH   191 491 243 HOH   HOH A . 
G 4 HOH   192 492 517 HOH   HOH A . 
G 4 HOH   193 493 368 HOH   HOH A . 
G 4 HOH   194 494 366 HOH   HOH A . 
G 4 HOH   195 495 390 HOH   HOH A . 
H 4 HOH   1   301 556 HOH   HOH C . 
H 4 HOH   2   302 505 HOH   HOH C . 
H 4 HOH   3   303 266 HOH   HOH C . 
H 4 HOH   4   304 469 HOH   HOH C . 
H 4 HOH   5   305 45  HOH   HOH C . 
H 4 HOH   6   306 457 HOH   HOH C . 
H 4 HOH   7   307 498 HOH   HOH C . 
H 4 HOH   8   308 460 HOH   HOH C . 
H 4 HOH   9   309 50  HOH   HOH C . 
H 4 HOH   10  310 163 HOH   HOH C . 
H 4 HOH   11  311 536 HOH   HOH C . 
H 4 HOH   12  312 16  HOH   HOH C . 
H 4 HOH   13  313 150 HOH   HOH C . 
H 4 HOH   14  314 43  HOH   HOH C . 
H 4 HOH   15  315 446 HOH   HOH C . 
H 4 HOH   16  316 61  HOH   HOH C . 
H 4 HOH   17  317 550 HOH   HOH C . 
H 4 HOH   18  318 174 HOH   HOH C . 
H 4 HOH   19  319 493 HOH   HOH C . 
H 4 HOH   20  320 499 HOH   HOH C . 
H 4 HOH   21  321 522 HOH   HOH C . 
H 4 HOH   22  322 461 HOH   HOH C . 
H 4 HOH   23  323 233 HOH   HOH C . 
H 4 HOH   24  324 541 HOH   HOH C . 
H 4 HOH   25  325 219 HOH   HOH C . 
H 4 HOH   26  326 32  HOH   HOH C . 
H 4 HOH   27  327 111 HOH   HOH C . 
H 4 HOH   28  328 37  HOH   HOH C . 
H 4 HOH   29  329 117 HOH   HOH C . 
H 4 HOH   30  330 130 HOH   HOH C . 
H 4 HOH   31  331 74  HOH   HOH C . 
H 4 HOH   32  332 105 HOH   HOH C . 
H 4 HOH   33  333 558 HOH   HOH C . 
H 4 HOH   34  334 489 HOH   HOH C . 
H 4 HOH   35  335 449 HOH   HOH C . 
H 4 HOH   36  336 437 HOH   HOH C . 
H 4 HOH   37  337 20  HOH   HOH C . 
H 4 HOH   38  338 144 HOH   HOH C . 
H 4 HOH   39  339 600 HOH   HOH C . 
H 4 HOH   40  340 280 HOH   HOH C . 
H 4 HOH   41  341 25  HOH   HOH C . 
H 4 HOH   42  342 73  HOH   HOH C . 
H 4 HOH   43  343 440 HOH   HOH C . 
H 4 HOH   44  344 509 HOH   HOH C . 
H 4 HOH   45  345 425 HOH   HOH C . 
H 4 HOH   46  346 456 HOH   HOH C . 
H 4 HOH   47  347 19  HOH   HOH C . 
H 4 HOH   48  348 525 HOH   HOH C . 
H 4 HOH   49  349 82  HOH   HOH C . 
H 4 HOH   50  350 71  HOH   HOH C . 
H 4 HOH   51  351 554 HOH   HOH C . 
H 4 HOH   52  352 430 HOH   HOH C . 
H 4 HOH   53  353 553 HOH   HOH C . 
H 4 HOH   54  354 95  HOH   HOH C . 
H 4 HOH   55  355 454 HOH   HOH C . 
H 4 HOH   56  356 165 HOH   HOH C . 
H 4 HOH   57  357 39  HOH   HOH C . 
H 4 HOH   58  358 126 HOH   HOH C . 
H 4 HOH   59  359 33  HOH   HOH C . 
H 4 HOH   60  360 131 HOH   HOH C . 
H 4 HOH   61  361 4   HOH   HOH C . 
H 4 HOH   62  362 265 HOH   HOH C . 
H 4 HOH   63  363 114 HOH   HOH C . 
H 4 HOH   64  364 524 HOH   HOH C . 
H 4 HOH   65  365 500 HOH   HOH C . 
H 4 HOH   66  366 72  HOH   HOH C . 
H 4 HOH   67  367 519 HOH   HOH C . 
H 4 HOH   68  368 523 HOH   HOH C . 
H 4 HOH   69  369 143 HOH   HOH C . 
H 4 HOH   70  370 101 HOH   HOH C . 
H 4 HOH   71  371 237 HOH   HOH C . 
H 4 HOH   72  372 98  HOH   HOH C . 
H 4 HOH   73  373 506 HOH   HOH C . 
H 4 HOH   74  374 514 HOH   HOH C . 
H 4 HOH   75  375 599 HOH   HOH C . 
H 4 HOH   76  376 250 HOH   HOH C . 
H 4 HOH   77  377 442 HOH   HOH C . 
H 4 HOH   78  378 482 HOH   HOH C . 
H 4 HOH   79  379 540 HOH   HOH C . 
H 4 HOH   80  380 422 HOH   HOH C . 
H 4 HOH   81  381 544 HOH   HOH C . 
H 4 HOH   82  382 178 HOH   HOH C . 
H 4 HOH   83  383 476 HOH   HOH C . 
H 4 HOH   84  384 584 HOH   HOH C . 
H 4 HOH   85  385 543 HOH   HOH C . 
H 4 HOH   86  386 497 HOH   HOH C . 
H 4 HOH   87  387 473 HOH   HOH C . 
H 4 HOH   88  388 8   HOH   HOH C . 
H 4 HOH   89  389 88  HOH   HOH C . 
H 4 HOH   90  390 85  HOH   HOH C . 
H 4 HOH   91  391 75  HOH   HOH C . 
H 4 HOH   92  392 217 HOH   HOH C . 
H 4 HOH   93  393 112 HOH   HOH C . 
H 4 HOH   94  394 3   HOH   HOH C . 
H 4 HOH   95  395 398 HOH   HOH C . 
H 4 HOH   96  396 472 HOH   HOH C . 
H 4 HOH   97  397 23  HOH   HOH C . 
H 4 HOH   98  398 510 HOH   HOH C . 
H 4 HOH   99  399 42  HOH   HOH C . 
H 4 HOH   100 400 137 HOH   HOH C . 
H 4 HOH   101 401 7   HOH   HOH C . 
H 4 HOH   102 402 80  HOH   HOH C . 
H 4 HOH   103 403 381 HOH   HOH C . 
H 4 HOH   104 404 471 HOH   HOH C . 
H 4 HOH   105 405 546 HOH   HOH C . 
H 4 HOH   106 406 77  HOH   HOH C . 
H 4 HOH   107 407 49  HOH   HOH C . 
H 4 HOH   108 408 373 HOH   HOH C . 
H 4 HOH   109 409 452 HOH   HOH C . 
H 4 HOH   110 410 577 HOH   HOH C . 
H 4 HOH   111 411 34  HOH   HOH C . 
H 4 HOH   112 412 68  HOH   HOH C . 
H 4 HOH   113 413 463 HOH   HOH C . 
H 4 HOH   114 414 46  HOH   HOH C . 
H 4 HOH   115 415 447 HOH   HOH C . 
H 4 HOH   116 416 575 HOH   HOH C . 
H 4 HOH   117 417 113 HOH   HOH C . 
H 4 HOH   118 418 35  HOH   HOH C . 
H 4 HOH   119 419 559 HOH   HOH C . 
H 4 HOH   120 420 451 HOH   HOH C . 
H 4 HOH   121 421 209 HOH   HOH C . 
H 4 HOH   122 422 15  HOH   HOH C . 
H 4 HOH   123 423 439 HOH   HOH C . 
H 4 HOH   124 424 58  HOH   HOH C . 
H 4 HOH   125 425 372 HOH   HOH C . 
H 4 HOH   126 426 153 HOH   HOH C . 
H 4 HOH   127 427 542 HOH   HOH C . 
H 4 HOH   128 428 30  HOH   HOH C . 
H 4 HOH   129 429 562 HOH   HOH C . 
H 4 HOH   130 430 511 HOH   HOH C . 
H 4 HOH   131 431 36  HOH   HOH C . 
H 4 HOH   132 432 429 HOH   HOH C . 
H 4 HOH   133 433 539 HOH   HOH C . 
H 4 HOH   134 434 315 HOH   HOH C . 
H 4 HOH   135 435 367 HOH   HOH C . 
H 4 HOH   136 436 507 HOH   HOH C . 
H 4 HOH   137 437 106 HOH   HOH C . 
H 4 HOH   138 438 547 HOH   HOH C . 
H 4 HOH   139 439 561 HOH   HOH C . 
H 4 HOH   140 440 119 HOH   HOH C . 
H 4 HOH   141 441 11  HOH   HOH C . 
H 4 HOH   142 442 520 HOH   HOH C . 
H 4 HOH   143 443 379 HOH   HOH C . 
H 4 HOH   144 444 172 HOH   HOH C . 
H 4 HOH   145 445 494 HOH   HOH C . 
H 4 HOH   146 446 145 HOH   HOH C . 
H 4 HOH   147 447 210 HOH   HOH C . 
H 4 HOH   148 448 529 HOH   HOH C . 
H 4 HOH   149 449 478 HOH   HOH C . 
H 4 HOH   150 450 127 HOH   HOH C . 
H 4 HOH   151 451 66  HOH   HOH C . 
H 4 HOH   152 452 518 HOH   HOH C . 
H 4 HOH   153 453 611 HOH   HOH C . 
H 4 HOH   154 454 21  HOH   HOH C . 
H 4 HOH   155 455 198 HOH   HOH C . 
H 4 HOH   156 456 592 HOH   HOH C . 
H 4 HOH   157 457 569 HOH   HOH C . 
H 4 HOH   158 458 267 HOH   HOH C . 
H 4 HOH   159 459 568 HOH   HOH C . 
H 4 HOH   160 460 374 HOH   HOH C . 
H 4 HOH   161 461 393 HOH   HOH C . 
H 4 HOH   162 462 224 HOH   HOH C . 
H 4 HOH   163 463 490 HOH   HOH C . 
H 4 HOH   164 464 607 HOH   HOH C . 
H 4 HOH   165 465 181 HOH   HOH C . 
H 4 HOH   166 466 230 HOH   HOH C . 
H 4 HOH   167 467 503 HOH   HOH C . 
H 4 HOH   168 468 192 HOH   HOH C . 
H 4 HOH   169 469 531 HOH   HOH C . 
H 4 HOH   170 470 380 HOH   HOH C . 
H 4 HOH   171 471 147 HOH   HOH C . 
H 4 HOH   172 472 305 HOH   HOH C . 
H 4 HOH   173 473 567 HOH   HOH C . 
H 4 HOH   174 474 102 HOH   HOH C . 
H 4 HOH   175 475 154 HOH   HOH C . 
H 4 HOH   176 476 604 HOH   HOH C . 
H 4 HOH   177 477 201 HOH   HOH C . 
H 4 HOH   178 478 612 HOH   HOH C . 
H 4 HOH   179 479 591 HOH   HOH C . 
H 4 HOH   180 480 400 HOH   HOH C . 
H 4 HOH   181 481 211 HOH   HOH C . 
H 4 HOH   182 482 587 HOH   HOH C . 
H 4 HOH   183 483 394 HOH   HOH C . 
H 4 HOH   184 484 370 HOH   HOH C . 
H 4 HOH   185 485 613 HOH   HOH C . 
H 4 HOH   186 486 480 HOH   HOH C . 
H 4 HOH   187 487 167 HOH   HOH C . 
H 4 HOH   188 488 67  HOH   HOH C . 
H 4 HOH   189 489 384 HOH   HOH C . 
H 4 HOH   190 490 574 HOH   HOH C . 
H 4 HOH   191 491 481 HOH   HOH C . 
H 4 HOH   192 492 286 HOH   HOH C . 
H 4 HOH   193 493 530 HOH   HOH C . 
H 4 HOH   194 494 608 HOH   HOH C . 
H 4 HOH   195 495 571 HOH   HOH C . 
H 4 HOH   196 496 512 HOH   HOH C . 
H 4 HOH   197 497 417 HOH   HOH C . 
H 4 HOH   198 498 406 HOH   HOH C . 
H 4 HOH   199 499 110 HOH   HOH C . 
H 4 HOH   200 500 376 HOH   HOH C . 
H 4 HOH   201 501 396 HOH   HOH C . 
H 4 HOH   202 502 588 HOH   HOH C . 
H 4 HOH   203 503 420 HOH   HOH C . 
H 4 HOH   204 504 589 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           7HVW 
_cell.length_a           72.752 
_cell.length_b           61.886 
_cell.length_c           65.406 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.13 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVW 
_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          7HVW 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.82 
_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                     7HVW 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             65.31 
_reflns.d_resolution_high            1.34 
_reflns.number_obs                   64465 
_reflns.percent_possible_obs         99.0 
_reflns.pdbx_Rmerge_I_obs            0.077 
_reflns.pdbx_netI_over_sigmaI        10.6 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.084 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     384458 
_reflns.pdbx_chi_squared             0.93 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.34 
_reflns_shell.d_res_low                   1.41 
_reflns_shell.number_measured_all         31012 
_reflns_shell.number_unique_obs           8819 
_reflns_shell.Rmerge_I_obs                1.014 
_reflns_shell.pdbx_chi_squared            0.83 
_reflns_shell.pdbx_redundancy             3.5 
_reflns_shell.percent_possible_obs        93.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.203 
_reflns_shell.pdbx_Rpim_I_all             0.628 
_reflns_shell.pdbx_CC_half                0.437 
_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                                 7HVW 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     64424 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             65.31 
_refine.ls_d_res_high                            1.339 
_refine.ls_percent_reflns_obs                    98.8 
_refine.ls_R_factor_obs                          0.1852 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1846 
_refine.ls_R_factor_R_free                       0.2039 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.290 
_refine.ls_number_reflns_R_free                  2120 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.B_iso_mean                               20.11 
_refine.aniso_B[1][1]                            -0.56640 
_refine.aniso_B[2][2]                            0.59600 
_refine.aniso_B[3][3]                            -0.02950 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.53850 
_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             0.054 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.055 
_refine.pdbx_overall_SU_R_Blow_DPI               0.058 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.058 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVW 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             399 
_refine_hist.number_atoms_total               2589 
_refine_hist.d_res_high                       1.339 
_refine_hist.d_res_low                        65.31 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.012 ? 2.00  2250 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3062 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  754  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  404  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2250 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.81  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.86 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2132 '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                       1.34 
_refine_ls_shell.d_res_low                        1.35 
_refine_ls_shell.number_reflns_R_work             1238 
_refine_ls_shell.R_factor_R_work                  0.3117 
_refine_ls_shell.percent_reflns_obs               82.37 
_refine_ls_shell.R_factor_R_free                  0.3832 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.96 
_refine_ls_shell.number_reflns_R_free             51 
_refine_ls_shell.number_reflns_all                1289 
_refine_ls_shell.R_factor_all                     0.3145 
# 
_struct.entry_id                  7HVW 
_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-0032527-001 (A71EV2A-x3616)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVW 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HVW A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HVW C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 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 ? ? ? ? ? ? ? 2.355 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 108.9 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.4 ? 
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_555 116.5 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.8 ? 
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_555 102.2 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 113.8 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 108.9 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.9 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N GLY B 43  ? N GLY C 49  O GLY B 7   ? O GLY C 13  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O GLN B 89  ? O GLN C 95  N ILE B 76  ? N ILE C 82  
# 
_pdbx_entry_details.entry_id                   7HVW 
_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 303 ? ? O A HOH 439 ? ? 1.95 
2 1 O C HOH 390 ? ? O C HOH 496 ? ? 2.11 
3 1 O C HOH 303 ? ? O C HOH 319 ? ? 2.11 
4 1 O C HOH 307 ? ? O C HOH 390 ? ? 2.12 
# 
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 14.9713 7.6611   14.3966 -0.0197 -0.0135 -0.0072 -0.0034 0.0038  -0.0030 0.7817 1.1101 0.3342 
0.5177  -0.2763 -0.1359 -0.0333 0.0101  0.0414 -0.0351 0.0437 -0.0539 0.0301 -0.0391 -0.0104 
'X-RAY DIFFRACTION' 2 ? refined 19.4089 -23.1234 18.5001 -0.0153 -0.0095 -0.0047 -0.0001 -0.0046 0.0022  0.5152 0.8868 0.3862 
-0.2575 0.0267  -0.0050 -0.0223 -0.0171 0.0346 -0.0163 0.0247 0.0374  0.0048 0.0105  -0.0024 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 503 ? 6.73 . 
2 1 O ? C HOH 504 ? 8.02 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BO1 N1   N  N N 1   
A1BO1 C4   C  Y N 2   
A1BO1 C5   C  Y N 3   
A1BO1 C6   C  Y N 4   
A1BO1 C7   C  N N 5   
A1BO1 C8   C  N N 6   
A1BO1 C10  C  N N 7   
A1BO1 C13  C  N N 8   
A1BO1 O1   O  N N 9   
A1BO1 N2   N  N N 10  
A1BO1 C12  C  N S 11  
A1BO1 C11  C  N N 12  
A1BO1 C9   C  N N 13  
A1BO1 C14  C  N N 14  
A1BO1 O    O  N N 15  
A1BO1 N    N  N N 16  
A1BO1 C1   C  Y N 17  
A1BO1 C    C  N N 18  
A1BO1 C3   C  Y N 19  
A1BO1 C2   C  Y N 20  
A1BO1 H6   H  N N 21  
A1BO1 H7   H  N N 22  
A1BO1 H9   H  N N 23  
A1BO1 H8   H  N N 24  
A1BO1 H13  H  N N 25  
A1BO1 H14  H  N N 26  
A1BO1 H18  H  N N 27  
A1BO1 H17  H  N N 28  
A1BO1 H    H  N N 29  
A1BO1 H15  H  N N 30  
A1BO1 H16  H  N N 31  
A1BO1 H11  H  N N 32  
A1BO1 H12  H  N N 33  
A1BO1 H19  H  N N 34  
A1BO1 H20  H  N N 35  
A1BO1 H10  H  N N 36  
A1BO1 H2   H  N N 37  
A1BO1 H1   H  N N 38  
A1BO1 H3   H  N N 39  
A1BO1 H5   H  N N 40  
A1BO1 H4   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TRP   N    N  N N 362 
TRP   CA   C  N S 363 
TRP   C    C  N N 364 
TRP   O    O  N N 365 
TRP   CB   C  N N 366 
TRP   CG   C  Y N 367 
TRP   CD1  C  Y N 368 
TRP   CD2  C  Y N 369 
TRP   NE1  N  Y N 370 
TRP   CE2  C  Y N 371 
TRP   CE3  C  Y N 372 
TRP   CZ2  C  Y N 373 
TRP   CZ3  C  Y N 374 
TRP   CH2  C  Y N 375 
TRP   OXT  O  N N 376 
TRP   H    H  N N 377 
TRP   H2   H  N N 378 
TRP   HA   H  N N 379 
TRP   HB2  H  N N 380 
TRP   HB3  H  N N 381 
TRP   HD1  H  N N 382 
TRP   HE1  H  N N 383 
TRP   HE3  H  N N 384 
TRP   HZ2  H  N N 385 
TRP   HZ3  H  N N 386 
TRP   HH2  H  N N 387 
TRP   HXT  H  N N 388 
TYR   N    N  N N 389 
TYR   CA   C  N S 390 
TYR   C    C  N N 391 
TYR   O    O  N N 392 
TYR   CB   C  N N 393 
TYR   CG   C  Y N 394 
TYR   CD1  C  Y N 395 
TYR   CD2  C  Y N 396 
TYR   CE1  C  Y N 397 
TYR   CE2  C  Y N 398 
TYR   CZ   C  Y N 399 
TYR   OH   O  N N 400 
TYR   OXT  O  N N 401 
TYR   H    H  N N 402 
TYR   H2   H  N N 403 
TYR   HA   H  N N 404 
TYR   HB2  H  N N 405 
TYR   HB3  H  N N 406 
TYR   HD1  H  N N 407 
TYR   HD2  H  N N 408 
TYR   HE1  H  N N 409 
TYR   HE2  H  N N 410 
TYR   HH   H  N N 411 
TYR   HXT  H  N N 412 
VAL   N    N  N N 413 
VAL   CA   C  N S 414 
VAL   C    C  N N 415 
VAL   O    O  N N 416 
VAL   CB   C  N N 417 
VAL   CG1  C  N N 418 
VAL   CG2  C  N N 419 
VAL   OXT  O  N N 420 
VAL   H    H  N N 421 
VAL   H2   H  N N 422 
VAL   HA   H  N N 423 
VAL   HB   H  N N 424 
VAL   HG11 H  N N 425 
VAL   HG12 H  N N 426 
VAL   HG13 H  N N 427 
VAL   HG21 H  N N 428 
VAL   HG22 H  N N 429 
VAL   HG23 H  N N 430 
VAL   HXT  H  N N 431 
ZN    ZN   ZN N N 432 
# 
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 
A1BO1 C   C1   sing N N 1   
A1BO1 C1  C2   doub Y N 2   
A1BO1 C2  C3   sing Y N 3   
A1BO1 C3  C4   doub Y N 4   
A1BO1 C4  C5   sing Y N 5   
A1BO1 C5  C6   doub Y N 6   
A1BO1 C1  C6   sing Y N 7   
A1BO1 C6  C7   sing N N 8   
A1BO1 C7  N    sing N N 9   
A1BO1 N   C8   sing N N 10  
A1BO1 O   C8   doub N N 11  
A1BO1 C8  N1   sing N N 12  
A1BO1 N1  C9   sing N N 13  
A1BO1 C9  C10  sing N N 14  
A1BO1 C10 C11  sing N N 15  
A1BO1 C11 C12  sing N N 16  
A1BO1 C12 C13  sing N N 17  
A1BO1 N2  C13  sing N N 18  
A1BO1 C13 O1   doub N N 19  
A1BO1 C14 C12  sing N N 20  
A1BO1 N1  C14  sing N N 21  
A1BO1 C4  H6   sing N N 22  
A1BO1 C5  H7   sing N N 23  
A1BO1 C7  H9   sing N N 24  
A1BO1 C7  H8   sing N N 25  
A1BO1 C10 H13  sing N N 26  
A1BO1 C10 H14  sing N N 27  
A1BO1 N2  H18  sing N N 28  
A1BO1 N2  H17  sing N N 29  
A1BO1 C12 H    sing N N 30  
A1BO1 C11 H15  sing N N 31  
A1BO1 C11 H16  sing N N 32  
A1BO1 C9  H11  sing N N 33  
A1BO1 C9  H12  sing N N 34  
A1BO1 C14 H19  sing N N 35  
A1BO1 C14 H20  sing N N 36  
A1BO1 N   H10  sing N N 37  
A1BO1 C   H2   sing N N 38  
A1BO1 C   H1   sing N N 39  
A1BO1 C   H3   sing N N 40  
A1BO1 C3  H5   sing N N 41  
A1BO1 C2  H4   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HVW 
_atom_sites.fract_transf_matrix[1][1]   0.013745 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000752 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016159 
_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]   0.015312 
_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   ? 18.214 7.305   24.530 1.00 17.38 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.461 7.411   23.762 1.00 17.46 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.628 6.257   22.802 1.00 17.70 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.001 5.201   22.966 1.00 18.40 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.649 7.505   24.719 1.00 20.08 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.825 6.281   25.415 1.00 22.40 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.452 6.448   21.781 1.00 16.33 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.770 5.399   20.827 1.00 15.77 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.120 5.956   19.461 1.00 15.25 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.750 7.087   19.122 1.00 16.01 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.854 5.191   18.672 1.00 14.16 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.258 5.607   17.338 1.00 14.53 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.335 4.413   16.394 1.00 14.64 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.353 3.246   16.836 1.00 15.12 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.654 6.276   17.432 1.00 15.73 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.390 4.696   15.074 1.00 13.27 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.615 3.693   14.047 1.00 13.73 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.034 3.923   13.527 1.00 14.15 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.406 5.067   13.229 1.00 14.67 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.633 3.879   12.876 1.00 13.81 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.181 3.816   13.367 1.00 13.04 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.840 2.798   11.814 1.00 15.37 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.182 4.383   12.294 1.00 14.21 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.830 2.861   13.392 1.00 15.16 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.186 2.975   12.876 1.00 15.88 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.280 2.196   11.569 1.00 16.48 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.238 0.984   11.595 1.00 18.23 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.188 2.427   13.922 1.00 15.84 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.236 3.244   15.186 1.00 16.44 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 26.390 2.959   16.251 1.00 18.64 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 28.008 4.390   15.262 1.00 17.72 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 26.376 3.755   17.395 1.00 19.88 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 28.038 5.163   16.411 1.00 19.26 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.211 4.850   17.470 1.00 20.01 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.206 5.671   18.574 1.00 22.64 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.321 2.877   10.420 1.00 15.79 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.369 2.214   9.114  1.00 17.39 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.516 2.822   8.324  1.00 18.58 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.632 4.043   8.228  1.00 18.53 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.995 2.340   8.378  1.00 18.89 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.477 3.776   8.391  1.00 19.55 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.085 1.826   6.958  1.00 20.93 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.453 1.991   7.863  1.00 19.26 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.608 2.493   7.121  1.00 20.35 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.398 3.503   7.934  1.00 20.00 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.674 3.225   9.103  1.00 20.11 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.664 4.696   7.378  1.00 19.84 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.345 5.721   8.177  1.00 19.02 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.382 6.791   8.639  1.00 17.81 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.742 7.966   8.727  1.00 18.08 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.545 6.324   7.452  1.00 21.93 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.670 5.318   7.327  1.00 28.95 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.382 5.019   8.296  1.00 32.09 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.800 4.732   6.158  1.00 28.34 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.158 6.374   9.002  1.00 16.65 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.141 7.329   9.458  1.00 15.29 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.556 6.900   10.799 1.00 14.45 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.412 5.715   11.081 1.00 15.64 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.978 7.379   8.437  1.00 15.08 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.377 7.924   7.077  1.00 15.97 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.012 9.162   6.953  1.00 17.56 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.136 7.197   5.921  1.00 18.59 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.375 9.666   5.702  1.00 19.23 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.483 7.693   4.669  1.00 19.34 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.136 8.912   4.566  1.00 20.94 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.472 9.425   3.330  1.00 23.48 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.146 7.881   11.599 1.00 13.32 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.433 7.709   12.850 1.00 13.73 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.128 8.516   12.688 1.00 14.14 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.182 9.723   12.371 1.00 14.30 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.283 8.222   14.028 1.00 13.68 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.521 8.500   15.319 1.00 16.10 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.404 8.859   16.509 1.00 17.67 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.811 9.886   17.387 1.00 18.32 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.242 9.653   18.567 1.00 19.69 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.051 8.399   18.992 1.00 20.55 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.762 10.659  19.289 1.00 18.92 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.968 7.848   12.840 1.00 14.27 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.660 8.501   12.714 1.00 13.44 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.092 8.621   14.099 1.00 13.03 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.930 7.596   14.796 1.00 13.04 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.690 7.683   11.833 1.00 13.69 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.409 8.495   11.575 1.00 13.74 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.362 7.204   10.532 1.00 14.42 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.753 9.845   14.513 1.00 12.32 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.198 10.081  15.857 1.00 12.94 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.984 11.001  15.757 1.00 12.46 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.759 11.700  14.745 1.00 13.09 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.251 10.741  16.776 1.00 15.23 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.342 9.756   17.119 1.00 19.55 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.801 12.037  16.158 1.00 15.94 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.203 11.099  16.842 1.00 11.48 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.137 12.114  16.905 1.00 11.39 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.848 13.477  16.908 1.00 12.09 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.794 13.698  17.692 1.00 12.36 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.325 12.011  18.208 1.00 12.22 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.499 10.765  18.280 1.00 13.00 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 16.953 9.747   18.807 1.00 14.57 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.286 10.817  17.718 1.00 12.89 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.365 14.431  16.082 1.00 10.90 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.030 15.717  15.993 1.00 11.85 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.034 16.424  17.384 1.00 12.97 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.029 17.054  17.769 1.00 13.31 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.353 16.556  14.919 1.00 11.25 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.132 17.862  14.621 1.00 10.70 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.231 18.722  13.740 1.00 13.21 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.850 19.970  13.250 1.00 14.66 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 18.859 21.123  13.904 1.00 14.72 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.451 21.183  15.171 1.00 14.58 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.331 22.227  13.314 1.00 14.89 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 17.941 16.237  18.161 1.00 12.04 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.859 16.908  19.473 1.00 12.26 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.815 16.318  20.501 1.00 13.67 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.001 16.957  21.543 1.00 16.68 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.392 16.981  19.995 1.00 13.95 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.830 15.679  20.489 1.00 13.18 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.270 14.745  19.632 1.00 13.26 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.705 15.231  21.763 1.00 14.19 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.817 13.741  20.409 1.00 12.85 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.095 13.977  21.694 1.00 14.35 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.387 15.133  20.232 1.00 13.13 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.363 14.506  21.138 1.00 13.10 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.800 14.542  20.601 1.00 14.60 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.704 13.973  21.209 1.00 15.08 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.957 13.059  21.455 1.00 13.62 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.558 12.913  22.097 1.00 14.66 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.226 11.420  22.280 1.00 16.67 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.491 13.677  23.452 1.00 15.75 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.020 15.247  19.476 1.00 14.13 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.355 15.290  18.887 1.00 13.56 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.336 15.981  19.832 1.00 14.15 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 23.987 16.934  20.490 1.00 15.53 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.306 16.006  17.545 1.00 14.49 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.546 15.444  19.875 1.00 14.56 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.598 15.984  20.747 1.00 15.15 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.419 17.059  20.043 1.00 15.33 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.320 17.250  18.823 1.00 16.05 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.538 14.830  21.176 1.00 17.36 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.277 14.349  20.038 1.00 17.54 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.798 13.687  21.854 1.00 18.64 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.345 17.724  20.795 1.00 16.44 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.263 18.685  20.176 1.00 17.30 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.109 17.973  19.110 1.00 15.90 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.303 18.526  18.018 1.00 17.18 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.240 19.236  21.248 1.00 20.94 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 29.580 20.041  22.322 1.00 28.37 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 28.584 20.958  22.035 1.00 32.45 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.816 20.051  23.656 1.00 31.43 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 28.226 21.476  23.202 1.00 33.50 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 28.931 20.946  24.210 1.00 33.37 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.552 16.719  19.386 1.00 15.84 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.340 15.968  18.394 1.00 15.88 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.522 15.647  17.129 1.00 15.24 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.041 15.714  16.005 1.00 16.25 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.929 14.698  18.999 1.00 17.12 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.213 14.995  19.695 1.00 22.96 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 33.998 15.843  19.241 1.00 24.01 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.394 14.405  20.870 1.00 23.67 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.219 15.314  17.286 1.00 13.73 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.366 15.089  16.092 1.00 13.89 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.346 16.346  15.200 1.00 13.92 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.496 16.243  13.969 1.00 14.43 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 26.920 14.763  16.515 1.00 14.40 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.734 13.353  17.040 1.00 16.23 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.390 12.438  16.516 1.00 16.41 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 25.969 13.182  18.032 1.00 15.77 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.110 17.526  15.827 1.00 13.04 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.068 18.758  15.056 1.00 14.51 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.418 19.123  14.436 1.00 15.82 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.432 19.620  13.301 1.00 16.37 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.539 19.907  15.933 1.00 14.34 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.027 19.912  16.030 1.00 14.70 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.264 19.460  17.067 1.00 16.41 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.108 20.424  15.050 1.00 14.02 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 23.922 19.670  16.804 1.00 15.98 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 23.797 20.220  15.551 1.00 15.28 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.261 20.976  13.787 1.00 15.05 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.652 20.628  14.845 1.00 15.07 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.121 21.359  13.089 1.00 16.38 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.843 21.191  13.622 1.00 16.66 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.526 18.769  15.083 1.00 15.75 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 31.861 19.064  14.506 1.00 16.54 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.190 18.124  13.321 1.00 17.13 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.118 18.382  12.535 1.00 19.00 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 32.927 18.888  15.577 1.00 17.11 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.512 16.973  13.255 1.00 16.00 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.701 16.030  12.174 1.00 17.36 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.400 15.894  11.343 1.00 16.23 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.081 14.840  10.813 1.00 15.25 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.120 14.703  12.749 1.00 18.79 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.495 14.775  13.360 1.00 20.72 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.505 14.752  12.655 1.00 22.15 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.557 14.872  14.680 1.00 20.47 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.653 16.983  11.208 1.00 14.53 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.346 16.983  10.528 1.00 14.32 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.397 16.596  9.055  1.00 15.70 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.185 17.145  8.281  1.00 17.89 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.758 18.399  10.655 1.00 14.83 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.395 18.586  9.996  1.00 14.63 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.319 17.757  10.729 1.00 15.49 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.977 20.064  10.030 1.00 15.82 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.527 15.671  8.643  1.00 15.36 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.343 15.292  7.238  1.00 16.95 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.028 15.901  6.722  1.00 17.20 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.961 16.524  5.647  1.00 19.02 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.330 13.745  7.099  1.00 17.54 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.944 13.333  5.672  1.00 18.86 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.708 13.168  7.461  1.00 18.21 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.951 15.721  7.501  1.00 15.02 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.618 16.178  7.087  1.00 15.38 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.738 16.258  8.319  1.00 14.00 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.865 15.423  9.228  1.00 14.95 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.023 15.146  6.103  1.00 15.82 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.558 15.310  5.755  1.00 16.83 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.000 16.158  4.830  1.00 18.52 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.477 14.568  6.323  1.00 16.08 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.620 16.029  4.848  1.00 19.00 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.282 15.023  5.720  1.00 17.46 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.401 13.573  7.295  1.00 16.41 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.028 14.469  6.029  1.00 17.04 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.165 13.034  7.606  1.00 16.87 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.995 13.494  6.994  1.00 16.85 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.831 17.219  8.354  1.00 14.03 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.852 17.320  9.431  1.00 14.40 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.546 17.908  8.883  1.00 14.57 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.553 18.703  7.928  1.00 15.23 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.386 18.107  10.639 1.00 15.52 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 21.950 19.476  10.307 1.00 15.65 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 20.942 20.602  10.091 1.00 16.92 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.259 21.511  9.287  1.00 21.12 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.865 20.604  10.713 1.00 16.45 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.424 17.557  9.525  1.00 13.51 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.126 18.044  9.101  1.00 13.33 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.231 18.141  10.332 1.00 13.89 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.774 17.133  10.880 1.00 13.83 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.542 17.109  8.014  1.00 15.74 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.247 17.573  7.401  1.00 21.38 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.470 18.213  8.096  1.00 22.46 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.982 17.223  6.235  1.00 21.80 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 15.991 19.389  10.785 1.00 14.06 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.152 19.674  11.936 0.50 14.79 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.166 19.624  11.960 0.50 14.82 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.748 19.134  11.741 1.00 15.06 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.140 18.650  12.697 1.00 16.26 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.082 21.179  12.164 0.50 17.61 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.176 21.098  12.367 0.50 17.58 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.334 21.486  13.320 0.50 22.21 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.532 21.889  11.386 0.50 22.13 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.232 19.224  10.478 1.00 14.78 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.868 18.734  10.254 1.00 15.66 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.758 17.225  10.427 1.00 16.37 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.657 16.750  10.616 1.00 17.28 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.340 19.125  8.877  1.00 18.72 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.875 18.334  7.834  1.00 24.79 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.863 16.485  10.345 1.00 14.57 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.823 15.022  10.542 1.00 13.16 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.369 14.594  11.916 1.00 13.61 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.327 13.390  12.240 1.00 13.14 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.696 14.336  9.472  1.00 13.03 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.119 14.514  8.059  1.00 13.12 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.932 13.874  6.945  1.00 14.27 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.965 12.411  7.087  1.00 13.62 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.164 11.562  6.084  1.00 14.64 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.350 12.016  4.840  1.00 16.14 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.104 10.248  6.297  1.00 14.07 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 13.907 15.513  12.715 1.00 12.22 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.620 15.184  13.967 1.00 12.08 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.787 14.223  13.716 1.00 12.20 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.064 13.390  14.581 1.00 12.50 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.694 14.674  15.091 1.00 12.60 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.375 14.447  16.433 1.00 11.84 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.193 15.317  16.846 1.00 12.55 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.074 13.403  17.091 1.00 12.70 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.506 14.385  12.590 1.00 11.56 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.678 13.540  12.315 1.00 11.35 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 18.947 14.316  12.113 1.00 11.47 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 18.933 15.438  11.553 1.00 12.69 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.471 12.702  11.045 1.00 12.59 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.438 11.572  11.150 1.00 12.98 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.349 10.840  9.791  1.00 14.08 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.785 10.565  12.254 1.00 13.63 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.070 13.736  12.543 1.00 11.75 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.388 14.294  12.233 1.00 11.75 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.276 13.082  11.955 1.00 12.22 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.198 12.028  12.618 1.00 12.54 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 21.903 15.129  13.411 1.00 11.22 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.294 15.779  13.197 1.00 12.19 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.364 17.150  13.880 1.00 13.90 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.444 14.886  13.715 1.00 12.98 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.164 13.244  10.965 1.00 11.82 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.152 12.208  10.589 1.00 12.21 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.550 12.843  10.671 1.00 13.23 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.773 13.957  10.144 1.00 14.25 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.928 11.685  9.164  1.00 13.26 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.018 10.662  8.780  1.00 14.53 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.542 11.033  9.064  1.00 14.43 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.450 12.167  11.389 1.00 13.75 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.849 12.611  11.527 1.00 13.55 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.772 11.534  10.956 1.00 15.33 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.393 10.372  10.800 1.00 15.58 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.162 12.923  12.994 1.00 14.39 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 27.993 11.815  13.869 1.00 15.52 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.007 11.932  10.655 1.00 15.16 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.001 11.002  10.120 1.00 16.00 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.756 10.300  11.245 1.00 17.45 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.967 10.845  12.322 1.00 19.15 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.961 11.738  9.184  1.00 18.49 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.638 12.765  9.885  1.00 20.85 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.225 9.074   10.972 1.00 17.91 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.967 8.286   11.971 1.00 20.13 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.308 7.836   11.386 1.00 22.71 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.437 7.715   10.162 1.00 23.96 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.181 7.024   12.416 1.00 21.97 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.123 6.106   11.339 1.00 23.57 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.750 7.330   12.871 1.00 22.39 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.272 7.529   12.256 1.00 24.25 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.548 6.995   11.784 1.00 25.82 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.459 5.442   11.687 1.00 28.17 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.099 4.833   10.816 1.00 30.46 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.706 7.448   12.704 1.00 27.83 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.361 7.114   14.057 1.00 29.26 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.976 8.937   12.617 1.00 28.95 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.681 4.810   12.573 1.00 26.71 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.548 3.351   12.560 1.00 26.78 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.375 2.913   11.663 1.00 26.16 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.389 3.638   11.528 1.00 25.67 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.313 2.864   13.981 1.00 27.79 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.445 1.708   11.119 1.00 26.06 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.364 1.113   10.304 1.00 26.53 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.213 0.643   11.185 1.00 27.26 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.454 0.007   12.208 1.00 28.47 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.947 -0.076  9.510  1.00 29.61 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.930 -0.856  8.707  1.00 35.71 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.498 -0.150  7.445  1.00 42.21 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.084 0.864   7.012  1.00 43.99 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.452 -0.691  6.815  1.00 43.04 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.972 0.978   10.821 1.00 26.65 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.810 0.639   11.654 1.00 27.60 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.240 -0.767  11.623 1.00 30.13 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.251 -1.404  10.580 1.00 33.42 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.548 -1.150  12.713 1.00 28.01 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.967 -2.468  12.944 1.00 27.05 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.587 -2.765  12.257 1.00 26.43 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.220 -3.937  12.186 1.00 25.63 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.869 -2.699  14.452 1.00 27.48 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 26.785 -1.517  15.329 1.00 29.37 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.836 -1.747  11.758 1.00 25.51 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.434 -1.893  11.248 1.00 23.54 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 24.211 -1.958  9.675  1.00 22.52 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 25.093 -1.461  8.949  1.00 25.18 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.622 -0.715  11.851 1.00 22.67 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.455 -0.802  13.369 1.00 25.91 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.002 -1.866  13.846 1.00 28.24 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.733 0.233   14.092 1.00 20.52 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 23.001 -2.517  9.170  1.00 20.82 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.421 -2.702  7.789  1.00 22.14 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 21.089 -1.905  7.729  1.00 20.31 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.255 -2.068  8.621  1.00 20.05 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 22.004 -4.232  7.508  1.00 26.68 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.179 -4.986  7.271  1.00 30.90 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.098 -4.408  6.229  1.00 27.90 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.874 -1.073  6.706  1.00 17.87 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.619 -0.309  6.581  1.00 16.43 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.638 -1.075  5.691  1.00 16.39 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 19.008 -1.559  4.595  1.00 17.60 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.877 1.102   5.977  1.00 16.10 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.987 1.844   6.753  1.00 17.59 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.592 1.934   5.951  1.00 16.87 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.684 2.074   8.251  1.00 18.44 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.397 -1.227  6.138  1.00 15.11 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.343 -1.867  5.342  1.00 15.23 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.991 -0.969  4.128  1.00 15.59 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.956 0.267   4.207  1.00 15.43 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 15.083 -2.065  6.206  1.00 14.77 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.749 -1.610  2.973  1.00 15.80 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.304 -0.893  1.759  1.00 17.27 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.027 -1.633  1.337  1.00 18.67 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.057 -2.575  0.537  1.00 20.11 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.382 -0.930  0.658  1.00 17.02 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.718 -0.361  1.104  1.00 17.97 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.687 1.139   1.482  1.00 20.90 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.031 1.594   1.856  1.00 19.80 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.284 2.744   2.475  1.00 21.91 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.299 3.577   2.772  1.00 18.53 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.526 3.066   2.802  1.00 22.05 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.906 -1.237  1.919  1.00 18.24 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.650 -2.002  1.803  1.00 18.49 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.464 -1.087  2.156  1.00 19.10 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.638 0.074   2.562  1.00 18.54 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.715 -3.172  2.785  1.00 17.20 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.690 -2.623  4.531  1.00 17.19 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.249  -1.669  2.067  1.00 20.55 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.051  -0.964  2.481  1.00 20.30 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.364  -1.711  3.619  1.00 19.29 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.152  -1.583  3.768  1.00 20.76 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.069  -0.749  1.311  1.00 25.24 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.484  -2.001  0.724  1.00 35.43 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.935  -3.114  1.103  1.00 35.35 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.556  -1.888  -0.108 1.00 43.30 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 8.135  -2.394  4.503  1.00 17.22 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.516  -3.060  5.671  1.00 16.14 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.753  -2.073  6.521  1.00 16.53 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.176  -0.916  6.664  1.00 16.41 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.582  -3.748  6.520  1.00 16.81 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.264  -5.270  5.804  1.00 17.79 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.646  -2.509  7.076  1.00 15.37 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.853  -1.756  8.044  1.00 15.08 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.688  -2.527  9.370  1.00 14.37 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.805  -2.201  10.179 1.00 13.86 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.483  -1.363  7.474  1.00 16.90 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.539  -0.149  6.556  1.00 22.36 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 2.108  0.273   6.252  1.00 26.29 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.611  0.028   5.148  1.00 29.79 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.421  0.915   7.196  1.00 22.02 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.523  -3.603  9.581  1.00 13.52 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.632  -4.309  10.857 1.00 13.66 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.111  -4.481  11.158 1.00 13.64 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.982  -4.540  10.261 1.00 13.77 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.900  -5.681  10.866 1.00 16.07 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.536  -6.572  9.968  1.00 18.51 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.426  -5.567  10.537 1.00 17.54 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.403  -4.538  12.444 1.00 12.94 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.767  -4.730  12.902 1.00 12.72 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.815  -4.824  14.424 1.00 11.80 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.791  -5.051  15.079 1.00 12.69 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.020 -4.661  14.959 1.00 11.59 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.284 -4.796  16.397 1.00 10.57 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.133 -3.605  16.811 1.00 11.21 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.100 -3.282  16.133 1.00 11.76 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.010 -6.140  16.707 1.00 12.08 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.390 -6.208  18.209 1.00 13.04 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.111 -7.339  16.364 1.00 13.63 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.787 -2.948  17.958 1.00 11.62 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.619 -1.848  18.447 1.00 10.11 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.136 -2.101  19.846 1.00 11.29 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.511 -2.843  20.620 1.00 11.51 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.908 -0.438  18.377 1.00 11.10 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.880  -0.189  19.463 1.00 10.76 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.618  -0.765  19.402 1.00 11.55 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.144 0.678   20.522 1.00 11.91 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.662  -0.518  20.383 1.00 11.93 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.191  0.926   21.516 1.00 11.79 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 7.954  0.309   21.444 1.00 12.24 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 6.948  0.524   22.387 1.00 13.68 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.258 -1.453  20.175 1.00 11.03 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.794 -1.526  21.526 1.00 11.24 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.279 -0.348  22.357 1.00 12.14 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.395 0.832   21.982 1.00 12.15 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.340 -1.579  21.514 1.00 11.97 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 15.879 -1.676  22.914 1.00 12.83 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.673 -2.809  23.664 1.00 13.82 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.551 -0.604  23.502 1.00 13.86 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.128 -2.893  24.974 1.00 14.91 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 16.975 -0.659  24.825 1.00 14.44 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.781 -1.811  25.542 1.00 15.79 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.226 -1.891  26.849 1.00 19.68 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.737 -0.674  23.531 1.00 12.23 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.181 0.299   24.471 1.00 11.78 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.052 0.311   25.752 1.00 12.26 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 12.954 -0.583  26.604 1.00 13.58 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.739 -0.079  24.787 1.00 12.42 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 9.976  0.943   26.083 1.00 13.83 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 13.916 1.335   25.879 1.00 12.18 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 14.819 1.401   27.008 1.00 13.07 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.126 1.543   28.359 1.00 13.39 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.596 0.972   29.354 1.00 14.97 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 15.848 2.494   26.793 1.00 16.01 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.290 3.786   26.775 1.00 22.76 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 12.950 2.222   28.389 1.00 12.71 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.176 2.399   29.638 1.00 12.85 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.493 1.133   30.138 1.00 12.70 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 10.915 1.138   31.235 1.00 14.15 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.166 3.529   29.517 1.00 14.24 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.181 3.217   28.539 1.00 13.80 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.612 0.037   29.381 1.00 12.51 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.145 -1.282  29.789 1.00 13.26 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.244 -2.354  29.691 1.00 13.23 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 11.996 -3.534  30.000 1.00 14.56 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 9.935  -1.691  28.915 1.00 14.23 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.704  -0.836  29.152 1.00 13.52 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.055  -1.170  30.483 1.00 14.07 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 6.837  -0.361  30.703 1.00 15.88 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 6.836  0.823   31.304 1.00 16.16 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 7.964  1.332   31.789 1.00 16.35 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 5.698  1.487   31.481 1.00 16.22 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.429 -1.982  29.153 1.00 14.56 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.500 -2.939  28.858 1.00 16.53 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 13.944 -4.118  28.031 1.00 16.71 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.217 -5.292  28.326 1.00 18.61 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.180 -3.422  30.140 1.00 19.98 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.391 -2.588  30.444 1.00 25.45 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.178 -3.202  31.584 1.00 28.24 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.748 -2.156  32.412 1.00 28.43 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.444 -1.973  33.704 1.00 28.27 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.536 -2.752  34.303 1.00 28.61 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 17.964 -0.950  34.374 1.00 25.75 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.083 -3.815  27.036 1.00 15.21 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.393 -4.895  26.294 1.00 14.61 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.209 -4.514  24.842 1.00 13.77 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.154 -3.326  24.518 1.00 14.06 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 10.975 -5.115  26.872 1.00 17.90 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.871 -6.082  28.065 1.00 26.07 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.407  -6.338  28.350 1.00 33.75 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.204  -7.487  29.318 1.00 40.17 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.650  -7.139  30.690 1.00 43.45 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.104 -5.504  23.971 1.00 13.27 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.733 -5.295  22.583 1.00 11.96 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.237 -5.598  22.437 1.00 13.59 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.695  -6.559  23.036 1.00 15.14 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.532 -6.244  21.663 1.00 12.18 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.005 -6.019  21.650 1.00 13.75 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.642 -5.224  20.698 1.00 17.04 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 14.929 -6.491  22.503 1.00 14.98 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 15.942 -5.305  20.985 1.00 16.16 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.150 -6.034  22.065 1.00 19.49 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.564  -4.821  21.595 1.00 11.57 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.142  -4.999  21.354 1.00 11.66 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.859  -5.057  19.830 1.00 12.28 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.382  -4.274  19.060 1.00 12.34 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.315  -3.806  21.935 1.00 12.54 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.323  -3.714  23.436 1.00 13.53 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.615  -4.623  24.220 1.00 15.05 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.015  -2.708  24.077 1.00 13.69 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.629  -4.542  25.618 1.00 15.42 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.012  -2.598  25.465 1.00 14.87 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.296  -3.499  26.228 1.00 16.16 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.315  -3.421  27.615 1.00 18.43 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 6.934  -5.920  19.426 1.00 11.52 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.492  -5.932  18.026 1.00 12.00 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.491  -4.772  17.796 1.00 13.50 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.673  -4.421  18.674 1.00 15.45 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.762  -7.288  17.893 1.00 12.94 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.237  -7.552  19.272 1.00 13.79 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.210  -6.920  20.248 1.00 12.19 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.542  -4.195  16.594 1.00 12.70 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.624  -3.080  16.258 1.00 12.97 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.147  -3.145  14.830 1.00 12.27 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.838  -3.632  13.937 1.00 13.45 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.311  -1.687  16.424 1.00 14.88 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.389  -1.282  17.893 1.00 16.24 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.695  -1.671  15.768 1.00 15.87 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.921  -2.633  14.603 1.00 12.73 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.391  -2.324  13.273 1.00 13.11 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.459  -0.754  13.192 1.00 13.81 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 1.999  -0.081  14.116 1.00 14.36 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.938  -2.764  13.152 1.00 16.88 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.935  -4.180  13.180 1.00 24.58 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.121  -0.192  12.176 1.00 12.50 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.316  1.259   12.087 1.00 12.38 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.818  1.829   10.777 1.00 13.03 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.737  1.147   9.745  1.00 14.30 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.797  1.627   12.331 1.00 12.82 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.846  0.878   11.536 1.00 12.47 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.361  -0.327  11.994 1.00 13.06 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.288  1.357   10.306 1.00 13.48 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.346  -1.020  11.270 1.00 13.27 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.275  0.651   9.570  1.00 14.24 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.789  -0.530  10.071 1.00 14.16 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.452  3.138   10.830 1.00 12.58 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.998  3.832   9.634  1.00 13.63 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.150  4.187   8.725  1.00 14.41 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.317  4.186   9.125  1.00 14.34 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.220  5.088   10.007 1.00 15.15 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.052  5.953   10.784 1.00 16.83 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.849  4.375   7.423  1.00 14.44 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.882  4.758   6.456  1.00 15.15 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.440  6.138   6.800  1.00 16.22 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.737  6.970   7.361  1.00 16.17 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.322  4.726   5.012  1.00 17.58 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 3.045  3.319   4.559  1.00 18.71 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.482  3.369   3.132  1.00 25.82 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.391  1.987   2.545  1.00 32.88 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.040  2.054   1.097  1.00 37.14 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.707  6.415   6.458  1.00 15.11 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.289  7.737   6.790  1.00 15.17 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.440  8.897   6.262  1.00 16.20 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.076  8.933   5.083  1.00 18.17 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.674  7.711   6.115  1.00 17.26 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.002  6.256   5.916  1.00 18.96 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.664  5.542   5.752  1.00 15.69 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.110  9.828   7.166  1.00 14.89 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.220  10.917  6.796  1.00 16.55 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.498  12.193  7.613  1.00 16.08 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.364  12.214  8.504  1.00 15.10 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.758  10.457  6.916  1.00 22.23 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.400  10.453  8.277  1.00 29.70 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.745  13.282  7.291  1.00 16.03 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.883  14.589  7.934  1.00 18.08 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.884  14.654  9.080  1.00 18.57 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.671  14.671  8.811  1.00 20.41 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.550  15.657  6.867  1.00 19.88 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 3.910  17.089  7.185  1.00 23.57 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 5.401  17.277  7.393  1.00 23.94 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 3.441  17.995  6.070  1.00 25.20 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.380  14.709  10.343 1.00 17.38 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.544  14.623  11.553 1.00 18.87 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 2.822  15.793  12.465 1.00 18.90 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 3.983  16.099  12.742 1.00 18.65 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.821  13.264  12.263 1.00 21.14 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.444  12.106  11.338 1.00 22.95 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.090  13.171  13.613 1.00 22.49 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.715  10.745  11.842 1.00 24.72 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.772  16.451  12.975 1.00 18.15 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 1.924  17.572  13.894 1.00 18.59 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.509  17.107  15.224 1.00 18.51 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.070  16.100  15.777 1.00 19.08 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.548  18.248  14.132 1.00 20.01 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 0.615  19.391  15.105 1.00 21.83 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.043  20.642  14.700 1.00 23.90 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.332  19.196  16.445 1.00 23.70 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.132  21.696  15.607 1.00 25.64 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.403  20.251  17.342 1.00 24.84 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 0.779  21.495  16.915 1.00 25.02 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.557  17.829  15.713 1.00 18.09 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.189  17.533  16.991 1.00 18.41 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.131  18.822  17.815 1.00 20.64 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 4.623  19.886  17.371 1.00 21.20 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.662  17.021  16.804 1.00 18.48 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 6.353  16.802  18.168 1.00 19.48 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.691  15.718  15.986 1.00 17.63 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 3.609  18.717  19.041 1.00 21.77 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 3.491  19.847  19.958 1.00 21.29 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 4.861  20.418  20.313 1.00 21.20 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 5.854  19.687  20.268 1.00 20.56 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 2.809  19.379  21.267 1.00 24.66 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 1.966  20.455  21.929 1.00 34.26 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.199  19.936  23.134 1.00 44.27 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.907  20.746  24.042 1.00 48.16 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.906  18.718  23.177 1.00 46.57 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 4.904  21.723  20.689 1.00 20.76 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.170  22.340  21.090 1.00 20.45 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 6.826  21.573  22.267 1.00 20.64 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.138  21.046  23.153 1.00 20.82 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 5.943  23.809  21.498 1.00 21.63 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.165  21.494  22.255 1.00 20.23 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 8.945  20.861  23.322 1.00 20.16 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.068 21.864  23.674 1.00 21.33 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 10.133 22.922  23.060 1.00 22.80 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 9.544  19.530  22.813 1.00 21.15 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 10.529 19.734  21.800 1.00 20.04 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.025 21.493  24.552 1.00 22.69 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 12.175 22.384  24.790 1.00 24.54 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 13.120 22.422  23.586 1.00 24.58 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 13.946 23.339  23.481 1.00 25.75 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 12.935 22.046  26.081 1.00 30.89 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.708 20.751  26.011 1.00 40.18 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.999 20.740  26.806 1.00 53.03 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 15.867 21.615  26.574 1.00 57.62 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 15.146 19.836  27.659 1.00 55.97 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.006 21.436  22.666 1.00 23.68 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 13.899 21.321  21.523 1.00 22.32 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 13.411 21.957  20.266 1.00 20.62 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.217 22.360  19.421 1.00 21.96 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 14.198 19.849  21.248 1.00 22.08 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 14.608 19.057  22.479 1.00 22.91 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 13.741 18.149  23.065 1.00 25.29 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.871 19.200  23.037 1.00 23.41 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 14.139 17.366  24.146 1.00 26.77 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 16.269 18.443  24.133 1.00 24.24 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 15.407 17.524  24.682 1.00 27.47 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 15.817 16.781  25.775 1.00 30.93 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.083 22.027  20.091 1.00 19.54 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 11.528 22.572  18.847 1.00 18.93 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.225 23.289  19.092 1.00 20.55 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 9.453  22.876  19.961 1.00 20.72 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.170 21.429  17.854 1.00 17.58 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.286 20.491  17.449 1.00 16.67 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.264 20.891  16.549 1.00 17.74 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.321 19.185  17.903 1.00 15.98 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.234 20.008  16.102 1.00 16.55 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.333 18.305  17.508 1.00 14.98 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.257 18.710  16.577 1.00 15.19 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.260 17.859  16.188 1.00 14.75 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 9.922  24.313  18.282 1.00 22.29 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.585  24.919  18.350 1.00 23.01 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.548  23.913  17.820 1.00 22.55 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.900  22.914  17.158 1.00 22.46 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.719  26.109  17.369 1.00 24.44 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.710  25.587  16.333 1.00 25.81 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.738 24.902  17.200 1.00 23.25 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.253  24.193  18.021 1.00 23.06 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.182  23.381  17.443 1.00 22.57 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.347  23.369  15.907 1.00 21.45 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.709  24.409  15.330 1.00 21.74 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.828  23.966  17.821 1.00 24.13 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.340  22.164  15.300 1.00 20.85 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.636  22.049  13.867 1.00 20.14 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.143  20.700  13.323 1.00 19.90 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 4.747  19.839  14.091 1.00 21.07 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.178  22.157  13.668 1.00 19.61 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 7.918  20.829  14.036 1.00 20.18 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.311  21.047  14.576 1.00 18.80 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.202 19.920  14.266 1.00 17.45 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.188 18.750  14.901 1.00 15.93 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.054 17.796  14.568 1.00 17.27 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.281  18.508  15.835 1.00 17.40 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.191  20.523  12.011 1.00 19.24 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 4.940  19.223  11.412 1.00 19.85 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.305  18.523  11.277 1.00 18.56 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.228  19.073  10.670 1.00 19.85 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.281  19.348  10.042 1.00 20.52 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.856  19.835  10.143 1.00 22.26 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.567  21.192  10.170 1.00 23.87 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 1.818  18.951  10.349 1.00 22.63 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.262  21.653  10.327 1.00 26.54 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 0.496  19.398  10.474 1.00 25.24 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.230  20.748  10.459 1.00 27.73 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.063 21.215  10.606 1.00 31.42 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.412  17.315  11.822 1.00 16.36 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.614  16.512  11.666 1.00 14.91 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.359  15.580  10.458 1.00 13.85 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.328  14.892  10.400 1.00 14.61 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 7.965  15.734  12.926 1.00 14.71 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.169  14.789  12.695 1.00 14.51 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.808  14.345  13.983 1.00 15.32 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 9.883  15.099  14.969 1.00 17.17 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.297 13.083  14.013 1.00 13.50 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.266  15.566  9.492  1.00 14.11 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.139  14.770  8.283  1.00 13.36 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.820  13.402  8.449  1.00 14.55 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.630  13.203  9.385  1.00 14.48 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.738  15.528  7.097  1.00 15.29 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.133 15.728  7.302  1.00 16.66 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.452  12.447  7.572  1.00 13.11 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.052  11.101  7.535  1.00 13.66 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.861  10.382  8.890  1.00 13.50 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.690  9.530   9.251  1.00 12.81 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.550 11.171  7.120  1.00 14.37 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.750 11.771  5.744  1.00 15.71 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.908 10.975  4.616  1.00 17.79 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.835 13.071  5.381  1.00 15.56 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 11.052 11.832  3.591  1.00 18.84 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.020 13.101  4.013  1.00 17.77 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.728  10.640  9.561  1.00 13.50 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.452  10.021  10.866 1.00 12.91 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.424  8.885   10.740 1.00 12.62 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.461  9.003   9.974  1.00 13.29 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 6.876  11.145  11.784 1.00 14.32 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.632  10.782  13.256 1.00 15.80 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 7.938  10.356  14.002 1.00 15.53 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.006  12.057  14.008 1.00 17.96 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.665  7.805   11.488 1.00 12.76 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.783  6.622   11.483 1.00 13.04 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.261  6.410   12.863 1.00 13.58 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.056  6.447   13.802 1.00 14.02 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.603  5.390   11.065 1.00 13.45 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.197  5.561   9.635  1.00 15.62 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.336  4.262   9.154  1.00 17.34 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.667  4.524   10.274 1.00 17.98 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.950  6.242   13.059 1.00 13.34 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.408  6.018   14.412 1.00 13.61 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 2.971  4.579   14.625 1.00 13.53 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.546  3.902   13.682 1.00 12.87 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.150  6.888   14.704 1.00 15.76 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.358  8.387   14.654 1.00 20.16 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.049  9.133   15.052 1.00 22.04 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.506  8.846   15.542 1.00 21.60 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.057  4.141   15.858 1.00 13.10 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.568  2.817   16.227 1.00 12.51 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.048  2.867   17.655 1.00 12.64 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.382  3.777   18.426 1.00 13.69 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.724  1.811   16.183 1.00 14.05 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.221  1.890   18.008 1.00 11.23 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.815  1.718   19.407 1.00 12.69 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.892  0.911   20.133 1.00 13.53 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.250  -0.211  19.728 1.00 14.84 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.536 0.997   19.464 1.00 13.71 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.947 0.754   20.922 1.00 15.08 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.575 1.835   18.739 1.00 13.89 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.425  1.516   21.184 1.00 13.23 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.490  0.911   21.979 1.00 13.22 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 3.939  1.887   23.044 1.00 13.45 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.701  3.095   22.943 1.00 15.10 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.508  1.376   24.128 1.00 13.67 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 4.990  2.229   25.183 1.00 13.42 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.224  3.019   24.794 1.00 13.35 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.177  2.473   24.194 1.00 13.79 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.316  1.416   26.433 1.00 13.69 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 5.799  2.273   27.565 1.00 13.84 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 4.950  3.190   28.179 1.00 14.98 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.067  2.470   28.039 1.00 14.21 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 5.707  3.863   29.047 1.00 16.09 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 6.984  3.441   29.011 1.00 14.82 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.271  4.281   25.182 1.00 13.93 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.482  5.091   25.023 1.00 13.46 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.447  6.266   26.003 1.00 14.98 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.356  6.735   26.378 1.00 15.82 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.720  5.561   23.588 1.00 13.54 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.691  6.442   23.195 1.00 14.64 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 8.654  6.703   26.421 1.00 13.98 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 8.981  7.859   27.251 1.00 14.39 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.147 8.618   26.557 1.00 15.81 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 10.833 8.107   25.679 1.00 16.56 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.443  7.384   28.653 1.00 17.18 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.308  6.683   29.354 1.00 17.85 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 8.652  6.045   30.709 1.00 17.49 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.377  6.679   31.518 1.00 20.83 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.207  4.898   30.946 1.00 17.76 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.338 9.921   26.870 1.00 17.77 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.336 10.738  26.126 1.00 16.97 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.755 10.162  26.002 1.00 17.31 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.349 10.164  24.906 1.00 18.23 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.312 12.072  26.891 1.00 18.32 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 9.907  12.160  27.426 1.00 19.73 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.538  10.729  27.811 1.00 18.17 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 13.224 9.540   27.075 1.00 15.77 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 14.530 8.890   27.091 1.00 15.68 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 14.606 7.660   26.190 1.00 14.82 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 15.692 7.132   25.966 1.00 14.70 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 13.467 7.184   25.633 1.00 13.41 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.499 6.082   24.667 1.00 12.44 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 13.937 6.511   23.276 1.00 11.80 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.204 5.645   22.440 1.00 12.95 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.116 5.404   24.555 1.00 12.53 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 11.783 4.614   25.800 1.00 12.65 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 12.699 4.020   26.366 1.00 13.76 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 10.592 4.645   26.235 1.00 13.62 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.101 7.826   23.036 1.00 11.57 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.542 8.303   21.709 1.00 11.85 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 15.893 7.685   21.347 1.00 11.93 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 16.750 7.558   22.212 1.00 13.21 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.613 9.829   21.670 1.00 12.36 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.008 10.641  21.558 1.00 14.40 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.025 7.239   20.120 1.00 11.20 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.267 6.589   19.680 1.00 11.49 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.152 5.072   19.625 1.00 12.74 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 17.981 4.417   18.999 1.00 13.76 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.131 4.499   20.262 1.00 11.68 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 15.895 3.045   20.162 1.00 11.53 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.609 2.650   18.714 1.00 12.06 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.840 3.320   18.008 1.00 12.19 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.203 1.556   18.288 1.00 11.52 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.027 1.135   16.899 1.00 10.47 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.746 0.335   16.659 1.00 11.47 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.399 -0.568  17.439 1.00 12.40 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.273 0.334   16.480 1.00 13.09 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.443 1.311   16.204 1.00 14.98 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.045 -0.573  15.228 1.00 14.88 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.843 0.532   15.961 1.00 17.06 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.122 0.607   15.515 1.00 10.98 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.013 -0.170  14.924 1.00 11.34 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.640 -0.961  13.765 1.00 12.34 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.340 -0.359  12.913 1.00 12.79 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.956 0.784   14.370 1.00 11.72 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.814 0.109   13.558 1.00 12.79 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.996  -0.872  14.436 1.00 13.35 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.871  1.188   12.935 1.00 13.81 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.425 -2.286  13.753 1.00 12.56 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.987 -3.151  12.717 1.00 14.38 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.910 -4.036  12.155 1.00 13.43 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.055 -4.533  12.886 1.00 13.72 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.987 -4.169  13.359 1.00 19.30 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.110 -3.641  14.196 1.00 26.39 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.965 -4.830  14.672 1.00 26.32 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.697 -5.326  13.523 1.00 29.01 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.865 -4.847  13.127 1.00 26.88 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.508 -3.960  13.867 1.00 24.51 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.397 -5.254  11.991 1.00 23.79 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 13.028 -4.369  10.864 1.00 13.58 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.189 -5.418  10.257 1.00 13.94 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 13.162 -6.544  9.823  1.00 14.19 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.368 -6.474  10.070 1.00 15.85 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.438 -4.858  9.060  1.00 15.44 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.557 -4.330  7.714  1.00 15.24 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.661 -7.592  9.134  1.00 15.51 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.531 -8.680  8.670  1.00 17.22 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.613 -8.231  7.672  1.00 18.40 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.568 -8.988  7.445  1.00 19.70 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.688 -9.804  8.014  1.00 19.50 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 12.009 -9.339  6.733  1.00 24.99 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.978 -10.330 6.246  1.00 34.06 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.764  -10.183 6.472  1.00 37.46 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.440 -11.344 5.549  1.00 33.05 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.531 -7.013  7.114  1.00 16.99 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.494 -6.503  6.112  1.00 17.26 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.594 -5.627  6.700  1.00 16.69 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.596 -5.368  6.023  1.00 18.55 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.784 -5.693  4.988  1.00 17.91 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.666 -6.458  4.328  1.00 18.18 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.332 -6.165  4.571  1.00 19.13 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.721 -7.514  3.463  1.00 21.32 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.618 -7.062  3.896  1.00 22.82 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.400 -7.900  3.223  1.00 23.07 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.419 -5.196  7.955  1.00 14.62 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.400 -4.340  8.601  1.00 14.83 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.778 -3.202  9.390  1.00 13.32 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.612 -3.251  9.770  1.00 14.02 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.574 -2.175  9.624  1.00 13.06 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.132 -1.023  10.412 1.00 13.17 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.160 -0.183  9.611  1.00 11.83 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.458 0.203   8.458  1.00 14.31 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.344 -0.193  10.883 1.00 13.23 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.886 1.099   11.569 1.00 14.71 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.229 -1.032  11.809 1.00 14.59 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.018 0.128   10.226 1.00 12.08 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.973 0.948   9.613  1.00 12.53 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.066 2.428   10.059 1.00 12.77 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.855 3.376   9.284  1.00 13.02 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.589 0.351   9.959  1.00 13.63 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.435 1.242   9.470  1.00 15.42 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.435 -1.057  9.386  1.00 13.39 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.288 2.630   11.371 1.00 11.77 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.302 3.992   11.917 1.00 12.95 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.605 4.009   13.393 1.00 11.68 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 14.974 2.970   13.954 1.00 12.48 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.458 5.199   14.017 1.00 11.13 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.741 5.330   15.444 1.00 11.99 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.587 6.025   16.146 1.00 11.42 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 12.925 6.915   15.581 1.00 10.52 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.071 6.083   15.731 1.00 13.05 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.149 7.436   14.982 1.00 13.48 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.267 5.166   15.455 1.00 14.33 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.427 8.263   15.455 1.00 15.29 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.353 5.693   17.449 1.00 10.87 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.314 6.418   18.211 1.00 9.99  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.598 7.937   18.225 1.00 9.81  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.754 8.336   18.456 1.00 10.31 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.263 5.881   19.654 1.00 10.64 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.254 6.680   20.502 1.00 11.16 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 11.861 4.396   19.683 1.00 11.79 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.568 8.756   17.994 1.00 10.60 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.712 10.204  17.972 1.00 11.64 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.624 10.929  18.766 1.00 12.46 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 10.848 12.066  19.209 1.00 13.57 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.690 10.665  16.509 1.00 11.98 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 11.783 12.092  16.390 1.00 13.05 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.433  10.318  18.946 1.00 12.04 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.347  11.010  19.711 1.00 13.52 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.451  9.899   20.285 1.00 12.79 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 7.766  8.708   20.103 1.00 12.90 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.607  12.070  18.848 1.00 17.56 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.756  12.849  19.729 1.00 19.27 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 6.784  11.447  17.786 1.00 19.00 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.406  10.258  20.984 1.00 14.28 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.471  9.284   21.529 1.00 14.84 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.618  9.894   22.629 1.00 15.06 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.536  11.117  22.765 1.00 16.52 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 3.921  9.050   23.358 1.00 16.06 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.101  9.444   24.504 1.00 16.73 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 1.774  8.773   24.456 1.00 16.52 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.317  8.387   23.367 1.00 17.21 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.138  8.630   25.612 1.00 16.33 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.216 8.081   25.700 1.00 16.97 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.401 6.732   25.028 1.00 16.89 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.487 6.474   24.476 1.00 17.92 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -1.221 9.131   25.144 1.00 19.49 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -1.143 10.392  25.963 1.00 25.32 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.283 10.344  27.173 1.00 27.14 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.868 11.514  25.300 1.00 27.59 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.591  5.855   25.100 1.00 15.35 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.484  4.541   24.476 1.00 14.80 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 0.846  4.536   23.005 1.00 14.44 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.675  3.499   22.359 1.00 16.01 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.437  5.644   22.486 1.00 13.21 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 1.953  5.755   21.129 1.00 12.53 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.483  5.833   21.153 1.00 11.92 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.089  6.261   22.133 1.00 13.06 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.424  7.004   20.386 1.00 13.10 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.105 6.948   20.133 1.00 15.77 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.611 8.329   19.745 1.00 18.80 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.406 5.926   19.006 1.00 16.11 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.086  5.405   20.051 1.00 11.34 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.524  5.564   19.821 1.00 10.82 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.691  6.014   18.361 1.00 11.93 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.031  5.473   17.467 1.00 12.86 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.337  4.295   20.191 1.00 11.16 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.835  3.024   19.485 1.00 13.46 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 7.811  4.545   19.999 1.00 11.84 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.550  7.026   18.129 1.00 11.39 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 6.796  7.567   16.796 1.00 11.96 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.235  7.375   16.380 1.00 11.76 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.130  7.596   17.200 1.00 12.47 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.462  6.922   15.149 1.00 11.10 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.807  6.590   14.646 1.00 11.39 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.155 7.445   13.432 1.00 11.42 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.358  7.570   12.500 1.00 11.69 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.867  5.126   14.179 1.00 11.72 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.376  4.119   15.195 1.00 11.36 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.231 3.632   16.175 1.00 11.94 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.054  3.638   15.150 1.00 12.76 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.778  2.694   17.094 1.00 11.82 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.613  2.670   16.047 1.00 12.27 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.465  2.229   17.050 1.00 11.51 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.368 8.010   13.446 1.00 10.59 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.899 8.746   12.319 1.00 10.64 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.414 7.678   11.331 1.00 10.70 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.377 6.939   11.639 1.00 12.10 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.076 9.631   12.763 1.00 11.23 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.876 7.670   10.092 1.00 10.86 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.318 6.727   9.070  1.00 12.40 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.687 7.092   8.558  1.00 12.50 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.014 8.289   8.399  1.00 12.79 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.315 6.753   7.869  1.00 14.48 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.624 5.724   6.806  1.00 18.75 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.761 4.552   7.147  1.00 18.00 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.753 6.107   5.629  1.00 22.58 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.496 6.048   8.214  1.00 11.34 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.805 6.269   7.586  1.00 11.57 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.923 5.511   6.250  1.00 13.09 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.962 5.600   5.613  1.00 13.98 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.020 5.925   8.488  1.00 13.25 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.022 6.809   9.743  1.00 14.67 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.051 4.433   8.833  1.00 12.66 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.898 4.752   5.836  1.00 12.84 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.986 3.859   4.656  1.00 13.50 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.160 4.585   3.353  1.00 15.38 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.670 3.998   2.378  1.00 16.40 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.764 2.919   4.596  1.00 13.82 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.708 1.898   5.762  1.00 14.92 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.414 1.099   5.633  1.00 14.80 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.274 1.979   5.915  1.00 13.16 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 10.020 1.539   6.029  1.00 14.63 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.723  0.262   5.757  1.00 15.25 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 9.056  2.365   6.425  1.00 15.25 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.740 5.857   3.300  1.00 14.54 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.878 6.633   2.056  1.00 15.88 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.281 7.227   1.870  1.00 16.29 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.569 7.784   0.804  1.00 16.94 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.840 7.765   2.021  1.00 16.38 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.999 8.787   3.113  1.00 19.91 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.167 8.388   4.266  1.00 18.08 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.959 9.999   2.809  1.00 22.50 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.129 7.202   2.902  1.00 15.59 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.464 7.837   2.834  1.00 14.65 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.405 6.863   2.185  1.00 15.26 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.191 6.177   2.844  1.00 16.30 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.895 8.192   4.270  1.00 14.60 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.913 9.157   4.997  1.00 15.74 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.360 9.398   6.453  1.00 16.20 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.770 10.470  4.291  1.00 15.88 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.314 6.766   0.845  1.00 15.60 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 20.090 5.723   0.144  1.00 16.61 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.583 5.907   0.231  1.00 18.19 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.340 4.919   0.137  1.00 19.61 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.671 5.636   -1.327 1.00 17.29 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 18.170 5.589   -1.606 1.00 19.48 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.925 5.368   -3.115 1.00 21.14 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.456 4.472   -0.774 1.00 19.34 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 22.014 7.173   0.391  1.00 17.82 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.425 7.527   0.472  1.00 18.24 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.112 6.960   1.731  1.00 19.88 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.347 6.946   1.793  1.00 21.43 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.602 9.052   0.356  1.00 18.78 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.806 9.849   1.351  1.00 17.69 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.560 10.390  1.178  1.00 18.49 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.197 10.164  2.696  1.00 16.94 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.174 11.055  2.323  1.00 18.36 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.176 10.960  3.256  1.00 17.75 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.353 9.931   3.445  1.00 17.69 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.247 11.461  4.566  1.00 17.11 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.446 10.459  4.726  1.00 17.74 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.407 11.234  5.256  1.00 17.63 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.337 6.474   2.740  1.00 18.68 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.974 5.914   3.940  1.00 20.05 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.798 4.656   3.607  1.00 24.03 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.720 4.326   4.360  1.00 25.28 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.918 5.538   4.997  1.00 18.99 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.233 6.675   5.733  1.00 17.77 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.113 6.089   6.621  1.00 17.97 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.240 7.491   6.622  1.00 17.58 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.442 3.955   2.488  1.00 27.80 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.036 2.706   1.977  1.00 33.55 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.261 2.884   1.130  1.00 38.34 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.770 1.875   0.652  1.00 40.17 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.049 1.967   1.057  1.00 37.52 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.830 1.408   1.691  1.00 45.67 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.868 1.136   2.903  1.00 48.10 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.824 1.227   0.973  1.00 50.92 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.682 4.109   0.843  1.00 41.21 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.898 4.339   0.059  1.00 44.35 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.779 5.390   0.722  1.00 46.53 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.935 5.556   0.330  1.00 48.26 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 27.587 4.727   -1.399 1.00 46.89 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 26.472 5.745   -1.552 1.00 52.71 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 25.264 5.179   -2.270 1.00 60.37 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.610 5.931   -3.030 1.00 62.07 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.983 3.973   -2.084 1.00 62.23 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 15.166 -23.958 8.620  1.00 20.69 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 14.029 -23.809 9.539  1.00 20.48 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 14.007 -24.944 10.571 1.00 19.66 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 14.601 -26.016 10.351 1.00 21.25 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 12.702 -23.762 8.773  1.00 22.37 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 12.500 -24.988 8.081  1.00 26.81 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 13.278 -24.749 11.661 1.00 17.26 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 13.115 -25.778 12.679 1.00 16.28 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 12.869 -25.185 14.048 1.00 15.25 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 13.243 -24.030 14.305 1.00 16.19 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 12.241 -25.942 14.938 1.00 14.51 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 11.938 -25.474 16.310 1.00 14.59 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 11.980 -26.630 17.297 1.00 14.65 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 11.979 -27.803 16.886 1.00 15.93 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 10.534 -24.823 16.334 1.00 15.72 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 12.050 -26.303 18.602 1.00 14.11 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 11.929 -27.264 19.690 1.00 13.43 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 10.573 -27.055 20.356 1.00 13.57 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 10.174 -25.926 20.604 1.00 13.48 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 13.055 -27.028 20.715 1.00 13.86 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 14.433 -27.072 20.070 1.00 14.15 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 12.955 -28.067 21.842 1.00 14.67 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 15.528 -26.431 21.005 1.00 15.82 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 9.837  -28.120 20.623 1.00 14.39 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 8.516  -28.074 21.241 1.00 15.32 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 8.576  -28.818 22.560 1.00 16.05 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 8.739  -30.036 22.563 1.00 16.70 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 7.476  -28.737 20.298 1.00 15.90 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 7.286  -27.949 19.014 1.00 15.44 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 6.464  -26.830 18.979 1.00 16.41 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 8.057  -28.220 17.891 1.00 16.89 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 6.354  -26.052 17.832 1.00 18.20 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 7.945  -27.451 16.729 1.00 17.88 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 7.069  -26.385 16.697 1.00 19.09 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 6.981  -25.569 15.586 1.00 21.23 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 8.545  -28.098 23.690 1.00 17.21 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 8.642  -28.709 25.006 1.00 18.05 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 7.527  -28.101 25.871 1.00 18.17 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 7.376  -26.886 25.925 1.00 17.43 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 10.066 -28.521 25.605 1.00 19.63 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 10.539 -27.078 25.493 1.00 20.17 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 10.130 -29.018 27.043 1.00 20.66 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 6.655  -28.930 26.459 1.00 19.60 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 5.555  -28.422 27.290 1.00 19.76 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 4.672  -27.479 26.499 1.00 19.51 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 4.322  -27.800 25.365 1.00 20.78 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 4.391  -26.275 27.011 1.00 19.63 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 3.629  -25.294 26.217 1.00 20.37 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 4.527  -24.207 25.649 1.00 17.91 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 4.114  -23.045 25.526 1.00 18.69 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 2.464  -24.709 26.992 1.00 24.16 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 1.388  -25.754 27.232 1.00 32.01 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 0.649  -26.160 26.316 1.00 35.33 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 1.305  -26.222 28.444 1.00 32.86 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 5.728  -24.598 25.219 1.00 16.58 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 6.685  -23.652 24.648 1.00 16.20 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 7.177  -24.108 23.272 1.00 15.71 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 7.356  -25.302 23.005 1.00 16.30 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 7.923  -23.561 25.562 1.00 16.53 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 7.643  -22.999 26.934 1.00 18.06 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 6.983  -21.784 27.087 1.00 19.64 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 8.046  -23.674 28.077 1.00 19.10 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 6.713  -21.264 28.351 1.00 21.12 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 7.812  -23.145 29.348 1.00 20.41 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 7.164  -21.928 29.473 1.00 22.17 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 6.912  -21.382 30.719 1.00 25.92 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 7.477  -23.129 22.425 1.00 13.30 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 8.103  -23.342 21.097 1.00 13.40 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 9.371  -22.480 21.121 1.00 13.44 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 9.305  -21.278 21.399 1.00 14.65 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 7.129  -22.895 19.978 1.00 14.24 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 7.779  -22.626 18.618 1.00 15.64 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 6.766  -22.324 17.521 1.00 15.30 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 7.221  -21.297 16.546 1.00 16.09 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 7.722  -21.542 15.333 1.00 16.61 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 7.971  -22.803 14.944 1.00 16.06 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 8.061  -20.534 14.527 1.00 16.94 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 10.544 -23.110 20.892 1.00 12.99 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 11.837 -22.422 20.862 1.00 12.32 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 12.257 -22.332 19.399 1.00 12.40 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 12.408 -23.368 18.725 1.00 13.61 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 12.899 -23.208 21.666 1.00 14.05 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 14.157 -22.363 21.779 1.00 15.02 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 12.379 -23.639 23.038 1.00 15.12 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 12.529 -21.103 18.928 1.00 12.08 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 12.940 -20.916 17.537 1.00 13.41 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 14.146 -19.967 17.492 1.00 12.14 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 14.393 -19.209 18.444 1.00 12.47 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 11.770 -20.304 16.703 1.00 15.51 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 10.683 -21.328 16.500 1.00 20.34 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 11.241 -19.000 17.320 1.00 14.30 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 14.825 -19.914 16.341 1.00 12.21 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 15.841 -18.878 16.141 1.00 12.07 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 15.098 -17.521 16.166 1.00 12.68 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 14.075 -17.356 15.456 1.00 12.66 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 16.513 -18.991 14.756 1.00 12.37 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.378 -20.209 14.613 1.00 13.57 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 16.918 -21.263 14.154 1.00 13.42 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 18.629 -20.106 15.048 1.00 13.00 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 15.606 -16.558 16.948 1.00 12.09 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 14.909 -15.267 17.056 1.00 11.63 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 14.764 -14.601 15.671 1.00 12.75 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 13.708 -14.040 15.377 1.00 12.95 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 15.661 -14.360 18.019 1.00 12.05 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 14.882 -13.060 18.387 1.00 12.49 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 15.835 -12.142 19.153 1.00 13.51 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 15.221 -10.889 19.663 1.00 13.14 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 15.123 -9.768  18.982 1.00 15.31 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 15.370 -9.751  17.673 1.00 16.69 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 14.638 -8.672  19.568 1.00 15.90 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 15.787 -14.777 14.784 1.00 12.49 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 15.698 -14.132 13.470 1.00 13.48 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 14.660 -14.767 12.561 1.00 14.20 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 14.338 -14.165 11.537 1.00 15.56 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.108 -14.042 12.795 1.00 13.36 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.660 -15.336 12.269 1.00 13.38 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 18.309 -16.232 13.081 1.00 13.97 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.646 -15.828 10.998 1.00 14.61 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 18.713 -17.247 12.289 1.00 14.60 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 18.326 -17.054 11.025 1.00 15.56 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 14.159 -15.969 12.897 1.00 13.69 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 13.125 -16.616 12.073 1.00 14.10 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 11.746 -16.594 12.749 1.00 15.51 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 10.820 -17.215 12.251 1.00 16.50 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 13.556 -18.104 11.793 1.00 14.35 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 14.869 -18.228 10.994 1.00 15.00 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 15.238 -19.724 10.764 1.00 16.53 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 14.762 -17.489 9.622  1.00 15.93 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 11.611 -15.872 13.882 1.00 14.83 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 10.335 -15.834 14.590 1.00 15.21 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 9.258  -15.196 13.722 1.00 15.22 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 9.534  -14.265 12.974 1.00 15.66 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 10.478 -15.079 15.917 1.00 14.92 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 8.057  -15.737 13.821 1.00 15.16 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 6.910  -15.256 13.044 1.00 16.16 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 6.123  -14.160 13.790 1.00 15.99 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 6.331  -13.955 14.993 1.00 15.62 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 5.971  -16.435 12.724 1.00 17.05 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 5.371  -16.904 13.934 1.00 17.74 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 6.676  -17.564 11.984 1.00 16.78 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 5.118  -13.547 13.122 1.00 16.27 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 4.226  -12.605 13.810 1.00 16.21 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 3.511  -13.315 14.977 1.00 16.20 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 3.364  -12.731 16.055 1.00 16.64 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 3.114  -12.152 12.822 1.00 17.94 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 3.609  -11.310 11.690 1.00 24.19 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 4.602  -10.350 11.864 1.00 28.25 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 3.219  -11.303 10.398 1.00 26.94 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 4.782  -9.794  10.675 1.00 28.94 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 3.980  -10.332 9.759  1.00 28.40 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 3.106  -14.591 14.764 1.00 15.50 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 2.421  -15.316 15.846 1.00 15.97 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 3.353  -15.552 17.035 1.00 15.62 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 2.925  -15.488 18.199 1.00 15.80 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 1.836  -16.639 15.357 1.00 18.11 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 1.007  -17.340 16.427 1.00 22.32 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? -0.123 -16.892 16.740 1.00 23.93 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 1.543  -18.434 17.014 1.00 23.47 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 4.663  -15.860 16.767 1.00 15.42 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 5.616  -16.036 17.880 1.00 15.17 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 5.713  -14.749 18.722 1.00 15.07 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 5.647  -14.787 19.959 1.00 15.74 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 7.015  -16.374 17.306 1.00 15.28 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 7.163  -17.789 16.782 1.00 16.53 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 6.552  -18.719 17.378 1.00 16.17 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 7.858  -17.963 15.748 1.00 16.05 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 5.848  -13.597 18.036 1.00 15.81 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 5.941  -12.327 18.739 1.00 16.73 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 4.637  -11.951 19.476 1.00 17.61 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 4.710  -11.331 20.537 1.00 18.76 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 6.384  -11.206 17.776 1.00 15.97 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 7.864  -11.168 17.577 1.00 14.75 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 8.568  -11.658 16.513 1.00 15.35 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 8.826  -10.567 18.465 1.00 14.89 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 9.915  -11.415 16.692 1.00 15.80 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 10.097 -10.742 17.882 1.00 15.19 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 8.734  -9.931  19.708 1.00 16.36 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 11.267 -10.263 18.478 1.00 15.91 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 9.902  -9.503  20.328 1.00 17.12 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 11.147 -9.660  19.703 1.00 16.18 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 3.478  -12.357 18.956 1.00 16.20 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 2.204  -12.041 19.622 1.00 17.34 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 1.996  -12.930 20.865 1.00 17.72 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 1.059  -12.687 21.638 1.00 19.41 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 1.046  -12.233 18.642 1.00 16.94 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 2.707  -14.070 20.941 1.00 16.80 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 2.599  -15.008 22.056 1.00 16.80 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 3.979  -15.155 22.730 1.00 16.40 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 4.381  -16.225 23.155 1.00 16.65 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 2.112  -16.356 21.531 1.00 18.25 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 0.672  -16.241 21.081 1.00 20.17 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? -0.271 -16.197 21.904 1.00 19.55 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 0.482  -16.076 19.769 1.00 19.67 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 4.664  -14.049 22.861 1.00 16.77 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 6.039  -14.027 23.371 1.00 15.94 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 6.174  -14.404 24.847 1.00 17.40 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 5.469  -13.844 25.701 1.00 18.88 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 6.596  -12.615 23.141 1.00 15.99 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 8.036  -12.392 23.618 1.00 16.70 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 9.029  -13.228 22.807 1.00 16.98 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 8.397  -10.909 23.528 1.00 17.29 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 7.096  -15.320 25.171 1.00 15.50 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 7.421  -15.680 26.547 1.00 16.19 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 8.770  -15.023 26.922 1.00 16.68 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 8.925  -14.432 27.999 1.00 18.25 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 7.503  -17.228 26.697 1.00 17.30 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 8.049  -17.601 28.087 1.00 18.41 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 6.118  -17.863 26.437 1.00 18.00 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 9.776  -15.178 26.056 1.00 14.81 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 11.120 -14.681 26.321 1.00 14.95 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 11.874 -14.582 25.013 1.00 15.05 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 11.695 -15.434 24.138 1.00 15.32 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 11.844 -15.664 27.284 1.00 16.72 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 13.323 -15.449 27.472 1.00 16.66 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 13.940 -14.587 28.327 1.00 19.05 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 14.371 -16.176 26.803 1.00 15.50 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 15.318 -14.717 28.210 1.00 19.69 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 15.602 -15.693 27.289 1.00 17.16 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 14.383 -17.200 25.847 1.00 16.32 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 16.833 -16.253 26.905 1.00 17.01 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 15.606 -17.734 25.455 1.00 16.40 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 16.813 -17.242 25.962 1.00 15.72 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 12.743 -13.588 24.866 1.00 14.62 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 13.625 -13.498 23.712 1.00 15.44 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 14.953 -12.883 24.136 1.00 15.10 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 15.009 -12.075 25.068 1.00 14.94 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 12.974 -12.729 22.539 1.00 15.99 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 12.433 -11.347 22.912 1.00 16.87 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 13.444 -10.206 22.992 1.00 19.49 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 13.221 -9.230  23.753 1.00 19.76 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 14.465 -10.256 22.269 1.00 16.89 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 16.035 -13.237 23.420 1.00 14.50 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.353 -12.709 23.715 1.00 14.40 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 18.129 -12.604 22.410 1.00 13.86 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 18.545 -13.619 21.820 1.00 13.26 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 18.049 -13.609 24.752 1.00 14.96 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 19.380 -13.126 25.232 1.00 18.96 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 20.091 -12.534 24.453 1.00 21.75 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 19.750 -13.452 26.379 1.00 19.68 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 18.300 -11.348 21.917 1.00 13.34 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 19.018 -11.085 20.679 0.50 12.86 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 18.997 -11.134 20.661 0.50 13.19 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 20.452 -11.583 20.765 1.00 13.72 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 20.971 -12.069 19.769 1.00 14.18 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 19.059 -9.586  20.402 0.50 14.07 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 18.926 -9.667  20.238 0.50 15.32 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 17.754 -9.094  20.194 0.50 18.05 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 19.601 -8.855  21.179 0.50 19.42 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 21.077 -11.459 21.971 1.00 12.78 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 22.485 -11.899 22.068 1.00 12.94 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 22.616 -13.409 21.889 1.00 13.89 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 23.719 -13.853 21.560 1.00 14.41 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 23.107 -11.485 23.397 1.00 16.08 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 22.692 -12.279 24.502 1.00 21.24 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 21.551 -14.177 22.091 1.00 12.54 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 21.591 -15.654 21.928 1.00 11.89 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 20.948 -16.119 20.607 1.00 11.60 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 20.984 -17.327 20.297 1.00 12.22 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 20.825 -16.320 23.089 1.00 11.99 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 21.554 -16.101 24.418 1.00 13.29 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 20.854 -16.755 25.621 1.00 13.06 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 20.892 -18.205 25.512 1.00 12.65 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 20.843 -19.028 26.556 1.00 13.51 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 20.782 -18.547 27.805 1.00 15.11 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 20.960 -20.338 26.378 1.00 14.65 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 20.306 -15.215 19.849 1.00 12.21 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 19.484 -15.599 18.679 1.00 11.91 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 18.381 -16.588 19.058 1.00 11.75 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 18.046 -17.453 18.266 1.00 12.09 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 20.312 -16.103 17.468 1.00 12.57 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 19.518 -16.395 16.204 1.00 12.31 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 18.625 -15.578 15.851 1.00 13.38 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 19.777 -17.459 15.551 1.00 12.42 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 17.772 -16.426 20.249 1.00 11.53 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 16.645 -17.295 20.630 1.00 11.13 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 15.381 -16.520 20.934 1.00 11.99 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 15.412 -15.423 21.502 1.00 12.56 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 16.978 -18.109 21.888 1.00 12.04 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 18.054 -19.194 21.724 1.00 13.32 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 18.278 -19.901 23.095 1.00 14.55 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.660 -20.223 20.678 1.00 14.24 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 14.238 -17.147 20.638 1.00 11.32 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 12.917 -16.628 21.027 1.00 11.97 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 12.069 -17.829 21.432 1.00 12.41 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 12.136 -18.881 20.804 1.00 12.81 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 12.293 -15.817 19.891 1.00 12.07 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 10.931 -15.177 20.229 1.00 12.23 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 10.772 -13.806 19.518 1.00 13.50 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 9.749  -16.117 19.824 1.00 13.68 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 11.279 -17.671 22.492 1.00 12.20 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 10.376 -18.708 22.991 1.00 12.24 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 8.958  -18.100 22.994 1.00 12.87 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 8.718  -16.991 23.536 1.00 13.47 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 10.749 -19.189 24.408 1.00 12.70 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 9.713  -20.206 24.920 1.00 14.68 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 12.148 -19.814 24.386 1.00 13.17 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 8.016  -18.818 22.353 1.00 13.49 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 6.608  -18.415 22.347 1.00 13.69 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 5.758  -19.504 23.020 1.00 15.60 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 6.188  -20.653 23.166 1.00 15.94 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 6.143  -18.157 20.922 1.00 14.81 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 6.301  -19.298 20.078 1.00 15.90 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 4.527  -19.125 23.411 1.00 15.77 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 3.625  -20.070 24.055 1.00 17.78 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 2.779  -20.815 23.002 1.00 20.42 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 2.470  -20.285 21.919 1.00 20.56 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 2.725  -19.334 25.043 1.00 19.01 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 1.955  -18.369 24.354 1.00 23.35 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 2.418  -22.072 23.333 1.00 21.72 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 1.635  -22.921 22.425 1.00 24.36 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 0.393  -23.455 23.141 1.00 26.81 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 0.398  -23.561 24.361 1.00 27.74 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 2.466  -24.170 21.984 1.00 26.11 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 2.667  -25.058 23.080 1.00 27.91 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 3.830  -23.821 21.397 1.00 27.17 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? -0.635 -23.856 22.385 1.00 28.76 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? -1.807 -24.497 22.974 1.00 30.74 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? -1.591 -26.023 23.065 1.00 31.28 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? -2.102 -26.670 23.991 1.00 33.36 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? -3.089 -24.131 22.207 1.00 32.98 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? -2.874 -24.387 20.816 1.00 35.73 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? -3.480 -22.657 22.400 1.00 33.75 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? -0.843 -26.609 22.122 1.00 29.68 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? -0.582 -28.047 22.106 1.00 29.53 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 0.627  -28.415 22.970 1.00 28.39 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 1.540  -27.617 23.110 1.00 28.52 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? -0.352 -28.517 20.681 1.00 29.96 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 0.648  -29.633 23.501 1.00 27.26 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 1.726  -30.125 24.355 1.00 26.51 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 2.902  -30.606 23.511 1.00 25.71 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 2.744  -31.436 22.616 1.00 26.84 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 1.186  -31.266 25.247 1.00 29.08 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 2.225  -31.971 26.114 1.00 34.82 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 2.694  -31.160 27.304 1.00 42.82 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 2.092  -30.143 27.686 1.00 46.15 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 3.774  -31.606 27.930 1.00 44.99 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 4.084  -30.075 23.818 1.00 22.62 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 5.320  -30.451 23.131 1.00 22.03 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 5.941  -31.641 23.811 1.00 22.45 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 5.940  -31.724 25.045 1.00 23.98 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 6.549  -32.513 23.025 1.00 20.54 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 7.098  -33.745 23.553 1.00 20.95 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 8.612  -33.894 23.417 1.00 20.39 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 9.128  -35.010 23.638 1.00 21.27 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 6.362  -34.935 22.944 1.00 23.15 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 4.595  -35.007 23.360 1.00 27.53 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 9.335  -32.808 23.103 1.00 17.05 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 10.803 -32.910 23.060 1.00 16.49 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 11.333 -32.888 24.495 1.00 17.54 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 10.792 -32.198 25.361 1.00 19.62 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 11.468 -31.752 22.261 1.00 17.48 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 11.120 -31.783 20.788 1.00 21.70 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 10.790 -32.872 20.273 1.00 23.67 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 11.189 -30.727 20.138 1.00 20.11 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 12.373 -33.637 24.734 1.00 17.51 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 13.053 -33.650 26.025 1.00 18.68 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 14.281 -32.747 25.864 1.00 16.53 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 15.063 -32.969 24.937 1.00 18.25 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 13.520 -35.096 26.344 1.00 23.30 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 12.351 -35.896 26.641 1.00 25.34 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 14.487 -35.150 27.537 1.00 24.59 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 14.538 -31.836 26.812 1.00 15.66 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 15.738 -30.992 26.765 1.00 15.04 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 16.845 -31.663 27.554 1.00 14.12 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 16.627 -32.142 28.691 1.00 15.42 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 15.465 -29.592 27.353 1.00 16.44 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 14.234 -28.934 26.699 1.00 19.00 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 16.721 -28.682 27.226 1.00 16.49 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 14.385 -28.737 25.182 1.00 21.29 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 18.045 -31.765 26.968 1.00 13.67 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 19.195 -32.350 27.690 1.00 13.69 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 19.620 -31.428 28.833 1.00 12.81 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 19.587 -30.192 28.707 1.00 12.75 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 20.350 -32.503 26.719 1.00 13.51 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 20.002 -32.045 29.972 1.00 12.52 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 20.513 -31.302 31.155 1.00 12.43 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 21.849 -31.967 31.475 1.00 12.49 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 21.907 -33.000 32.171 1.00 14.57 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 19.531 -31.349 32.350 1.00 12.66 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 18.136 -30.854 31.997 1.00 14.06 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 18.130 -29.362 31.603 1.00 14.95 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 16.744 -28.914 31.338 1.00 15.81 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 16.404 -27.801 30.700 1.00 16.82 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.331 -26.962 30.284 1.00 15.03 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 15.121 -27.519 30.477 1.00 18.80 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 22.914 -31.437 30.868 1.00 11.80 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 24.221 -32.090 30.828 1.00 12.62 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 25.321 -31.162 30.336 1.00 13.59 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 25.025 -30.052 29.900 1.00 13.18 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 24.105 -33.292 29.892 1.00 12.13 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 23.964 -32.832 28.139 1.00 12.70 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 26.565 -31.674 30.307 1.00 13.58 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 27.702 -30.971 29.725 1.00 14.38 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 28.329 -31.795 28.574 1.00 13.62 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 29.527 -31.656 28.292 1.00 13.55 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 28.753 -30.575 30.769 1.00 16.84 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 29.453 -31.739 31.397 1.00 18.86 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 29.078 -32.906 31.122 1.00 20.61 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 30.411 -31.506 32.186 1.00 25.71 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 27.513 -32.569 27.837 1.00 12.69 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 28.010 -33.317 26.664 1.00 12.90 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 28.676 -32.401 25.675 1.00 12.69 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 28.286 -31.230 25.500 1.00 12.27 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 26.858 -34.022 25.955 1.00 13.14 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 26.278 -35.512 26.798 1.00 14.36 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 29.679 -32.957 25.011 1.00 11.41 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 30.409 -32.325 23.898 1.00 12.15 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 30.420 -33.220 22.680 1.00 12.34 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 31.222 -33.012 21.768 1.00 12.62 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 31.862 -31.927 24.286 1.00 11.55 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 31.855 -30.629 25.144 1.00 12.59 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 33.274 -30.246 25.440 1.00 15.01 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 33.751 -30.413 26.579 1.00 17.68 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 33.993 -29.783 24.432 1.00 14.00 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 29.527 -34.232 22.595 1.00 12.05 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 29.360 -35.028 21.384 1.00 13.10 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 27.850 -35.212 21.208 1.00 13.64 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 27.064 -35.281 22.180 1.00 14.46 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 30.090 -36.358 21.390 1.00 18.53 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 29.542 -37.218 22.386 1.00 21.16 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 31.558 -36.245 21.628 1.00 21.61 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 27.458 -35.248 19.933 1.00 12.92 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 26.047 -35.375 19.602 1.00 12.63 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 25.815 -35.513 18.106 1.00 10.71 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 26.758 -35.750 17.368 1.00 12.58 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 24.562 -35.373 17.678 1.00 10.59 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 24.193 -35.542 16.261 1.00 10.67 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 23.319 -34.359 15.890 1.00 12.07 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 22.371 -34.056 16.619 1.00 12.05 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 23.408 -36.876 16.064 1.00 11.89 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 22.944 -37.007 14.597 1.00 13.95 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 24.273 -38.080 16.441 1.00 13.28 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 23.592 -33.707 14.707 1.00 11.50 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 22.692 -32.634 14.279 1.00 10.71 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 22.076 -32.923 12.913 1.00 11.72 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 22.643 -33.665 12.093 1.00 12.19 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 23.382 -31.229 14.261 1.00 11.74 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 24.327 -30.987 13.099 1.00 11.88 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 25.611 -31.544 13.085 1.00 12.48 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 23.963 -30.155 12.041 1.00 11.87 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 26.498 -31.297 12.037 1.00 14.21 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 24.842 -29.912 10.978 1.00 12.11 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 26.094 -30.513 10.969 1.00 14.12 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 27.013 -30.264 9.972  1.00 15.86 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 20.896 -32.336 12.675 1.00 12.10 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 20.256 -32.449 11.390 1.00 12.54 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 20.692 -31.297 10.488 1.00 12.32 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 20.555 -30.128 10.854 1.00 11.90 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 18.722 -32.525 11.524 1.00 12.71 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 18.080 -32.663 10.165 1.00 14.28 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 18.227 -33.824 9.427  1.00 14.13 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.328 -31.633 9.622  1.00 16.15 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.672 -33.953 8.146  1.00 16.58 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 16.775 -31.743 8.342  1.00 16.94 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 16.936 -32.909 7.625  1.00 18.38 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 16.410 -33.016 6.339  1.00 20.81 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 21.128 -31.662 9.281  1.00 12.19 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 21.583 -30.695 8.269  1.00 12.03 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 20.600 -30.751 7.049  1.00 13.45 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 20.650 -31.678 6.224  1.00 15.57 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 23.012 -31.028 7.873  1.00 12.54 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 23.612 -30.024 6.477  1.00 15.02 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 19.705 -29.750 6.968  1.00 13.87 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 18.704 -29.761 5.900  1.00 15.80 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 19.307 -29.633 4.523  1.00 16.11 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 18.818 -30.283 3.585  1.00 16.27 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.641 -28.713 6.154  1.00 20.82 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 18.182 -27.425 6.060  1.00 28.05 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 20.441 -28.907 4.385  1.00 15.00 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 21.089 -28.745 3.062  1.00 15.63 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 21.781 -29.990 2.531  1.00 16.47 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 22.263 -30.004 1.377  1.00 17.60 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 22.057 -27.573 3.094  1.00 16.05 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 23.138 -27.833 3.977  1.00 15.02 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 21.807 -31.074 3.326  1.00 14.90 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 22.304 -32.382 2.912  1.00 14.26 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 21.246 -33.476 3.138  1.00 15.29 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 21.526 -34.665 2.833  1.00 17.11 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 23.581 -32.729 3.695  1.00 15.64 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 24.730 -31.809 3.377  1.00 17.12 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 25.306 -32.130 1.997  1.00 19.03 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 26.468 -31.291 1.711  1.00 22.03 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 26.421 -30.134 1.077  1.00 24.51 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 25.258 -29.652 0.634  1.00 23.92 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 27.537 -29.452 0.854  1.00 26.74 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 20.074 -33.123 3.727  1.00 16.79 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 19.031 -34.092 4.137  1.00 18.47 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 19.655 -35.225 4.936  1.00 20.31 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 19.388 -36.407 4.680  1.00 21.68 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 18.296 -34.619 2.887  1.00 22.56 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 16.978 -33.924 2.721  1.00 31.36 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 16.892 -32.962 1.591  1.00 39.13 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 16.855 -31.608 2.129  1.00 43.73 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 15.879 -30.737 1.930  1.00 44.29 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 14.842 -31.055 1.163  1.00 45.21 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 15.938 -29.530 2.481  1.00 42.49 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 20.571 -34.875 5.882  1.00 19.20 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 21.332 -35.917 6.572  1.00 18.39 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 21.604 -35.495 8.000  1.00 15.61 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 21.676 -34.292 8.283  1.00 14.65 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 22.737 -36.083 5.909  1.00 22.00 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 22.817 -37.100 4.781  1.00 32.85 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 24.274 -37.323 4.426  1.00 41.18 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 24.487 -38.504 3.498  1.00 47.81 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 23.987 -38.217 2.129  1.00 51.31 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 21.802 -36.458 8.880  1.00 14.08 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 22.262 -36.229 10.249 1.00 13.06 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 23.746 -36.486 10.278 1.00 15.64 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 24.262 -37.472 9.663  1.00 18.35 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 21.557 -37.182 11.217 1.00 13.69 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 20.085 -36.937 11.353 1.00 14.63 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 19.540 -36.173 12.374 1.00 17.57 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 19.082 -37.397 10.571 1.00 14.57 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 18.222 -36.218 12.198 1.00 16.47 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 17.905 -36.929 11.126 1.00 18.51 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 24.468 -35.667 11.064 1.00 12.84 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 25.902 -35.856 11.197 1.00 12.72 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 26.292 -35.924 12.673 1.00 12.48 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 25.909 -35.056 13.461 1.00 12.83 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 26.689 -34.679 10.570 1.00 13.98 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 26.580 -34.579 9.073  1.00 16.08 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 27.263 -35.458 8.254  1.00 17.63 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 25.843 -33.559 8.471  1.00 17.13 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 27.193 -35.357 6.873  1.00 18.38 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 25.751 -33.463 7.088  1.00 18.18 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 26.432 -34.360 6.296  1.00 19.91 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 26.361 -34.266 4.908  1.00 22.70 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 27.153 -36.892 13.046 1.00 12.22 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 27.700 -36.920 14.398 1.00 11.78 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 28.862 -35.918 14.494 1.00 13.45 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 29.734 -35.901 13.599 1.00 15.78 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 28.208 -38.361 14.544 1.00 13.24 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 28.547 -38.785 13.169 1.00 13.62 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 27.641 -38.016 12.208 1.00 12.41 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 28.910 -35.119 15.580 1.00 12.18 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 30.010 -34.142 15.762 1.00 12.59 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 30.426 -34.042 17.210 1.00 12.25 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 29.624 -34.264 18.121 1.00 14.19 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 29.551 -32.726 15.307 1.00 15.06 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 29.499 -32.591 13.769 1.00 16.70 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 28.252 -32.275 15.981 1.00 15.60 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 31.680 -33.594 17.426 1.00 12.14 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 32.096 -33.077 18.704 1.00 12.52 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 31.827 -31.526 18.653 1.00 11.68 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 31.911 -30.900 17.575 1.00 12.81 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 33.599 -33.249 18.913 1.00 14.57 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 33.917 -34.631 18.955 1.00 20.65 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 31.504 -30.923 19.796 1.00 10.91 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 31.201 -29.498 19.833 1.00 11.49 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 31.776 -28.863 21.089 1.00 11.95 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 32.045 -29.537 22.097 1.00 12.99 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 29.678 -29.211 19.623 1.00 11.90 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 28.747 -29.926 20.584 1.00 11.04 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 28.270 -31.193 20.302 1.00 12.06 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 28.326 -29.305 21.756 1.00 12.32 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 27.403 -31.848 21.179 1.00 11.86 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 27.428 -29.939 22.619 1.00 11.81 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 27.005 -31.222 22.351 1.00 11.59 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 31.990 -27.529 21.018 1.00 10.97 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 32.624 -26.827 22.127 1.00 12.39 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 31.679 -26.486 23.282 1.00 12.58 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 30.483 -26.820 23.261 1.00 13.27 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 33.310 -25.568 21.564 1.00 12.97 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 32.345 -24.639 21.082 1.00 14.47 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 32.231 -25.864 24.331 1.00 12.97 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 31.408 -25.434 25.445 1.00 14.04 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 30.732 -24.090 25.100 1.00 14.28 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 31.368 -23.234 24.456 1.00 16.24 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 32.280 -25.267 26.694 1.00 15.41 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 33.022 -26.556 27.026 1.00 17.86 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 33.923 -26.308 28.255 1.00 26.53 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 34.462 -27.569 28.879 1.00 35.90 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 35.164 -27.237 30.150 1.00 40.19 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 29.503 -23.839 25.592 1.00 13.30 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 28.817 -22.559 25.273 1.00 13.54 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 29.661 -21.337 25.642 1.00 15.00 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 30.186 -21.240 26.772 1.00 17.21 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 27.512 -22.612 26.062 1.00 15.51 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 27.280 -24.080 26.334 1.00 18.26 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 28.657 -24.720 26.432 1.00 14.49 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 29.812 -20.419 24.700 1.00 14.64 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 30.674 -19.268 24.934 1.00 15.23 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 30.278 -18.083 24.060 1.00 15.46 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 29.360 -18.180 23.224 1.00 14.01 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 32.133 -19.671 24.681 1.00 18.83 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 32.395 -19.797 23.291 1.00 25.51 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 30.952 -16.943 24.275 1.00 15.92 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 30.762 -15.729 23.477 1.00 17.08 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 31.638 -15.841 22.245 1.00 16.89 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 32.874 -15.943 22.391 1.00 18.76 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 31.239 -14.524 24.287 1.00 18.69 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 30.197 -13.996 25.241 1.00 22.83 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 30.889 -13.211 26.414 1.00 25.30 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 29.204 -13.102 24.496 1.00 24.64 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 31.052 -15.780 21.057 1.00 14.96 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 31.721 -15.912 19.753 1.00 16.28 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 31.315 -14.804 18.793 1.00 17.05 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 30.123 -14.509 18.664 1.00 15.95 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 31.441 -17.293 19.145 1.00 18.85 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 31.946 -18.369 20.115 1.00 21.32 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 32.061 -17.433 17.750 1.00 21.65 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 31.716 -19.755 19.723 1.00 23.32 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 32.280 -14.156 18.134 1.00 18.34 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 32.006 -13.080 17.204 1.00 19.19 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 31.269 -13.565 15.974 1.00 18.94 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 31.654 -14.583 15.389 1.00 19.86 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 33.338 -12.403 16.775 1.00 20.79 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 33.144 -11.248 15.817 1.00 23.40 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 32.744 -10.012 16.277 1.00 25.74 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 33.260 -11.438 14.447 1.00 25.77 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 32.540 -8.953  15.382 1.00 27.90 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 33.050 -10.388 13.555 1.00 27.85 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 32.702 -9.155  14.028 1.00 28.16 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 30.189 -12.861 15.608 1.00 18.33 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 29.386 -13.154 14.429 1.00 18.92 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 29.312 -11.881 13.588 1.00 19.08 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 28.916 -10.820 14.070 1.00 18.59 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 27.963 -13.644 14.837 1.00 17.45 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 27.117 -13.909 13.580 1.00 18.23 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 28.055 -14.921 15.691 1.00 16.39 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 29.654 -12.012 12.292 1.00 21.01 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 29.589 -10.898 11.357 1.00 21.56 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 28.192 -10.331 11.204 1.00 20.54 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 27.212 -11.067 11.402 1.00 19.57 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 30.024 -11.392 9.965  1.00 25.18 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 31.383 -12.042 9.926  1.00 30.42 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 32.527 -11.068 9.743  1.00 37.04 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 33.678 -11.550 9.665  1.00 39.29 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 32.293 -9.838  9.691  1.00 37.26 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 28.066 -9.041  10.820 1.00 20.71 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 26.771 -8.406  10.596 1.00 20.77 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 25.966 -9.163  9.537  1.00 19.32 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 26.495 -9.747  8.570  1.00 20.04 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 26.954 -6.940  10.159 1.00 22.50 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 24.668 -9.139  9.728  1.00 17.45 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 23.736 -9.707  8.788  1.00 17.00 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 22.564 -8.710  8.669  1.00 17.96 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 22.561 -7.646  9.341  1.00 19.16 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 23.221 -11.064 9.300  1.00 16.99 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 22.432 -10.895 10.472 1.00 17.18 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 21.548 -9.058  7.877  1.00 18.63 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 20.345 -8.208  7.804  1.00 19.30 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 19.541 -8.275  9.102  1.00 20.49 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 18.717 -7.385  9.339  1.00 21.35 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 19.467 -8.619  6.606  1.00 23.75 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 18.871 -10.003 6.710  1.00 30.51 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 19.636 -11.080 5.966  1.00 40.83 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 20.872 -11.179 6.160  1.00 38.18 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 19.000 -11.829 5.185  1.00 46.80 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 19.800 -9.261  9.976  1.00 19.32 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 19.092 -9.462  11.220 1.00 19.75 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 19.741 -8.808  12.412 1.00 19.28 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 19.050 -8.451  13.377 1.00 21.40 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 18.990 -10.973 11.493 1.00 19.64 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 18.417 -11.746 10.342 1.00 21.57 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.079 -11.634 9.999  1.00 23.43 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 19.197 -12.621 9.619  1.00 22.50 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 16.547 -12.349 8.935  1.00 24.79 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 18.666 -13.381 8.589  1.00 24.96 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.338 -13.239 8.242  1.00 26.99 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 16.781 -13.992 7.235  1.00 31.37 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 21.066 -8.698  12.406 1.00 17.64 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 21.799 -8.206  13.557 1.00 18.37 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 23.013 -7.426  13.128 1.00 20.77 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 23.688 -7.786  12.152 1.00 19.64 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 22.354 -9.388  14.429 1.00 17.29 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 21.327 -10.350 14.965 1.00 15.85 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 21.224 -11.641 14.462 1.00 15.65 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 20.496 -9.993  16.022 1.00 15.36 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 20.314 -12.543 14.973 1.00 15.64 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 19.603 -10.901 16.564 1.00 15.40 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 19.494 -12.171 16.023 1.00 15.28 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 18.547 -13.038 16.514 1.00 15.16 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 23.415 -6.450  13.951 1.00 22.92 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 24.699 -5.827  13.712 1.00 23.17 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 25.828 -6.825  14.024 1.00 22.40 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 25.595 -7.838  14.715 1.00 20.99 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 24.711 -4.680  14.751 1.00 24.38 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 23.869 -5.207  15.862 1.00 25.11 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 22.762 -5.941  15.184 1.00 23.23 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 27.069 -6.539  13.642 1.00 21.64 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 28.235 -7.344  14.039 1.00 22.20 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 28.293 -7.326  15.583 1.00 21.16 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 28.003 -6.270  16.190 1.00 22.32 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 29.520 -6.735  13.470 1.00 23.77 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 28.425 -8.514  16.208 1.00 19.22 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 28.342 -8.606  17.666 1.00 18.78 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 28.910 -9.925  18.161 1.00 18.49 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 29.187 -10.823 17.370 1.00 19.15 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 26.847 -8.517  18.076 1.00 18.90 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 26.059 -9.853  17.802 1.00 17.34 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 24.608 -9.645  17.512 1.00 17.43 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 23.759 -10.760 17.914 1.00 15.03 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 23.700 -11.938 17.290 1.00 16.39 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 22.890 -12.886 17.733 1.00 15.04 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 24.491 -12.191 16.241 1.00 16.66 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 29.044 -10.067 19.483 1.00 18.73 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 29.357 -11.364 20.065 1.00 18.84 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 28.022 -12.042 20.390 1.00 17.28 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 27.175 -11.475 21.101 1.00 18.25 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 30.155 -11.189 21.364 1.00 19.75 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 31.597 -10.839 21.077 1.00 22.60 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 32.535 -11.831 20.835 1.00 24.13 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 31.999 -9.520  20.953 1.00 25.30 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 33.857 -11.518 20.525 1.00 26.46 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 33.321 -9.191  20.683 1.00 26.49 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 34.242 -10.192 20.450 1.00 28.38 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? 35.546 -9.852  20.157 1.00 32.37 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 27.838 -13.269 19.870 1.00 13.71 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 26.649 -14.048 20.217 1.00 13.67 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 27.043 -14.936 21.404 1.00 13.44 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 28.098 -15.605 21.375 1.00 14.99 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 26.189 -14.877 19.031 1.00 13.94 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 25.010 -15.817 19.402 1.00 13.71 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 24.262 -16.301 18.184 1.00 12.88 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 24.059 -15.561 17.223 1.00 13.76 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 23.792 -17.577 18.241 1.00 12.73 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 26.245 -14.918 22.461 1.00 12.30 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 26.492 -15.683 23.661 1.00 12.14 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 25.851 -17.088 23.605 1.00 12.52 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 24.966 -17.366 22.771 1.00 12.64 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 25.998 -14.917 24.897 1.00 14.65 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 24.588 -14.750 24.827 1.00 16.51 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 26.333 -17.982 24.493 1.00 12.65 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 25.796 -19.336 24.643 1.00 12.60 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 25.908 -20.119 23.304 1.00 13.32 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 25.065 -20.985 23.042 1.00 13.48 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 24.345 -19.292 25.203 1.00 12.85 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 24.260 -18.644 26.551 1.00 13.62 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 24.260 -19.398 27.719 1.00 16.33 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 24.155 -17.333 26.874 1.00 14.91 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 24.181 -18.515 28.726 1.00 16.45 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 24.116 -17.262 28.263 1.00 17.02 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 26.963 -19.854 22.529 1.00 12.43 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 27.126 -20.490 21.213 1.00 12.56 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 28.191 -21.588 21.292 1.00 12.94 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 29.215 -21.414 21.947 1.00 13.32 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 27.543 -19.393 20.191 1.00 13.79 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 27.645 -19.770 18.737 1.00 15.95 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 26.270 -20.180 18.176 1.00 15.34 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 28.110 -18.546 17.872 1.00 19.14 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 27.949 -22.693 20.599 1.00 12.16 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 28.889 -23.834 20.549 1.00 11.74 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 29.270 -24.107 19.109 1.00 12.48 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 28.396 -24.017 18.236 1.00 13.95 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 28.183 -25.096 21.100 1.00 12.41 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 27.775 -24.866 22.545 1.00 14.69 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 26.756 -26.180 23.172 1.00 15.69 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 25.192 -25.988 22.129 1.00 14.97 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 30.548 -24.419 18.825 1.00 11.44 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 30.959 -24.699 17.456 1.00 10.48 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 31.323 -26.168 17.250 1.00 11.50 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 31.830 -26.831 18.150 1.00 11.79 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 32.206 -23.855 17.021 1.00 12.39 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 32.038 -22.344 17.115 1.00 13.74 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 33.334 -21.605 16.687 1.00 16.43 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 30.824 -21.867 16.257 1.00 15.99 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 31.101 -26.617 16.024 1.00 11.64 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 31.570 -27.945 15.593 1.00 12.03 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 32.147 -27.801 14.180 1.00 11.96 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 31.818 -26.864 13.435 1.00 12.31 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 30.423 -28.987 15.566 1.00 12.57 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 32.993 -28.733 13.798 1.00 12.25 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 33.475 -28.821 12.413 1.00 12.97 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 32.456 -29.594 11.614 1.00 14.24 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 32.183 -30.762 11.912 1.00 15.77 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? 34.869 -29.494 12.376 1.00 13.89 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? 35.342 -29.637 10.932 1.00 14.62 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? 35.859 -28.651 13.178 1.00 15.23 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 31.851 -28.940 10.650 1.00 14.80 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 30.797 -29.588 9.874  1.00 17.35 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 30.149 -28.645 8.897  1.00 17.22 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 30.401 -27.415 8.888  1.00 17.75 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 29.334 -29.226 7.999  1.00 15.77 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 28.683 -28.445 6.976  1.00 15.03 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 27.426 -27.757 7.454  1.00 14.94 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 26.591 -28.373 8.120  1.00 14.78 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 28.317 -29.344 5.769  1.00 16.03 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 27.666 -28.549 4.684  1.00 17.86 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 28.394 -27.605 3.957  1.00 19.62 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 26.349 -28.455 4.318  1.00 18.29 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 27.520 -27.001 3.165  1.00 20.88 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 26.285 -27.506 3.316  1.00 21.16 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 27.255 -26.501 7.051  1.00 14.93 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 26.012 -25.767 7.264  1.00 14.86 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 25.892 -24.623 6.246  1.00 15.90 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 26.894 -24.086 5.757  1.00 17.42 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 25.869 -25.274 8.710  1.00 15.75 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 26.892 -24.348 9.012  1.00 16.58 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 24.636 -24.238 5.976  1.00 15.73 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 24.188 -23.131 5.113  1.00 17.95 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 23.044 -22.416 5.845  1.00 18.19 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 22.440 -22.959 6.768  1.00 18.82 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 23.678 -23.675 3.762  1.00 20.08 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 24.780 -24.342 2.981  1.00 21.43 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 24.389 -25.010 1.673  1.00 25.83 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 23.569 -24.427 0.937  1.00 32.04 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 24.884 -26.120 1.388  1.00 25.76 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 22.736 -21.140 5.518  1.00 19.95 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 21.741 -20.368 6.313  1.00 19.57 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 20.370 -21.023 6.534  1.00 18.17 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 19.800 -20.962 7.654  1.00 17.96 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 21.618 -19.057 5.520  1.00 20.92 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 22.970 -18.887 4.902  1.00 21.60 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 23.410 -20.297 4.523  1.00 20.78 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 19.874 -21.727 5.501  1.00 17.37 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 18.622 -22.450 5.596  1.00 17.63 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 18.645 -23.625 6.569  1.00 16.12 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.599 -24.203 6.898  1.00 17.15 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 19.855 -23.981 7.055  1.00 15.12 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 19.984 -25.034 8.073  1.00 14.01 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 19.646 -24.548 9.468  1.00 12.28 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 19.509 -25.389 10.369 1.00 14.51 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 21.414 -25.646 8.084  1.00 14.00 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 21.707 -26.457 6.835  1.00 16.00 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 20.787 -27.086 6.320  1.00 17.08 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 22.860 -26.409 6.343  1.00 15.64 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 19.468 -23.223 9.674  1.00 11.91 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 19.102 -22.727 11.022 1.00 12.71 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 17.834 -23.377 11.520 1.00 13.17 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 16.904 -23.559 10.728 1.00 14.61 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 18.946 -21.208 11.030 1.00 13.35 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 20.513 -20.317 10.962 1.00 15.58 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 17.826 -23.768 12.793 1.00 12.80 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 16.678 -24.445 13.378 1.00 13.31 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 16.854 -25.954 13.448 1.00 14.05 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 16.106 -26.627 14.152 1.00 15.49 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 17.856 -26.499 12.735 1.00 13.09 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 18.158 -27.936 12.828 1.00 12.77 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 18.589 -28.278 14.254 1.00 12.04 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 19.373 -27.555 14.871 1.00 12.60 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 18.060 -29.382 14.777 1.00 12.08 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 18.375 -29.759 16.160 1.00 12.25 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 19.694 -30.510 16.300 1.00 10.98 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 19.988 -31.413 15.483 1.00 12.13 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.169 -30.582 16.710 1.00 16.11 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 15.998 -29.608 17.047 1.00 19.41 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.546 -31.396 17.980 1.00 17.92 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 14.666 -30.409 17.481 1.00 21.67 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 20.408 -30.190 17.384 1.00 10.55 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 21.585 -30.926 17.873 1.00 10.63 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 21.087 -31.710 19.098 1.00 11.62 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 20.476 -31.122 20.013 1.00 11.89 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 22.676 -29.927 18.306 1.00 12.15 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 23.906 -30.568 18.998 1.00 12.80 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 24.662 -31.557 18.055 1.00 13.38 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 24.877 -29.458 19.478 1.00 12.73 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 21.309 -33.037 19.100 1.00 12.31 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 20.840 -33.909 20.195 1.00 13.33 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 22.011 -34.720 20.711 1.00 13.37 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 22.831 -35.220 19.933 1.00 14.25 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 19.824 -34.961 19.658 1.00 16.32 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 18.611 -34.450 18.961 1.00 24.38 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.700 -35.619 18.544 1.00 28.74 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.135 -36.177 19.761 1.00 35.16 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 16.001 -35.758 20.313 1.00 37.09 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 15.220 -34.893 19.673 1.00 38.00 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 15.635 -36.208 21.496 1.00 36.12 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 22.001 -34.994 22.009 1.00 13.15 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 22.971 -35.929 22.611 1.00 13.69 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 22.146 -37.096 23.187 1.00 15.50 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 20.932 -37.144 23.044 1.00 14.78 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 23.805 -35.248 23.702 1.00 12.98 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 22.799 -34.695 25.134 1.00 12.97 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 22.829 -38.024 23.911 1.00 17.03 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 22.111 -39.134 24.542 1.00 18.49 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 21.050 -38.673 25.586 1.00 18.87 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 20.164 -39.455 25.963 1.00 21.56 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 23.103 -40.115 25.201 1.00 21.05 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 23.806 -39.524 26.408 1.00 24.30 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 24.862 -40.452 26.955 1.00 32.75 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 26.060 -40.251 26.723 1.00 36.96 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 24.448 -41.443 27.731 1.00 33.50 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 21.110 -37.389 26.051 1.00 16.33 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 20.177 -36.910 27.069 1.00 15.82 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 18.971 -36.164 26.497 1.00 17.10 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 18.032 -35.870 27.234 1.00 19.33 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 20.900 -36.004 28.084 1.00 15.23 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 22.081 -36.649 28.740 1.00 14.93 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 23.377 -36.320 28.383 1.00 14.43 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 22.117 -37.602 29.705 1.00 17.99 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 24.165 -37.117 29.099 1.00 16.97 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 23.454 -37.887 29.934 1.00 19.43 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 19.015 -35.805 25.210 1.00 15.87 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 17.933 -35.031 24.626 1.00 14.57 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 18.415 -33.892 23.742 1.00 13.09 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 19.537 -33.915 23.230 1.00 12.92 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.584 -32.882 23.598 1.00 13.02 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 17.894 -31.731 22.732 1.00 13.26 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 18.880 -30.827 23.400 1.00 12.91 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 18.672 -30.376 24.559 1.00 13.40 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 16.599 -30.976 22.388 1.00 14.14 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 16.929 -29.693 21.617 1.00 15.17 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 15.672 -31.891 21.574 1.00 15.15 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 19.988 -30.517 22.700 1.00 11.24 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 21.053 -29.644 23.203 1.00 11.51 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 20.889 -28.197 22.733 1.00 12.34 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 21.113 -27.238 23.484 1.00 12.08 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 22.426 -30.190 22.729 1.00 11.55 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 23.575 -29.240 23.089 1.00 13.23 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 22.674 -31.573 23.312 1.00 12.74 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 20.491 -28.035 21.468 1.00 12.41 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 20.394 -26.691 20.895 1.00 12.84 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 19.987 -26.741 19.439 1.00 11.12 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 19.604 -27.810 18.939 1.00 12.19 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 20.048 -25.581 18.799 1.00 11.64 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 19.636 -25.487 17.399 1.00 11.33 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 20.675 -24.744 16.573 1.00 11.40 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 21.352 -23.830 17.057 1.00 11.70 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 18.260 -24.796 17.220 1.00 12.26 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 18.194 -23.424 17.925 1.00 13.07 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.091 -25.717 17.610 1.00 14.16 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 16.819 -22.628 17.587 1.00 14.65 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 20.803 -25.108 15.255 1.00 11.17 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 21.765 -24.390 14.396 1.00 10.83 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 21.404 -22.877 14.355 1.00 10.70 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 20.210 -22.529 14.180 1.00 11.49 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 21.706 -24.970 12.959 1.00 10.73 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 22.578 -24.139 12.015 1.00 12.67 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 22.183 -26.424 12.955 1.00 11.75 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 22.400 -22.009 14.494 1.00 10.12 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 22.185 -20.571 14.505 1.00 10.97 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 23.135 -19.810 13.582 1.00 13.49 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 22.780 -18.728 13.094 1.00 13.42 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 22.294 -20.071 15.947 1.00 11.66 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 22.144 -18.645 16.022 1.00 11.76 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 24.338 -20.333 13.342 1.00 13.15 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 25.312 -19.656 12.467 1.00 14.38 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 26.240 -20.711 11.856 1.00 14.45 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 26.094 -21.905 12.142 1.00 13.97 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 26.064 -18.551 13.237 1.00 17.05 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 26.788 -17.739 12.258 1.00 19.42 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 27.028 -19.129 14.248 1.00 18.47 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 27.142 -20.276 10.980 1.00 15.43 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 28.080 -21.206 10.372 1.00 17.44 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 28.939 -20.502 9.341  1.00 19.61 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 28.818 -19.314 9.103  1.00 18.42 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 29.755 -21.282 8.682  1.00 23.24 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 30.682 -20.747 7.677  1.00 25.22 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 32.093 -21.221 7.956  1.00 25.57 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 32.375 -21.721 9.037  1.00 25.21 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 33.017 -21.041 6.991  1.00 25.84 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 34.393 -21.519 7.116  1.00 25.63 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 34.476 -23.026 7.532  1.00 23.31 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? 35.429 -23.393 8.206  1.00 23.87 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? 35.173 -20.663 8.125  1.00 28.17 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? 35.607 -19.332 7.609  1.00 32.77 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? 35.643 -19.078 6.404  1.00 34.69 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? 36.034 -18.481 8.519  1.00 33.71 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 33.496 -23.874 7.170  1.00 20.71 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 33.520 -25.287 7.561  1.00 19.15 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 33.150 -25.555 9.021  1.00 16.23 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 33.442 -26.638 9.548  1.00 16.39 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 32.552 -24.569 9.668  1.00 15.16 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 32.115 -24.661 11.051 1.00 16.00 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 30.600 -24.469 11.145 1.00 18.02 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 30.027 -23.684 10.359 1.00 22.21 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 32.800 -23.593 11.893 1.00 17.81 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 34.327 -23.633 11.866 1.00 20.26 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? 34.912 -22.260 12.272 1.00 23.08 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? 34.867 -24.771 12.740 1.00 19.91 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 29.966 -25.096 12.127 1.00 13.75 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 28.529 -24.937 12.359 1.00 13.88 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 28.407 -24.460 13.814 1.00 13.05 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 29.081 -24.996 14.734 1.00 12.90 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 27.728 -26.236 12.109 1.00 15.13 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 28.293 -27.467 12.775 1.00 18.73 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 26.212 -26.064 12.364 1.00 13.60 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 27.544 -23.460 14.030 1.00 11.95 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 27.346 -22.926 15.364 1.00 12.48 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 25.946 -23.198 15.870 1.00 12.11 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 24.969 -22.997 15.141 1.00 12.85 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 25.852 -23.661 17.121 1.00 10.72 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 24.573 -24.034 17.734 1.00 10.93 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 24.295 -23.181 18.958 1.00 11.33 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 25.179 -23.006 19.814 1.00 11.88 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 24.631 -25.495 18.247 1.00 11.71 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 25.047 -26.508 17.194 1.00 11.45 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 24.112 -27.058 16.326 1.00 11.40 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 26.368 -26.912 17.084 1.00 12.67 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 24.506 -27.984 15.364 1.00 12.25 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 26.744 -27.873 16.144 1.00 13.86 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 25.816 -28.384 15.271 1.00 13.64 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 23.058 -22.658 19.029 1.00 10.77 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 22.591 -21.924 20.197 1.00 10.83 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 22.216 -22.962 21.247 1.00 10.95 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 21.262 -23.741 21.045 1.00 11.50 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 21.345 -21.086 19.832 1.00 11.29 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 22.893 -22.928 22.408 1.00 10.58 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 22.599 -23.847 23.499 1.00 10.47 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 21.261 -23.534 24.153 1.00 11.30 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 20.904 -22.360 24.297 1.00 11.59 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 23.730 -23.724 24.588 1.00 12.51 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 23.564 -24.734 25.707 1.00 17.26 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 23.438 -25.911 25.410 1.00 16.57 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 23.513 -24.321 26.881 1.00 19.89 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 20.523 -24.574 24.581 1.00 11.25 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 19.269 -24.375 25.346 1.00 12.02 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 19.325 -25.116 26.682 1.00 12.06 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 18.358 -25.063 27.436 1.00 13.35 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 17.970 -24.774 24.589 1.00 13.24 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 17.816 -23.936 23.320 1.00 13.51 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 17.946 -26.278 24.248 1.00 13.37 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 20.448 -25.812 27.011 1.00 11.61 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 20.493 -26.695 28.167 1.00 11.82 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 20.422 -25.924 29.502 1.00 13.45 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 20.060 -26.514 30.534 1.00 14.42 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 21.753 -27.577 28.139 1.00 11.66 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 21.731 -28.586 27.001 1.00 12.14 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 23.058 -29.329 26.968 1.00 12.02 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 24.138 -28.410 26.571 1.00 11.51 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 25.390 -28.799 26.345 1.00 11.89 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 25.765 -30.057 26.594 1.00 12.06 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 26.283 -27.936 25.876 1.00 12.71 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 20.801 -24.641 29.501 1.00 12.99 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 20.742 -23.849 30.734 1.00 14.22 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 19.360 -23.280 31.013 1.00 14.91 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 19.171 -22.758 32.121 1.00 16.75 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 21.750 -22.705 30.672 1.00 14.51 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 21.462 -21.694 29.577 1.00 16.99 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 21.184 -22.126 28.434 1.00 17.30 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 21.511 -20.451 29.875 1.00 19.51 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 18.407 -23.366 30.073 1.00 13.38 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.065 -22.758 30.252 1.00 14.43 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 16.203 -23.732 30.987 1.00 13.81 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 15.343 -24.415 30.419 1.00 14.80 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 16.480 -22.447 28.859 1.00 14.97 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.346 -21.505 28.022 1.00 16.19 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 16.726 -21.318 26.609 1.00 16.25 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.516 -20.157 28.693 1.00 15.60 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 16.427 -23.808 32.323 1.00 13.32 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 15.749 -24.850 33.117 1.00 15.21 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 14.245 -24.662 33.178 1.00 17.01 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 13.508 -25.626 33.364 1.00 17.86 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 16.331 -24.948 34.532 1.00 15.86 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 17.830 -24.968 34.666 1.00 16.08 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 18.253 -25.139 36.112 1.00 18.16 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 18.487 -26.029 33.766 1.00 17.46 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 13.787 -23.406 33.055 1.00 16.45 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 12.368 -23.087 33.120 1.00 17.39 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 11.544 -23.684 31.947 1.00 18.22 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 10.310 -23.703 32.025 1.00 18.51 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 12.180 -21.563 33.231 1.00 16.79 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 12.830 -20.781 32.107 1.00 16.58 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 14.077 -20.227 32.103 1.00 16.99 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 12.261 -20.516 30.802 1.00 16.65 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 14.310 -19.600 30.891 1.00 17.13 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 13.189 -19.736 30.096 1.00 16.38 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 11.002 -20.783 30.211 1.00 16.56 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 12.953 -19.316 28.776 1.00 17.90 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 10.757 -20.319 28.922 1.00 17.72 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 11.708 -19.552 28.246 1.00 17.44 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 12.201 -24.181 30.883 1.00 17.78 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 11.449 -24.801 29.767 1.00 19.19 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 10.706 -26.066 30.227 1.00 23.32 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 9.713  -26.433 29.578 1.00 23.99 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 12.403 -25.195 28.618 1.00 17.34 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 12.985 -24.055 27.778 1.00 17.60 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 14.028 -24.615 26.799 1.00 17.44 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 11.858 -23.313 26.987 1.00 17.87 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 11.224 -26.730 31.307 1.00 25.28 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 10.728 -27.980 31.914 1.00 29.69 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 9.582  -27.798 32.870 1.00 32.93 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 9.152  -28.800 33.435 1.00 34.01 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 11.830 -28.660 32.730 1.00 32.34 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 12.999 -29.207 31.965 1.00 37.99 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 12.840 -29.503 30.780 1.00 40.31 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 14.086 -29.357 32.572 1.00 40.96 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 9.160  -26.569 33.161 1.00 33.76 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 8.025  -26.352 34.061 1.00 36.70 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 7.031  -25.362 33.458 1.00 38.55 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 5.919  -25.220 33.986 1.00 40.35 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 8.474  -25.920 35.466 1.00 40.43 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 9.564  -24.871 35.481 1.00 45.35 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 10.853 -25.385 36.089 1.00 54.92 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 11.558 -24.595 36.760 1.00 56.85 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 11.154 -26.587 35.901 1.00 58.64 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1BO1 C 2 .   ? 9.307  15.519  22.221 1.00 18.65 ? 201 A1BO1 A N1  1 
HETATM 2156 C  C4  . A1BO1 C 2 .   ? 9.425  10.345  22.985 1.00 19.24 ? 201 A1BO1 A C4  1 
HETATM 2157 C  C5  . A1BO1 C 2 .   ? 9.068  11.639  23.327 1.00 20.10 ? 201 A1BO1 A C5  1 
HETATM 2158 C  C6  . A1BO1 C 2 .   ? 7.989  11.885  24.175 1.00 20.07 ? 201 A1BO1 A C6  1 
HETATM 2159 C  C7  . A1BO1 C 2 .   ? 7.556  13.294  24.536 1.00 20.53 ? 201 A1BO1 A C7  1 
HETATM 2160 C  C8  . A1BO1 C 2 .   ? 8.352  14.642  22.675 1.00 20.58 ? 201 A1BO1 A C8  1 
HETATM 2161 C  C10 . A1BO1 C 2 .   ? 11.794 15.272  22.122 1.00 18.64 ? 201 A1BO1 A C10 1 
HETATM 2162 C  C13 . A1BO1 C 2 .   ? 10.286 15.629  18.574 1.00 15.97 ? 201 A1BO1 A C13 1 
HETATM 2163 O  O1  . A1BO1 C 2 .   ? 9.910  16.757  18.232 1.00 17.12 ? 201 A1BO1 A O1  1 
HETATM 2164 N  N2  . A1BO1 C 2 .   ? 10.588 14.672  17.703 1.00 15.15 ? 201 A1BO1 A N2  1 
HETATM 2165 C  C12 . A1BO1 C 2 .   ? 10.384 15.244  20.039 1.00 15.99 ? 201 A1BO1 A C12 1 
HETATM 2166 C  C11 . A1BO1 C 2 .   ? 11.743 15.624  20.636 1.00 17.39 ? 201 A1BO1 A C11 1 
HETATM 2167 C  C9  . A1BO1 C 2 .   ? 10.589 15.845  22.879 1.00 19.08 ? 201 A1BO1 A C9  1 
HETATM 2168 C  C14 . A1BO1 C 2 .   ? 9.258  15.929  20.813 1.00 17.67 ? 201 A1BO1 A C14 1 
HETATM 2169 O  O   . A1BO1 C 2 .   ? 7.492  14.172  21.931 1.00 20.89 ? 201 A1BO1 A O   1 
HETATM 2170 N  N   . A1BO1 C 2 .   ? 8.397  14.349  23.982 1.00 20.42 ? 201 A1BO1 A N   1 
HETATM 2171 C  C1  . A1BO1 C 2 .   ? 7.275  10.799  24.701 1.00 20.18 ? 201 A1BO1 A C1  1 
HETATM 2172 C  C   . A1BO1 C 2 .   ? 6.161  10.981  25.698 1.00 21.01 ? 201 A1BO1 A C   1 
HETATM 2173 C  C3  . A1BO1 C 2 .   ? 8.688  9.288   23.446 1.00 19.77 ? 201 A1BO1 A C3  1 
HETATM 2174 C  C2  . A1BO1 C 2 .   ? 7.632  9.511   24.301 1.00 19.68 ? 201 A1BO1 A C2  1 
HETATM 2175 ZN ZN  . ZN    D 3 .   ? 11.506 -4.652  5.713  1.00 17.39 2 202 ZN    A ZN  1 
HETATM 2176 N  N1  . A1BO1 E 2 .   ? 23.883 -15.361 9.925  1.00 17.18 ? 201 A1BO1 C N1  1 
HETATM 2177 C  C4  . A1BO1 E 2 .   ? 23.940 -20.559 9.322  1.00 18.68 ? 201 A1BO1 C C4  1 
HETATM 2178 C  C5  . A1BO1 E 2 .   ? 24.182 -19.264 8.893  1.00 19.37 ? 201 A1BO1 C C5  1 
HETATM 2179 C  C6  . A1BO1 E 2 .   ? 25.189 -18.994 7.965  1.00 18.38 ? 201 A1BO1 C C6  1 
HETATM 2180 C  C7  . A1BO1 E 2 .   ? 25.486 -17.581 7.503  1.00 18.69 ? 201 A1BO1 C C7  1 
HETATM 2181 C  C8  . A1BO1 E 2 .   ? 24.818 -16.205 9.394  1.00 18.72 ? 201 A1BO1 C C8  1 
HETATM 2182 C  C10 . A1BO1 E 2 .   ? 21.443 -15.486 10.210 1.00 17.88 ? 201 A1BO1 C C10 1 
HETATM 2183 C  C13 . A1BO1 E 2 .   ? 23.233 -15.108 13.641 1.00 14.60 ? 201 A1BO1 C C13 1 
HETATM 2184 O  O1  . A1BO1 E 2 .   ? 23.590 -13.947 13.915 1.00 13.34 ? 201 A1BO1 C O1  1 
HETATM 2185 N  N2  . A1BO1 E 2 .   ? 23.062 -16.048 14.554 1.00 13.73 ? 201 A1BO1 C N2  1 
HETATM 2186 C  C12 . A1BO1 E 2 .   ? 23.007 -15.544 12.203 1.00 15.28 ? 201 A1BO1 C C12 1 
HETATM 2187 C  C11 . A1BO1 E 2 .   ? 21.623 -15.129 11.691 1.00 17.89 ? 201 A1BO1 C C11 1 
HETATM 2188 C  C9  . A1BO1 E 2 .   ? 22.585 -14.960 9.362  1.00 17.13 ? 201 A1BO1 C C9  1 
HETATM 2189 C  C14 . A1BO1 E 2 .   ? 24.084 -14.938 11.314 1.00 16.71 ? 201 A1BO1 C C14 1 
HETATM 2190 O  O   . A1BO1 E 2 .   ? 25.757 -16.649 10.060 1.00 19.82 ? 201 A1BO1 C O   1 
HETATM 2191 N  N   . A1BO1 E 2 .   ? 24.646 -16.548 8.098  1.00 18.88 ? 201 A1BO1 C N   1 
HETATM 2192 C  C1  . A1BO1 E 2 .   ? 25.940 -20.054 7.441  1.00 19.69 ? 201 A1BO1 C C1  1 
HETATM 2193 C  C   . A1BO1 E 2 .   ? 26.953 -19.841 6.345  1.00 21.07 ? 201 A1BO1 C C   1 
HETATM 2194 C  C3  . A1BO1 E 2 .   ? 24.686 -21.593 8.830  1.00 18.72 ? 201 A1BO1 C C3  1 
HETATM 2195 C  C2  . A1BO1 E 2 .   ? 25.669 -21.344 7.890  1.00 19.20 ? 201 A1BO1 C C2  1 
HETATM 2196 ZN ZN  . ZN    F 3 .   ? 24.049 -34.881 27.050 1.00 13.64 2 202 ZN    C ZN  1 
HETATM 2197 O  O   . HOH   G 4 .   ? 19.867 23.213  8.185  1.00 21.12 ? 301 HOH   A O   1 
HETATM 2198 O  O   . HOH   G 4 .   ? 9.101  -4.178  0.566  1.00 32.35 ? 302 HOH   A O   1 
HETATM 2199 O  O   . HOH   G 4 .   ? 7.724  21.312  9.579  1.00 46.10 ? 303 HOH   A O   1 
HETATM 2200 O  O   . HOH   G 4 .   ? 16.626 23.399  24.887 1.00 50.01 ? 304 HOH   A O   1 
HETATM 2201 O  O   . HOH   G 4 .   ? 2.720  8.152   9.538  1.00 28.51 ? 305 HOH   A O   1 
HETATM 2202 O  O   . HOH   G 4 .   ? 10.785 8.266   4.508  1.00 20.54 ? 306 HOH   A O   1 
HETATM 2203 O  O   . HOH   G 4 .   ? -0.264 16.184  7.897  1.00 36.27 ? 307 HOH   A O   1 
HETATM 2204 O  O   . HOH   G 4 .   ? 3.687  -1.402  2.878  1.00 40.44 ? 308 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 4 .   ? 23.457 22.330  8.094  1.00 26.98 ? 309 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 4 .   ? 21.795 -3.681  12.356 1.00 28.64 ? 310 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 4 .   ? 23.485 11.498  21.771 1.00 38.88 ? 311 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 4 .   ? 6.200  -5.247  29.213 1.00 24.41 ? 312 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 4 .   ? 9.181  19.091  19.583 1.00 16.95 ? 313 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 4 .   ? 27.396 8.412   0.893  1.00 34.89 ? 314 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 4 .   ? 22.469 4.480   24.292 1.00 44.12 ? 315 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 4 .   ? 27.852 16.612  3.739  1.00 36.00 ? 316 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 4 .   ? 19.577 9.510   19.358 1.00 14.03 ? 317 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 4 .   ? 16.806 -6.774  11.175 1.00 22.93 ? 318 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 4 .   ? 18.185 -6.483  3.639  1.00 30.49 ? 319 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 4 .   ? 18.542 0.204   27.923 1.00 25.03 ? 320 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 4 .   ? 15.964 -10.491 5.238  1.00 33.29 ? 321 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 4 .   ? 0.133  0.025   16.064 1.00 13.52 ? 322 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 4 .   ? 23.473 0.779   16.863 1.00 23.42 ? 323 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 4 .   ? 20.159 17.344  23.964 1.00 43.78 ? 324 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 4 .   ? -0.327 14.985  16.383 1.00 24.39 ? 325 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 4 .   ? 34.395 20.764  12.274 1.00 30.59 ? 326 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 4 .   ? 36.473 16.619  12.534 1.00 23.64 ? 327 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 4 .   ? 4.085  13.335  19.574 1.00 34.31 ? 328 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 4 .   ? 6.516  3.896   32.828 1.00 20.35 ? 329 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 4 .   ? 23.051 -0.851  4.763  1.00 25.67 ? 330 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 4 .   ? 17.470 21.603  9.858  1.00 19.86 ? 331 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 4 .   ? 11.956 7.466   31.054 1.00 22.49 ? 332 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 4 .   ? 30.406 10.754  14.601 1.00 26.79 ? 333 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 4 .   ? -0.106 -5.649  11.120 1.00 30.09 ? 334 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 4 .   ? 4.923  8.131   28.247 1.00 25.37 ? 335 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 4 .   ? 25.604 4.875   20.653 1.00 31.29 ? 336 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 4 .   ? 2.305  3.666   27.597 1.00 27.04 ? 337 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 4 .   ? 7.512  20.211  17.491 1.00 17.79 ? 338 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 4 .   ? 6.204  17.427  21.797 1.00 35.15 ? 339 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 4 .   ? 34.605 15.449  9.988  1.00 55.66 ? 340 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 4 .   ? 10.722 4.794   3.429  1.00 19.79 ? 341 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 4 .   ? 14.429 2.979   23.381 1.00 13.74 ? 342 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 4 .   ? 29.470 11.872  20.344 1.00 28.68 ? 343 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 4 .   ? 31.585 12.646  22.005 1.00 38.76 ? 344 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 4 .   ? 13.833 -11.539 4.173  1.00 48.15 ? 345 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 4 .   ? 28.439 4.164   3.856  1.00 43.70 ? 346 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 4 .   ? 20.886 19.682  17.986 1.00 29.10 ? 347 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 4 .   ? 11.142 11.856  11.291 1.00 13.85 ? 348 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 4 .   ? 29.505 3.946   11.559 1.00 20.53 ? 349 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 4 .   ? 15.733 11.309  1.106  1.00 38.31 ? 350 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 4 .   ? 5.082  26.957  16.270 1.00 38.88 ? 351 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 4 .   ? 16.793 21.378  18.989 1.00 25.52 ? 352 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 4 .   ? 16.941 17.377  4.246  1.00 38.67 ? 353 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 4 .   ? 22.221 18.899  19.570 1.00 32.21 ? 354 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 4 .   ? 29.746 11.909  3.107  1.00 45.88 ? 355 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 4 .   ? 29.549 -4.158  10.148 1.00 44.21 ? 356 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 4 .   ? 17.245 1.266   30.237 1.00 33.05 ? 357 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 4 .   ? 19.517 -3.136  2.323  1.00 46.51 ? 358 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 4 .   ? 9.259  2.508   2.849  1.00 21.30 ? 359 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 4 .   ? 12.386 9.626   29.759 1.00 22.39 ? 360 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 4 .   ? 32.703 15.063  8.260  1.00 45.20 ? 361 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 4 .   ? 10.804 2.729   33.558 1.00 16.00 ? 362 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 4 .   ? 17.996 19.640  5.773  1.00 34.09 ? 363 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 4 .   ? 14.602 12.700  24.160 1.00 17.42 ? 364 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 4 .   ? 17.319 2.982   23.421 1.00 20.30 ? 365 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 4 .   ? 30.514 21.234  17.244 1.00 33.25 ? 366 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 4 .   ? 4.690  7.265   2.832  1.00 30.90 ? 367 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 4 .   ? 9.447  5.152   33.898 1.00 18.36 ? 368 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 4 .   ? 10.013 -8.407  9.707  1.00 33.07 ? 369 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 4 .   ? 13.048 10.770  9.379  1.00 13.59 ? 370 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 4 .   ? 29.722 11.596  17.906 1.00 33.92 ? 371 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 4 .   ? 15.522 -4.911  -0.165 1.00 51.90 ? 372 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 4 .   ? 24.271 17.840  3.773  1.00 36.89 ? 373 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 4 .   ? 7.264  -4.241  -1.490 1.00 46.30 ? 374 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 4 .   ? 18.128 9.781   25.934 1.00 21.60 ? 375 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 4 .   ? 5.754  -6.869  14.262 1.00 35.93 ? 376 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 4 .   ? 10.347 -13.974 5.434  1.00 52.75 ? 377 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 4 .   ? 17.477 19.417  17.188 1.00 14.58 ? 378 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 4 .   ? 30.576 20.914  11.031 1.00 21.87 ? 379 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 4 .   ? 3.726  6.090   24.962 1.00 17.52 ? 380 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 4 .   ? 3.939  -2.331  20.633 1.00 26.08 ? 381 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 4 .   ? 14.220 -6.784  30.768 1.00 35.88 ? 382 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 4 .   ? 6.296  1.772   5.953  1.00 19.55 ? 383 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 4 .   ? 36.940 0.301   11.063 1.00 41.81 ? 384 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 4 .   ? -2.358 8.229   28.783 1.00 32.04 ? 385 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 4 .   ? 4.337  -4.912  6.208  1.00 27.96 ? 386 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 4 .   ? 0.540  1.224   24.111 1.00 15.60 ? 387 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 4 .   ? 30.377 5.213   4.564  1.00 36.23 ? 388 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 4 .   ? 0.172  4.194   6.385  1.00 25.99 ? 389 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 4 .   ? 4.853  -1.460  24.469 1.00 17.58 ? 390 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 4 .   ? 29.751 6.822   19.265 1.00 40.72 ? 391 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 4 .   ? 38.811 4.681   14.566 1.00 34.27 ? 392 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 4 .   ? 17.749 5.368   26.944 1.00 25.30 ? 393 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 4 .   ? 6.219  18.350  24.187 1.00 30.92 ? 394 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 4 .   ? 18.302 0.297   19.845 1.00 22.05 ? 395 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 4 .   ? 18.554 -4.296  27.784 1.00 50.23 ? 396 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 4 .   ? 2.606  9.650   27.899 1.00 27.65 ? 397 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 4 .   ? 7.162  7.929   32.922 1.00 46.94 ? 398 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 4 .   ? 1.405  10.679  21.581 1.00 35.40 ? 399 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 4 .   ? 13.974 14.556  26.137 1.00 30.51 ? 400 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 4 .   ? 6.772  12.885  5.234  1.00 22.35 ? 401 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 4 .   ? 34.852 11.260  11.033 1.00 32.58 ? 402 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 4 .   ? 31.238 19.066  9.049  1.00 26.13 ? 403 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 4 .   ? 9.363  15.550  26.456 1.00 31.21 ? 404 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 4 .   ? 23.611 14.958  23.809 1.00 54.82 ? 405 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 4 .   ? 7.711  19.875  7.887  1.00 35.06 ? 406 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 4 .   ? 1.615  -1.801  17.340 1.00 19.54 ? 407 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 4 .   ? 7.212  -7.859  23.930 1.00 31.08 ? 408 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 4 .   ? 1.954  13.057  4.967  1.00 31.30 ? 409 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 4 .   ? 12.486 -7.404  13.421 1.00 24.08 ? 410 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 4 .   ? -0.922 15.547  12.164 1.00 24.09 ? 411 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 4 .   ? 14.604 -3.975  17.549 1.00 23.07 ? 412 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 4 .   ? 8.211  -6.934  8.537  1.00 31.41 ? 413 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 4 .   ? 14.295 21.372  8.478  1.00 30.11 ? 414 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 4 .   ? 4.371  -1.260  29.326 1.00 33.51 ? 415 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 4 .   ? 14.973 24.438  9.937  1.00 52.51 ? 416 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 4 .   ? 16.532 -4.368  2.216  1.00 29.54 ? 417 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 4 .   ? 31.190 3.472   13.529 1.00 28.05 ? 418 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 4 .   ? 10.672 19.002  26.152 1.00 41.28 ? 419 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 4 .   ? 14.687 14.755  3.705  1.00 29.09 ? 420 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 4 .   ? 31.909 9.595   6.513  1.00 31.03 ? 421 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 4 .   ? 5.507  -6.954  7.005  1.00 61.63 ? 422 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 4 .   ? 27.948 17.274  23.728 1.00 27.98 ? 423 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 4 .   ? 20.223 2.426   19.056 1.00 30.37 ? 424 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 4 .   ? 30.794 15.770  22.224 1.00 22.43 ? 425 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 4 .   ? 11.446 -10.515 2.093  1.00 45.87 ? 426 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 4 .   ? 2.755  15.947  19.835 1.00 29.50 ? 427 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 4 .   ? 5.874  22.903  10.304 1.00 29.12 ? 428 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 4 .   ? 17.099 23.260  16.875 1.00 32.40 ? 429 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 4 .   ? 8.525  9.565   31.556 1.00 32.30 ? 430 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 4 .   ? 0.874  -1.733  9.674  1.00 33.94 ? 431 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 4 .   ? 4.648  15.165  21.958 1.00 49.81 ? 432 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 4 .   ? 5.285  26.839  19.111 1.00 26.85 ? 433 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 4 .   ? 11.575 21.684  12.094 1.00 22.56 ? 434 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 4 .   ? 19.505 24.133  15.672 1.00 20.17 ? 435 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 4 .   ? 22.703 -1.791  16.869 1.00 29.53 ? 436 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 4 .   ? 36.069 12.235  13.414 1.00 33.38 ? 437 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 4 .   ? 23.483 3.104   20.223 1.00 25.23 ? 438 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 4 .   ? 9.347  21.298  10.666 1.00 34.44 ? 439 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 4 .   ? 21.354 9.384   21.629 1.00 18.73 ? 440 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 4 .   ? 22.364 19.364  6.201  1.00 26.74 ? 441 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 4 .   ? 18.996 13.240  2.406  1.00 44.22 ? 442 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 4 .   ? 2.527  23.673  21.174 1.00 24.64 ? 443 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 4 .   ? 2.766  -6.110  14.798 1.00 33.18 ? 444 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 4 .   ? 7.512  -5.051  31.705 1.00 29.17 ? 445 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 4 .   ? 23.882 8.015   21.294 1.00 30.95 ? 446 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 4 .   ? 8.193  -5.598  2.772  1.00 31.09 ? 447 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 4 .   ? 35.264 3.426   3.571  1.00 59.30 ? 448 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 4 .   ? 18.622 9.203   -1.275 1.00 34.06 ? 449 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 4 .   ? 2.051  -5.959  17.430 1.00 36.75 ? 450 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 4 .   ? 34.453 9.435   7.340  1.00 37.77 ? 451 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 4 .   ? 14.832 -9.085  12.104 1.00 26.99 ? 452 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 4 .   ? 33.742 18.094  9.249  1.00 45.55 ? 453 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 4 .   ? 31.740 12.388  16.471 1.00 49.57 ? 454 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 4 .   ? 18.292 10.902  0.403  1.00 37.60 ? 455 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 4 .   ? 29.564 3.593   20.064 1.00 68.08 ? 456 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 4 .   ? 25.665 -7.216  6.215  1.00 50.12 ? 457 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 4 .   ? 36.633 7.148   6.525  1.00 94.00 ? 458 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 4 .   ? 32.121 22.514  24.575 1.00 48.53 ? 459 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 4 .   ? 11.325 19.974  4.703  1.00 51.90 ? 460 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 4 .   ? 14.926 12.473  28.309 1.00 34.28 ? 461 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 4 .   ? 11.487 23.729  13.824 1.00 34.42 ? 462 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 4 .   ? 19.456 16.385  26.379 1.00 52.36 ? 463 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 4 .   ? 20.752 22.602  17.786 1.00 28.05 ? 464 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 4 .   ? 16.572 11.730  26.055 1.00 25.28 ? 465 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 4 .   ? 1.616  1.288   26.539 1.00 33.72 ? 466 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 4 .   ? 16.604 13.625  2.253  1.00 40.89 ? 467 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 4 .   ? 2.846  10.827  19.361 1.00 47.54 ? 468 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 4 .   ? 3.688  -2.147  26.901 1.00 28.95 ? 469 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 4 .   ? 6.624  2.600   3.351  1.00 24.93 ? 470 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 4 .   ? 2.711  12.486  27.012 1.00 43.95 ? 471 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 4 .   ? 9.979  -8.053  12.538 1.00 27.75 ? 472 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 4 .   ? 0.791  -1.531  23.437 1.00 22.99 ? 473 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 4 .   ? 8.963  7.124   2.739  1.00 38.00 ? 474 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 4 .   ? 32.387 22.496  12.323 1.00 30.24 ? 475 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 4 .   ? 8.432  17.950  26.124 1.00 44.02 ? 476 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 4 .   ? 7.161  14.660  28.023 1.00 40.26 ? 477 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 4 .   ? 32.218 22.146  20.167 1.00 44.51 ? 478 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 4 .   ? 31.397 11.923  5.297  1.00 35.87 ? 479 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 4 .   ? 12.021 15.411  27.571 1.00 32.53 ? 480 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 4 .   ? 3.215  -3.034  23.006 1.00 22.83 ? 481 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 4 .   ? 18.230 -2.392  19.019 1.00 38.30 ? 482 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 4 .   ? 37.782 3.576   16.829 1.00 39.59 ? 483 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 4 .   ? 21.755 10.612  24.109 1.00 31.97 ? 484 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 4 .   ? 1.876  -5.047  6.962  1.00 37.13 ? 485 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 4 .   ? 29.781 1.908   17.933 1.00 44.68 ? 486 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 4 .   ? 6.612  10.048  29.614 1.00 32.19 ? 487 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 4 .   ? 2.896  -4.782  27.158 1.00 49.18 ? 488 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 4 .   ? 2.733  26.383  20.121 1.00 33.18 ? 489 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 4 .   ? 0.209  11.904  17.630 1.00 54.07 ? 490 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 4 .   ? 4.396  18.472  27.036 1.00 59.26 ? 491 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 4 .   ? 9.878  25.597  12.766 1.00 38.84 ? 492 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 4 .   ? 5.953  -8.592  25.888 1.00 38.16 ? 493 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 4 .   ? 27.084 0.282   19.013 1.00 56.94 ? 494 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 4 .   ? 39.116 8.980   7.061  1.00 75.13 ? 495 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 4 .   ? 21.243 -24.071 1.433  1.00 30.92 ? 301 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 4 .   ? 9.529  -36.576 21.679 1.00 38.91 ? 302 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 4 .   ? 10.122 -19.663 12.273 1.00 38.23 ? 303 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 4 .   ? 31.994 -22.217 22.172 1.00 23.76 ? 304 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 4 .   ? 24.509 -22.106 27.760 1.00 19.67 ? 305 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 4 .   ? -1.078 -14.475 16.874 1.00 25.62 ? 306 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 4 .   ? 3.422  -9.733  22.162 1.00 27.85 ? 307 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 4 .   ? 28.037 -15.376 9.741  1.00 33.32 ? 308 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 4 .   ? 11.004 -8.391  24.901 1.00 22.71 ? 309 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 4 .   ? 20.613 -18.961 31.868 1.00 31.25 ? 310 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 4 .   ? 34.363 -14.087 10.020 1.00 32.07 ? 311 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 4 .   ? 14.235 -21.593 13.938 1.00 14.10 ? 312 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 4 .   ? 30.193 -35.537 11.006 1.00 28.13 ? 313 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 4 .   ? 11.169 -30.431 17.496 1.00 21.92 ? 314 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 4 .   ? 28.072 -22.653 3.845  1.00 28.62 ? 315 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 4 .   ? 24.142 -11.628 12.380 1.00 15.98 ? 316 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 4 .   ? 27.527 -38.324 25.610 1.00 38.93 ? 317 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 4 .   ? 17.367 -37.063 29.523 1.00 33.80 ? 318 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 4 .   ? 9.766  -18.798 10.381 1.00 26.10 ? 319 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 4 .   ? 7.211  -27.028 30.308 1.00 35.55 ? 320 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 4 .   ? 7.087  -14.061 29.907 1.00 38.99 ? 321 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 4 .   ? 23.393 -35.507 1.104  1.00 28.52 ? 322 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 4 .   ? 18.097 -13.426 28.492 1.00 33.05 ? 323 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 4 .   ? 8.265  -22.140 32.909 1.00 42.73 ? 324 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 4 .   ? 37.488 -23.728 6.506  1.00 33.45 ? 325 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 4 .   ? 10.618 -11.890 13.636 1.00 26.05 ? 326 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 4 .   ? 24.717 -25.377 29.050 1.00 15.61 ? 327 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 4 .   ? 29.569 -24.855 7.973  1.00 29.83 ? 328 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 4 .   ? 24.145 -26.628 -1.159 1.00 25.80 ? 329 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 4 .   ? 23.115 -19.686 31.910 1.00 46.65 ? 330 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 4 .   ? 4.277  -19.353 13.577 1.00 23.60 ? 331 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 4 .   ? 3.874  -20.720 19.647 1.00 31.39 ? 332 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 4 .   ? 3.322  -14.898 26.984 1.00 40.02 ? 333 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 4 .   ? 4.585  -24.461 14.954 1.00 32.36 ? 334 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 4 .   ? 23.378 -12.954 27.041 1.00 56.03 ? 335 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 4 .   ? 30.997 -22.708 28.909 1.00 22.34 ? 336 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 4 .   ? 22.124 -5.330  10.704 1.00 29.00 ? 337 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 4 .   ? 11.866 -35.373 20.329 1.00 31.90 ? 338 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 4 .   ? -1.977 -18.665 17.658 1.00 34.42 ? 339 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 4 .   ? 33.948 -15.862 14.621 1.00 27.18 ? 340 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 4 .   ? 33.755 -30.923 15.549 1.00 14.26 ? 341 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 4 .   ? 22.361 -28.680 -1.021 1.00 20.41 ? 342 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 4 .   ? 25.997 -10.532 14.393 1.00 17.72 ? 343 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 4 .   ? 16.561 -9.325  14.129 1.00 29.64 ? 344 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 4 .   ? 23.333 -18.800 21.095 1.00 13.36 ? 345 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 4 .   ? 22.840 -35.274 33.396 1.00 26.72 ? 346 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 4 .   ? 19.299 -28.093 9.502  1.00 15.08 ? 347 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 4 .   ? 27.432 -36.263 3.352  1.00 32.84 ? 348 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 4 .   ? 16.515 -11.160 27.190 1.00 33.67 ? 349 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 4 .   ? 26.253 -27.592 29.636 1.00 17.69 ? 350 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 4 .   ? -0.429 -15.011 24.394 1.00 41.31 ? 351 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 4 .   ? 12.536 -11.536 15.523 1.00 22.03 ? 352 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 4 .   ? 5.932  -9.274  14.043 1.00 42.84 ? 353 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 4 .   ? 34.397 -28.551 7.781  1.00 34.22 ? 354 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 4 .   ? 13.201 -35.740 22.748 1.00 25.97 ? 355 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 4 .   ? 36.125 -30.803 27.969 1.00 34.76 ? 356 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 4 .   ? 5.333  -27.187 22.730 1.00 20.08 ? 357 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 4 .   ? 8.310  -32.241 26.635 1.00 36.81 ? 358 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 4 .   ? 16.368 -28.070 9.681  1.00 20.49 ? 359 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 4 .   ? 14.904 -30.791 5.575  1.00 27.19 ? 360 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 4 .   ? 16.895 -9.177  23.130 1.00 18.66 ? 361 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 4 .   ? 14.039 -14.370 6.809  1.00 49.70 ? 362 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 4 .   ? 20.408 -21.731 2.751  1.00 25.67 ? 363 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 4 .   ? 31.877 -30.207 28.775 1.00 31.66 ? 364 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 4 .   ? 29.759 -30.228 34.597 1.00 32.02 ? 365 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 4 .   ? 18.532 -18.274 8.505  1.00 20.51 ? 366 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 4 .   ? -1.027 -28.360 26.803 1.00 42.54 ? 367 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 4 .   ? 0.685  -20.062 19.762 1.00 41.59 ? 368 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 4 .   ? 4.107  -30.169 30.326 1.00 49.94 ? 369 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 4 .   ? 8.258  -26.597 13.291 1.00 36.69 ? 370 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 4 .   ? 18.253 -37.901 22.552 1.00 39.14 ? 371 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 4 .   ? 3.411  -9.914  16.310 1.00 21.13 ? 372 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 4 .   ? 32.313 -36.850 18.241 1.00 36.97 ? 373 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 4 .   ? 30.522 -7.667  10.093 1.00 28.95 ? 374 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 4 .   ? 14.038 -28.536 14.494 1.00 29.27 ? 375 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 4 .   ? 13.865 -27.732 35.232 1.00 38.71 ? 376 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 4 .   ? 12.569 -31.614 28.895 1.00 26.94 ? 377 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 4 .   ? 1.467  -16.167 26.087 1.00 41.38 ? 378 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 4 .   ? 26.795 -4.714  18.245 1.00 38.18 ? 379 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 4 .   ? 21.623 -19.850 23.161 1.00 12.70 ? 380 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 4 .   ? 17.795 -7.103  18.148 1.00 31.90 ? 381 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 4 .   ? 15.087 -21.562 7.068  1.00 27.84 ? 382 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 4 .   ? 4.094  -19.621 16.234 1.00 26.53 ? 383 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 4 .   ? 10.827 -13.030 29.612 1.00 34.90 ? 384 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 4 .   ? 33.768 -33.133 12.152 1.00 32.34 ? 385 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 4 .   ? 8.261  -20.892 11.692 1.00 26.46 ? 386 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 4 .   ? 26.561 -13.219 9.619  1.00 28.55 ? 387 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 4 .   ? 30.937 -35.429 25.795 1.00 24.02 ? 388 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 4 .   ? 5.086  -25.451 29.685 1.00 33.31 ? 389 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 4 .   ? 5.475  -9.318  22.457 1.00 41.80 ? 390 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 4 .   ? 16.211 -11.597 15.586 1.00 15.69 ? 391 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 4 .   ? 29.429 -17.134 7.293  1.00 35.07 ? 392 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 4 .   ? 15.149 -26.506 7.234  1.00 30.85 ? 393 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 4 .   ? 29.007 -32.103 8.211  1.00 19.28 ? 394 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 4 .   ? 0.314  -12.361 24.428 1.00 55.15 ? 395 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 4 .   ? 3.390  -21.293 27.741 1.00 28.54 ? 396 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 4 .   ? 29.103 -28.438 25.285 1.00 14.67 ? 397 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 4 .   ? 26.466 -38.830 8.301  1.00 30.87 ? 398 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 4 .   ? 28.156 -17.552 26.741 1.00 21.76 ? 399 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 4 .   ? 2.520  -15.735 12.135 1.00 19.65 ? 400 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 4 .   ? 20.514 -15.903 29.031 1.00 25.67 ? 401 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 4 .   ? 19.835 -35.007 15.493 1.00 20.33 ? 402 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 4 .   ? 12.571 -13.975 9.200  1.00 30.31 ? 403 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 4 .   ? 35.066 -14.955 18.626 1.00 25.64 ? 404 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 4 .   ? 10.784 -26.845 9.590  1.00 37.36 ? 405 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 4 .   ? 9.778  -23.003 12.627 1.00 21.46 ? 406 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 4 .   ? 5.486  -13.869 10.217 1.00 27.43 ? 407 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 4 .   ? 15.805 -30.718 13.422 1.00 21.33 ? 408 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 4 .   ? 6.087  -32.397 20.098 1.00 27.94 ? 409 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 4 .   ? 9.967  -14.255 10.039 1.00 41.77 ? 410 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 4 .   ? 26.629 -34.285 32.078 1.00 19.02 ? 411 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 4 .   ? 25.913 -37.867 23.076 1.00 26.60 ? 412 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 4 .   ? 23.224 -15.468 5.720  1.00 27.66 ? 413 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 4 .   ? 8.300  -32.323 18.736 1.00 25.74 ? 414 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 4 .   ? 13.558 -11.291 11.529 1.00 27.17 ? 415 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 4 .   ? 25.947 -12.371 7.235  1.00 39.53 ? 416 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 4 .   ? 19.357 -34.779 31.014 1.00 22.30 ? 417 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 4 .   ? 15.070 -6.504  17.538 1.00 20.27 ? 418 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 4 .   ? -0.620 -19.667 23.485 1.00 42.99 ? 419 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 4 .   ? 32.793 -16.912 26.665 1.00 28.54 ? 420 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 4 .   ? 28.877 -32.477 3.109  1.00 43.87 ? 421 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 4 .   ? 12.305 -11.438 26.964 1.00 24.34 ? 422 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 4 .   ? 22.626 -9.071  20.181 1.00 24.10 ? 423 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 4 .   ? 28.599 -7.586  21.216 1.00 27.36 ? 424 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 4 .   ? 5.592  -18.652 31.138 1.00 57.27 ? 425 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 4 .   ? 25.129 -9.287  21.743 1.00 36.03 ? 426 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 4 .   ? 18.646 -16.380 6.718  1.00 34.51 ? 427 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 4 .   ? 12.261 -21.848 11.911 1.00 18.43 ? 428 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 4 .   ? 20.293 -9.351  24.144 1.00 30.75 ? 429 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 4 .   ? -1.853 -31.351 22.921 1.00 40.23 ? 430 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 4 .   ? 16.612 -17.529 30.979 1.00 38.36 ? 431 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 4 .   ? 33.439 -33.583 14.875 1.00 19.70 ? 432 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 4 .   ? 30.045 -14.887 11.178 1.00 27.89 ? 433 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 4 .   ? 3.542  -27.952 20.752 1.00 25.60 ? 434 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 4 .   ? 10.958 -16.753 9.177  1.00 61.86 ? 435 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 4 .   ? 3.152  -11.533 23.918 1.00 37.33 ? 436 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 4 .   ? 10.564 -28.289 13.738 1.00 24.42 ? 437 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 4 .   ? 4.368  -10.932 25.973 1.00 37.20 ? 438 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 4 .   ? 17.609 -21.230 34.362 1.00 33.97 ? 439 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 4 .   ? 14.412 -7.979  15.277 1.00 28.10 ? 440 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 4 .   ? 22.543 -38.358 19.699 1.00 29.66 ? 441 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 4 .   ? 36.897 -34.926 17.886 1.00 45.67 ? 442 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 4 .   ? 23.349 -10.246 26.960 1.00 50.76 ? 443 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 4 .   ? 30.579 -33.063 10.252 1.00 42.85 ? 444 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 4 .   ? 16.926 -38.200 8.215  1.00 37.49 ? 445 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 4 .   ? 27.717 -19.671 28.400 1.00 37.80 ? 446 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 4 .   ? 3.983  -22.996 30.406 1.00 35.95 ? 447 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 4 .   ? 35.276 -35.160 15.917 1.00 34.09 ? 448 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 4 .   ? 23.723 -12.994 6.113  1.00 38.28 ? 449 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 4 .   ? 17.608 -33.800 14.888 1.00 37.96 ? 450 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 4 .   ? 27.584 -35.694 29.738 1.00 21.83 ? 451 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 4 .   ? 14.566 -22.913 37.037 1.00 36.80 ? 452 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 4 .   ? 28.340 -34.551 34.080 1.00 36.98 ? 453 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 4 .   ? 30.124 -28.275 27.787 1.00 33.26 ? 454 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 4 .   ? 17.612 -19.347 4.370  1.00 36.14 ? 455 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 4 .   ? 15.249 -23.265 4.490  1.00 35.31 ? 456 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 4 .   ? 17.944 -19.431 32.403 1.00 34.56 ? 457 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 4 .   ? 0.391  -24.227 18.999 1.00 50.34 ? 458 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 4 .   ? 15.342 -21.093 35.318 1.00 29.04 ? 459 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 4 .   ? 6.209  -23.998 37.372 1.00 53.85 ? 460 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 4 .   ? 4.149  -30.462 19.355 1.00 35.50 ? 461 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 4 .   ? 16.457 -19.496 6.859  1.00 27.43 ? 462 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 4 .   ? 30.407 -21.543 4.320  1.00 35.18 ? 463 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 4 .   ? 29.790 -32.902 5.672  1.00 36.44 ? 464 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 4 .   ? 3.194  -21.864 17.023 1.00 38.88 ? 465 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 4 .   ? -0.841 -23.107 28.934 1.00 79.03 ? 466 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 4 .   ? 8.551  -9.822  13.473 1.00 38.63 ? 467 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 4 .   ? 6.850  -29.569 30.437 1.00 53.60 ? 468 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 4 .   ? 5.441  -21.251 11.685 1.00 26.90 ? 469 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 4 .   ? -0.294 -30.779 30.846 1.00 77.32 ? 470 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 4 .   ? 17.164 -11.716 1.569  1.00 69.08 ? 471 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 4 .   ? 36.723 -22.575 4.388  1.00 47.79 ? 472 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 4 .   ? 11.769 -28.915 11.076 1.00 45.83 ? 473 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 4 .   ? 26.246 -23.247 29.799 1.00 30.60 ? 474 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 4 .   ? 36.808 -15.706 4.268  1.00 62.11 ? 475 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 4 .   ? 2.060  -18.467 11.963 1.00 25.28 ? 476 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 4 .   ? 30.644 -17.076 28.421 1.00 56.05 ? 477 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 4 .   ? 22.264 -6.921  18.554 1.00 35.30 ? 478 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 4 .   ? 20.783 -15.603 5.716  1.00 56.43 ? 479 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 4 .   ? 18.599 -40.169 21.235 1.00 38.02 ? 480 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 4 .   ? 27.644 -38.215 30.394 1.00 41.49 ? 481 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 4 .   ? 8.555  -17.094 8.654  1.00 37.56 ? 482 HOH   C O   1 
HETATM 2574 O  O   . HOH   H 4 .   ? 35.216 -6.264  22.462 1.00 43.67 ? 483 HOH   C O   1 
HETATM 2575 O  O   . HOH   H 4 .   ? 1.764  -8.528  17.986 1.00 27.55 ? 484 HOH   C O   1 
HETATM 2576 O  O   . HOH   H 4 .   ? 2.624  -26.077 18.866 1.00 28.98 ? 485 HOH   C O   1 
HETATM 2577 O  O   . HOH   H 4 .   ? -2.967 -15.994 25.320 1.00 60.02 ? 486 HOH   C O   1 
HETATM 2578 O  O   . HOH   H 4 .   ? 0.820  -21.118 27.996 1.00 48.06 ? 487 HOH   C O   1 
HETATM 2579 O  O   . HOH   H 4 .   ? 11.694 -20.597 9.545  1.00 27.76 ? 488 HOH   C O   1 
HETATM 2580 O  O   . HOH   H 4 .   ? 31.972 -6.297  18.291 1.00 52.81 ? 489 HOH   C O   1 
HETATM 2581 O  O   . HOH   H 4 .   ? 21.637 -19.262 34.263 1.00 33.08 ? 490 HOH   C O   1 
HETATM 2582 O  O   . HOH   H 4 .   ? 29.304 -24.276 30.127 1.00 33.93 ? 491 HOH   C O   1 
HETATM 2583 O  O   . HOH   H 4 .   ? 30.184 -18.513 4.419  1.00 41.84 ? 492 HOH   C O   1 
HETATM 2584 O  O   . HOH   H 4 .   ? 28.912 -26.916 29.635 1.00 28.55 ? 493 HOH   C O   1 
HETATM 2585 O  O   . HOH   H 4 .   ? 29.148 -39.129 9.372  1.00 28.70 ? 494 HOH   C O   1 
HETATM 2586 O  O   . HOH   H 4 .   ? 14.003 -18.758 35.552 1.00 31.15 ? 495 HOH   C O   1 
HETATM 2587 O  O   . HOH   H 4 .   ? 4.810  -7.702  23.633 1.00 28.68 ? 496 HOH   C O   1 
HETATM 2588 O  O   . HOH   H 4 .   ? -1.048 -9.121  24.058 1.00 58.85 ? 497 HOH   C O   1 
HETATM 2589 O  O   . HOH   H 4 .   ? 4.890  -29.775 16.606 1.00 48.92 ? 498 HOH   C O   1 
HETATM 2590 O  O   . HOH   H 4 .   ? 26.169 -6.493  21.361 1.00 55.63 ? 499 HOH   C O   1 
HETATM 2591 O  O   . HOH   H 4 .   ? 6.772  -30.518 15.122 1.00 43.52 ? 500 HOH   C O   1 
HETATM 2592 O  O   . HOH   H 4 .   ? 12.547 -35.767 0.611  1.00 48.35 ? 501 HOH   C O   1 
HETATM 2593 O  O   . HOH   H 4 .   ? 5.736  -17.110 8.369  1.00 44.28 ? 502 HOH   C O   1 
HETATM 2594 O  O   . HOH   H 4 .   ? 0.249  -7.651  26.033 1.00 65.24 ? 503 HOH   C O   1 
HETATM 2595 O  O   . HOH   H 4 .   ? 6.190  -18.836 5.909  1.00 40.40 ? 504 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   ? 0.2179 0.2247 0.2176 -0.0055 -0.0152 -0.0069 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2151 0.2236 0.2246 -0.0039 -0.0167 -0.0060 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2165 0.2247 0.2313 -0.0018 -0.0154 -0.0033 7   SER   A C   
4    O O   . SER   A 1   ? 0.2271 0.2340 0.2379 -0.0017 -0.0149 -0.0015 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2474 0.2573 0.2581 -0.0057 -0.0224 -0.0049 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2778 0.2874 0.2860 -0.0062 -0.0261 -0.0009 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1960 0.2049 0.2196 -0.0003 -0.0140 -0.0035 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1874 0.1952 0.2165 0.0012  -0.0117 -0.0017 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1792 0.1866 0.2138 0.0019  -0.0077 -0.0034 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1893 0.1971 0.2221 0.0015  -0.0064 -0.0054 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1635 0.1696 0.2049 0.0027  -0.0054 -0.0025 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1672 0.1721 0.2128 0.0027  -0.0009 -0.0041 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1691 0.1706 0.2163 0.0026  0.0036  -0.0039 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1751 0.1756 0.2237 0.0032  0.0030  -0.0022 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1783 0.1851 0.2342 0.0033  -0.0021 -0.0044 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1527 0.1519 0.1994 0.0015  0.0085  -0.0057 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1596 0.1546 0.2074 0.0004  0.0141  -0.0065 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1614 0.1557 0.2204 0.0010  0.0174  -0.0074 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1671 0.1628 0.2275 0.0006  0.0175  -0.0083 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1650 0.1574 0.2024 -0.0024 0.0174  -0.0079 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1577 0.1518 0.1860 -0.0030 0.0140  -0.0069 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1868 0.1739 0.2234 -0.0046 0.0237  -0.0095 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1757 0.1691 0.1952 -0.0058 0.0152  -0.0072 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1719 0.1641 0.2400 0.0018  0.0207  -0.0072 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1771 0.1686 0.2579 0.0023  0.0249  -0.0081 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1872 0.1722 0.2667 0.0000  0.0339  -0.0109 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2095 0.1915 0.2916 0.0003  0.0365  -0.0107 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1703 0.1651 0.2663 0.0053  0.0211  -0.0051 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1759 0.1766 0.2722 0.0063  0.0124  -0.0028 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2059 0.2081 0.2940 0.0066  0.0064  -0.0007 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1891 0.1930 0.2914 0.0063  0.0107  -0.0035 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2209 0.2276 0.3069 0.0066  -0.0008 0.0007  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2073 0.2160 0.3086 0.0064  0.0031  -0.0021 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2194 0.2292 0.3118 0.0064  -0.0025 -0.0002 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2525 0.2659 0.3418 0.0055  -0.0091 0.0003  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1813 0.1635 0.2552 -0.0028 0.0388  -0.0135 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2053 0.1805 0.2749 -0.0063 0.0479  -0.0167 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2184 0.1918 0.2956 -0.0073 0.0540  -0.0187 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2175 0.1934 0.2930 -0.0075 0.0517  -0.0183 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2316 0.2041 0.2820 -0.0104 0.0477  -0.0176 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2411 0.2174 0.2845 -0.0107 0.0426  -0.0161 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2623 0.2272 0.3057 -0.0154 0.0569  -0.0212 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2248 0.1940 0.3130 -0.0074 0.0619  -0.0208 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2363 0.2034 0.3334 -0.0085 0.0690  -0.0230 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2252 0.1996 0.3351 -0.0051 0.0630  -0.0206 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2210 0.2008 0.3421 -0.0012 0.0565  -0.0175 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2243 0.1987 0.3310 -0.0069 0.0644  -0.0215 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2078 0.1890 0.3257 -0.0042 0.0584  -0.0195 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1956 0.1803 0.3009 -0.0043 0.0504  -0.0178 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1973 0.1845 0.3052 -0.0043 0.0484  -0.0176 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2417 0.2215 0.3703 -0.0054 0.0655  -0.0216 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3247 0.3030 0.4723 -0.0041 0.0725  -0.0227 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3566 0.3407 0.5221 -0.0004 0.0679  -0.0201 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3209 0.2913 0.4647 -0.0074 0.0836  -0.0263 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1850 0.1697 0.2780 -0.0043 0.0459  -0.0166 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1704 0.1580 0.2524 -0.0042 0.0391  -0.0151 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1584 0.1503 0.2403 -0.0016 0.0314  -0.0129 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1733 0.1643 0.2565 -0.0008 0.0316  -0.0123 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1750 0.1582 0.2397 -0.0078 0.0415  -0.0156 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1893 0.1675 0.2498 -0.0115 0.0484  -0.0172 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2073 0.1869 0.2728 -0.0114 0.0486  -0.0170 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2278 0.1996 0.2789 -0.0156 0.0551  -0.0191 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2318 0.2063 0.2926 -0.0151 0.0553  -0.0181 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2410 0.2076 0.2860 -0.0198 0.0617  -0.0205 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2591 0.2270 0.3094 -0.0194 0.0619  -0.0199 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2954 0.2577 0.3389 -0.0240 0.0685  -0.0209 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1437 0.1396 0.2229 -0.0007 0.0251  -0.0118 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1489 0.1482 0.2246 0.0008  0.0182  -0.0101 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1584 0.1575 0.2215 -0.0003 0.0166  -0.0101 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1605 0.1598 0.2230 -0.0010 0.0169  -0.0106 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1433 0.1476 0.2290 0.0024  0.0127  -0.0093 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1751 0.1823 0.2544 0.0028  0.0058  -0.0083 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1908 0.2024 0.2783 0.0032  0.0000  -0.0074 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2009 0.2141 0.2810 0.0022  -0.0043 -0.0084 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2200 0.2346 0.2937 0.0018  -0.0092 -0.0076 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2314 0.2458 0.3038 0.0025  -0.0110 -0.0051 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2121 0.2272 0.2795 0.0003  -0.0115 -0.0093 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1633 0.1617 0.2173 -0.0006 0.0153  -0.0093 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1559 0.1546 0.2001 -0.0015 0.0137  -0.0087 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1500 0.1519 0.1930 -0.0001 0.0085  -0.0081 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1503 0.1526 0.1927 0.0006  0.0068  -0.0074 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1630 0.1589 0.1981 -0.0037 0.0161  -0.0084 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1659 0.1628 0.1934 -0.0047 0.0141  -0.0070 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1739 0.1652 0.2088 -0.0061 0.0222  -0.0097 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1408 0.1444 0.1831 0.0002  0.0065  -0.0084 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1485 0.1544 0.1887 0.0009  0.0026  -0.0086 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1439 0.1500 0.1796 0.0006  0.0029  -0.0086 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1522 0.1572 0.1880 0.0001  0.0050  -0.0079 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1749 0.1826 0.2213 0.0012  -0.0001 -0.0098 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2273 0.2359 0.2798 0.0017  -0.0016 -0.0089 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1824 0.1896 0.2335 0.0008  0.0019  -0.0110 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1322 0.1394 0.1646 0.0008  0.0009  -0.0091 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1313 0.1388 0.1626 0.0009  0.0018  -0.0092 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1386 0.1457 0.1752 0.0010  0.0024  -0.0107 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1410 0.1484 0.1801 0.0006  0.0009  -0.0126 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1430 0.1511 0.1703 0.0008  0.0007  -0.0104 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1543 0.1628 0.1767 0.0006  0.0003  -0.0090 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1751 0.1833 0.1952 0.0003  -0.0013 -0.0087 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1531 0.1622 0.1746 0.0006  0.0017  -0.0076 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1230 0.1293 0.1618 0.0012  0.0044  -0.0095 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1335 0.1388 0.1779 0.0012  0.0055  -0.0107 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1474 0.1527 0.1927 0.0009  0.0050  -0.0141 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1507 0.1555 0.1995 0.0001  0.0047  -0.0164 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1256 0.1299 0.1720 0.0015  0.0074  -0.0079 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1171 0.1196 0.1696 0.0014  0.0091  -0.0086 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1485 0.1501 0.2033 0.0019  0.0104  -0.0049 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1657 0.1649 0.2262 0.0018  0.0124  -0.0045 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1649 0.1627 0.2315 0.0024  0.0140  -0.0065 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1629 0.1614 0.2298 0.0028  0.0140  -0.0100 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1662 0.1615 0.2381 0.0022  0.0160  -0.0054 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1367 0.1423 0.1783 0.0010  0.0051  -0.0148 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1402 0.1447 0.1809 -0.0001 0.0056  -0.0186 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1592 0.1643 0.1958 -0.0020 0.0023  -0.0206 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1985 0.2022 0.2332 -0.0040 0.0023  -0.0241 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1624 0.1665 0.2011 0.0002  0.0080  -0.0190 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1546 0.1600 0.1864 -0.0002 0.0065  -0.0182 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1553 0.1624 0.1863 0.0009  0.0057  -0.0146 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1698 0.1744 0.1948 -0.0020 0.0059  -0.0206 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1520 0.1595 0.1768 0.0001  0.0048  -0.0149 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1729 0.1788 0.1937 -0.0017 0.0048  -0.0182 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1523 0.1590 0.1876 -0.0017 -0.0005 -0.0184 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1522 0.1600 0.1855 -0.0032 -0.0046 -0.0190 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1682 0.1774 0.2092 -0.0030 -0.0062 -0.0183 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1733 0.1842 0.2155 -0.0040 -0.0101 -0.0177 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1604 0.1689 0.1883 -0.0029 -0.0065 -0.0167 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1763 0.1837 0.1969 -0.0034 -0.0048 -0.0174 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2032 0.2110 0.2190 -0.0032 -0.0064 -0.0148 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.1924 0.1982 0.2078 -0.0063 -0.0050 -0.0211 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1606 0.1690 0.2074 -0.0020 -0.0031 -0.0180 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1504 0.1598 0.2051 -0.0019 -0.0034 -0.0176 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1562 0.1668 0.2145 -0.0041 -0.0064 -0.0200 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1750 0.1843 0.2307 -0.0056 -0.0060 -0.0228 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1616 0.1691 0.2200 -0.0011 0.0009  -0.0168 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1584 0.1715 0.2234 -0.0043 -0.0092 -0.0189 24  THR   A N   
135  C CA  . THR   A 18  ? 0.1635 0.1788 0.2331 -0.0068 -0.0132 -0.0207 24  THR   A CA  
136  C C   . THR   A 18  ? 0.1630 0.1779 0.2416 -0.0072 -0.0105 -0.0222 24  THR   A C   
137  O O   . THR   A 18  ? 0.1717 0.1849 0.2534 -0.0055 -0.0056 -0.0214 24  THR   A O   
138  C CB  . THR   A 18  ? 0.1886 0.2076 0.2633 -0.0069 -0.0183 -0.0177 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.1872 0.2070 0.2724 -0.0047 -0.0154 -0.0158 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2078 0.2267 0.2739 -0.0066 -0.0210 -0.0156 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1748 0.1918 0.2581 -0.0101 -0.0139 -0.0243 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.1824 0.1993 0.2757 -0.0107 -0.0115 -0.0257 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1606 0.1793 0.2642 -0.0086 -0.0095 -0.0229 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1760 0.1925 0.2842 -0.0078 -0.0041 -0.0231 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2262 0.2461 0.3236 -0.0147 -0.0168 -0.0280 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3245 0.3418 0.4117 -0.0181 -0.0179 -0.0319 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3795 0.3918 0.4616 -0.0174 -0.0121 -0.0344 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3645 0.3834 0.4461 -0.0224 -0.0239 -0.0336 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3961 0.4067 0.4701 -0.0212 -0.0137 -0.0382 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3940 0.4081 0.4660 -0.0246 -0.0208 -0.0380 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1576 0.1796 0.2647 -0.0077 -0.0131 -0.0201 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1542 0.1772 0.2721 -0.0057 -0.0100 -0.0179 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1496 0.1680 0.2616 -0.0036 -0.0032 -0.0172 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1608 0.1776 0.2790 -0.0031 0.0023  -0.0172 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.1665 0.1934 0.2905 -0.0050 -0.0150 -0.0147 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.2346 0.2668 0.3711 -0.0071 -0.0205 -0.0143 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.2446 0.2775 0.3904 -0.0081 -0.0181 -0.0161 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.2425 0.2784 0.3783 -0.0084 -0.0285 -0.0120 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1353 0.1516 0.2349 -0.0028 -0.0033 -0.0168 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1407 0.1530 0.2339 -0.0017 0.0023  -0.0160 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1420 0.1514 0.2356 -0.0024 0.0068  -0.0171 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1491 0.1558 0.2434 -0.0024 0.0118  -0.0162 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1518 0.1629 0.2327 -0.0011 0.0008  -0.0154 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1752 0.1877 0.2538 -0.0003 -0.0019 -0.0137 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1754 0.1880 0.2600 0.0005  -0.0003 -0.0123 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1716 0.1847 0.2428 -0.0006 -0.0054 -0.0137 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1312 0.1405 0.2236 -0.0034 0.0052  -0.0189 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1504 0.1567 0.2443 -0.0039 0.0093  -0.0195 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1634 0.1698 0.2679 -0.0049 0.0121  -0.0200 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1715 0.1746 0.2761 -0.0052 0.0171  -0.0191 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1492 0.1547 0.2408 -0.0049 0.0078  -0.0217 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1575 0.1611 0.2399 -0.0037 0.0082  -0.0208 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1809 0.1857 0.2570 -0.0037 0.0052  -0.0216 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1508 0.1514 0.2303 -0.0027 0.0117  -0.0184 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1779 0.1807 0.2487 -0.0025 0.0072  -0.0204 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1690 0.1696 0.2421 -0.0018 0.0106  -0.0180 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1641 0.1620 0.2458 -0.0028 0.0154  -0.0162 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1677 0.1663 0.2384 -0.0008 0.0127  -0.0151 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1831 0.1787 0.2606 -0.0021 0.0170  -0.0130 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1878 0.1842 0.2609 -0.0009 0.0153  -0.0124 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1582 0.1685 0.2718 -0.0055 0.0091  -0.0209 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1637 0.1749 0.2899 -0.0064 0.0120  -0.0215 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1710 0.1804 0.2995 -0.0055 0.0174  -0.0198 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1921 0.2006 0.3293 -0.0064 0.0223  -0.0203 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1655 0.1823 0.3023 -0.0075 0.0064  -0.0223 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1591 0.1681 0.2808 -0.0042 0.0169  -0.0183 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1770 0.1834 0.2991 -0.0039 0.0225  -0.0174 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1693 0.1710 0.2763 -0.0042 0.0252  -0.0163 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1592 0.1589 0.2615 -0.0041 0.0277  -0.0156 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1920 0.2015 0.3204 -0.0024 0.0199  -0.0165 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2091 0.2236 0.3545 -0.0024 0.0174  -0.0167 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2235 0.2376 0.3804 -0.0028 0.0226  -0.0173 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2038 0.2230 0.3510 -0.0024 0.0094  -0.0162 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1507 0.1505 0.2508 -0.0048 0.0248  -0.0159 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1535 0.1500 0.2406 -0.0051 0.0258  -0.0139 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1743 0.1661 0.2562 -0.0072 0.0319  -0.0129 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2016 0.1908 0.2872 -0.0089 0.0367  -0.0133 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1609 0.1564 0.2460 -0.0053 0.0247  -0.0133 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1629 0.1558 0.2372 -0.0055 0.0249  -0.0103 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1750 0.1703 0.2433 -0.0041 0.0208  -0.0099 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1780 0.1695 0.2537 -0.0054 0.0247  -0.0093 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1738 0.1641 0.2459 -0.0077 0.0321  -0.0117 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1985 0.1837 0.2617 -0.0108 0.0374  -0.0108 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2061 0.1897 0.2577 -0.0121 0.0352  -0.0074 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2324 0.2121 0.2783 -0.0149 0.0381  -0.0054 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2072 0.1914 0.2678 -0.0112 0.0393  -0.0120 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2299 0.2083 0.2782 -0.0154 0.0445  -0.0115 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2107 0.1962 0.2852 -0.0099 0.0421  -0.0145 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1784 0.1652 0.2271 -0.0101 0.0298  -0.0063 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1860 0.1723 0.2261 -0.0110 0.0272  -0.0027 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1663 0.1569 0.2087 -0.0079 0.0220  -0.0026 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1768 0.1698 0.2214 -0.0063 0.0204  -0.0049 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1963 0.1800 0.2249 -0.0142 0.0285  -0.0015 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2115 0.1960 0.2318 -0.0154 0.0246  0.0026  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2352 0.2179 0.2503 -0.0178 0.0237  0.0071  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2019 0.1895 0.2194 -0.0143 0.0207  0.0031  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2420 0.2273 0.2528 -0.0179 0.0190  0.0106  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2211 0.2093 0.2329 -0.0160 0.0175  0.0079  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2045 0.1947 0.2243 -0.0122 0.0195  0.0004  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2157 0.2071 0.2246 -0.0157 0.0135  0.0095  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2109 0.2035 0.2266 -0.0120 0.0160  0.0019  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2119 0.2054 0.2228 -0.0137 0.0132  0.0061  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1666 0.1578 0.2086 -0.0073 0.0197  0.0002  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1696 0.1642 0.2133 -0.0049 0.0160  0.0002  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1727 0.1674 0.2136 -0.0052 0.0142  0.0048  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1820 0.1743 0.2223 -0.0067 0.0152  0.0082  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1805 0.1764 0.2326 -0.0027 0.0155  -0.0029 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1809 0.1747 0.2389 -0.0030 0.0176  -0.0025 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.1968 0.1897 0.2564 -0.0023 0.0171  0.0009  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2503 0.2403 0.3120 -0.0033 0.0192  0.0032  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1901 0.1849 0.2499 -0.0008 0.0151  0.0014  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1585 0.1561 0.1988 -0.0039 0.0115  0.0054  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1558 0.1546 0.1961 -0.0039 0.0093  0.0102  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1601 0.1620 0.2054 -0.0012 0.0079  0.0088  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1598 0.1637 0.2018 -0.0011 0.0067  0.0073  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1895 0.1882 0.2202 -0.0072 0.0078  0.0134  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2602 0.2608 0.2912 -0.0080 0.0045  0.0195  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2703 0.2735 0.3095 -0.0052 0.0032  0.0206  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2687 0.2682 0.2914 -0.0118 0.0031  0.0231  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1596 0.1612 0.2133 0.0007  0.0088  0.0092  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1664 0.1699 0.2256 0.0029  0.0090  0.0075  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1669 0.1704 0.2258 0.0029  0.0089  0.0073  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1689 0.1756 0.2275 0.0029  0.0067  0.0111  36  SER   A C   
244  O O   . SER   A 30  ? 0.1834 0.1919 0.2423 0.0039  0.0069  0.0086  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1995 0.2012 0.2685 0.0045  0.0112  0.0079  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1993 0.2009 0.2678 0.0045  0.0114  0.0068  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2557 0.2581 0.3300 0.0061  0.0128  0.0051  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2553 0.2566 0.3289 0.0048  0.0108  0.0130  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1657 0.1730 0.2231 0.0014  0.0044  0.0171  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1753 0.1864 0.2333 0.0010  0.0015  0.0211  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1868 0.1994 0.2357 -0.0006 0.0004  0.0186  37  SER   A C   
252  O O   . SER   A 31  ? 0.1968 0.2127 0.2472 -0.0006 -0.0013 0.0202  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2138 0.2257 0.2717 -0.0010 -0.0018 0.0287  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2953 0.3055 0.3410 -0.0050 -0.0031 0.0295  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1675 0.1776 0.2085 -0.0020 0.0016  0.0150  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1520 0.1626 0.1853 -0.0034 0.0011  0.0127  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1576 0.1679 0.1916 -0.0014 0.0028  0.0073  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1532 0.1639 0.1821 -0.0022 0.0025  0.0055  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1544 0.1619 0.1789 -0.0066 0.0018  0.0125  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1570 0.1645 0.1769 -0.0101 -0.0005 0.0179  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1763 0.1797 0.1860 -0.0143 0.0013  0.0173  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1705 0.1732 0.1737 -0.0159 0.0023  0.0139  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1878 0.1873 0.1810 -0.0205 0.0036  0.0135  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2100 0.2066 0.1966 -0.0245 0.0038  0.0163  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1823 0.1811 0.1712 -0.0217 0.0048  0.0104  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1385 0.1478 0.1781 0.0005  0.0044  0.0047  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1372 0.1459 0.1761 0.0014  0.0053  -0.0001 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1407 0.1479 0.1749 0.0003  0.0052  -0.0016 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1452 0.1528 0.1771 0.0005  0.0046  -0.0039 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1435 0.1539 0.1814 0.0021  0.0051  -0.0016 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1348 0.1442 0.1707 0.0023  0.0054  -0.0059 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1433 0.1513 0.1822 0.0025  0.0062  -0.0082 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1471 0.1572 0.1782 0.0018  0.0047  -0.0067 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1334 0.1388 0.1669 -0.0009 0.0061  -0.0003 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1321 0.1357 0.1635 -0.0018 0.0073  -0.0021 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1324 0.1345 0.1687 -0.0017 0.0090  -0.0034 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1475 0.1485 0.1863 -0.0020 0.0099  -0.0018 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1505 0.1525 0.1753 -0.0045 0.0082  -0.0002 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1567 0.1600 0.1763 -0.0053 0.0068  0.0005  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1741 0.1749 0.1861 -0.0090 0.0082  0.0017  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1646 0.1684 0.1847 -0.0040 0.0066  -0.0021 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1353 0.1371 0.1741 -0.0015 0.0095  -0.0058 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1337 0.1343 0.1783 -0.0017 0.0115  -0.0070 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1398 0.1395 0.1852 -0.0023 0.0132  -0.0080 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1436 0.1445 0.1883 -0.0016 0.0116  -0.0085 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1244 0.1266 0.1751 -0.0006 0.0097  -0.0093 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1344 0.1360 0.1927 -0.0010 0.0114  -0.0107 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1545 0.1564 0.2171 -0.0008 0.0106  -0.0122 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1420 0.1453 0.2057 -0.0008 0.0103  -0.0121 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1347 0.1319 0.1825 -0.0037 0.0170  -0.0083 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1391 0.1347 0.1902 -0.0043 0.0203  -0.0096 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1482 0.1444 0.2101 -0.0039 0.0220  -0.0110 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1612 0.1561 0.2240 -0.0048 0.0237  -0.0108 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1564 0.1477 0.1999 -0.0073 0.0250  -0.0091 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1715 0.1603 0.2201 -0.0080 0.0299  -0.0112 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1745 0.1658 0.2079 -0.0082 0.0228  -0.0076 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1511 0.1495 0.2219 -0.0025 0.0210  -0.0120 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1439 0.1437 0.2271 -0.0022 0.0221  -0.0132 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1646 0.1628 0.2552 -0.0024 0.0269  -0.0138 43  SER   A C   
300  O O   . SER   A 37  ? 0.1695 0.1660 0.2564 -0.0023 0.0282  -0.0135 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1509 0.1556 0.2403 -0.0008 0.0156  -0.0134 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1645 0.1713 0.2540 0.0004  0.0118  -0.0123 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1585 0.1569 0.2606 -0.0027 0.0302  -0.0149 44  SER   A N   
304  C CA  . SER   A 38  ? 0.1663 0.1632 0.2785 -0.0028 0.0359  -0.0158 44  SER   A CA  
305  C C   . SER   A 38  ? 0.1783 0.1803 0.3046 -0.0003 0.0313  -0.0146 44  SER   A C   
306  O O   . SER   A 38  ? 0.1965 0.2036 0.3275 0.0007  0.0244  -0.0136 44  SER   A O   
307  C CB  . SER   A 38  ? 0.1965 0.1910 0.3153 -0.0046 0.0426  -0.0174 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2215 0.2206 0.3501 -0.0039 0.0386  -0.0173 44  SER   A OG  
309  N N   . THR   A 39  ? 0.1820 0.1825 0.3160 0.0005  0.0354  -0.0145 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2035 0.2088 0.3526 0.0030  0.0309  -0.0122 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2301 0.2348 0.3981 0.0035  0.0378  -0.0130 45  THR   A C   
312  O O   . THR   A 39  ? 0.2486 0.2475 0.4144 0.0016  0.0475  -0.0157 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2292 0.2333 0.3723 0.0043  0.0286  -0.0105 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2519 0.2499 0.3937 0.0034  0.0376  -0.0123 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2407 0.2447 0.3652 0.0037  0.0235  -0.0101 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2414 0.2520 0.4278 0.0056  0.0331  -0.0103 46  THR   A N   
317  C CA  . THR   A 40  ? 0.2542 0.2649 0.4619 0.0065  0.0397  -0.0105 46  THR   A CA  
318  C C   . THR   A 40  ? 0.2833 0.2909 0.4962 0.0083  0.0434  -0.0093 46  THR   A C   
319  O O   . THR   A 40  ? 0.3101 0.3135 0.5339 0.0082  0.0535  -0.0112 46  THR   A O   
320  C CB  . THR   A 40  ? 0.2700 0.2893 0.4980 0.0077  0.0327  -0.0077 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.2870 0.3114 0.5132 0.0090  0.0212  -0.0035 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2843 0.3055 0.5101 0.0055  0.0314  -0.0097 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2668 0.2759 0.4722 0.0096  0.0360  -0.0063 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2672 0.2730 0.4774 0.0113  0.0391  -0.0048 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2689 0.2665 0.4586 0.0091  0.0459  -0.0084 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2696 0.2661 0.4398 0.0071  0.0434  -0.0099 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2776 0.2887 0.4896 0.0135  0.0277  0.0007  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2679 0.2599 0.4626 0.0094  0.0537  -0.0094 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2826 0.2667 0.4587 0.0067  0.0598  -0.0127 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2956 0.2811 0.4592 0.0076  0.0516  -0.0099 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3061 0.2953 0.4803 0.0106  0.0457  -0.0054 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3199 0.2972 0.5078 0.0065  0.0715  -0.0152 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4059 0.3746 0.5761 0.0031  0.0782  -0.0189 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.4962 0.4593 0.6483 -0.0022 0.0848  -0.0239 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5176 0.4820 0.6719 -0.0032 0.0867  -0.0251 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5151 0.4718 0.6485 -0.0060 0.0883  -0.0266 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2960 0.2788 0.4377 0.0048  0.0510  -0.0119 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3116 0.2960 0.4412 0.0054  0.0435  -0.0094 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3460 0.3256 0.4730 0.0053  0.0465  -0.0092 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3907 0.3634 0.5159 0.0029  0.0559  -0.0129 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3197 0.3022 0.4423 0.0068  0.0387  -0.0056 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3095 0.2882 0.4301 0.0071  0.0399  -0.0044 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3099 0.2836 0.4109 0.0034  0.0431  -0.0077 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3013 0.2705 0.4019 0.0030  0.0465  -0.0079 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3121 0.2960 0.4362 0.0100  0.0300  0.0013  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3401 0.3294 0.4463 0.0089  0.0203  0.0022  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3028 0.2774 0.3889 0.0007  0.0420  -0.0100 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2848 0.2567 0.3528 -0.0029 0.0426  -0.0119 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2773 0.2426 0.3357 -0.0080 0.0511  -0.0167 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3099 0.2736 0.3731 -0.0088 0.0560  -0.0188 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2750 0.2527 0.3335 -0.0026 0.0345  -0.0102 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3134 0.2959 0.3751 0.0006  0.0266  -0.0062 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3437 0.3246 0.4046 0.0010  0.0261  -0.0047 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2426 0.2303 0.3065 0.0022  0.0210  -0.0047 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2618 0.2236 0.3057 -0.0119 0.0524  -0.0184 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2853 0.2410 0.3151 -0.0183 0.0584  -0.0224 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2655 0.2253 0.2807 -0.0205 0.0516  -0.0208 52  THR   A C   
358  O O   . THR   A 46  ? 0.2615 0.2252 0.2752 -0.0186 0.0456  -0.0183 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3458 0.2948 0.3729 -0.0210 0.0640  -0.0249 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3967 0.3403 0.4369 -0.0200 0.0723  -0.0270 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3691 0.3128 0.3781 -0.0287 0.0678  -0.0286 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2383 0.1972 0.2436 -0.0245 0.0526  -0.0220 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2225 0.1855 0.2162 -0.0266 0.0461  -0.0197 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2280 0.1867 0.2081 -0.0330 0.0482  -0.0216 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2478 0.1994 0.2217 -0.0381 0.0555  -0.0253 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2188 0.1835 0.2095 -0.0275 0.0450  -0.0187 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2320 0.2001 0.2363 -0.0220 0.0438  -0.0176 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2299 0.1994 0.2119 -0.0288 0.0378  -0.0154 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2382 0.2129 0.2497 -0.0167 0.0365  -0.0147 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2121 0.1747 0.1873 -0.0333 0.0425  -0.0195 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2187 0.1786 0.1812 -0.0398 0.0429  -0.0208 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2274 0.1870 0.1780 -0.0454 0.0417  -0.0201 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2232 0.1876 0.1754 -0.0432 0.0371  -0.0168 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2111 0.1767 0.1735 -0.0382 0.0363  -0.0180 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2362 0.1896 0.1744 -0.0531 0.0459  -0.0231 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2598 0.2124 0.1840 -0.0599 0.0440  -0.0219 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2813 0.2338 0.1944 -0.0664 0.0411  -0.0220 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3053 0.2505 0.2084 -0.0733 0.0468  -0.0265 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2616 0.2056 0.1794 -0.0647 0.0529  -0.0260 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2693 0.2132 0.2004 -0.0584 0.0567  -0.0264 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3023 0.2535 0.2383 -0.0540 0.0496  -0.0212 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2844 0.2350 0.2329 -0.0489 0.0538  -0.0223 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3063 0.2627 0.2634 -0.0436 0.0491  -0.0189 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2622 0.2248 0.2172 -0.0424 0.0409  -0.0143 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3043 0.2602 0.2731 -0.0397 0.0530  -0.0201 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2722 0.2329 0.1880 -0.0642 0.0325  -0.0174 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2769 0.2392 0.1863 -0.0690 0.0290  -0.0171 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2804 0.2525 0.1929 -0.0672 0.0191  -0.0108 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2692 0.2462 0.1892 -0.0619 0.0156  -0.0070 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2585 0.2191 0.1760 -0.0652 0.0325  -0.0200 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2499 0.2188 0.1846 -0.0541 0.0277  -0.0161 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2991 0.2741 0.2076 -0.0714 0.0150  -0.0098 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2907 0.2753 0.2051 -0.0695 0.0063  -0.0039 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2740 0.2620 0.1970 -0.0658 0.0057  -0.0045 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2895 0.2842 0.2152 -0.0669 -0.0003 -0.0009 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3562 0.3432 0.2595 -0.0783 0.0002  -0.0005 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4901 0.4734 0.3828 -0.0867 0.0014  -0.0040 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4909 0.4683 0.3839 -0.0861 0.0084  -0.0097 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5914 0.5778 0.4759 -0.0941 -0.0048 -0.0008 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2471 0.2312 0.1761 -0.0608 0.0114  -0.0081 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2298 0.2168 0.1666 -0.0571 0.0108  -0.0080 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2286 0.2245 0.1749 -0.0521 0.0049  -0.0033 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2247 0.2232 0.1755 -0.0481 0.0032  -0.0010 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2382 0.2199 0.1807 -0.0520 0.0169  -0.0112 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2565 0.2274 0.1919 -0.0573 0.0255  -0.0173 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2113 0.2115 0.1613 -0.0523 0.0024  -0.0021 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2016 0.2094 0.1619 -0.0475 -0.0015 0.0016  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1910 0.1983 0.1567 -0.0437 0.0013  0.0000  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1802 0.1931 0.1532 -0.0412 -0.0009 0.0022  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2219 0.2368 0.1835 -0.0516 -0.0076 0.0057  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2905 0.3082 0.2509 -0.0530 -0.0120 0.0095  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3356 0.3618 0.3016 -0.0557 -0.0188 0.0148  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3822 0.4091 0.3406 -0.0630 -0.0226 0.0164  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2749 0.3075 0.2542 -0.0504 -0.0204 0.0175  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1837 0.1838 0.1461 -0.0435 0.0065  -0.0036 60  THR   A N   
416  C CA  . THR   A 54  ? 0.1847 0.1831 0.1515 -0.0396 0.0091  -0.0044 60  THR   A CA  
417  C C   . THR   A 54  ? 0.1860 0.1786 0.1536 -0.0359 0.0129  -0.0062 60  THR   A C   
418  O O   . THR   A 54  ? 0.1904 0.1785 0.1542 -0.0378 0.0154  -0.0082 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2168 0.2127 0.1809 -0.0436 0.0111  -0.0060 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2524 0.2410 0.2098 -0.0479 0.0151  -0.0095 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2333 0.2355 0.1979 -0.0478 0.0070  -0.0041 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1754 0.1682 0.1481 -0.0310 0.0133  -0.0054 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1731 0.1615 0.1486 -0.0273 0.0159  -0.0061 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1597 0.1492 0.1394 -0.0230 0.0149  -0.0043 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1702 0.1621 0.1496 -0.0234 0.0139  -0.0032 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1564 0.1441 0.1398 -0.0193 0.0152  -0.0038 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1427 0.1304 0.1286 -0.0158 0.0139  -0.0018 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1489 0.1393 0.1379 -0.0126 0.0114  -0.0011 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1553 0.1446 0.1470 -0.0120 0.0122  -0.0021 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1629 0.1448 0.1512 -0.0152 0.0165  -0.0012 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.1743 0.1565 0.1645 -0.0120 0.0139  0.0019  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1846 0.1633 0.1698 -0.0187 0.0194  -0.0021 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1532 0.1467 0.1418 -0.0108 0.0088  0.0001  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1324 0.1279 0.1236 -0.0083 0.0065  0.0003  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1479 0.1424 0.1387 -0.0067 0.0045  0.0022  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1522 0.1454 0.1396 -0.0075 0.0048  0.0035  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1436 0.1437 0.1346 -0.0082 0.0053  -0.0005 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1393 0.1414 0.1281 -0.0084 0.0050  -0.0002 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1495 0.1524 0.1367 -0.0103 0.0064  0.0001  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1538 0.1568 0.1421 -0.0070 0.0038  -0.0005 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1543 0.1588 0.1403 -0.0106 0.0072  0.0000  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1527 0.1567 0.1383 -0.0077 0.0048  -0.0009 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1585 0.1632 0.1433 -0.0094 0.0068  -0.0006 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.1770 0.1825 0.1602 -0.0102 0.0088  -0.0012 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1433 0.1385 0.1374 -0.0048 0.0023  0.0026  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1464 0.1413 0.1393 -0.0040 -0.0008 0.0047  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1585 0.1559 0.1469 -0.0046 -0.0022 0.0034  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1571 0.1569 0.1475 -0.0041 -0.0022 0.0014  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1535 0.1478 0.1534 -0.0022 -0.0029 0.0062  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.1649 0.1593 0.1631 -0.0021 -0.0074 0.0092  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.1793 0.1710 0.1748 -0.0027 -0.0083 0.0125  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.1771 0.1741 0.1756 -0.0020 -0.0110 0.0088  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.1943 0.1859 0.1865 -0.0033 -0.0131 0.0160  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.1856 0.1826 0.1804 -0.0031 -0.0157 0.0116  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2047 0.1992 0.1961 -0.0038 -0.0170 0.0154  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2556 0.2499 0.2421 -0.0055 -0.0224 0.0189  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1620 0.1585 0.1441 -0.0058 -0.0029 0.0046  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1577 0.1553 0.1343 -0.0071 -0.0029 0.0028  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.1659 0.1622 0.1379 -0.0081 -0.0070 0.0047  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.1853 0.1790 0.1517 -0.0094 -0.0081 0.0074  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.1676 0.1647 0.1396 -0.0088 0.0004  0.0023  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.1878 0.1849 0.1528 -0.0109 0.0022  -0.0002 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.1636 0.1614 0.1376 -0.0077 -0.0094 0.0034  66  SER   A N   
464  C CA  . SER   A 60  ? 0.1765 0.1737 0.1464 -0.0093 -0.0142 0.0053  66  SER   A CA  
465  C C   . SER   A 60  ? 0.1854 0.1803 0.1430 -0.0129 -0.0140 0.0047  66  SER   A C   
466  O O   . SER   A 60  ? 0.2080 0.2012 0.1595 -0.0150 -0.0180 0.0081  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2113 0.2108 0.1864 -0.0087 -0.0166 0.0037  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.2971 0.2973 0.2703 -0.0095 -0.0137 -0.0008 66  SER   A OG  
469  N N   . SER   A 61  ? 0.1779 0.1727 0.1323 -0.0138 -0.0088 0.0007  67  SER   A N   
470  C CA  . SER   A 61  ? 0.1845 0.1765 0.1272 -0.0176 -0.0067 -0.0009 67  SER   A CA  
471  C C   . SER   A 61  ? 0.1856 0.1748 0.1221 -0.0190 -0.0056 0.0021  67  SER   A C   
472  O O   . SER   A 61  ? 0.2086 0.1948 0.1341 -0.0227 -0.0037 0.0013  67  SER   A O   
473  C CB  . SER   A 61  ? 0.2016 0.1942 0.1453 -0.0180 -0.0007 -0.0060 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.1929 0.1874 0.1440 -0.0156 0.0031  -0.0061 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.1810 0.1706 0.1237 -0.0166 -0.0065 0.0055  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.1930 0.1796 0.1312 -0.0177 -0.0059 0.0091  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.1916 0.1771 0.1338 -0.0162 -0.0110 0.0146  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2103 0.1929 0.1501 -0.0168 -0.0109 0.0184  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2034 0.1908 0.1465 -0.0165 -0.0005 0.0075  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.1948 0.1832 0.1355 -0.0181 0.0048  0.0031  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2070 0.1915 0.1360 -0.0220 0.0072  0.0035  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2298 0.2150 0.1585 -0.0234 0.0136  -0.0011 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2348 0.2195 0.1598 -0.0250 0.0156  -0.0049 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2393 0.2228 0.1590 -0.0260 0.0111  -0.0048 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2347 0.2198 0.1616 -0.0260 0.0223  -0.0088 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2048 0.1928 0.1554 -0.0139 -0.0147 0.0152  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2273 0.2149 0.1860 -0.0118 -0.0185 0.0201  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2286 0.2141 0.1924 -0.0102 -0.0144 0.0211  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.2531 0.2356 0.2182 -0.0099 -0.0158 0.0258  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2736 0.2593 0.2263 -0.0140 -0.0247 0.0257  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3409 0.3296 0.2966 -0.0143 -0.0305 0.0263  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.3780 0.3655 0.3294 -0.0166 -0.0380 0.0332  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.3821 0.3715 0.3267 -0.0201 -0.0431 0.0322  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.3863 0.3732 0.3147 -0.0255 -0.0457 0.0331  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.3956 0.3780 0.3133 -0.0277 -0.0432 0.0350  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.3561 0.3444 0.2778 -0.0292 -0.0498 0.0311  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2084 0.1951 0.1745 -0.0095 -0.0093 0.0167  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2005 0.1851 0.1694 -0.0092 -0.0052 0.0169  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.1869 0.1737 0.1625 -0.0079 -0.0021 0.0131  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.1894 0.1794 0.1656 -0.0076 -0.0021 0.0101  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2454 0.2288 0.2059 -0.0118 -0.0019 0.0159  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3526 0.3319 0.3058 -0.0137 -0.0031 0.0203  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4523 0.4305 0.3997 -0.0161 0.0017  0.0185  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5373 0.5106 0.4783 -0.0181 0.0017  0.0230  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.5829 0.5543 0.5136 -0.0204 -0.0020 0.0258  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.1799 0.1644 0.1599 -0.0076 0.0007  0.0133  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.1618 0.1476 0.1453 -0.0078 0.0039  0.0098  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.1837 0.1698 0.1628 -0.0102 0.0069  0.0083  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2053 0.1886 0.1813 -0.0115 0.0081  0.0101  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.1634 0.1457 0.1537 -0.0070 0.0059  0.0102  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.1809 0.1632 0.1784 -0.0045 0.0038  0.0117  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2204 0.2045 0.2225 -0.0037 0.0045  0.0091  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.1956 0.1765 0.1970 -0.0030 0.0007  0.0159  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2068 0.1906 0.2165 -0.0016 0.0024  0.0115  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2494 0.2317 0.2593 -0.0010 -0.0004 0.0158  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1567 0.1463 0.1365 -0.0110 0.0080  0.0055  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1580 0.1491 0.1359 -0.0134 0.0102  0.0043  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1646 0.1569 0.1451 -0.0150 0.0114  0.0024  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1641 0.1580 0.1467 -0.0143 0.0105  0.0013  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1680 0.1636 0.1448 -0.0134 0.0099  0.0033  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.1828 0.1769 0.1545 -0.0133 0.0096  0.0043  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2043 0.1959 0.1717 -0.0151 0.0115  0.0056  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.1850 0.1799 0.1554 -0.0121 0.0076  0.0039  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2119 0.2014 0.1725 -0.0159 0.0114  0.0068  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2028 0.1958 0.1664 -0.0131 0.0073  0.0046  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2219 0.2121 0.1801 -0.0151 0.0092  0.0061  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.2544 0.2421 0.2039 -0.0169 0.0090  0.0069  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1557 0.1471 0.1350 -0.0179 0.0135  0.0019  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1610 0.1538 0.1409 -0.0207 0.0140  0.0001  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.1772 0.1766 0.1590 -0.0213 0.0121  0.0001  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2006 0.2029 0.1835 -0.0207 0.0122  0.0008  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.1746 0.1643 0.1528 -0.0240 0.0166  -0.0002 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.1857 0.1753 0.1629 -0.0230 0.0170  0.0016  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1657 0.1548 0.1427 -0.0192 0.0152  0.0031  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1663 0.1677 0.1487 -0.0226 0.0108  -0.0006 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1663 0.1742 0.1522 -0.0231 0.0084  0.0003  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1573 0.1669 0.1420 -0.0273 0.0069  0.0004  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1751 0.1807 0.1554 -0.0294 0.0078  -0.0010 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.1889 0.1987 0.1776 -0.0196 0.0069  0.0007  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2058 0.2157 0.1957 -0.0165 0.0078  0.0007  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2035 0.2095 0.1900 -0.0189 0.0071  -0.0003 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1597 0.1754 0.1487 -0.0289 0.0046  0.0021  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1634 0.1826 0.1521 -0.0329 0.0013  0.0034  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1688 0.1924 0.1634 -0.0298 -0.0013 0.0058  75  SER   A C   
545  O O   . SER   A 69  ? 0.1723 0.1993 0.1740 -0.0265 -0.0008 0.0066  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2084 0.2324 0.2007 -0.0365 -0.0003 0.0048  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3093 0.3285 0.2961 -0.0396 0.0025  0.0025  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1536 0.1763 0.1450 -0.0308 -0.0031 0.0064  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1492 0.1750 0.1460 -0.0278 -0.0050 0.0086  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1563 0.1857 0.1530 -0.0315 -0.0096 0.0121  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1755 0.2033 0.1645 -0.0370 -0.0109 0.0120  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1575 0.1783 0.1514 -0.0245 -0.0027 0.0065  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1579 0.1727 0.1434 -0.0270 -0.0009 0.0042  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1682 0.1780 0.1502 -0.0270 0.0025  0.0014  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1724 0.1861 0.1537 -0.0297 -0.0020 0.0050  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1748 0.1785 0.1510 -0.0291 0.0053  -0.0010 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1867 0.1940 0.1604 -0.0323 0.0011  0.0022  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1879 0.1903 0.1600 -0.0318 0.0050  -0.0009 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1460 0.1802 0.1516 -0.0289 -0.0119 0.0155  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1577 0.1957 0.1645 -0.0320 -0.0170 0.0202  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1721 0.2053 0.1702 -0.0333 -0.0170 0.0198  77  SER   A C   
562  O O   . SER   A 71  ? 0.1740 0.2019 0.1688 -0.0305 -0.0130 0.0163  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1701 0.2144 0.1912 -0.0284 -0.0190 0.0244  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1911 0.2327 0.2157 -0.0230 -0.0155 0.0224  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1736 0.2081 0.1668 -0.0386 -0.0215 0.0235  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1874 0.2170 0.1714 -0.0407 -0.0211 0.0235  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1981 0.2281 0.1899 -0.0352 -0.0206 0.0252  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.1916 0.2270 0.1958 -0.0315 -0.0224 0.0284  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2204 0.2514 0.1963 -0.0484 -0.0267 0.0277  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2391 0.2675 0.2043 -0.0549 -0.0260 0.0244  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3318 0.3616 0.2877 -0.0634 -0.0322 0.0287  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4271 0.4525 0.3697 -0.0711 -0.0306 0.0244  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4854 0.5106 0.4153 -0.0806 -0.0361 0.0280  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1880 0.2124 0.1737 -0.0348 -0.0176 0.0231  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.1862 0.2107 0.1795 -0.0299 -0.0168 0.0244  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.1950 0.2248 0.1959 -0.0301 -0.0221 0.0314  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2217 0.2522 0.2163 -0.0355 -0.0264 0.0357  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2181 0.2358 0.2018 -0.0316 -0.0134 0.0217  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2444 0.2577 0.2182 -0.0352 -0.0103 0.0171  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2021 0.2195 0.1747 -0.0390 -0.0141 0.0190  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1728 0.2058 0.1872 -0.0246 -0.0216 0.0327  80  SER   A N   
582  C CA  . SER   A 74  ? 0.1884 0.2267 0.2136 -0.0239 -0.0262 0.0397  80  SER   A CA  
583  C C   . SER   A 74  ? 0.1783 0.2166 0.2160 -0.0177 -0.0232 0.0396  80  SER   A C   
584  O O   . SER   A 74  ? 0.1674 0.2019 0.2043 -0.0144 -0.0182 0.0339  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2556 0.3008 0.2881 -0.0254 -0.0299 0.0429  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3463 0.3932 0.3890 -0.0204 -0.0259 0.0395  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.1722 0.2147 0.2220 -0.0165 -0.0267 0.0463  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.1940 0.2361 0.2569 -0.0112 -0.0238 0.0469  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.1940 0.2404 0.2710 -0.0075 -0.0214 0.0456  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2121 0.2646 0.2989 -0.0084 -0.0252 0.0510  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2140 0.2581 0.2831 -0.0123 -0.0288 0.0556  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2576 0.2997 0.3383 -0.0077 -0.0259 0.0569  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2677 0.3028 0.3391 -0.0068 -0.0210 0.0509  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2753 0.3198 0.3624 -0.0092 -0.0317 0.0669  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.1797 0.2228 0.2578 -0.0040 -0.0151 0.0387  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.1945 0.2400 0.2826 -0.0013 -0.0113 0.0360  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.1925 0.2353 0.2902 0.0030  -0.0058 0.0331  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.1934 0.2309 0.2843 0.0038  -0.0033 0.0290  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2278 0.2714 0.3040 -0.0027 -0.0091 0.0297  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2529 0.2987 0.3205 -0.0073 -0.0139 0.0323  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2420 0.2867 0.3258 -0.0004 -0.0042 0.0261  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2798 0.3233 0.3363 -0.0090 -0.0120 0.0272  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.1764 0.2225 0.2907 0.0055  -0.0035 0.0349  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.1798 0.2226 0.3040 0.0091  0.0029  0.0315  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.1835 0.2216 0.2981 0.0092  0.0087  0.0227  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.1919 0.2313 0.3016 0.0079  0.0096  0.0201  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.1891 0.2365 0.3346 0.0115  0.0050  0.0354  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2100 0.2532 0.3663 0.0148  0.0130  0.0312  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2343 0.2750 0.3987 0.0168  0.0135  0.0338  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2343 0.2752 0.3911 0.0153  0.0204  0.0241  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2548 0.2907 0.4288 0.0193  0.0215  0.0293  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2474 0.2835 0.4128 0.0174  0.0284  0.0195  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.2475 0.2812 0.4221 0.0195  0.0290  0.0219  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.1813 0.2138 0.2924 0.0103  0.0122  0.0182  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.1899 0.2178 0.2917 0.0099  0.0169  0.0103  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.2159 0.2403 0.3279 0.0119  0.0235  0.0068  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.2218 0.2442 0.3395 0.0132  0.0237  0.0083  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.1971 0.2216 0.2834 0.0083  0.0142  0.0077  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.2142 0.2344 0.2917 0.0076  0.0180  0.0004  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.1887 0.2157 0.2654 0.0061  0.0090  0.0105  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.2305 0.2532 0.3434 0.0116  0.0295  0.0017  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.2232 0.2415 0.3443 0.0126  0.0372  -0.0030 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.2270 0.2395 0.3390 0.0117  0.0381  -0.0078 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.2240 0.2358 0.3214 0.0099  0.0339  -0.0092 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.2672 0.2839 0.3857 0.0112  0.0436  -0.0087 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.3846 0.3987 0.5184 0.0125  0.0528  -0.0115 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5127 0.5254 0.6440 0.0106  0.0596  -0.0166 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5609 0.5691 0.6997 0.0104  0.0688  -0.0217 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5441 0.5595 0.6657 0.0090  0.0562  -0.0158 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.2196 0.2280 0.3411 0.0127  0.0440  -0.0105 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.2201 0.2230 0.3339 0.0112  0.0452  -0.0156 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.2294 0.2292 0.3256 0.0076  0.0458  -0.0225 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.2332 0.2324 0.3257 0.0061  0.0494  -0.0256 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.2323 0.2303 0.3594 0.0123  0.0529  -0.0186 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.2285 0.2264 0.3139 0.0059  0.0420  -0.0243 87  SER   A N   
636  C CA  . SER   A 81  ? 0.2338 0.2290 0.3033 0.0022  0.0412  -0.0298 87  SER   A CA  
637  C C   . SER   A 81  ? 0.2507 0.2413 0.3184 0.0005  0.0424  -0.0343 87  SER   A C   
638  O O   . SER   A 81  ? 0.2660 0.2555 0.3448 0.0024  0.0443  -0.0330 87  SER   A O   
639  C CB  . SER   A 81  ? 0.2484 0.2474 0.3079 0.0020  0.0335  -0.0262 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.2334 0.2336 0.2943 0.0031  0.0290  -0.0232 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.2733 0.2616 0.3274 -0.0033 0.0404  -0.0387 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.2983 0.2832 0.3511 -0.0054 0.0404  -0.0425 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.2964 0.2843 0.3533 -0.0032 0.0348  -0.0379 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.3109 0.2963 0.3710 -0.0040 0.0354  -0.0399 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.3846 0.3667 0.4223 -0.0107 0.0390  -0.0482 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5043 0.4903 0.5322 -0.0113 0.0310  -0.0450 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.6709 0.6553 0.6887 -0.0159 0.0269  -0.0484 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7281 0.7113 0.7499 -0.0168 0.0266  -0.0504 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7120 0.6967 0.7180 -0.0188 0.0237  -0.0488 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.2836 0.2762 0.3401 -0.0009 0.0299  -0.0320 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.2649 0.2598 0.3234 0.0005  0.0252  -0.0279 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.2393 0.2353 0.3089 0.0035  0.0261  -0.0228 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.2554 0.2512 0.3277 0.0040  0.0243  -0.0206 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.2634 0.2618 0.3139 0.0004  0.0199  -0.0250 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.2777 0.2755 0.3172 -0.0025 0.0181  -0.0286 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.3095 0.3080 0.3432 -0.0030 0.0185  -0.0285 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.2859 0.2826 0.3211 -0.0050 0.0155  -0.0315 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.3322 0.3300 0.3550 -0.0059 0.0163  -0.0307 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.2998 0.2963 0.3248 -0.0080 0.0126  -0.0335 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.3429 0.3397 0.3612 -0.0085 0.0130  -0.0329 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.3905 0.3867 0.3981 -0.0118 0.0098  -0.0343 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.2230 0.2202 0.2992 0.0054  0.0285  -0.0202 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.2111 0.2100 0.2981 0.0081  0.0280  -0.0138 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.2277 0.2263 0.3269 0.0099  0.0330  -0.0130 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.2303 0.2290 0.3280 0.0093  0.0358  -0.0159 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.1938 0.1974 0.2770 0.0086  0.0228  -0.0079 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.1855 0.1898 0.2580 0.0071  0.0184  -0.0079 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.1992 0.2025 0.2722 0.0069  0.0168  -0.0060 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.1794 0.1854 0.2426 0.0059  0.0162  -0.0093 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.1866 0.1906 0.2517 0.0056  0.0138  -0.0058 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.1690 0.1755 0.2247 0.0048  0.0128  -0.0090 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.1715 0.1771 0.2286 0.0047  0.0118  -0.0073 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.1677 0.1734 0.2191 0.0037  0.0096  -0.0073 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.2456 0.2438 0.3574 0.0120  0.0341  -0.0085 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2496 0.2484 0.3762 0.0144  0.0382  -0.0061 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2414 0.2464 0.3688 0.0152  0.0341  -0.0005 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.2427 0.2508 0.3599 0.0140  0.0281  0.0024  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2641 0.2615 0.4030 0.0164  0.0381  -0.0007 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2843 0.2833 0.4128 0.0151  0.0315  0.0029  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2574 0.2547 0.3714 0.0125  0.0314  -0.0046 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2428 0.2497 0.3836 0.0170  0.0376  0.0015  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2332 0.2466 0.3778 0.0177  0.0335  0.0076  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2177 0.2345 0.3630 0.0179  0.0259  0.0163  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.2197 0.2342 0.3723 0.0191  0.0260  0.0195  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2462 0.2610 0.4096 0.0200  0.0389  0.0090  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2124 0.2331 0.3468 0.0160  0.0197  0.0191  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2039 0.2266 0.3347 0.0148  0.0129  0.0262  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2021 0.2297 0.3244 0.0125  0.0074  0.0291  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2177 0.2467 0.3361 0.0119  0.0090  0.0252  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2029 0.2208 0.3215 0.0135  0.0127  0.0228  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.2158 0.2334 0.3176 0.0111  0.0114  0.0176  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2024 0.2151 0.2968 0.0105  0.0138  0.0115  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.1899 0.2026 0.2707 0.0083  0.0107  0.0101  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.1731 0.1868 0.2456 0.0073  0.0102  0.0068  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.1936 0.2067 0.2558 0.0056  0.0080  0.0058  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.1904 0.2054 0.2655 0.0079  0.0123  0.0047  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.1942 0.2240 0.3127 0.0105  0.0013  0.0357  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2045 0.2375 0.3120 0.0072  -0.0037 0.0375  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.1954 0.2241 0.2856 0.0050  -0.0036 0.0327  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2142 0.2395 0.3008 0.0045  -0.0038 0.0336  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2106 0.2477 0.3213 0.0052  -0.0104 0.0470  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2245 0.2673 0.3540 0.0072  -0.0115 0.0526  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2394 0.2817 0.3857 0.0105  -0.0096 0.0565  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2265 0.2747 0.3585 0.0061  -0.0133 0.0532  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2648 0.3124 0.4313 0.0129  -0.0097 0.0615  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2511 0.3050 0.4028 0.0081  -0.0139 0.0585  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2768 0.3305 0.4462 0.0116  -0.0121 0.0627  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3143 0.3737 0.5059 0.0140  -0.0120 0.0680  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1706 0.1995 0.2514 0.0037  -0.0030 0.0280  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1583 0.1836 0.2247 0.0017  -0.0030 0.0241  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1472 0.1742 0.2048 -0.0023 -0.0076 0.0280  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1553 0.1862 0.2138 -0.0036 -0.0099 0.0300  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1579 0.1817 0.2192 0.0024  0.0001  0.0173  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1607 0.1814 0.2093 0.0005  -0.0003 0.0143  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1728 0.1914 0.2180 0.0015  0.0024  0.0083  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.1950 0.2126 0.2450 0.0033  0.0050  0.0054  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1531 0.1707 0.1893 -0.0001 0.0017  0.0064  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1544 0.1783 0.2035 -0.0047 -0.0086 0.0290  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1482 0.1723 0.1870 -0.0094 -0.0122 0.0320  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1681 0.1895 0.1954 -0.0114 -0.0102 0.0265  96  SER   A C   
721  O O   . SER   A 90  ? 0.1681 0.1870 0.1952 -0.0089 -0.0066 0.0211  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1749 0.1962 0.2101 -0.0116 -0.0135 0.0361  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1950 0.2112 0.2266 -0.0106 -0.0093 0.0314  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1527 0.1744 0.1709 -0.0160 -0.0127 0.0281  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1645 0.1828 0.1719 -0.0185 -0.0104 0.0233  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1608 0.1803 0.1718 -0.0154 -0.0083 0.0190  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1550 0.1711 0.1608 -0.0153 -0.0054 0.0146  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1774 0.1899 0.1788 -0.0191 -0.0067 0.0203  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.1969 0.2073 0.1926 -0.0230 -0.0081 0.0244  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2287 0.2357 0.2115 -0.0291 -0.0079 0.0242  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.1933 0.2039 0.1939 -0.0220 -0.0093 0.0284  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2437 0.2491 0.2230 -0.0319 -0.0094 0.0286  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2257 0.2333 0.2160 -0.0275 -0.0104 0.0315  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1565 0.1806 0.1759 -0.0134 -0.0098 0.0208  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1479 0.1728 0.1697 -0.0111 -0.0075 0.0170  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1443 0.1718 0.1634 -0.0140 -0.0092 0.0178  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1508 0.1822 0.1721 -0.0165 -0.0129 0.0222  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1608 0.1885 0.1947 -0.0071 -0.0065 0.0177  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1788 0.2065 0.2150 -0.0049 -0.0034 0.0136  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1793 0.2024 0.2085 -0.0039 -0.0009 0.0087  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2015 0.2311 0.2500 -0.0017 -0.0013 0.0141  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1483 0.1737 0.1629 -0.0138 -0.0068 0.0138  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1523 0.1793 0.1640 -0.0166 -0.0076 0.0138  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1571 0.1854 0.1736 -0.0138 -0.0053 0.0118  99  MET   A C   
745  O O   . MET   A 93  ? 0.1639 0.1892 0.1794 -0.0112 -0.0026 0.0087  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1627 0.1845 0.1637 -0.0193 -0.0059 0.0108  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1933 0.2126 0.1875 -0.0230 -0.0069 0.0120  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2211 0.2331 0.2048 -0.0259 -0.0029 0.0076  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2285 0.2378 0.2169 -0.0203 0.0005  0.0045  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1505 0.1834 0.1728 -0.0146 -0.0063 0.0137  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1524 0.1860 0.1787 -0.0125 -0.0032 0.0115  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1535 0.1863 0.1744 -0.0151 -0.0025 0.0102  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1457 0.1798 0.1636 -0.0189 -0.0050 0.0118  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1734 0.2126 0.2128 -0.0111 -0.0031 0.0141  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2262 0.2661 0.2738 -0.0082 -0.0029 0.0156  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2432 0.2883 0.3061 -0.0065 -0.0016 0.0180  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2474 0.2822 0.2910 -0.0055 0.0006  0.0114  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1493 0.1798 0.1686 -0.0136 0.0009  0.0074  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1435 0.1730 0.1587 -0.0158 0.0022  0.0064  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1443 0.1738 0.1623 -0.0140 0.0059  0.0048  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1571 0.1857 0.1773 -0.0114 0.0078  0.0034  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1682 0.1917 0.1737 -0.0164 0.0029  0.0043  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1264 0.1564 0.1439 -0.0161 0.0073  0.0046  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1455 0.1739 0.1627 -0.0153 0.0116  0.0028  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1619 0.1840 0.1683 -0.0150 0.0125  0.0010  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1811 0.2005 0.1821 -0.0167 0.0115  0.0013  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1558 0.1875 0.1776 -0.0178 0.0129  0.0037  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1746 0.2038 0.1948 -0.0176 0.0181  0.0017  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1514 0.1903 0.1861 -0.0180 0.0111  0.0064  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1597 0.1792 0.1636 -0.0132 0.0144  -0.0006 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.1646 0.1786 0.1592 -0.0129 0.0143  -0.0015 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.1687 0.1810 0.1611 -0.0117 0.0158  -0.0033 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.1868 0.2015 0.1853 -0.0105 0.0167  -0.0043 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.1759 0.1839 0.1597 -0.0124 0.0161  -0.0038 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.1748 0.1806 0.1543 -0.0124 0.0171  -0.0058 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.1735 0.1793 0.1542 -0.0106 0.0138  -0.0062 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.1795 0.1847 0.1597 -0.0097 0.0103  -0.0045 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.1835 0.1845 0.1521 -0.0144 0.0173  -0.0053 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.1885 0.1869 0.1505 -0.0156 0.0180  -0.0077 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2026 0.2009 0.1655 -0.0168 0.0233  -0.0110 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.1958 0.1919 0.1520 -0.0159 0.0141  -0.0074 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2202 0.2154 0.1757 -0.0183 0.0227  -0.0131 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2060 0.2002 0.1571 -0.0180 0.0167  -0.0107 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.1803 0.1863 0.1628 -0.0102 0.0154  -0.0087 105 SER   A N   
785  C CA  . SER   A 99  ? 0.1742 0.1798 0.1572 -0.0090 0.0126  -0.0094 105 SER   A CA  
786  C C   . SER   A 99  ? 0.1947 0.1986 0.1757 -0.0101 0.0155  -0.0130 105 SER   A C   
787  O O   . SER   A 99  ? 0.2044 0.2085 0.1882 -0.0107 0.0205  -0.0149 105 SER   A O   
788  C CB  . SER   A 99  ? 0.1714 0.1802 0.1629 -0.0068 0.0108  -0.0082 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.1817 0.1933 0.1813 -0.0061 0.0136  -0.0087 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.1841 0.1861 0.1609 -0.0106 0.0127  -0.0140 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.1911 0.1908 0.1650 -0.0121 0.0145  -0.0178 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2069 0.2079 0.1861 -0.0104 0.0110  -0.0178 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2145 0.2174 0.1971 -0.0085 0.0072  -0.0149 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2322 0.2279 0.1925 -0.0160 0.0131  -0.0185 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2433 0.2371 0.1978 -0.0181 0.0172  -0.0187 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.2452 0.2346 0.1846 -0.0225 0.0157  -0.0183 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.2910 0.2778 0.2228 -0.0255 0.0142  -0.0206 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.2505 0.2389 0.1855 -0.0233 0.0157  -0.0155 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2315 0.2313 0.2125 -0.0110 0.0132  -0.0213 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2187 0.2198 0.2062 -0.0093 0.0107  -0.0214 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2236 0.2253 0.2088 -0.0094 0.0046  -0.0192 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2322 0.2360 0.2243 -0.0070 0.0025  -0.0172 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2370 0.2353 0.2239 -0.0113 0.0145  -0.0263 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2554 0.2522 0.2420 -0.0122 0.0209  -0.0283 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2383 0.2352 0.2170 -0.0133 0.0193  -0.0257 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2079 0.2076 0.1835 -0.0121 0.0017  -0.0190 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2067 0.2073 0.1817 -0.0122 -0.0044 -0.0161 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.1939 0.1962 0.1732 -0.0095 -0.0061 -0.0119 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.1910 0.1943 0.1733 -0.0088 -0.0102 -0.0094 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.1755 0.1782 0.1560 -0.0083 -0.0026 -0.0112 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.1615 0.1652 0.1459 -0.0064 -0.0035 -0.0080 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1499 0.1554 0.1428 -0.0042 -0.0032 -0.0078 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1637 0.1693 0.1593 -0.0032 -0.0036 -0.0057 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.1634 0.1670 0.1458 -0.0066 -0.0003 -0.0074 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.1686 0.1698 0.1421 -0.0089 -0.0005 -0.0067 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.1844 0.1842 0.1543 -0.0097 -0.0043 -0.0046 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.1821 0.1827 0.1525 -0.0102 0.0033  -0.0080 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1455 0.1518 0.1423 -0.0037 -0.0022 -0.0099 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1462 0.1537 0.1502 -0.0021 -0.0018 -0.0094 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.1464 0.1537 0.1531 -0.0015 -0.0043 -0.0079 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.1631 0.1702 0.1688 -0.0022 -0.0072 -0.0079 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.1513 0.1591 0.1592 -0.0019 -0.0003 -0.0117 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.1761 0.1845 0.1863 -0.0015 0.0038  -0.0125 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1360 0.1433 0.1461 -0.0007 -0.0032 -0.0066 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1384 0.1451 0.1528 0.0000  -0.0041 -0.0055 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.1554 0.1606 0.1681 -0.0001 -0.0039 -0.0036 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.1671 0.1711 0.1845 0.0004  -0.0031 -0.0028 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1441 0.1488 0.1509 -0.0009 -0.0040 -0.0031 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1433 0.1461 0.1486 -0.0012 -0.0033 -0.0013 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1500 0.1517 0.1566 -0.0016 0.0000  -0.0018 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1517 0.1547 0.1569 -0.0024 0.0013  -0.0027 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1432 0.1423 0.1524 -0.0016 0.0014  -0.0010 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1306 0.1276 0.1395 -0.0030 0.0051  -0.0021 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1455 0.1416 0.1486 -0.0051 0.0064  -0.0020 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1583 0.1533 0.1597 -0.0050 0.0060  -0.0008 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1628 0.1566 0.1781 -0.0023 0.0073  -0.0020 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.1841 0.1792 0.2058 -0.0011 0.0071  -0.0027 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1875 0.1772 0.2008 -0.0047 0.0123  -0.0035 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2079 0.2005 0.2398 0.0001  0.0095  -0.0023 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1402 0.1365 0.1403 -0.0073 0.0080  -0.0030 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1468 0.1422 0.1418 -0.0103 0.0094  -0.0033 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1614 0.1520 0.1556 -0.0126 0.0134  -0.0049 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1671 0.1568 0.1621 -0.0131 0.0148  -0.0059 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1511 0.1503 0.1437 -0.0119 0.0078  -0.0028 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1664 0.1655 0.1542 -0.0159 0.0084  -0.0027 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1738 0.1729 0.1606 -0.0161 0.0085  -0.0024 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1778 0.1815 0.1654 -0.0173 0.0057  -0.0011 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1657 0.1528 0.1585 -0.0141 0.0158  -0.0054 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1910 0.1724 0.1831 -0.0167 0.0208  -0.0077 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1819 0.1612 0.1672 -0.0212 0.0224  -0.0089 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1854 0.1662 0.1698 -0.0210 0.0207  -0.0077 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2521 0.2296 0.2517 -0.0141 0.0232  -0.0073 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3384 0.3178 0.3463 -0.0097 0.0209  -0.0054 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3362 0.3116 0.3523 -0.0078 0.0232  -0.0042 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3708 0.3410 0.3904 -0.0094 0.0297  -0.0070 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3415 0.3114 0.3685 -0.0081 0.0317  -0.0078 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.3079 0.2827 0.3407 -0.0048 0.0270  -0.0055 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3036 0.2682 0.3321 -0.0104 0.0388  -0.0112 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1868 0.1620 0.1672 -0.0256 0.0263  -0.0116 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.1948 0.1665 0.1685 -0.0308 0.0287  -0.0135 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.1999 0.1633 0.1760 -0.0320 0.0360  -0.0167 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2188 0.1804 0.2029 -0.0283 0.0383  -0.0167 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2163 0.1896 0.1809 -0.0364 0.0272  -0.0142 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2166 0.1853 0.1772 -0.0393 0.0315  -0.0168 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2203 0.1786 0.1904 -0.0373 0.0401  -0.0197 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2441 0.1934 0.2170 -0.0388 0.0483  -0.0233 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2604 0.2059 0.2329 -0.0403 0.0533  -0.0262 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2771 0.2156 0.2558 -0.0400 0.0607  -0.0289 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.2774 0.2214 0.2420 -0.0456 0.0520  -0.0267 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3515 0.2958 0.3025 -0.0532 0.0511  -0.0290 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.4702 0.4111 0.4126 -0.0602 0.0526  -0.0317 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5125 0.4594 0.4514 -0.0620 0.0465  -0.0294 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.4617 0.3930 0.4012 -0.0648 0.0611  -0.0369 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2431 0.1926 0.2099 -0.0416 0.0498  -0.0254 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2484 0.1941 0.2133 -0.0437 0.0547  -0.0280 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2363 0.1854 0.2125 -0.0373 0.0534  -0.0257 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2605 0.2057 0.2386 -0.0381 0.0588  -0.0280 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2610 0.2081 0.2115 -0.0502 0.0520  -0.0283 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2693 0.2138 0.2077 -0.0577 0.0521  -0.0303 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.2804 0.2318 0.2145 -0.0589 0.0441  -0.0269 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3145 0.2502 0.2452 -0.0645 0.0595  -0.0355 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3318 0.2791 0.2561 -0.0662 0.0461  -0.0298 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3392 0.2768 0.2604 -0.0700 0.0553  -0.0352 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2053 0.1612 0.1888 -0.0313 0.0468  -0.0215 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2034 0.1630 0.1971 -0.0258 0.0446  -0.0193 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1817 0.1494 0.1748 -0.0228 0.0363  -0.0156 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.1912 0.1621 0.1792 -0.0236 0.0322  -0.0141 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1755 0.1462 0.1745 -0.0196 0.0346  -0.0145 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1744 0.1519 0.1740 -0.0167 0.0278  -0.0115 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1598 0.1395 0.1501 -0.0202 0.0255  -0.0111 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1937 0.1707 0.1794 -0.0235 0.0284  -0.0124 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1713 0.1509 0.1804 -0.0128 0.0269  -0.0108 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1882 0.1738 0.1969 -0.0107 0.0210  -0.0087 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1853 0.1640 0.2049 -0.0094 0.0275  -0.0099 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1622 0.1466 0.1502 -0.0195 0.0205  -0.0089 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1688 0.1565 0.1508 -0.0222 0.0173  -0.0072 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1687 0.1610 0.1554 -0.0188 0.0138  -0.0051 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.1723 0.1658 0.1565 -0.0205 0.0125  -0.0037 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1830 0.1731 0.1617 -0.0237 0.0147  -0.0062 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2051 0.2000 0.1807 -0.0258 0.0104  -0.0034 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1835 0.1685 0.1568 -0.0279 0.0185  -0.0085 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1531 0.1480 0.1463 -0.0145 0.0119  -0.0047 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1653 0.1640 0.1628 -0.0117 0.0091  -0.0033 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1471 0.1474 0.1494 -0.0081 0.0075  -0.0035 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1576 0.1560 0.1606 -0.0074 0.0083  -0.0040 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1381 0.1414 0.1434 -0.0061 0.0053  -0.0030 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1478 0.1522 0.1557 -0.0038 0.0037  -0.0035 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1397 0.1470 0.1472 -0.0033 0.0024  -0.0031 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1273 0.1364 0.1362 -0.0036 0.0024  -0.0022 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1595 0.1638 0.1726 -0.0021 0.0033  -0.0044 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1639 0.1690 0.1793 -0.0022 0.0038  -0.0044 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1756 0.1773 0.1917 -0.0020 0.0047  -0.0047 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.1849 0.1901 0.2060 -0.0008 0.0032  -0.0056 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1331 0.1407 0.1392 -0.0026 0.0016  -0.0036 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1213 0.1309 0.1274 -0.0024 0.0017  -0.0040 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1172 0.1277 0.1277 -0.0013 0.0019  -0.0049 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1235 0.1330 0.1354 -0.0007 0.0011  -0.0060 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1311 0.1398 0.1334 -0.0025 0.0013  -0.0047 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1374 0.1472 0.1395 -0.0027 0.0028  -0.0060 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1473 0.1547 0.1458 -0.0035 0.0015  -0.0034 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1255 0.1380 0.1393 -0.0011 0.0029  -0.0043 125 SER   A N   
922  C CA  . SER   A 119 ? 0.1368 0.1496 0.1559 -0.0001 0.0037  -0.0050 125 SER   A CA  
923  C C   . SER   A 119 ? 0.1457 0.1596 0.1682 0.0004  0.0059  -0.0059 125 SER   A C   
924  O O   . SER   A 119 ? 0.1588 0.1718 0.1850 0.0011  0.0074  -0.0078 125 SER   A O   
925  C CB  . SER   A 119 ? 0.1397 0.1534 0.1621 -0.0002 0.0031  -0.0023 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.1512 0.1650 0.1797 0.0009  0.0040  -0.0022 125 SER   A OG  
927  N N   . THR   A 120 ? 0.1398 0.1554 0.1621 -0.0002 0.0067  -0.0050 126 THR   A N   
928  C CA  . THR   A 120 ? 0.1566 0.1731 0.1839 0.0003  0.0100  -0.0061 126 THR   A CA  
929  C C   . THR   A 120 ? 0.1484 0.1656 0.1719 -0.0010 0.0109  -0.0062 126 THR   A C   
930  O O   . THR   A 120 ? 0.1522 0.1688 0.1693 -0.0020 0.0088  -0.0053 126 THR   A O   
931  C CB  . THR   A 120 ? 0.2033 0.2225 0.2414 0.0016  0.0105  -0.0034 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2228 0.2419 0.2674 0.0023  0.0149  -0.0053 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2197 0.2424 0.2599 0.0008  0.0080  0.0009  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.1657 0.1836 0.1933 -0.0010 0.0146  -0.0073 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.1735 0.1920 0.1985 -0.0024 0.0162  -0.0073 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.1753 0.1929 0.2038 -0.0026 0.0219  -0.0102 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.1917 0.2088 0.2272 -0.0015 0.0247  -0.0117 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.1896 0.2067 0.2140 -0.0043 0.0243  -0.0111 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.1982 0.2134 0.2240 -0.0054 0.0309  -0.0144 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.1926 0.2110 0.2240 -0.0060 0.0332  -0.0128 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.1975 0.2207 0.2357 -0.0052 0.0296  -0.0088 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.1922 0.2079 0.2205 -0.0079 0.0392  -0.0159 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.1969 0.2156 0.2323 -0.0087 0.0428  -0.0149 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.1959 0.2174 0.2284 -0.0095 0.0379  -0.0112 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2037 0.2302 0.2469 -0.0095 0.0382  -0.0087 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2207 0.2442 0.2757 -0.0064 0.0457  -0.0136 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.2949 0.3143 0.3529 -0.0060 0.0524  -0.0181 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3222 0.3366 0.3725 -0.0086 0.0588  -0.0227 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3197 0.3406 0.3878 -0.0034 0.0511  -0.0170 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.1820 0.2002 0.2011 -0.0105 0.0338  -0.0108 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.1754 0.1952 0.1916 -0.0116 0.0301  -0.0078 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.1681 0.1915 0.1889 -0.0103 0.0242  -0.0047 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.1882 0.2128 0.2072 -0.0116 0.0215  -0.0026 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1509 0.1751 0.1759 -0.0082 0.0224  -0.0045 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1407 0.1672 0.1680 -0.0075 0.0171  -0.0018 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1373 0.1596 0.1560 -0.0067 0.0148  -0.0030 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1544 0.1733 0.1686 -0.0063 0.0167  -0.0057 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1421 0.1731 0.1824 -0.0058 0.0166  0.0003  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.1702 0.2068 0.2224 -0.0065 0.0176  0.0028  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2023 0.2427 0.2693 -0.0043 0.0182  0.0049  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1740 0.2138 0.2244 -0.0090 0.0126  0.0061  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1305 0.1532 0.1471 -0.0070 0.0109  -0.0011 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1266 0.1462 0.1383 -0.0061 0.0088  -0.0017 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1386 0.1604 0.1543 -0.0061 0.0060  0.0006  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1492 0.1734 0.1659 -0.0079 0.0044  0.0028  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1352 0.1509 0.1380 -0.0070 0.0080  -0.0023 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1647 0.1808 0.1657 -0.0091 0.0073  -0.0007 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.1453 0.1587 0.1459 -0.0059 0.0061  -0.0028 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1314 0.1524 0.1489 -0.0045 0.0054  0.0002  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1373 0.1596 0.1576 -0.0047 0.0031  0.0026  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1377 0.1565 0.1527 -0.0047 0.0023  0.0016  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1479 0.1644 0.1615 -0.0034 0.0031  -0.0007 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1304 0.1488 0.1425 -0.0067 0.0008  0.0032  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1367 0.1514 0.1446 -0.0070 0.0011  0.0020  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1367 0.1514 0.1457 -0.0079 0.0003  0.0037  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1396 0.1563 0.1483 -0.0101 -0.0014 0.0065  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1437 0.1561 0.1455 -0.0096 0.0016  0.0015  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1398 0.1519 0.1400 -0.0094 0.0023  0.0006  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1484 0.1579 0.1474 -0.0078 0.0031  -0.0009 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1567 0.1713 0.1568 -0.0113 0.0019  0.0018  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1479 0.1566 0.1446 -0.0080 0.0037  -0.0010 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1515 0.1653 0.1496 -0.0115 0.0031  0.0010  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1436 0.1542 0.1396 -0.0098 0.0041  -0.0003 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1267 0.1391 0.1366 -0.0065 0.0012  0.0024  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1276 0.1390 0.1376 -0.0075 0.0011  0.0038  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1318 0.1398 0.1348 -0.0107 0.0024  0.0031  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1508 0.1560 0.1529 -0.0101 0.0045  0.0006  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1343 0.1441 0.1484 -0.0052 0.0023  0.0020  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1354 0.1434 0.1339 -0.0143 0.0014  0.0055  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1589 0.1628 0.1493 -0.0184 0.0035  0.0043  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1617 0.1616 0.1518 -0.0184 0.0067  0.0027  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1639 0.1646 0.1576 -0.0171 0.0061  0.0042  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.1870 0.1921 0.1711 -0.0233 0.0008  0.0076  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2462 0.2464 0.2199 -0.0288 0.0034  0.0057  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2380 0.2359 0.2099 -0.0292 0.0060  0.0026  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.2976 0.2956 0.2646 -0.0329 0.0033  0.0073  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1497 0.1450 0.1361 -0.0202 0.0107  -0.0004 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1539 0.1450 0.1406 -0.0209 0.0149  -0.0022 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.1783 0.1640 0.1549 -0.0268 0.0187  -0.0036 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.1913 0.1727 0.1672 -0.0282 0.0234  -0.0055 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.1727 0.1628 0.1678 -0.0170 0.0174  -0.0049 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1865 0.1812 0.1895 -0.0124 0.0137  -0.0039 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.1661 0.1540 0.1607 -0.0173 0.0195  -0.0069 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.1778 0.1634 0.1467 -0.0307 0.0174  -0.0031 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.1918 0.1714 0.1498 -0.0372 0.0216  -0.0055 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2195 0.1963 0.1687 -0.0422 0.0224  -0.0042 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2376 0.2076 0.1779 -0.0476 0.0280  -0.0072 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.1975 0.1782 0.1494 -0.0406 0.0191  -0.0053 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2090 0.1903 0.1676 -0.0368 0.0201  -0.0073 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2090 0.1917 0.1616 -0.0406 0.0175  -0.0067 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.1849 0.1750 0.1400 -0.0395 0.0106  -0.0021 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2029 0.1965 0.1565 -0.0416 0.0070  -0.0006 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2139 0.2040 0.1615 -0.0458 0.0094  -0.0033 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2065 0.2070 0.1657 -0.0396 0.0016  0.0036  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2068 0.1878 0.1579 -0.0410 0.0173  0.0005  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2277 0.2059 0.1699 -0.0459 0.0174  0.0029  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2329 0.2071 0.1787 -0.0444 0.0230  0.0009  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2452 0.2157 0.1829 -0.0489 0.0246  0.0024  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2313 0.2156 0.1756 -0.0452 0.0098  0.0096  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.2696 0.2586 0.2282 -0.0377 0.0078  0.0111  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2432 0.2341 0.2099 -0.0328 0.0087  0.0083  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3012 0.2914 0.2621 -0.0371 0.0055  0.0152  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2197 0.1950 0.1778 -0.0382 0.0254  -0.0018 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2065 0.1792 0.1708 -0.0363 0.0300  -0.0034 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2179 0.1836 0.1784 -0.0398 0.0383  -0.0083 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2282 0.1932 0.1981 -0.0365 0.0420  -0.0117 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.1993 0.1769 0.1785 -0.0289 0.0280  -0.0039 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2103 0.1941 0.1936 -0.0256 0.0210  0.0002  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2107 0.1983 0.2064 -0.0194 0.0196  -0.0012 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2127 0.1965 0.1941 -0.0270 0.0193  0.0041  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2287 0.1887 0.1752 -0.0471 0.0416  -0.0086 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2459 0.1980 0.1873 -0.0516 0.0508  -0.0141 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2632 0.2124 0.2154 -0.0489 0.0582  -0.0173 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.2817 0.2259 0.2374 -0.0496 0.0660  -0.0221 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2631 0.2090 0.1849 -0.0611 0.0530  -0.0140 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.2935 0.2427 0.2040 -0.0651 0.0448  -0.0098 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3239 0.2659 0.2135 -0.0759 0.0475  -0.0104 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.2892 0.2416 0.2040 -0.0627 0.0424  -0.0115 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2555 0.2075 0.2139 -0.0460 0.0561  -0.0145 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2577 0.2079 0.2275 -0.0436 0.0623  -0.0170 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2712 0.2252 0.2590 -0.0367 0.0624  -0.0190 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.2876 0.2400 0.2867 -0.0351 0.0683  -0.0216 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2631 0.2155 0.2347 -0.0425 0.0593  -0.0132 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2448 0.2051 0.2223 -0.0373 0.0497  -0.0089 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2566 0.2196 0.2261 -0.0386 0.0428  -0.0041 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2281 0.1942 0.2214 -0.0304 0.0464  -0.0091 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2493 0.2190 0.2292 -0.0327 0.0365  -0.0018 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2366 0.2080 0.2299 -0.0280 0.0386  -0.0050 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2324 0.1998 0.2400 -0.0264 0.0493  -0.0120 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2227 0.1996 0.2279 -0.0222 0.0343  -0.0047 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2272 0.2007 0.2463 -0.0209 0.0439  -0.0110 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2251 0.2028 0.2420 -0.0192 0.0369  -0.0078 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2533 0.2124 0.2442 -0.0331 0.0560  -0.0177 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2643 0.2268 0.2709 -0.0272 0.0554  -0.0188 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3148 0.2717 0.3263 -0.0285 0.0641  -0.0230 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3248 0.2836 0.3520 -0.0241 0.0653  -0.0237 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2492 0.2170 0.2556 -0.0242 0.0478  -0.0166 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2312 0.2053 0.2385 -0.0212 0.0398  -0.0130 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2332 0.2110 0.2385 -0.0193 0.0342  -0.0116 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2229 0.2008 0.2441 -0.0165 0.0382  -0.0128 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.3693 0.3192 0.3676 -0.0348 0.0700  -0.0257 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4440 0.3867 0.4442 -0.0374 0.0797  -0.0304 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5054 0.4421 0.5094 -0.0400 0.0899  -0.0339 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5302 0.4601 0.5361 -0.0426 0.0993  -0.0383 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5023 0.4393 0.4839 -0.0445 0.0818  -0.0324 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6056 0.5464 0.5834 -0.0432 0.0746  -0.0303 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6303 0.5762 0.6210 -0.0369 0.0704  -0.0286 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6782 0.6168 0.6397 -0.0491 0.0730  -0.0303 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5412 0.4793 0.5452 -0.0402 0.0892  -0.0323 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.5813 0.5138 0.5899 -0.0428 0.0995  -0.0356 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6015 0.5400 0.6264 -0.0374 0.0968  -0.0334 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6207 0.5564 0.6566 -0.0376 0.1049  -0.0360 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6231 0.5480 0.6104 -0.0515 0.1043  -0.0368 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7003 0.6291 0.6734 -0.0530 0.0944  -0.0315 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8056 0.7305 0.7575 -0.0600 0.0928  -0.0314 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8327 0.7567 0.7692 -0.0649 0.0891  -0.0281 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8304 0.7530 0.7812 -0.0608 0.0950  -0.0344 145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.2716 0.2545 0.2601 -0.0012 -0.0240 0.0059  7   SER   C N   
1079 C CA  . SER   B 1   ? 0.2643 0.2511 0.2626 -0.0020 -0.0253 0.0056  7   SER   C CA  
1080 C C   . SER   B 1   ? 0.2515 0.2410 0.2547 -0.0029 -0.0234 0.0045  7   SER   C C   
1081 O O   . SER   B 1   ? 0.2736 0.2611 0.2726 -0.0030 -0.0228 0.0036  7   SER   C O   
1082 C CB  . SER   B 1   ? 0.2882 0.2736 0.2884 -0.0017 -0.0308 0.0054  7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.3465 0.3290 0.3433 -0.0019 -0.0338 0.0038  7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2169 0.2104 0.2286 -0.0034 -0.0225 0.0048  8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2023 0.1979 0.2185 -0.0042 -0.0205 0.0043  8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.1858 0.1855 0.2081 -0.0039 -0.0173 0.0050  8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.1977 0.1981 0.2191 -0.0032 -0.0161 0.0054  8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.1738 0.1756 0.2018 -0.0045 -0.0158 0.0052  9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.1721 0.1773 0.2048 -0.0038 -0.0122 0.0059  9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.1723 0.1781 0.2061 -0.0040 -0.0092 0.0064  9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.1893 0.1932 0.2228 -0.0050 -0.0102 0.0063  9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.1828 0.1907 0.2240 -0.0037 -0.0135 0.0063  9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.1645 0.1724 0.1991 -0.0028 -0.0054 0.0069  10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1554 0.1638 0.1911 -0.0026 -0.0019 0.0080  10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.1534 0.1647 0.1975 -0.0025 0.0003  0.0092  10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1509 0.1642 0.1971 -0.0014 0.0007  0.0089  10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.1633 0.1713 0.1922 -0.0007 0.0007  0.0077  10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.1698 0.1759 0.1921 -0.0007 -0.0012 0.0065  10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.1738 0.1815 0.2022 0.0000  0.0043  0.0093  10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.1924 0.1991 0.2098 0.0012  0.0002  0.0057  10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.1619 0.1735 0.2114 -0.0036 0.0018  0.0107  11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.1693 0.1843 0.2284 -0.0037 0.0046  0.0122  11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.1793 0.1938 0.2368 -0.0027 0.0103  0.0143  11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.1884 0.2005 0.2455 -0.0040 0.0108  0.0154  11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.1731 0.1888 0.2420 -0.0063 0.0013  0.0124  11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.1670 0.1828 0.2369 -0.0067 -0.0045 0.0106  11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.1761 0.1952 0.2521 -0.0058 -0.0051 0.0105  11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.1889 0.2009 0.2518 -0.0074 -0.0089 0.0091  11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.1991 0.2177 0.2746 -0.0057 -0.0104 0.0092  11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2021 0.2134 0.2638 -0.0073 -0.0138 0.0078  11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2142 0.2287 0.2824 -0.0065 -0.0148 0.0080  11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.2424 0.2558 0.3086 -0.0060 -0.0196 0.0071  11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.1943 0.2102 0.2493 -0.0002 0.0144  0.0148  12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2065 0.2215 0.2579 0.0014  0.0199  0.0169  12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2049 0.2232 0.2622 0.0030  0.0248  0.0181  12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.1949 0.2150 0.2523 0.0046  0.0243  0.0165  12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2317 0.2438 0.2703 0.0037  0.0199  0.0157  12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2395 0.2525 0.2745 0.0052  0.0175  0.0129  12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2471 0.2577 0.2802 0.0062  0.0254  0.0179  12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2206 0.2398 0.2843 0.0024  0.0296  0.0212  13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2193 0.2420 0.2895 0.0041  0.0352  0.0227  13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2112 0.2383 0.2919 0.0034  0.0323  0.0212  13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2242 0.2524 0.3128 0.0004  0.0274  0.0206  13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2123 0.2413 0.2922 0.0063  0.0343  0.0200  14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2173 0.2500 0.3068 0.0060  0.0308  0.0185  14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.1896 0.2199 0.2708 0.0069  0.0255  0.0152  14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.1979 0.2300 0.2823 0.0085  0.0246  0.0138  14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.2610 0.2979 0.3588 0.0083  0.0365  0.0196  14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.3552 0.3955 0.4655 0.0065  0.0411  0.0230  14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.3919 0.4353 0.5152 0.0034  0.0376  0.0235  14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.3675 0.4069 0.4742 0.0082  0.0487  0.0256  14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.1772 0.2038 0.2491 0.0057  0.0220  0.0142  15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.1755 0.1997 0.2401 0.0062  0.0173  0.0116  15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.1701 0.1927 0.2342 0.0034  0.0115  0.0110  15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.1779 0.1993 0.2419 0.0015  0.0110  0.0120  15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.1850 0.2059 0.2370 0.0082  0.0190  0.0106  15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2054 0.2266 0.2543 0.0117  0.0242  0.0104  15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2236 0.2463 0.2763 0.0136  0.0249  0.0091  15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2218 0.2410 0.2630 0.0135  0.0284  0.0115  15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.2437 0.2661 0.2927 0.0173  0.0299  0.0087  15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.2400 0.2588 0.2765 0.0172  0.0332  0.0112  15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.2606 0.2809 0.3008 0.0191  0.0339  0.0096  15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3103 0.3296 0.3450 0.0232  0.0388  0.0089  15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1403 0.1621 0.2030 0.0034  0.0072  0.0093  16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.1433 0.1627 0.2030 0.0014  0.0019  0.0086  16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1478 0.1645 0.1982 0.0024  0.0010  0.0070  16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1631 0.1800 0.2136 0.0040  0.0013  0.0061  16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.1508 0.1717 0.2184 0.0006  -0.0023 0.0086  16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.1714 0.1891 0.2336 -0.0004 -0.0076 0.0077  16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1646 0.1831 0.2336 -0.0009 -0.0124 0.0078  16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.1774 0.1930 0.2411 -0.0002 -0.0161 0.0073  16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.1871 0.1993 0.2448 -0.0011 -0.0202 0.0071  16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.1814 0.1922 0.2367 -0.0027 -0.0212 0.0068  16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.1938 0.2032 0.2468 -0.0003 -0.0227 0.0072  16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1454 0.1596 0.1886 0.0016  0.0001  0.0067  17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1400 0.1522 0.1759 0.0022  -0.0008 0.0053  17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1422 0.1525 0.1764 0.0006  -0.0047 0.0052  17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.1582 0.1675 0.1913 -0.0007 -0.0060 0.0056  17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.1643 0.1756 0.1939 0.0027  0.0012  0.0051  17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.1788 0.1889 0.2031 0.0034  0.0002  0.0034  17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.1774 0.1898 0.2074 0.0043  0.0053  0.0059  17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1387 0.1480 0.1721 0.0009  -0.0063 0.0046  18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1573 0.1642 0.1879 -0.0001 -0.0094 0.0049  18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1433 0.1484 0.1695 0.0000  -0.0091 0.0043  18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1470 0.1527 0.1739 0.0010  -0.0076 0.0033  18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.1824 0.1892 0.2177 0.0000  -0.0123 0.0057  18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2412 0.2497 0.2818 -0.0007 -0.0135 0.0061  18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1654 0.1731 0.2047 0.0015  -0.0115 0.0053  18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1462 0.1490 0.1686 -0.0008 -0.0106 0.0049  19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1458 0.1469 0.1658 -0.0010 -0.0103 0.0048  19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1526 0.1529 0.1763 -0.0003 -0.0112 0.0050  19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1521 0.1515 0.1776 0.0001  -0.0134 0.0061  19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1521 0.1505 0.1674 -0.0018 -0.0112 0.0061  19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1685 0.1672 0.1800 -0.0022 -0.0101 0.0057  19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.1672 0.1654 0.1772 -0.0023 -0.0111 0.0058  19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1612 0.1609 0.1720 -0.0024 -0.0081 0.0051  19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1448 0.1448 0.1696 0.0001  -0.0101 0.0039  20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1383 0.1369 0.1666 0.0011  -0.0109 0.0038  20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1541 0.1493 0.1812 0.0007  -0.0129 0.0060  20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.1559 0.1503 0.1860 0.0018  -0.0146 0.0067  20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1436 0.1416 0.1725 0.0014  -0.0098 0.0019  20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1485 0.1447 0.1812 0.0029  -0.0103 0.0012  20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1621 0.1565 0.1948 0.0028  -0.0099 -0.0011 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1572 0.1492 0.1929 0.0045  -0.0102 -0.0024 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.1852 0.1734 0.2229 0.0043  -0.0115 -0.0014 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2037 0.1901 0.2403 0.0027  -0.0124 0.0016  20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.1926 0.1783 0.2331 0.0060  -0.0117 -0.0031 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1529 0.1462 0.1756 -0.0006 -0.0127 0.0072  21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1677 0.1569 0.1876 -0.0007 -0.0142 0.0097  21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.1775 0.1663 0.1957 0.0001  -0.0170 0.0108  21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.1968 0.1819 0.2125 0.0007  -0.0189 0.0128  21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.1683 0.1554 0.1840 -0.0021 -0.0123 0.0109  21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.1699 0.1579 0.1807 -0.0026 -0.0115 0.0111  21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.1759 0.1674 0.1876 -0.0030 -0.0099 0.0092  21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.1883 0.1737 0.1929 -0.0023 -0.0122 0.0128  21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.1857 0.1767 0.1923 -0.0031 -0.0095 0.0098  21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2006 0.1879 0.2026 -0.0027 -0.0108 0.0118  21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.1696 0.1615 0.1889 0.0000  -0.0174 0.0096  22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.1750 0.1666 0.1940 0.0005  -0.0208 0.0102  22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.1890 0.1840 0.2162 0.0014  -0.0221 0.0094  22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2006 0.1963 0.2299 0.0016  -0.0250 0.0095  22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.1794 0.1715 0.1943 -0.0004 -0.0205 0.0095  22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.1913 0.1804 0.1983 -0.0009 -0.0190 0.0103  22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2118 0.2012 0.2150 -0.0013 -0.0188 0.0093  22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2066 0.1907 0.2078 0.0000  -0.0211 0.0125  22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.1781 0.1750 0.2102 0.0021  -0.0198 0.0085  23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.1791 0.1795 0.2193 0.0033  -0.0200 0.0079  23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.1784 0.1778 0.2221 0.0045  -0.0239 0.0091  23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.1865 0.1818 0.2266 0.0051  -0.0255 0.0104  23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.1741 0.1757 0.2171 0.0043  -0.0167 0.0065  23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.1740 0.1769 0.2249 0.0050  -0.0254 0.0089  24  THR   C N   
1212 C CA  . THR   B 18  ? 0.1851 0.1880 0.2410 0.0064  -0.0299 0.0098  24  THR   C CA  
1213 C C   . THR   B 18  ? 0.1796 0.1845 0.2436 0.0086  -0.0286 0.0096  24  THR   C C   
1214 O O   . THR   B 18  ? 0.1737 0.1804 0.2395 0.0090  -0.0242 0.0085  24  THR   C O   
1215 C CB  . THR   B 18  ? 0.1933 0.1996 0.2549 0.0055  -0.0327 0.0095  24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.1973 0.2090 0.2677 0.0054  -0.0290 0.0087  24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.1933 0.1972 0.2471 0.0037  -0.0341 0.0093  24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.1814 0.1862 0.2505 0.0103  -0.0328 0.0106  25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.1770 0.1841 0.2550 0.0128  -0.0317 0.0102  25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.1715 0.1853 0.2587 0.0128  -0.0278 0.0090  25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.1755 0.1907 0.2661 0.0144  -0.0236 0.0081  25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.1969 0.2041 0.2805 0.0147  -0.0376 0.0115  25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.2813 0.2815 0.3563 0.0156  -0.0413 0.0133  25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.3367 0.3318 0.4049 0.0157  -0.0385 0.0137  25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.3179 0.3155 0.3901 0.0164  -0.0474 0.0148  25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.3496 0.3390 0.4112 0.0165  -0.0424 0.0160  25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.3419 0.3323 0.4047 0.0172  -0.0478 0.0166  25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.1603 0.1775 0.2510 0.0110  -0.0290 0.0091  26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.1613 0.1844 0.2611 0.0108  -0.0247 0.0086  26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.1591 0.1816 0.2526 0.0103  -0.0185 0.0077  26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.1588 0.1845 0.2572 0.0116  -0.0136 0.0072  26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.1856 0.2118 0.2908 0.0086  -0.0274 0.0088  26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.2331 0.2655 0.3495 0.0083  -0.0227 0.0089  26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.2479 0.2849 0.3762 0.0101  -0.0220 0.0092  26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.2487 0.2813 0.3616 0.0062  -0.0190 0.0089  26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.1618 0.1801 0.2439 0.0086  -0.0187 0.0075  27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.1609 0.1785 0.2369 0.0084  -0.0136 0.0065  27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.1602 0.1765 0.2358 0.0109  -0.0110 0.0053  27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.1680 0.1860 0.2442 0.0122  -0.0064 0.0043  27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.1673 0.1807 0.2325 0.0065  -0.0149 0.0064  27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.1836 0.1975 0.2472 0.0043  -0.0162 0.0069  27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.1760 0.1933 0.2450 0.0038  -0.0141 0.0070  27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.1808 0.1912 0.2377 0.0031  -0.0191 0.0072  27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.1713 0.1840 0.2454 0.0118  -0.0140 0.0055  28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.1836 0.1943 0.2576 0.0141  -0.0121 0.0041  28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.1904 0.2049 0.2739 0.0170  -0.0098 0.0036  28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2055 0.2192 0.2881 0.0191  -0.0062 0.0019  28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.1771 0.1823 0.2476 0.0142  -0.0157 0.0048  28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.1660 0.1672 0.2274 0.0122  -0.0156 0.0046  28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.1760 0.1751 0.2319 0.0099  -0.0179 0.0061  28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.1699 0.1685 0.2272 0.0123  -0.0132 0.0026  28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.1849 0.1810 0.2344 0.0086  -0.0165 0.0055  28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.1768 0.1727 0.2276 0.0098  -0.0140 0.0032  28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.1883 0.1867 0.2468 0.0144  -0.0104 0.0001  28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.1881 0.1814 0.2350 0.0091  -0.0126 0.0015  28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2007 0.1961 0.2539 0.0138  -0.0094 -0.0020 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.1912 0.1843 0.2394 0.0111  -0.0107 -0.0012 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.1681 0.1867 0.2607 0.0172  -0.0117 0.0050  29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.1774 0.2006 0.2808 0.0200  -0.0091 0.0048  29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.1802 0.2075 0.2855 0.0201  -0.0029 0.0044  29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.1978 0.2288 0.3109 0.0226  0.0010  0.0042  29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.1676 0.1944 0.2816 0.0200  -0.0136 0.0064  29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.1706 0.1978 0.2701 0.0173  -0.0021 0.0048  30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.1695 0.1996 0.2693 0.0173  0.0037  0.0050  30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.1701 0.1960 0.2568 0.0168  0.0056  0.0037  30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.1744 0.2008 0.2574 0.0154  0.0079  0.0044  30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.1846 0.2183 0.2905 0.0144  0.0024  0.0069  30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2024 0.2412 0.3230 0.0151  0.0008  0.0079  30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.1900 0.2333 0.3197 0.0170  0.0057  0.0084  30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.1954 0.2334 0.3185 0.0140  -0.0060 0.0082  30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.1784 0.2001 0.2589 0.0182  0.0047  0.0019  31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.1729 0.1905 0.2421 0.0177  0.0052  0.0003  31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.1927 0.2109 0.2574 0.0197  0.0106  -0.0008 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2104 0.2294 0.2775 0.0229  0.0143  -0.0017 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.1762 0.1892 0.2422 0.0187  0.0027  -0.0015 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.1899 0.1988 0.2461 0.0181  0.0024  -0.0036 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.1950 0.2034 0.2469 0.0147  -0.0001 -0.0023 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.1991 0.2034 0.2543 0.0192  0.0004  -0.0055 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.1714 0.1886 0.2287 0.0182  0.0113  -0.0006 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.1828 0.1992 0.2332 0.0203  0.0157  -0.0016 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.1937 0.2056 0.2344 0.0208  0.0135  -0.0045 32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2161 0.2258 0.2514 0.0238  0.0155  -0.0069 32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.1966 0.2150 0.2459 0.0186  0.0177  0.0008  32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2144 0.2309 0.2541 0.0210  0.0216  0.0000  32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2002 0.2232 0.2606 0.0180  0.0201  0.0035  32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.1713 0.1817 0.2096 0.0179  0.0094  -0.0044 33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.1767 0.1836 0.2078 0.0177  0.0071  -0.0069 33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.1778 0.1838 0.2101 0.0144  0.0029  -0.0061 33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.1798 0.1877 0.2147 0.0123  0.0022  -0.0037 33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2016 0.2085 0.2251 0.0184  0.0088  -0.0072 33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2038 0.2081 0.2210 0.0178  0.0058  -0.0095 33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2368 0.2381 0.2491 0.0198  0.0047  -0.0130 33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.1894 0.1942 0.2053 0.0151  0.0034  -0.0085 33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2462 0.2466 0.2554 0.0181  0.0014  -0.0142 33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2126 0.2153 0.2240 0.0154  0.0010  -0.0114 33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.1983 0.2050 0.2166 0.0125  0.0030  -0.0058 33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2110 0.2143 0.2208 0.0134  -0.0013 -0.0112 33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2004 0.2069 0.2159 0.0108  0.0010  -0.0058 33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.1934 0.1986 0.2054 0.0113  -0.0010 -0.0083 33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.1740 0.1768 0.2045 0.0140  0.0004  -0.0080 34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.1847 0.1864 0.2155 0.0110  -0.0027 -0.0070 34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.1824 0.1815 0.2097 0.0106  -0.0043 -0.0096 34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.1817 0.1787 0.2075 0.0126  -0.0042 -0.0125 34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.1903 0.1908 0.2263 0.0103  -0.0045 -0.0054 34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2015 0.1994 0.2402 0.0124  -0.0046 -0.0070 34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2365 0.2301 0.2737 0.0119  -0.0064 -0.0092 34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2408 0.2317 0.2783 0.0140  -0.0062 -0.0118 34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2044 0.1969 0.2404 0.0092  -0.0081 -0.0082 34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1751 0.1743 0.2015 0.0081  -0.0059 -0.0087 35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1749 0.1724 0.2000 0.0072  -0.0076 -0.0110 35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1674 0.1645 0.1948 0.0042  -0.0088 -0.0089 35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1595 0.1587 0.1856 0.0029  -0.0084 -0.0071 35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.1829 0.1822 0.2032 0.0082  -0.0073 -0.0126 35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2341 0.2324 0.2538 0.0077  -0.0097 -0.0154 35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.2684 0.2658 0.2920 0.0053  -0.0112 -0.0151 35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2447 0.2432 0.2599 0.0097  -0.0102 -0.0178 35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.1608 0.1546 0.1914 0.0032  -0.0100 -0.0090 36  SER   C N   
1318 C CA  A SER   B 30  ? 0.1545 0.1471 0.1871 0.0006  -0.0105 -0.0066 36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.1587 0.1514 0.1912 0.0006  -0.0104 -0.0065 36  SER   C CA  
1320 C C   . SER   B 30  ? 0.1648 0.1594 0.1972 -0.0011 -0.0106 -0.0073 36  SER   C C   
1321 O O   . SER   B 30  ? 0.1704 0.1658 0.2026 -0.0028 -0.0098 -0.0048 36  SER   C O   
1322 C CB  A SER   B 30  ? 0.1701 0.1582 0.2063 0.0000  -0.0115 -0.0069 36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.1859 0.1742 0.2219 0.0000  -0.0114 -0.0063 36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.2208 0.2072 0.2578 0.0017  -0.0115 -0.0059 36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2378 0.2244 0.2757 0.0000  -0.0126 -0.0098 36  SER   C OG  
1326 N N   . SER   B 31  ? 0.1527 0.1479 0.1849 -0.0003 -0.0118 -0.0108 37  SER   C N   
1327 C CA  . SER   B 31  ? 0.1536 0.1512 0.1870 -0.0017 -0.0125 -0.0116 37  SER   C CA  
1328 C C   . SER   B 31  ? 0.1656 0.1667 0.1955 -0.0014 -0.0112 -0.0100 37  SER   C C   
1329 O O   . SER   B 31  ? 0.1709 0.1742 0.2025 -0.0027 -0.0112 -0.0096 37  SER   C O   
1330 C CB  . SER   B 31  ? 0.1933 0.1906 0.2270 -0.0007 -0.0149 -0.0160 37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.2602 0.2588 0.2880 0.0022  -0.0150 -0.0177 37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1495 0.1513 0.1755 0.0004  -0.0101 -0.0092 38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1416 0.1459 0.1644 0.0007  -0.0089 -0.0076 38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1382 0.1421 0.1606 -0.0003 -0.0077 -0.0044 38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1463 0.1516 0.1663 -0.0003 -0.0069 -0.0032 38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1439 0.1489 0.1627 0.0033  -0.0082 -0.0086 38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1610 0.1661 0.1778 0.0049  -0.0097 -0.0119 38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1599 0.1650 0.1712 0.0079  -0.0085 -0.0126 38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.1550 0.1620 0.1637 0.0081  -0.0071 -0.0104 38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.1676 0.1747 0.1711 0.0105  -0.0062 -0.0106 38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.1897 0.1953 0.1889 0.0132  -0.0067 -0.0131 38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.1823 0.1904 0.1839 0.0105  -0.0051 -0.0085 38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1460 0.1475 0.1703 -0.0010 -0.0079 -0.0031 39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1429 0.1435 0.1661 -0.0014 -0.0077 -0.0004 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1407 0.1430 0.1628 -0.0001 -0.0073 -0.0002 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1454 0.1479 0.1660 -0.0006 -0.0074 0.0014  39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1520 0.1523 0.1733 -0.0029 -0.0071 0.0015  39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1501 0.1485 0.1690 -0.0030 -0.0075 0.0039  39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1640 0.1603 0.1842 -0.0027 -0.0086 0.0048  39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1525 0.1513 0.1681 -0.0032 -0.0071 0.0048  39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1374 0.1405 0.1602 0.0016  -0.0068 -0.0018 40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1318 0.1365 0.1548 0.0027  -0.0057 -0.0012 40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1415 0.1460 0.1681 0.0041  -0.0054 -0.0013 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1489 0.1520 0.1763 0.0051  -0.0055 -0.0030 40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1437 0.1500 0.1638 0.0040  -0.0041 -0.0023 40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1607 0.1677 0.1777 0.0032  -0.0042 -0.0020 40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.1772 0.1850 0.1907 0.0052  -0.0029 -0.0030 40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.1722 0.1793 0.1894 0.0020  -0.0042 0.0001  40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1316 0.1376 0.1610 0.0042  -0.0050 0.0002  41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1379 0.1449 0.1720 0.0058  -0.0042 0.0002  41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1418 0.1515 0.1781 0.0061  -0.0022 0.0013  41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1468 0.1571 0.1828 0.0045  -0.0030 0.0026  41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1384 0.1441 0.1763 0.0055  -0.0067 0.0013  41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1379 0.1449 0.1820 0.0074  -0.0062 0.0013  41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1544 0.1583 0.2003 0.0079  -0.0086 0.0015  41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1533 0.1635 0.2029 0.0071  -0.0065 0.0030  41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1379 0.1492 0.1766 0.0082  0.0007  0.0009  42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1362 0.1503 0.1783 0.0085  0.0035  0.0023  42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1408 0.1571 0.1912 0.0098  0.0044  0.0028  42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1484 0.1641 0.1994 0.0120  0.0054  0.0014  42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1440 0.1580 0.1807 0.0103  0.0073  0.0017  42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.1668 0.1833 0.2078 0.0106  0.0111  0.0039  42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1529 0.1651 0.1824 0.0093  0.0060  0.0012  42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1453 0.1642 0.2029 0.0084  0.0036  0.0046  43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1435 0.1656 0.2111 0.0096  0.0044  0.0053  43  SER   C CA  
1376 C C   . SER   B 37  ? 0.1645 0.1902 0.2380 0.0094  0.0086  0.0070  43  SER   C C   
1377 O O   . SER   B 37  ? 0.1700 0.1952 0.2404 0.0079  0.0096  0.0079  43  SER   C O   
1378 C CB  . SER   B 37  ? 0.1559 0.1781 0.2286 0.0082  -0.0009 0.0059  43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.1699 0.1919 0.2422 0.0055  -0.0036 0.0068  43  SER   C OG  
1380 N N   . SER   B 38  ? 0.1624 0.1917 0.2452 0.0111  0.0111  0.0076  44  SER   C N   
1381 C CA  . SER   B 38  ? 0.1840 0.2171 0.2743 0.0109  0.0158  0.0096  44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2127 0.2489 0.3142 0.0081  0.0122  0.0110  44  SER   C C   
1383 O O   . SER   B 38  ? 0.2131 0.2495 0.3187 0.0075  0.0067  0.0103  44  SER   C O   
1384 C CB  . SER   B 38  ? 0.1970 0.2329 0.2925 0.0143  0.0211  0.0096  44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.2484 0.2863 0.3525 0.0152  0.0180  0.0089  44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2272 0.2651 0.3331 0.0063  0.0151  0.0129  45  THR   C N   
1387 C CA  . THR   B 39  ? 0.2560 0.2964 0.3730 0.0033  0.0116  0.0139  45  THR   C CA  
1388 C C   . THR   B 39  ? 0.2808 0.3265 0.4113 0.0032  0.0170  0.0162  45  THR   C C   
1389 O O   . THR   B 39  ? 0.2934 0.3394 0.4212 0.0050  0.0242  0.0175  45  THR   C O   
1390 C CB  . THR   B 39  ? 0.2817 0.3184 0.3921 0.0004  0.0094  0.0142  45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3056 0.3417 0.4133 0.0005  0.0156  0.0160  45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3013 0.3329 0.3980 0.0005  0.0054  0.0123  45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.2994 0.3490 0.4442 0.0011  0.0137  0.0168  46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3177 0.3727 0.4775 0.0002  0.0188  0.0192  46  THR   C CA  
1395 C C   . THR   B 40  ? 0.3252 0.3782 0.4852 -0.0031 0.0201  0.0210  46  THR   C C   
1396 O O   . THR   B 40  ? 0.3488 0.4040 0.5150 -0.0034 0.0273  0.0237  46  THR   C O   
1397 C CB  . THR   B 40  ? 0.3382 0.3991 0.5156 -0.0003 0.0145  0.0190  46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.3741 0.4327 0.5506 -0.0027 0.0051  0.0172  46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.3466 0.4099 0.5257 0.0037  0.0152  0.0179  46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.3086 0.3572 0.4618 -0.0055 0.0138  0.0195  47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.3078 0.3536 0.4607 -0.0085 0.0143  0.0208  47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.3003 0.3409 0.4374 -0.0073 0.0189  0.0216  47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.3070 0.3451 0.4314 -0.0048 0.0184  0.0200  47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.3144 0.3572 0.4667 -0.0112 0.0052  0.0185  47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.2862 0.3251 0.4244 -0.0089 0.0229  0.0240  48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.2831 0.3170 0.4072 -0.0076 0.0272  0.0251  48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.2784 0.3068 0.3916 -0.0088 0.0212  0.0230  48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.2915 0.3184 0.4098 -0.0118 0.0167  0.0224  48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.3135 0.3473 0.4440 -0.0088 0.0342  0.0291  48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.3928 0.4210 0.5092 -0.0073 0.0384  0.0309  48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.4981 0.5259 0.6030 -0.0029 0.0438  0.0313  48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.5377 0.5695 0.6461 -0.0007 0.0464  0.0310  48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.5321 0.5547 0.6227 -0.0011 0.0455  0.0320  48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.2452 0.2706 0.3438 -0.0062 0.0213  0.0217  49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.2429 0.2634 0.3307 -0.0068 0.0167  0.0198  49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.2516 0.2681 0.3335 -0.0069 0.0201  0.0218  49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.2720 0.2884 0.3507 -0.0049 0.0263  0.0241  49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.2297 0.2423 0.3085 -0.0086 0.0161  0.0208  50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.2378 0.2461 0.3120 -0.0088 0.0188  0.0227  50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.2367 0.2408 0.2973 -0.0071 0.0166  0.0211  50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.2504 0.2503 0.3073 -0.0073 0.0177  0.0224  50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.2628 0.2695 0.3472 -0.0123 0.0171  0.0235  50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.3105 0.3224 0.4132 -0.0144 0.0210  0.0263  50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.1962 0.2015 0.2501 -0.0055 0.0140  0.0186  51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.1939 0.1961 0.2364 -0.0039 0.0125  0.0173  51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2098 0.2113 0.2451 -0.0009 0.0172  0.0190  51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2350 0.2390 0.2713 0.0005  0.0206  0.0200  51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2074 0.2109 0.2457 -0.0033 0.0085  0.0143  51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.2598 0.2628 0.3020 -0.0055 0.0035  0.0126  51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.2844 0.2849 0.3300 -0.0073 0.0020  0.0128  51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.2394 0.2439 0.2809 -0.0053 0.0008  0.0110  51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2131 0.2111 0.2410 0.0002  0.0171  0.0193  52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2312 0.2280 0.2506 0.0035  0.0203  0.0206  52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2060 0.2038 0.2183 0.0052  0.0170  0.0175  52  THR   C C   
1435 O O   . THR   B 46  ? 0.2286 0.2254 0.2396 0.0044  0.0134  0.0158  52  THR   C O   
1436 C CB  . THR   B 46  ? 0.2924 0.2844 0.3084 0.0039  0.0215  0.0228  52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3162 0.3071 0.3395 0.0021  0.0253  0.0260  52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3129 0.3031 0.3183 0.0077  0.0233  0.0237  52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.1962 0.1954 0.2035 0.0078  0.0184  0.0170  53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.1900 0.1900 0.1916 0.0093  0.0152  0.0141  53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.1818 0.1793 0.1754 0.0119  0.0152  0.0146  53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2005 0.1960 0.1896 0.0142  0.0185  0.0169  53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2072 0.2096 0.2080 0.0107  0.0158  0.0126  53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2360 0.2408 0.2452 0.0087  0.0162  0.0125  53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2090 0.2121 0.2055 0.0117  0.0121  0.0094  53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2631 0.2688 0.2769 0.0059  0.0120  0.0110  53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.1768 0.1742 0.1683 0.0120  0.0118  0.0128  54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.1800 0.1756 0.1646 0.0148  0.0110  0.0130  54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.1706 0.1671 0.1492 0.0178  0.0107  0.0116  54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.1684 0.1674 0.1487 0.0173  0.0093  0.0092  54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.1772 0.1735 0.1626 0.0141  0.0075  0.0110  54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.1702 0.1641 0.1415 0.0211  0.0117  0.0131  55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.1717 0.1655 0.1353 0.0246  0.0106  0.0115  55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.1744 0.1670 0.1332 0.0271  0.0075  0.0112  55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2039 0.1928 0.1570 0.0295  0.0091  0.0140  55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.1772 0.1684 0.1352 0.0270  0.0152  0.0139  55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.1922 0.1851 0.1570 0.0246  0.0188  0.0147  55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2012 0.1974 0.1694 0.0236  0.0163  0.0109  55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2093 0.2071 0.1841 0.0218  0.0198  0.0119  55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2193 0.2199 0.1998 0.0201  0.0183  0.0096  55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.1964 0.1981 0.1767 0.0197  0.0138  0.0063  55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2417 0.2437 0.2287 0.0188  0.0213  0.0107  55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.1636 0.1593 0.1256 0.0264  0.0032  0.0080  56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.1743 0.1702 0.1352 0.0281  0.0000  0.0075  56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.1835 0.1837 0.1490 0.0273  -0.0043 0.0037  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.1762 0.1787 0.1458 0.0250  -0.0046 0.0018  56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.1673 0.1616 0.1320 0.0263  0.0015  0.0097  56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.1703 0.1678 0.1446 0.0216  0.0011  0.0080  56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.1830 0.1843 0.1489 0.0289  -0.0073 0.0030  57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.1894 0.1953 0.1618 0.0279  -0.0109 -0.0001 57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.1775 0.1847 0.1554 0.0267  -0.0104 0.0006  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.1738 0.1846 0.1563 0.0272  -0.0131 -0.0012 57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2210 0.2284 0.1906 0.0312  -0.0155 -0.0025 57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.2486 0.2542 0.2136 0.0350  -0.0171 -0.0011 57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.2725 0.2750 0.2357 0.0353  -0.0142 0.0021  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.3355 0.3426 0.2987 0.0380  -0.0218 -0.0032 57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.1664 0.1709 0.1447 0.0250  -0.0071 0.0029  58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.1676 0.1724 0.1502 0.0239  -0.0065 0.0032  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.1613 0.1706 0.1505 0.0218  -0.0074 0.0009  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.1546 0.1656 0.1459 0.0196  -0.0075 -0.0003 58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1720 0.1730 0.1543 0.0218  -0.0033 0.0052  58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.1914 0.1864 0.1679 0.0240  -0.0014 0.0086  58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1434 0.1543 0.1360 0.0225  -0.0077 0.0005  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1493 0.1641 0.1484 0.0206  -0.0075 -0.0011 59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1523 0.1650 0.1517 0.0201  -0.0051 -0.0003 59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1534 0.1689 0.1573 0.0196  -0.0042 -0.0011 59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1382 0.1581 0.1425 0.0223  -0.0102 -0.0029 59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.1502 0.1725 0.1556 0.0217  -0.0129 -0.0047 59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.1769 0.2045 0.1891 0.0229  -0.0161 -0.0068 59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2112 0.2393 0.2214 0.0258  -0.0197 -0.0077 59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1601 0.1916 0.1804 0.0209  -0.0148 -0.0074 59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1518 0.1593 0.1467 0.0202  -0.0037 0.0014  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.1663 0.1708 0.1608 0.0196  -0.0018 0.0016  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.1755 0.1757 0.1671 0.0173  -0.0009 0.0028  60  THR   C C   
1495 O O   . THR   B 54  ? 0.1871 0.1856 0.1766 0.0174  -0.0010 0.0041  60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2361 0.2384 0.2296 0.0225  -0.0017 0.0019  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.2721 0.2703 0.2615 0.0240  -0.0021 0.0037  60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2721 0.2793 0.2696 0.0250  -0.0028 0.0008  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1669 0.1653 0.1586 0.0155  0.0000  0.0022  61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.1649 0.1597 0.1553 0.0131  0.0002  0.0030  61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1417 0.1341 0.1313 0.0118  0.0004  0.0019  61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.1655 0.1581 0.1544 0.0130  0.0011  0.0009  61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1409 0.1311 0.1304 0.0095  -0.0002 0.0022  62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1437 0.1306 0.1312 0.0084  -0.0009 0.0010  62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1604 0.1490 0.1493 0.0061  -0.0018 0.0011  62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1589 0.1484 0.1505 0.0049  -0.0023 0.0021  62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.1614 0.1425 0.1479 0.0080  -0.0018 0.0009  62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.1896 0.1670 0.1733 0.0070  -0.0034 -0.0008 62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.1802 0.1590 0.1653 0.0105  -0.0008 0.0010  62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1539 0.1424 0.1405 0.0058  -0.0020 0.0002  63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1434 0.1326 0.1308 0.0039  -0.0032 0.0005  63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1591 0.1438 0.1425 0.0033  -0.0051 -0.0004 63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.1676 0.1490 0.1464 0.0047  -0.0048 -0.0016 63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1546 0.1479 0.1433 0.0037  -0.0021 0.0010  63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1579 0.1505 0.1431 0.0045  -0.0006 0.0006  63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1652 0.1589 0.1500 0.0064  0.0015  0.0001  63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1592 0.1503 0.1417 0.0037  -0.0011 0.0010  63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.1881 0.1816 0.1702 0.0073  0.0038  0.0001  63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.1638 0.1539 0.1423 0.0047  0.0011  0.0011  63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.1889 0.1802 0.1673 0.0064  0.0038  0.0006  63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2121 0.2031 0.1874 0.0075  0.0068  0.0010  63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.1634 0.1478 0.1486 0.0017  -0.0074 -0.0001 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.1717 0.1520 0.1529 0.0013  -0.0101 -0.0012 64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.1701 0.1507 0.1471 0.0017  -0.0095 -0.0007 64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1627 0.1466 0.1430 0.0010  -0.0091 0.0005  64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.1724 0.1521 0.1583 -0.0006 -0.0133 -0.0011 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.1953 0.1705 0.1768 -0.0007 -0.0171 -0.0026 64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.1967 0.1667 0.1734 0.0001  -0.0186 -0.0046 64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2186 0.1944 0.2005 -0.0013 -0.0196 -0.0021 64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2312 0.1963 0.2024 0.0003  -0.0228 -0.0064 64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2319 0.2032 0.2086 -0.0010 -0.0237 -0.0035 64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2537 0.2196 0.2249 -0.0002 -0.0255 -0.0058 64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.2885 0.2492 0.2531 0.0005  -0.0301 -0.0076 64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.1724 0.1488 0.1419 0.0031  -0.0097 -0.0018 65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.1725 0.1481 0.1365 0.0039  -0.0086 -0.0010 65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.1945 0.1646 0.1521 0.0041  -0.0127 -0.0019 65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2253 0.1903 0.1761 0.0054  -0.0140 -0.0038 65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.1805 0.1558 0.1403 0.0059  -0.0045 -0.0012 65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2154 0.1883 0.1670 0.0072  -0.0021 0.0002  65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.1987 0.1697 0.1586 0.0030  -0.0152 -0.0008 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2265 0.1928 0.1812 0.0033  -0.0201 -0.0017 66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2361 0.1972 0.1787 0.0056  -0.0194 -0.0018 66  SER   C C   
1543 O O   . SER   B 60  ? 0.2424 0.1978 0.1779 0.0067  -0.0232 -0.0038 66  SER   C O   
1544 C CB  . SER   B 60  ? 0.2873 0.2561 0.2478 0.0020  -0.0228 -0.0003 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.3788 0.3490 0.3380 0.0023  -0.0201 0.0020  66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2226 0.1850 0.1625 0.0065  -0.0143 0.0002  67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2363 0.1936 0.1641 0.0090  -0.0123 0.0007  67  SER   C CA  
1548 C C   . SER   B 61  ? 0.2505 0.2040 0.1711 0.0111  -0.0107 -0.0016 67  SER   C C   
1549 O O   . SER   B 61  ? 0.2704 0.2188 0.1795 0.0137  -0.0090 -0.0016 67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2403 0.2005 0.1691 0.0089  -0.0069 0.0039  67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2232 0.1886 0.1589 0.0084  -0.0023 0.0040  67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2282 0.1834 0.1547 0.0104  -0.0112 -0.0037 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2234 0.1743 0.1441 0.0125  -0.0106 -0.0064 68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2366 0.1845 0.1598 0.0114  -0.0162 -0.0092 68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.2626 0.2061 0.1815 0.0130  -0.0165 -0.0119 68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2376 0.1930 0.1635 0.0130  -0.0049 -0.0058 68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.2560 0.2142 0.1804 0.0141  0.0009  -0.0033 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.2865 0.2386 0.1978 0.0175  0.0034  -0.0041 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3236 0.2787 0.2347 0.0184  0.0100  -0.0012 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.3567 0.3109 0.2638 0.0183  0.0115  0.0015  68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.3521 0.3024 0.2543 0.0176  0.0064  0.0018  68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.3836 0.3406 0.2918 0.0189  0.0181  0.0043  68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2521 0.2026 0.1833 0.0088  -0.0204 -0.0087 69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.2719 0.2209 0.2090 0.0071  -0.0251 -0.0108 69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.2937 0.2433 0.2347 0.0071  -0.0224 -0.0117 69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3133 0.2578 0.2526 0.0075  -0.0250 -0.0144 69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3290 0.2705 0.2576 0.0081  -0.0310 -0.0139 69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.4388 0.3813 0.3716 0.0064  -0.0366 -0.0134 69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.5415 0.4810 0.4644 0.0083  -0.0386 -0.0128 69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.5958 0.5413 0.5245 0.0072  -0.0361 -0.0091 69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.6020 0.5482 0.5327 0.0067  -0.0400 -0.0080 69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.6161 0.5579 0.5436 0.0072  -0.0472 -0.0102 69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.5758 0.5270 0.5118 0.0059  -0.0372 -0.0048 69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2761 0.2314 0.2221 0.0071  -0.0172 -0.0095 70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2649 0.2204 0.2133 0.0080  -0.0145 -0.0101 70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2244 0.1868 0.1820 0.0067  -0.0117 -0.0076 70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2098 0.1769 0.1701 0.0059  -0.0104 -0.0057 70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3137 0.2677 0.2545 0.0111  -0.0102 -0.0106 70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4570 0.4031 0.3881 0.0135  -0.0116 -0.0138 70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5639 0.5102 0.4904 0.0167  -0.0061 -0.0138 70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6536 0.5920 0.5711 0.0197  -0.0067 -0.0173 70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.7040 0.6358 0.6098 0.0209  -0.0095 -0.0191 70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2036 0.1661 0.1654 0.0067  -0.0108 -0.0078 71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.1865 0.1547 0.1551 0.0064  -0.0081 -0.0057 71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2195 0.1889 0.1859 0.0090  -0.0045 -0.0058 71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2569 0.2218 0.2185 0.0111  -0.0040 -0.0076 71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.1930 0.1600 0.1670 0.0053  -0.0093 -0.0053 71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2034 0.1704 0.1821 0.0025  -0.0123 -0.0049 71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2368 0.2088 0.2219 0.0011  -0.0115 -0.0028 71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2042 0.1668 0.1825 0.0013  -0.0162 -0.0066 71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2219 0.1928 0.2110 -0.0010 -0.0145 -0.0030 71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2507 0.2162 0.2364 -0.0011 -0.0176 -0.0052 71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.1806 0.1561 0.1511 0.0091  -0.0020 -0.0042 72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.1783 0.1562 0.1489 0.0115  0.0012  -0.0042 72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.1717 0.1540 0.1484 0.0117  0.0017  -0.0030 72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.1736 0.1597 0.1543 0.0102  0.0012  -0.0017 72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.1933 0.1747 0.1631 0.0118  0.0037  -0.0035 72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2240 0.2009 0.1860 0.0125  0.0041  -0.0044 72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2468 0.2199 0.2031 0.0152  0.0059  -0.0059 72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2383 0.2145 0.1979 0.0109  0.0027  -0.0036 72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2609 0.2293 0.2083 0.0164  0.0065  -0.0068 72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2561 0.2275 0.2070 0.0120  0.0028  -0.0042 72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2816 0.2490 0.2259 0.0147  0.0048  -0.0058 72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3222 0.2841 0.2561 0.0164  0.0051  -0.0065 72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.1684 0.1503 0.1456 0.0142  0.0029  -0.0033 73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.1599 0.1459 0.1418 0.0150  0.0032  -0.0022 73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.1777 0.1701 0.1632 0.0157  0.0049  -0.0020 73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2073 0.2003 0.1919 0.0171  0.0072  -0.0027 73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.1800 0.1623 0.1605 0.0177  0.0036  -0.0028 73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.1876 0.1663 0.1636 0.0190  0.0047  -0.0046 73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.1740 0.1509 0.1466 0.0165  0.0038  -0.0050 73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1586 0.1556 0.1484 0.0149  0.0041  -0.0011 74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.1602 0.1633 0.1549 0.0152  0.0051  -0.0012 74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.1534 0.1601 0.1519 0.0162  0.0034  -0.0009 74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.1791 0.1841 0.1760 0.0159  0.0018  -0.0002 74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.1906 0.1953 0.1862 0.0125  0.0052  -0.0008 74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2136 0.2156 0.2052 0.0120  0.0072  -0.0008 74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.1981 0.2016 0.1931 0.0105  0.0031  -0.0002 74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1483 0.1605 0.1524 0.0173  0.0038  -0.0014 75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1505 0.1668 0.1585 0.0178  0.0014  -0.0017 75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1379 0.1569 0.1489 0.0149  0.0011  -0.0019 75  SER   C C   
1622 O O   . SER   B 69  ? 0.1518 0.1711 0.1639 0.0132  0.0032  -0.0016 75  SER   C O   
1623 C CB  . SER   B 69  ? 0.1726 0.1940 0.1869 0.0202  0.0013  -0.0024 75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.2513 0.2702 0.2633 0.0232  0.0016  -0.0023 75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1277 0.1478 0.1392 0.0145  -0.0014 -0.0022 76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1336 0.1554 0.1477 0.0120  -0.0020 -0.0026 76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1370 0.1623 0.1547 0.0128  -0.0051 -0.0041 76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1507 0.1761 0.1667 0.0154  -0.0071 -0.0044 76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1417 0.1593 0.1510 0.0102  -0.0017 -0.0017 76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1334 0.1480 0.1379 0.0113  -0.0027 -0.0012 76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1489 0.1597 0.1496 0.0121  -0.0017 -0.0001 76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1497 0.1648 0.1535 0.0116  -0.0043 -0.0016 76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1486 0.1565 0.1457 0.0129  -0.0020 0.0009  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1458 0.1579 0.1450 0.0127  -0.0043 -0.0006 76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1451 0.1538 0.1414 0.0133  -0.0030 0.0009  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1221 0.1499 0.1448 0.0107  -0.0056 -0.0049 77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1377 0.1686 0.1645 0.0113  -0.0092 -0.0070 77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1429 0.1711 0.1641 0.0119  -0.0115 -0.0077 77  SER   C C   
1639 O O   . SER   B 71  ? 0.1550 0.1792 0.1699 0.0118  -0.0100 -0.0064 77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1409 0.1753 0.1764 0.0086  -0.0088 -0.0077 77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1615 0.1930 0.1951 0.0061  -0.0075 -0.0070 77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1464 0.1767 0.1698 0.0128  -0.0152 -0.0100 78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.1629 0.1904 0.1803 0.0138  -0.0171 -0.0110 78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.1656 0.1919 0.1850 0.0110  -0.0164 -0.0116 78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.1871 0.2159 0.2141 0.0086  -0.0165 -0.0123 78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.1794 0.2088 0.1974 0.0163  -0.0220 -0.0137 78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.2105 0.2411 0.2271 0.0194  -0.0231 -0.0130 78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.3194 0.3519 0.3365 0.0221  -0.0288 -0.0159 78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.4395 0.4719 0.4527 0.0262  -0.0307 -0.0151 78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.4939 0.5273 0.5058 0.0291  -0.0370 -0.0181 78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.1564 0.1792 0.1697 0.0113  -0.0158 -0.0114 79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.1592 0.1806 0.1745 0.0090  -0.0153 -0.0120 79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.1751 0.1983 0.1964 0.0081  -0.0185 -0.0150 79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2034 0.2271 0.2234 0.0102  -0.0222 -0.0176 79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.1878 0.2057 0.1958 0.0106  -0.0144 -0.0117 79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2248 0.2417 0.2273 0.0127  -0.0130 -0.0096 79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.1754 0.1950 0.1801 0.0139  -0.0151 -0.0103 79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.1682 0.1920 0.1960 0.0051  -0.0174 -0.0146 80  SER   C N   
1659 C CA  . SER   B 74  ? 0.1727 0.1981 0.2080 0.0036  -0.0203 -0.0172 80  SER   C CA  
1660 C C   . SER   B 74  ? 0.1748 0.1983 0.2144 0.0006  -0.0185 -0.0163 80  SER   C C   
1661 O O   . SER   B 74  ? 0.1582 0.1794 0.1946 -0.0002 -0.0152 -0.0137 80  SER   C O   
1662 C CB  . SER   B 74  ? 0.2141 0.2443 0.2570 0.0033  -0.0213 -0.0175 80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.2967 0.3283 0.3441 0.0011  -0.0172 -0.0146 80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.1780 0.2021 0.2249 -0.0011 -0.0210 -0.0187 81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.1917 0.2136 0.2438 -0.0041 -0.0194 -0.0177 81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.1858 0.2107 0.2452 -0.0066 -0.0163 -0.0150 81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2055 0.2346 0.2726 -0.0071 -0.0177 -0.0161 81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2105 0.2315 0.2682 -0.0050 -0.0236 -0.0216 81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.2668 0.2833 0.3174 -0.0030 -0.0256 -0.0241 81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.2971 0.3132 0.3510 -0.0024 -0.0313 -0.0293 81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.2912 0.3036 0.3415 -0.0045 -0.0230 -0.0222 81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.1628 0.1854 0.2201 -0.0078 -0.0123 -0.0115 82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.1776 0.2018 0.2392 -0.0096 -0.0083 -0.0082 82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.1881 0.2085 0.2513 -0.0120 -0.0058 -0.0058 82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.1777 0.1938 0.2346 -0.0115 -0.0058 -0.0050 82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2123 0.2371 0.2668 -0.0078 -0.0056 -0.0061 82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.2426 0.2709 0.2963 -0.0054 -0.0080 -0.0082 82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2466 0.2723 0.3038 -0.0091 -0.0010 -0.0028 82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.2701 0.2985 0.3174 -0.0034 -0.0061 -0.0067 82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2011 0.2228 0.2730 -0.0146 -0.0036 -0.0043 83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2126 0.2302 0.2861 -0.0168 -0.0010 -0.0014 83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2135 0.2280 0.2780 -0.0159 0.0028  0.0025  83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2253 0.2421 0.2871 -0.0149 0.0055  0.0039  83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2280 0.2482 0.3138 -0.0198 0.0013  -0.0003 83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.2621 0.2773 0.3498 -0.0222 0.0044  0.0033  83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.2919 0.3030 0.3829 -0.0236 0.0018  0.0019  83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.2935 0.3074 0.3781 -0.0225 0.0101  0.0080  83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3206 0.3264 0.4129 -0.0256 0.0047  0.0055  83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3216 0.3301 0.4066 -0.0243 0.0132  0.0118  83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3254 0.3300 0.4147 -0.0259 0.0104  0.0106  83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2093 0.2184 0.2690 -0.0160 0.0027  0.0039  84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2209 0.2262 0.2719 -0.0151 0.0053  0.0075  84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2238 0.2244 0.2767 -0.0170 0.0073  0.0106  84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2175 0.2152 0.2737 -0.0178 0.0051  0.0096  84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2056 0.2091 0.2485 -0.0129 0.0024  0.0062  84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2196 0.2191 0.2541 -0.0120 0.0042  0.0095  84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.1914 0.1990 0.2323 -0.0111 0.0009  0.0035  84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2499 0.2488 0.2997 -0.0172 0.0118  0.0147  85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.2586 0.2522 0.3085 -0.0186 0.0144  0.0186  85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.2498 0.2376 0.2932 -0.0174 0.0118  0.0193  85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.2396 0.2276 0.2762 -0.0152 0.0091  0.0178  85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3068 0.2991 0.3509 -0.0180 0.0198  0.0228  85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.3692 0.3674 0.4194 -0.0186 0.0233  0.0226  85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.4488 0.4480 0.5106 -0.0217 0.0271  0.0248  85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.4733 0.4778 0.5417 -0.0222 0.0302  0.0248  85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.4521 0.4467 0.5171 -0.0235 0.0269  0.0264  85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.2528 0.2355 0.2987 -0.0188 0.0126  0.0218  86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.2573 0.2343 0.2977 -0.0174 0.0101  0.0228  86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.2437 0.2182 0.2722 -0.0149 0.0105  0.0254  86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.2545 0.2289 0.2779 -0.0145 0.0141  0.0280  86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.2797 0.2508 0.3245 -0.0192 0.0117  0.0260  86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.2221 0.1946 0.2463 -0.0130 0.0067  0.0243  87  SER   C N   
1713 C CA  . SER   B 81  ? 0.2207 0.1905 0.2348 -0.0106 0.0056  0.0262  87  SER   C CA  
1714 C C   . SER   B 81  ? 0.2349 0.1996 0.2480 -0.0094 0.0026  0.0274  87  SER   C C   
1715 O O   . SER   B 81  ? 0.2482 0.2115 0.2683 -0.0105 0.0018  0.0265  87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2200 0.1944 0.2313 -0.0092 0.0032  0.0229  87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2200 0.1966 0.2360 -0.0087 -0.0003 0.0196  87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.2471 0.2090 0.2519 -0.0071 0.0004  0.0288  88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.2569 0.2148 0.2615 -0.0055 -0.0031 0.0297  88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.2685 0.2305 0.2796 -0.0050 -0.0064 0.0254  88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.2793 0.2386 0.2932 -0.0039 -0.0087 0.0254  88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.3179 0.2721 0.3123 -0.0029 -0.0054 0.0321  88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.4032 0.3617 0.3944 -0.0018 -0.0079 0.0294  88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.5362 0.4952 0.5200 -0.0018 -0.0054 0.0300  88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.5012 0.4621 0.4875 -0.0036 -0.0010 0.0302  88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.6148 0.5725 0.5909 0.0000  -0.0079 0.0300  88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.2508 0.2188 0.2643 -0.0055 -0.0063 0.0218  89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.2533 0.2252 0.2717 -0.0048 -0.0085 0.0180  89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.2446 0.2178 0.2701 -0.0061 -0.0078 0.0153  89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.2699 0.2440 0.2991 -0.0050 -0.0095 0.0127  89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.2512 0.2280 0.2671 -0.0044 -0.0089 0.0161  89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.2784 0.2538 0.2872 -0.0032 -0.0101 0.0180  89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3028 0.2767 0.3106 -0.0014 -0.0135 0.0185  89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.2921 0.2676 0.2953 -0.0037 -0.0082 0.0190  89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3228 0.2951 0.3241 -0.0003 -0.0156 0.0199  89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3262 0.2999 0.3221 -0.0023 -0.0098 0.0201  89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.3529 0.3248 0.3477 -0.0007 -0.0139 0.0205  89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4115 0.3813 0.3991 0.0006  -0.0164 0.0211  89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2229 0.1967 0.2506 -0.0082 -0.0052 0.0155  90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2293 0.2049 0.2640 -0.0096 -0.0052 0.0124  90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.2589 0.2323 0.2979 -0.0121 -0.0028 0.0143  90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.2455 0.2188 0.2820 -0.0131 0.0001  0.0174  90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2134 0.1952 0.2485 -0.0096 -0.0052 0.0092  90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.1953 0.1799 0.2270 -0.0075 -0.0068 0.0074  90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.1935 0.1806 0.2204 -0.0069 -0.0062 0.0083  90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.1884 0.1733 0.2220 -0.0059 -0.0086 0.0047  90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.1933 0.1828 0.2181 -0.0053 -0.0075 0.0069  90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.1886 0.1764 0.2200 -0.0041 -0.0093 0.0034  90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.1877 0.1778 0.2151 -0.0040 -0.0088 0.0046  90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.1857 0.1783 0.2120 -0.0025 -0.0094 0.0037  90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.2842 0.2564 0.3303 -0.0134 -0.0037 0.0119  91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.2856 0.2569 0.3381 -0.0164 -0.0015 0.0132  91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.2729 0.2506 0.3277 -0.0175 -0.0002 0.0116  91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.2544 0.2366 0.3065 -0.0159 -0.0018 0.0087  91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.2994 0.2681 0.3590 -0.0171 -0.0041 0.0097  91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3085 0.2801 0.3653 -0.0144 -0.0072 0.0053  91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.2874 0.2592 0.3362 -0.0121 -0.0068 0.0078  91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.2608 0.2393 0.3219 -0.0202 0.0026  0.0132  92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.2642 0.2492 0.3300 -0.0213 0.0034  0.0114  92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.2486 0.2365 0.3187 -0.0208 -0.0011 0.0055  92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.2634 0.2477 0.3372 -0.0213 -0.0037 0.0034  92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.2812 0.2663 0.3558 -0.0245 0.0070  0.0140  92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2232 0.2165 0.2906 -0.0192 -0.0024 0.0030  93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2167 0.2119 0.2851 -0.0180 -0.0066 -0.0022 93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2113 0.2127 0.2784 -0.0168 -0.0071 -0.0039 93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2199 0.2236 0.2843 -0.0166 -0.0042 -0.0013 93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2216 0.2136 0.2827 -0.0153 -0.0084 -0.0033 93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2041 0.1984 0.2565 -0.0130 -0.0074 -0.0019 93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2082 0.1989 0.2553 -0.0112 -0.0076 -0.0006 93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.1790 0.1721 0.2201 -0.0089 -0.0081 -0.0014 93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.1969 0.1922 0.2337 -0.0084 -0.0067 0.0005  93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.1807 0.1777 0.2132 -0.0065 -0.0073 -0.0003 93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2002 0.1958 0.2370 -0.0099 -0.0045 0.0031  93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2136 0.2169 0.2814 -0.0155 -0.0109 -0.0085 94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2145 0.2226 0.2790 -0.0136 -0.0118 -0.0100 94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.1985 0.2051 0.2529 -0.0107 -0.0120 -0.0100 94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2126 0.2162 0.2645 -0.0094 -0.0138 -0.0121 94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.2236 0.2340 0.2927 -0.0133 -0.0162 -0.0148 94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.2548 0.2685 0.3354 -0.0161 -0.0162 -0.0148 94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.2713 0.2906 0.3548 -0.0160 -0.0149 -0.0139 94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.2868 0.2980 0.3763 -0.0190 -0.0169 -0.0153 94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.2955 0.3186 0.3911 -0.0186 -0.0144 -0.0137 94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.2968 0.3114 0.3985 -0.0219 -0.0166 -0.0152 94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.3174 0.3384 0.4225 -0.0217 -0.0151 -0.0142 94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.3620 0.3871 0.4808 -0.0247 -0.0143 -0.0138 94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.1543 0.1630 0.2037 -0.0096 -0.0099 -0.0078 95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.1566 0.1645 0.1981 -0.0071 -0.0100 -0.0078 95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1534 0.1644 0.1928 -0.0051 -0.0119 -0.0105 95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.1711 0.1856 0.2129 -0.0053 -0.0119 -0.0106 95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.1616 0.1692 0.1988 -0.0071 -0.0072 -0.0043 95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.1610 0.1684 0.1916 -0.0049 -0.0074 -0.0043 95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.1522 0.1580 0.1791 -0.0051 -0.0057 -0.0012 95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.1641 0.1672 0.1915 -0.0062 -0.0049 0.0008  95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1514 0.1581 0.1740 -0.0038 -0.0053 -0.0009 95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1409 0.1505 0.1758 -0.0029 -0.0134 -0.0126 96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1396 0.1509 0.1708 -0.0005 -0.0152 -0.0149 96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1462 0.1584 0.1712 0.0012  -0.0132 -0.0128 96  SER   C C   
1798 O O   . SER   B 90  ? 0.1486 0.1596 0.1720 0.0006  -0.0109 -0.0102 96  SER   C O   
1799 C CB  . SER   B 90  ? 0.1730 0.1818 0.2016 0.0014  -0.0176 -0.0183 96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.1988 0.2049 0.2235 0.0024  -0.0156 -0.0171 96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1483 0.1622 0.1701 0.0033  -0.0144 -0.0140 97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1495 0.1636 0.1656 0.0050  -0.0127 -0.0122 97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1578 0.1728 0.1753 0.0034  -0.0104 -0.0092 97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1614 0.1754 0.1752 0.0039  -0.0086 -0.0073 97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.1552 0.1667 0.1663 0.0066  -0.0113 -0.0118 97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.1665 0.1766 0.1744 0.0088  -0.0131 -0.0148 97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2032 0.2128 0.2045 0.0119  -0.0134 -0.0155 97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.1828 0.1911 0.1926 0.0087  -0.0147 -0.0173 97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2062 0.2139 0.2048 0.0138  -0.0153 -0.0187 97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2120 0.2188 0.2158 0.0118  -0.0162 -0.0200 97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1443 0.1612 0.1671 0.0017  -0.0104 -0.0090 98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1456 0.1629 0.1689 0.0005  -0.0079 -0.0064 98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1493 0.1694 0.1731 0.0017  -0.0078 -0.0065 98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1519 0.1747 0.1795 0.0022  -0.0098 -0.0084 98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1595 0.1765 0.1879 -0.0020 -0.0069 -0.0055 98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.1873 0.2036 0.2150 -0.0031 -0.0040 -0.0028 98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.1827 0.1958 0.2045 -0.0027 -0.0033 -0.0012 98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2264 0.2419 0.2590 -0.0054 -0.0027 -0.0016 98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1408 0.1600 0.1611 0.0021  -0.0059 -0.0047 99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1348 0.1561 0.1553 0.0036  -0.0055 -0.0046 99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1438 0.1650 0.1652 0.0026  -0.0027 -0.0029 99  MET   C C   
1822 O O   . MET   B 93  ? 0.1646 0.1827 0.1826 0.0015  -0.0013 -0.0015 99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1460 0.1652 0.1603 0.0056  -0.0055 -0.0040 99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.1758 0.1946 0.1878 0.0071  -0.0076 -0.0053 99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.1918 0.2075 0.1968 0.0091  -0.0066 -0.0038 99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.1838 0.1967 0.1882 0.0067  -0.0045 -0.0020 99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1282 0.1526 0.1540 0.0030  -0.0017 -0.0031 100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1162 0.1402 0.1419 0.0026  0.0016  -0.0015 100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1301 0.1540 0.1528 0.0049  0.0027  -0.0013 100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1326 0.1586 0.1567 0.0068  0.0010  -0.0024 100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1362 0.1642 0.1705 0.0012  0.0033  -0.0013 100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.1520 0.1797 0.1905 -0.0013 0.0026  -0.0013 100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.1814 0.2130 0.2297 -0.0029 0.0046  -0.0009 100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.1842 0.2069 0.2166 -0.0025 0.0038  0.0005  100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1342 0.1553 0.1527 0.0049  0.0054  0.0000  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1403 0.1606 0.1560 0.0071  0.0069  -0.0001 101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1397 0.1597 0.1551 0.0070  0.0110  0.0010  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1450 0.1634 0.1593 0.0052  0.0123  0.0023  101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1514 0.1666 0.1595 0.0080  0.0058  0.0000  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1430 0.1638 0.1585 0.0092  0.0131  0.0008  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1534 0.1729 0.1664 0.0099  0.0176  0.0018  102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.1754 0.1880 0.1776 0.0107  0.0174  0.0017  102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.1967 0.2069 0.1956 0.0124  0.0158  0.0005  102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1617 0.1856 0.1804 0.0123  0.0203  0.0013  102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.1729 0.1948 0.1877 0.0135  0.0257  0.0024  102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1723 0.2034 0.2031 0.0112  0.0197  0.0012  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.1855 0.1945 0.1824 0.0094  0.0184  0.0029  103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2234 0.2256 0.2102 0.0101  0.0171  0.0025  103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2247 0.2234 0.2062 0.0087  0.0176  0.0040  103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2291 0.2303 0.2149 0.0070  0.0189  0.0057  103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2116 0.2040 0.1834 0.0097  0.0164  0.0034  104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2059 0.1942 0.1711 0.0091  0.0162  0.0048  104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2044 0.1921 0.1712 0.0069  0.0118  0.0051  104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2021 0.1893 0.1701 0.0064  0.0082  0.0037  104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.2248 0.2060 0.1782 0.0114  0.0159  0.0036  104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.2522 0.2287 0.1975 0.0113  0.0153  0.0051  104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.2752 0.2518 0.2186 0.0116  0.0201  0.0078  104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.2610 0.2329 0.2009 0.0107  0.0104  0.0047  104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.2954 0.2669 0.2311 0.0115  0.0179  0.0090  104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3007 0.2693 0.2340 0.0112  0.0118  0.0070  104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.2045 0.1917 0.1711 0.0056  0.0125  0.0072  105 SER   C N   
1862 C CA  . SER   B 99  ? 0.2039 0.1898 0.1710 0.0040  0.0085  0.0077  105 SER   C CA  
1863 C C   . SER   B 99  ? 0.2197 0.2024 0.1822 0.0039  0.0097  0.0103  105 SER   C C   
1864 O O   . SER   B 99  ? 0.2387 0.2219 0.2012 0.0041  0.0143  0.0122  105 SER   C O   
1865 C CB  . SER   B 99  ? 0.2102 0.2011 0.1872 0.0022  0.0070  0.0073  105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.2173 0.2120 0.2005 0.0013  0.0100  0.0085  105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2196 0.1990 0.1789 0.0035  0.0057  0.0105  106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.2507 0.2261 0.2052 0.0035  0.0053  0.0130  106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.2514 0.2281 0.2118 0.0019  0.0010  0.0129  106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.2567 0.2361 0.2223 0.0013  -0.0017 0.0109  106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.2842 0.2529 0.2260 0.0057  0.0035  0.0129  106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.3043 0.2710 0.2391 0.0078  0.0082  0.0129  106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.3670 0.3265 0.2878 0.0106  0.0066  0.0121  106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.4495 0.4043 0.3635 0.0112  0.0035  0.0133  106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.3681 0.3262 0.2843 0.0123  0.0080  0.0100  106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.2743 0.2491 0.2347 0.0015  0.0008  0.0153  107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.2666 0.2431 0.2338 0.0002  -0.0026 0.0151  107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.2488 0.2251 0.2164 0.0006  -0.0079 0.0132  107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.2423 0.2223 0.2179 -0.0004 -0.0094 0.0119  107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.2862 0.2586 0.2502 0.0005  -0.0021 0.0184  107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.2962 0.2677 0.2570 0.0006  0.0035  0.0204  107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.2877 0.2591 0.2428 0.0020  0.0045  0.0186  107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2430 0.2149 0.2022 0.0021  -0.0104 0.0127  108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2460 0.2176 0.2063 0.0022  -0.0156 0.0107  108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2238 0.1991 0.1897 0.0013  -0.0154 0.0082  108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2353 0.2114 0.2051 0.0008  -0.0190 0.0067  108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2100 0.1876 0.1769 0.0011  -0.0111 0.0080  109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.1932 0.1741 0.1652 0.0006  -0.0106 0.0061  109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.1666 0.1523 0.1478 -0.0007 -0.0104 0.0061  109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.1928 0.1807 0.1778 -0.0010 -0.0104 0.0049  109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.1935 0.1752 0.1633 0.0013  -0.0064 0.0057  109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2237 0.2004 0.1839 0.0031  -0.0063 0.0051  109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2397 0.2129 0.1962 0.0034  -0.0102 0.0037  109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2204 0.1968 0.1769 0.0041  -0.0023 0.0058  109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.1605 0.1472 0.1448 -0.0012 -0.0103 0.0074  110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.1667 0.1574 0.1589 -0.0020 -0.0101 0.0070  110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.1709 0.1626 0.1668 -0.0022 -0.0127 0.0061  110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.1905 0.1798 0.1849 -0.0020 -0.0158 0.0061  110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.1741 0.1646 0.1687 -0.0023 -0.0101 0.0083  110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2022 0.1931 0.1968 -0.0028 -0.0064 0.0094  110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1636 0.1585 0.1642 -0.0024 -0.0113 0.0053  111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1682 0.1643 0.1732 -0.0026 -0.0126 0.0048  111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.1783 0.1735 0.1818 -0.0027 -0.0124 0.0041  111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.1948 0.1912 0.2025 -0.0031 -0.0124 0.0040  111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1690 0.1619 0.1666 -0.0022 -0.0117 0.0037  112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1659 0.1575 0.1618 -0.0020 -0.0113 0.0028  112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1546 0.1491 0.1538 -0.0016 -0.0087 0.0030  112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1607 0.1577 0.1604 -0.0011 -0.0069 0.0032  112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1547 0.1485 0.1559 -0.0019 -0.0088 0.0029  113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1555 0.1513 0.1585 -0.0012 -0.0064 0.0035  113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1409 0.1360 0.1402 0.0002  -0.0050 0.0030  113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1575 0.1495 0.1537 0.0005  -0.0056 0.0024  113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2031 0.1983 0.2106 -0.0020 -0.0065 0.0043  113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2423 0.2401 0.2552 -0.0028 -0.0068 0.0049  113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2261 0.2215 0.2334 -0.0009 -0.0038 0.0052  113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.2687 0.2665 0.2882 -0.0039 -0.0065 0.0060  113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1345 0.1323 0.1342 0.0013  -0.0033 0.0033  114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1361 0.1340 0.1336 0.0031  -0.0022 0.0030  114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1486 0.1459 0.1469 0.0038  -0.0012 0.0042  114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1509 0.1499 0.1509 0.0038  -0.0006 0.0048  114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1540 0.1555 0.1521 0.0039  -0.0017 0.0024  114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1623 0.1649 0.1594 0.0060  -0.0012 0.0021  114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1708 0.1715 0.1659 0.0068  -0.0007 0.0017  114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1593 0.1659 0.1586 0.0064  -0.0015 0.0012  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1589 0.1532 0.1555 0.0046  -0.0009 0.0046  115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1723 0.1650 0.1691 0.0053  0.0005  0.0062  115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.1742 0.1660 0.1679 0.0078  0.0010  0.0064  115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.1862 0.1768 0.1785 0.0085  0.0004  0.0053  115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2109 0.1996 0.2098 0.0036  0.0002  0.0069  115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3114 0.3005 0.3143 0.0012  -0.0012 0.0066  115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3670 0.3521 0.3729 -0.0004 -0.0020 0.0069  115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.4475 0.4322 0.4562 -0.0004 0.0007  0.0094  115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.4694 0.4563 0.4835 -0.0016 0.0021  0.0109  115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.4788 0.4681 0.4970 -0.0032 0.0003  0.0099  115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.4569 0.4434 0.4721 -0.0010 0.0055  0.0135  115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.1719 0.1635 0.1641 0.0094  0.0022  0.0079  116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.1804 0.1704 0.1694 0.0122  0.0024  0.0086  116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2050 0.1904 0.1935 0.0122  0.0042  0.0112  116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.1953 0.1795 0.1869 0.0099  0.0052  0.0122  116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.1711 0.1643 0.1578 0.0146  0.0019  0.0083  116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.1716 0.1649 0.1562 0.0151  0.0036  0.0100  116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2265 0.2092 0.2114 0.0150  0.0046  0.0125  117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.2469 0.2247 0.2311 0.0152  0.0068  0.0156  117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.2515 0.2299 0.2356 0.0147  0.0094  0.0179  117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.2864 0.2611 0.2718 0.0139  0.0120  0.0208  117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.2819 0.2565 0.2615 0.0188  0.0067  0.0169  117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.3238 0.3011 0.2986 0.0220  0.0062  0.0173  117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.4331 0.4076 0.4037 0.0259  0.0052  0.0183  117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.4853 0.4628 0.4561 0.0278  0.0026  0.0161  117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.4456 0.4146 0.4127 0.0274  0.0073  0.0218  117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2182 0.2011 0.2012 0.0153  0.0091  0.0168  118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2119 0.1953 0.1939 0.0155  0.0119  0.0187  118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2251 0.2110 0.2136 0.0123  0.0127  0.0181  118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.2530 0.2393 0.2422 0.0123  0.0157  0.0199  118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2056 0.1915 0.1817 0.0187  0.0110  0.0176  118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2045 0.1883 0.1744 0.0223  0.0096  0.0181  118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.1974 0.1840 0.1671 0.0235  0.0058  0.0152  118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.2467 0.2261 0.2108 0.0251  0.0114  0.0212  118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.2320 0.2161 0.1966 0.0269  0.0050  0.0165  118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.2662 0.2456 0.2265 0.0282  0.0082  0.0202  118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2075 0.1951 0.2002 0.0099  0.0101  0.0157  119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.1884 0.1784 0.1870 0.0073  0.0101  0.0150  119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.1683 0.1616 0.1676 0.0065  0.0071  0.0120  119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.1669 0.1603 0.1636 0.0073  0.0051  0.0104  119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.1652 0.1612 0.1682 0.0053  0.0072  0.0115  120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.1671 0.1656 0.1711 0.0044  0.0047  0.0092  120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1633 0.1638 0.1635 0.0064  0.0043  0.0079  120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.1698 0.1711 0.1681 0.0080  0.0059  0.0083  120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.1758 0.1760 0.1855 0.0026  0.0047  0.0093  120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.1881 0.1903 0.1981 0.0021  0.0023  0.0074  120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.1875 0.1859 0.2022 0.0004  0.0039  0.0101  120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1423 0.1436 0.1412 0.0064  0.0022  0.0062  121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1456 0.1492 0.1426 0.0078  0.0012  0.0046  121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1546 0.1602 0.1543 0.0065  0.0001  0.0032  121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1509 0.1580 0.1502 0.0075  -0.0003 0.0021  121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1465 0.1502 0.1422 0.0086  0.0000  0.0038  121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.1667 0.1734 0.1626 0.0095  -0.0015 0.0020  121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1634 0.1646 0.1560 0.0104  0.0008  0.0052  121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1548 0.1599 0.1570 0.0045  -0.0006 0.0033  122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1590 0.1653 0.1634 0.0034  -0.0016 0.0024  122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1374 0.1423 0.1429 0.0017  -0.0026 0.0029  122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1518 0.1548 0.1566 0.0012  -0.0027 0.0035  122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1435 0.1488 0.1501 0.0008  -0.0034 0.0025  123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1403 0.1437 0.1465 -0.0004 -0.0046 0.0030  123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1417 0.1450 0.1466 -0.0007 -0.0046 0.0029  123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1444 0.1493 0.1509 -0.0007 -0.0041 0.0024  123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.1510 0.1543 0.1605 -0.0010 -0.0058 0.0035  123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.1600 0.1648 0.1718 -0.0006 -0.0054 0.0031  123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.1743 0.1775 0.1863 -0.0012 -0.0058 0.0041  123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.1789 0.1834 0.1945 -0.0010 -0.0067 0.0037  123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1407 0.1415 0.1423 -0.0011 -0.0050 0.0034  124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1371 0.1375 0.1371 -0.0013 -0.0040 0.0038  124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1346 0.1350 0.1371 -0.0021 -0.0045 0.0045  124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1448 0.1440 0.1480 -0.0023 -0.0063 0.0049  124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1388 0.1356 0.1333 -0.0011 -0.0043 0.0043  124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1645 0.1603 0.1567 -0.0012 -0.0026 0.0054  124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1528 0.1489 0.1448 -0.0002 -0.0037 0.0035  124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1260 0.1277 0.1306 -0.0025 -0.0032 0.0045  125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1361 0.1372 0.1435 -0.0033 -0.0036 0.0050  125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1685 0.1685 0.1756 -0.0041 -0.0018 0.0065  125 SER   C C   
2001 O O   . SER   B 119 ? 0.1683 0.1659 0.1758 -0.0047 -0.0021 0.0078  125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1425 0.1462 0.1544 -0.0031 -0.0040 0.0033  125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1431 0.1457 0.1580 -0.0038 -0.0045 0.0034  125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1638 0.1653 0.1707 -0.0040 0.0003  0.0065  126 THR   C N   
2005 C CA  . THR   B 120 ? 0.1793 0.1801 0.1869 -0.0049 0.0030  0.0083  126 THR   C CA  
2006 C C   . THR   B 120 ? 0.1808 0.1824 0.1856 -0.0040 0.0056  0.0085  126 THR   C C   
2007 O O   . THR   B 120 ? 0.1753 0.1777 0.1778 -0.0028 0.0048  0.0072  126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2098 0.2129 0.2251 -0.0063 0.0034  0.0077  126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2399 0.2415 0.2564 -0.0074 0.0063  0.0101  126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2246 0.2325 0.2446 -0.0059 0.0033  0.0055  126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.1934 0.1945 0.1983 -0.0044 0.0090  0.0104  127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2193 0.2214 0.2219 -0.0032 0.0121  0.0106  127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2472 0.2482 0.2499 -0.0037 0.0165  0.0134  127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2320 0.2312 0.2366 -0.0052 0.0171  0.0152  127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.2938 0.2953 0.2939 -0.0023 0.0200  0.0138  128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.3191 0.3199 0.3192 -0.0024 0.0256  0.0167  128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.3189 0.3256 0.3269 -0.0021 0.0291  0.0160  128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.3107 0.3219 0.3251 -0.0021 0.0265  0.0134  128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.3223 0.3290 0.3304 -0.0017 0.0351  0.0186  129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.3150 0.3276 0.3313 -0.0010 0.0391  0.0182  129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.2858 0.3002 0.2997 0.0017  0.0372  0.0151  129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.2876 0.3082 0.3111 0.0019  0.0376  0.0137  129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3398 0.3588 0.3717 -0.0038 0.0383  0.0178  129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.3963 0.4148 0.4340 -0.0064 0.0422  0.0212  129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4243 0.4386 0.4552 -0.0057 0.0473  0.0246  129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4025 0.4252 0.4530 -0.0091 0.0402  0.0203  129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2586 0.2676 0.2606 0.0036  0.0347  0.0140  130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2394 0.2491 0.2392 0.0059  0.0328  0.0112  130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.1994 0.2123 0.2050 0.0051  0.0273  0.0087  130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2005 0.2151 0.2071 0.0069  0.0262  0.0068  130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.1846 0.1978 0.1937 0.0027  0.0242  0.0089  131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.1930 0.2086 0.2063 0.0020  0.0193  0.0068  131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2223 0.2331 0.2291 0.0013  0.0157  0.0067  131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2779 0.2851 0.2808 0.0003  0.0163  0.0084  131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2106 0.2312 0.2350 0.0000  0.0187  0.0066  131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2367 0.2629 0.2704 0.0003  0.0219  0.0068  131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2675 0.2973 0.3121 -0.0025 0.0219  0.0072  131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2300 0.2600 0.2666 0.0026  0.0199  0.0045  131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1684 0.1794 0.1748 0.0018  0.0121  0.0049  132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1723 0.1801 0.1748 0.0010  0.0088  0.0047  132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1588 0.1697 0.1673 0.0003  0.0062  0.0035  132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1547 0.1689 0.1667 0.0013  0.0056  0.0022  132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.1917 0.1958 0.1875 0.0024  0.0074  0.0040  132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2363 0.2421 0.2331 0.0041  0.0074  0.0026  132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.1738 0.1753 0.1675 0.0015  0.0041  0.0039  132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1452 0.1548 0.1542 -0.0011 0.0046  0.0038  133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1497 0.1615 0.1631 -0.0014 0.0023  0.0024  133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1468 0.1565 0.1569 -0.0011 0.0002  0.0021  133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1582 0.1648 0.1652 -0.0016 -0.0002 0.0031  133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1283 0.1396 0.1392 0.0000  -0.0012 0.0007  134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1324 0.1421 0.1409 0.0005  -0.0023 0.0007  134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1363 0.1472 0.1471 0.0007  -0.0035 -0.0005 134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1419 0.1549 0.1545 0.0015  -0.0042 -0.0020 134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1431 0.1527 0.1491 0.0020  -0.0022 0.0005  134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1411 0.1492 0.1445 0.0023  -0.0011 0.0011  134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1428 0.1475 0.1430 0.0019  -0.0014 0.0018  134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1556 0.1656 0.1601 0.0033  -0.0001 0.0006  134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1554 0.1580 0.1522 0.0025  -0.0006 0.0018  134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.1722 0.1805 0.1738 0.0041  0.0012  0.0009  134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1723 0.1765 0.1695 0.0037  0.0010  0.0014  134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1297 0.1391 0.1403 0.0004  -0.0040 -0.0002 135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1300 0.1398 0.1417 0.0011  -0.0047 -0.0014 135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1324 0.1425 0.1413 0.0029  -0.0042 -0.0015 135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1401 0.1490 0.1479 0.0029  -0.0034 -0.0002 135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1360 0.1441 0.1489 0.0005  -0.0049 -0.0008 135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1277 0.1389 0.1355 0.0045  -0.0049 -0.0031 136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1277 0.1385 0.1317 0.0066  -0.0042 -0.0028 136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1390 0.1486 0.1420 0.0073  -0.0029 -0.0025 136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1420 0.1515 0.1468 0.0072  -0.0034 -0.0036 136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1537 0.1656 0.1559 0.0085  -0.0060 -0.0049 136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2160 0.2269 0.2128 0.0112  -0.0054 -0.0042 136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2080 0.2181 0.2035 0.0113  -0.0041 -0.0023 136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2507 0.2609 0.2440 0.0133  -0.0061 -0.0056 136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1393 0.1480 0.1401 0.0082  -0.0010 -0.0008 137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1494 0.1575 0.1498 0.0093  0.0012  -0.0001 137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.1521 0.1591 0.1469 0.0121  0.0028  0.0005  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.1691 0.1754 0.1627 0.0134  0.0055  0.0013  137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1634 0.1714 0.1682 0.0076  0.0027  0.0020  137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.1653 0.1738 0.1743 0.0055  0.0007  0.0015  137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.1656 0.1726 0.1699 0.0070  0.0034  0.0039  137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.1478 0.1545 0.1389 0.0133  0.0015  0.0002  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1531 0.1580 0.1379 0.0161  0.0030  0.0015  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.1760 0.1799 0.1552 0.0191  0.0032  -0.0002 138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.1910 0.1928 0.1642 0.0217  0.0056  0.0014  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1520 0.1567 0.1345 0.0169  0.0010  0.0015  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.1569 0.1613 0.1430 0.0148  0.0016  0.0032  138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.1559 0.1604 0.1404 0.0161  -0.0004 0.0028  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1475 0.1550 0.1350 0.0155  -0.0033 0.0002  138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.1514 0.1604 0.1400 0.0163  -0.0052 -0.0006 138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.1550 0.1624 0.1407 0.0181  -0.0049 0.0008  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.1592 0.1713 0.1523 0.0152  -0.0072 -0.0027 138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.1693 0.1742 0.1499 0.0189  0.0006  -0.0033 139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.1873 0.1907 0.1621 0.0219  0.0003  -0.0055 139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.1962 0.1988 0.1715 0.0224  0.0039  -0.0050 139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2223 0.2230 0.1913 0.0256  0.0046  -0.0066 139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.1902 0.1945 0.1668 0.0215  -0.0042 -0.0094 139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2185 0.2241 0.2031 0.0183  -0.0047 -0.0102 139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2203 0.2272 0.2100 0.0156  -0.0035 -0.0079 139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2504 0.2552 0.2357 0.0186  -0.0064 -0.0131 139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.1740 0.1780 0.1563 0.0198  0.0061  -0.0029 140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.1864 0.1905 0.1713 0.0203  0.0094  -0.0024 140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.1798 0.1831 0.1619 0.0220  0.0142  0.0007  140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.1900 0.1945 0.1779 0.0200  0.0167  0.0036  140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.1895 0.1956 0.1837 0.0168  0.0087  -0.0016 140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2038 0.2104 0.2009 0.0149  0.0045  -0.0040 140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2016 0.2095 0.2063 0.0119  0.0040  -0.0026 140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.1974 0.2027 0.1926 0.0166  0.0032  -0.0072 140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.1776 0.1784 0.1502 0.0258  0.0157  0.0002  141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2034 0.2026 0.1718 0.0278  0.0209  0.0038  141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2239 0.2244 0.1979 0.0277  0.0262  0.0058  141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2341 0.2345 0.2098 0.0275  0.0308  0.0096  141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2173 0.2128 0.1727 0.0324  0.0212  0.0030  141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2221 0.2167 0.1722 0.0333  0.0153  0.0004  141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2543 0.2449 0.1909 0.0384  0.0155  -0.0001 141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2377 0.2335 0.1923 0.0305  0.0133  0.0023  141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2153 0.2170 0.1927 0.0279  0.0258  0.0032  142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2245 0.2280 0.2082 0.0282  0.0307  0.0047  142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2296 0.2366 0.2259 0.0241  0.0313  0.0075  142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2304 0.2395 0.2336 0.0242  0.0357  0.0095  142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2167 0.2202 0.2010 0.0298  0.0294  0.0010  142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2120 0.2164 0.2015 0.0268  0.0232  -0.0017 142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2194 0.2221 0.2042 0.0268  0.0182  -0.0050 142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2082 0.2155 0.2088 0.0234  0.0217  -0.0009 142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2182 0.2222 0.2104 0.0236  0.0144  -0.0059 142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2049 0.2115 0.2060 0.0217  0.0164  -0.0035 142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2028 0.2132 0.2134 0.0218  0.0243  0.0017  142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2208 0.2291 0.2302 0.0187  0.0137  -0.0032 142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2141 0.2263 0.2330 0.0189  0.0208  0.0015  142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2114 0.2222 0.2290 0.0177  0.0158  -0.0008 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2229 0.2304 0.2224 0.0208  0.0269  0.0076  143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2363 0.2463 0.2465 0.0171  0.0267  0.0098  143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.2879 0.2978 0.3003 0.0170  0.0318  0.0138  143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.2921 0.3044 0.3150 0.0145  0.0328  0.0156  143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2129 0.2225 0.2237 0.0142  0.0215  0.0090  143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2156 0.2257 0.2275 0.0132  0.0167  0.0060  143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2141 0.2235 0.2250 0.0109  0.0128  0.0057  143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2151 0.2276 0.2363 0.0118  0.0163  0.0061  143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3170 0.3238 0.3198 0.0195  0.0345  0.0152  144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.3735 0.3788 0.3760 0.0198  0.0397  0.0194  144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4138 0.4198 0.4175 0.0222  0.0468  0.0217  144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4281 0.4326 0.4315 0.0225  0.0519  0.0256  144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4126 0.4135 0.4028 0.0223  0.0394  0.0201  144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.4849 0.4848 0.4739 0.0203  0.0338  0.0190  144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.5108 0.5123 0.5084 0.0167  0.0314  0.0190  144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5267 0.5239 0.5057 0.0228  0.0318  0.0181  144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4237 0.4314 0.4276 0.0242  0.0476  0.0194  145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.4602 0.4689 0.4656 0.0269  0.0551  0.0214  145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.4780 0.4914 0.4954 0.0259  0.0551  0.0199  145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.4981 0.5138 0.5214 0.0273  0.0615  0.0221  145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5138 0.5185 0.5038 0.0323  0.0579  0.0203  145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.5796 0.5824 0.5612 0.0339  0.0515  0.0151  145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7070 0.7052 0.6747 0.0361  0.0488  0.0144  145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.7357 0.7312 0.6931 0.0394  0.0463  0.0107  145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.7546 0.7516 0.7218 0.0346  0.0490  0.0175  145 GLU   C OE2 
2155 N N1  . A1BO1 C .   ? 0.2209 0.2282 0.2594 0.0010  0.0216  -0.0185 201 A1BO1 A N1  
2156 C C4  . A1BO1 C .   ? 0.2378 0.2470 0.2464 -0.0031 0.0122  -0.0140 201 A1BO1 A C4  
2157 C C5  . A1BO1 C .   ? 0.2472 0.2555 0.2609 -0.0028 0.0159  -0.0166 201 A1BO1 A C5  
2158 C C6  . A1BO1 C .   ? 0.2469 0.2542 0.2613 -0.0038 0.0210  -0.0189 201 A1BO1 A C6  
2159 C C7  . A1BO1 C .   ? 0.2509 0.2567 0.2725 -0.0035 0.0263  -0.0220 201 A1BO1 A C7  
2160 C C8  . A1BO1 C .   ? 0.2460 0.2544 0.2817 0.0003  0.0228  -0.0182 201 A1BO1 A C8  
2161 C C10 . A1BO1 C .   ? 0.2246 0.2300 0.2535 -0.0004 0.0150  -0.0197 201 A1BO1 A C10 
2162 C C13 . A1BO1 C .   ? 0.1821 0.1946 0.2300 0.0042  0.0126  -0.0072 201 A1BO1 A C13 
2163 O O1  . A1BO1 C .   ? 0.1937 0.2062 0.2506 0.0055  0.0144  -0.0059 201 A1BO1 A O1  
2164 N N2  . A1BO1 C .   ? 0.1729 0.1868 0.2160 0.0035  0.0092  -0.0045 201 A1BO1 A N2  
2165 C C12 . A1BO1 C .   ? 0.1852 0.1957 0.2265 0.0029  0.0144  -0.0119 201 A1BO1 A C12 
2166 C C11 . A1BO1 C .   ? 0.2054 0.2130 0.2423 0.0018  0.0138  -0.0155 201 A1BO1 A C11 
2167 C C9  . A1BO1 C .   ? 0.2296 0.2337 0.2616 -0.0008 0.0205  -0.0222 201 A1BO1 A C9  
2168 C C14 . A1BO1 C .   ? 0.2047 0.2146 0.2519 0.0032  0.0194  -0.0139 201 A1BO1 A C14 
2169 O O   . A1BO1 C .   ? 0.2470 0.2590 0.2877 0.0014  0.0219  -0.0144 201 A1BO1 A O   
2170 N N   . A1BO1 C .   ? 0.2479 0.2532 0.2747 -0.0022 0.0251  -0.0223 201 A1BO1 A N   
2171 C C1  . A1BO1 C .   ? 0.2502 0.2575 0.2591 -0.0052 0.0219  -0.0184 201 A1BO1 A C1  
2172 C C   . A1BO1 C .   ? 0.2613 0.2670 0.2701 -0.0068 0.0282  -0.0212 201 A1BO1 A C   
2173 C C3  . A1BO1 C .   ? 0.2461 0.2552 0.2499 -0.0042 0.0130  -0.0133 201 A1BO1 A C3  
2174 C C2  . A1BO1 C .   ? 0.2453 0.2536 0.2490 -0.0053 0.0176  -0.0154 201 A1BO1 A C2  
2176 N N1  . A1BO1 E .   ? 0.2207 0.2072 0.2248 -0.0070 0.0034  0.0167  201 A1BO1 C N1  
2177 C C4  . A1BO1 E .   ? 0.2439 0.2340 0.2319 -0.0026 0.0028  0.0119  201 A1BO1 C C4  
2178 C C5  . A1BO1 E .   ? 0.2528 0.2412 0.2419 -0.0035 0.0043  0.0141  201 A1BO1 C C5  
2179 C C6  . A1BO1 E .   ? 0.2416 0.2285 0.2280 -0.0034 0.0084  0.0164  201 A1BO1 C C6  
2180 C C7  . A1BO1 E .   ? 0.2458 0.2303 0.2338 -0.0045 0.0105  0.0194  201 A1BO1 C C7  
2181 C C8  . A1BO1 E .   ? 0.2408 0.2286 0.2421 -0.0067 0.0064  0.0171  201 A1BO1 C C8  
2182 C C10 . A1BO1 E .   ? 0.2311 0.2157 0.2324 -0.0051 -0.0031 0.0153  201 A1BO1 C C10 
2183 C C13 . A1BO1 E .   ? 0.1804 0.1752 0.1993 -0.0073 -0.0020 0.0087  201 A1BO1 C C13 
2184 O O1  . A1BO1 E .   ? 0.1631 0.1569 0.1868 -0.0084 -0.0019 0.0087  201 A1BO1 C O1  
2185 N N2  . A1BO1 E .   ? 0.1683 0.1663 0.1871 -0.0064 -0.0030 0.0065  201 A1BO1 C N2  
2186 C C12 . A1BO1 E .   ? 0.1921 0.1840 0.2044 -0.0068 -0.0010 0.0115  201 A1BO1 C C12 
2187 C C11 . A1BO1 E .   ? 0.2275 0.2158 0.2366 -0.0058 -0.0034 0.0127  201 A1BO1 C C11 
2188 C C9  . A1BO1 E .   ? 0.2230 0.2053 0.2226 -0.0059 0.0006  0.0180  201 A1BO1 C C9  
2189 C C14 . A1BO1 E .   ? 0.2108 0.2010 0.2233 -0.0080 0.0023  0.0141  201 A1BO1 C C14 
2190 O O   . A1BO1 E .   ? 0.2515 0.2437 0.2578 -0.0073 0.0078  0.0155  201 A1BO1 C O   
2191 N N   . A1BO1 E .   ? 0.2471 0.2308 0.2395 -0.0054 0.0075  0.0193  201 A1BO1 C N   
2192 C C1  . A1BO1 E .   ? 0.2596 0.2469 0.2418 -0.0021 0.0110  0.0160  201 A1BO1 C C1  
2193 C C   . A1BO1 E .   ? 0.2790 0.2643 0.2573 -0.0016 0.0162  0.0187  201 A1BO1 C C   
2194 C C3  . A1BO1 E .   ? 0.2457 0.2358 0.2297 -0.0015 0.0049  0.0115  201 A1BO1 C C3  
2195 C C2  . A1BO1 E .   ? 0.2532 0.2420 0.2342 -0.0011 0.0090  0.0134  201 A1BO1 C C2  
# 
