data_7I32
# 
_entry.id   7I32 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I32         pdb_00007i32 10.2210/pdb7i32/pdb 
WWPDB D_1001408253 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I32 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                           15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn 'N-[2-(1,3-oxazol-4-yl)ethyl]benzamide' 216.236   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                              65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                    78.133    2   ?         ? ? ? 
5 water       nat water                                   18.015    371 ?         ? ? ? 
# 
_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 'N-[2-(1,3-oxazol-4-yl)ethyl]benzamide' A1B04 
3 'ZINC ION'                              ZN    
4 'DIMETHYL SULFOXIDE'                    DMS   
5 water                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B04 non-polymer         . 'N-[2-(1,3-oxazol-4-yl)ethyl]benzamide' ? 'C12 H12 N2 O2'  216.236 
ALA   'L-peptide linking' y ALANINE                                 ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                              ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                         ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                    ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                               ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                         ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                 ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                               ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                   ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                              ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                 ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                  ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                              ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                           ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                 ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                  ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                               ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                              ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                  ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                              ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B04 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B04 
_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 A1B04 1   201 201 A1B04 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 106 HOH   HOH A . 
H 5 HOH   2   302 359 HOH   HOH A . 
H 5 HOH   3   303 352 HOH   HOH A . 
H 5 HOH   4   304 225 HOH   HOH A . 
H 5 HOH   5   305 217 HOH   HOH A . 
H 5 HOH   6   306 63  HOH   HOH A . 
H 5 HOH   7   307 213 HOH   HOH A . 
H 5 HOH   8   308 346 HOH   HOH A . 
H 5 HOH   9   309 255 HOH   HOH A . 
H 5 HOH   10  310 135 HOH   HOH A . 
H 5 HOH   11  311 309 HOH   HOH A . 
H 5 HOH   12  312 231 HOH   HOH A . 
H 5 HOH   13  313 160 HOH   HOH A . 
H 5 HOH   14  314 258 HOH   HOH A . 
H 5 HOH   15  315 249 HOH   HOH A . 
H 5 HOH   16  316 203 HOH   HOH A . 
H 5 HOH   17  317 112 HOH   HOH A . 
H 5 HOH   18  318 248 HOH   HOH A . 
H 5 HOH   19  319 111 HOH   HOH A . 
H 5 HOH   20  320 321 HOH   HOH A . 
H 5 HOH   21  321 97  HOH   HOH A . 
H 5 HOH   22  322 122 HOH   HOH A . 
H 5 HOH   23  323 123 HOH   HOH A . 
H 5 HOH   24  324 157 HOH   HOH A . 
H 5 HOH   25  325 282 HOH   HOH A . 
H 5 HOH   26  326 130 HOH   HOH A . 
H 5 HOH   27  327 201 HOH   HOH A . 
H 5 HOH   28  328 17  HOH   HOH A . 
H 5 HOH   29  329 4   HOH   HOH A . 
H 5 HOH   30  330 89  HOH   HOH A . 
H 5 HOH   31  331 84  HOH   HOH A . 
H 5 HOH   32  332 292 HOH   HOH A . 
H 5 HOH   33  333 136 HOH   HOH A . 
H 5 HOH   34  334 296 HOH   HOH A . 
H 5 HOH   35  335 85  HOH   HOH A . 
H 5 HOH   36  336 350 HOH   HOH A . 
H 5 HOH   37  337 263 HOH   HOH A . 
H 5 HOH   38  338 262 HOH   HOH A . 
H 5 HOH   39  339 266 HOH   HOH A . 
H 5 HOH   40  340 60  HOH   HOH A . 
H 5 HOH   41  341 8   HOH   HOH A . 
H 5 HOH   42  342 15  HOH   HOH A . 
H 5 HOH   43  343 35  HOH   HOH A . 
H 5 HOH   44  344 82  HOH   HOH A . 
H 5 HOH   45  345 83  HOH   HOH A . 
H 5 HOH   46  346 170 HOH   HOH A . 
H 5 HOH   47  347 57  HOH   HOH A . 
H 5 HOH   48  348 185 HOH   HOH A . 
H 5 HOH   49  349 20  HOH   HOH A . 
H 5 HOH   50  350 102 HOH   HOH A . 
H 5 HOH   51  351 164 HOH   HOH A . 
H 5 HOH   52  352 68  HOH   HOH A . 
H 5 HOH   53  353 337 HOH   HOH A . 
H 5 HOH   54  354 354 HOH   HOH A . 
H 5 HOH   55  355 206 HOH   HOH A . 
H 5 HOH   56  356 28  HOH   HOH A . 
H 5 HOH   57  357 361 HOH   HOH A . 
H 5 HOH   58  358 75  HOH   HOH A . 
H 5 HOH   59  359 110 HOH   HOH A . 
H 5 HOH   60  360 91  HOH   HOH A . 
H 5 HOH   61  361 165 HOH   HOH A . 
H 5 HOH   62  362 200 HOH   HOH A . 
H 5 HOH   63  363 186 HOH   HOH A . 
H 5 HOH   64  364 1   HOH   HOH A . 
H 5 HOH   65  365 210 HOH   HOH A . 
H 5 HOH   66  366 24  HOH   HOH A . 
H 5 HOH   67  367 283 HOH   HOH A . 
H 5 HOH   68  368 211 HOH   HOH A . 
H 5 HOH   69  369 298 HOH   HOH A . 
H 5 HOH   70  370 336 HOH   HOH A . 
H 5 HOH   71  371 351 HOH   HOH A . 
H 5 HOH   72  372 161 HOH   HOH A . 
H 5 HOH   73  373 166 HOH   HOH A . 
H 5 HOH   74  374 371 HOH   HOH A . 
H 5 HOH   75  375 12  HOH   HOH A . 
H 5 HOH   76  376 145 HOH   HOH A . 
H 5 HOH   77  377 257 HOH   HOH A . 
H 5 HOH   78  378 271 HOH   HOH A . 
H 5 HOH   79  379 159 HOH   HOH A . 
H 5 HOH   80  380 241 HOH   HOH A . 
H 5 HOH   81  381 43  HOH   HOH A . 
H 5 HOH   82  382 199 HOH   HOH A . 
H 5 HOH   83  383 223 HOH   HOH A . 
H 5 HOH   84  384 33  HOH   HOH A . 
H 5 HOH   85  385 227 HOH   HOH A . 
H 5 HOH   86  386 99  HOH   HOH A . 
H 5 HOH   87  387 76  HOH   HOH A . 
H 5 HOH   88  388 27  HOH   HOH A . 
H 5 HOH   89  389 140 HOH   HOH A . 
H 5 HOH   90  390 356 HOH   HOH A . 
H 5 HOH   91  391 32  HOH   HOH A . 
H 5 HOH   92  392 52  HOH   HOH A . 
H 5 HOH   93  393 156 HOH   HOH A . 
H 5 HOH   94  394 267 HOH   HOH A . 
H 5 HOH   95  395 150 HOH   HOH A . 
H 5 HOH   96  396 261 HOH   HOH A . 
H 5 HOH   97  397 96  HOH   HOH A . 
H 5 HOH   98  398 116 HOH   HOH A . 
H 5 HOH   99  399 220 HOH   HOH A . 
H 5 HOH   100 400 293 HOH   HOH A . 
H 5 HOH   101 401 87  HOH   HOH A . 
H 5 HOH   102 402 46  HOH   HOH A . 
H 5 HOH   103 403 117 HOH   HOH A . 
H 5 HOH   104 404 51  HOH   HOH A . 
H 5 HOH   105 405 58  HOH   HOH A . 
H 5 HOH   106 406 236 HOH   HOH A . 
H 5 HOH   107 407 148 HOH   HOH A . 
H 5 HOH   108 408 113 HOH   HOH A . 
H 5 HOH   109 409 45  HOH   HOH A . 
H 5 HOH   110 410 316 HOH   HOH A . 
H 5 HOH   111 411 252 HOH   HOH A . 
H 5 HOH   112 412 270 HOH   HOH A . 
H 5 HOH   113 413 341 HOH   HOH A . 
H 5 HOH   114 414 67  HOH   HOH A . 
H 5 HOH   115 415 14  HOH   HOH A . 
H 5 HOH   116 416 6   HOH   HOH A . 
H 5 HOH   117 417 162 HOH   HOH A . 
H 5 HOH   118 418 125 HOH   HOH A . 
H 5 HOH   119 419 357 HOH   HOH A . 
H 5 HOH   120 420 54  HOH   HOH A . 
H 5 HOH   121 421 187 HOH   HOH A . 
H 5 HOH   122 422 189 HOH   HOH A . 
H 5 HOH   123 423 98  HOH   HOH A . 
H 5 HOH   124 424 259 HOH   HOH A . 
H 5 HOH   125 425 284 HOH   HOH A . 
H 5 HOH   126 426 193 HOH   HOH A . 
H 5 HOH   127 427 238 HOH   HOH A . 
H 5 HOH   128 428 80  HOH   HOH A . 
H 5 HOH   129 429 36  HOH   HOH A . 
H 5 HOH   130 430 268 HOH   HOH A . 
H 5 HOH   131 431 29  HOH   HOH A . 
H 5 HOH   132 432 237 HOH   HOH A . 
H 5 HOH   133 433 347 HOH   HOH A . 
H 5 HOH   134 434 59  HOH   HOH A . 
H 5 HOH   135 435 365 HOH   HOH A . 
H 5 HOH   136 436 180 HOH   HOH A . 
H 5 HOH   137 437 339 HOH   HOH A . 
H 5 HOH   138 438 286 HOH   HOH A . 
H 5 HOH   139 439 9   HOH   HOH A . 
H 5 HOH   140 440 127 HOH   HOH A . 
H 5 HOH   141 441 115 HOH   HOH A . 
H 5 HOH   142 442 205 HOH   HOH A . 
H 5 HOH   143 443 40  HOH   HOH A . 
H 5 HOH   144 444 3   HOH   HOH A . 
H 5 HOH   145 445 328 HOH   HOH A . 
H 5 HOH   146 446 222 HOH   HOH A . 
H 5 HOH   147 447 173 HOH   HOH A . 
H 5 HOH   148 448 327 HOH   HOH A . 
H 5 HOH   149 449 273 HOH   HOH A . 
H 5 HOH   150 450 313 HOH   HOH A . 
H 5 HOH   151 451 353 HOH   HOH A . 
H 5 HOH   152 452 254 HOH   HOH A . 
H 5 HOH   153 453 229 HOH   HOH A . 
H 5 HOH   154 454 275 HOH   HOH A . 
H 5 HOH   155 455 318 HOH   HOH A . 
H 5 HOH   156 456 324 HOH   HOH A . 
H 5 HOH   157 457 335 HOH   HOH A . 
H 5 HOH   158 458 305 HOH   HOH A . 
H 5 HOH   159 459 372 HOH   HOH A . 
H 5 HOH   160 460 334 HOH   HOH A . 
H 5 HOH   161 461 310 HOH   HOH A . 
H 5 HOH   162 462 303 HOH   HOH A . 
H 5 HOH   163 463 233 HOH   HOH A . 
H 5 HOH   164 464 317 HOH   HOH A . 
H 5 HOH   165 465 375 HOH   HOH A . 
H 5 HOH   166 466 320 HOH   HOH A . 
H 5 HOH   167 467 178 HOH   HOH A . 
H 5 HOH   168 468 174 HOH   HOH A . 
H 5 HOH   169 469 325 HOH   HOH A . 
H 5 HOH   170 470 197 HOH   HOH A . 
H 5 HOH   171 471 302 HOH   HOH A . 
H 5 HOH   172 472 212 HOH   HOH A . 
H 5 HOH   173 473 107 HOH   HOH A . 
H 5 HOH   174 474 167 HOH   HOH A . 
H 5 HOH   175 475 345 HOH   HOH A . 
H 5 HOH   176 476 319 HOH   HOH A . 
H 5 HOH   177 477 114 HOH   HOH A . 
H 5 HOH   178 478 348 HOH   HOH A . 
H 5 HOH   179 479 272 HOH   HOH A . 
H 5 HOH   180 480 269 HOH   HOH A . 
H 5 HOH   181 481 370 HOH   HOH A . 
H 5 HOH   182 482 332 HOH   HOH A . 
H 5 HOH   183 483 288 HOH   HOH A . 
H 5 HOH   184 484 253 HOH   HOH A . 
H 5 HOH   185 485 306 HOH   HOH A . 
I 5 HOH   1   301 279 HOH   HOH C . 
I 5 HOH   2   302 228 HOH   HOH C . 
I 5 HOH   3   303 364 HOH   HOH C . 
I 5 HOH   4   304 139 HOH   HOH C . 
I 5 HOH   5   305 342 HOH   HOH C . 
I 5 HOH   6   306 90  HOH   HOH C . 
I 5 HOH   7   307 373 HOH   HOH C . 
I 5 HOH   8   308 311 HOH   HOH C . 
I 5 HOH   9   309 215 HOH   HOH C . 
I 5 HOH   10  310 218 HOH   HOH C . 
I 5 HOH   11  311 265 HOH   HOH C . 
I 5 HOH   12  312 95  HOH   HOH C . 
I 5 HOH   13  313 71  HOH   HOH C . 
I 5 HOH   14  314 260 HOH   HOH C . 
I 5 HOH   15  315 128 HOH   HOH C . 
I 5 HOH   16  316 53  HOH   HOH C . 
I 5 HOH   17  317 119 HOH   HOH C . 
I 5 HOH   18  318 126 HOH   HOH C . 
I 5 HOH   19  319 276 HOH   HOH C . 
I 5 HOH   20  320 295 HOH   HOH C . 
I 5 HOH   21  321 340 HOH   HOH C . 
I 5 HOH   22  322 120 HOH   HOH C . 
I 5 HOH   23  323 301 HOH   HOH C . 
I 5 HOH   24  324 7   HOH   HOH C . 
I 5 HOH   25  325 37  HOH   HOH C . 
I 5 HOH   26  326 214 HOH   HOH C . 
I 5 HOH   27  327 79  HOH   HOH C . 
I 5 HOH   28  328 121 HOH   HOH C . 
I 5 HOH   29  329 22  HOH   HOH C . 
I 5 HOH   30  330 55  HOH   HOH C . 
I 5 HOH   31  331 323 HOH   HOH C . 
I 5 HOH   32  332 147 HOH   HOH C . 
I 5 HOH   33  333 132 HOH   HOH C . 
I 5 HOH   34  334 61  HOH   HOH C . 
I 5 HOH   35  335 30  HOH   HOH C . 
I 5 HOH   36  336 204 HOH   HOH C . 
I 5 HOH   37  337 2   HOH   HOH C . 
I 5 HOH   38  338 5   HOH   HOH C . 
I 5 HOH   39  339 81  HOH   HOH C . 
I 5 HOH   40  340 219 HOH   HOH C . 
I 5 HOH   41  341 281 HOH   HOH C . 
I 5 HOH   42  342 338 HOH   HOH C . 
I 5 HOH   43  343 169 HOH   HOH C . 
I 5 HOH   44  344 294 HOH   HOH C . 
I 5 HOH   45  345 18  HOH   HOH C . 
I 5 HOH   46  346 49  HOH   HOH C . 
I 5 HOH   47  347 133 HOH   HOH C . 
I 5 HOH   48  348 176 HOH   HOH C . 
I 5 HOH   49  349 179 HOH   HOH C . 
I 5 HOH   50  350 100 HOH   HOH C . 
I 5 HOH   51  351 182 HOH   HOH C . 
I 5 HOH   52  352 144 HOH   HOH C . 
I 5 HOH   53  353 104 HOH   HOH C . 
I 5 HOH   54  354 278 HOH   HOH C . 
I 5 HOH   55  355 66  HOH   HOH C . 
I 5 HOH   56  356 47  HOH   HOH C . 
I 5 HOH   57  357 11  HOH   HOH C . 
I 5 HOH   58  358 101 HOH   HOH C . 
I 5 HOH   59  359 163 HOH   HOH C . 
I 5 HOH   60  360 105 HOH   HOH C . 
I 5 HOH   61  361 208 HOH   HOH C . 
I 5 HOH   62  362 207 HOH   HOH C . 
I 5 HOH   63  363 153 HOH   HOH C . 
I 5 HOH   64  364 65  HOH   HOH C . 
I 5 HOH   65  365 62  HOH   HOH C . 
I 5 HOH   66  366 367 HOH   HOH C . 
I 5 HOH   67  367 232 HOH   HOH C . 
I 5 HOH   68  368 362 HOH   HOH C . 
I 5 HOH   69  369 191 HOH   HOH C . 
I 5 HOH   70  370 109 HOH   HOH C . 
I 5 HOH   71  371 280 HOH   HOH C . 
I 5 HOH   72  372 368 HOH   HOH C . 
I 5 HOH   73  373 230 HOH   HOH C . 
I 5 HOH   74  374 50  HOH   HOH C . 
I 5 HOH   75  375 134 HOH   HOH C . 
I 5 HOH   76  376 21  HOH   HOH C . 
I 5 HOH   77  377 343 HOH   HOH C . 
I 5 HOH   78  378 151 HOH   HOH C . 
I 5 HOH   79  379 44  HOH   HOH C . 
I 5 HOH   80  380 73  HOH   HOH C . 
I 5 HOH   81  381 168 HOH   HOH C . 
I 5 HOH   82  382 26  HOH   HOH C . 
I 5 HOH   83  383 41  HOH   HOH C . 
I 5 HOH   84  384 239 HOH   HOH C . 
I 5 HOH   85  385 172 HOH   HOH C . 
I 5 HOH   86  386 308 HOH   HOH C . 
I 5 HOH   87  387 158 HOH   HOH C . 
I 5 HOH   88  388 209 HOH   HOH C . 
I 5 HOH   89  389 34  HOH   HOH C . 
I 5 HOH   90  390 312 HOH   HOH C . 
I 5 HOH   91  391 304 HOH   HOH C . 
I 5 HOH   92  392 78  HOH   HOH C . 
I 5 HOH   93  393 23  HOH   HOH C . 
I 5 HOH   94  394 226 HOH   HOH C . 
I 5 HOH   95  395 88  HOH   HOH C . 
I 5 HOH   96  396 56  HOH   HOH C . 
I 5 HOH   97  397 198 HOH   HOH C . 
I 5 HOH   98  398 243 HOH   HOH C . 
I 5 HOH   99  399 146 HOH   HOH C . 
I 5 HOH   100 400 19  HOH   HOH C . 
I 5 HOH   101 401 129 HOH   HOH C . 
I 5 HOH   102 402 124 HOH   HOH C . 
I 5 HOH   103 403 16  HOH   HOH C . 
I 5 HOH   104 404 69  HOH   HOH C . 
I 5 HOH   105 405 314 HOH   HOH C . 
I 5 HOH   106 406 103 HOH   HOH C . 
I 5 HOH   107 407 138 HOH   HOH C . 
I 5 HOH   108 408 247 HOH   HOH C . 
I 5 HOH   109 409 42  HOH   HOH C . 
I 5 HOH   110 410 131 HOH   HOH C . 
I 5 HOH   111 411 221 HOH   HOH C . 
I 5 HOH   112 412 177 HOH   HOH C . 
I 5 HOH   113 413 48  HOH   HOH C . 
I 5 HOH   114 414 181 HOH   HOH C . 
I 5 HOH   115 415 92  HOH   HOH C . 
I 5 HOH   116 416 349 HOH   HOH C . 
I 5 HOH   117 417 118 HOH   HOH C . 
I 5 HOH   118 418 70  HOH   HOH C . 
I 5 HOH   119 419 74  HOH   HOH C . 
I 5 HOH   120 420 31  HOH   HOH C . 
I 5 HOH   121 421 344 HOH   HOH C . 
I 5 HOH   122 422 183 HOH   HOH C . 
I 5 HOH   123 423 329 HOH   HOH C . 
I 5 HOH   124 424 175 HOH   HOH C . 
I 5 HOH   125 425 315 HOH   HOH C . 
I 5 HOH   126 426 250 HOH   HOH C . 
I 5 HOH   127 427 72  HOH   HOH C . 
I 5 HOH   128 428 369 HOH   HOH C . 
I 5 HOH   129 429 202 HOH   HOH C . 
I 5 HOH   130 430 184 HOH   HOH C . 
I 5 HOH   131 431 38  HOH   HOH C . 
I 5 HOH   132 432 194 HOH   HOH C . 
I 5 HOH   133 433 152 HOH   HOH C . 
I 5 HOH   134 434 25  HOH   HOH C . 
I 5 HOH   135 435 77  HOH   HOH C . 
I 5 HOH   136 436 171 HOH   HOH C . 
I 5 HOH   137 437 64  HOH   HOH C . 
I 5 HOH   138 438 246 HOH   HOH C . 
I 5 HOH   139 439 245 HOH   HOH C . 
I 5 HOH   140 440 13  HOH   HOH C . 
I 5 HOH   141 441 190 HOH   HOH C . 
I 5 HOH   142 442 307 HOH   HOH C . 
I 5 HOH   143 443 108 HOH   HOH C . 
I 5 HOH   144 444 39  HOH   HOH C . 
I 5 HOH   145 445 93  HOH   HOH C . 
I 5 HOH   146 446 154 HOH   HOH C . 
I 5 HOH   147 447 242 HOH   HOH C . 
I 5 HOH   148 448 244 HOH   HOH C . 
I 5 HOH   149 449 143 HOH   HOH C . 
I 5 HOH   150 450 240 HOH   HOH C . 
I 5 HOH   151 451 141 HOH   HOH C . 
I 5 HOH   152 452 10  HOH   HOH C . 
I 5 HOH   153 453 322 HOH   HOH C . 
I 5 HOH   154 454 360 HOH   HOH C . 
I 5 HOH   155 455 291 HOH   HOH C . 
I 5 HOH   156 456 333 HOH   HOH C . 
I 5 HOH   157 457 366 HOH   HOH C . 
I 5 HOH   158 458 358 HOH   HOH C . 
I 5 HOH   159 459 285 HOH   HOH C . 
I 5 HOH   160 460 142 HOH   HOH C . 
I 5 HOH   161 461 86  HOH   HOH C . 
I 5 HOH   162 462 355 HOH   HOH C . 
I 5 HOH   163 463 277 HOH   HOH C . 
I 5 HOH   164 464 274 HOH   HOH C . 
I 5 HOH   165 465 289 HOH   HOH C . 
I 5 HOH   166 466 224 HOH   HOH C . 
I 5 HOH   167 467 195 HOH   HOH C . 
I 5 HOH   168 468 188 HOH   HOH C . 
I 5 HOH   169 469 155 HOH   HOH C . 
I 5 HOH   170 470 363 HOH   HOH C . 
I 5 HOH   171 471 149 HOH   HOH C . 
I 5 HOH   172 472 326 HOH   HOH C . 
I 5 HOH   173 473 137 HOH   HOH C . 
I 5 HOH   174 474 264 HOH   HOH C . 
I 5 HOH   175 475 196 HOH   HOH C . 
I 5 HOH   176 476 330 HOH   HOH C . 
I 5 HOH   177 477 256 HOH   HOH C . 
I 5 HOH   178 478 299 HOH   HOH C . 
I 5 HOH   179 479 216 HOH   HOH C . 
I 5 HOH   180 480 192 HOH   HOH C . 
I 5 HOH   181 481 331 HOH   HOH C . 
I 5 HOH   182 482 251 HOH   HOH C . 
I 5 HOH   183 483 374 HOH   HOH C . 
I 5 HOH   184 484 287 HOH   HOH C . 
I 5 HOH   185 485 300 HOH   HOH C . 
I 5 HOH   186 486 290 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           7I32 
_cell.length_a           86.651 
_cell.length_b           56.879 
_cell.length_c           64.919 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.69 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I32 
_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          7I32 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   50.96 
_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   2024-11-13 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92202 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I32 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.51 
_reflns.d_resolution_high            1.20 
_reflns.number_obs                   43045 
_reflns.percent_possible_obs         84.3 
_reflns.pdbx_Rmerge_I_obs            0.131 
_reflns.pdbx_netI_over_sigmaI        2.4 
_reflns.pdbx_redundancy              5.0 
_reflns.pdbx_Rrim_I_all              0.144 
_reflns.pdbx_Rpim_I_all              0.060 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_number_measured_all     213842 
_reflns.pdbx_chi_squared             0.44 
_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                  1.20 
_reflns_shell.d_res_low                   1.26 
_reflns_shell.number_measured_all         3952 
_reflns_shell.number_unique_obs           2452 
_reflns_shell.Rmerge_I_obs                1.000 
_reflns_shell.pdbx_chi_squared            0.19 
_reflns_shell.pdbx_redundancy             1.6 
_reflns_shell.percent_possible_obs        33.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             1.382 
_reflns_shell.pdbx_Rpim_I_all             0.949 
_reflns_shell.pdbx_CC_half                0.669 
_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                                 7I32 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     85424 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             16.53 
_refine.ls_d_res_high                            1.151 
_refine.ls_percent_reflns_obs                    76.9 
_refine.ls_R_factor_obs                          0.1738 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1731 
_refine.ls_R_factor_R_free                       0.1860 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.010 
_refine.ls_number_reflns_R_free                  4276 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.B_iso_mean                               16.65 
_refine.aniso_B[1][1]                            -0.56920 
_refine.aniso_B[2][2]                            0.45950 
_refine.aniso_B[3][3]                            0.10970 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.01370 
_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             0.040 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.041 
_refine.pdbx_overall_SU_R_Blow_DPI               0.043 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.043 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I32 
_refine_analyze.Luzzati_coordinate_error_obs    0.14 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             371 
_refine_hist.number_atoms_total               2563 
_refine_hist.d_res_high                       1.151 
_refine_hist.d_res_low                        16.53 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.014 ? 2.00  2287 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.15  ? 2.00  3121 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  769  '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  417  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2287 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.42  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           13.78 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  284  '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  2146 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1631 
_refine_ls_shell.R_factor_R_work                  0.2425 
_refine_ls_shell.percent_reflns_obs               12.54 
_refine_ls_shell.R_factor_R_free                  0.2559 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.56 
_refine_ls_shell.number_reflns_R_free             78 
_refine_ls_shell.number_reflns_all                1709 
_refine_ls_shell.R_factor_all                     0.2430 
# 
_struct.entry_id                  7I32 
_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-0032228-001 (A71EV2A-x3435)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I32 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I32 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I32 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
# 
_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_555 111.6 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.9 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.7 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.7 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.3 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 115.1 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.1 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.3 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.2 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.2 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I32 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O C HOH 405 ? ? O C HOH 435 ? ? 1.63 
2 1 O C HOH 301 ? ? O C HOH 412 ? ? 1.76 
3 1 O A HOH 382 ? ? O A HOH 390 ? ? 1.93 
4 1 O A HOH 304 ? ? O A HOH 336 ? ? 1.98 
5 1 O A HOH 354 ? ? O A HOH 421 ? ? 2.06 
6 1 O A HOH 418 ? ? O A HOH 475 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     144 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH2 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     69 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 125 ? ? -134.90 -32.17 
2 1 ASN C 14  ? ? -104.22 40.15  
# 
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 14.8879 8.1141   14.4301 -0.0170 -0.0137 0.0024 0.0046 0.0007  0.0069 1.4185 0.8051 0.4582 0.9052  
-0.5746 -0.3266 -0.0084 0.0550 0.1237 0.0227 0.0521 0.0319 -0.0085 -0.0404 -0.0437 
'X-RAY DIFFRACTION' 2 ? refined 25.8938 -20.0966 17.8148 -0.0157 -0.0120 0.0084 0.0054 -0.0009 0.0163 0.6574 0.9603 0.1338 -0.3902 
-0.1114 -0.0467 -0.0141 0.0136 0.1021 0.0410 0.0365 0.0045 0.0288  0.0057  -0.0224 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B04 N1   N  Y N 1   
A1B04 C4   C  Y N 2   
A1B04 C5   C  Y N 3   
A1B04 C6   C  Y N 4   
A1B04 C7   C  Y N 5   
A1B04 C8   C  Y N 6   
A1B04 C10  C  Y N 7   
A1B04 O    O  N N 8   
A1B04 C    C  N N 9   
A1B04 C11  C  Y N 10  
A1B04 C9   C  Y N 11  
A1B04 N    N  N N 12  
A1B04 C1   C  N N 13  
A1B04 C2   C  N N 14  
A1B04 C3   C  Y N 15  
A1B04 O1   O  Y N 16  
A1B04 H5   H  N N 17  
A1B04 H6   H  N N 18  
A1B04 H7   H  N N 19  
A1B04 H8   H  N N 20  
A1B04 H10  H  N N 21  
A1B04 H11  H  N N 22  
A1B04 H9   H  N N 23  
A1B04 H    H  N N 24  
A1B04 H1   H  N N 25  
A1B04 H2   H  N N 26  
A1B04 H3   H  N N 27  
A1B04 H4   H  N N 28  
ALA   N    N  N N 29  
ALA   CA   C  N S 30  
ALA   C    C  N N 31  
ALA   O    O  N N 32  
ALA   CB   C  N N 33  
ALA   OXT  O  N N 34  
ALA   H    H  N N 35  
ALA   H2   H  N N 36  
ALA   HA   H  N N 37  
ALA   HB1  H  N N 38  
ALA   HB2  H  N N 39  
ALA   HB3  H  N N 40  
ALA   HXT  H  N N 41  
ARG   N    N  N N 42  
ARG   CA   C  N S 43  
ARG   C    C  N N 44  
ARG   O    O  N N 45  
ARG   CB   C  N N 46  
ARG   CG   C  N N 47  
ARG   CD   C  N N 48  
ARG   NE   N  N N 49  
ARG   CZ   C  N N 50  
ARG   NH1  N  N N 51  
ARG   NH2  N  N N 52  
ARG   OXT  O  N N 53  
ARG   H    H  N N 54  
ARG   H2   H  N N 55  
ARG   HA   H  N N 56  
ARG   HB2  H  N N 57  
ARG   HB3  H  N N 58  
ARG   HG2  H  N N 59  
ARG   HG3  H  N N 60  
ARG   HD2  H  N N 61  
ARG   HD3  H  N N 62  
ARG   HE   H  N N 63  
ARG   HH11 H  N N 64  
ARG   HH12 H  N N 65  
ARG   HH21 H  N N 66  
ARG   HH22 H  N N 67  
ARG   HXT  H  N N 68  
ASN   N    N  N N 69  
ASN   CA   C  N S 70  
ASN   C    C  N N 71  
ASN   O    O  N N 72  
ASN   CB   C  N N 73  
ASN   CG   C  N N 74  
ASN   OD1  O  N N 75  
ASN   ND2  N  N N 76  
ASN   OXT  O  N N 77  
ASN   H    H  N N 78  
ASN   H2   H  N N 79  
ASN   HA   H  N N 80  
ASN   HB2  H  N N 81  
ASN   HB3  H  N N 82  
ASN   HD21 H  N N 83  
ASN   HD22 H  N N 84  
ASN   HXT  H  N N 85  
ASP   N    N  N N 86  
ASP   CA   C  N S 87  
ASP   C    C  N N 88  
ASP   O    O  N N 89  
ASP   CB   C  N N 90  
ASP   CG   C  N N 91  
ASP   OD1  O  N N 92  
ASP   OD2  O  N N 93  
ASP   OXT  O  N N 94  
ASP   H    H  N N 95  
ASP   H2   H  N N 96  
ASP   HA   H  N N 97  
ASP   HB2  H  N N 98  
ASP   HB3  H  N N 99  
ASP   HD2  H  N N 100 
ASP   HXT  H  N N 101 
CYS   N    N  N N 102 
CYS   CA   C  N R 103 
CYS   C    C  N N 104 
CYS   O    O  N N 105 
CYS   CB   C  N N 106 
CYS   SG   S  N N 107 
CYS   OXT  O  N N 108 
CYS   H    H  N N 109 
CYS   H2   H  N N 110 
CYS   HA   H  N N 111 
CYS   HB2  H  N N 112 
CYS   HB3  H  N N 113 
CYS   HG   H  N N 114 
CYS   HXT  H  N N 115 
DMS   S    S  N N 116 
DMS   O    O  N N 117 
DMS   C1   C  N N 118 
DMS   C2   C  N N 119 
DMS   H11  H  N N 120 
DMS   H12  H  N N 121 
DMS   H13  H  N N 122 
DMS   H21  H  N N 123 
DMS   H22  H  N N 124 
DMS   H23  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
ZN    ZN   ZN N N 429 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1B04 C   O    doub N N 1   
A1B04 N   C    sing N N 2   
A1B04 C1  N    sing N N 3   
A1B04 C2  C1   sing N N 4   
A1B04 C3  C2   sing N N 5   
A1B04 C3  C4   doub Y N 6   
A1B04 C4  O1   sing Y N 7   
A1B04 O1  C5   sing Y N 8   
A1B04 C5  N1   doub Y N 9   
A1B04 N1  C3   sing Y N 10  
A1B04 C6  C    sing N N 11  
A1B04 C6  C7   doub Y N 12  
A1B04 C7  C8   sing Y N 13  
A1B04 C8  C9   doub Y N 14  
A1B04 C9  C10  sing Y N 15  
A1B04 C10 C11  doub Y N 16  
A1B04 C11 C6   sing Y N 17  
A1B04 C4  H5   sing N N 18  
A1B04 C5  H6   sing N N 19  
A1B04 C7  H7   sing N N 20  
A1B04 C8  H8   sing N N 21  
A1B04 C10 H10  sing N N 22  
A1B04 C11 H11  sing N N 23  
A1B04 C9  H9   sing N N 24  
A1B04 N   H    sing N N 25  
A1B04 C1  H1   sing N N 26  
A1B04 C1  H2   sing N N 27  
A1B04 C2  H3   sing N N 28  
A1B04 C2  H4   sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
CYS   N   CA   sing N N 99  
CYS   N   H    sing N N 100 
CYS   N   H2   sing N N 101 
CYS   CA  C    sing N N 102 
CYS   CA  CB   sing N N 103 
CYS   CA  HA   sing N N 104 
CYS   C   O    doub N N 105 
CYS   C   OXT  sing N N 106 
CYS   CB  SG   sing N N 107 
CYS   CB  HB2  sing N N 108 
CYS   CB  HB3  sing N N 109 
CYS   SG  HG   sing N N 110 
CYS   OXT HXT  sing N N 111 
DMS   S   O    doub N N 112 
DMS   S   C1   sing N N 113 
DMS   S   C2   sing N N 114 
DMS   C1  H11  sing N N 115 
DMS   C1  H12  sing N N 116 
DMS   C1  H13  sing N N 117 
DMS   C2  H21  sing N N 118 
DMS   C2  H22  sing N N 119 
DMS   C2  H23  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TRP   N   CA   sing N N 344 
TRP   N   H    sing N N 345 
TRP   N   H2   sing N N 346 
TRP   CA  C    sing N N 347 
TRP   CA  CB   sing N N 348 
TRP   CA  HA   sing N N 349 
TRP   C   O    doub N N 350 
TRP   C   OXT  sing N N 351 
TRP   CB  CG   sing N N 352 
TRP   CB  HB2  sing N N 353 
TRP   CB  HB3  sing N N 354 
TRP   CG  CD1  doub Y N 355 
TRP   CG  CD2  sing Y N 356 
TRP   CD1 NE1  sing Y N 357 
TRP   CD1 HD1  sing N N 358 
TRP   CD2 CE2  doub Y N 359 
TRP   CD2 CE3  sing Y N 360 
TRP   NE1 CE2  sing Y N 361 
TRP   NE1 HE1  sing N N 362 
TRP   CE2 CZ2  sing Y N 363 
TRP   CE3 CZ3  doub Y N 364 
TRP   CE3 HE3  sing N N 365 
TRP   CZ2 CH2  doub Y N 366 
TRP   CZ2 HZ2  sing N N 367 
TRP   CZ3 CH2  sing Y N 368 
TRP   CZ3 HZ3  sing N N 369 
TRP   CH2 HH2  sing N N 370 
TRP   OXT HXT  sing N N 371 
TYR   N   CA   sing N N 372 
TYR   N   H    sing N N 373 
TYR   N   H2   sing N N 374 
TYR   CA  C    sing N N 375 
TYR   CA  CB   sing N N 376 
TYR   CA  HA   sing N N 377 
TYR   C   O    doub N N 378 
TYR   C   OXT  sing N N 379 
TYR   CB  CG   sing N N 380 
TYR   CB  HB2  sing N N 381 
TYR   CB  HB3  sing N N 382 
TYR   CG  CD1  doub Y N 383 
TYR   CG  CD2  sing Y N 384 
TYR   CD1 CE1  sing Y N 385 
TYR   CD1 HD1  sing N N 386 
TYR   CD2 CE2  doub Y N 387 
TYR   CD2 HD2  sing N N 388 
TYR   CE1 CZ   doub Y N 389 
TYR   CE1 HE1  sing N N 390 
TYR   CE2 CZ   sing Y N 391 
TYR   CE2 HE2  sing N N 392 
TYR   CZ  OH   sing N N 393 
TYR   OH  HH   sing N N 394 
TYR   OXT HXT  sing N N 395 
VAL   N   CA   sing N N 396 
VAL   N   H    sing N N 397 
VAL   N   H2   sing N N 398 
VAL   CA  C    sing N N 399 
VAL   CA  CB   sing N N 400 
VAL   CA  HA   sing N N 401 
VAL   C   O    doub N N 402 
VAL   C   OXT  sing N N 403 
VAL   CB  CG1  sing N N 404 
VAL   CB  CG2  sing N N 405 
VAL   CB  HB   sing N N 406 
VAL   CG1 HG11 sing N N 407 
VAL   CG1 HG12 sing N N 408 
VAL   CG1 HG13 sing N N 409 
VAL   CG2 HG21 sing N N 410 
VAL   CG2 HG22 sing N N 411 
VAL   CG2 HG23 sing N N 412 
VAL   OXT HXT  sing N N 413 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I32 
_atom_sites.fract_transf_matrix[1][1]   0.011541 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000947 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017581 
_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]   0.015456 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.724 7.945   24.896 1.00 12.75 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.989 8.045   24.118 1.00 12.85 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.125 6.845   23.168 1.00 12.73 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.426 5.849   23.359 1.00 13.66 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.180 8.090   25.076 1.00 14.95 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.276 6.869   25.775 1.00 18.12 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.019 6.936   22.194 1.00 11.75 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.316 5.851   21.275 1.00 11.67 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.715 6.324   19.898 1.00 9.72  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.401 7.452   19.512 1.00 11.18 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.379 5.479   19.168 1.00 9.94  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.844 5.847   17.821 1.00 9.27  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.815 4.633   16.910 1.00 9.68  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.750 3.481   17.376 1.00 10.44 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.298 6.373   17.911 1.00 11.38 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.887 4.870   15.600 1.00 9.27  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.096 3.837   14.586 1.00 9.19  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.559 3.932   14.161 1.00 9.11  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.052 5.034   13.883 1.00 10.17 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.216 4.057   13.344 1.00 8.89  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.745 4.185   13.706 1.00 10.66 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.403 2.896   12.337 1.00 10.39 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.916 4.786   12.529 1.00 11.06 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.266 2.806   14.115 1.00 9.62  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.673 2.760   13.682 1.00 10.73 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.777 1.941   12.416 1.00 11.13 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.737 0.690   12.466 1.00 12.54 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.550 2.161   14.797 1.00 11.90 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.628 3.029   16.038 1.00 11.66 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.480 4.138   16.095 1.00 12.21 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.789 2.812   17.121 1.00 13.55 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.494 4.997   17.200 1.00 13.03 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.793 3.671   18.237 1.00 13.99 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.658 4.757   18.267 1.00 14.19 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.651 5.635   19.348 1.00 16.54 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.776 2.590   11.266 1.00 10.94 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.851 1.968   9.954  1.00 12.28 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.103 2.462   9.229  1.00 12.33 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.339 3.682   9.172  1.00 11.92 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.564 2.240   9.130  1.00 12.98 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.217 3.734   9.031  1.00 14.25 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.669 1.620   7.748  1.00 14.44 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.945 1.559   8.699  1.00 13.36 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.195 1.999   8.054  1.00 14.14 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.022 2.851   9.003  1.00 12.80 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.152 2.546   10.199 1.00 13.11 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.519 3.996   8.496  1.00 12.61 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.230 4.974   9.339  1.00 12.16 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.310 6.161   9.653  1.00 11.65 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.816 7.293   9.773  1.00 12.41 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.579 5.418   8.741  1.00 14.40 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.633 4.330   8.820  1.00 17.73 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.378 4.240   9.806  1.00 21.14 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.645 3.464   7.845  1.00 16.91 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.042 5.873   9.914  1.00 10.49 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.074 6.902   10.287 1.00 10.34 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.417 6.575   11.630 1.00 10.51 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.131 5.394   11.939 1.00 10.92 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.953 7.015   9.227  1.00 10.97 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.447 7.430   7.860  1.00 11.51 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.124 8.636   7.672  1.00 13.14 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.242 6.617   6.753  1.00 14.12 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.586 9.015   6.417  1.00 14.37 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.675 7.010   5.488  1.00 15.87 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.318 8.217   5.328  1.00 16.53 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.758 8.625   4.075  1.00 19.52 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.081 7.630   12.374 1.00 9.15  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.308 7.555   13.614 1.00 8.91  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.074 8.438   13.372 1.00 8.74  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.229 9.644   13.090 1.00 9.71  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.150 8.084   14.796 1.00 10.49 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.364 8.414   16.061 1.00 11.18 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.322 8.775   17.233 1.00 12.44 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.801 9.836   18.097 1.00 12.73 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.131 9.660   19.235 1.00 13.32 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.802 8.426   19.644 1.00 14.63 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.703 10.716  19.928 1.00 13.47 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.878 7.851   13.455 1.00 8.78  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.606 8.565   13.242 1.00 8.78  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.956 8.784   14.597 1.00 9.02  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.665 7.785   15.295 1.00 9.53  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.661 7.809   12.313 1.00 9.36  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.439 8.663   11.997 1.00 10.67 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.340 7.308   11.054 1.00 10.93 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.735 10.039  14.975 1.00 8.22  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.134 10.381  16.274 0.50 8.28  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.185 10.356  16.291 0.50 9.85  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 20.024 11.371  16.124 1.00 8.64  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.887 12.030  15.068 1.00 9.90  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.163 10.972  17.281 0.50 8.14  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.359 10.941  17.170 0.50 12.76 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.084 9.894   17.792 0.50 9.86  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.961 11.176  18.610 0.50 12.82 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.894 12.210  16.695 0.50 5.62  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.566 10.043  17.148 0.50 15.86 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.199 11.526  17.177 1.00 8.72  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.214 12.617  17.167 1.00 9.26  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 19.041 13.935  17.163 1.00 9.57  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.967 14.101  17.956 1.00 9.80  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.368 12.617  18.433 1.00 9.60  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.477 11.392  18.518 1.00 9.65  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.869 10.374  19.097 1.00 10.11 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.288 11.477  17.940 1.00 10.58 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.639 14.873  16.305 1.00 9.97  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.408 16.160  16.245 1.00 10.25 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.438 16.825  17.613 1.00 11.16 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.466 17.377  18.011 1.00 12.13 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.778 17.067  15.197 1.00 10.79 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.592 18.378  14.940 1.00 11.01 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.810 19.236  13.969 1.00 12.61 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.529 20.445  13.516 1.00 13.50 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.569 21.596  14.177 1.00 14.17 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 19.028 21.699  15.384 1.00 15.95 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.143 22.669  13.626 1.00 15.62 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.301 16.736  18.366 1.00 10.89 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.263 17.435  19.667 1.00 12.46 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 19.133 16.809  20.749 1.00 12.91 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.318 17.413  21.826 1.00 15.30 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.807 17.630  20.166 1.00 13.55 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 16.125 16.363  20.655 1.00 13.35 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.482 15.480  19.785 1.00 13.07 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 16.000 15.882  21.925 1.00 14.09 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.970 14.497  20.564 1.00 13.94 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.263 14.705  21.848 1.00 14.57 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.636 15.580  20.508 1.00 12.38 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.514 14.870  21.437 1.00 11.93 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.969 14.814  20.969 1.00 12.55 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.814 14.207  21.622 1.00 13.80 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.989 13.479  21.769 1.00 11.96 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.608 13.465  22.416 1.00 12.54 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.155 11.994  22.667 1.00 13.38 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.615 14.239  23.754 1.00 14.90 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.281 15.467  19.822 1.00 12.17 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.643 15.426  19.283 1.00 11.82 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.624 16.079  20.264 1.00 12.69 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.299 17.104  20.882 1.00 13.34 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.673 16.149  17.941 1.00 12.40 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.819 15.492  20.377 1.00 12.47 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.851 16.016  21.287 1.00 12.38 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.780 17.015  20.544 1.00 12.81 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.720 17.155  19.309 1.00 12.17 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.716 14.840  21.776 1.00 14.31 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.400 14.300  20.643 1.00 13.83 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.883 13.730  22.453 1.00 15.79 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.720 17.657  21.268 1.00 13.01 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.699 18.514  20.637 1.00 13.39 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.527 17.702  19.645 1.00 12.98 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.790 18.170  18.526 1.00 12.86 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.643 19.151  21.684 1.00 14.01 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.920 19.749  21.057 1.00 19.06 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.896 20.922  20.279 1.00 21.61 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.169 19.203  20.930 1.00 21.96 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 33.148 21.155  19.904 1.00 22.10 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.944 20.103  20.192 1.00 23.28 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.902 16.444  20.004 1.00 12.78 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.661 15.630  19.075 1.00 12.84 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.871 15.354  17.784 1.00 11.70 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.448 15.374  16.692 1.00 12.15 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.112 14.304  19.703 1.00 14.96 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.070 13.571  18.767 1.00 20.56 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.240 13.986  18.590 1.00 24.47 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.608 12.490  18.117 1.00 21.62 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.547 15.123  17.913 1.00 11.47 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.744 14.972  16.690 1.00 10.09 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.803 16.217  15.782 1.00 9.83  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 29.007 16.112  14.561 1.00 10.93 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.291 14.674  17.048 1.00 10.94 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 27.035 13.308  17.651 1.00 11.14 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.660 12.341  17.192 1.00 12.27 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.180 13.228  18.586 1.00 11.67 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.592 17.393  16.386 1.00 10.11 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.614 18.648  15.607 1.00 10.59 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 30.019 18.908  15.019 1.00 10.21 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.087 19.476  13.922 1.00 11.08 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.202 19.823  16.513 1.00 10.43 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.704 19.886  16.675 1.00 10.69 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.975 19.579  17.789 1.00 12.17 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.753 20.338  15.690 1.00 10.43 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.630 19.808  17.554 1.00 11.88 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.468 20.270  16.266 1.00 11.13 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.873 20.820  14.377 1.00 12.24 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.301 20.649  15.561 1.00 12.99 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.734 21.147  13.668 1.00 13.25 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.484 21.131  14.268 1.00 13.63 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.084 18.492  15.717 1.00 10.26 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.446 18.704  15.226 1.00 11.23 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.858 17.709  14.141 1.00 11.86 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.896 17.870  13.490 1.00 13.06 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.421 18.653  16.383 1.00 13.45 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.050 16.653  13.923 1.00 11.24 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.317 15.595  12.917 1.00 11.41 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.043 15.431  12.060 1.00 11.04 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.630 14.298  11.718 1.00 11.57 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.714 14.264  13.601 1.00 12.78 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.064 14.428  14.259 1.00 13.84 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.107 14.361  13.574 1.00 17.00 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.123 14.726  15.562 1.00 14.88 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.397 16.523  11.737 1.00 11.30 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.087 16.503  11.098 1.00 10.05 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.109 16.076  9.680  1.00 11.22 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.935 16.538  8.881  1.00 13.37 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.512 17.917  11.189 1.00 10.91 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.095 18.078  10.619 1.00 10.94 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.069 17.292  11.437 1.00 11.96 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.677 19.566  10.576 1.00 14.27 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.174 15.192  9.286  1.00 10.27 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 27.973 14.793  7.891  1.00 11.12 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.735 15.502  7.341  1.00 10.85 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.769 16.037  6.228  1.00 12.54 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.867 13.259  7.773  1.00 10.77 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.490 12.838  6.335  1.00 13.81 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.153 12.574  8.253  1.00 12.22 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.609 15.486  8.075  1.00 11.31 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.339 16.024  7.592  1.00 11.33 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.413 16.253  8.776  1.00 11.27 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.457 15.460  9.749  1.00 11.04 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.696 15.010  6.577  1.00 12.63 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.268 15.299  6.176  1.00 13.68 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.839 16.146  5.187  1.00 15.96 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.091 14.688  6.712  1.00 12.84 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.470 16.108  5.093  1.00 16.90 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 19.989 15.200  5.995  1.00 14.72 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.866 13.730  7.691  1.00 13.08 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.672 14.765  6.246  1.00 16.01 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.576 13.292  7.911  1.00 14.55 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.491 13.855  7.245  1.00 15.83 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.568 17.272  8.739  1.00 11.23 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.592 17.487  9.793  1.00 11.99 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.344 18.140  9.194  1.00 12.45 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.439 18.918  8.208  1.00 13.11 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.166 18.307  10.950 1.00 13.63 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.724 19.679  10.563 1.00 14.03 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.745 20.847  10.368 1.00 13.86 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.081 21.820  9.637  1.00 15.79 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.663 20.856  11.000 1.00 14.42 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.195 17.843  9.764  1.00 12.08 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.936 18.414  9.303  1.00 12.49 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.987 18.587  10.492 1.00 12.35 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.473 17.598  11.048 1.00 12.51 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.329 17.504  8.215  1.00 14.92 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.047 18.011  7.591  1.00 17.05 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.215 18.561  8.319  1.00 18.12 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.839 17.769  6.399  1.00 21.27 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.756 19.845  10.901 1.00 12.36 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.917 20.175  12.029 0.50 12.44 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.931 20.118  12.050 0.50 13.80 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.479 19.733  11.838 1.00 13.74 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.860 19.237  12.781 1.00 14.70 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.969 21.677  12.287 0.50 12.95 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.083 21.570  12.479 0.50 17.92 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.131 22.013  13.381 0.50 11.68 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.755 22.418  11.398 0.50 24.24 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.947 19.886  10.626 1.00 14.61 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.559 19.497  10.357 1.00 14.54 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.342 17.993  10.533 1.00 13.86 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.211 17.573  10.782 1.00 15.61 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.126 19.928  8.961  1.00 18.36 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.629 19.121  7.920  1.00 20.85 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.403 17.173  10.442 1.00 12.32 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.317 15.716  10.629 1.00 12.35 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.785 15.272  12.010 1.00 12.18 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.683 14.056  12.320 1.00 11.92 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.158 14.987  9.556  1.00 13.03 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.626 15.226  8.141  1.00 15.32 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.482 14.544  7.099  1.00 14.21 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.402 13.074  7.203  1.00 12.40 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.576 12.249  6.175  1.00 12.57 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.840 12.729  4.960  1.00 14.96 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.422 10.924  6.336  1.00 13.82 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.368 16.148  12.814 1.00 12.46 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 15.006 15.800  14.079 1.00 11.43 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.145 14.777  13.875 1.00 10.39 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.346 13.912  14.744 1.00 10.68 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 14.006 15.321  15.163 1.00 11.75 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.657 15.082  16.520 1.00 11.51 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.543 15.893  16.948 1.00 11.52 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.252 14.107  17.243 1.00 12.94 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.925 14.903  12.776 1.00 10.26 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 18.024 13.949  12.554 1.00 9.92  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.361 14.658  12.398 1.00 9.71  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.446 15.761  11.805 1.00 10.42 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.765 13.169  11.276 1.00 10.06 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.697 12.052  11.346 1.00 11.63 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.593 11.347  9.999  1.00 12.41 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.983 11.033  12.456 1.00 11.48 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.415 13.978  12.840 1.00 9.11  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.798 14.421  12.602 1.00 8.89  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.627 13.176  12.411 1.00 8.61  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.429 12.151  13.113 1.00 9.14  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.284 15.261  13.791 1.00 9.41  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.719 15.828  13.675 1.00 10.01 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.815 17.202  14.368 1.00 12.08 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.744 14.871  14.299 1.00 10.15 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.584 13.251  11.472 1.00 8.80  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.510 12.155  11.180 1.00 8.75  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.932 12.682  11.339 1.00 8.67  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.252 13.733  10.748 1.00 9.74  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.270 11.598  9.779  1.00 9.26  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.287 10.496  9.468  1.00 10.62 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.820 11.082  9.653  1.00 9.92  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.755 11.984  12.098 1.00 8.80  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.177 12.319  12.273 1.00 9.10  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.018 11.122  11.797 1.00 9.82  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.543 9.994   11.567 1.00 10.31 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.485 12.666  13.727 1.00 10.23 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.169 11.587  14.584 1.00 10.98 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.304 11.391  11.556 1.00 10.99 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.243 10.346  11.112 1.00 11.73 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.856 9.618   12.291 1.00 13.44 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.072 10.214  13.379 1.00 15.89 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.344 10.956  10.241 1.00 13.63 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.054 11.925  10.994 1.00 16.56 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.194 8.316   12.099 1.00 13.76 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.788 7.515   13.165 1.00 15.65 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.137 6.947   12.724 1.00 17.61 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.354 6.683   11.538 1.00 16.86 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.866 6.332   13.553 1.00 16.03 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.720 5.445   12.453 1.00 16.62 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.475 6.782   13.985 1.00 16.44 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.993 6.649   13.707 1.00 19.17 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.274 6.020   13.408 1.00 21.05 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.067 4.513   13.179 1.00 21.10 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.589 3.965   12.204 1.00 22.91 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.290 6.368   14.509 1.00 25.70 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.813 5.887   15.751 1.00 30.40 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.519 7.846   14.622 1.00 26.65 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.245 3.871   14.024 1.00 21.21 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.957 2.438   13.874 1.00 22.09 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.728 2.166   12.965 1.00 19.62 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.777 2.953   12.982 1.00 19.17 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.683 1.835   15.240 1.00 24.70 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.696 1.046   12.257 1.00 18.11 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.544 0.624   11.430 1.00 18.94 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.450 -0.010  12.291 1.00 18.15 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.740 -0.777  13.197 1.00 19.33 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 32.965 -0.369  10.348 1.00 22.13 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.846 0.238   9.244  1.00 28.64 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.184 -0.828  8.254  1.00 35.48 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.044 -1.694  8.515  1.00 35.72 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.488 -0.811  7.119  1.00 36.49 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.191 0.357   12.031 1.00 15.54 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.034 -0.143  12.779 1.00 15.30 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.442 -1.422  12.207 1.00 14.70 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.705 -1.795  11.052 1.00 15.85 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.489 -2.009  12.983 1.00 13.91 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.884 -3.284  12.616 1.00 13.73 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.430 -3.202  12.164 1.00 12.88 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.864 -4.232  11.764 1.00 13.65 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.023 -4.265  13.774 1.00 16.08 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.729 -4.681  14.176 1.00 18.53 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.777 -2.049  12.337 1.00 12.16 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.395 -1.934  11.915 1.00 12.08 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.301 -1.882  10.394 1.00 12.85 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.185 -1.303  9.736  1.00 14.69 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.749 -0.675  12.517 1.00 11.23 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.649 -0.727  14.025 1.00 12.17 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.289 -1.832  14.561 1.00 12.96 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.889 0.316   14.680 1.00 12.29 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.262 -2.402  9.822  1.00 13.65 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.956 -2.288  8.383  1.00 15.00 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.612 -1.557  8.218  1.00 13.69 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.695 -1.728  9.037  1.00 15.01 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.930 -3.639  7.708  1.00 20.55 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 20.950 -4.420  8.336  1.00 23.99 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.301 -4.337  7.783  1.00 22.34 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.482 -0.736  7.199  1.00 13.26 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.267 0.032   6.968  1.00 12.21 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.277 -0.711  6.079  1.00 12.32 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.645 -1.235  5.010  1.00 13.74 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.587 1.429   6.362  1.00 12.65 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.703 2.161   7.164  1.00 13.21 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.332 2.300   6.244  1.00 12.78 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.355 2.436   8.684  1.00 13.65 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.017 -0.735  6.469  1.00 11.31 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 15.937 -1.301  5.656  1.00 11.30 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.666 -0.404  4.417  1.00 11.85 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.700 0.832   4.491  1.00 11.59 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.640 -1.334  6.469  1.00 11.51 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.381 -1.048  3.268  1.00 13.53 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.021 -0.324  2.038  1.00 14.65 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.702 -0.946  1.562  1.00 15.83 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.719 -1.920  0.797  1.00 17.00 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.162 -0.415  0.990  1.00 17.15 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.534 0.079   1.508  1.00 16.59 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.623 1.568   1.836  1.00 15.49 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 18.961 1.971   2.319  1.00 14.56 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.202 3.118   2.956  1.00 14.45 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.227 4.003   3.151  1.00 14.17 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.426 3.388   3.427  1.00 16.86 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.568 -0.341  1.969  1.00 15.69 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.217 -0.941  1.903  1.00 15.45 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.136 0.067   2.257  1.00 15.87 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.390 1.197   2.684  1.00 17.05 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.189 -2.112  2.875  1.00 15.38 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.150 -1.575  4.598  1.00 14.15 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.843  -0.410  2.158  1.00 17.36 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.673  0.361   2.582  1.00 18.92 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 6.921  -0.413  3.672  1.00 17.57 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.700  -0.234  3.814  1.00 18.38 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.738  0.754   1.410  1.00 23.71 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.087  -0.411  0.740  1.00 28.98 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.394  -1.580  1.120  1.00 29.59 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.245  -0.179  -0.182 1.00 33.48 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.623  -1.225  4.541  1.00 15.15 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 6.924  -1.899  5.659  1.00 14.74 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.216  -0.893  6.530  1.00 14.35 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.695  0.244   6.736  1.00 14.77 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 7.904  -2.670  6.540  1.00 14.74 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.589  -4.157  5.788  1.00 16.29 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.132  -1.364  7.084  1.00 13.18 ? 59  GLN   A N   1 
ATOM   411  C  CA  A GLN   A 1 53  ? 4.316  -0.660  8.074  0.50 12.31 ? 59  GLN   A CA  1 
ATOM   412  C  CA  B GLN   A 1 53  ? 4.395  -0.611  8.044  0.50 13.38 ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.144  -1.466  9.324  1.00 11.46 ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.315  -1.131  10.111 1.00 12.37 ? 59  GLN   A O   1 
ATOM   415  C  CB  A GLN   A 1 53  ? 2.944  -0.178  7.554  0.50 12.96 ? 59  GLN   A CB  1 
ATOM   416  C  CB  B GLN   A 1 53  ? 3.155  0.018   7.377  0.50 16.68 ? 59  GLN   A CB  1 
ATOM   417  C  CG  A GLN   A 1 53  ? 3.049  1.021   6.592  0.50 12.88 ? 59  GLN   A CG  1 
ATOM   418  C  CG  B GLN   A 1 53  ? 3.524  0.947   6.149  0.50 20.47 ? 59  GLN   A CG  1 
ATOM   419  C  CD  A GLN   A 1 53  ? 1.702  1.571   6.171  0.50 14.15 ? 59  GLN   A CD  1 
ATOM   420  C  CD  B GLN   A 1 53  ? 4.626  1.982   6.430  0.50 26.47 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 A GLN   A 1 53  ? 1.235  1.366   5.026  0.50 17.25 ? 59  GLN   A OE1 1 
ATOM   422  O  OE1 B GLN   A 1 53  ? 4.737  2.492   7.545  0.50 26.61 ? 59  GLN   A OE1 1 
ATOM   423  N  NE2 A GLN   A 1 53  ? 1.041  2.238   7.068  0.50 11.51 ? 59  GLN   A NE2 1 
ATOM   424  N  NE2 B GLN   A 1 53  ? 5.491  2.327   5.453  0.50 29.20 ? 59  GLN   A NE2 1 
ATOM   425  N  N   . THR   A 1 54  ? 4.901  -2.584  9.497  1.00 10.72 ? 60  THR   A N   1 
ATOM   426  C  CA  . THR   A 1 54  ? 4.917  -3.350  10.738 1.00 11.07 ? 60  THR   A CA  1 
ATOM   427  C  C   . THR   A 1 54  ? 6.374  -3.595  11.112 1.00 9.89  ? 60  THR   A C   1 
ATOM   428  O  O   . THR   A 1 54  ? 7.231  -3.781  10.242 1.00 11.68 ? 60  THR   A O   1 
ATOM   429  C  CB  . THR   A 1 54  ? 4.160  -4.619  10.685 1.00 14.20 ? 60  THR   A CB  1 
ATOM   430  O  OG1 . THR   A 1 54  ? 4.750  -5.494  9.805  1.00 20.57 ? 60  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A 1 54  ? 2.720  -4.453  10.316 1.00 13.94 ? 60  THR   A CG2 1 
ATOM   432  N  N   . GLY   A 1 55  ? 6.653  -3.564  12.403 1.00 10.06 ? 61  GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 55  ? 8.031  -3.743  12.864 1.00 9.59  ? 61  GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 55  ? 8.041  -3.818  14.387 1.00 8.17  ? 61  GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 55  ? 7.005  -4.063  15.017 1.00 8.92  ? 61  GLY   A O   1 
ATOM   436  N  N   . VAL   A 1 56  ? 9.205  -3.585  14.989 1.00 8.32  ? 62  VAL   A N   1 
ATOM   437  C  CA  . VAL   A 1 56  ? 9.411  -3.675  16.442 1.00 7.52  ? 62  VAL   A CA  1 
ATOM   438  C  C   . VAL   A 1 56  ? 10.264 -2.509  16.864 1.00 7.77  ? 62  VAL   A C   1 
ATOM   439  O  O   . VAL   A 1 56  ? 11.262 -2.203  16.194 1.00 8.65  ? 62  VAL   A O   1 
ATOM   440  C  CB  . VAL   A 1 56  ? 10.114 -5.022  16.772 1.00 8.90  ? 62  VAL   A CB  1 
ATOM   441  C  CG1 . VAL   A 1 56  ? 10.506 -5.132  18.234 1.00 10.99 ? 62  VAL   A CG1 1 
ATOM   442  C  CG2 . VAL   A 1 56  ? 9.234  -6.205  16.402 1.00 9.82  ? 62  VAL   A CG2 1 
ATOM   443  N  N   . TYR   A 1 57  ? 9.902  -1.855  17.978 1.00 7.66  ? 63  TYR   A N   1 
ATOM   444  C  CA  . TYR   A 1 57  ? 10.758 -0.764  18.481 1.00 7.45  ? 63  TYR   A CA  1 
ATOM   445  C  C   . TYR   A 1 57  ? 11.213 -0.985  19.917 1.00 8.39  ? 63  TYR   A C   1 
ATOM   446  O  O   . TYR   A 1 57  ? 10.517 -1.647  20.695 1.00 9.16  ? 63  TYR   A O   1 
ATOM   447  C  CB  . TYR   A 1 57  ? 10.095 0.655   18.357 1.00 8.53  ? 63  TYR   A CB  1 
ATOM   448  C  CG  . TYR   A 1 57  ? 9.121  1.046   19.448 1.00 7.99  ? 63  TYR   A CG  1 
ATOM   449  C  CD1 . TYR   A 1 57  ? 7.846  0.488   19.503 1.00 9.07  ? 63  TYR   A CD1 1 
ATOM   450  C  CD2 . TYR   A 1 57  ? 9.470  1.946   20.445 1.00 8.99  ? 63  TYR   A CD2 1 
ATOM   451  C  CE1 . TYR   A 1 57  ? 6.941  0.823   20.513 1.00 9.99  ? 63  TYR   A CE1 1 
ATOM   452  C  CE2 . TYR   A 1 57  ? 8.550  2.328   21.432 1.00 9.87  ? 63  TYR   A CE2 1 
ATOM   453  C  CZ  . TYR   A 1 57  ? 7.302  1.753   21.461 1.00 10.44 ? 63  TYR   A CZ  1 
ATOM   454  O  OH  . TYR   A 1 57  ? 6.360  2.042   22.443 1.00 13.39 ? 63  TYR   A OH  1 
ATOM   455  N  N   . TYR   A 1 58  ? 12.327 -0.361  20.304 1.00 7.83  ? 64  TYR   A N   1 
ATOM   456  C  CA  . TYR   A 1 58  ? 12.816 -0.431  21.673 1.00 8.31  ? 64  TYR   A CA  1 
ATOM   457  C  C   . TYR   A 1 58  ? 12.345 0.784   22.480 1.00 8.10  ? 64  TYR   A C   1 
ATOM   458  O  O   . TYR   A 1 58  ? 12.579 1.936   22.091 1.00 8.26  ? 64  TYR   A O   1 
ATOM   459  C  CB  . TYR   A 1 58  ? 14.367 -0.492  21.701 1.00 9.22  ? 64  TYR   A CB  1 
ATOM   460  C  CG  . TYR   A 1 58  ? 14.840 -0.640  23.141 1.00 9.56  ? 64  TYR   A CG  1 
ATOM   461  C  CD1 . TYR   A 1 58  ? 14.504 -1.748  23.890 1.00 10.16 ? 64  TYR   A CD1 1 
ATOM   462  C  CD2 . TYR   A 1 58  ? 15.584 0.368   23.760 1.00 10.36 ? 64  TYR   A CD2 1 
ATOM   463  C  CE1 . TYR   A 1 58  ? 14.887 -1.855  25.226 1.00 11.88 ? 64  TYR   A CE1 1 
ATOM   464  C  CE2 . TYR   A 1 58  ? 15.981 0.258   25.089 1.00 11.70 ? 64  TYR   A CE2 1 
ATOM   465  C  CZ  . TYR   A 1 58  ? 15.643 -0.862  25.803 1.00 11.11 ? 64  TYR   A CZ  1 
ATOM   466  O  OH  . TYR   A 1 58  ? 16.001 -0.997  27.148 1.00 14.30 ? 64  TYR   A OH  1 
ATOM   467  N  N   . CYS   A 1 59  ? 11.738 0.479   23.626 1.00 8.48  ? 65  CYS   A N   1 
ATOM   468  C  CA  . CYS   A 1 59  ? 11.205 1.464   24.584 1.00 8.88  ? 65  CYS   A CA  1 
ATOM   469  C  C   . CYS   A 1 59  ? 12.022 1.459   25.879 1.00 9.22  ? 65  CYS   A C   1 
ATOM   470  O  O   . CYS   A 1 59  ? 11.824 0.545   26.724 1.00 9.89  ? 65  CYS   A O   1 
ATOM   471  C  CB  . CYS   A 1 59  ? 9.748  1.167   24.868 1.00 9.25  ? 65  CYS   A CB  1 
ATOM   472  S  SG  . CYS   A 1 59  ? 9.004  2.306   26.094 1.00 10.27 ? 65  CYS   A SG  1 
ATOM   473  N  N   . SER   A 1 60  ? 12.944 2.397   26.042 1.00 9.30  ? 66  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 60  ? 13.834 2.378   27.217 1.00 10.79 ? 66  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 60  ? 13.098 2.569   28.535 1.00 9.95  ? 66  SER   A C   1 
ATOM   476  O  O   . SER   A 1 60  ? 13.505 2.003   29.561 1.00 11.85 ? 66  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 60  ? 14.967 3.388   27.041 1.00 12.89 ? 66  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 60  ? 14.562 4.728   27.196 1.00 14.80 ? 66  SER   A OG  1 
ATOM   479  N  N   . SER   A 1 61  ? 11.977 3.318   28.513 1.00 9.61  ? 67  SER   A N   1 
ATOM   480  C  CA  . SER   A 1 61  ? 11.182 3.534   29.720 1.00 9.97  ? 67  SER   A CA  1 
ATOM   481  C  C   . SER   A 1 61  ? 10.364 2.322   30.165 1.00 9.67  ? 67  SER   A C   1 
ATOM   482  O  O   . SER   A 1 61  ? 9.745  2.347   31.239 1.00 10.46 ? 67  SER   A O   1 
ATOM   483  C  CB  . SER   A 1 61  ? 10.294 4.775   29.603 1.00 11.43 ? 67  SER   A CB  1 
ATOM   484  O  OG  . SER   A 1 61  ? 9.304  4.573   28.617 1.00 11.50 ? 67  SER   A OG  1 
ATOM   485  N  N   . ARG   A 1 62  ? 10.438 1.215   29.391 1.00 10.14 ? 68  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? 9.848  -0.066  29.776 1.00 10.36 ? 68  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? 10.896 -1.194  29.726 1.00 11.33 ? 68  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? 10.539 -2.350  29.996 1.00 11.97 ? 68  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? 8.675  -0.381  28.835 1.00 10.74 ? 68  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? 7.494  0.576   28.988 1.00 11.03 ? 68  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? 6.724  0.292   30.263 1.00 11.90 ? 68  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? 5.595  1.223   30.440 1.00 13.16 ? 68  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? 5.661  2.386   31.085 1.00 12.14 ? 68  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? 6.815  2.801   31.626 1.00 13.57 ? 68  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? 4.558  3.141   31.231 1.00 14.89 ? 68  ARG   A NH2 1 
ATOM   496  N  N   . ARG   A 1 63  ? 12.129 -0.941  29.291 1.00 12.00 ? 69  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 63  ? 13.114 -2.008  28.980 1.00 13.02 ? 69  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 63  ? 12.498 -3.123  28.120 1.00 14.85 ? 69  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 63  ? 12.674 -4.330  28.397 1.00 16.77 ? 69  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 63  ? 13.731 -2.630  30.234 1.00 16.50 ? 69  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 63  ? 14.664 -1.718  30.866 1.00 17.84 ? 69  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 63  ? 15.486 -2.557  31.862 1.00 18.50 ? 69  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 63  ? 16.263 -1.647  32.672 1.00 19.44 ? 69  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 63  ? 15.933 -1.246  33.896 1.00 17.07 ? 69  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 63  ? 14.846 -1.734  34.497 1.00 17.83 ? 69  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 63  ? 16.702 -0.385  34.544 1.00 18.90 ? 69  ARG   A NH2 1 
ATOM   507  N  N   . LYS   A 1 64  ? 11.761 -2.732  27.111 1.00 12.33 ? 70  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 64  ? 11.056 -3.724  26.301 1.00 12.73 ? 70  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 64  ? 11.031 -3.329  24.849 1.00 11.60 ? 70  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 64  ? 10.945 -2.129  24.520 1.00 11.52 ? 70  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 64  ? 9.598  -3.830  26.820 1.00 15.65 ? 70  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 64  ? 9.436  -4.755  28.036 1.00 24.62 ? 70  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 64  ? 7.983  -5.097  28.305 1.00 32.71 ? 70  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 64  ? 7.832  -5.928  29.563 1.00 39.47 ? 70  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 64  ? 8.403  -5.249  30.761 1.00 44.17 ? 70  LYS   A NZ  1 
ATOM   516  N  N   . HIS   A 1 65  ? 11.002 -4.350  23.976 1.00 10.35 ? 71  HIS   A N   1 
ATOM   517  C  CA  . HIS   A 1 65  ? 10.762 -4.176  22.560 1.00 9.59  ? 71  HIS   A CA  1 
ATOM   518  C  C   . HIS   A 1 65  ? 9.294  -4.513  22.299 1.00 11.15 ? 71  HIS   A C   1 
ATOM   519  O  O   . HIS   A 1 65  ? 8.795  -5.581  22.749 1.00 13.64 ? 71  HIS   A O   1 
ATOM   520  C  CB  . HIS   A 1 65  ? 11.655 -5.129  21.745 1.00 9.91  ? 71  HIS   A CB  1 
ATOM   521  C  CG  . HIS   A 1 65  ? 13.124 -4.792  21.840 1.00 11.05 ? 71  HIS   A CG  1 
ATOM   522  N  ND1 . HIS   A 1 65  ? 13.840 -4.134  20.863 1.00 13.17 ? 71  HIS   A ND1 1 
ATOM   523  C  CD2 . HIS   A 1 65  ? 13.986 -5.113  22.839 1.00 10.90 ? 71  HIS   A CD2 1 
ATOM   524  C  CE1 . HIS   A 1 65  ? 15.126 -4.082  21.284 1.00 11.23 ? 71  HIS   A CE1 1 
ATOM   525  N  NE2 . HIS   A 1 65  ? 15.230 -4.642  22.466 1.00 13.95 ? 71  HIS   A NE2 1 
ATOM   526  N  N   . TYR   A 1 66  ? 8.607  -3.680  21.530 1.00 9.33  ? 72  TYR   A N   1 
ATOM   527  C  CA  . TYR   A 1 66  ? 7.182  -3.849  21.250 1.00 9.28  ? 72  TYR   A CA  1 
ATOM   528  C  C   . TYR   A 1 66  ? 6.950  -3.963  19.760 1.00 8.85  ? 72  TYR   A C   1 
ATOM   529  O  O   . TYR   A 1 66  ? 7.460  -3.131  18.994 1.00 9.29  ? 72  TYR   A O   1 
ATOM   530  C  CB  . TYR   A 1 66  ? 6.368  -2.632  21.743 1.00 10.35 ? 72  TYR   A CB  1 
ATOM   531  C  CG  . TYR   A 1 66  ? 6.296  -2.462  23.251 1.00 10.66 ? 72  TYR   A CG  1 
ATOM   532  C  CD1 . TYR   A 1 66  ? 5.467  -3.274  24.027 1.00 12.69 ? 72  TYR   A CD1 1 
ATOM   533  C  CD2 . TYR   A 1 66  ? 7.055  -1.499  23.890 1.00 11.64 ? 72  TYR   A CD2 1 
ATOM   534  C  CE1 . TYR   A 1 66  ? 5.362  -3.100  25.406 1.00 13.38 ? 72  TYR   A CE1 1 
ATOM   535  C  CE2 . TYR   A 1 66  ? 6.970  -1.312  25.270 1.00 12.48 ? 72  TYR   A CE2 1 
ATOM   536  C  CZ  . TYR   A 1 66  ? 6.121  -2.117  26.023 1.00 12.88 ? 72  TYR   A CZ  1 
ATOM   537  O  OH  . TYR   A 1 66  ? 6.033  -1.901  27.398 1.00 14.89 ? 72  TYR   A OH  1 
ATOM   538  N  N   . PRO   A 1 67  ? 6.137  -4.934  19.338 1.00 8.96  ? 73  PRO   A N   1 
ATOM   539  C  CA  . PRO   A 1 67  ? 5.710  -4.973  17.923 1.00 9.65  ? 73  PRO   A CA  1 
ATOM   540  C  C   . PRO   A 1 67  ? 4.677  -3.866  17.667 1.00 9.78  ? 73  PRO   A C   1 
ATOM   541  O  O   . PRO   A 1 67  ? 3.730  -3.713  18.488 1.00 12.15 ? 73  PRO   A O   1 
ATOM   542  C  CB  . PRO   A 1 67  ? 5.060  -6.376  17.764 1.00 11.40 ? 73  PRO   A CB  1 
ATOM   543  C  CG  . PRO   A 1 67  ? 4.671  -6.781  19.158 1.00 13.61 ? 73  PRO   A CG  1 
ATOM   544  C  CD  . PRO   A 1 67  ? 5.556  -6.032  20.154 1.00 10.12 ? 73  PRO   A CD  1 
ATOM   545  N  N   . VAL   A 1 68  ? 4.775  -3.194  16.560 1.00 8.18  ? 74  VAL   A N   1 
ATOM   546  C  CA  . VAL   A 1 68  ? 3.863  -2.078  16.218 1.00 9.90  ? 74  VAL   A CA  1 
ATOM   547  C  C   . VAL   A 1 68  ? 3.551  -2.045  14.746 1.00 9.81  ? 74  VAL   A C   1 
ATOM   548  O  O   . VAL   A 1 68  ? 4.350  -2.419  13.893 1.00 10.27 ? 74  VAL   A O   1 
ATOM   549  C  CB  . VAL   A 1 68  ? 4.487  -0.702  16.598 1.00 12.85 ? 74  VAL   A CB  1 
ATOM   550  C  CG1 . VAL   A 1 68  ? 4.433  -0.482  18.108 1.00 14.35 ? 74  VAL   A CG1 1 
ATOM   551  C  CG2 . VAL   A 1 68  ? 5.877  -0.511  16.022 1.00 14.07 ? 74  VAL   A CG2 1 
ATOM   552  N  N   A SER   A 1 69  ? 2.359  -1.458  14.408 0.50 10.26 ? 75  SER   A N   1 
ATOM   553  N  N   B SER   A 1 69  ? 2.346  -1.507  14.456 0.50 10.38 ? 75  SER   A N   1 
ATOM   554  C  CA  A SER   A 1 69  ? 1.984  -1.016  13.047 0.50 9.90  ? 75  SER   A CA  1 
ATOM   555  C  CA  B SER   A 1 69  ? 1.875  -1.051  13.152 0.50 10.61 ? 75  SER   A CA  1 
ATOM   556  C  C   A SER   A 1 69  ? 2.169  0.498   13.023 0.50 9.46  ? 75  SER   A C   1 
ATOM   557  C  C   B SER   A 1 69  ? 2.192  0.478   13.092 0.50 10.22 ? 75  SER   A C   1 
ATOM   558  O  O   A SER   A 1 69  ? 1.766  1.186   13.952 0.50 9.73  ? 75  SER   A O   1 
ATOM   559  O  O   B SER   A 1 69  ? 1.976  1.150   14.103 0.50 10.75 ? 75  SER   A O   1 
ATOM   560  C  CB  A SER   A 1 69  ? 0.528  -1.303  12.727 0.50 10.70 ? 75  SER   A CB  1 
ATOM   561  C  CB  B SER   A 1 69  ? 0.365  -1.238  13.075 0.50 11.65 ? 75  SER   A CB  1 
ATOM   562  O  OG  A SER   A 1 69  ? 0.248  -2.673  12.902 0.50 14.87 ? 75  SER   A OG  1 
ATOM   563  O  OG  B SER   A 1 69  ? -0.074 -0.800  11.801 0.50 15.25 ? 75  SER   A OG  1 
ATOM   564  N  N   . PHE   A 1 70  ? 2.754  1.007   11.988 1.00 10.31 ? 76  PHE   A N   1 
ATOM   565  C  CA  . PHE   A 1 70  ? 3.088  2.420   11.917 1.00 10.32 ? 76  PHE   A CA  1 
ATOM   566  C  C   . PHE   A 1 70  ? 2.700  3.007   10.587 1.00 11.58 ? 76  PHE   A C   1 
ATOM   567  O  O   . PHE   A 1 70  ? 2.614  2.318   9.575  1.00 12.14 ? 76  PHE   A O   1 
ATOM   568  C  CB  . PHE   A 1 70  ? 4.603  2.642   12.282 1.00 11.27 ? 76  PHE   A CB  1 
ATOM   569  C  CG  . PHE   A 1 70  ? 5.596  1.853   11.461 1.00 10.19 ? 76  PHE   A CG  1 
ATOM   570  C  CD1 . PHE   A 1 70  ? 6.005  0.580   11.851 1.00 10.15 ? 76  PHE   A CD1 1 
ATOM   571  C  CD2 . PHE   A 1 70  ? 6.169  2.398   10.318 1.00 10.90 ? 76  PHE   A CD2 1 
ATOM   572  C  CE1 . PHE   A 1 70  ? 6.937  -0.126  11.117 1.00 10.56 ? 76  PHE   A CE1 1 
ATOM   573  C  CE2 . PHE   A 1 70  ? 7.124  1.680   9.589  1.00 11.82 ? 76  PHE   A CE2 1 
ATOM   574  C  CZ  . PHE   A 1 70  ? 7.465  0.412   9.975  1.00 11.15 ? 76  PHE   A CZ  1 
ATOM   575  N  N   . SER   A 1 71  ? 2.436  4.317   10.579 1.00 11.56 ? 77  SER   A N   1 
ATOM   576  C  CA  . SER   A 1 71  ? 2.034  5.012   9.347  1.00 12.47 ? 77  SER   A CA  1 
ATOM   577  C  C   . SER   A 1 71  ? 3.213  5.227   8.392  1.00 12.09 ? 77  SER   A C   1 
ATOM   578  O  O   . SER   A 1 71  ? 4.389  5.075   8.781  1.00 13.02 ? 77  SER   A O   1 
ATOM   579  C  CB  . SER   A 1 71  ? 1.359  6.343   9.701  1.00 14.04 ? 77  SER   A CB  1 
ATOM   580  O  OG  . SER   A 1 71  ? 2.227  7.214   10.393 1.00 15.99 ? 77  SER   A OG  1 
ATOM   581  N  N   . LYS   A 1 72  ? 2.947  5.573   7.160  1.00 12.91 ? 78  LYS   A N   1 
ATOM   582  C  CA  . LYS   A 1 72  ? 4.008  5.914   6.204  1.00 13.46 ? 78  LYS   A CA  1 
ATOM   583  C  C   . LYS   A 1 72  ? 4.611  7.274   6.574  1.00 14.06 ? 78  LYS   A C   1 
ATOM   584  O  O   . LYS   A 1 72  ? 3.937  8.127   7.141  1.00 16.09 ? 78  LYS   A O   1 
ATOM   585  C  CB  . LYS   A 1 72  ? 3.438  5.936   4.766  1.00 16.14 ? 78  LYS   A CB  1 
ATOM   586  C  CG  . LYS   A 1 72  ? 2.925  4.572   4.375  1.00 18.06 ? 78  LYS   A CG  1 
ATOM   587  C  CD  . LYS   A 1 72  ? 2.554  4.505   2.913  1.00 25.36 ? 78  LYS   A CD  1 
ATOM   588  C  CE  . LYS   A 1 72  ? 2.216  3.075   2.565  1.00 31.40 ? 78  LYS   A CE  1 
ATOM   589  N  NZ  . LYS   A 1 72  ? 2.158  2.854   1.097  1.00 36.43 ? 78  LYS   A NZ  1 
ATOM   590  N  N   . PRO   A 1 73  ? 5.876  7.531   6.233  1.00 13.30 ? 79  PRO   A N   1 
ATOM   591  C  CA  . PRO   A 1 73  ? 6.510  8.810   6.587  1.00 13.84 ? 79  PRO   A CA  1 
ATOM   592  C  C   . PRO   A 1 73  ? 5.721  9.999   6.038  1.00 15.24 ? 79  PRO   A C   1 
ATOM   593  O  O   . PRO   A 1 73  ? 5.389  10.040  4.841  1.00 17.00 ? 79  PRO   A O   1 
ATOM   594  C  CB  . PRO   A 1 73  ? 7.915  8.695   5.980  1.00 15.34 ? 79  PRO   A CB  1 
ATOM   595  C  CG  . PRO   A 1 73  ? 8.183  7.269   5.833  1.00 17.62 ? 79  PRO   A CG  1 
ATOM   596  C  CD  . PRO   A 1 73  ? 6.828  6.606   5.566  1.00 15.21 ? 79  PRO   A CD  1 
ATOM   597  N  N   . SER   A 1 74  ? 5.439  10.956  6.917  1.00 15.60 ? 80  SER   A N   1 
ATOM   598  C  CA  . SER   A 1 74  ? 4.510  12.060  6.618  1.00 16.84 ? 80  SER   A CA  1 
ATOM   599  C  C   . SER   A 1 74  ? 4.961  13.347  7.295  1.00 15.38 ? 80  SER   A C   1 
ATOM   600  O  O   . SER   A 1 74  ? 5.794  13.345  8.197  1.00 14.45 ? 80  SER   A O   1 
ATOM   601  C  CB  . SER   A 1 74  ? 3.083  11.734  7.138  1.00 20.96 ? 80  SER   A CB  1 
ATOM   602  O  OG  . SER   A 1 74  ? 2.671  10.388  6.972  1.00 26.72 ? 80  SER   A OG  1 
ATOM   603  N  N   . LEU   A 1 75  ? 4.254  14.454  6.953  1.00 16.78 ? 81  LEU   A N   1 
ATOM   604  C  CA  . LEU   A 1 75  ? 4.451  15.768  7.535  1.00 17.85 ? 81  LEU   A CA  1 
ATOM   605  C  C   . LEU   A 1 75  ? 3.339  15.898  8.583  1.00 17.97 ? 81  LEU   A C   1 
ATOM   606  O  O   . LEU   A 1 75  ? 2.125  15.960  8.242  1.00 20.00 ? 81  LEU   A O   1 
ATOM   607  C  CB  . LEU   A 1 75  ? 4.283  16.835  6.439  1.00 19.27 ? 81  LEU   A CB  1 
ATOM   608  C  CG  . LEU   A 1 75  ? 4.558  18.256  6.877  1.00 22.83 ? 81  LEU   A CG  1 
ATOM   609  C  CD1 . LEU   A 1 75  ? 6.036  18.447  7.228  1.00 22.56 ? 81  LEU   A CD1 1 
ATOM   610  C  CD2 . LEU   A 1 75  ? 4.149  19.250  5.766  1.00 24.54 ? 81  LEU   A CD2 1 
ATOM   611  N  N   . ILE   A 1 76  ? 3.709  15.892  9.865  1.00 16.83 ? 82  ILE   A N   1 
ATOM   612  C  CA  . ILE   A 1 76  ? 2.777  15.903  11.000 1.00 18.24 ? 82  ILE   A CA  1 
ATOM   613  C  C   . ILE   A 1 76  ? 3.044  17.032  11.957 1.00 19.31 ? 82  ILE   A C   1 
ATOM   614  O  O   . ILE   A 1 76  ? 4.213  17.301  12.277 1.00 18.43 ? 82  ILE   A O   1 
ATOM   615  C  CB  . ILE   A 1 76  ? 2.931  14.543  11.730 1.00 20.24 ? 82  ILE   A CB  1 
ATOM   616  C  CG1 . ILE   A 1 76  ? 2.667  13.369  10.757 1.00 22.18 ? 82  ILE   A CG1 1 
ATOM   617  C  CG2 . ILE   A 1 76  ? 2.103  14.475  13.009 1.00 21.51 ? 82  ILE   A CG2 1 
ATOM   618  C  CD1 . ILE   A 1 76  ? 2.755  11.987  11.324 1.00 21.49 ? 82  ILE   A CD1 1 
ATOM   619  N  N   . PHE   A 1 77  ? 1.984  17.687  12.466 1.00 19.34 ? 83  PHE   A N   1 
ATOM   620  C  CA  . PHE   A 1 77  ? 2.129  18.730  13.456 1.00 20.18 ? 83  PHE   A CA  1 
ATOM   621  C  C   . PHE   A 1 77  ? 2.377  18.091  14.791 1.00 22.04 ? 83  PHE   A C   1 
ATOM   622  O  O   . PHE   A 1 77  ? 1.616  17.215  15.216 1.00 25.49 ? 83  PHE   A O   1 
ATOM   623  C  CB  . PHE   A 1 77  ? 0.846  19.578  13.539 1.00 21.65 ? 83  PHE   A CB  1 
ATOM   624  C  CG  . PHE   A 1 77  ? 1.093  20.848  14.295 1.00 23.92 ? 83  PHE   A CG  1 
ATOM   625  C  CD1 . PHE   A 1 77  ? 1.850  21.863  13.740 1.00 25.52 ? 83  PHE   A CD1 1 
ATOM   626  C  CD2 . PHE   A 1 77  ? 0.650  20.985  15.605 1.00 27.08 ? 83  PHE   A CD2 1 
ATOM   627  C  CE1 . PHE   A 1 77  ? 2.103  23.026  14.454 1.00 27.74 ? 83  PHE   A CE1 1 
ATOM   628  C  CE2 . PHE   A 1 77  ? 0.888  22.143  16.314 1.00 28.16 ? 83  PHE   A CE2 1 
ATOM   629  C  CZ  . PHE   A 1 77  ? 1.607  23.165  15.733 1.00 28.22 ? 83  PHE   A CZ  1 
ATOM   630  N  N   . VAL   A 1 78  ? 3.498  18.441  15.414 1.00 20.20 ? 84  VAL   A N   1 
ATOM   631  C  CA  . VAL   A 1 78  ? 3.935  17.890  16.690 1.00 18.64 ? 84  VAL   A CA  1 
ATOM   632  C  C   . VAL   A 1 78  ? 3.905  18.997  17.722 1.00 18.44 ? 84  VAL   A C   1 
ATOM   633  O  O   . VAL   A 1 78  ? 4.432  20.083  17.471 1.00 19.25 ? 84  VAL   A O   1 
ATOM   634  C  CB  . VAL   A 1 78  ? 5.384  17.301  16.562 1.00 16.98 ? 84  VAL   A CB  1 
ATOM   635  C  CG1 . VAL   A 1 78  ? 5.871  16.739  17.909 1.00 16.80 ? 84  VAL   A CG1 1 
ATOM   636  C  CG2 . VAL   A 1 78  ? 5.429  16.202  15.494 1.00 18.00 ? 84  VAL   A CG2 1 
ATOM   637  N  N   . GLU   A 1 79  ? 3.354  18.691  18.912 1.00 18.42 ? 85  GLU   A N   1 
ATOM   638  C  CA  . GLU   A 1 79  ? 3.286  19.669  19.984 1.00 19.44 ? 85  GLU   A CA  1 
ATOM   639  C  C   . GLU   A 1 79  ? 4.672  20.011  20.519 1.00 19.55 ? 85  GLU   A C   1 
ATOM   640  O  O   . GLU   A 1 79  ? 5.650  19.277  20.320 1.00 18.86 ? 85  GLU   A O   1 
ATOM   641  C  CB  . GLU   A 1 79  ? 2.374  19.177  21.127 1.00 22.15 ? 85  GLU   A CB  1 
ATOM   642  C  CG  . GLU   A 1 79  ? 0.891  19.061  20.733 1.00 25.86 ? 85  GLU   A CG  1 
ATOM   643  C  CD  . GLU   A 1 79  ? 0.292  20.332  20.146 1.00 32.57 ? 85  GLU   A CD  1 
ATOM   644  O  OE1 . GLU   A 1 79  ? 0.579  21.442  20.657 1.00 35.53 ? 85  GLU   A OE1 1 
ATOM   645  O  OE2 . GLU   A 1 79  ? -0.456 20.217  19.151 1.00 38.17 ? 85  GLU   A OE2 1 
ATOM   646  N  N   . ALA   A 1 80  ? 4.739  21.150  21.212 1.00 20.55 ? 86  ALA   A N   1 
ATOM   647  C  CA  . ALA   A 1 80  ? 5.979  21.641  21.789 1.00 21.18 ? 86  ALA   A CA  1 
ATOM   648  C  C   . ALA   A 1 80  ? 6.564  20.658  22.770 1.00 21.66 ? 86  ALA   A C   1 
ATOM   649  O  O   . ALA   A 1 80  ? 5.857  19.927  23.485 1.00 22.95 ? 86  ALA   A O   1 
ATOM   650  C  CB  . ALA   A 1 80  ? 5.700  22.945  22.526 1.00 22.86 ? 86  ALA   A CB  1 
ATOM   651  N  N   . SER   A 1 81  ? 7.884  20.629  22.790 1.00 20.72 ? 87  SER   A N   1 
ATOM   652  C  CA  . SER   A 1 81  ? 8.613  19.829  23.753 1.00 21.28 ? 87  SER   A CA  1 
ATOM   653  C  C   . SER   A 1 81  ? 9.690  20.773  24.376 1.00 22.67 ? 87  SER   A C   1 
ATOM   654  O  O   . SER   A 1 81  ? 9.719  21.957  24.092 1.00 22.55 ? 87  SER   A O   1 
ATOM   655  C  CB  . SER   A 1 81  ? 9.277  18.634  23.061 1.00 20.85 ? 87  SER   A CB  1 
ATOM   656  O  OG  . SER   A 1 81  ? 10.371 19.086  22.277 1.00 19.97 ? 87  SER   A OG  1 
ATOM   657  N  N   . GLU   A 1 82  ? 10.619 20.230  25.157 1.00 23.37 ? 88  GLU   A N   1 
ATOM   658  C  CA  . GLU   A 1 82  ? 11.739 21.004  25.698 1.00 23.74 ? 88  GLU   A CA  1 
ATOM   659  C  C   . GLU   A 1 82  ? 12.744 21.398  24.543 1.00 21.79 ? 88  GLU   A C   1 
ATOM   660  O  O   . GLU   A 1 82  ? 13.512 22.352  24.654 1.00 23.05 ? 88  GLU   A O   1 
ATOM   661  C  CB  . GLU   A 1 82  ? 12.474 20.089  26.696 1.00 28.35 ? 88  GLU   A CB  1 
ATOM   662  C  CG  . GLU   A 1 82  ? 13.656 20.703  27.410 1.00 36.57 ? 88  GLU   A CG  1 
ATOM   663  C  CD  . GLU   A 1 82  ? 14.422 19.721  28.280 1.00 45.74 ? 88  GLU   A CD  1 
ATOM   664  O  OE1 . GLU   A 1 82  ? 13.813 18.728  28.747 1.00 44.14 ? 88  GLU   A OE1 1 
ATOM   665  O  OE2 . GLU   A 1 82  ? 15.634 19.949  28.501 1.00 50.02 ? 88  GLU   A OE2 1 
ATOM   666  N  N   . TYR   A 1 83  ? 12.674 20.686  23.408 1.00 19.92 ? 89  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 83  ? 13.646 20.810  22.325 1.00 18.01 ? 89  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 83  ? 13.154 21.540  21.081 1.00 17.38 ? 89  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 83  ? 13.966 22.063  20.293 1.00 17.97 ? 89  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 83  ? 14.161 19.407  21.963 1.00 17.83 ? 89  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 83  ? 14.849 18.766  23.143 1.00 19.26 ? 89  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 83  ? 16.156 19.097  23.475 1.00 21.46 ? 89  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 83  ? 14.184 17.858  23.952 1.00 20.73 ? 89  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 83  ? 16.812 18.476  24.534 1.00 23.57 ? 89  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 83  ? 14.816 17.262  25.032 1.00 22.79 ? 89  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 83  ? 16.123 17.578  25.328 1.00 25.56 ? 89  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 83  ? 16.736 16.944  26.383 1.00 29.10 ? 89  TYR   A OH  1 
ATOM   678  N  N   . TYR   A 1 84  ? 11.842 21.514  20.863 1.00 18.53 ? 90  TYR   A N   1 
ATOM   679  C  CA  . TYR   A 1 84  ? 11.295 22.190  19.695 1.00 18.18 ? 90  TYR   A CA  1 
ATOM   680  C  C   . TYR   A 1 84  ? 9.995  22.852  20.070 1.00 18.98 ? 90  TYR   A C   1 
ATOM   681  O  O   . TYR   A 1 84  ? 9.227  22.284  20.852 1.00 18.46 ? 90  TYR   A O   1 
ATOM   682  C  CB  . TYR   A 1 84  ? 10.982 21.192  18.568 1.00 17.07 ? 90  TYR   A CB  1 
ATOM   683  C  CG  . TYR   A 1 84  ? 12.175 20.451  17.989 1.00 16.03 ? 90  TYR   A CG  1 
ATOM   684  C  CD1 . TYR   A 1 84  ? 13.056 21.082  17.124 1.00 15.45 ? 90  TYR   A CD1 1 
ATOM   685  C  CD2 . TYR   A 1 84  ? 12.420 19.116  18.315 1.00 15.54 ? 90  TYR   A CD2 1 
ATOM   686  C  CE1 . TYR   A 1 84  ? 14.137 20.406  16.577 1.00 14.79 ? 90  TYR   A CE1 1 
ATOM   687  C  CE2 . TYR   A 1 84  ? 13.500 18.426  17.777 1.00 15.40 ? 90  TYR   A CE2 1 
ATOM   688  C  CZ  . TYR   A 1 84  ? 14.375 19.088  16.939 1.00 14.08 ? 90  TYR   A CZ  1 
ATOM   689  O  OH  . TYR   A 1 84  ? 15.469 18.436  16.437 1.00 13.98 ? 90  TYR   A OH  1 
ATOM   690  N  N   . PRO   A 1 85  ? 9.674  24.000  19.451 1.00 19.93 ? 91  PRO   A N   1 
ATOM   691  C  CA  . PRO   A 1 85  ? 8.322  24.551  19.635 1.00 20.65 ? 91  PRO   A CA  1 
ATOM   692  C  C   . PRO   A 1 85  ? 7.341  23.651  18.860 1.00 20.27 ? 91  PRO   A C   1 
ATOM   693  O  O   . PRO   A 1 85  ? 7.777  22.758  18.075 1.00 19.69 ? 91  PRO   A O   1 
ATOM   694  C  CB  . PRO   A 1 85  ? 8.428  25.930  18.956 1.00 22.99 ? 91  PRO   A CB  1 
ATOM   695  C  CG  . PRO   A 1 85  ? 9.446  25.728  17.866 1.00 24.32 ? 91  PRO   A CG  1 
ATOM   696  C  CD  . PRO   A 1 85  ? 10.453 24.761  18.440 1.00 20.66 ? 91  PRO   A CD  1 
ATOM   697  N  N   . ALA   A 1 86  ? 6.027  23.855  19.004 1.00 21.55 ? 92  ALA   A N   1 
ATOM   698  C  CA  . ALA   A 1 86  ? 5.044  23.122  18.218 1.00 21.68 ? 92  ALA   A CA  1 
ATOM   699  C  C   . ALA   A 1 86  ? 5.299  23.496  16.741 1.00 22.70 ? 92  ALA   A C   1 
ATOM   700  O  O   . ALA   A 1 86  ? 5.535  24.680  16.425 1.00 24.38 ? 92  ALA   A O   1 
ATOM   701  C  CB  . ALA   A 1 86  ? 3.634  23.529  18.643 1.00 23.21 ? 92  ALA   A CB  1 
ATOM   702  N  N   . ARG   A 1 87  ? 5.409  22.491  15.885 1.00 22.68 ? 93  ARG   A N   1 
ATOM   703  C  CA  . ARG   A 1 87  ? 5.777  22.718  14.497 1.00 22.17 ? 93  ARG   A CA  1 
ATOM   704  C  C   . ARG   A 1 87  ? 5.447  21.476  13.681 1.00 21.09 ? 93  ARG   A C   1 
ATOM   705  O  O   . ARG   A 1 87  ? 5.136  20.409  14.230 1.00 21.87 ? 93  ARG   A O   1 
ATOM   706  C  CB  . ARG   A 1 87  ? 7.306  22.969  14.415 1.00 23.27 ? 93  ARG   A CB  1 
ATOM   707  C  CG  . ARG   A 1 87  ? 8.073  21.639  14.697 1.00 24.33 ? 93  ARG   A CG  1 
ATOM   708  C  CD  . ARG   A 1 87  ? 9.471  21.780  15.061 1.00 23.58 ? 93  ARG   A CD  1 
ATOM   709  N  NE  . ARG   A 1 87  ? 10.347 20.688  14.628 1.00 21.00 ? 93  ARG   A NE  1 
ATOM   710  C  CZ  . ARG   A 1 87  ? 10.411 19.423  15.003 1.00 22.95 ? 93  ARG   A CZ  1 
ATOM   711  N  NH1 . ARG   A 1 87  ? 9.417  18.877  15.735 1.00 21.58 ? 93  ARG   A NH1 1 
ATOM   712  N  NH2 . ARG   A 1 87  ? 11.407 18.653  14.555 1.00 18.85 ? 93  ARG   A NH2 1 
ATOM   713  N  N   . TYR   A 1 88  ? 5.591  21.599  12.360 1.00 20.87 ? 94  TYR   A N   1 
ATOM   714  C  CA  . TYR   A 1 88  ? 5.480  20.452  11.487 1.00 21.06 ? 94  TYR   A CA  1 
ATOM   715  C  C   . TYR   A 1 88  ? 6.813  19.728  11.438 1.00 19.25 ? 94  TYR   A C   1 
ATOM   716  O  O   . TYR   A 1 88  ? 7.854  20.353  11.210 1.00 20.68 ? 94  TYR   A O   1 
ATOM   717  C  CB  . TYR   A 1 88  ? 5.100  20.884  10.084 1.00 22.67 ? 94  TYR   A CB  1 
ATOM   718  C  CG  . TYR   A 1 88  ? 3.615  21.164  9.997  1.00 23.30 ? 94  TYR   A CG  1 
ATOM   719  C  CD1 . TYR   A 1 88  ? 2.697  20.129  9.924  1.00 24.24 ? 94  TYR   A CD1 1 
ATOM   720  C  CD2 . TYR   A 1 88  ? 3.120  22.451  10.126 1.00 24.41 ? 94  TYR   A CD2 1 
ATOM   721  C  CE1 . TYR   A 1 88  ? 1.333  20.364  9.898  1.00 25.86 ? 94  TYR   A CE1 1 
ATOM   722  C  CE2 . TYR   A 1 88  ? 1.748  22.697  10.129 1.00 25.35 ? 94  TYR   A CE2 1 
ATOM   723  C  CZ  . TYR   A 1 88  ? 0.857  21.648  10.012 1.00 26.70 ? 94  TYR   A CZ  1 
ATOM   724  O  OH  . TYR   A 1 88  ? -0.501 21.826  9.987  1.00 29.70 ? 94  TYR   A OH  1 
ATOM   725  N  N   . GLN   A 1 89  ? 6.799  18.380  11.668 1.00 17.09 ? 95  GLN   A N   1 
ATOM   726  C  CA  . GLN   A 1 89  ? 7.989  17.518  11.569 1.00 15.12 ? 95  GLN   A CA  1 
ATOM   727  C  C   . GLN   A 1 89  ? 7.774  16.655  10.338 1.00 14.82 ? 95  GLN   A C   1 
ATOM   728  O  O   . GLN   A 1 89  ? 6.685  16.074  10.143 1.00 16.33 ? 95  GLN   A O   1 
ATOM   729  C  CB  . GLN   A 1 89  ? 8.190  16.695  12.849 1.00 15.84 ? 95  GLN   A CB  1 
ATOM   730  C  CG  . GLN   A 1 89  ? 9.426  15.807  12.742 1.00 15.75 ? 95  GLN   A CG  1 
ATOM   731  C  CD  . GLN   A 1 89  ? 9.989  15.305  14.050 1.00 14.48 ? 95  GLN   A CD  1 
ATOM   732  O  OE1 . GLN   A 1 89  ? 10.524 14.166  14.105 1.00 14.90 ? 95  GLN   A OE1 1 
ATOM   733  N  NE2 . GLN   A 1 89  ? 9.985  16.074  15.096 1.00 12.69 ? 95  GLN   A NE2 1 
ATOM   734  N  N   . SER   A 1 90  ? 8.795  16.588  9.474  1.00 13.95 ? 96  SER   A N   1 
ATOM   735  C  CA  . SER   A 1 90  ? 8.690  15.824  8.252  1.00 14.01 ? 96  SER   A CA  1 
ATOM   736  C  C   . SER   A 1 90  ? 9.282  14.401  8.418  1.00 12.95 ? 96  SER   A C   1 
ATOM   737  O  O   . SER   A 1 90  ? 10.045 14.132  9.354  1.00 12.55 ? 96  SER   A O   1 
ATOM   738  C  CB  . SER   A 1 90  ? 9.408  16.564  7.124  1.00 16.06 ? 96  SER   A CB  1 
ATOM   739  O  OG  . SER   A 1 90  ? 10.782 16.646  7.435  1.00 18.26 ? 96  SER   A OG  1 
ATOM   740  N  N   . HIS   A 1 91  ? 8.909  13.525  7.473  1.00 12.93 ? 97  HIS   A N   1 
ATOM   741  C  CA  . HIS   A 1 91  ? 9.395  12.139  7.431  1.00 12.77 ? 97  HIS   A CA  1 
ATOM   742  C  C   . HIS   A 1 91  ? 9.125  11.396  8.743  1.00 11.81 ? 97  HIS   A C   1 
ATOM   743  O  O   . HIS   A 1 91  ? 9.962  10.564  9.171  1.00 12.63 ? 97  HIS   A O   1 
ATOM   744  C  CB  . HIS   A 1 91  ? 10.909 12.111  7.053  1.00 14.48 ? 97  HIS   A CB  1 
ATOM   745  C  CG  . HIS   A 1 91  ? 11.220 12.715  5.716  1.00 14.43 ? 97  HIS   A CG  1 
ATOM   746  N  ND1 . HIS   A 1 91  ? 11.319 11.936  4.585  1.00 15.91 ? 97  HIS   A ND1 1 
ATOM   747  C  CD2 . HIS   A 1 91  ? 11.351 14.017  5.359  1.00 16.83 ? 97  HIS   A CD2 1 
ATOM   748  C  CE1 . HIS   A 1 91  ? 11.558 12.782  3.568  1.00 17.58 ? 97  HIS   A CE1 1 
ATOM   749  N  NE2 . HIS   A 1 91  ? 11.593 14.037  3.996  1.00 18.44 ? 97  HIS   A NE2 1 
ATOM   750  N  N   . LEU   A 1 92  ? 8.009  11.650  9.362  1.00 11.62 ? 98  LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 92  ? 7.652  11.109  10.674 1.00 11.52 ? 98  LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 92  ? 6.602  10.009  10.501 1.00 11.63 ? 98  LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 92  ? 5.650  10.183  9.699  1.00 12.21 ? 98  LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 92  ? 7.101  12.230  11.589 1.00 12.70 ? 98  LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 92  ? 6.791  11.829  13.045 1.00 14.39 ? 98  LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 92  ? 8.035  11.492  13.803 1.00 14.47 ? 98  LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 92  ? 6.037  12.984  13.785 1.00 17.46 ? 98  LEU   A CD2 1 
ATOM   758  N  N   . MET   A 1 93  ? 6.722  8.917   11.280 1.00 10.86 ? 99  MET   A N   1 
ATOM   759  C  CA  . MET   A 1 93  ? 5.765  7.786   11.244 1.00 11.11 ? 99  MET   A CA  1 
ATOM   760  C  C   . MET   A 1 93  ? 5.178  7.634   12.622 1.00 10.78 ? 99  MET   A C   1 
ATOM   761  O  O   . MET   A 1 93  ? 5.931  7.670   13.605 1.00 11.91 ? 99  MET   A O   1 
ATOM   762  C  CB  . MET   A 1 93  ? 6.515  6.511   10.880 1.00 11.45 ? 99  MET   A CB  1 
ATOM   763  C  CG  . MET   A 1 93  ? 7.155  6.617   9.518  1.00 12.89 ? 99  MET   A CG  1 
ATOM   764  S  SD  . MET   A 1 93  ? 8.267  5.258   9.074  1.00 15.11 ? 99  MET   A SD  1 
ATOM   765  C  CE  . MET   A 1 93  ? 9.604  5.549   10.307 1.00 15.94 ? 99  MET   A CE  1 
ATOM   766  N  N   . LEU   A 1 94  ? 3.873  7.438   12.760 1.00 10.64 ? 100 LEU   A N   1 
ATOM   767  C  CA  . LEU   A 1 94  ? 3.264  7.291   14.075 1.00 11.63 ? 100 LEU   A CA  1 
ATOM   768  C  C   . LEU   A 1 94  ? 2.764  5.862   14.328 1.00 10.69 ? 100 LEU   A C   1 
ATOM   769  O  O   . LEU   A 1 94  ? 2.327  5.161   13.390 1.00 12.48 ? 100 LEU   A O   1 
ATOM   770  C  CB  . LEU   A 1 94  ? 2.035  8.228   14.234 1.00 13.78 ? 100 LEU   A CB  1 
ATOM   771  C  CG  . LEU   A 1 94  ? 2.299  9.717   14.223 1.00 17.26 ? 100 LEU   A CG  1 
ATOM   772  C  CD1 . LEU   A 1 94  ? 1.004  10.530  14.540 1.00 19.32 ? 100 LEU   A CD1 1 
ATOM   773  C  CD2 . LEU   A 1 94  ? 3.363  10.136  15.228 1.00 20.59 ? 100 LEU   A CD2 1 
ATOM   774  N  N   . ALA   A 1 95  ? 2.817  5.447   15.563 1.00 10.95 ? 101 ALA   A N   1 
ATOM   775  C  CA  . ALA   A 1 95  ? 2.286  4.153   16.020 1.00 10.42 ? 101 ALA   A CA  1 
ATOM   776  C  C   . ALA   A 1 95  ? 1.657  4.343   17.399 1.00 10.65 ? 101 ALA   A C   1 
ATOM   777  O  O   . ALA   A 1 95  ? 1.942  5.344   18.103 1.00 10.72 ? 101 ALA   A O   1 
ATOM   778  C  CB  . ALA   A 1 95  ? 3.424  3.092   16.135 1.00 11.19 ? 101 ALA   A CB  1 
ATOM   779  N  N   . VAL   A 1 96  ? 0.867  3.367   17.825 1.00 10.48 ? 102 VAL   A N   1 
ATOM   780  C  CA  . VAL   A 1 96  ? 0.347  3.341   19.166 1.00 10.18 ? 102 VAL   A CA  1 
ATOM   781  C  C   . VAL   A 1 96  ? 1.385  2.579   20.030 1.00 11.43 ? 102 VAL   A C   1 
ATOM   782  O  O   . VAL   A 1 96  ? 1.679  1.404   19.787 1.00 13.51 ? 102 VAL   A O   1 
ATOM   783  C  CB  . VAL   A 1 96  ? -1.028 2.636   19.190 1.00 10.18 ? 102 VAL   A CB  1 
ATOM   784  C  CG1 . VAL   A 1 96  ? -1.526 2.448   20.648 1.00 11.55 ? 102 VAL   A CG1 1 
ATOM   785  C  CG2 . VAL   A 1 96  ? -2.010 3.424   18.308 1.00 10.41 ? 102 VAL   A CG2 1 
ATOM   786  N  N   . GLY   A 1 97  ? 1.867  3.288   21.032 1.00 11.89 ? 103 GLY   A N   1 
ATOM   787  C  CA  . GLY   A 1 97  ? 2.851  2.704   21.933 1.00 12.85 ? 103 GLY   A CA  1 
ATOM   788  C  C   . GLY   A 1 97  ? 3.326  3.730   22.903 1.00 13.98 ? 103 GLY   A C   1 
ATOM   789  O  O   . GLY   A 1 97  ? 3.087  4.907   22.794 1.00 15.09 ? 103 GLY   A O   1 
ATOM   790  N  N   . HIS   A 1 98  ? 3.961  3.198   23.984 1.00 15.29 ? 104 HIS   A N   1 
ATOM   791  C  CA  . HIS   A 1 98  ? 4.469  4.032   25.017 1.00 15.45 ? 104 HIS   A CA  1 
ATOM   792  C  C   . HIS   A 1 98  ? 5.729  4.748   24.635 1.00 14.80 ? 104 HIS   A C   1 
ATOM   793  O  O   . HIS   A 1 98  ? 6.675  4.117   24.097 1.00 14.82 ? 104 HIS   A O   1 
ATOM   794  C  CB  . HIS   A 1 98  ? 4.676  3.204   26.329 1.00 15.41 ? 104 HIS   A CB  1 
ATOM   795  C  CG  . HIS   A 1 98  ? 5.056  4.086   27.471 1.00 15.89 ? 104 HIS   A CG  1 
ATOM   796  N  ND1 . HIS   A 1 98  ? 4.144  4.944   28.040 1.00 16.11 ? 104 HIS   A ND1 1 
ATOM   797  C  CD2 . HIS   A 1 98  ? 6.258  4.287   28.067 1.00 16.91 ? 104 HIS   A CD2 1 
ATOM   798  C  CE1 . HIS   A 1 98  ? 4.822  5.618   28.968 1.00 16.67 ? 104 HIS   A CE1 1 
ATOM   799  N  NE2 . HIS   A 1 98  ? 6.096  5.246   28.999 1.00 17.82 ? 104 HIS   A NE2 1 
ATOM   800  N  N   . SER   A 1 99  ? 5.815  5.980   24.921 1.00 15.53 ? 105 SER   A N   1 
ATOM   801  C  CA  . SER   A 1 99  ? 6.974  6.742   24.799 1.00 15.84 ? 105 SER   A CA  1 
ATOM   802  C  C   . SER   A 1 99  ? 6.970  7.878   25.823 1.00 17.06 ? 105 SER   A C   1 
ATOM   803  O  O   . SER   A 1 99  ? 5.856  8.342   26.180 1.00 20.23 ? 105 SER   A O   1 
ATOM   804  C  CB  . SER   A 1 99  ? 7.221  7.187   23.366 1.00 16.25 ? 105 SER   A CB  1 
ATOM   805  O  OG  . SER   A 1 99  ? 6.138  7.959   22.921 1.00 19.90 ? 105 SER   A OG  1 
ATOM   806  N  N   . GLU   A 1 100 ? 8.201  8.261   26.273 1.00 13.87 ? 106 GLU   A N   1 
ATOM   807  C  CA  . GLU   A 1 100 ? 8.603  9.396   27.147 1.00 15.60 ? 106 GLU   A CA  1 
ATOM   808  C  C   . GLU   A 1 100 ? 9.805  10.077  26.507 1.00 16.12 ? 106 GLU   A C   1 
ATOM   809  O  O   . GLU   A 1 100 ? 10.451 9.532   25.596 1.00 15.43 ? 106 GLU   A O   1 
ATOM   810  C  CB  . GLU   A 1 100 ? 8.984  8.882   28.546 1.00 17.65 ? 106 GLU   A CB  1 
ATOM   811  C  CG  . GLU   A 1 100 ? 7.790  8.226   29.205 1.00 18.53 ? 106 GLU   A CG  1 
ATOM   812  C  CD  . GLU   A 1 100 ? 8.044  7.602   30.580 1.00 18.80 ? 106 GLU   A CD  1 
ATOM   813  O  OE1 . GLU   A 1 100 ? 8.891  8.121   31.343 1.00 23.98 ? 106 GLU   A OE1 1 
ATOM   814  O  OE2 . GLU   A 1 100 ? 7.385  6.592   30.898 1.00 17.98 ? 106 GLU   A OE2 1 
ATOM   815  N  N   . PRO   A 1 101 ? 10.123 11.342  26.880 1.00 16.84 ? 107 PRO   A N   1 
ATOM   816  C  CA  . PRO   A 1 101 ? 11.198 12.069  26.154 1.00 15.95 ? 107 PRO   A CA  1 
ATOM   817  C  C   . PRO   A 1 101 ? 12.517 11.330  26.019 1.00 15.07 ? 107 PRO   A C   1 
ATOM   818  O  O   . PRO   A 1 101 ? 13.092 11.285  24.923 1.00 15.07 ? 107 PRO   A O   1 
ATOM   819  C  CB  . PRO   A 1 101 ? 11.340 13.386  26.952 1.00 18.36 ? 107 PRO   A CB  1 
ATOM   820  C  CG  . PRO   A 1 101 ? 9.979  13.603  27.471 1.00 20.63 ? 107 PRO   A CG  1 
ATOM   821  C  CD  . PRO   A 1 101 ? 9.429  12.229  27.846 1.00 18.46 ? 107 PRO   A CD  1 
ATOM   822  N  N   . GLY   A 1 102 ? 12.994 10.699  27.089 1.00 14.43 ? 108 GLY   A N   1 
ATOM   823  C  CA  . GLY   A 1 102 ? 14.236 9.944   27.084 1.00 14.00 ? 108 GLY   A CA  1 
ATOM   824  C  C   . GLY   A 1 102 ? 14.197 8.646   26.281 1.00 12.09 ? 108 GLY   A C   1 
ATOM   825  O  O   . GLY   A 1 102 ? 15.218 7.997   26.099 1.00 12.68 ? 108 GLY   A O   1 
ATOM   826  N  N   . ASP   A 1 103 ? 13.008 8.263   25.732 1.00 10.93 ? 109 ASP   A N   1 
ATOM   827  C  CA  . ASP   A 1 103 ? 12.932 7.113   24.805 1.00 9.99  ? 109 ASP   A CA  1 
ATOM   828  C  C   . ASP   A 1 103 ? 13.451 7.472   23.412 1.00 9.92  ? 109 ASP   A C   1 
ATOM   829  O  O   . ASP   A 1 103 ? 13.701 6.560   22.592 1.00 9.79  ? 109 ASP   A O   1 
ATOM   830  C  CB  . ASP   A 1 103 ? 11.472 6.615   24.691 1.00 10.22 ? 109 ASP   A CB  1 
ATOM   831  C  CG  . ASP   A 1 103 ? 11.074 5.853   25.941 1.00 10.24 ? 109 ASP   A CG  1 
ATOM   832  O  OD1 . ASP   A 1 103 ? 11.949 5.146   26.497 1.00 11.55 ? 109 ASP   A OD1 1 
ATOM   833  O  OD2 . ASP   A 1 103 ? 9.877  5.957   26.354 1.00 10.98 ? 109 ASP   A OD2 1 
ATOM   834  N  N   . CYS   A 1 104 ? 13.689 8.774   23.132 1.00 10.08 ? 110 CYS   A N   1 
ATOM   835  C  CA  . CYS   A 1 104 ? 14.272 9.146   21.822 1.00 10.22 ? 110 CYS   A CA  1 
ATOM   836  C  C   . CYS   A 1 104 ? 15.563 8.416   21.559 1.00 9.25  ? 110 CYS   A C   1 
ATOM   837  O  O   . CYS   A 1 104 ? 16.397 8.276   22.450 1.00 10.34 ? 110 CYS   A O   1 
ATOM   838  C  CB  . CYS   A 1 104 ? 14.491 10.652  21.756 1.00 10.28 ? 110 CYS   A CB  1 
ATOM   839  S  SG  . CYS   A 1 104 ? 12.936 11.594  21.538 1.00 12.80 ? 110 CYS   A SG  1 
ATOM   840  N  N   . GLY   A 1 105 ? 15.722 7.910   20.330 1.00 8.61  ? 111 GLY   A N   1 
ATOM   841  C  CA  . GLY   A 1 105 ? 16.904 7.170   19.940 1.00 9.36  ? 111 GLY   A CA  1 
ATOM   842  C  C   . GLY   A 1 105 ? 16.703 5.667   19.868 1.00 9.00  ? 111 GLY   A C   1 
ATOM   843  O  O   . GLY   A 1 105 ? 17.552 4.982   19.296 1.00 9.89  ? 111 GLY   A O   1 
ATOM   844  N  N   . GLY   A 1 106 ? 15.621 5.166   20.480 1.00 8.85  ? 112 GLY   A N   1 
ATOM   845  C  CA  . GLY   A 1 106 ? 15.345 3.735   20.378 1.00 8.65  ? 112 GLY   A CA  1 
ATOM   846  C  C   . GLY   A 1 106 ? 15.087 3.343   18.920 1.00 7.34  ? 112 GLY   A C   1 
ATOM   847  O  O   . GLY   A 1 106 ? 14.381 4.085   18.187 1.00 8.35  ? 112 GLY   A O   1 
ATOM   848  N  N   . ILE   A 1 107 ? 15.576 2.188   18.496 1.00 7.83  ? 113 ILE   A N   1 
ATOM   849  C  CA  . ILE   A 1 107 ? 15.427 1.794   17.106 1.00 7.91  ? 113 ILE   A CA  1 
ATOM   850  C  C   . ILE   A 1 107 ? 14.081 1.148   16.829 1.00 7.35  ? 113 ILE   A C   1 
ATOM   851  O  O   . ILE   A 1 107 ? 13.620 0.287   17.608 1.00 7.97  ? 113 ILE   A O   1 
ATOM   852  C  CB  . ILE   A 1 107 ? 16.574 0.812   16.726 1.00 8.50  ? 113 ILE   A CB  1 
ATOM   853  C  CG1 . ILE   A 1 107 ? 17.856 1.667   16.469 1.00 10.22 ? 113 ILE   A CG1 1 
ATOM   854  C  CG2 . ILE   A 1 107 ? 16.249 -0.067  15.494 1.00 9.23  ? 113 ILE   A CG2 1 
ATOM   855  C  CD1 . ILE   A 1 107 ? 19.125 0.836   16.295 1.00 12.53 ? 113 ILE   A CD1 1 
ATOM   856  N  N   . LEU   A 1 108 ? 13.501 1.475   15.670 1.00 7.07  ? 114 LEU   A N   1 
ATOM   857  C  CA  . LEU   A 1 108 ? 12.396 0.753   15.029 1.00 7.48  ? 114 LEU   A CA  1 
ATOM   858  C  C   . LEU   A 1 108 ? 13.007 -0.069  13.885 1.00 7.36  ? 114 LEU   A C   1 
ATOM   859  O  O   . LEU   A 1 108 ? 13.780 0.477   13.072 1.00 7.73  ? 114 LEU   A O   1 
ATOM   860  C  CB  . LEU   A 1 108 ? 11.405 1.775   14.442 1.00 7.50  ? 114 LEU   A CB  1 
ATOM   861  C  CG  . LEU   A 1 108 ? 10.266 1.163   13.557 1.00 8.17  ? 114 LEU   A CG  1 
ATOM   862  C  CD1 . LEU   A 1 108 ? 9.280  0.334   14.392 1.00 9.86  ? 114 LEU   A CD1 1 
ATOM   863  C  CD2 . LEU   A 1 108 ? 9.510  2.304   12.817 1.00 10.07 ? 114 LEU   A CD2 1 
ATOM   864  N  N   . ARG   A 1 109 ? 12.688 -1.357  13.848 1.00 7.72  ? 115 ARG   A N   1 
ATOM   865  C  CA  . ARG   A 1 109 ? 13.236 -2.239  12.791 1.00 8.53  ? 115 ARG   A CA  1 
ATOM   866  C  C   . ARG   A 1 109 ? 12.146 -3.123  12.213 1.00 8.84  ? 115 ARG   A C   1 
ATOM   867  O  O   . ARG   A 1 109 ? 11.152 -3.447  12.895 1.00 9.11  ? 115 ARG   A O   1 
ATOM   868  C  CB  . ARG   A 1 109 ? 14.396 -3.102  13.361 1.00 9.35  ? 115 ARG   A CB  1 
ATOM   869  C  CG  . ARG   A 1 109 ? 13.951 -4.086  14.440 1.00 10.02 ? 115 ARG   A CG  1 
ATOM   870  C  CD  . ARG   A 1 109 ? 15.160 -4.821  15.040 1.00 11.83 ? 115 ARG   A CD  1 
ATOM   871  N  NE  . ARG   A 1 109 ? 15.948 -3.937  15.886 1.00 11.76 ? 115 ARG   A NE  1 
ATOM   872  C  CZ  . ARG   A 1 109 ? 17.250 -3.733  15.793 1.00 10.67 ? 115 ARG   A CZ  1 
ATOM   873  N  NH1 . ARG   A 1 109 ? 17.934 -4.166  14.725 1.00 12.65 ? 115 ARG   A NH1 1 
ATOM   874  N  NH2 . ARG   A 1 109 ? 17.879 -3.024  16.714 1.00 12.84 ? 115 ARG   A NH2 1 
ATOM   875  N  N   . CYS   A 1 110 ? 12.331 -3.549  10.970 1.00 11.39 ? 116 CYS   A N   1 
ATOM   876  C  CA  . CYS   A 1 110 ? 11.381 -4.446  10.282 1.00 13.43 ? 116 CYS   A CA  1 
ATOM   877  C  C   . CYS   A 1 110 ? 12.187 -5.642  9.843  1.00 15.13 ? 116 CYS   A C   1 
ATOM   878  O  O   . CYS   A 1 110 ? 13.370 -5.813  10.173 1.00 14.88 ? 116 CYS   A O   1 
ATOM   879  C  CB  . CYS   A 1 110 ? 10.718 -3.740  9.095  1.00 13.31 ? 116 CYS   A CB  1 
ATOM   880  S  SG  . CYS   A 1 110 ? 11.894 -3.364  7.775  1.00 13.30 ? 116 CYS   A SG  1 
ATOM   881  N  N   . GLN   A 1 111 ? 11.509 -6.548  9.067  1.00 15.67 ? 117 GLN   A N   1 
ATOM   882  C  CA  . GLN   A 1 111 ? 12.188 -7.702  8.527  1.00 17.57 ? 117 GLN   A CA  1 
ATOM   883  C  C   . GLN   A 1 111 ? 13.423 -7.345  7.666  1.00 19.16 ? 117 GLN   A C   1 
ATOM   884  O  O   . GLN   A 1 111 ? 14.333 -8.187  7.551  1.00 21.99 ? 117 GLN   A O   1 
ATOM   885  C  CB  . GLN   A 1 111 ? 11.207 -8.598  7.716  1.00 19.21 ? 117 GLN   A CB  1 
ATOM   886  C  CG  . GLN   A 1 111 ? 10.777 -7.948  6.410  1.00 21.72 ? 117 GLN   A CG  1 
ATOM   887  C  CD  . GLN   A 1 111 ? 9.880  -8.889  5.629  1.00 28.99 ? 117 GLN   A CD  1 
ATOM   888  O  OE1 . GLN   A 1 111 ? 8.645  -8.834  5.722  1.00 32.75 ? 117 GLN   A OE1 1 
ATOM   889  N  NE2 . GLN   A 1 111 ? 10.494 -9.779  4.851  1.00 30.55 ? 117 GLN   A NE2 1 
ATOM   890  N  N   . HIS   A 1 112 ? 13.509 -6.131  7.095  1.00 16.10 ? 118 HIS   A N   1 
ATOM   891  C  CA  . HIS   A 1 112 ? 14.629 -5.743  6.198  1.00 16.68 ? 118 HIS   A CA  1 
ATOM   892  C  C   . HIS   A 1 112 ? 15.809 -5.032  6.914  1.00 17.05 ? 118 HIS   A C   1 
ATOM   893  O  O   . HIS   A 1 112 ? 16.847 -4.778  6.297  1.00 20.00 ? 118 HIS   A O   1 
ATOM   894  C  CB  . HIS   A 1 112 ? 14.068 -4.821  5.111  1.00 16.40 ? 118 HIS   A CB  1 
ATOM   895  C  CG  . HIS   A 1 112 ? 12.924 -5.457  4.328  1.00 18.79 ? 118 HIS   A CG  1 
ATOM   896  N  ND1 . HIS   A 1 112 ? 11.602 -5.039  4.462  1.00 15.57 ? 118 HIS   A ND1 1 
ATOM   897  C  CD2 . HIS   A 1 112 ? 12.961 -6.376  3.318  1.00 21.13 ? 118 HIS   A CD2 1 
ATOM   898  C  CE1 . HIS   A 1 112 ? 10.880 -5.791  3.644  1.00 18.76 ? 118 HIS   A CE1 1 
ATOM   899  N  NE2 . HIS   A 1 112 ? 11.655 -6.618  2.947  1.00 23.05 ? 118 HIS   A NE2 1 
ATOM   900  N  N   . GLY   A 1 113 ? 15.630 -4.601  8.178  1.00 14.30 ? 119 GLY   A N   1 
ATOM   901  C  CA  . GLY   A 1 113 ? 16.680 -3.871  8.893  1.00 13.65 ? 119 GLY   A CA  1 
ATOM   902  C  C   . GLY   A 1 113 ? 16.130 -2.687  9.686  1.00 11.36 ? 119 GLY   A C   1 
ATOM   903  O  O   . GLY   A 1 113 ? 14.933 -2.660  10.006 1.00 11.54 ? 119 GLY   A O   1 
ATOM   904  N  N   . VAL   A 1 114 ? 17.010 -1.702  9.971  1.00 10.53 ? 120 VAL   A N   1 
ATOM   905  C  CA  . VAL   A 1 114 ? 16.597 -0.512  10.741 1.00 10.35 ? 120 VAL   A CA  1 
ATOM   906  C  C   . VAL   A 1 114 ? 15.754 0.414   9.891  1.00 8.47  ? 120 VAL   A C   1 
ATOM   907  O  O   . VAL   A 1 114 ? 16.141 0.781   8.766  1.00 10.00 ? 120 VAL   A O   1 
ATOM   908  C  CB  . VAL   A 1 114 ? 17.843 0.211   11.309 1.00 10.41 ? 120 VAL   A CB  1 
ATOM   909  C  CG1 . VAL   A 1 114 ? 17.458 1.544   11.972 1.00 11.29 ? 120 VAL   A CG1 1 
ATOM   910  C  CG2 . VAL   A 1 114 ? 18.606 -0.714  12.271 1.00 11.77 ? 120 VAL   A CG2 1 
ATOM   911  N  N   . VAL   A 1 115 ? 14.636 0.842   10.414 1.00 8.83  ? 121 VAL   A N   1 
ATOM   912  C  CA  . VAL   A 1 115 ? 13.689 1.717   9.763  1.00 8.63  ? 121 VAL   A CA  1 
ATOM   913  C  C   . VAL   A 1 115 ? 13.849 3.164   10.195 1.00 8.44  ? 121 VAL   A C   1 
ATOM   914  O  O   . VAL   A 1 115 ? 13.681 4.115   9.407  1.00 9.64  ? 121 VAL   A O   1 
ATOM   915  C  CB  . VAL   A 1 115 ? 12.238 1.247   10.067 1.00 9.52  ? 121 VAL   A CB  1 
ATOM   916  C  CG1 . VAL   A 1 115 ? 11.189 2.229   9.525  1.00 12.07 ? 121 VAL   A CG1 1 
ATOM   917  C  CG2 . VAL   A 1 115 ? 11.983 -0.149  9.529  1.00 11.09 ? 121 VAL   A CG2 1 
ATOM   918  N  N   . GLY   A 1 116 ? 14.043 3.381   11.507 1.00 8.55  ? 122 GLY   A N   1 
ATOM   919  C  CA  . GLY   A 1 116 ? 14.124 4.749   12.035 1.00 9.29  ? 122 GLY   A CA  1 
ATOM   920  C  C   . GLY   A 1 116 ? 14.366 4.735   13.537 1.00 7.90  ? 122 GLY   A C   1 
ATOM   921  O  O   . GLY   A 1 116 ? 14.668 3.672   14.120 1.00 8.65  ? 122 GLY   A O   1 
ATOM   922  N  N   . ILE   A 1 117 ? 14.285 5.917   14.168 1.00 8.14  ? 123 ILE   A N   1 
ATOM   923  C  CA  . ILE   A 1 117 ? 14.496 6.039   15.628 1.00 7.82  ? 123 ILE   A CA  1 
ATOM   924  C  C   . ILE   A 1 117 ? 13.355 6.814   16.259 1.00 8.14  ? 123 ILE   A C   1 
ATOM   925  O  O   . ILE   A 1 117 ? 12.776 7.736   15.623 1.00 8.99  ? 123 ILE   A O   1 
ATOM   926  C  CB  . ILE   A 1 117 ? 15.857 6.723   15.980 1.00 8.59  ? 123 ILE   A CB  1 
ATOM   927  C  CG1 . ILE   A 1 117 ? 16.035 8.058   15.252 1.00 10.28 ? 123 ILE   A CG1 1 
ATOM   928  C  CG2 . ILE   A 1 117 ? 16.986 5.747   15.752 1.00 10.31 ? 123 ILE   A CG2 1 
ATOM   929  C  CD1 . ILE   A 1 117 ? 17.300 8.845   15.748 1.00 10.99 ? 123 ILE   A CD1 1 
ATOM   930  N  N   . VAL   A 1 118 ? 13.060 6.540   17.533 1.00 8.09  ? 124 VAL   A N   1 
ATOM   931  C  CA  . VAL   A 1 118 ? 12.029 7.277   18.249 1.00 8.50  ? 124 VAL   A CA  1 
ATOM   932  C  C   . VAL   A 1 118 ? 12.419 8.762   18.273 1.00 8.91  ? 124 VAL   A C   1 
ATOM   933  O  O   . VAL   A 1 118 ? 13.590 9.117   18.568 1.00 8.82  ? 124 VAL   A O   1 
ATOM   934  C  CB  . VAL   A 1 118 ? 11.910 6.774   19.707 1.00 8.73  ? 124 VAL   A CB  1 
ATOM   935  C  CG1 . VAL   A 1 118 ? 10.929 7.632   20.539 1.00 9.22  ? 124 VAL   A CG1 1 
ATOM   936  C  CG2 . VAL   A 1 118 ? 11.447 5.303   19.746 1.00 9.37  ? 124 VAL   A CG2 1 
ATOM   937  N  N   . SER   A 1 119 ? 11.446 9.643   18.009 1.00 9.18  ? 125 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 119 ? 11.622 11.100  17.995 1.00 10.31 ? 125 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 119 ? 10.514 11.834  18.721 1.00 11.82 ? 125 SER   A C   1 
ATOM   940  O  O   . SER   A 1 119 ? 10.813 12.938  19.295 1.00 14.25 ? 125 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 119 ? 11.768 11.573  16.558 1.00 10.77 ? 125 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 119 ? 11.845 13.003  16.454 1.00 13.74 ? 125 SER   A OG  1 
ATOM   943  N  N   . THR   A 1 120 ? 9.253  11.323  18.722 1.00 12.10 ? 126 THR   A N   1 
ATOM   944  C  CA  . THR   A 1 120 ? 8.149  12.072  19.366 1.00 12.88 ? 126 THR   A CA  1 
ATOM   945  C  C   . THR   A 1 120 ? 7.299  11.119  20.207 1.00 15.04 ? 126 THR   A C   1 
ATOM   946  O  O   . THR   A 1 120 ? 7.456  9.882   20.088 1.00 12.48 ? 126 THR   A O   1 
ATOM   947  C  CB  . THR   A 1 120 ? 7.253  12.768  18.282 1.00 13.10 ? 126 THR   A CB  1 
ATOM   948  O  OG1 . THR   A 1 120 ? 6.494  11.766  17.578 1.00 13.56 ? 126 THR   A OG1 1 
ATOM   949  C  CG2 . THR   A 1 120 ? 8.026  13.599  17.292 1.00 13.10 ? 126 THR   A CG2 1 
ATOM   950  N  N   . GLY   A 1 121 ? 6.387  11.649  21.030 1.00 18.00 ? 127 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 121 ? 5.488  10.785  21.771 1.00 21.17 ? 127 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 121 ? 4.482  11.481  22.667 1.00 21.69 ? 127 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 121 ? 4.468  12.705  22.717 1.00 23.83 ? 127 GLY   A O   1 
ATOM   954  N  N   . GLY   A 1 122 ? 3.728  10.640  23.395 1.00 21.11 ? 128 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 122 ? 2.714  11.046  24.378 1.00 19.42 ? 128 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 122 ? 1.380  10.339  24.186 1.00 19.78 ? 128 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 122 ? 1.000  10.009  23.054 1.00 20.54 ? 128 GLY   A O   1 
ATOM   958  N  N   . ASN   A 1 123 ? 0.599  10.257  25.267 1.00 18.43 ? 129 ASN   A N   1 
ATOM   959  C  CA  . ASN   A 1 123 ? -0.782 9.749   25.276 1.00 19.67 ? 129 ASN   A CA  1 
ATOM   960  C  C   . ASN   A 1 123 ? -0.963 8.449   24.493 1.00 19.38 ? 129 ASN   A C   1 
ATOM   961  O  O   . ASN   A 1 123 ? -2.007 8.261   23.837 1.00 20.60 ? 129 ASN   A O   1 
ATOM   962  C  CB  . ASN   A 1 123 ? -1.703 10.836  24.715 1.00 21.59 ? 129 ASN   A CB  1 
ATOM   963  C  CG  . ASN   A 1 123 ? -1.688 12.099  25.524 1.00 24.83 ? 129 ASN   A CG  1 
ATOM   964  O  OD1 . ASN   A 1 123 ? -1.933 12.052  26.731 1.00 28.10 ? 129 ASN   A OD1 1 
ATOM   965  N  ND2 . ASN   A 1 123 ? -1.412 13.234  24.869 1.00 24.66 ? 129 ASN   A ND2 1 
ATOM   966  N  N   . GLY   A 1 124 ? -0.038 7.515   24.635 1.00 16.73 ? 130 GLY   A N   1 
ATOM   967  C  CA  . GLY   A 1 124 ? -0.147 6.221   23.997 1.00 16.41 ? 130 GLY   A CA  1 
ATOM   968  C  C   . GLY   A 1 124 ? 0.257  6.255   22.538 1.00 12.41 ? 130 GLY   A C   1 
ATOM   969  O  O   . GLY   A 1 124 ? 0.094  5.232   21.931 1.00 15.33 ? 130 GLY   A O   1 
ATOM   970  N  N   . LEU   A 1 125 ? 0.869  7.354   22.045 1.00 14.08 ? 131 LEU   A N   1 
ATOM   971  C  CA  . LEU   A 1 125 ? 1.494  7.392   20.681 1.00 13.24 ? 131 LEU   A CA  1 
ATOM   972  C  C   . LEU   A 1 125 ? 3.029  7.428   20.772 1.00 12.80 ? 131 LEU   A C   1 
ATOM   973  O  O   . LEU   A 1 125 ? 3.604  7.925   21.783 1.00 15.07 ? 131 LEU   A O   1 
ATOM   974  C  CB  . LEU   A 1 125 ? 1.006  8.596   19.889 1.00 13.73 ? 131 LEU   A CB  1 
ATOM   975  C  CG  . LEU   A 1 125 ? -0.527 8.553   19.614 1.00 14.70 ? 131 LEU   A CG  1 
ATOM   976  C  CD1 . LEU   A 1 125 ? -1.089 9.937   19.306 1.00 17.72 ? 131 LEU   A CD1 1 
ATOM   977  C  CD2 . LEU   A 1 125 ? -0.902 7.496   18.557 1.00 14.95 ? 131 LEU   A CD2 1 
ATOM   978  N  N   . VAL   A 1 126 ? 3.686  6.944   19.719 1.00 10.10 ? 132 VAL   A N   1 
ATOM   979  C  CA  . VAL   A 1 126 ? 5.155  7.052   19.560 1.00 9.88  ? 132 VAL   A CA  1 
ATOM   980  C  C   . VAL   A 1 126 ? 5.391  7.435   18.100 1.00 10.45 ? 132 VAL   A C   1 
ATOM   981  O  O   . VAL   A 1 126 ? 4.754  6.867   17.197 1.00 10.96 ? 132 VAL   A O   1 
ATOM   982  C  CB  . VAL   A 1 126 ? 5.860  5.755   20.001 1.00 10.40 ? 132 VAL   A CB  1 
ATOM   983  C  CG1 . VAL   A 1 126 ? 5.296  4.510   19.330 1.00 10.93 ? 132 VAL   A CG1 1 
ATOM   984  C  CG2 . VAL   A 1 126 ? 7.395  5.867   19.829 1.00 10.40 ? 132 VAL   A CG2 1 
ATOM   985  N  N   . GLY   A 1 127 ? 6.282  8.394   17.848 1.00 10.46 ? 133 GLY   A N   1 
ATOM   986  C  CA  . GLY   A 1 127 ? 6.626  8.793   16.498 1.00 10.16 ? 133 GLY   A CA  1 
ATOM   987  C  C   . GLY   A 1 127 ? 8.084  8.496   16.211 1.00 9.78  ? 133 GLY   A C   1 
ATOM   988  O  O   . GLY   A 1 127 ? 8.958  8.697   17.086 1.00 10.83 ? 133 GLY   A O   1 
ATOM   989  N  N   . PHE   A 1 128 ? 8.333  8.030   15.004 1.00 9.25  ? 134 PHE   A N   1 
ATOM   990  C  CA  . PHE   A 1 128 ? 9.685  7.624   14.572 1.00 9.41  ? 134 PHE   A CA  1 
ATOM   991  C  C   . PHE   A 1 128 ? 10.137 8.451   13.392 1.00 9.28  ? 134 PHE   A C   1 
ATOM   992  O  O   . PHE   A 1 128 ? 9.375  8.620   12.416 1.00 9.61  ? 134 PHE   A O   1 
ATOM   993  C  CB  . PHE   A 1 128 ? 9.659  6.145   14.125 1.00 9.77  ? 134 PHE   A CB  1 
ATOM   994  C  CG  . PHE   A 1 128 ? 9.055  5.202   15.141 1.00 8.69  ? 134 PHE   A CG  1 
ATOM   995  C  CD1 . PHE   A 1 128 ? 9.817  4.704   16.189 1.00 8.34  ? 134 PHE   A CD1 1 
ATOM   996  C  CD2 . PHE   A 1 128 ? 7.720  4.804   15.036 1.00 9.99  ? 134 PHE   A CD2 1 
ATOM   997  C  CE1 . PHE   A 1 128 ? 9.254  3.832   17.122 1.00 8.56  ? 134 PHE   A CE1 1 
ATOM   998  C  CE2 . PHE   A 1 128 ? 7.167  3.918   15.970 1.00 10.03 ? 134 PHE   A CE2 1 
ATOM   999  C  CZ  . PHE   A 1 128 ? 7.959  3.416   16.991 1.00 9.16  ? 134 PHE   A CZ  1 
ATOM   1000 N  N   . ALA   A 1 129 ? 11.389 8.937   13.458 1.00 8.86  ? 135 ALA   A N   1 
ATOM   1001 C  CA  . ALA   A 1 129 ? 12.029 9.626   12.321 1.00 9.56  ? 135 ALA   A CA  1 
ATOM   1002 C  C   . ALA   A 1 129 ? 12.508 8.547   11.344 1.00 9.27  ? 135 ALA   A C   1 
ATOM   1003 O  O   . ALA   A 1 129 ? 13.377 7.722   11.713 1.00 9.59  ? 135 ALA   A O   1 
ATOM   1004 C  CB  . ALA   A 1 129 ? 13.195 10.455  12.826 1.00 9.76  ? 135 ALA   A CB  1 
ATOM   1005 N  N   . ASP   A 1 130 ? 11.966 8.523   10.132 1.00 9.69  ? 136 ASP   A N   1 
ATOM   1006 C  CA  . ASP   A 1 130 ? 12.370 7.542   9.138  1.00 10.26 ? 136 ASP   A CA  1 
ATOM   1007 C  C   . ASP   A 1 130 ? 13.780 7.811   8.633  1.00 9.83  ? 136 ASP   A C   1 
ATOM   1008 O  O   . ASP   A 1 130 ? 14.188 8.989   8.502  1.00 11.28 ? 136 ASP   A O   1 
ATOM   1009 C  CB  . ASP   A 1 130 ? 11.416 7.644   7.927  1.00 12.05 ? 136 ASP   A CB  1 
ATOM   1010 C  CG  . ASP   A 1 130 ? 11.665 6.630   6.849  1.00 13.54 ? 136 ASP   A CG  1 
ATOM   1011 O  OD1 . ASP   A 1 130 ? 11.709 5.416   7.157  1.00 15.48 ? 136 ASP   A OD1 1 
ATOM   1012 O  OD2 . ASP   A 1 130 ? 11.925 7.067   5.689  1.00 17.01 ? 136 ASP   A OD2 1 
ATOM   1013 N  N   . VAL   A 1 131 ? 14.520 6.732   8.297  1.00 9.26  ? 137 VAL   A N   1 
ATOM   1014 C  CA  . VAL   A 1 131 ? 15.848 6.855   7.647  1.00 9.70  ? 137 VAL   A CA  1 
ATOM   1015 C  C   . VAL   A 1 131 ? 15.923 6.047   6.356  1.00 10.17 ? 137 VAL   A C   1 
ATOM   1016 O  O   . VAL   A 1 131 ? 16.990 6.044   5.716  1.00 10.09 ? 137 VAL   A O   1 
ATOM   1017 C  CB  . VAL   A 1 131 ? 17.014 6.469   8.592  1.00 10.15 ? 137 VAL   A CB  1 
ATOM   1018 C  CG1 . VAL   A 1 131 ? 17.030 7.380   9.829  1.00 11.27 ? 137 VAL   A CG1 1 
ATOM   1019 C  CG2 . VAL   A 1 131 ? 17.010 4.995   8.990  1.00 11.07 ? 137 VAL   A CG2 1 
ATOM   1020 N  N   . ARG   A 1 132 ? 14.841 5.367   5.945  1.00 10.19 ? 138 ARG   A N   1 
ATOM   1021 C  CA  . ARG   A 1 132 ? 14.903 4.466   4.802  1.00 10.58 ? 138 ARG   A CA  1 
ATOM   1022 C  C   . ARG   A 1 132 ? 15.149 5.175   3.469  1.00 12.44 ? 138 ARG   A C   1 
ATOM   1023 O  O   . ARG   A 1 132 ? 15.611 4.536   2.501  1.00 13.24 ? 138 ARG   A O   1 
ATOM   1024 C  CB  . ARG   A 1 132 ? 13.629 3.620   4.707  1.00 10.85 ? 138 ARG   A CB  1 
ATOM   1025 C  CG  . ARG   A 1 132 ? 13.506 2.663   5.887  1.00 10.04 ? 138 ARG   A CG  1 
ATOM   1026 C  CD  . ARG   A 1 132 ? 12.193 1.908   5.769  1.00 12.28 ? 138 ARG   A CD  1 
ATOM   1027 N  NE  . ARG   A 1 132 ? 11.073 2.836   5.997  1.00 12.06 ? 138 ARG   A NE  1 
ATOM   1028 C  CZ  . ARG   A 1 132 ? 9.786  2.495   6.100  1.00 13.60 ? 138 ARG   A CZ  1 
ATOM   1029 N  NH1 . ARG   A 1 132 ? 9.400  1.267   5.816  1.00 14.29 ? 138 ARG   A NH1 1 
ATOM   1030 N  NH2 . ARG   A 1 132 ? 8.888  3.399   6.474  1.00 13.88 ? 138 ARG   A NH2 1 
ATOM   1031 N  N   . ASP   A 1 133 ? 14.828 6.487   3.370  1.00 12.21 ? 139 ASP   A N   1 
ATOM   1032 C  CA  . ASP   A 1 133 ? 15.105 7.232   2.152  1.00 13.18 ? 139 ASP   A CA  1 
ATOM   1033 C  C   . ASP   A 1 133 ? 16.557 7.706   2.047  1.00 12.86 ? 139 ASP   A C   1 
ATOM   1034 O  O   . ASP   A 1 133 ? 16.949 8.231   0.984  1.00 14.68 ? 139 ASP   A O   1 
ATOM   1035 C  CB  . ASP   A 1 133 ? 14.159 8.469   2.074  1.00 15.41 ? 139 ASP   A CB  1 
ATOM   1036 C  CG  . ASP   A 1 133 ? 14.403 9.485   3.164  1.00 17.50 ? 139 ASP   A CG  1 
ATOM   1037 O  OD1 . ASP   A 1 133 ? 14.607 9.084   4.313  1.00 15.88 ? 139 ASP   A OD1 1 
ATOM   1038 O  OD2 . ASP   A 1 133 ? 14.360 10.701  2.875  1.00 20.31 ? 139 ASP   A OD2 1 
ATOM   1039 N  N   . LEU   A 1 134 ? 17.365 7.602   3.113  1.00 11.80 ? 140 LEU   A N   1 
ATOM   1040 C  CA  . LEU   A 1 134 ? 18.734 8.154   3.119  1.00 11.22 ? 140 LEU   A CA  1 
ATOM   1041 C  C   . LEU   A 1 134 ? 19.667 7.103   2.532  1.00 11.21 ? 140 LEU   A C   1 
ATOM   1042 O  O   . LEU   A 1 134 ? 20.374 6.367   3.263  1.00 11.61 ? 140 LEU   A O   1 
ATOM   1043 C  CB  . LEU   A 1 134 ? 19.114 8.529   4.556  1.00 11.38 ? 140 LEU   A CB  1 
ATOM   1044 C  CG  . LEU   A 1 134 ? 18.191 9.569   5.266  1.00 12.81 ? 140 LEU   A CG  1 
ATOM   1045 C  CD1 . LEU   A 1 134 ? 18.604 9.772   6.732  1.00 14.29 ? 140 LEU   A CD1 1 
ATOM   1046 C  CD2 . LEU   A 1 134 ? 18.148 10.902  4.531  1.00 14.85 ? 140 LEU   A CD2 1 
ATOM   1047 N  N   . LEU   A 1 135 ? 19.643 6.964   1.187  1.00 11.87 ? 141 LEU   A N   1 
ATOM   1048 C  CA  . LEU   A 1 135 ? 20.376 5.862   0.547  1.00 12.97 ? 141 LEU   A CA  1 
ATOM   1049 C  C   . LEU   A 1 135 ? 21.877 5.944   0.709  1.00 13.14 ? 141 LEU   A C   1 
ATOM   1050 O  O   . LEU   A 1 135 ? 22.586 4.926   0.742  1.00 14.66 ? 141 LEU   A O   1 
ATOM   1051 C  CB  . LEU   A 1 135 ? 20.008 5.764   -0.955 1.00 14.77 ? 141 LEU   A CB  1 
ATOM   1052 C  CG  . LEU   A 1 135 ? 18.496 5.762   -1.253 1.00 15.91 ? 141 LEU   A CG  1 
ATOM   1053 C  CD1 . LEU   A 1 135 ? 18.248 5.425   -2.751 1.00 17.87 ? 141 LEU   A CD1 1 
ATOM   1054 C  CD2 . LEU   A 1 135 ? 17.705 4.756   -0.420 1.00 17.28 ? 141 LEU   A CD2 1 
ATOM   1055 N  N   . TRP   A 1 136 ? 22.363 7.176   0.877  1.00 12.52 ? 142 TRP   A N   1 
ATOM   1056 C  CA  . TRP   A 1 136 ? 23.788 7.428   1.037  1.00 13.08 ? 142 TRP   A CA  1 
ATOM   1057 C  C   . TRP   A 1 136 ? 24.350 6.836   2.329  1.00 12.50 ? 142 TRP   A C   1 
ATOM   1058 O  O   . TRP   A 1 136 ? 25.586 6.684   2.439  1.00 14.44 ? 142 TRP   A O   1 
ATOM   1059 C  CB  . TRP   A 1 136 ? 24.108 8.936   0.919  1.00 13.94 ? 142 TRP   A CB  1 
ATOM   1060 C  CG  . TRP   A 1 136 ? 23.308 9.772   1.880  1.00 12.45 ? 142 TRP   A CG  1 
ATOM   1061 C  CD1 . TRP   A 1 136 ? 22.157 10.443  1.610  1.00 12.77 ? 142 TRP   A CD1 1 
ATOM   1062 C  CD2 . TRP   A 1 136 ? 23.654 10.084  3.247  1.00 12.72 ? 142 TRP   A CD2 1 
ATOM   1063 N  NE1 . TRP   A 1 136 ? 21.737 11.135  2.740  1.00 13.87 ? 142 TRP   A NE1 1 
ATOM   1064 C  CE2 . TRP   A 1 136 ? 22.650 10.931  3.749  1.00 13.03 ? 142 TRP   A CE2 1 
ATOM   1065 C  CE3 . TRP   A 1 136 ? 24.724 9.748   4.085  1.00 13.09 ? 142 TRP   A CE3 1 
ATOM   1066 C  CZ2 . TRP   A 1 136 ? 22.695 11.450  5.065  1.00 14.13 ? 142 TRP   A CZ2 1 
ATOM   1067 C  CZ3 . TRP   A 1 136 ? 24.767 10.273  5.377  1.00 14.51 ? 142 TRP   A CZ3 1 
ATOM   1068 C  CH2 . TRP   A 1 136 ? 23.777 11.128  5.824  1.00 14.45 ? 142 TRP   A CH2 1 
ATOM   1069 N  N   . LEU   A 1 137 ? 23.515 6.496   3.332  1.00 11.85 ? 143 LEU   A N   1 
ATOM   1070 C  CA  . LEU   A 1 137 ? 24.045 5.823   4.532  1.00 12.77 ? 143 LEU   A CA  1 
ATOM   1071 C  C   . LEU   A 1 137 ? 24.734 4.510   4.198  1.00 14.85 ? 143 LEU   A C   1 
ATOM   1072 O  O   . LEU   A 1 137 ? 25.569 4.042   4.993  1.00 15.99 ? 143 LEU   A O   1 
ATOM   1073 C  CB  . LEU   A 1 137 ? 22.918 5.542   5.535  1.00 12.55 ? 143 LEU   A CB  1 
ATOM   1074 C  CG  . LEU   A 1 137 ? 22.375 6.785   6.232  1.00 12.33 ? 143 LEU   A CG  1 
ATOM   1075 C  CD1 . LEU   A 1 137 ? 21.117 6.442   7.028  1.00 13.55 ? 143 LEU   A CD1 1 
ATOM   1076 C  CD2 . LEU   A 1 137 ? 23.445 7.425   7.184  1.00 13.81 ? 143 LEU   A CD2 1 
ATOM   1077 N  N   . ASP   A 1 138 ? 24.382 3.892   3.019  1.00 16.72 ? 144 ASP   A N   1 
ATOM   1078 C  CA  . ASP   A 1 138 ? 24.917 2.577   2.601  1.00 19.78 ? 144 ASP   A CA  1 
ATOM   1079 C  C   . ASP   A 1 138 ? 26.252 2.632   1.897  1.00 23.90 ? 144 ASP   A C   1 
ATOM   1080 O  O   . ASP   A 1 138 ? 26.756 1.577   1.489  1.00 26.01 ? 144 ASP   A O   1 
ATOM   1081 C  CB  . ASP   A 1 138 ? 23.928 1.869   1.635  1.00 20.63 ? 144 ASP   A CB  1 
ATOM   1082 C  CG  . ASP   A 1 138 ? 22.579 1.529   2.217  1.00 21.90 ? 144 ASP   A CG  1 
ATOM   1083 O  OD1 . ASP   A 1 138 ? 22.433 1.570   3.470  1.00 23.74 ? 144 ASP   A OD1 1 
ATOM   1084 O  OD2 . ASP   A 1 138 ? 21.635 1.204   1.433  1.00 28.47 ? 144 ASP   A OD2 1 
ATOM   1085 N  N   . GLU   A 1 139 ? 26.826 3.819   1.695  1.00 24.99 ? 145 GLU   A N   1 
ATOM   1086 C  CA  . GLU   A 1 139 ? 28.104 3.914   0.964  1.00 29.49 ? 145 GLU   A CA  1 
ATOM   1087 C  C   . GLU   A 1 139 ? 29.003 5.043   1.469  1.00 32.45 ? 145 GLU   A C   1 
ATOM   1088 O  O   . GLU   A 1 139 ? 28.601 5.800   2.356  1.00 32.66 ? 145 GLU   A O   1 
ATOM   1089 C  CB  . GLU   A 1 139 ? 27.784 4.106   -0.528 1.00 34.86 ? 145 GLU   A CB  1 
ATOM   1090 C  CG  . GLU   A 1 139 ? 26.996 5.378   -0.783 1.00 44.20 ? 145 GLU   A CG  1 
ATOM   1091 C  CD  . GLU   A 1 139 ? 26.254 5.452   -2.103 1.00 56.01 ? 145 GLU   A CD  1 
ATOM   1092 O  OE1 . GLU   A 1 139 ? 25.330 6.292   -2.217 1.00 58.01 ? 145 GLU   A OE1 1 
ATOM   1093 O  OE2 . GLU   A 1 139 ? 26.597 4.680   -3.028 1.00 60.86 ? 145 GLU   A OE2 1 
ATOM   1094 N  N   . GLU   A 1 140 ? 30.215 5.169   0.882  1.00 34.58 ? 146 GLU   A N   1 
ATOM   1095 C  CA  . GLU   A 1 140 ? 31.197 6.246   1.083  1.00 37.19 ? 146 GLU   A CA  1 
ATOM   1096 C  C   . GLU   A 1 140 ? 31.493 6.481   2.544  1.00 38.63 ? 146 GLU   A C   1 
ATOM   1097 O  O   . GLU   A 1 140 ? 31.800 7.597   2.968  1.00 39.07 ? 146 GLU   A O   1 
ATOM   1098 C  CB  . GLU   A 1 140 ? 30.727 7.521   0.333  1.00 40.81 ? 146 GLU   A CB  1 
ATOM   1099 C  CG  . GLU   A 1 140 ? 31.237 8.883   0.804  1.00 48.18 ? 146 GLU   A CG  1 
ATOM   1100 C  CD  . GLU   A 1 140 ? 32.594 9.361   0.314  1.00 58.06 ? 146 GLU   A CD  1 
ATOM   1101 O  OE1 . GLU   A 1 140 ? 32.774 10.595  0.196  1.00 59.70 ? 146 GLU   A OE1 1 
ATOM   1102 O  OE2 . GLU   A 1 140 ? 33.475 8.510   0.045  1.00 61.46 ? 146 GLU   A OE2 1 
ATOM   1103 N  N   . SER   B 1 1   ? 21.927 -21.226 7.681  1.00 14.62 ? 7   SER   C N   1 
ATOM   1104 C  CA  . SER   B 1 1   ? 20.765 -21.024 8.585  1.00 13.38 ? 7   SER   C CA  1 
ATOM   1105 C  C   . SER   B 1 1   ? 20.739 -22.138 9.665  1.00 13.13 ? 7   SER   C C   1 
ATOM   1106 O  O   . SER   B 1 1   ? 21.388 -23.187 9.520  1.00 15.39 ? 7   SER   C O   1 
ATOM   1107 C  CB  . SER   B 1 1   ? 19.453 -21.070 7.792  1.00 16.85 ? 7   SER   C CB  1 
ATOM   1108 O  OG  . SER   B 1 1   ? 19.319 -22.358 7.218  1.00 22.07 ? 7   SER   C OG  1 
ATOM   1109 N  N   . GLY   B 1 2   ? 19.974 -21.924 10.734 1.00 13.59 ? 8   GLY   C N   1 
ATOM   1110 C  CA  . GLY   B 1 2   ? 19.782 -22.933 11.770 1.00 13.18 ? 8   GLY   C CA  1 
ATOM   1111 C  C   . GLY   B 1 2   ? 19.500 -22.328 13.127 1.00 11.46 ? 8   GLY   C C   1 
ATOM   1112 O  O   . GLY   B 1 2   ? 19.897 -21.184 13.400 1.00 12.58 ? 8   GLY   C O   1 
ATOM   1113 N  N   . ALA   B 1 3   ? 18.844 -23.078 13.999 1.00 11.10 ? 9   ALA   C N   1 
ATOM   1114 C  CA  . ALA   B 1 3   ? 18.510 -22.590 15.336 1.00 11.47 ? 9   ALA   C CA  1 
ATOM   1115 C  C   . ALA   B 1 3   ? 18.645 -23.704 16.367 1.00 10.25 ? 9   ALA   C C   1 
ATOM   1116 O  O   . ALA   B 1 3   ? 18.720 -24.907 16.003 1.00 11.84 ? 9   ALA   C O   1 
ATOM   1117 C  CB  . ALA   B 1 3   ? 17.067 -22.062 15.344 1.00 13.31 ? 9   ALA   C CB  1 
ATOM   1118 N  N   . ILE   B 1 4   ? 18.635 -23.346 17.644 1.00 10.45 ? 10  ILE   C N   1 
ATOM   1119 C  CA  . ILE   B 1 4   ? 18.552 -24.275 18.774 1.00 10.70 ? 10  ILE   C CA  1 
ATOM   1120 C  C   . ILE   B 1 4   ? 17.156 -24.079 19.373 1.00 10.52 ? 10  ILE   C C   1 
ATOM   1121 O  O   . ILE   B 1 4   ? 16.721 -22.935 19.596 1.00 11.70 ? 10  ILE   C O   1 
ATOM   1122 C  CB  . ILE   B 1 4   ? 19.592 -23.954 19.852 1.00 10.09 ? 10  ILE   C CB  1 
ATOM   1123 C  CG1 . ILE   B 1 4   ? 21.023 -23.828 19.277 1.00 11.53 ? 10  ILE   C CG1 1 
ATOM   1124 C  CG2 . ILE   B 1 4   ? 19.548 -25.060 20.936 1.00 12.71 ? 10  ILE   C CG2 1 
ATOM   1125 C  CD1 . ILE   B 1 4   ? 21.973 -23.217 20.329 1.00 11.76 ? 10  ILE   C CD1 1 
ATOM   1126 N  N   . TYR   B 1 5   ? 16.444 -25.175 19.662 1.00 11.17 ? 11  TYR   C N   1 
ATOM   1127 C  CA  . TYR   B 1 5   ? 15.100 -25.124 20.247 1.00 11.95 ? 11  TYR   C CA  1 
ATOM   1128 C  C   . TYR   B 1 5   ? 15.163 -25.819 21.609 1.00 11.92 ? 11  TYR   C C   1 
ATOM   1129 O  O   . TYR   B 1 5   ? 15.251 -27.067 21.672 1.00 13.82 ? 11  TYR   C O   1 
ATOM   1130 C  CB  . TYR   B 1 5   ? 14.061 -25.862 19.331 1.00 13.23 ? 11  TYR   C CB  1 
ATOM   1131 C  CG  . TYR   B 1 5   ? 13.867 -25.096 18.029 1.00 12.47 ? 11  TYR   C CG  1 
ATOM   1132 C  CD1 . TYR   B 1 5   ? 13.062 -23.960 17.975 1.00 13.07 ? 11  TYR   C CD1 1 
ATOM   1133 C  CD2 . TYR   B 1 5   ? 14.567 -25.441 16.883 1.00 13.73 ? 11  TYR   C CD2 1 
ATOM   1134 C  CE1 . TYR   B 1 5   ? 12.927 -23.228 16.798 1.00 14.10 ? 11  TYR   C CE1 1 
ATOM   1135 C  CE2 . TYR   B 1 5   ? 14.449 -24.716 15.701 1.00 15.04 ? 11  TYR   C CE2 1 
ATOM   1136 C  CZ  . TYR   B 1 5   ? 13.616 -23.617 15.663 1.00 14.51 ? 11  TYR   C CZ  1 
ATOM   1137 O  OH  . TYR   B 1 5   ? 13.543 -22.869 14.509 1.00 16.64 ? 11  TYR   C OH  1 
ATOM   1138 N  N   . VAL   B 1 6   ? 15.222 -25.092 22.695 1.00 13.61 ? 12  VAL   C N   1 
ATOM   1139 C  CA  . VAL   B 1 6   ? 15.310 -25.612 24.074 1.00 13.76 ? 12  VAL   C CA  1 
ATOM   1140 C  C   . VAL   B 1 6   ? 14.177 -25.005 24.894 1.00 14.28 ? 12  VAL   C C   1 
ATOM   1141 O  O   . VAL   B 1 6   ? 13.990 -23.786 24.881 1.00 13.49 ? 12  VAL   C O   1 
ATOM   1142 C  CB  . VAL   B 1 6   ? 16.724 -25.314 24.672 1.00 15.66 ? 12  VAL   C CB  1 
ATOM   1143 C  CG1 . VAL   B 1 6   ? 17.099 -23.833 24.587 1.00 16.09 ? 12  VAL   C CG1 1 
ATOM   1144 C  CG2 . VAL   B 1 6   ? 16.820 -25.814 26.097 1.00 16.80 ? 12  VAL   C CG2 1 
ATOM   1145 N  N   . GLY   B 1 7   ? 13.365 -25.843 25.587 1.00 15.60 ? 13  GLY   C N   1 
ATOM   1146 C  CA  . GLY   B 1 7   ? 12.243 -25.307 26.341 1.00 16.31 ? 13  GLY   C CA  1 
ATOM   1147 C  C   . GLY   B 1 7   ? 11.309 -24.471 25.471 1.00 16.31 ? 13  GLY   C C   1 
ATOM   1148 O  O   . GLY   B 1 7   ? 11.032 -24.868 24.331 1.00 16.95 ? 13  GLY   C O   1 
ATOM   1149 N  N   . ASN   B 1 8   ? 10.944 -23.282 25.921 1.00 15.38 ? 14  ASN   C N   1 
ATOM   1150 C  CA  . ASN   B 1 8   ? 10.141 -22.375 25.084 1.00 15.13 ? 14  ASN   C CA  1 
ATOM   1151 C  C   . ASN   B 1 8   ? 11.035 -21.249 24.523 1.00 13.73 ? 14  ASN   C C   1 
ATOM   1152 O  O   . ASN   B 1 8   ? 10.573 -20.106 24.362 1.00 13.91 ? 14  ASN   C O   1 
ATOM   1153 C  CB  . ASN   B 1 8   ? 8.906  -21.807 25.828 1.00 17.96 ? 14  ASN   C CB  1 
ATOM   1154 C  CG  . ASN   B 1 8   ? 7.841  -22.868 25.987 1.00 23.97 ? 14  ASN   C CG  1 
ATOM   1155 O  OD1 . ASN   B 1 8   ? 6.989  -23.035 25.122 1.00 27.04 ? 14  ASN   C OD1 1 
ATOM   1156 N  ND2 . ASN   B 1 8   ? 7.964  -23.682 27.025 1.00 27.01 ? 14  ASN   C ND2 1 
ATOM   1157 N  N   . TYR   B 1 9   ? 12.259 -21.606 24.120 1.00 12.02 ? 15  TYR   C N   1 
ATOM   1158 C  CA  . TYR   B 1 9   ? 13.224 -20.651 23.544 1.00 11.92 ? 15  TYR   C CA  1 
ATOM   1159 C  C   . TYR   B 1 9   ? 13.699 -21.123 22.170 1.00 11.67 ? 15  TYR   C C   1 
ATOM   1160 O  O   . TYR   B 1 9   ? 13.875 -22.334 21.945 1.00 12.57 ? 15  TYR   C O   1 
ATOM   1161 C  CB  . TYR   B 1 9   ? 14.455 -20.488 24.460 1.00 13.15 ? 15  TYR   C CB  1 
ATOM   1162 C  CG  . TYR   B 1 9   ? 14.121 -19.964 25.841 1.00 13.53 ? 15  TYR   C CG  1 
ATOM   1163 C  CD1 . TYR   B 1 9   ? 13.559 -18.708 26.009 1.00 15.41 ? 15  TYR   C CD1 1 
ATOM   1164 C  CD2 . TYR   B 1 9   ? 14.437 -20.699 26.981 1.00 15.72 ? 15  TYR   C CD2 1 
ATOM   1165 C  CE1 . TYR   B 1 9   ? 13.260 -18.219 27.281 1.00 18.97 ? 15  TYR   C CE1 1 
ATOM   1166 C  CE2 . TYR   B 1 9   ? 14.173 -20.200 28.258 1.00 18.58 ? 15  TYR   C CE2 1 
ATOM   1167 C  CZ  . TYR   B 1 9   ? 13.604 -18.953 28.392 1.00 21.36 ? 15  TYR   C CZ  1 
ATOM   1168 O  OH  . TYR   B 1 9   ? 13.304 -18.414 29.629 1.00 26.65 ? 15  TYR   C OH  1 
ATOM   1169 N  N   . ARG   B 1 10  ? 13.941 -20.166 21.274 1.00 10.76 ? 16  ARG   C N   1 
ATOM   1170 C  CA  . ARG   B 1 10  ? 14.576 -20.383 19.966 1.00 10.68 ? 16  ARG   C CA  1 
ATOM   1171 C  C   . ARG   B 1 10  ? 15.838 -19.511 19.974 1.00 9.93  ? 16  ARG   C C   1 
ATOM   1172 O  O   . ARG   B 1 10  ? 15.738 -18.285 20.168 1.00 10.92 ? 16  ARG   C O   1 
ATOM   1173 C  CB  . ARG   B 1 10  ? 13.616 -19.953 18.831 1.00 11.41 ? 16  ARG   C CB  1 
ATOM   1174 C  CG  . ARG   B 1 10  ? 14.242 -19.771 17.443 1.00 12.54 ? 16  ARG   C CG  1 
ATOM   1175 C  CD  . ARG   B 1 10  ? 13.161 -19.494 16.398 1.00 12.79 ? 16  ARG   C CD  1 
ATOM   1176 N  NE  . ARG   B 1 10  ? 13.575 -18.542 15.358 1.00 13.23 ? 16  ARG   C NE  1 
ATOM   1177 C  CZ  . ARG   B 1 10  ? 14.100 -18.830 14.166 1.00 13.78 ? 16  ARG   C CZ  1 
ATOM   1178 N  NH1 . ARG   B 1 10  ? 14.341 -20.105 13.815 1.00 15.89 ? 16  ARG   C NH1 1 
ATOM   1179 N  NH2 . ARG   B 1 10  ? 14.441 -17.845 13.328 1.00 14.62 ? 16  ARG   C NH2 1 
ATOM   1180 N  N   . VAL   B 1 11  ? 17.004 -20.110 19.712 1.00 9.87  ? 17  VAL   C N   1 
ATOM   1181 C  CA  . VAL   B 1 11  ? 18.290 -19.396 19.698 1.00 9.30  ? 17  VAL   C CA  1 
ATOM   1182 C  C   . VAL   B 1 11  ? 18.760 -19.341 18.282 1.00 9.93  ? 17  VAL   C C   1 
ATOM   1183 O  O   . VAL   B 1 11  ? 18.942 -20.403 17.620 1.00 10.61 ? 17  VAL   C O   1 
ATOM   1184 C  CB  . VAL   B 1 11  ? 19.355 -20.119 20.572 1.00 10.20 ? 17  VAL   C CB  1 
ATOM   1185 C  CG1 . VAL   B 1 11  ? 20.615 -19.256 20.668 1.00 12.00 ? 17  VAL   C CG1 1 
ATOM   1186 C  CG2 . VAL   B 1 11  ? 18.836 -20.469 21.958 1.00 11.64 ? 17  VAL   C CG2 1 
ATOM   1187 N  N   . VAL   B 1 12  ? 19.009 -18.134 17.762 1.00 9.25  ? 18  VAL   C N   1 
ATOM   1188 C  CA  A VAL   B 1 12  ? 19.466 -17.947 16.382 0.50 9.06  ? 18  VAL   C CA  1 
ATOM   1189 C  CA  B VAL   B 1 12  ? 19.412 -17.969 16.372 0.50 11.03 ? 18  VAL   C CA  1 
ATOM   1190 C  C   . VAL   B 1 12  ? 20.612 -16.945 16.307 1.00 9.94  ? 18  VAL   C C   1 
ATOM   1191 O  O   . VAL   B 1 12  ? 20.870 -16.189 17.274 1.00 10.59 ? 18  VAL   C O   1 
ATOM   1192 C  CB  A VAL   B 1 12  ? 18.341 -17.419 15.449 0.50 8.98  ? 18  VAL   C CB  1 
ATOM   1193 C  CB  B VAL   B 1 12  ? 18.148 -17.435 15.590 0.50 15.30 ? 18  VAL   C CB  1 
ATOM   1194 C  CG1 A VAL   B 1 12  ? 17.358 -18.528 15.147 0.50 10.09 ? 18  VAL   C CG1 1 
ATOM   1195 C  CG1 B VAL   B 1 12  ? 18.388 -17.337 14.103 0.50 16.16 ? 18  VAL   C CG1 1 
ATOM   1196 C  CG2 A VAL   B 1 12  ? 17.681 -16.125 15.993 0.50 6.71  ? 18  VAL   C CG2 1 
ATOM   1197 C  CG2 B VAL   B 1 12  ? 16.937 -18.317 15.829 0.50 18.25 ? 18  VAL   C CG2 1 
ATOM   1198 N  N   . ASN   B 1 13  ? 21.310 -16.876 15.163 1.00 9.73  ? 19  ASN   C N   1 
ATOM   1199 C  CA  . ASN   B 1 13  ? 22.295 -15.828 14.962 1.00 9.34  ? 19  ASN   C CA  1 
ATOM   1200 C  C   . ASN   B 1 13  ? 21.482 -14.488 14.921 1.00 10.04 ? 19  ASN   C C   1 
ATOM   1201 O  O   . ASN   B 1 13  ? 20.481 -14.384 14.215 1.00 9.99  ? 19  ASN   C O   1 
ATOM   1202 C  CB  . ASN   B 1 13  ? 23.000 -15.965 13.616 1.00 9.38  ? 19  ASN   C CB  1 
ATOM   1203 C  CG  . ASN   B 1 13  ? 23.870 -17.224 13.535 1.00 9.59  ? 19  ASN   C CG  1 
ATOM   1204 O  OD1 . ASN   B 1 13  ? 23.409 -18.287 13.107 1.00 10.64 ? 19  ASN   C OD1 1 
ATOM   1205 N  ND2 . ASN   B 1 13  ? 25.128 -17.122 13.990 1.00 10.72 ? 19  ASN   C ND2 1 
ATOM   1206 N  N   . ARG   B 1 14  ? 22.000 -13.464 15.627 1.00 9.59  ? 20  ARG   C N   1 
ATOM   1207 C  CA  . ARG   B 1 14  ? 21.263 -12.163 15.633 1.00 10.04 ? 20  ARG   C CA  1 
ATOM   1208 C  C   . ARG   B 1 14  ? 21.104 -11.635 14.205 1.00 10.45 ? 20  ARG   C C   1 
ATOM   1209 O  O   . ARG   B 1 14  ? 20.017 -11.107 13.863 1.00 10.74 ? 20  ARG   C O   1 
ATOM   1210 C  CB  . ARG   B 1 14  ? 22.000 -11.157 16.491 1.00 10.65 ? 20  ARG   C CB  1 
ATOM   1211 C  CG  . ARG   B 1 14  ? 21.185 -9.836  16.724 1.00 11.03 ? 20  ARG   C CG  1 
ATOM   1212 C  CD  . ARG   B 1 14  ? 22.058 -8.875  17.496 1.00 10.86 ? 20  ARG   C CD  1 
ATOM   1213 N  NE  . ARG   B 1 14  ? 21.376 -7.611  17.926 1.00 11.20 ? 20  ARG   C NE  1 
ATOM   1214 C  CZ  . ARG   B 1 14  ? 21.254 -6.520  17.177 1.00 10.50 ? 20  ARG   C CZ  1 
ATOM   1215 N  NH1 . ARG   B 1 14  ? 21.657 -6.525  15.915 1.00 12.86 ? 20  ARG   C NH1 1 
ATOM   1216 N  NH2 . ARG   B 1 14  ? 20.766 -5.397  17.700 1.00 11.97 ? 20  ARG   C NH2 1 
ATOM   1217 N  N   . HIS   B 1 15  ? 22.120 -11.827 13.349 1.00 10.29 ? 21  HIS   C N   1 
ATOM   1218 C  CA  . HIS   B 1 15  ? 22.031 -11.283 11.979 1.00 11.49 ? 21  HIS   C CA  1 
ATOM   1219 C  C   . HIS   B 1 15  ? 21.033 -12.031 11.080 1.00 11.22 ? 21  HIS   C C   1 
ATOM   1220 O  O   . HIS   B 1 15  ? 20.741 -11.520 9.992  1.00 13.57 ? 21  HIS   C O   1 
ATOM   1221 C  CB  . HIS   B 1 15  ? 23.427 -11.156 11.330 1.00 12.38 ? 21  HIS   C CB  1 
ATOM   1222 C  CG  . HIS   B 1 15  ? 24.014 -12.474 10.889 1.00 11.31 ? 21  HIS   C CG  1 
ATOM   1223 N  ND1 . HIS   B 1 15  ? 24.749 -13.302 11.764 1.00 11.64 ? 21  HIS   C ND1 1 
ATOM   1224 C  CD2 . HIS   B 1 15  ? 24.021 -13.046 9.655  1.00 11.94 ? 21  HIS   C CD2 1 
ATOM   1225 C  CE1 . HIS   B 1 15  ? 25.146 -14.361 11.039 1.00 12.60 ? 21  HIS   C CE1 1 
ATOM   1226 N  NE2 . HIS   B 1 15  ? 24.745 -14.245 9.770  1.00 12.03 ? 21  HIS   C NE2 1 
ATOM   1227 N  N   . LEU   B 1 16  ? 20.498 -13.174 11.526 1.00 10.19 ? 22  LEU   C N   1 
ATOM   1228 C  CA  . LEU   B 1 16  ? 19.496 -13.945 10.770 1.00 11.44 ? 22  LEU   C CA  1 
ATOM   1229 C  C   . LEU   B 1 16  ? 18.107 -13.893 11.444 1.00 11.94 ? 22  LEU   C C   1 
ATOM   1230 O  O   . LEU   B 1 16  ? 17.175 -14.591 11.000 1.00 12.88 ? 22  LEU   C O   1 
ATOM   1231 C  CB  . LEU   B 1 16  ? 19.982 -15.391 10.576 1.00 11.25 ? 22  LEU   C CB  1 
ATOM   1232 C  CG  . LEU   B 1 16  ? 21.278 -15.536 9.774  1.00 12.23 ? 22  LEU   C CG  1 
ATOM   1233 C  CD1 . LEU   B 1 16  ? 21.684 -17.017 9.686  1.00 13.39 ? 22  LEU   C CD1 1 
ATOM   1234 C  CD2 . LEU   B 1 16  ? 21.152 -14.930 8.377  1.00 13.71 ? 22  LEU   C CD2 1 
ATOM   1235 N  N   . ALA   B 1 17  ? 17.944 -13.133 12.556 1.00 12.25 ? 23  ALA   C N   1 
ATOM   1236 C  CA  . ALA   B 1 17  ? 16.662 -13.080 13.269 1.00 11.77 ? 23  ALA   C CA  1 
ATOM   1237 C  C   . ALA   B 1 17  ? 15.571 -12.515 12.356 1.00 12.42 ? 23  ALA   C C   1 
ATOM   1238 O  O   . ALA   B 1 17  ? 15.814 -11.580 11.567 1.00 13.59 ? 23  ALA   C O   1 
ATOM   1239 C  CB  . ALA   B 1 17  ? 16.821 -12.213 14.515 1.00 13.35 ? 23  ALA   C CB  1 
ATOM   1240 N  N   . THR   B 1 18  ? 14.371 -13.060 12.508 1.00 12.95 ? 24  THR   C N   1 
ATOM   1241 C  CA  . THR   B 1 18  ? 13.218 -12.626 11.715 1.00 13.44 ? 24  THR   C CA  1 
ATOM   1242 C  C   . THR   B 1 18  ? 12.387 -11.586 12.502 1.00 12.69 ? 24  THR   C C   1 
ATOM   1243 O  O   . THR   B 1 18  ? 12.615 -11.281 13.667 1.00 13.16 ? 24  THR   C O   1 
ATOM   1244 C  CB  . THR   B 1 18  ? 12.297 -13.859 11.449 1.00 13.99 ? 24  THR   C CB  1 
ATOM   1245 O  OG1 . THR   B 1 18  ? 11.791 -14.283 12.700 1.00 14.44 ? 24  THR   C OG1 1 
ATOM   1246 C  CG2 . THR   B 1 18  ? 13.035 -15.033 10.757 1.00 15.41 ? 24  THR   C CG2 1 
ATOM   1247 N  N   . HIS   B 1 19  ? 11.393 -10.969 11.813 1.00 14.34 ? 25  HIS   C N   1 
ATOM   1248 C  CA  . HIS   B 1 19  ? 10.456 -10.060 12.485 1.00 14.73 ? 25  HIS   C CA  1 
ATOM   1249 C  C   . HIS   B 1 19  ? 9.763  -10.808 13.623 1.00 12.54 ? 25  HIS   C C   1 
ATOM   1250 O  O   . HIS   B 1 19  ? 9.670  -10.242 14.722 1.00 14.75 ? 25  HIS   C O   1 
ATOM   1251 C  CB  . HIS   B 1 19  ? 9.342  -9.573  11.512 1.00 15.88 ? 25  HIS   C CB  1 
ATOM   1252 C  CG  . HIS   B 1 19  ? 8.186  -8.867  12.209 1.00 16.08 ? 25  HIS   C CG  1 
ATOM   1253 N  ND1 . HIS   B 1 19  ? 8.353  -7.623  12.826 1.00 18.08 ? 25  HIS   C ND1 1 
ATOM   1254 C  CD2 . HIS   B 1 19  ? 6.989  -9.359  12.580 1.00 18.16 ? 25  HIS   C CD2 1 
ATOM   1255 C  CE1 . HIS   B 1 19  ? 7.161  -7.313  13.345 1.00 17.81 ? 25  HIS   C CE1 1 
ATOM   1256 N  NE2 . HIS   B 1 19  ? 6.327  -8.346  13.266 1.00 17.99 ? 25  HIS   C NE2 1 
ATOM   1257 N  N   . ASN   B 1 20  ? 9.333  -12.075 13.403 1.00 13.46 ? 26  ASN   C N   1 
ATOM   1258 C  CA  . ASN   B 1 20  ? 8.689  -12.800 14.486 1.00 14.60 ? 26  ASN   C CA  1 
ATOM   1259 C  C   . ASN   B 1 20  ? 9.608  -12.991 15.691 1.00 13.41 ? 26  ASN   C C   1 
ATOM   1260 O  O   . ASN   B 1 20  ? 9.186  -12.905 16.834 1.00 13.33 ? 26  ASN   C O   1 
ATOM   1261 C  CB  . ASN   B 1 20  ? 8.169  -14.163 14.032 1.00 16.63 ? 26  ASN   C CB  1 
ATOM   1262 C  CG  . ASN   B 1 20  ? 7.350  -14.860 15.121 1.00 22.72 ? 26  ASN   C CG  1 
ATOM   1263 O  OD1 . ASN   B 1 20  ? 6.214  -14.436 15.435 1.00 25.65 ? 26  ASN   C OD1 1 
ATOM   1264 N  ND2 . ASN   B 1 20  ? 7.901  -15.911 15.767 1.00 24.07 ? 26  ASN   C ND2 1 
ATOM   1265 N  N   . ASP   B 1 21  ? 10.933 -13.201 15.441 1.00 12.16 ? 27  ASP   C N   1 
ATOM   1266 C  CA  . ASP   B 1 21  ? 11.877 -13.295 16.545 1.00 12.08 ? 27  ASP   C CA  1 
ATOM   1267 C  C   . ASP   B 1 21  ? 11.919 -11.989 17.360 1.00 11.59 ? 27  ASP   C C   1 
ATOM   1268 O  O   . ASP   B 1 21  ? 11.853 -12.010 18.593 1.00 12.42 ? 27  ASP   C O   1 
ATOM   1269 C  CB  . ASP   B 1 21  ? 13.295 -13.608 16.035 1.00 11.72 ? 27  ASP   C CB  1 
ATOM   1270 C  CG  . ASP   B 1 21  ? 13.493 -15.029 15.536 1.00 12.62 ? 27  ASP   C CG  1 
ATOM   1271 O  OD1 . ASP   B 1 21  ? 12.911 -15.955 16.142 1.00 13.93 ? 27  ASP   C OD1 1 
ATOM   1272 O  OD2 . ASP   B 1 21  ? 14.214 -15.199 14.517 1.00 12.98 ? 27  ASP   C OD2 1 
ATOM   1273 N  N   . TRP   B 1 22  ? 12.023 -10.837 16.651 1.00 11.52 ? 28  TRP   C N   1 
ATOM   1274 C  CA  . TRP   B 1 22  ? 12.068 -9.557  17.358 1.00 11.95 ? 28  TRP   C CA  1 
ATOM   1275 C  C   . TRP   B 1 22  ? 10.714 -9.228  18.066 1.00 11.98 ? 28  TRP   C C   1 
ATOM   1276 O  O   . TRP   B 1 22  ? 10.739 -8.615  19.134 1.00 13.26 ? 28  TRP   C O   1 
ATOM   1277 C  CB  . TRP   B 1 22  ? 12.460 -8.448  16.390 1.00 12.27 ? 28  TRP   C CB  1 
ATOM   1278 C  CG  . TRP   B 1 22  ? 13.928 -8.390  16.106 1.00 12.57 ? 28  TRP   C CG  1 
ATOM   1279 C  CD1 . TRP   B 1 22  ? 14.587 -8.911  15.036 1.00 13.94 ? 28  TRP   C CD1 1 
ATOM   1280 C  CD2 . TRP   B 1 22  ? 14.929 -7.801  16.954 1.00 10.56 ? 28  TRP   C CD2 1 
ATOM   1281 N  NE1 . TRP   B 1 22  ? 15.947 -8.638  15.141 1.00 13.35 ? 28  TRP   C NE1 1 
ATOM   1282 C  CE2 . TRP   B 1 22  ? 16.173 -7.937  16.305 1.00 12.30 ? 28  TRP   C CE2 1 
ATOM   1283 C  CE3 . TRP   B 1 22  ? 14.885 -7.085  18.173 1.00 13.54 ? 28  TRP   C CE3 1 
ATOM   1284 C  CZ2 . TRP   B 1 22  ? 17.353 -7.411  16.819 1.00 11.75 ? 28  TRP   C CZ2 1 
ATOM   1285 C  CZ3 . TRP   B 1 22  ? 16.074 -6.567  18.682 1.00 14.77 ? 28  TRP   C CZ3 1 
ATOM   1286 C  CH2 . TRP   B 1 22  ? 17.289 -6.739  18.006 1.00 13.78 ? 28  TRP   C CH2 1 
ATOM   1287 N  N   . ALA   B 1 23  ? 9.614  -9.699  17.488 1.00 12.47 ? 29  ALA   C N   1 
ATOM   1288 C  CA  . ALA   B 1 23  ? 8.281  -9.465  18.075 1.00 12.61 ? 29  ALA   C CA  1 
ATOM   1289 C  C   . ALA   B 1 23  ? 8.019  -10.340 19.301 1.00 13.98 ? 29  ALA   C C   1 
ATOM   1290 O  O   . ALA   B 1 23  ? 7.030  -10.141 20.020 1.00 15.35 ? 29  ALA   C O   1 
ATOM   1291 C  CB  . ALA   B 1 23  ? 7.187  -9.692  17.029 1.00 14.78 ? 29  ALA   C CB  1 
ATOM   1292 N  N   . ASN   B 1 24  ? 8.865  -11.368 19.537 1.00 13.81 ? 30  ASN   C N   1 
ATOM   1293 C  CA  . ASN   B 1 24  ? 8.788  -12.316 20.664 1.00 13.36 ? 30  ASN   C CA  1 
ATOM   1294 C  C   . ASN   B 1 24  ? 10.160 -12.361 21.357 1.00 13.56 ? 30  ASN   C C   1 
ATOM   1295 O  O   . ASN   B 1 24  ? 10.591 -13.433 21.795 1.00 13.64 ? 30  ASN   C O   1 
ATOM   1296 C  CB  . ASN   B 1 24  ? 8.337  -13.701 20.147 1.00 14.85 ? 30  ASN   C CB  1 
ATOM   1297 C  CG  . ASN   B 1 24  ? 6.927  -13.650 19.658 1.00 15.84 ? 30  ASN   C CG  1 
ATOM   1298 O  OD1 . ASN   B 1 24  ? 5.967  -13.684 20.480 1.00 18.59 ? 30  ASN   C OD1 1 
ATOM   1299 N  ND2 . ASN   B 1 24  ? 6.702  -13.499 18.363 1.00 16.90 ? 30  ASN   C ND2 1 
ATOM   1300 N  N   . LEU   B 1 25  ? 10.851 -11.230 21.451 1.00 13.89 ? 31  LEU   C N   1 
ATOM   1301 C  CA  . LEU   B 1 25  ? 12.230 -11.206 21.947 1.00 13.12 ? 31  LEU   C CA  1 
ATOM   1302 C  C   . LEU   B 1 25  ? 12.357 -11.545 23.413 1.00 14.09 ? 31  LEU   C C   1 
ATOM   1303 O  O   . LEU   B 1 25  ? 11.587 -11.041 24.248 1.00 15.14 ? 31  LEU   C O   1 
ATOM   1304 C  CB  . LEU   B 1 25  ? 12.777 -9.801  21.702 1.00 14.31 ? 31  LEU   C CB  1 
ATOM   1305 C  CG  . LEU   B 1 25  ? 14.246 -9.629  22.068 1.00 13.98 ? 31  LEU   C CG  1 
ATOM   1306 C  CD1 . LEU   B 1 25  ? 15.169 -10.493 21.190 1.00 13.91 ? 31  LEU   C CD1 1 
ATOM   1307 C  CD2 . LEU   B 1 25  ? 14.657 -8.181  21.965 1.00 15.96 ? 31  LEU   C CD2 1 
ATOM   1308 N  N   . VAL   B 1 26  ? 13.353 -12.363 23.750 1.00 12.61 ? 32  VAL   C N   1 
ATOM   1309 C  CA  . VAL   B 1 26  ? 13.711 -12.641 25.144 1.00 13.09 ? 32  VAL   C CA  1 
ATOM   1310 C  C   . VAL   B 1 26  ? 15.015 -11.909 25.479 1.00 13.32 ? 32  VAL   C C   1 
ATOM   1311 O  O   . VAL   B 1 26  ? 15.131 -11.236 26.512 1.00 16.02 ? 32  VAL   C O   1 
ATOM   1312 C  CB  . VAL   B 1 26  ? 13.845 -14.145 25.388 1.00 14.08 ? 32  VAL   C CB  1 
ATOM   1313 C  CG1 . VAL   B 1 26  ? 14.399 -14.447 26.791 1.00 16.22 ? 32  VAL   C CG1 1 
ATOM   1314 C  CG2 . VAL   B 1 26  ? 12.503 -14.839 25.169 1.00 14.74 ? 32  VAL   C CG2 1 
ATOM   1315 N  N   . TRP   B 1 27  ? 16.047 -12.029 24.617 1.00 12.41 ? 33  TRP   C N   1 
ATOM   1316 C  CA  . TRP   B 1 27  ? 17.372 -11.468 24.890 1.00 12.85 ? 33  TRP   C CA  1 
ATOM   1317 C  C   . TRP   B 1 27  ? 18.151 -11.394 23.576 1.00 12.38 ? 33  TRP   C C   1 
ATOM   1318 O  O   . TRP   B 1 27  ? 17.971 -12.270 22.718 1.00 12.71 ? 33  TRP   C O   1 
ATOM   1319 C  CB  . TRP   B 1 27  ? 18.121 -12.352 25.947 1.00 13.85 ? 33  TRP   C CB  1 
ATOM   1320 C  CG  . TRP   B 1 27  ? 19.603 -12.068 26.112 1.00 14.31 ? 33  TRP   C CG  1 
ATOM   1321 C  CD1 . TRP   B 1 27  ? 20.188 -11.127 26.920 1.00 16.65 ? 33  TRP   C CD1 1 
ATOM   1322 C  CD2 . TRP   B 1 27  ? 20.687 -12.776 25.479 1.00 13.41 ? 33  TRP   C CD2 1 
ATOM   1323 N  NE1 . TRP   B 1 27  ? 21.568 -11.203 26.824 1.00 17.64 ? 33  TRP   C NE1 1 
ATOM   1324 C  CE2 . TRP   B 1 27  ? 21.898 -12.233 25.967 1.00 15.73 ? 33  TRP   C CE2 1 
ATOM   1325 C  CE3 . TRP   B 1 27  ? 20.747 -13.832 24.562 1.00 13.38 ? 33  TRP   C CE3 1 
ATOM   1326 C  CZ2 . TRP   B 1 27  ? 23.164 -12.737 25.579 1.00 14.82 ? 33  TRP   C CZ2 1 
ATOM   1327 C  CZ3 . TRP   B 1 27  ? 21.996 -14.336 24.204 1.00 13.84 ? 33  TRP   C CZ3 1 
ATOM   1328 C  CH2 . TRP   B 1 27  ? 23.181 -13.743 24.650 1.00 14.27 ? 33  TRP   C CH2 1 
ATOM   1329 N  N   . GLU   B 1 28  ? 19.010 -10.402 23.417 1.00 11.65 ? 34  GLU   C N   1 
ATOM   1330 C  CA  . GLU   B 1 28  ? 19.856 -10.295 22.232 1.00 12.82 ? 34  GLU   C CA  1 
ATOM   1331 C  C   . GLU   B 1 28  ? 21.151 -9.612  22.595 1.00 12.81 ? 34  GLU   C C   1 
ATOM   1332 O  O   . GLU   B 1 28  ? 21.176 -8.729  23.513 1.00 13.50 ? 34  GLU   C O   1 
ATOM   1333 C  CB  . GLU   B 1 28  ? 19.146 -9.634  21.053 1.00 13.67 ? 34  GLU   C CB  1 
ATOM   1334 C  CG  . GLU   B 1 28  ? 18.613 -8.244  21.349 1.00 14.45 ? 34  GLU   C CG  1 
ATOM   1335 C  CD  . GLU   B 1 28  ? 19.601 -7.097  21.287 1.00 15.51 ? 34  GLU   C CD  1 
ATOM   1336 O  OE1 . GLU   B 1 28  ? 19.306 -6.052  21.918 1.00 18.44 ? 34  GLU   C OE1 1 
ATOM   1337 O  OE2 . GLU   B 1 28  ? 20.599 -7.164  20.526 1.00 15.19 ? 34  GLU   C OE2 1 
ATOM   1338 N  N   . ASP   B 1 29  ? 22.236 -9.966  21.893 1.00 12.08 ? 35  ASP   C N   1 
ATOM   1339 C  CA  . ASP   B 1 29  ? 23.534 -9.339  22.124 1.00 12.24 ? 35  ASP   C CA  1 
ATOM   1340 C  C   . ASP   B 1 29  ? 24.306 -9.309  20.813 1.00 12.02 ? 35  ASP   C C   1 
ATOM   1341 O  O   . ASP   B 1 29  ? 24.768 -10.357 20.324 1.00 11.84 ? 35  ASP   C O   1 
ATOM   1342 C  CB  . ASP   B 1 29  ? 24.253 -10.121 23.234 1.00 13.69 ? 35  ASP   C CB  1 
ATOM   1343 C  CG  . ASP   B 1 29  ? 25.604 -9.584  23.634 1.00 16.24 ? 35  ASP   C CG  1 
ATOM   1344 O  OD1 . ASP   B 1 29  ? 26.337 -9.125  22.760 1.00 16.78 ? 35  ASP   C OD1 1 
ATOM   1345 O  OD2 . ASP   B 1 29  ? 25.977 -9.730  24.819 1.00 19.61 ? 35  ASP   C OD2 1 
ATOM   1346 N  N   . SER   B 1 30  ? 24.483 -8.102  20.244 1.00 12.43 ? 36  SER   C N   1 
ATOM   1347 C  CA  A SER   B 1 30  ? 25.192 -7.921  18.984 0.50 12.33 ? 36  SER   C CA  1 
ATOM   1348 C  CA  B SER   B 1 30  ? 25.170 -7.982  18.974 0.50 12.93 ? 36  SER   C CA  1 
ATOM   1349 C  C   . SER   B 1 30  ? 26.655 -8.383  19.076 1.00 12.84 ? 36  SER   C C   1 
ATOM   1350 O  O   . SER   B 1 30  ? 27.161 -9.011  18.127 1.00 12.92 ? 36  SER   C O   1 
ATOM   1351 C  CB  A SER   B 1 30  ? 25.149 -6.463  18.542 0.50 12.76 ? 36  SER   C CB  1 
ATOM   1352 C  CB  B SER   B 1 30  ? 24.998 -6.592  18.389 0.50 15.01 ? 36  SER   C CB  1 
ATOM   1353 O  OG  A SER   B 1 30  ? 26.048 -6.236  17.463 0.50 12.72 ? 36  SER   C OG  1 
ATOM   1354 O  OG  B SER   B 1 30  ? 25.454 -5.642  19.329 0.50 16.28 ? 36  SER   C OG  1 
ATOM   1355 N  N   . SER   B 1 31  ? 27.318 -8.103  20.202 1.00 12.53 ? 37  SER   C N   1 
ATOM   1356 C  CA  . SER   B 1 31  ? 28.729 -8.494  20.328 1.00 13.26 ? 37  SER   C CA  1 
ATOM   1357 C  C   . SER   B 1 31  ? 28.909 -10.013 20.296 1.00 11.80 ? 37  SER   C C   1 
ATOM   1358 O  O   . SER   B 1 31  ? 29.984 -10.452 19.906 1.00 13.00 ? 37  SER   C O   1 
ATOM   1359 C  CB  . SER   B 1 31  ? 29.324 -7.934  21.603 1.00 16.93 ? 37  SER   C CB  1 
ATOM   1360 O  OG  . SER   B 1 31  ? 28.970 -8.650  22.766 1.00 20.90 ? 37  SER   C OG  1 
ATOM   1361 N  N   . ARG   B 1 32  ? 27.853 -10.805 20.614 1.00 11.16 ? 38  ARG   C N   1 
ATOM   1362 C  CA  . ARG   B 1 32  ? 27.931 -12.273 20.563 1.00 10.89 ? 38  ARG   C CA  1 
ATOM   1363 C  C   . ARG   B 1 32  ? 27.305 -12.842 19.291 1.00 10.82 ? 38  ARG   C C   1 
ATOM   1364 O  O   . ARG   B 1 32  ? 27.349 -14.070 19.081 1.00 10.59 ? 38  ARG   C O   1 
ATOM   1365 C  CB  . ARG   B 1 32  ? 27.187 -12.869 21.781 1.00 12.71 ? 38  ARG   C CB  1 
ATOM   1366 C  CG  . ARG   B 1 32  ? 27.859 -12.486 23.098 1.00 14.10 ? 38  ARG   C CG  1 
ATOM   1367 C  CD  . ARG   B 1 32  ? 27.125 -13.065 24.298 1.00 11.73 ? 38  ARG   C CD  1 
ATOM   1368 N  NE  . ARG   B 1 32  ? 27.176 -14.543 24.332 1.00 11.43 ? 38  ARG   C NE  1 
ATOM   1369 C  CZ  . ARG   B 1 32  ? 27.143 -15.287 25.449 1.00 11.16 ? 38  ARG   C CZ  1 
ATOM   1370 N  NH1 . ARG   B 1 32  ? 27.024 -14.716 26.635 1.00 12.87 ? 38  ARG   C NH1 1 
ATOM   1371 N  NH2 . ARG   B 1 32  ? 27.282 -16.604 25.380 1.00 12.21 ? 38  ARG   C NH2 1 
ATOM   1372 N  N   . ASP   B 1 33  ? 26.644 -11.993 18.458 1.00 10.47 ? 39  ASP   C N   1 
ATOM   1373 C  CA  . ASP   B 1 33  ? 25.856 -12.451 17.320 1.00 10.06 ? 39  ASP   C CA  1 
ATOM   1374 C  C   . ASP   B 1 33  ? 24.754 -13.429 17.759 1.00 9.58  ? 39  ASP   C C   1 
ATOM   1375 O  O   . ASP   B 1 33  ? 24.452 -14.381 16.986 1.00 9.87  ? 39  ASP   C O   1 
ATOM   1376 C  CB  . ASP   B 1 33  ? 26.695 -13.066 16.190 1.00 9.95  ? 39  ASP   C CB  1 
ATOM   1377 C  CG  . ASP   B 1 33  ? 25.920 -13.396 14.925 1.00 11.05 ? 39  ASP   C CG  1 
ATOM   1378 O  OD1 . ASP   B 1 33  ? 25.019 -12.600 14.545 1.00 11.32 ? 39  ASP   C OD1 1 
ATOM   1379 O  OD2 . ASP   B 1 33  ? 26.252 -14.431 14.280 1.00 10.78 ? 39  ASP   C OD2 1 
ATOM   1380 N  N   . LEU   B 1 34  ? 24.080 -13.205 18.908 1.00 9.51  ? 40  LEU   C N   1 
ATOM   1381 C  CA  . LEU   B 1 34  ? 23.001 -14.104 19.335 1.00 9.68  ? 40  LEU   C CA  1 
ATOM   1382 C  C   . LEU   B 1 34  ? 21.691 -13.353 19.590 1.00 9.84  ? 40  LEU   C C   1 
ATOM   1383 O  O   . LEU   B 1 34  ? 21.707 -12.194 20.073 1.00 9.94  ? 40  LEU   C O   1 
ATOM   1384 C  CB  . LEU   B 1 34  ? 23.405 -14.801 20.655 1.00 10.53 ? 40  LEU   C CB  1 
ATOM   1385 C  CG  . LEU   B 1 34  ? 24.474 -15.917 20.548 1.00 10.47 ? 40  LEU   C CG  1 
ATOM   1386 C  CD1 . LEU   B 1 34  ? 24.734 -16.512 21.948 1.00 12.52 ? 40  LEU   C CD1 1 
ATOM   1387 C  CD2 . LEU   B 1 34  ? 24.031 -17.033 19.578 1.00 11.03 ? 40  LEU   C CD2 1 
ATOM   1388 N  N   . LEU   B 1 35  ? 20.591 -14.038 19.357 1.00 9.51  ? 41  LEU   C N   1 
ATOM   1389 C  CA  . LEU   B 1 35  ? 19.264 -13.548 19.723 1.00 10.17 ? 41  LEU   C CA  1 
ATOM   1390 C  C   . LEU   B 1 35  ? 18.434 -14.765 20.122 1.00 9.42  ? 41  LEU   C C   1 
ATOM   1391 O  O   . LEU   B 1 35  ? 18.532 -15.842 19.491 1.00 10.53 ? 41  LEU   C O   1 
ATOM   1392 C  CB  . LEU   B 1 35  ? 18.622 -12.815 18.510 1.00 10.68 ? 41  LEU   C CB  1 
ATOM   1393 C  CG  . LEU   B 1 35  ? 17.235 -12.205 18.764 1.00 11.20 ? 41  LEU   C CG  1 
ATOM   1394 C  CD1 . LEU   B 1 35  ? 17.040 -10.902 18.000 1.00 12.92 ? 41  LEU   C CD1 1 
ATOM   1395 C  CD2 . LEU   B 1 35  ? 16.129 -13.234 18.393 1.00 12.41 ? 41  LEU   C CD2 1 
ATOM   1396 N  N   . VAL   B 1 36  ? 17.641 -14.590 21.167 1.00 9.77  ? 42  VAL   C N   1 
ATOM   1397 C  CA  . VAL   B 1 36  ? 16.730 -15.614 21.680 1.00 10.28 ? 42  VAL   C CA  1 
ATOM   1398 C  C   . VAL   B 1 36  ? 15.306 -15.089 21.683 1.00 10.16 ? 42  VAL   C C   1 
ATOM   1399 O  O   . VAL   B 1 36  ? 15.076 -13.963 22.193 1.00 11.57 ? 42  VAL   C O   1 
ATOM   1400 C  CB  . VAL   B 1 36  ? 17.137 -16.055 23.108 1.00 10.94 ? 42  VAL   C CB  1 
ATOM   1401 C  CG1 . VAL   B 1 36  ? 16.162 -17.110 23.649 1.00 13.02 ? 42  VAL   C CG1 1 
ATOM   1402 C  CG2 . VAL   B 1 36  ? 18.584 -16.602 23.098 1.00 12.02 ? 42  VAL   C CG2 1 
ATOM   1403 N  N   . SER   B 1 37  ? 14.383 -15.845 21.104 1.00 10.87 ? 43  SER   C N   1 
ATOM   1404 C  CA  . SER   B 1 37  ? 12.953 -15.492 21.069 1.00 11.20 ? 43  SER   C CA  1 
ATOM   1405 C  C   . SER   B 1 37  ? 12.163 -16.606 21.774 1.00 11.77 ? 43  SER   C C   1 
ATOM   1406 O  O   . SER   B 1 37  ? 12.652 -17.708 22.042 1.00 12.34 ? 43  SER   C O   1 
ATOM   1407 C  CB  . SER   B 1 37  ? 12.466 -15.285 19.638 1.00 11.89 ? 43  SER   C CB  1 
ATOM   1408 O  OG  . SER   B 1 37  ? 12.648 -16.449 18.848 1.00 12.18 ? 43  SER   C OG  1 
ATOM   1409 N  N   . SER   B 1 38  ? 10.944 -16.270 22.173 1.00 12.80 ? 44  SER   C N   1 
ATOM   1410 C  CA  . SER   B 1 38  ? 10.049 -17.227 22.823 1.00 14.14 ? 44  SER   C CA  1 
ATOM   1411 C  C   . SER   B 1 38  ? 9.236  -18.033 21.805 1.00 15.50 ? 44  SER   C C   1 
ATOM   1412 O  O   . SER   B 1 38  ? 8.888  -17.541 20.731 1.00 17.17 ? 44  SER   C O   1 
ATOM   1413 C  CB  . SER   B 1 38  ? 9.137  -16.527 23.822 1.00 16.35 ? 44  SER   C CB  1 
ATOM   1414 O  OG  . SER   B 1 38  ? 8.310  -15.630 23.118 1.00 19.99 ? 44  SER   C OG  1 
ATOM   1415 N  N   . THR   B 1 39  ? 8.895  -19.268 22.142 1.00 15.36 ? 45  THR   C N   1 
ATOM   1416 C  CA  . THR   B 1 39  ? 8.141  -20.158 21.253 1.00 16.86 ? 45  THR   C CA  1 
ATOM   1417 C  C   . THR   B 1 39  ? 6.840  -20.606 21.939 1.00 18.72 ? 45  THR   C C   1 
ATOM   1418 O  O   . THR   B 1 39  ? 6.780  -20.731 23.159 1.00 18.76 ? 45  THR   C O   1 
ATOM   1419 C  CB  . THR   B 1 39  ? 8.985  -21.419 20.877 1.00 17.43 ? 45  THR   C CB  1 
ATOM   1420 O  OG1 . THR   B 1 39  ? 9.268  -22.164 22.047 1.00 18.20 ? 45  THR   C OG1 1 
ATOM   1421 C  CG2 . THR   B 1 39  ? 10.341 -21.084 20.217 1.00 18.05 ? 45  THR   C CG2 1 
ATOM   1422 N  N   . THR   B 1 40  ? 5.853  -20.988 21.121 1.00 21.15 ? 46  THR   C N   1 
ATOM   1423 C  CA  . THR   B 1 40  ? 4.610  -21.538 21.667 1.00 23.49 ? 46  THR   C CA  1 
ATOM   1424 C  C   . THR   B 1 40  ? 4.823  -23.008 22.015 1.00 23.54 ? 46  THR   C C   1 
ATOM   1425 O  O   . THR   B 1 40  ? 4.403  -23.468 23.093 1.00 25.88 ? 46  THR   C O   1 
ATOM   1426 C  CB  . THR   B 1 40  ? 3.469  -21.273 20.678 1.00 27.36 ? 46  THR   C CB  1 
ATOM   1427 O  OG1 . THR   B 1 40  ? 3.806  -21.847 19.416 1.00 30.59 ? 46  THR   C OG1 1 
ATOM   1428 C  CG2 . THR   B 1 40  ? 3.247  -19.802 20.457 1.00 27.00 ? 46  THR   C CG2 1 
ATOM   1429 N  N   . ALA   B 1 41  ? 5.518  -23.754 21.130 1.00 21.28 ? 47  ALA   C N   1 
ATOM   1430 C  CA  . ALA   B 1 41  ? 5.789  -25.162 21.362 1.00 22.50 ? 47  ALA   C CA  1 
ATOM   1431 C  C   . ALA   B 1 41  ? 7.105  -25.405 22.121 1.00 21.30 ? 47  ALA   C C   1 
ATOM   1432 O  O   . ALA   B 1 41  ? 8.045  -24.650 21.931 1.00 21.44 ? 47  ALA   C O   1 
ATOM   1433 C  CB  . ALA   B 1 41  ? 5.845  -25.882 20.021 1.00 24.74 ? 47  ALA   C CB  1 
ATOM   1434 N  N   . GLN   B 1 42  ? 7.193  -26.450 22.935 1.00 20.74 ? 48  GLN   C N   1 
ATOM   1435 C  CA  . GLN   B 1 42  ? 8.408  -26.814 23.637 1.00 21.00 ? 48  GLN   C CA  1 
ATOM   1436 C  C   . GLN   B 1 42  ? 9.376  -27.511 22.691 1.00 19.42 ? 48  GLN   C C   1 
ATOM   1437 O  O   . GLN   B 1 42  ? 9.000  -28.352 21.879 1.00 20.65 ? 48  GLN   C O   1 
ATOM   1438 C  CB  . GLN   B 1 42  ? 8.102  -27.746 24.828 1.00 26.63 ? 48  GLN   C CB  1 
ATOM   1439 C  CG  . GLN   B 1 42  ? 7.471  -27.021 26.007 1.00 35.60 ? 48  GLN   C CG  1 
ATOM   1440 C  CD  . GLN   B 1 42  ? 7.360  -27.990 27.155 1.00 45.65 ? 48  GLN   C CD  1 
ATOM   1441 O  OE1 . GLN   B 1 42  ? 6.524  -28.905 27.158 1.00 49.43 ? 48  GLN   C OE1 1 
ATOM   1442 N  NE2 . GLN   B 1 42  ? 8.214  -27.841 28.149 1.00 47.75 ? 48  GLN   C NE2 1 
ATOM   1443 N  N   . GLY   B 1 43  ? 10.634 -27.135 22.815 1.00 16.92 ? 49  GLY   C N   1 
ATOM   1444 C  CA  . GLY   B 1 43  ? 11.719 -27.734 22.060 1.00 16.93 ? 49  GLY   C CA  1 
ATOM   1445 C  C   . GLY   B 1 43  ? 12.427 -28.786 22.884 1.00 16.16 ? 49  GLY   C C   1 
ATOM   1446 O  O   . GLY   B 1 43  ? 12.225 -28.868 24.110 1.00 19.18 ? 49  GLY   C O   1 
ATOM   1447 N  N   . CYS   B 1 44  ? 13.250 -29.571 22.222 1.00 14.88 ? 50  CYS   C N   1 
ATOM   1448 C  CA  . CYS   B 1 44  ? 13.879 -30.754 22.813 1.00 15.53 ? 50  CYS   C CA  1 
ATOM   1449 C  C   . CYS   B 1 44  ? 15.378 -30.781 22.781 1.00 15.51 ? 50  CYS   C C   1 
ATOM   1450 O  O   . CYS   B 1 44  ? 15.974 -31.833 23.159 1.00 18.05 ? 50  CYS   C O   1 
ATOM   1451 C  CB  . CYS   B 1 44  ? 13.328 -31.993 22.123 1.00 17.03 ? 50  CYS   C CB  1 
ATOM   1452 S  SG  . CYS   B 1 44  ? 11.552 -32.164 22.275 1.00 21.69 ? 50  CYS   C SG  1 
ATOM   1453 N  N   . ASP   B 1 45  ? 16.043 -29.723 22.326 1.00 13.70 ? 51  ASP   C N   1 
ATOM   1454 C  CA  . ASP   B 1 45  ? 17.496 -29.724 22.293 1.00 14.24 ? 51  ASP   C CA  1 
ATOM   1455 C  C   . ASP   B 1 45  ? 17.953 -29.557 23.751 1.00 14.79 ? 51  ASP   C C   1 
ATOM   1456 O  O   . ASP   B 1 45  ? 17.287 -28.854 24.551 1.00 17.63 ? 51  ASP   C O   1 
ATOM   1457 C  CB  . ASP   B 1 45  ? 18.044 -28.583 21.443 1.00 14.12 ? 51  ASP   C CB  1 
ATOM   1458 C  CG  . ASP   B 1 45  ? 17.852 -28.771 19.965 1.00 16.94 ? 51  ASP   C CG  1 
ATOM   1459 O  OD1 . ASP   B 1 45  ? 17.934 -29.921 19.499 1.00 19.54 ? 51  ASP   C OD1 1 
ATOM   1460 O  OD2 . ASP   B 1 45  ? 17.708 -27.741 19.230 1.00 15.49 ? 51  ASP   C OD2 1 
ATOM   1461 N  N   . THR   B 1 46  ? 19.057 -30.207 24.093 1.00 13.24 ? 52  THR   C N   1 
ATOM   1462 C  CA  . THR   B 1 46  ? 19.666 -30.040 25.399 1.00 13.43 ? 52  THR   C CA  1 
ATOM   1463 C  C   . THR   B 1 46  ? 20.923 -29.168 25.228 1.00 12.40 ? 52  THR   C C   1 
ATOM   1464 O  O   . THR   B 1 46  ? 21.769 -29.503 24.362 1.00 12.83 ? 52  THR   C O   1 
ATOM   1465 C  CB  . THR   B 1 46  ? 20.060 -31.404 25.948 1.00 15.43 ? 52  THR   C CB  1 
ATOM   1466 O  OG1 . THR   B 1 46  ? 18.851 -32.170 26.182 1.00 17.33 ? 52  THR   C OG1 1 
ATOM   1467 C  CG2 . THR   B 1 46  ? 20.857 -31.301 27.258 1.00 17.63 ? 52  THR   C CG2 1 
ATOM   1468 N  N   . ILE   B 1 47  ? 21.106 -28.135 26.050 1.00 12.42 ? 53  ILE   C N   1 
ATOM   1469 C  CA  . ILE   B 1 47  ? 22.306 -27.309 26.013 1.00 11.97 ? 53  ILE   C CA  1 
ATOM   1470 C  C   . ILE   B 1 47  ? 23.394 -27.992 26.859 1.00 12.08 ? 53  ILE   C C   1 
ATOM   1471 O  O   . ILE   B 1 47  ? 23.147 -28.435 27.997 1.00 13.23 ? 53  ILE   C O   1 
ATOM   1472 C  CB  . ILE   B 1 47  ? 22.027 -25.928 26.595 1.00 13.22 ? 53  ILE   C CB  1 
ATOM   1473 C  CG1 . ILE   B 1 47  ? 20.808 -25.263 25.902 1.00 14.25 ? 53  ILE   C CG1 1 
ATOM   1474 C  CG2 . ILE   B 1 47  ? 23.287 -25.067 26.501 1.00 13.33 ? 53  ILE   C CG2 1 
ATOM   1475 C  CD1 . ILE   B 1 47  ? 21.016 -25.097 24.365 1.00 16.04 ? 53  ILE   C CD1 1 
ATOM   1476 N  N   . ALA   B 1 48  ? 24.607 -28.067 26.325 1.00 11.39 ? 54  ALA   C N   1 
ATOM   1477 C  CA  . ALA   B 1 48  ? 25.748 -28.627 27.080 1.00 10.77 ? 54  ALA   C CA  1 
ATOM   1478 C  C   . ALA   B 1 48  ? 26.091 -27.681 28.248 1.00 10.22 ? 54  ALA   C C   1 
ATOM   1479 O  O   . ALA   B 1 48  ? 26.055 -26.441 28.093 1.00 10.67 ? 54  ALA   C O   1 
ATOM   1480 C  CB  . ALA   B 1 48  ? 26.958 -28.707 26.152 1.00 10.55 ? 54  ALA   C CB  1 
ATOM   1481 N  N   . ARG   B 1 49  ? 26.456 -28.277 29.399 1.00 10.82 ? 55  ARG   C N   1 
ATOM   1482 C  CA  . ARG   B 1 49  ? 26.908 -27.515 30.559 1.00 10.80 ? 55  ARG   C CA  1 
ATOM   1483 C  C   . ARG   B 1 49  ? 28.228 -28.163 30.946 1.00 11.08 ? 55  ARG   C C   1 
ATOM   1484 O  O   . ARG   B 1 49  ? 28.246 -29.188 31.643 1.00 12.17 ? 55  ARG   C O   1 
ATOM   1485 C  CB  . ARG   B 1 49  ? 25.875 -27.558 31.692 1.00 12.18 ? 55  ARG   C CB  1 
ATOM   1486 C  CG  . ARG   B 1 49  ? 24.505 -26.995 31.259 1.00 11.56 ? 55  ARG   C CG  1 
ATOM   1487 C  CD  . ARG   B 1 49  ? 24.492 -25.515 30.899 1.00 13.00 ? 55  ARG   C CD  1 
ATOM   1488 N  NE  . ARG   B 1 49  ? 23.133 -25.089 30.525 1.00 12.63 ? 55  ARG   C NE  1 
ATOM   1489 C  CZ  . ARG   B 1 49  ? 22.873 -23.991 29.813 1.00 12.60 ? 55  ARG   C CZ  1 
ATOM   1490 N  NH1 . ARG   B 1 49  ? 23.844 -23.150 29.499 1.00 12.87 ? 55  ARG   C NH1 1 
ATOM   1491 N  NH2 . ARG   B 1 49  ? 21.613 -23.705 29.430 1.00 14.00 ? 55  ARG   C NH2 1 
ATOM   1492 N  N   . CYS   B 1 50  ? 29.329 -27.588 30.430 1.00 10.14 ? 56  CYS   C N   1 
ATOM   1493 C  CA  . CYS   B 1 50  ? 30.666 -28.230 30.436 1.00 10.40 ? 56  CYS   C CA  1 
ATOM   1494 C  C   . CYS   B 1 50  ? 31.708 -27.239 29.922 1.00 10.74 ? 56  CYS   C C   1 
ATOM   1495 O  O   . CYS   B 1 50  ? 31.378 -26.145 29.466 1.00 11.00 ? 56  CYS   C O   1 
ATOM   1496 C  CB  . CYS   B 1 50  ? 30.624 -29.450 29.508 1.00 9.93  ? 56  CYS   C CB  1 
ATOM   1497 S  SG  . CYS   B 1 50  ? 30.470 -29.002 27.747 1.00 10.57 ? 56  CYS   C SG  1 
ATOM   1498 N  N   . ASP   B 1 51  ? 33.002 -27.682 29.975 1.00 11.45 ? 57  ASP   C N   1 
ATOM   1499 C  CA  . ASP   B 1 51  ? 34.121 -26.962 29.389 1.00 12.69 ? 57  ASP   C CA  1 
ATOM   1500 C  C   . ASP   B 1 51  ? 34.779 -27.843 28.305 1.00 11.35 ? 57  ASP   C C   1 
ATOM   1501 O  O   . ASP   B 1 51  ? 35.987 -27.675 28.044 1.00 13.06 ? 57  ASP   C O   1 
ATOM   1502 C  CB  . ASP   B 1 51  ? 35.133 -26.508 30.452 1.00 14.92 ? 57  ASP   C CB  1 
ATOM   1503 C  CG  . ASP   B 1 51  ? 35.829 -27.632 31.166 1.00 19.27 ? 57  ASP   C CG  1 
ATOM   1504 O  OD1 . ASP   B 1 51  ? 35.514 -28.805 30.905 1.00 17.92 ? 57  ASP   C OD1 1 
ATOM   1505 O  OD2 . ASP   B 1 51  ? 36.760 -27.338 31.984 1.00 24.75 ? 57  ASP   C OD2 1 
ATOM   1506 N  N   . CYS   B 1 52  ? 34.006 -28.708 27.586 1.00 10.81 ? 58  CYS   C N   1 
ATOM   1507 C  CA  . CYS   B 1 52  ? 34.610 -29.457 26.456 1.00 10.98 ? 58  CYS   C CA  1 
ATOM   1508 C  C   . CYS   B 1 52  ? 35.269 -28.534 25.450 1.00 10.14 ? 58  CYS   C C   1 
ATOM   1509 O  O   . CYS   B 1 52  ? 34.823 -27.386 25.222 1.00 10.54 ? 58  CYS   C O   1 
ATOM   1510 C  CB  . CYS   B 1 52  ? 33.552 -30.299 25.722 1.00 10.80 ? 58  CYS   C CB  1 
ATOM   1511 S  SG  . CYS   B 1 52  ? 32.914 -31.705 26.667 1.00 11.32 ? 58  CYS   C SG  1 
ATOM   1512 N  N   . GLN   B 1 53  ? 36.304 -29.065 24.819 1.00 9.51  ? 59  GLN   C N   1 
ATOM   1513 C  CA  . GLN   B 1 53  ? 36.985 -28.469 23.681 1.00 10.73 ? 59  GLN   C CA  1 
ATOM   1514 C  C   . GLN   B 1 53  ? 37.057 -29.398 22.507 1.00 9.73  ? 59  GLN   C C   1 
ATOM   1515 O  O   . GLN   B 1 53  ? 37.827 -29.161 21.568 1.00 10.58 ? 59  GLN   C O   1 
ATOM   1516 C  CB  . GLN   B 1 53  ? 38.402 -27.962 24.045 1.00 11.68 ? 59  GLN   C CB  1 
ATOM   1517 C  CG  . GLN   B 1 53  ? 38.387 -26.763 24.975 1.00 14.88 ? 59  GLN   C CG  1 
ATOM   1518 C  CD  . GLN   B 1 53  ? 39.756 -26.203 25.204 1.00 15.95 ? 59  GLN   C CD  1 
ATOM   1519 O  OE1 . GLN   B 1 53  ? 40.243 -26.225 26.350 1.00 18.82 ? 59  GLN   C OE1 1 
ATOM   1520 N  NE2 . GLN   B 1 53  ? 40.393 -25.663 24.157 1.00 15.00 ? 59  GLN   C NE2 1 
ATOM   1521 N  N   . THR   B 1 54  ? 36.277 -30.495 22.509 1.00 9.63  ? 60  THR   C N   1 
ATOM   1522 C  CA  . THR   B 1 54  ? 36.171 -31.360 21.329 1.00 9.85  ? 60  THR   C CA  1 
ATOM   1523 C  C   . THR   B 1 54  ? 34.676 -31.612 21.083 1.00 9.57  ? 60  THR   C C   1 
ATOM   1524 O  O   . THR   B 1 54  ? 33.890 -31.744 22.027 1.00 10.74 ? 60  THR   C O   1 
ATOM   1525 C  CB  . THR   B 1 54  ? 36.912 -32.645 21.429 1.00 13.42 ? 60  THR   C CB  1 
ATOM   1526 O  OG1 . THR   B 1 54  ? 36.348 -33.394 22.427 1.00 18.01 ? 60  THR   C OG1 1 
ATOM   1527 C  CG2 . THR   B 1 54  ? 38.363 -32.463 21.740 1.00 13.80 ? 60  THR   C CG2 1 
ATOM   1528 N  N   . GLY   B 1 55  ? 34.292 -31.681 19.804 1.00 9.19  ? 61  GLY   C N   1 
ATOM   1529 C  CA  . GLY   B 1 55  ? 32.883 -31.912 19.478 1.00 9.23  ? 61  GLY   C CA  1 
ATOM   1530 C  C   . GLY   B 1 55  ? 32.755 -32.096 17.977 1.00 8.22  ? 61  GLY   C C   1 
ATOM   1531 O  O   . GLY   B 1 55  ? 33.753 -32.382 17.290 1.00 9.00  ? 61  GLY   C O   1 
ATOM   1532 N  N   . VAL   B 1 56  ? 31.541 -31.974 17.465 1.00 7.64  ? 62  VAL   C N   1 
ATOM   1533 C  CA  . VAL   B 1 56  ? 31.238 -32.192 16.040 1.00 7.76  ? 62  VAL   C CA  1 
ATOM   1534 C  C   . VAL   B 1 56  ? 30.318 -31.065 15.600 1.00 7.69  ? 62  VAL   C C   1 
ATOM   1535 O  O   . VAL   B 1 56  ? 29.374 -30.727 16.313 1.00 8.47  ? 62  VAL   C O   1 
ATOM   1536 C  CB  . VAL   B 1 56  ? 30.511 -33.561 15.862 1.00 7.96  ? 62  VAL   C CB  1 
ATOM   1537 C  CG1 . VAL   B 1 56  ? 30.034 -33.741 14.418 1.00 9.69  ? 62  VAL   C CG1 1 
ATOM   1538 C  CG2 . VAL   B 1 56  ? 31.444 -34.713 16.280 1.00 9.19  ? 62  VAL   C CG2 1 
ATOM   1539 N  N   . TYR   B 1 57  ? 30.611 -30.444 14.423 1.00 7.92  ? 63  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 57  ? 29.715 -29.386 13.930 1.00 7.61  ? 63  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 57  ? 29.167 -29.734 12.558 1.00 8.09  ? 63  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 57  ? 29.822 -30.429 11.773 1.00 8.63  ? 63  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 57  ? 30.379 -27.963 13.907 1.00 8.07  ? 63  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 57  ? 31.259 -27.638 12.708 1.00 8.21  ? 63  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 57  ? 32.529 -28.169 12.586 1.00 9.56  ? 63  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 57  ? 30.804 -26.809 11.693 1.00 8.34  ? 63  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 57  ? 33.358 -27.846 11.506 1.00 9.82  ? 63  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 57  ? 31.619 -26.463 10.607 1.00 9.33  ? 63  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 57  ? 32.889 -26.996 10.506 1.00 9.48  ? 63  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 57  ? 33.753 -26.700 9.454  1.00 11.90 ? 63  TYR   C OH  1 
ATOM   1551 N  N   . TYR   B 1 58  ? 27.995 -29.159 12.257 1.00 7.78  ? 64  TYR   C N   1 
ATOM   1552 C  CA  . TYR   B 1 58  ? 27.395 -29.333 10.930 1.00 8.32  ? 64  TYR   C CA  1 
ATOM   1553 C  C   . TYR   B 1 58  ? 27.784 -28.173 10.004 1.00 8.65  ? 64  TYR   C C   1 
ATOM   1554 O  O   . TYR   B 1 58  ? 27.540 -26.989 10.330 1.00 8.93  ? 64  TYR   C O   1 
ATOM   1555 C  CB  . TYR   B 1 58  ? 25.869 -29.418 11.018 1.00 9.25  ? 64  TYR   C CB  1 
ATOM   1556 C  CG  . TYR   B 1 58  ? 25.272 -29.682 9.642  1.00 10.28 ? 64  TYR   C CG  1 
ATOM   1557 C  CD1 . TYR   B 1 58  ? 25.626 -30.817 8.920  1.00 10.70 ? 64  TYR   C CD1 1 
ATOM   1558 C  CD2 . TYR   B 1 58  ? 24.423 -28.770 9.040  1.00 10.96 ? 64  TYR   C CD2 1 
ATOM   1559 C  CE1 . TYR   B 1 58  ? 25.110 -31.060 7.642  1.00 11.98 ? 64  TYR   C CE1 1 
ATOM   1560 C  CE2 . TYR   B 1 58  ? 23.880 -29.025 7.763  1.00 11.71 ? 64  TYR   C CE2 1 
ATOM   1561 C  CZ  . TYR   B 1 58  ? 24.260 -30.156 7.085  1.00 11.53 ? 64  TYR   C CZ  1 
ATOM   1562 O  OH  . TYR   B 1 58  ? 23.813 -30.434 5.791  1.00 14.20 ? 64  TYR   C OH  1 
ATOM   1563 N  N   . CYS   B 1 59  ? 28.289 -28.525 8.811  1.00 8.69  ? 65  CYS   C N   1 
ATOM   1564 C  CA  . CYS   B 1 59  ? 28.697 -27.573 7.769  1.00 9.16  ? 65  CYS   C CA  1 
ATOM   1565 C  C   . CYS   B 1 59  ? 27.774 -27.738 6.558  1.00 8.87  ? 65  CYS   C C   1 
ATOM   1566 O  O   . CYS   B 1 59  ? 27.957 -28.677 5.760  1.00 10.30 ? 65  CYS   C O   1 
ATOM   1567 C  CB  . CYS   B 1 59  ? 30.143 -27.832 7.409  1.00 9.60  ? 65  CYS   C CB  1 
ATOM   1568 S  SG  . CYS   B 1 59  ? 30.753 -26.768 6.071  1.00 11.09 ? 65  CYS   C SG  1 
ATOM   1569 N  N   . SER   B 1 60  ? 26.768 -26.882 6.448  1.00 9.84  ? 66  SER   C N   1 
ATOM   1570 C  CA  A SER   B 1 60  ? 25.803 -27.045 5.365  0.50 11.50 ? 66  SER   C CA  1 
ATOM   1571 C  CA  B SER   B 1 60  ? 25.797 -26.976 5.367  0.50 10.79 ? 66  SER   C CA  1 
ATOM   1572 C  C   . SER   B 1 60  ? 26.427 -26.908 3.972  1.00 11.61 ? 66  SER   C C   1 
ATOM   1573 O  O   . SER   B 1 60  ? 26.010 -27.636 3.084  1.00 12.83 ? 66  SER   C O   1 
ATOM   1574 C  CB  A SER   B 1 60  ? 24.619 -26.116 5.545  0.50 14.41 ? 66  SER   C CB  1 
ATOM   1575 C  CB  B SER   B 1 60  ? 24.759 -25.874 5.498  0.50 11.39 ? 66  SER   C CB  1 
ATOM   1576 O  OG  A SER   B 1 60  ? 25.032 -24.771 5.398  0.50 17.16 ? 66  SER   C OG  1 
ATOM   1577 O  OG  B SER   B 1 60  ? 23.763 -26.086 4.510  0.50 11.90 ? 66  SER   C OG  1 
ATOM   1578 N  N   . SER   B 1 61  ? 27.447 -26.042 3.820  1.00 10.76 ? 67  SER   C N   1 
ATOM   1579 C  CA  . SER   B 1 61  ? 28.129 -25.859 2.508  1.00 11.49 ? 67  SER   C CA  1 
ATOM   1580 C  C   . SER   B 1 61  ? 28.963 -27.055 2.094  1.00 12.00 ? 67  SER   C C   1 
ATOM   1581 O  O   . SER   B 1 61  ? 29.480 -27.051 0.964  1.00 13.47 ? 67  SER   C O   1 
ATOM   1582 C  CB  . SER   B 1 61  ? 28.960 -24.585 2.491  1.00 12.45 ? 67  SER   C CB  1 
ATOM   1583 O  OG  . SER   B 1 61  ? 30.060 -24.683 3.370  1.00 12.90 ? 67  SER   C OG  1 
ATOM   1584 N  N   . ARG   B 1 62  ? 29.076 -28.101 2.943  1.00 11.02 ? 68  ARG   C N   1 
ATOM   1585 C  CA  . ARG   B 1 62  ? 29.715 -29.371 2.572  1.00 11.75 ? 68  ARG   C CA  1 
ATOM   1586 C  C   . ARG   B 1 62  ? 28.768 -30.558 2.770  1.00 11.59 ? 68  ARG   C C   1 
ATOM   1587 O  O   . ARG   B 1 62  ? 29.175 -31.711 2.540  1.00 13.20 ? 68  ARG   C O   1 
ATOM   1588 C  CB  . ARG   B 1 62  ? 30.987 -29.578 3.398  1.00 12.14 ? 68  ARG   C CB  1 
ATOM   1589 C  CG  . ARG   B 1 62  ? 32.059 -28.519 3.170  1.00 15.16 ? 68  ARG   C CG  1 
ATOM   1590 C  CD  . ARG   B 1 62  ? 32.718 -28.730 1.831  1.00 16.18 ? 68  ARG   C CD  1 
ATOM   1591 N  NE  . ARG   B 1 62  ? 33.775 -27.741 1.581  1.00 17.14 ? 68  ARG   C NE  1 
ATOM   1592 C  CZ  . ARG   B 1 62  ? 33.606 -26.577 1.003  1.00 18.07 ? 68  ARG   C CZ  1 
ATOM   1593 N  NH1 . ARG   B 1 62  ? 32.431 -26.253 0.466  1.00 19.43 ? 68  ARG   C NH1 1 
ATOM   1594 N  NH2 . ARG   B 1 62  ? 34.660 -25.783 0.774  1.00 22.18 ? 68  ARG   C NH2 1 
ATOM   1595 N  N   . ARG   B 1 63  ? 27.554 -30.334 3.278  1.00 11.99 ? 69  ARG   C N   1 
ATOM   1596 C  CA  . ARG   B 1 63  ? 26.598 -31.404 3.704  1.00 13.59 ? 69  ARG   C CA  1 
ATOM   1597 C  C   . ARG   B 1 63  ? 27.312 -32.442 4.560  1.00 14.37 ? 69  ARG   C C   1 
ATOM   1598 O  O   . ARG   B 1 63  ? 27.157 -33.655 4.358  1.00 16.64 ? 69  ARG   C O   1 
ATOM   1599 C  CB  . ARG   B 1 63  ? 25.958 -32.094 2.477  1.00 15.50 ? 69  ARG   C CB  1 
ATOM   1600 C  CG  . ARG   B 1 63  ? 25.153 -31.193 1.605  1.00 18.90 ? 69  ARG   C CG  1 
ATOM   1601 C  CD  . ARG   B 1 63  ? 23.923 -30.749 2.310  1.00 23.35 ? 69  ARG   C CD  1 
ATOM   1602 N  NE  . ARG   B 1 63  ? 22.923 -30.282 1.355  1.00 25.44 ? 69  ARG   C NE  1 
ATOM   1603 C  CZ  . ARG   B 1 63  ? 22.709 -29.012 1.063  1.00 26.70 ? 69  ARG   C CZ  1 
ATOM   1604 N  NH1 . ARG   B 1 63  ? 23.448 -28.056 1.626  1.00 26.38 ? 69  ARG   C NH1 1 
ATOM   1605 N  NH2 . ARG   B 1 63  ? 21.750 -28.677 0.217  1.00 26.60 ? 69  ARG   C NH2 1 
ATOM   1606 N  N   . LYS   B 1 64  ? 28.109 -31.953 5.530  1.00 12.34 ? 70  LYS   C N   1 
ATOM   1607 C  CA  . LYS   B 1 64  ? 28.907 -32.861 6.332  1.00 12.68 ? 70  LYS   C CA  1 
ATOM   1608 C  C   . LYS   B 1 64  ? 29.022 -32.393 7.766  1.00 10.91 ? 70  LYS   C C   1 
ATOM   1609 O  O   . LYS   B 1 64  ? 29.045 -31.170 8.008  1.00 11.99 ? 70  LYS   C O   1 
ATOM   1610 C  CB  . LYS   B 1 64  ? 30.326 -32.918 5.726  1.00 17.23 ? 70  LYS   C CB  1 
ATOM   1611 C  CG  . LYS   B 1 64  ? 30.470 -33.925 4.587  1.00 27.26 ? 70  LYS   C CG  1 
ATOM   1612 C  CD  . LYS   B 1 64  ? 31.929 -34.234 4.281  1.00 35.27 ? 70  LYS   C CD  1 
ATOM   1613 C  CE  . LYS   B 1 64  ? 32.053 -35.141 3.083  1.00 40.58 ? 70  LYS   C CE  1 
ATOM   1614 N  NZ  . LYS   B 1 64  ? 31.438 -34.537 1.870  1.00 44.01 ? 70  LYS   C NZ  1 
ATOM   1615 N  N   . HIS   B 1 65  ? 29.122 -33.349 8.675  1.00 9.93  ? 71  HIS   C N   1 
ATOM   1616 C  CA  . HIS   B 1 65  ? 29.432 -33.079 10.084 1.00 10.12 ? 71  HIS   C CA  1 
ATOM   1617 C  C   . HIS   B 1 65  ? 30.910 -33.362 10.269 1.00 12.41 ? 71  HIS   C C   1 
ATOM   1618 O  O   . HIS   B 1 65  ? 31.401 -34.464 9.889  1.00 15.43 ? 71  HIS   C O   1 
ATOM   1619 C  CB  . HIS   B 1 65  ? 28.619 -33.992 11.003 1.00 10.60 ? 71  HIS   C CB  1 
ATOM   1620 C  CG  . HIS   B 1 65  ? 27.143 -33.720 10.982 1.00 10.04 ? 71  HIS   C CG  1 
ATOM   1621 N  ND1 . HIS   B 1 65  ? 26.484 -32.955 11.936 1.00 12.87 ? 71  HIS   C ND1 1 
ATOM   1622 C  CD2 . HIS   B 1 65  ? 26.230 -34.135 10.073 1.00 9.74  ? 71  HIS   C CD2 1 
ATOM   1623 C  CE1 . HIS   B 1 65  ? 25.181 -32.970 11.601 1.00 10.63 ? 71  HIS   C CE1 1 
ATOM   1624 N  NE2 . HIS   B 1 65  ? 24.986 -33.664 10.498 1.00 13.64 ? 71  HIS   C NE2 1 
ATOM   1625 N  N   . TYR   B 1 66  ? 31.661 -32.437 10.885 1.00 10.16 ? 72  TYR   C N   1 
ATOM   1626 C  CA  . TYR   B 1 66  ? 33.095 -32.599 11.058 1.00 9.20  ? 72  TYR   C CA  1 
ATOM   1627 C  C   . TYR   B 1 66  ? 33.443 -32.642 12.549 1.00 9.11  ? 72  TYR   C C   1 
ATOM   1628 O  O   . TYR   B 1 66  ? 33.001 -31.759 13.309 1.00 8.76  ? 72  TYR   C O   1 
ATOM   1629 C  CB  . TYR   B 1 66  ? 33.842 -31.380 10.481 1.00 10.13 ? 72  TYR   C CB  1 
ATOM   1630 C  CG  . TYR   B 1 66  ? 33.799 -31.284 8.963  1.00 10.63 ? 72  TYR   C CG  1 
ATOM   1631 C  CD1 . TYR   B 1 66  ? 34.657 -32.038 8.176  1.00 12.93 ? 72  TYR   C CD1 1 
ATOM   1632 C  CD2 . TYR   B 1 66  ? 32.980 -30.366 8.323  1.00 11.68 ? 72  TYR   C CD2 1 
ATOM   1633 C  CE1 . TYR   B 1 66  ? 34.671 -31.911 6.791  1.00 13.86 ? 72  TYR   C CE1 1 
ATOM   1634 C  CE2 . TYR   B 1 66  ? 32.972 -30.237 6.937  1.00 12.44 ? 72  TYR   C CE2 1 
ATOM   1635 C  CZ  . TYR   B 1 66  ? 33.792 -31.042 6.176  1.00 12.33 ? 72  TYR   C CZ  1 
ATOM   1636 O  OH  . TYR   B 1 66  ? 33.797 -30.844 4.805  1.00 15.08 ? 72  TYR   C OH  1 
ATOM   1637 N  N   . PRO   B 1 67  ? 34.260 -33.609 12.959 1.00 8.81  ? 73  PRO   C N   1 
ATOM   1638 C  CA  . PRO   B 1 67  ? 34.776 -33.594 14.332 1.00 10.01 ? 73  PRO   C CA  1 
ATOM   1639 C  C   . PRO   B 1 67  ? 35.877 -32.505 14.436 1.00 9.93  ? 73  PRO   C C   1 
ATOM   1640 O  O   . PRO   B 1 67  ? 36.789 -32.458 13.563 1.00 11.93 ? 73  PRO   C O   1 
ATOM   1641 C  CB  . PRO   B 1 67  ? 35.411 -35.006 14.504 1.00 11.84 ? 73  PRO   C CB  1 
ATOM   1642 C  CG  . PRO   B 1 67  ? 35.700 -35.478 13.136 1.00 13.99 ? 73  PRO   C CG  1 
ATOM   1643 C  CD  . PRO   B 1 67  ? 34.776 -34.763 12.163 1.00 10.46 ? 73  PRO   C CD  1 
ATOM   1644 N  N   . VAL   B 1 68  ? 35.870 -31.730 15.494 1.00 8.68  ? 74  VAL   C N   1 
ATOM   1645 C  CA  . VAL   B 1 68  ? 36.836 -30.625 15.666 1.00 9.64  ? 74  VAL   C CA  1 
ATOM   1646 C  C   . VAL   B 1 68  ? 37.223 -30.455 17.096 1.00 9.61  ? 74  VAL   C C   1 
ATOM   1647 O  O   . VAL   B 1 68  ? 36.465 -30.756 18.036 1.00 9.95  ? 74  VAL   C O   1 
ATOM   1648 C  CB  . VAL   B 1 68  ? 36.244 -29.246 15.175 1.00 11.46 ? 74  VAL   C CB  1 
ATOM   1649 C  CG1 . VAL   B 1 68  ? 36.145 -29.176 13.626 1.00 12.72 ? 74  VAL   C CG1 1 
ATOM   1650 C  CG2 . VAL   B 1 68  ? 34.892 -28.955 15.833 1.00 12.31 ? 74  VAL   C CG2 1 
ATOM   1651 N  N   . SER   B 1 69  ? 38.453 -29.925 17.292 1.00 9.30  ? 75  SER   C N   1 
ATOM   1652 C  CA  . SER   B 1 69  ? 38.874 -29.283 18.539 1.00 9.31  ? 75  SER   C CA  1 
ATOM   1653 C  C   . SER   B 1 69  ? 38.578 -27.800 18.438 1.00 8.73  ? 75  SER   C C   1 
ATOM   1654 O  O   . SER   B 1 69  ? 38.735 -27.192 17.352 1.00 9.84  ? 75  SER   C O   1 
ATOM   1655 C  CB  . SER   B 1 69  ? 40.381 -29.452 18.744 1.00 11.69 ? 75  SER   C CB  1 
ATOM   1656 O  OG  . SER   B 1 69  ? 40.650 -30.835 18.854 1.00 17.09 ? 75  SER   C OG  1 
ATOM   1657 N  N   . PHE   B 1 70  ? 38.122 -27.174 19.512 1.00 8.65  ? 76  PHE   C N   1 
ATOM   1658 C  CA  . PHE   B 1 70  ? 37.763 -25.758 19.488 1.00 9.16  ? 76  PHE   C CA  1 
ATOM   1659 C  C   . PHE   B 1 70  ? 38.230 -25.041 20.745 1.00 9.48  ? 76  PHE   C C   1 
ATOM   1660 O  O   . PHE   B 1 70  ? 38.405 -25.659 21.804 1.00 10.23 ? 76  PHE   C O   1 
ATOM   1661 C  CB  . PHE   B 1 70  ? 36.242 -25.574 19.227 1.00 9.50  ? 76  PHE   C CB  1 
ATOM   1662 C  CG  . PHE   B 1 70  ? 35.318 -26.273 20.229 1.00 8.89  ? 76  PHE   C CG  1 
ATOM   1663 C  CD1 . PHE   B 1 70  ? 34.885 -27.587 20.018 1.00 8.91  ? 76  PHE   C CD1 1 
ATOM   1664 C  CD2 . PHE   B 1 70  ? 34.888 -25.613 21.378 1.00 9.79  ? 76  PHE   C CD2 1 
ATOM   1665 C  CE1 . PHE   B 1 70  ? 34.060 -28.209 20.955 1.00 8.86  ? 76  PHE   C CE1 1 
ATOM   1666 C  CE2 . PHE   B 1 70  ? 33.999 -26.241 22.271 1.00 9.46  ? 76  PHE   C CE2 1 
ATOM   1667 C  CZ  . PHE   B 1 70  ? 33.654 -27.551 22.083 1.00 9.29  ? 76  PHE   C CZ  1 
ATOM   1668 N  N   . SER   B 1 71  ? 38.495 -23.761 20.605 1.00 9.27  ? 77  SER   C N   1 
ATOM   1669 C  CA  . SER   B 1 71  ? 39.086 -22.972 21.679 1.00 9.85  ? 77  SER   C CA  1 
ATOM   1670 C  C   . SER   B 1 71  ? 38.089 -22.598 22.752 1.00 10.28 ? 77  SER   C C   1 
ATOM   1671 O  O   . SER   B 1 71  ? 36.880 -22.853 22.650 1.00 11.77 ? 77  SER   C O   1 
ATOM   1672 C  CB  . SER   B 1 71  ? 39.798 -21.730 21.124 1.00 11.05 ? 77  SER   C CB  1 
ATOM   1673 O  OG  . SER   B 1 71  ? 38.900 -20.856 20.449 1.00 12.83 ? 77  SER   C OG  1 
ATOM   1674 N  N   . LYS   B 1 72  ? 38.570 -21.979 23.818 1.00 12.75 ? 78  LYS   C N   1 
ATOM   1675 C  CA  . LYS   B 1 72  ? 37.710 -21.550 24.922 1.00 12.30 ? 78  LYS   C CA  1 
ATOM   1676 C  C   . LYS   B 1 72  ? 37.004 -20.244 24.524 1.00 12.22 ? 78  LYS   C C   1 
ATOM   1677 O  O   . LYS   B 1 72  ? 37.584 -19.414 23.818 1.00 14.21 ? 78  LYS   C O   1 
ATOM   1678 C  CB  . LYS   B 1 72  ? 38.601 -21.279 26.164 1.00 15.92 ? 78  LYS   C CB  1 
ATOM   1679 C  CG  . LYS   B 1 72  ? 39.390 -22.513 26.564 1.00 19.20 ? 78  LYS   C CG  1 
ATOM   1680 C  CD  . LYS   B 1 72  ? 40.312 -22.253 27.764 1.00 28.03 ? 78  LYS   C CD  1 
ATOM   1681 C  CE  . LYS   B 1 72  ? 39.491 -22.000 28.996 1.00 33.95 ? 78  LYS   C CE  1 
ATOM   1682 N  NZ  . LYS   B 1 72  ? 38.384 -22.981 29.101 1.00 39.60 ? 78  LYS   C NZ  1 
ATOM   1683 N  N   . PRO   B 1 73  ? 35.761 -20.000 24.984 1.00 11.95 ? 79  PRO   C N   1 
ATOM   1684 C  CA  . PRO   B 1 73  ? 35.026 -18.762 24.557 1.00 11.93 ? 79  PRO   C CA  1 
ATOM   1685 C  C   . PRO   B 1 73  ? 35.801 -17.507 24.922 1.00 12.28 ? 79  PRO   C C   1 
ATOM   1686 O  O   . PRO   B 1 73  ? 36.259 -17.352 26.083 1.00 14.72 ? 79  PRO   C O   1 
ATOM   1687 C  CB  . PRO   B 1 73  ? 33.706 -18.822 25.324 1.00 13.99 ? 79  PRO   C CB  1 
ATOM   1688 C  CG  . PRO   B 1 73  ? 33.525 -20.263 25.695 1.00 17.26 ? 79  PRO   C CG  1 
ATOM   1689 C  CD  . PRO   B 1 73  ? 34.932 -20.869 25.843 1.00 13.42 ? 79  PRO   C CD  1 
ATOM   1690 N  N   . SER   B 1 74  ? 36.039 -16.628 23.945 1.00 12.53 ? 80  SER   C N   1 
ATOM   1691 C  CA  A SER   B 1 74  ? 36.885 -15.455 24.156 0.50 13.45 ? 80  SER   C CA  1 
ATOM   1692 C  CA  B SER   B 1 74  ? 36.862 -15.442 24.181 0.50 13.44 ? 80  SER   C CA  1 
ATOM   1693 C  C   . SER   B 1 74  ? 36.486 -14.281 23.253 1.00 12.96 ? 80  SER   C C   1 
ATOM   1694 O  O   . SER   B 1 74  ? 35.620 -14.433 22.382 1.00 13.32 ? 80  SER   C O   1 
ATOM   1695 C  CB  A SER   B 1 74  ? 38.345 -15.816 23.887 0.50 15.33 ? 80  SER   C CB  1 
ATOM   1696 C  CB  B SER   B 1 74  ? 38.348 -15.783 24.055 0.50 14.99 ? 80  SER   C CB  1 
ATOM   1697 O  OG  A SER   B 1 74  ? 38.749 -16.946 24.639 0.50 17.15 ? 80  SER   C OG  1 
ATOM   1698 O  OG  B SER   B 1 74  ? 38.733 -15.991 22.707 0.50 15.80 ? 80  SER   C OG  1 
ATOM   1699 N  N   . LEU   B 1 75  ? 37.144 -13.117 23.439 1.00 14.06 ? 81  LEU   C N   1 
ATOM   1700 C  CA  . LEU   B 1 75  ? 36.946 -11.904 22.638 1.00 14.32 ? 81  LEU   C CA  1 
ATOM   1701 C  C   . LEU   B 1 75  ? 37.981 -11.964 21.513 1.00 15.27 ? 81  LEU   C C   1 
ATOM   1702 O  O   . LEU   B 1 75  ? 39.217 -11.905 21.782 1.00 17.40 ? 81  LEU   C O   1 
ATOM   1703 C  CB  . LEU   B 1 75  ? 37.190 -10.679 23.545 1.00 15.61 ? 81  LEU   C CB  1 
ATOM   1704 C  CG  . LEU   B 1 75  ? 36.916 -9.323  22.905 1.00 18.57 ? 81  LEU   C CG  1 
ATOM   1705 C  CD1 . LEU   B 1 75  ? 35.453 -9.139  22.640 1.00 18.32 ? 81  LEU   C CD1 1 
ATOM   1706 C  CD2 . LEU   B 1 75  ? 37.411 -8.182  23.819 1.00 21.46 ? 81  LEU   C CD2 1 
ATOM   1707 N  N   . ILE   B 1 76  ? 37.527 -12.116 20.279 1.00 16.18 ? 82  ILE   C N   1 
ATOM   1708 C  CA  A ILE   B 1 76  ? 38.342 -12.402 19.084 0.50 16.65 ? 82  ILE   C CA  1 
ATOM   1709 C  CA  B ILE   B 1 76  ? 38.424 -12.265 19.145 0.50 17.09 ? 82  ILE   C CA  1 
ATOM   1710 C  C   . ILE   B 1 76  ? 38.105 -11.286 18.042 1.00 16.85 ? 82  ILE   C C   1 
ATOM   1711 O  O   . ILE   B 1 76  ? 36.935 -10.995 17.776 1.00 15.50 ? 82  ILE   C O   1 
ATOM   1712 C  CB  A ILE   B 1 76  ? 37.840 -13.790 18.502 0.50 16.33 ? 82  ILE   C CB  1 
ATOM   1713 C  CB  B ILE   B 1 76  ? 38.273 -13.685 18.614 0.50 17.21 ? 82  ILE   C CB  1 
ATOM   1714 C  CG1 A ILE   B 1 76  ? 38.031 -14.955 19.512 0.50 16.85 ? 82  ILE   C CG1 1 
ATOM   1715 C  CG1 B ILE   B 1 76  ? 38.651 -14.704 19.678 0.50 16.54 ? 82  ILE   C CG1 1 
ATOM   1716 C  CG2 A ILE   B 1 76  ? 38.438 -14.132 17.098 0.50 17.48 ? 82  ILE   C CG2 1 
ATOM   1717 C  CG2 B ILE   B 1 76  ? 39.060 -13.906 17.305 0.50 19.28 ? 82  ILE   C CG2 1 
ATOM   1718 C  CD1 A ILE   B 1 76  ? 39.514 -15.472 19.677 0.50 17.30 ? 82  ILE   C CD1 1 
ATOM   1719 C  CD1 B ILE   B 1 76  ? 38.121 -16.044 19.313 0.50 13.28 ? 82  ILE   C CD1 1 
ATOM   1720 N  N   . PHE   B 1 77  ? 39.154 -10.761 17.385 1.00 16.71 ? 83  PHE   C N   1 
ATOM   1721 C  CA  . PHE   B 1 77  ? 38.953 -9.840  16.285 1.00 17.18 ? 83  PHE   C CA  1 
ATOM   1722 C  C   . PHE   B 1 77  ? 38.635 -10.719 15.048 1.00 17.53 ? 83  PHE   C C   1 
ATOM   1723 O  O   . PHE   B 1 77  ? 39.419 -11.631 14.651 1.00 19.45 ? 83  PHE   C O   1 
ATOM   1724 C  CB  . PHE   B 1 77  ? 40.235 -9.025  16.013 1.00 17.46 ? 83  PHE   C CB  1 
ATOM   1725 C  CG  . PHE   B 1 77  ? 39.937 -7.904  15.044 1.00 17.71 ? 83  PHE   C CG  1 
ATOM   1726 C  CD1 . PHE   B 1 77  ? 39.198 -6.804  15.440 1.00 18.79 ? 83  PHE   C CD1 1 
ATOM   1727 C  CD2 . PHE   B 1 77  ? 40.326 -7.985  13.711 1.00 19.55 ? 83  PHE   C CD2 1 
ATOM   1728 C  CE1 . PHE   B 1 77  ? 38.878 -5.785  14.537 1.00 20.39 ? 83  PHE   C CE1 1 
ATOM   1729 C  CE2 . PHE   B 1 77  ? 40.017 -6.955  12.823 1.00 20.93 ? 83  PHE   C CE2 1 
ATOM   1730 C  CZ  . PHE   B 1 77  ? 39.336 -5.855  13.254 1.00 20.00 ? 83  PHE   C CZ  1 
ATOM   1731 N  N   . VAL   B 1 78  ? 37.482 -10.443 14.429 1.00 14.90 ? 84  VAL   C N   1 
ATOM   1732 C  CA  . VAL   B 1 78  ? 36.978 -11.185 13.260 1.00 14.97 ? 84  VAL   C CA  1 
ATOM   1733 C  C   . VAL   B 1 78  ? 37.072 -10.225 12.043 1.00 13.90 ? 84  VAL   C C   1 
ATOM   1734 O  O   . VAL   B 1 78  ? 36.584 -9.090  12.133 1.00 15.52 ? 84  VAL   C O   1 
ATOM   1735 C  CB  . VAL   B 1 78  ? 35.509 -11.627 13.537 1.00 15.05 ? 84  VAL   C CB  1 
ATOM   1736 C  CG1 . VAL   B 1 78  ? 34.963 -12.401 12.345 1.00 15.42 ? 84  VAL   C CG1 1 
ATOM   1737 C  CG2 . VAL   B 1 78  ? 35.427 -12.462 14.830 1.00 15.69 ? 84  VAL   C CG2 1 
ATOM   1738 N  N   . GLU   B 1 79  ? 37.584 -10.693 10.896 1.00 13.99 ? 85  GLU   C N   1 
ATOM   1739 C  CA  . GLU   B 1 79  ? 37.631 -9.889  9.680  1.00 14.90 ? 85  GLU   C CA  1 
ATOM   1740 C  C   . GLU   B 1 79  ? 36.210 -9.689  9.134  1.00 14.25 ? 85  GLU   C C   1 
ATOM   1741 O  O   . GLU   B 1 79  ? 35.258 -10.373 9.519  1.00 13.63 ? 85  GLU   C O   1 
ATOM   1742 C  CB  . GLU   B 1 79  ? 38.540 -10.512 8.602  1.00 16.81 ? 85  GLU   C CB  1 
ATOM   1743 C  CG  . GLU   B 1 79  ? 40.022 -10.510 8.977  1.00 20.67 ? 85  GLU   C CG  1 
ATOM   1744 C  CD  . GLU   B 1 79  ? 40.590 -9.131  9.271  1.00 24.47 ? 85  GLU   C CD  1 
ATOM   1745 O  OE1 . GLU   B 1 79  ? 40.184 -8.131  8.622  1.00 26.69 ? 85  GLU   C OE1 1 
ATOM   1746 O  OE2 . GLU   B 1 79  ? 41.449 -9.038  10.180 1.00 28.77 ? 85  GLU   C OE2 1 
ATOM   1747 N  N   . ALA   B 1 80  ? 36.056 -8.719  8.232  1.00 15.38 ? 86  ALA   C N   1 
ATOM   1748 C  CA  . ALA   B 1 80  ? 34.748 -8.398  7.660  1.00 16.51 ? 86  ALA   C CA  1 
ATOM   1749 C  C   . ALA   B 1 80  ? 34.163 -9.606  6.942  1.00 15.61 ? 86  ALA   C C   1 
ATOM   1750 O  O   . ALA   B 1 80  ? 34.896 -10.415 6.341  1.00 17.41 ? 86  ALA   C O   1 
ATOM   1751 C  CB  . ALA   B 1 80  ? 34.920 -7.264  6.652  1.00 18.14 ? 86  ALA   C CB  1 
ATOM   1752 N  N   . SER   B 1 81  ? 32.865 -9.771  7.101  1.00 14.91 ? 87  SER   C N   1 
ATOM   1753 C  CA  . SER   B 1 81  ? 32.158 -10.799 6.413  1.00 15.58 ? 87  SER   C CA  1 
ATOM   1754 C  C   . SER   B 1 81  ? 31.055 -10.131 5.577  1.00 16.00 ? 87  SER   C C   1 
ATOM   1755 O  O   . SER   B 1 81  ? 30.906 -8.878  5.589  1.00 16.99 ? 87  SER   C O   1 
ATOM   1756 C  CB  . SER   B 1 81  ? 31.545 -11.776 7.427  1.00 14.75 ? 87  SER   C CB  1 
ATOM   1757 O  OG  . SER   B 1 81  ? 30.489 -11.100 8.122  1.00 13.85 ? 87  SER   C OG  1 
ATOM   1758 N  N   . GLU   B 1 82  ? 30.213 -10.959 4.941  1.00 16.58 ? 88  GLU   C N   1 
ATOM   1759 C  CA  . GLU   B 1 82  ? 29.131 -10.337 4.187  1.00 18.45 ? 88  GLU   C CA  1 
ATOM   1760 C  C   . GLU   B 1 82  ? 28.069 -9.696  5.102  1.00 17.15 ? 88  GLU   C C   1 
ATOM   1761 O  O   . GLU   B 1 82  ? 27.279 -8.865  4.622  1.00 18.66 ? 88  GLU   C O   1 
ATOM   1762 C  CB  . GLU   B 1 82  ? 28.532 -11.333 3.201  1.00 23.95 ? 88  GLU   C CB  1 
ATOM   1763 C  CG  . GLU   B 1 82  ? 27.503 -12.283 3.739  1.00 32.85 ? 88  GLU   C CG  1 
ATOM   1764 C  CD  . GLU   B 1 82  ? 26.833 -13.092 2.643  1.00 37.97 ? 88  GLU   C CD  1 
ATOM   1765 O  OE1 . GLU   B 1 82  ? 27.486 -13.340 1.599  1.00 38.32 ? 88  GLU   C OE1 1 
ATOM   1766 O  OE2 . GLU   B 1 82  ? 25.659 -13.487 2.838  1.00 37.84 ? 88  GLU   C OE2 1 
ATOM   1767 N  N   . TYR   B 1 83  ? 28.068 -10.008 6.398  1.00 14.85 ? 89  TYR   C N   1 
ATOM   1768 C  CA  . TYR   B 1 83  ? 27.024 -9.547  7.303  1.00 14.15 ? 89  TYR   C CA  1 
ATOM   1769 C  C   . TYR   B 1 83  ? 27.520 -8.705  8.504  1.00 15.44 ? 89  TYR   C C   1 
ATOM   1770 O  O   . TYR   B 1 83  ? 26.671 -8.120  9.189  1.00 16.82 ? 89  TYR   C O   1 
ATOM   1771 C  CB  . TYR   B 1 83  ? 26.156 -10.755 7.766  1.00 14.05 ? 89  TYR   C CB  1 
ATOM   1772 C  CG  . TYR   B 1 83  ? 26.986 -11.930 8.268  1.00 13.13 ? 89  TYR   C CG  1 
ATOM   1773 C  CD1 . TYR   B 1 83  ? 27.454 -12.904 7.394  1.00 13.35 ? 89  TYR   C CD1 1 
ATOM   1774 C  CD2 . TYR   B 1 83  ? 27.342 -12.040 9.608  1.00 12.74 ? 89  TYR   C CD2 1 
ATOM   1775 C  CE1 . TYR   B 1 83  ? 28.212 -13.991 7.847  1.00 13.41 ? 89  TYR   C CE1 1 
ATOM   1776 C  CE2 . TYR   B 1 83  ? 28.139 -13.095 10.065 1.00 12.74 ? 89  TYR   C CE2 1 
ATOM   1777 C  CZ  . TYR   B 1 83  ? 28.538 -14.093 9.182  1.00 12.68 ? 89  TYR   C CZ  1 
ATOM   1778 O  OH  . TYR   B 1 83  ? 29.370 -15.130 9.557  1.00 13.71 ? 89  TYR   C OH  1 
ATOM   1779 N  N   . TYR   B 1 84  ? 28.825 -8.581  8.773  1.00 13.71 ? 90  TYR   C N   1 
ATOM   1780 C  CA  . TYR   B 1 84  ? 29.343 -7.665  9.795  1.00 14.30 ? 90  TYR   C CA  1 
ATOM   1781 C  C   . TYR   B 1 84  ? 30.668 -7.052  9.282  1.00 14.30 ? 90  TYR   C C   1 
ATOM   1782 O  O   . TYR   B 1 84  ? 31.407 -7.691  8.524  1.00 14.74 ? 90  TYR   C O   1 
ATOM   1783 C  CB  . TYR   B 1 84  ? 29.707 -8.399  11.113 1.00 13.27 ? 90  TYR   C CB  1 
ATOM   1784 C  CG  . TYR   B 1 84  ? 28.537 -8.827  11.969 1.00 12.69 ? 90  TYR   C CG  1 
ATOM   1785 C  CD1 . TYR   B 1 84  ? 27.576 -7.905  12.411 1.00 13.40 ? 90  TYR   C CD1 1 
ATOM   1786 C  CD2 . TYR   B 1 84  ? 28.369 -10.144 12.312 1.00 12.20 ? 90  TYR   C CD2 1 
ATOM   1787 C  CE1 . TYR   B 1 84  ? 26.524 -8.295  13.246 1.00 13.67 ? 90  TYR   C CE1 1 
ATOM   1788 C  CE2 . TYR   B 1 84  ? 27.303 -10.550 13.124 1.00 11.99 ? 90  TYR   C CE2 1 
ATOM   1789 C  CZ  . TYR   B 1 84  ? 26.392 -9.621  13.611 1.00 12.69 ? 90  TYR   C CZ  1 
ATOM   1790 O  OH  . TYR   B 1 84  ? 25.310 -9.991  14.417 1.00 11.90 ? 90  TYR   C OH  1 
ATOM   1791 N  N   . PRO   B 1 85  ? 31.011 -5.828  9.703  1.00 15.09 ? 91  PRO   C N   1 
ATOM   1792 C  CA  . PRO   B 1 85  ? 32.359 -5.322  9.429  1.00 15.58 ? 91  PRO   C CA  1 
ATOM   1793 C  C   . PRO   B 1 85  ? 33.376 -6.088  10.293 1.00 15.37 ? 91  PRO   C C   1 
ATOM   1794 O  O   . PRO   B 1 85  ? 33.035 -6.889  11.205 1.00 14.38 ? 91  PRO   C O   1 
ATOM   1795 C  CB  . PRO   B 1 85  ? 32.244 -3.857  9.884  1.00 17.20 ? 91  PRO   C CB  1 
ATOM   1796 C  CG  . PRO   B 1 85  ? 31.321 -3.933  11.013 1.00 16.95 ? 91  PRO   C CG  1 
ATOM   1797 C  CD  . PRO   B 1 85  ? 30.265 -4.987  10.668 1.00 15.71 ? 91  PRO   C CD  1 
ATOM   1798 N  N   . ALA   B 1 86  ? 34.678 -5.817  10.068 1.00 15.22 ? 92  ALA   C N   1 
ATOM   1799 C  CA  . ALA   B 1 86  ? 35.735 -6.326  10.928 1.00 16.50 ? 92  ALA   C CA  1 
ATOM   1800 C  C   . ALA   B 1 86  ? 35.513 -5.729  12.330 1.00 17.83 ? 92  ALA   C C   1 
ATOM   1801 O  O   . ALA   B 1 86  ? 35.208 -4.525  12.455 1.00 18.92 ? 92  ALA   C O   1 
ATOM   1802 C  CB  . ALA   B 1 86  ? 37.105 -5.908  10.390 1.00 17.23 ? 92  ALA   C CB  1 
ATOM   1803 N  N   . ARG   B 1 87  ? 35.533 -6.579  13.356 1.00 16.77 ? 93  ARG   C N   1 
ATOM   1804 C  CA  . ARG   B 1 87  ? 35.194 -6.129  14.696 1.00 16.97 ? 93  ARG   C CA  1 
ATOM   1805 C  C   . ARG   B 1 87  ? 35.591 -7.191  15.712 1.00 16.50 ? 93  ARG   C C   1 
ATOM   1806 O  O   . ARG   B 1 87  ? 35.866 -8.335  15.351 1.00 15.59 ? 93  ARG   C O   1 
ATOM   1807 C  CB  . ARG   B 1 87  ? 33.647 -5.909  14.811 1.00 16.63 ? 93  ARG   C CB  1 
ATOM   1808 C  CG  . ARG   B 1 87  ? 32.871 -7.234  14.757 1.00 15.61 ? 93  ARG   C CG  1 
ATOM   1809 C  CD  . ARG   B 1 87  ? 31.374 -7.023  14.682 1.00 16.01 ? 93  ARG   C CD  1 
ATOM   1810 N  NE  . ARG   B 1 87  ? 30.704 -8.294  15.011 1.00 14.78 ? 93  ARG   C NE  1 
ATOM   1811 C  CZ  . ARG   B 1 87  ? 29.653 -8.471  15.794 1.00 14.27 ? 93  ARG   C CZ  1 
ATOM   1812 N  NH1 . ARG   B 1 87  ? 29.009 -7.423  16.314 1.00 16.39 ? 93  ARG   C NH1 1 
ATOM   1813 N  NH2 . ARG   B 1 87  ? 29.233 -9.695  16.066 1.00 15.30 ? 93  ARG   C NH2 1 
ATOM   1814 N  N   . TYR   B 1 88  ? 35.521 -6.814  17.006 1.00 17.26 ? 94  TYR   C N   1 
ATOM   1815 C  CA  . TYR   B 1 88  ? 35.688 -7.812  18.053 1.00 17.67 ? 94  TYR   C CA  1 
ATOM   1816 C  C   . TYR   B 1 88  ? 34.331 -8.495  18.311 1.00 15.68 ? 94  TYR   C C   1 
ATOM   1817 O  O   . TYR   B 1 88  ? 33.309 -7.836  18.456 1.00 16.83 ? 94  TYR   C O   1 
ATOM   1818 C  CB  . TYR   B 1 88  ? 36.136 -7.146  19.356 1.00 19.34 ? 94  TYR   C CB  1 
ATOM   1819 C  CG  . TYR   B 1 88  ? 37.607 -6.829  19.311 1.00 21.21 ? 94  TYR   C CG  1 
ATOM   1820 C  CD1 . TYR   B 1 88  ? 38.550 -7.813  19.532 1.00 21.75 ? 94  TYR   C CD1 1 
ATOM   1821 C  CD2 . TYR   B 1 88  ? 38.059 -5.560  18.933 1.00 21.86 ? 94  TYR   C CD2 1 
ATOM   1822 C  CE1 . TYR   B 1 88  ? 39.914 -7.545  19.433 1.00 23.61 ? 94  TYR   C CE1 1 
ATOM   1823 C  CE2 . TYR   B 1 88  ? 39.413 -5.284  18.813 1.00 23.34 ? 94  TYR   C CE2 1 
ATOM   1824 C  CZ  . TYR   B 1 88  ? 40.341 -6.276  19.070 1.00 24.32 ? 94  TYR   C CZ  1 
ATOM   1825 O  OH  . TYR   B 1 88  ? 41.689 -5.968  18.944 1.00 26.37 ? 94  TYR   C OH  1 
ATOM   1826 N  N   . GLN   B 1 89  ? 34.321 -9.828  18.379 1.00 13.55 ? 95  GLN   C N   1 
ATOM   1827 C  CA  . GLN   B 1 89  ? 33.129 -10.602 18.750 1.00 12.74 ? 95  GLN   C CA  1 
ATOM   1828 C  C   . GLN   B 1 89  ? 33.446 -11.330 20.051 1.00 12.55 ? 95  GLN   C C   1 
ATOM   1829 O  O   . GLN   B 1 89  ? 34.547 -11.919 20.189 1.00 13.87 ? 95  GLN   C O   1 
ATOM   1830 C  CB  . GLN   B 1 89  ? 32.778 -11.572 17.614 1.00 13.63 ? 95  GLN   C CB  1 
ATOM   1831 C  CG  . GLN   B 1 89  ? 31.537 -12.411 17.937 1.00 14.11 ? 95  GLN   C CG  1 
ATOM   1832 C  CD  . GLN   B 1 89  ? 30.820 -12.966 16.733 1.00 12.20 ? 95  GLN   C CD  1 
ATOM   1833 O  OE1 . GLN   B 1 89  ? 30.790 -12.342 15.632 1.00 13.02 ? 95  GLN   C OE1 1 
ATOM   1834 N  NE2 . GLN   B 1 89  ? 30.251 -14.144 16.924 1.00 12.25 ? 95  GLN   C NE2 1 
ATOM   1835 N  N   . SER   B 1 90  ? 32.540 -11.299 21.013 1.00 11.62 ? 96  SER   C N   1 
ATOM   1836 C  CA  . SER   B 1 90  ? 32.730 -11.933 22.321 1.00 11.51 ? 96  SER   C CA  1 
ATOM   1837 C  C   . SER   B 1 90  ? 32.128 -13.350 22.382 1.00 11.08 ? 96  SER   C C   1 
ATOM   1838 O  O   . SER   B 1 90  ? 31.282 -13.718 21.566 1.00 10.92 ? 96  SER   C O   1 
ATOM   1839 C  CB  . SER   B 1 90  ? 32.154 -11.045 23.435 1.00 13.15 ? 96  SER   C CB  1 
ATOM   1840 O  OG  . SER   B 1 90  ? 30.760 -11.037 23.333 1.00 13.78 ? 96  SER   C OG  1 
ATOM   1841 N  N   . HIS   B 1 91  ? 32.584 -14.120 23.380 1.00 11.40 ? 97  HIS   C N   1 
ATOM   1842 C  CA  . HIS   B 1 91  ? 32.086 -15.482 23.648 1.00 11.40 ? 97  HIS   C CA  1 
ATOM   1843 C  C   . HIS   B 1 91  ? 32.201 -16.370 22.387 1.00 10.33 ? 97  HIS   C C   1 
ATOM   1844 O  O   . HIS   B 1 91  ? 31.288 -17.192 22.129 1.00 11.54 ? 97  HIS   C O   1 
ATOM   1845 C  CB  . HIS   B 1 91  ? 30.641 -15.452 24.185 1.00 11.98 ? 97  HIS   C CB  1 
ATOM   1846 C  CG  . HIS   B 1 91  ? 30.507 -14.715 25.491 1.00 13.16 ? 97  HIS   C CG  1 
ATOM   1847 N  ND1 . HIS   B 1 91  ? 30.497 -15.378 26.713 1.00 15.27 ? 97  HIS   C ND1 1 
ATOM   1848 C  CD2 . HIS   B 1 91  ? 30.420 -13.376 25.719 1.00 14.53 ? 97  HIS   C CD2 1 
ATOM   1849 C  CE1 . HIS   B 1 91  ? 30.387 -14.434 27.648 1.00 15.96 ? 97  HIS   C CE1 1 
ATOM   1850 N  NE2 . HIS   B 1 91  ? 30.314 -13.214 27.100 1.00 15.97 ? 97  HIS   C NE2 1 
ATOM   1851 N  N   . LEU   B 1 92  ? 33.287 -16.204 21.647 1.00 10.22 ? 98  LEU   C N   1 
ATOM   1852 C  CA  . LEU   B 1 92  ? 33.479 -16.896 20.384 1.00 10.67 ? 98  LEU   C CA  1 
ATOM   1853 C  C   . LEU   B 1 92  ? 34.555 -17.980 20.568 1.00 10.70 ? 98  LEU   C C   1 
ATOM   1854 O  O   . LEU   B 1 92  ? 35.538 -17.770 21.287 1.00 11.03 ? 98  LEU   C O   1 
ATOM   1855 C  CB  . LEU   B 1 92  ? 33.942 -15.880 19.299 1.00 11.40 ? 98  LEU   C CB  1 
ATOM   1856 C  CG  . LEU   B 1 92  ? 34.083 -16.431 17.881 1.00 12.52 ? 98  LEU   C CG  1 
ATOM   1857 C  CD1 . LEU   B 1 92  ? 32.751 -16.815 17.308 1.00 13.15 ? 98  LEU   C CD1 1 
ATOM   1858 C  CD2 . LEU   B 1 92  ? 34.782 -15.404 16.948 1.00 15.36 ? 98  LEU   C CD2 1 
ATOM   1859 N  N   . MET   B 1 93  ? 34.390 -19.125 19.909 1.00 10.11 ? 99  MET   C N   1 
ATOM   1860 C  CA  . MET   B 1 93  ? 35.322 -20.253 19.954 1.00 9.57  ? 99  MET   C CA  1 
ATOM   1861 C  C   . MET   B 1 93  ? 35.751 -20.562 18.527 1.00 10.02 ? 99  MET   C C   1 
ATOM   1862 O  O   . MET   B 1 93  ? 34.870 -20.607 17.642 1.00 11.05 ? 99  MET   C O   1 
ATOM   1863 C  CB  . MET   B 1 93  ? 34.618 -21.480 20.534 1.00 10.79 ? 99  MET   C CB  1 
ATOM   1864 C  CG  . MET   B 1 93  ? 34.127 -21.231 21.946 1.00 11.99 ? 99  MET   C CG  1 
ATOM   1865 S  SD  . MET   B 1 93  ? 33.116 -22.532 22.609 1.00 12.87 ? 99  MET   C SD  1 
ATOM   1866 C  CE  . MET   B 1 93  ? 31.615 -22.400 21.468 1.00 13.54 ? 99  MET   C CE  1 
ATOM   1867 N  N   . LEU   B 1 94  ? 37.021 -20.816 18.259 1.00 9.66  ? 100 LEU   C N   1 
ATOM   1868 C  CA  . LEU   B 1 94  ? 37.482 -21.115 16.905 1.00 10.05 ? 100 LEU   C CA  1 
ATOM   1869 C  C   . LEU   B 1 94  ? 37.917 -22.580 16.770 1.00 9.20  ? 100 LEU   C C   1 
ATOM   1870 O  O   . LEU   B 1 94  ? 38.450 -23.180 17.725 1.00 10.32 ? 100 LEU   C O   1 
ATOM   1871 C  CB  . LEU   B 1 94  ? 38.724 -20.250 16.532 1.00 11.47 ? 100 LEU   C CB  1 
ATOM   1872 C  CG  . LEU   B 1 94  ? 38.546 -18.729 16.490 1.00 13.12 ? 100 LEU   C CG  1 
ATOM   1873 C  CD1 . LEU   B 1 94  ? 39.865 -18.060 16.030 1.00 15.76 ? 100 LEU   C CD1 1 
ATOM   1874 C  CD2 . LEU   B 1 94  ? 37.393 -18.316 15.578 1.00 13.15 ? 100 LEU   C CD2 1 
ATOM   1875 N  N   . ALA   B 1 95  ? 37.784 -23.078 15.574 1.00 10.14 ? 101 ALA   C N   1 
ATOM   1876 C  CA  . ALA   B 1 95  ? 38.334 -24.374 15.153 1.00 9.95  ? 101 ALA   C CA  1 
ATOM   1877 C  C   . ALA   B 1 95  ? 38.895 -24.220 13.733 1.00 9.91  ? 101 ALA   C C   1 
ATOM   1878 O  O   . ALA   B 1 95  ? 38.503 -23.309 12.993 1.00 9.81  ? 101 ALA   C O   1 
ATOM   1879 C  CB  . ALA   B 1 95  ? 37.243 -25.475 15.175 1.00 10.56 ? 101 ALA   C CB  1 
ATOM   1880 N  N   . VAL   B 1 96  ? 39.753 -25.170 13.335 1.00 9.59  ? 102 VAL   C N   1 
ATOM   1881 C  CA  . VAL   B 1 96  ? 40.218 -25.231 11.960 1.00 10.49 ? 102 VAL   C CA  1 
ATOM   1882 C  C   . VAL   B 1 96  ? 39.147 -25.984 11.139 1.00 10.63 ? 102 VAL   C C   1 
ATOM   1883 O  O   . VAL   B 1 96  ? 38.840 -27.171 11.424 1.00 12.20 ? 102 VAL   C O   1 
ATOM   1884 C  CB  . VAL   B 1 96  ? 41.603 -25.933 11.929 1.00 11.43 ? 102 VAL   C CB  1 
ATOM   1885 C  CG1 . VAL   B 1 96  ? 42.073 -26.106 10.494 1.00 14.33 ? 102 VAL   C CG1 1 
ATOM   1886 C  CG2 . VAL   B 1 96  ? 42.613 -25.154 12.773 1.00 12.52 ? 102 VAL   C CG2 1 
ATOM   1887 N  N   . GLY   B 1 97  ? 38.556 -25.310 10.187 1.00 11.81 ? 103 GLY   C N   1 
ATOM   1888 C  CA  . GLY   B 1 97  ? 37.497 -25.930 9.395  1.00 12.49 ? 103 GLY   C CA  1 
ATOM   1889 C  C   . GLY   B 1 97  ? 36.835 -24.960 8.468  1.00 12.03 ? 103 GLY   C C   1 
ATOM   1890 O  O   . GLY   B 1 97  ? 37.102 -23.740 8.525  1.00 14.82 ? 103 GLY   C O   1 
ATOM   1891 N  N   . HIS   B 1 98  ? 35.953 -25.457 7.616  1.00 12.21 ? 104 HIS   C N   1 
ATOM   1892 C  CA  . HIS   B 1 98  ? 35.269 -24.645 6.652  1.00 12.41 ? 104 HIS   C CA  1 
ATOM   1893 C  C   . HIS   B 1 98  ? 34.015 -23.979 7.173  1.00 11.36 ? 104 HIS   C C   1 
ATOM   1894 O  O   . HIS   B 1 98  ? 33.175 -24.636 7.820  1.00 11.31 ? 104 HIS   C O   1 
ATOM   1895 C  CB  . HIS   B 1 98  ? 34.949 -25.515 5.448  1.00 14.56 ? 104 HIS   C CB  1 
ATOM   1896 C  CG  . HIS   B 1 98  ? 34.427 -24.704 4.330  1.00 15.22 ? 104 HIS   C CG  1 
ATOM   1897 N  ND1 . HIS   B 1 98  ? 35.221 -23.750 3.686  1.00 18.09 ? 104 HIS   C ND1 1 
ATOM   1898 C  CD2 . HIS   B 1 98  ? 33.167 -24.651 3.835  1.00 16.82 ? 104 HIS   C CD2 1 
ATOM   1899 C  CE1 . HIS   B 1 98  ? 34.414 -23.167 2.815  1.00 20.11 ? 104 HIS   C CE1 1 
ATOM   1900 N  NE2 . HIS   B 1 98  ? 33.175 -23.693 2.855  1.00 19.72 ? 104 HIS   C NE2 1 
ATOM   1901 N  N   . SER   B 1 99  ? 33.807 -22.722 6.827  1.00 11.90 ? 105 SER   C N   1 
ATOM   1902 C  CA  . SER   B 1 99  ? 32.583 -21.982 7.209  1.00 12.64 ? 105 SER   C CA  1 
ATOM   1903 C  C   . SER   B 1 99  ? 32.369 -20.812 6.216  1.00 13.59 ? 105 SER   C C   1 
ATOM   1904 O  O   . SER   B 1 99  ? 33.243 -19.952 6.090  1.00 15.59 ? 105 SER   C O   1 
ATOM   1905 C  CB  . SER   B 1 99  ? 32.802 -21.389 8.604  1.00 13.11 ? 105 SER   C CB  1 
ATOM   1906 O  OG  . SER   B 1 99  ? 31.678 -20.576 8.945  1.00 13.69 ? 105 SER   C OG  1 
ATOM   1907 N  N   . GLU   B 1 100 ? 31.244 -20.763 5.599  1.00 13.03 ? 106 GLU   C N   1 
ATOM   1908 C  CA  . GLU   B 1 100 ? 30.811 -19.693 4.701  1.00 14.74 ? 106 GLU   C CA  1 
ATOM   1909 C  C   . GLU   B 1 100 ? 29.583 -19.071 5.308  1.00 13.16 ? 106 GLU   C C   1 
ATOM   1910 O  O   . GLU   B 1 100 ? 28.989 -19.624 6.223  1.00 12.38 ? 106 GLU   C O   1 
ATOM   1911 C  CB  . GLU   B 1 100 ? 30.348 -20.340 3.383  1.00 18.07 ? 106 GLU   C CB  1 
ATOM   1912 C  CG  . GLU   B 1 100 ? 31.467 -20.900 2.579  1.00 23.64 ? 106 GLU   C CG  1 
ATOM   1913 C  CD  . GLU   B 1 100 ? 31.003 -21.616 1.330  1.00 25.93 ? 106 GLU   C CD  1 
ATOM   1914 O  OE1 . GLU   B 1 100 ? 29.977 -21.228 0.724  1.00 34.85 ? 106 GLU   C OE1 1 
ATOM   1915 O  OE2 . GLU   B 1 100 ? 31.717 -22.550 0.933  1.00 26.77 ? 106 GLU   C OE2 1 
ATOM   1916 N  N   . PRO   B 1 101 ? 29.127 -17.883 4.814  1.00 14.07 ? 107 PRO   C N   1 
ATOM   1917 C  CA  . PRO   B 1 101 ? 27.989 -17.237 5.470  1.00 13.82 ? 107 PRO   C CA  1 
ATOM   1918 C  C   . PRO   B 1 101 ? 26.749 -18.124 5.608  1.00 13.18 ? 107 PRO   C C   1 
ATOM   1919 O  O   . PRO   B 1 101 ? 26.145 -18.072 6.678  1.00 13.14 ? 107 PRO   C O   1 
ATOM   1920 C  CB  . PRO   B 1 101 ? 27.702 -16.008 4.565  1.00 16.06 ? 107 PRO   C CB  1 
ATOM   1921 C  CG  . PRO   B 1 101 ? 29.027 -15.645 4.117  1.00 18.20 ? 107 PRO   C CG  1 
ATOM   1922 C  CD  . PRO   B 1 101 ? 29.765 -16.964 3.843  1.00 16.20 ? 107 PRO   C CD  1 
ATOM   1923 N  N   . GLY   B 1 102 ? 26.425 -18.948 4.607  1.00 13.12 ? 108 GLY   C N   1 
ATOM   1924 C  CA  . GLY   B 1 102 ? 25.229 -19.789 4.694  1.00 13.52 ? 108 GLY   C CA  1 
ATOM   1925 C  C   . GLY   B 1 102 ? 25.344 -20.875 5.757  1.00 11.84 ? 108 GLY   C C   1 
ATOM   1926 O  O   . GLY   B 1 102 ? 24.351 -21.553 6.053  1.00 13.42 ? 108 GLY   C O   1 
ATOM   1927 N  N   . ASP   B 1 103 ? 26.564 -21.135 6.288  1.00 11.16 ? 109 ASP   C N   1 
ATOM   1928 C  CA  . ASP   B 1 103 ? 26.759 -22.147 7.343  1.00 10.44 ? 109 ASP   C CA  1 
ATOM   1929 C  C   . ASP   B 1 103 ? 26.347 -21.662 8.706  1.00 9.96  ? 109 ASP   C C   1 
ATOM   1930 O  O   . ASP   B 1 103 ? 26.244 -22.456 9.645  1.00 9.49  ? 109 ASP   C O   1 
ATOM   1931 C  CB  . ASP   B 1 103 ? 28.219 -22.587 7.370  1.00 11.33 ? 109 ASP   C CB  1 
ATOM   1932 C  CG  . ASP   B 1 103 ? 28.567 -23.362 6.131  1.00 12.30 ? 109 ASP   C CG  1 
ATOM   1933 O  OD1 . ASP   B 1 103 ? 27.733 -24.146 5.672  1.00 12.98 ? 109 ASP   C OD1 1 
ATOM   1934 O  OD2 . ASP   B 1 103 ? 29.706 -23.187 5.614  1.00 12.96 ? 109 ASP   C OD2 1 
ATOM   1935 N  N   . CYS   B 1 104 ? 26.132 -20.323 8.887  1.00 9.58  ? 110 CYS   C N   1 
ATOM   1936 C  CA  . CYS   B 1 104 ? 25.716 -19.811 10.196 1.00 9.22  ? 110 CYS   C CA  1 
ATOM   1937 C  C   . CYS   B 1 104 ? 24.482 -20.515 10.684 1.00 9.17  ? 110 CYS   C C   1 
ATOM   1938 O  O   . CYS   B 1 104 ? 23.535 -20.736 9.910  1.00 10.82 ? 110 CYS   C O   1 
ATOM   1939 C  CB  . CYS   B 1 104 ? 25.494 -18.292 10.140 1.00 10.41 ? 110 CYS   C CB  1 
ATOM   1940 S  SG  . CYS   B 1 104 ? 27.035 -17.329 10.025 1.00 11.97 ? 110 CYS   C SG  1 
ATOM   1941 N  N   . GLY   B 1 105 ? 24.471 -20.878 11.962 1.00 8.58  ? 111 GLY   C N   1 
ATOM   1942 C  CA  . GLY   B 1 105 ? 23.333 -21.564 12.574 1.00 9.38  ? 111 GLY   C CA  1 
ATOM   1943 C  C   . GLY   B 1 105 ? 23.551 -23.062 12.726 1.00 9.34  ? 111 GLY   C C   1 
ATOM   1944 O  O   . GLY   B 1 105 ? 22.780 -23.724 13.443 1.00 10.33 ? 111 GLY   C O   1 
ATOM   1945 N  N   . GLY   B 1 106 ? 24.573 -23.624 12.047 1.00 9.35  ? 112 GLY   C N   1 
ATOM   1946 C  CA  . GLY   B 1 106 ? 24.884 -25.058 12.191 1.00 9.71  ? 112 GLY   C CA  1 
ATOM   1947 C  C   . GLY   B 1 106 ? 25.284 -25.348 13.638 1.00 8.77  ? 112 GLY   C C   1 
ATOM   1948 O  O   . GLY   B 1 106 ? 26.014 -24.549 14.277 1.00 8.83  ? 112 GLY   C O   1 
ATOM   1949 N  N   . ILE   B 1 107 ? 24.847 -26.487 14.171 1.00 8.62  ? 113 ILE   C N   1 
ATOM   1950 C  CA  . ILE   B 1 107 ? 25.110 -26.813 15.564 1.00 8.51  ? 113 ILE   C CA  1 
ATOM   1951 C  C   . ILE   B 1 107 ? 26.495 -27.420 15.734 1.00 7.94  ? 113 ILE   C C   1 
ATOM   1952 O  O   . ILE   B 1 107 ? 26.925 -28.285 14.962 1.00 8.13  ? 113 ILE   C O   1 
ATOM   1953 C  CB  . ILE   B 1 107 ? 24.015 -27.811 16.056 1.00 10.62 ? 113 ILE   C CB  1 
ATOM   1954 C  CG1 . ILE   B 1 107 ? 22.762 -26.866 16.465 1.00 14.46 ? 113 ILE   C CG1 1 
ATOM   1955 C  CG2 . ILE   B 1 107 ? 24.451 -28.640 17.272 1.00 10.50 ? 113 ILE   C CG2 1 
ATOM   1956 C  CD1 . ILE   B 1 107 ? 21.433 -27.546 16.839 1.00 18.75 ? 113 ILE   C CD1 1 
ATOM   1957 N  N   . LEU   B 1 108 ? 27.168 -26.996 16.834 1.00 7.51  ? 114 LEU   C N   1 
ATOM   1958 C  CA  . LEU   B 1 108 ? 28.357 -27.659 17.404 1.00 7.06  ? 114 LEU   C CA  1 
ATOM   1959 C  C   . LEU   B 1 108 ? 27.864 -28.403 18.661 1.00 7.44  ? 114 LEU   C C   1 
ATOM   1960 O  O   . LEU   B 1 108 ? 27.193 -27.808 19.507 1.00 7.75  ? 114 LEU   C O   1 
ATOM   1961 C  CB  . LEU   B 1 108 ? 29.384 -26.589 17.815 1.00 7.82  ? 114 LEU   C CB  1 
ATOM   1962 C  CG  . LEU   B 1 108 ? 30.599 -27.122 18.616 1.00 8.38  ? 114 LEU   C CG  1 
ATOM   1963 C  CD1 . LEU   B 1 108 ? 31.495 -28.022 17.768 1.00 9.80  ? 114 LEU   C CD1 1 
ATOM   1964 C  CD2 . LEU   B 1 108 ? 31.409 -25.922 19.152 1.00 9.76  ? 114 LEU   C CD2 1 
ATOM   1965 N  N   . ARG   B 1 109 ? 28.140 -29.723 18.722 1.00 7.81  ? 115 ARG   C N   1 
ATOM   1966 C  CA  . ARG   B 1 109 ? 27.664 -30.526 19.866 1.00 7.99  ? 115 ARG   C CA  1 
ATOM   1967 C  C   . ARG   B 1 109 ? 28.823 -31.348 20.430 1.00 8.26  ? 115 ARG   C C   1 
ATOM   1968 O  O   . ARG   B 1 109 ? 29.736 -31.784 19.693 1.00 8.90  ? 115 ARG   C O   1 
ATOM   1969 C  CB  . ARG   B 1 109 ? 26.533 -31.475 19.403 1.00 11.08 ? 115 ARG   C CB  1 
ATOM   1970 C  CG  . ARG   B 1 109 ? 26.957 -32.479 18.333 1.00 13.50 ? 115 ARG   C CG  1 
ATOM   1971 C  CD  . ARG   B 1 109 ? 25.827 -33.386 17.871 1.00 16.62 ? 115 ARG   C CD  1 
ATOM   1972 N  NE  . ARG   B 1 109 ? 24.954 -32.643 16.966 1.00 21.28 ? 115 ARG   C NE  1 
ATOM   1973 C  CZ  . ARG   B 1 109 ? 23.640 -32.551 17.102 1.00 28.54 ? 115 ARG   C CZ  1 
ATOM   1974 N  NH1 . ARG   B 1 109 ? 23.033 -33.116 18.136 1.00 32.56 ? 115 ARG   C NH1 1 
ATOM   1975 N  NH2 . ARG   B 1 109 ? 22.920 -31.860 16.220 1.00 31.76 ? 115 ARG   C NH2 1 
ATOM   1976 N  N   . CYS   B 1 110 ? 28.751 -31.598 21.747 1.00 9.04  ? 116 CYS   C N   1 
ATOM   1977 C  CA  . CYS   B 1 110 ? 29.723 -32.486 22.435 1.00 10.01 ? 116 CYS   C CA  1 
ATOM   1978 C  C   . CYS   B 1 110 ? 28.850 -33.589 23.098 1.00 10.61 ? 116 CYS   C C   1 
ATOM   1979 O  O   . CYS   B 1 110 ? 27.627 -33.701 22.906 1.00 11.05 ? 116 CYS   C O   1 
ATOM   1980 C  CB  . CYS   B 1 110 ? 30.508 -31.696 23.483 1.00 9.74  ? 116 CYS   C CB  1 
ATOM   1981 S  SG  . CYS   B 1 110 ? 29.444 -31.070 24.807 1.00 9.95  ? 116 CYS   C SG  1 
ATOM   1982 N  N   . GLN   B 1 111 ? 29.508 -34.430 23.942 1.00 11.11 ? 117 GLN   C N   1 
ATOM   1983 C  CA  . GLN   B 1 111 ? 28.757 -35.485 24.622 1.00 13.04 ? 117 GLN   C CA  1 
ATOM   1984 C  C   . GLN   B 1 111 ? 27.676 -34.950 25.544 1.00 12.85 ? 117 GLN   C C   1 
ATOM   1985 O  O   . GLN   B 1 111 ? 26.724 -35.689 25.872 1.00 14.91 ? 117 GLN   C O   1 
ATOM   1986 C  CB  . GLN   B 1 111 ? 29.671 -36.430 25.443 1.00 14.26 ? 117 GLN   C CB  1 
ATOM   1987 C  CG  . GLN   B 1 111 ? 30.341 -35.720 26.614 1.00 15.07 ? 117 GLN   C CG  1 
ATOM   1988 C  CD  . GLN   B 1 111 ? 31.246 -36.627 27.402 1.00 26.24 ? 117 GLN   C CD  1 
ATOM   1989 O  OE1 . GLN   B 1 111 ? 32.448 -36.707 27.136 1.00 30.02 ? 117 GLN   C OE1 1 
ATOM   1990 N  NE2 . GLN   B 1 111 ? 30.671 -37.298 28.375 1.00 26.85 ? 117 GLN   C NE2 1 
ATOM   1991 N  N   . HIS   B 1 112 ? 27.749 -33.662 25.961 1.00 11.22 ? 118 HIS   C N   1 
ATOM   1992 C  CA  . HIS   B 1 112 ? 26.755 -33.119 26.890 1.00 12.08 ? 118 HIS   C CA  1 
ATOM   1993 C  C   . HIS   B 1 112 ? 25.563 -32.419 26.234 1.00 12.51 ? 118 HIS   C C   1 
ATOM   1994 O  O   . HIS   B 1 112 ? 24.609 -32.014 26.924 1.00 14.21 ? 118 HIS   C O   1 
ATOM   1995 C  CB  . HIS   B 1 112 ? 27.455 -32.153 27.848 1.00 12.39 ? 118 HIS   C CB  1 
ATOM   1996 C  CG  . HIS   B 1 112 ? 28.645 -32.760 28.566 1.00 11.71 ? 118 HIS   C CG  1 
ATOM   1997 N  ND1 . HIS   B 1 112 ? 29.944 -32.470 28.197 1.00 10.57 ? 118 HIS   C ND1 1 
ATOM   1998 C  CD2 . HIS   B 1 112 ? 28.681 -33.586 29.658 1.00 13.89 ? 118 HIS   C CD2 1 
ATOM   1999 C  CE1 . HIS   B 1 112 ? 30.729 -33.164 28.998 1.00 11.85 ? 118 HIS   C CE1 1 
ATOM   2000 N  NE2 . HIS   B 1 112 ? 30.007 -33.842 29.892 1.00 14.67 ? 118 HIS   C NE2 1 
ATOM   2001 N  N   . GLY   B 1 113 ? 25.626 -32.168 24.915 1.00 11.13 ? 119 GLY   C N   1 
ATOM   2002 C  CA  . GLY   B 1 113 ? 24.556 -31.478 24.205 1.00 11.12 ? 119 GLY   C CA  1 
ATOM   2003 C  C   . GLY   B 1 113 ? 25.112 -30.422 23.269 1.00 9.80  ? 119 GLY   C C   1 
ATOM   2004 O  O   . GLY   B 1 113 ? 26.256 -30.480 22.794 1.00 9.76  ? 119 GLY   C O   1 
ATOM   2005 N  N   . VAL   B 1 114 ? 24.268 -29.408 23.021 1.00 9.91  ? 120 VAL   C N   1 
ATOM   2006 C  CA  . VAL   B 1 114 ? 24.593 -28.336 22.080 1.00 9.36  ? 120 VAL   C CA  1 
ATOM   2007 C  C   . VAL   B 1 114 ? 25.505 -27.338 22.771 1.00 8.56  ? 120 VAL   C C   1 
ATOM   2008 O  O   . VAL   B 1 114 ? 25.185 -26.776 23.832 1.00 9.86  ? 120 VAL   C O   1 
ATOM   2009 C  CB  . VAL   B 1 114 ? 23.295 -27.645 21.600 1.00 10.12 ? 120 VAL   C CB  1 
ATOM   2010 C  CG1 . VAL   B 1 114 ? 23.622 -26.427 20.729 1.00 11.03 ? 120 VAL   C CG1 1 
ATOM   2011 C  CG2 . VAL   B 1 114 ? 22.391 -28.629 20.847 1.00 11.63 ? 120 VAL   C CG2 1 
ATOM   2012 N  N   . VAL   B 1 115 ? 26.660 -27.075 22.175 1.00 7.85  ? 121 VAL   C N   1 
ATOM   2013 C  CA  . VAL   B 1 115 ? 27.668 -26.140 22.677 1.00 8.51  ? 121 VAL   C CA  1 
ATOM   2014 C  C   . VAL   B 1 115 ? 27.425 -24.716 22.173 1.00 9.00  ? 121 VAL   C C   1 
ATOM   2015 O  O   . VAL   B 1 115 ? 27.685 -23.724 22.885 1.00 9.50  ? 121 VAL   C O   1 
ATOM   2016 C  CB  . VAL   B 1 115 ? 29.070 -26.638 22.264 1.00 8.56  ? 121 VAL   C CB  1 
ATOM   2017 C  CG1 . VAL   B 1 115 ? 30.146 -25.654 22.664 1.00 10.17 ? 121 VAL   C CG1 1 
ATOM   2018 C  CG2 . VAL   B 1 115 ? 29.354 -28.034 22.833 1.00 10.40 ? 121 VAL   C CG2 1 
ATOM   2019 N  N   . GLY   B 1 116 ? 27.071 -24.612 20.877 1.00 8.63  ? 122 GLY   C N   1 
ATOM   2020 C  CA  . GLY   B 1 116 ? 26.871 -23.304 20.252 1.00 10.08 ? 122 GLY   C CA  1 
ATOM   2021 C  C   . GLY   B 1 116 ? 26.540 -23.493 18.777 1.00 7.89  ? 122 GLY   C C   1 
ATOM   2022 O  O   . GLY   B 1 116 ? 26.217 -24.606 18.342 1.00 9.00  ? 122 GLY   C O   1 
ATOM   2023 N  N   . ILE   B 1 117 ? 26.517 -22.346 18.040 1.00 7.85  ? 123 ILE   C N   1 
ATOM   2024 C  CA  . ILE   B 1 117 ? 26.177 -22.355 16.617 1.00 7.96  ? 123 ILE   C CA  1 
ATOM   2025 C  C   . ILE   B 1 117 ? 27.227 -21.638 15.829 1.00 7.88  ? 123 ILE   C C   1 
ATOM   2026 O  O   . ILE   B 1 117 ? 27.852 -20.669 16.312 1.00 8.95  ? 123 ILE   C O   1 
ATOM   2027 C  CB  . ILE   B 1 117 ? 24.755 -21.731 16.357 1.00 8.88  ? 123 ILE   C CB  1 
ATOM   2028 C  CG1 . ILE   B 1 117 ? 24.628 -20.346 17.009 1.00 10.44 ? 123 ILE   C CG1 1 
ATOM   2029 C  CG2 . ILE   B 1 117 ? 23.647 -22.712 16.782 1.00 11.13 ? 123 ILE   C CG2 1 
ATOM   2030 C  CD1 . ILE   B 1 117 ? 23.319 -19.554 16.583 1.00 11.32 ? 123 ILE   C CD1 1 
ATOM   2031 N  N   . VAL   B 1 118 ? 27.410 -22.043 14.562 1.00 7.78  ? 124 VAL   C N   1 
ATOM   2032 C  CA  . VAL   B 1 118 ? 28.347 -21.362 13.672 1.00 8.35  ? 124 VAL   C CA  1 
ATOM   2033 C  C   . VAL   B 1 118 ? 27.949 -19.879 13.561 1.00 8.63  ? 124 VAL   C C   1 
ATOM   2034 O  O   . VAL   B 1 118 ? 26.752 -19.546 13.348 1.00 8.71  ? 124 VAL   C O   1 
ATOM   2035 C  CB  . VAL   B 1 118 ? 28.333 -21.996 12.277 1.00 8.56  ? 124 VAL   C CB  1 
ATOM   2036 C  CG1 . VAL   B 1 118 ? 29.199 -21.233 11.287 1.00 9.42  ? 124 VAL   C CG1 1 
ATOM   2037 C  CG2 . VAL   B 1 118 ? 28.794 -23.459 12.326 1.00 9.27  ? 124 VAL   C CG2 1 
ATOM   2038 N  N   . SER   B 1 119 ? 28.963 -19.003 13.663 1.00 8.44  ? 125 SER   C N   1 
ATOM   2039 C  CA  . SER   B 1 119 ? 28.768 -17.546 13.546 1.00 9.03  ? 125 SER   C CA  1 
ATOM   2040 C  C   . SER   B 1 119 ? 29.802 -16.852 12.664 1.00 9.87  ? 125 SER   C C   1 
ATOM   2041 O  O   . SER   B 1 119 ? 29.469 -15.770 12.124 1.00 10.27 ? 125 SER   C O   1 
ATOM   2042 C  CB  . SER   B 1 119 ? 28.788 -16.952 14.950 1.00 10.70 ? 125 SER   C CB  1 
ATOM   2043 O  OG  . SER   B 1 119 ? 28.684 -15.528 14.955 1.00 11.29 ? 125 SER   C OG  1 
ATOM   2044 N  N   . THR   B 1 120 ? 31.037 -17.380 12.527 1.00 9.43  ? 126 THR   C N   1 
ATOM   2045 C  CA  . THR   B 1 120 ? 32.058 -16.709 11.735 1.00 9.71  ? 126 THR   C CA  1 
ATOM   2046 C  C   . THR   B 1 120 ? 32.768 -17.715 10.811 1.00 9.08  ? 126 THR   C C   1 
ATOM   2047 O  O   . THR   B 1 120 ? 32.722 -18.943 11.046 1.00 9.23  ? 126 THR   C O   1 
ATOM   2048 C  CB  . THR   B 1 120 ? 33.140 -15.997 12.618 1.00 10.03 ? 126 THR   C CB  1 
ATOM   2049 O  OG1 . THR   B 1 120 ? 33.955 -16.957 13.274 1.00 10.63 ? 126 THR   C OG1 1 
ATOM   2050 C  CG2 . THR   B 1 120 ? 32.543 -15.047 13.652 1.00 11.72 ? 126 THR   C CG2 1 
ATOM   2051 N  N   . GLY   B 1 121 ? 33.453 -17.217 9.813  1.00 9.65  ? 127 GLY   C N   1 
ATOM   2052 C  CA  . GLY   B 1 121 ? 34.286 -18.040 8.939  1.00 11.98 ? 127 GLY   C CA  1 
ATOM   2053 C  C   . GLY   B 1 121 ? 35.309 -17.171 8.220  1.00 14.44 ? 127 GLY   C C   1 
ATOM   2054 O  O   . GLY   B 1 121 ? 34.996 -16.074 7.751  1.00 17.68 ? 127 GLY   C O   1 
ATOM   2055 N  N   . GLY   B 1 122 ? 36.518 -17.640 8.066  1.00 17.85 ? 128 GLY   C N   1 
ATOM   2056 C  CA  . GLY   B 1 122 ? 37.558 -16.884 7.344  1.00 19.63 ? 128 GLY   C CA  1 
ATOM   2057 C  C   . GLY   B 1 122 ? 38.885 -17.512 7.595  1.00 20.41 ? 128 GLY   C C   1 
ATOM   2058 O  O   . GLY   B 1 122 ? 39.111 -18.076 8.656  1.00 19.88 ? 128 GLY   C O   1 
ATOM   2059 N  N   . ASN   B 1 123 ? 39.810 -17.381 6.639  1.00 18.58 ? 129 ASN   C N   1 
ATOM   2060 C  CA  . ASN   B 1 123 ? 41.190 -17.844 6.779  1.00 18.62 ? 129 ASN   C CA  1 
ATOM   2061 C  C   . ASN   B 1 123 ? 41.250 -19.301 7.212  1.00 17.00 ? 129 ASN   C C   1 
ATOM   2062 O  O   . ASN   B 1 123 ? 42.156 -19.671 7.957  1.00 20.12 ? 129 ASN   C O   1 
ATOM   2063 C  CB  . ASN   B 1 123 ? 41.994 -16.932 7.774  1.00 21.08 ? 129 ASN   C CB  1 
ATOM   2064 C  CG  . ASN   B 1 123 ? 42.792 -15.806 7.141  1.00 26.30 ? 129 ASN   C CG  1 
ATOM   2065 O  OD1 . ASN   B 1 123 ? 43.189 -15.874 5.976  1.00 28.27 ? 129 ASN   C OD1 1 
ATOM   2066 N  ND2 . ASN   B 1 123 ? 43.062 -14.733 7.893  1.00 26.34 ? 129 ASN   C ND2 1 
ATOM   2067 N  N   . GLY   B 1 124 ? 40.314 -20.138 6.755  1.00 15.27 ? 130 GLY   C N   1 
ATOM   2068 C  CA  . GLY   B 1 124 ? 40.338 -21.561 7.143  1.00 15.15 ? 130 GLY   C CA  1 
ATOM   2069 C  C   . GLY   B 1 124 ? 39.929 -21.869 8.565  1.00 13.19 ? 130 GLY   C C   1 
ATOM   2070 O  O   . GLY   B 1 124 ? 40.197 -22.977 9.054  1.00 13.55 ? 130 GLY   C O   1 
ATOM   2071 N  N   . LEU   B 1 125 ? 39.300 -20.920 9.220  1.00 11.78 ? 131 LEU   C N   1 
ATOM   2072 C  CA  . LEU   B 1 125 ? 38.813 -21.073 10.582 1.00 11.97 ? 131 LEU   C CA  1 
ATOM   2073 C  C   . LEU   B 1 125 ? 37.284 -20.962 10.624 1.00 11.19 ? 131 LEU   C C   1 
ATOM   2074 O  O   . LEU   B 1 125 ? 36.697 -20.172 9.857  1.00 14.34 ? 131 LEU   C O   1 
ATOM   2075 C  CB  . LEU   B 1 125 ? 39.450 -20.019 11.511 1.00 13.80 ? 131 LEU   C CB  1 
ATOM   2076 C  CG  . LEU   B 1 125 ? 40.991 -20.109 11.565 1.00 16.08 ? 131 LEU   C CG  1 
ATOM   2077 C  CD1 . LEU   B 1 125 ? 41.656 -18.754 11.899 1.00 20.05 ? 131 LEU   C CD1 1 
ATOM   2078 C  CD2 . LEU   B 1 125 ? 41.459 -21.276 12.400 1.00 16.73 ? 131 LEU   C CD2 1 
ATOM   2079 N  N   . VAL   B 1 126 ? 36.671 -21.674 11.496 1.00 9.22  ? 132 VAL   C N   1 
ATOM   2080 C  CA  . VAL   B 1 126 ? 35.219 -21.577 11.758 1.00 9.22  ? 132 VAL   C CA  1 
ATOM   2081 C  C   . VAL   B 1 126 ? 35.090 -21.112 13.195 1.00 8.57  ? 132 VAL   C C   1 
ATOM   2082 O  O   . VAL   B 1 126 ? 35.744 -21.659 14.106 1.00 9.49  ? 132 VAL   C O   1 
ATOM   2083 C  CB  . VAL   B 1 126 ? 34.479 -22.923 11.507 1.00 9.36  ? 132 VAL   C CB  1 
ATOM   2084 C  CG1 . VAL   B 1 126 ? 35.121 -24.121 12.165 1.00 11.76 ? 132 VAL   C CG1 1 
ATOM   2085 C  CG2 . VAL   B 1 126 ? 32.988 -22.836 11.866 1.00 10.15 ? 132 VAL   C CG2 1 
ATOM   2086 N  N   . GLY   B 1 127 ? 34.188 -20.151 13.409 1.00 8.46  ? 133 GLY   C N   1 
ATOM   2087 C  CA  . GLY   B 1 127 ? 33.926 -19.647 14.763 1.00 9.06  ? 133 GLY   C CA  1 
ATOM   2088 C  C   . GLY   B 1 127 ? 32.493 -19.958 15.197 1.00 8.75  ? 133 GLY   C C   1 
ATOM   2089 O  O   . GLY   B 1 127 ? 31.541 -19.830 14.391 1.00 9.29  ? 133 GLY   C O   1 
ATOM   2090 N  N   . PHE   B 1 128 ? 32.348 -20.341 16.450 1.00 8.58  ? 134 PHE   C N   1 
ATOM   2091 C  CA  . PHE   B 1 128 ? 31.063 -20.729 17.065 1.00 8.67  ? 134 PHE   C CA  1 
ATOM   2092 C  C   . PHE   B 1 128 ? 30.734 -19.791 18.206 1.00 8.34  ? 134 PHE   C C   1 
ATOM   2093 O  O   . PHE   B 1 128 ? 31.580 -19.522 19.075 1.00 9.47  ? 134 PHE   C O   1 
ATOM   2094 C  CB  . PHE   B 1 128 ? 31.130 -22.153 17.642 1.00 8.24  ? 134 PHE   C CB  1 
ATOM   2095 C  CG  . PHE   B 1 128 ? 31.673 -23.168 16.650 1.00 8.36  ? 134 PHE   C CG  1 
ATOM   2096 C  CD1 . PHE   B 1 128 ? 30.830 -23.763 15.714 1.00 8.39  ? 134 PHE   C CD1 1 
ATOM   2097 C  CD2 . PHE   B 1 128 ? 33.016 -23.528 16.668 1.00 8.91  ? 134 PHE   C CD2 1 
ATOM   2098 C  CE1 . PHE   B 1 128 ? 31.316 -24.713 14.829 1.00 8.87  ? 134 PHE   C CE1 1 
ATOM   2099 C  CE2 . PHE   B 1 128 ? 33.513 -24.477 15.759 1.00 9.63  ? 134 PHE   C CE2 1 
ATOM   2100 C  CZ  . PHE   B 1 128 ? 32.659 -25.082 14.860 1.00 9.61  ? 134 PHE   C CZ  1 
ATOM   2101 N  N   . ALA   B 1 129 ? 29.483 -19.307 18.220 1.00 8.77  ? 135 ALA   C N   1 
ATOM   2102 C  CA  . ALA   B 1 129 ? 28.960 -18.513 19.331 1.00 9.01  ? 135 ALA   C CA  1 
ATOM   2103 C  C   . ALA   B 1 129 ? 28.571 -19.487 20.463 1.00 8.84  ? 135 ALA   C C   1 
ATOM   2104 O  O   . ALA   B 1 129 ? 27.673 -20.325 20.296 1.00 9.17  ? 135 ALA   C O   1 
ATOM   2105 C  CB  . ALA   B 1 129 ? 27.734 -17.720 18.872 1.00 9.48  ? 135 ALA   C CB  1 
ATOM   2106 N  N   . ASP   B 1 130 ? 29.269 -19.405 21.611 1.00 8.88  ? 136 ASP   C N   1 
ATOM   2107 C  CA  . ASP   B 1 130 ? 28.979 -20.275 22.749 1.00 9.22  ? 136 ASP   C CA  1 
ATOM   2108 C  C   . ASP   B 1 130 ? 27.618 -19.938 23.332 1.00 10.05 ? 136 ASP   C C   1 
ATOM   2109 O  O   . ASP   B 1 130 ? 27.222 -18.753 23.416 1.00 10.31 ? 136 ASP   C O   1 
ATOM   2110 C  CB  . ASP   B 1 130 ? 30.050 -20.038 23.832 1.00 10.68 ? 136 ASP   C CB  1 
ATOM   2111 C  CG  . ASP   B 1 130 ? 29.944 -20.963 25.028 1.00 11.41 ? 136 ASP   C CG  1 
ATOM   2112 O  OD1 . ASP   B 1 130 ? 29.814 -22.195 24.838 1.00 12.08 ? 136 ASP   C OD1 1 
ATOM   2113 O  OD2 . ASP   B 1 130 ? 29.863 -20.438 26.175 1.00 14.73 ? 136 ASP   C OD2 1 
ATOM   2114 N  N   . VAL   B 1 131 ? 26.926 -20.963 23.828 1.00 9.78  ? 137 VAL   C N   1 
ATOM   2115 C  CA  . VAL   B 1 131 ? 25.674 -20.803 24.586 1.00 9.45  ? 137 VAL   C CA  1 
ATOM   2116 C  C   . VAL   B 1 131 ? 25.739 -21.463 25.956 1.00 10.37 ? 137 VAL   C C   1 
ATOM   2117 O  O   . VAL   B 1 131 ? 24.750 -21.413 26.696 1.00 11.12 ? 137 VAL   C O   1 
ATOM   2118 C  CB  . VAL   B 1 131 ? 24.412 -21.270 23.823 1.00 10.11 ? 137 VAL   C CB  1 
ATOM   2119 C  CG1 . VAL   B 1 131 ? 24.231 -20.447 22.527 1.00 10.68 ? 137 VAL   C CG1 1 
ATOM   2120 C  CG2 . VAL   B 1 131 ? 24.436 -22.754 23.512 1.00 11.26 ? 137 VAL   C CG2 1 
ATOM   2121 N  N   . ARG   B 1 132 ? 26.875 -22.119 26.322 1.00 9.98  ? 138 ARG   C N   1 
ATOM   2122 C  CA  . ARG   B 1 132 ? 26.930 -22.904 27.562 1.00 10.02 ? 138 ARG   C CA  1 
ATOM   2123 C  C   . ARG   B 1 132 ? 26.860 -22.070 28.822 1.00 10.49 ? 138 ARG   C C   1 
ATOM   2124 O  O   . ARG   B 1 132 ? 26.521 -22.635 29.882 1.00 12.30 ? 138 ARG   C O   1 
ATOM   2125 C  CB  . ARG   B 1 132 ? 28.187 -23.754 27.551 1.00 10.05 ? 138 ARG   C CB  1 
ATOM   2126 C  CG  . ARG   B 1 132 ? 28.202 -24.810 26.420 1.00 10.12 ? 138 ARG   C CG  1 
ATOM   2127 C  CD  . ARG   B 1 132 ? 29.524 -25.572 26.482 1.00 9.87  ? 138 ARG   C CD  1 
ATOM   2128 N  NE  . ARG   B 1 132 ? 30.605 -24.680 26.091 1.00 9.95  ? 138 ARG   C NE  1 
ATOM   2129 C  CZ  . ARG   B 1 132 ? 31.864 -25.042 25.924 1.00 10.36 ? 138 ARG   C CZ  1 
ATOM   2130 N  NH1 . ARG   B 1 132 ? 32.257 -26.281 26.242 1.00 10.69 ? 138 ARG   C NH1 1 
ATOM   2131 N  NH2 . ARG   B 1 132 ? 32.752 -24.171 25.435 1.00 10.93 ? 138 ARG   C NH2 1 
ATOM   2132 N  N   . ASP   B 1 133 ? 27.170 -20.775 28.760 1.00 10.54 ? 139 ASP   C N   1 
ATOM   2133 C  CA  . ASP   B 1 133 ? 27.078 -19.902 29.932 1.00 11.52 ? 139 ASP   C CA  1 
ATOM   2134 C  C   . ASP   B 1 133 ? 25.649 -19.364 30.145 1.00 12.31 ? 139 ASP   C C   1 
ATOM   2135 O  O   . ASP   B 1 133 ? 25.403 -18.722 31.181 1.00 13.96 ? 139 ASP   C O   1 
ATOM   2136 C  CB  . ASP   B 1 133 ? 28.052 -18.709 29.805 1.00 13.21 ? 139 ASP   C CB  1 
ATOM   2137 C  CG  . ASP   B 1 133 ? 27.698 -17.795 28.651 1.00 13.82 ? 139 ASP   C CG  1 
ATOM   2138 O  OD1 . ASP   B 1 133 ? 27.317 -18.300 27.578 1.00 13.72 ? 139 ASP   C OD1 1 
ATOM   2139 O  OD2 . ASP   B 1 133 ? 27.785 -16.533 28.827 1.00 16.51 ? 139 ASP   C OD2 1 
ATOM   2140 N  N   . LEU   B 1 134 ? 24.708 -19.580 29.184 1.00 11.51 ? 140 LEU   C N   1 
ATOM   2141 C  CA  . LEU   B 1 134 ? 23.353 -19.000 29.285 1.00 12.10 ? 140 LEU   C CA  1 
ATOM   2142 C  C   . LEU   B 1 134 ? 22.479 -19.984 30.052 1.00 11.74 ? 140 LEU   C C   1 
ATOM   2143 O  O   . LEU   B 1 134 ? 21.690 -20.736 29.490 1.00 12.34 ? 140 LEU   C O   1 
ATOM   2144 C  CB  . LEU   B 1 134 ? 22.812 -18.750 27.874 1.00 12.59 ? 140 LEU   C CB  1 
ATOM   2145 C  CG  . LEU   B 1 134 ? 23.660 -17.797 26.994 1.00 12.43 ? 140 LEU   C CG  1 
ATOM   2146 C  CD1 . LEU   B 1 134 ? 23.083 -17.748 25.556 1.00 13.03 ? 140 LEU   C CD1 1 
ATOM   2147 C  CD2 . LEU   B 1 134 ? 23.777 -16.400 27.621 1.00 14.21 ? 140 LEU   C CD2 1 
ATOM   2148 N  N   . LEU   B 1 135 ? 22.705 -20.043 31.383 1.00 12.78 ? 141 LEU   C N   1 
ATOM   2149 C  CA  . LEU   B 1 135 ? 22.075 -21.088 32.206 1.00 13.35 ? 141 LEU   C CA  1 
ATOM   2150 C  C   . LEU   B 1 135 ? 20.559 -20.991 32.252 1.00 13.64 ? 141 LEU   C C   1 
ATOM   2151 O  O   . LEU   B 1 135 ? 19.865 -21.997 32.435 1.00 14.76 ? 141 LEU   C O   1 
ATOM   2152 C  CB  . LEU   B 1 135 ? 22.623 -21.067 33.644 1.00 14.14 ? 141 LEU   C CB  1 
ATOM   2153 C  CG  . LEU   B 1 135 ? 24.178 -21.074 33.757 1.00 15.30 ? 141 LEU   C CG  1 
ATOM   2154 C  CD1 . LEU   B 1 135 ? 24.672 -21.147 35.222 1.00 16.79 ? 141 LEU   C CD1 1 
ATOM   2155 C  CD2 . LEU   B 1 135 ? 24.825 -22.217 32.953 1.00 15.28 ? 141 LEU   C CD2 1 
ATOM   2156 N  N   . TRP   B 1 136 ? 20.035 -19.774 32.062 1.00 13.21 ? 142 TRP   C N   1 
ATOM   2157 C  CA  . TRP   B 1 136 ? 18.587 -19.520 32.071 1.00 14.34 ? 142 TRP   C CA  1 
ATOM   2158 C  C   . TRP   B 1 136 ? 17.872 -20.218 30.934 1.00 14.92 ? 142 TRP   C C   1 
ATOM   2159 O  O   . TRP   B 1 136 ? 16.643 -20.365 31.001 1.00 15.76 ? 142 TRP   C O   1 
ATOM   2160 C  CB  . TRP   B 1 136 ? 18.297 -18.013 32.082 1.00 14.68 ? 142 TRP   C CB  1 
ATOM   2161 C  CG  . TRP   B 1 136 ? 18.998 -17.269 30.983 1.00 14.34 ? 142 TRP   C CG  1 
ATOM   2162 C  CD1 . TRP   B 1 136 ? 20.172 -16.586 31.066 1.00 14.64 ? 142 TRP   C CD1 1 
ATOM   2163 C  CD2 . TRP   B 1 136 ? 18.499 -17.045 29.642 1.00 14.13 ? 142 TRP   C CD2 1 
ATOM   2164 N  NE1 . TRP   B 1 136 ? 20.471 -15.996 29.847 1.00 15.73 ? 142 TRP   C NE1 1 
ATOM   2165 C  CE2 . TRP   B 1 136 ? 19.443 -16.246 28.967 1.00 14.94 ? 142 TRP   C CE2 1 
ATOM   2166 C  CE3 . TRP   B 1 136 ? 17.336 -17.420 28.981 1.00 14.49 ? 142 TRP   C CE3 1 
ATOM   2167 C  CZ2 . TRP   B 1 136 ? 19.258 -15.831 27.631 1.00 14.93 ? 142 TRP   C CZ2 1 
ATOM   2168 C  CZ3 . TRP   B 1 136 ? 17.130 -16.973 27.681 1.00 14.70 ? 142 TRP   C CZ3 1 
ATOM   2169 C  CH2 . TRP   B 1 136 ? 18.104 -16.224 27.017 1.00 14.66 ? 142 TRP   C CH2 1 
ATOM   2170 N  N   . LEU   B 1 137 ? 18.567 -20.645 29.861 1.00 13.57 ? 143 LEU   C N   1 
ATOM   2171 C  CA  . LEU   B 1 137 ? 17.888 -21.422 28.803 1.00 14.13 ? 143 LEU   C CA  1 
ATOM   2172 C  C   . LEU   B 1 137 ? 17.275 -22.706 29.366 1.00 17.08 ? 143 LEU   C C   1 
ATOM   2173 O  O   . LEU   B 1 137 ? 16.351 -23.245 28.743 1.00 19.10 ? 143 LEU   C O   1 
ATOM   2174 C  CB  . LEU   B 1 137 ? 18.842 -21.781 27.656 1.00 13.18 ? 143 LEU   C CB  1 
ATOM   2175 C  CG  . LEU   B 1 137 ? 19.309 -20.587 26.813 1.00 12.69 ? 143 LEU   C CG  1 
ATOM   2176 C  CD1 . LEU   B 1 137 ? 20.470 -20.999 25.886 1.00 14.32 ? 143 LEU   C CD1 1 
ATOM   2177 C  CD2 . LEU   B 1 137 ? 18.146 -20.017 25.945 1.00 14.27 ? 143 LEU   C CD2 1 
ATOM   2178 N  N   . ASP   B 1 138 ? 17.809 -23.217 30.520 1.00 15.96 ? 144 ASP   C N   1 
ATOM   2179 C  CA  . ASP   B 1 138 ? 17.372 -24.494 31.118 1.00 18.24 ? 144 ASP   C CA  1 
ATOM   2180 C  C   . ASP   B 1 138 ? 16.116 -24.373 31.970 1.00 20.63 ? 144 ASP   C C   1 
ATOM   2181 O  O   . ASP   B 1 138 ? 15.675 -25.404 32.501 1.00 22.63 ? 144 ASP   C O   1 
ATOM   2182 C  CB  . ASP   B 1 138 ? 18.480 -25.108 32.000 1.00 18.41 ? 144 ASP   C CB  1 
ATOM   2183 C  CG  . ASP   B 1 138 ? 19.731 -25.540 31.235 1.00 18.03 ? 144 ASP   C CG  1 
ATOM   2184 O  OD1 . ASP   B 1 138 ? 19.691 -25.594 29.995 1.00 18.55 ? 144 ASP   C OD1 1 
ATOM   2185 O  OD2 . ASP   B 1 138 ? 20.754 -25.840 31.896 1.00 22.24 ? 144 ASP   C OD2 1 
ATOM   2186 N  N   . GLU   B 1 139 ? 15.539 -23.183 32.123 1.00 20.70 ? 145 GLU   C N   1 
ATOM   2187 C  CA  . GLU   B 1 139 ? 14.365 -23.018 32.994 1.00 25.17 ? 145 GLU   C CA  1 
ATOM   2188 C  C   . GLU   B 1 139 ? 13.410 -21.909 32.521 1.00 29.17 ? 145 GLU   C C   1 
ATOM   2189 O  O   . GLU   B 1 139 ? 13.683 -21.241 31.533 1.00 30.03 ? 145 GLU   C O   1 
ATOM   2190 C  CB  . GLU   B 1 139 ? 14.882 -22.718 34.416 1.00 30.17 ? 145 GLU   C CB  1 
ATOM   2191 C  CG  . GLU   B 1 139 ? 15.689 -21.435 34.478 1.00 36.97 ? 145 GLU   C CG  1 
ATOM   2192 C  CD  . GLU   B 1 139 ? 16.615 -21.272 35.666 1.00 46.26 ? 145 GLU   C CD  1 
ATOM   2193 O  OE1 . GLU   B 1 139 ? 17.521 -20.409 35.592 1.00 49.41 ? 145 GLU   C OE1 1 
ATOM   2194 O  OE2 . GLU   B 1 139 ? 16.423 -21.984 36.676 1.00 47.43 ? 145 GLU   C OE2 1 
ATOM   2195 N  N   . GLU   B 1 140 ? 12.298 -21.692 33.268 1.00 32.20 ? 146 GLU   C N   1 
ATOM   2196 C  CA  . GLU   B 1 140 ? 11.334 -20.583 33.117 1.00 34.89 ? 146 GLU   C CA  1 
ATOM   2197 C  C   . GLU   B 1 140 ? 10.823 -20.455 31.706 1.00 36.89 ? 146 GLU   C C   1 
ATOM   2198 O  O   . GLU   B 1 140 ? 10.463 -19.377 31.247 1.00 37.66 ? 146 GLU   C O   1 
ATOM   2199 C  CB  . GLU   B 1 140 ? 11.961 -19.274 33.661 1.00 37.52 ? 146 GLU   C CB  1 
ATOM   2200 C  CG  . GLU   B 1 140 ? 11.425 -17.925 33.178 1.00 46.03 ? 146 GLU   C CG  1 
ATOM   2201 C  CD  . GLU   B 1 140 ? 10.166 -17.352 33.805 1.00 55.09 ? 146 GLU   C CD  1 
ATOM   2202 O  OE1 . GLU   B 1 140 ? 10.044 -16.106 33.824 1.00 58.72 ? 146 GLU   C OE1 1 
ATOM   2203 O  OE2 . GLU   B 1 140 ? 9.292  -18.135 34.243 1.00 57.10 ? 146 GLU   C OE2 1 
HETATM 2204 N  N1  . A1B04 C 2 .   ? 10.163 17.421  20.268 1.00 23.90 ? 201 A1B04 A N1  1 
HETATM 2205 C  C4  . A1B04 C 2 .   ? 10.370 16.093  18.501 1.00 24.54 ? 201 A1B04 A C4  1 
HETATM 2206 C  C5  . A1B04 C 2 .   ? 9.307  17.728  19.361 1.00 24.11 ? 201 A1B04 A C5  1 
HETATM 2207 C  C6  . A1B04 C 2 .   ? 9.064  13.092  23.355 1.00 23.44 ? 201 A1B04 A C6  1 
HETATM 2208 C  C7  . A1B04 C 2 .   ? 9.354  11.830  22.820 1.00 24.53 ? 201 A1B04 A C7  1 
HETATM 2209 C  C8  . A1B04 C 2 .   ? 8.609  10.725  23.195 1.00 25.48 ? 201 A1B04 A C8  1 
HETATM 2210 C  C10 . A1B04 C 2 .   ? 7.291  12.101  24.655 1.00 24.48 ? 201 A1B04 A C10 1 
HETATM 2211 O  O   . A1B04 C 2 .   ? 10.080 15.078  24.111 1.00 25.93 ? 201 A1B04 A O   1 
HETATM 2212 C  C   . A1B04 C 2 .   ? 9.958  14.271  23.190 1.00 24.08 ? 201 A1B04 A C   1 
HETATM 2213 C  C11 . A1B04 C 2 .   ? 8.020  13.212  24.270 1.00 24.46 ? 201 A1B04 A C11 1 
HETATM 2214 C  C9  . A1B04 C 2 .   ? 7.569  10.863  24.108 1.00 24.82 ? 201 A1B04 A C9  1 
HETATM 2215 N  N   . A1B04 C 2 .   ? 10.651 14.366  22.045 1.00 22.45 ? 201 A1B04 A N   1 
HETATM 2216 C  C1  . A1B04 C 2 .   ? 11.691 15.381  21.892 1.00 22.38 ? 201 A1B04 A C1  1 
HETATM 2217 C  C2  . A1B04 C 2 .   ? 11.999 15.697  20.444 1.00 23.01 ? 201 A1B04 A C2  1 
HETATM 2218 C  C3  . A1B04 C 2 .   ? 10.866 16.352  19.718 1.00 23.77 ? 201 A1B04 A C3  1 
HETATM 2219 O  O1  . A1B04 C 2 .   ? 9.357  16.978  18.241 1.00 24.74 ? 201 A1B04 A O1  1 
HETATM 2220 ZN ZN  . ZN    D 3 .   ? 10.820 -3.568  5.733  1.00 14.77 2 202 ZN    A ZN  1 
HETATM 2221 S  S   . DMS   E 4 .   ? 19.404 -1.939  24.443 1.00 77.00 ? 203 DMS   A S   1 
HETATM 2222 O  O   . DMS   E 4 .   ? 20.331 -0.811  24.090 1.00 76.97 ? 203 DMS   A O   1 
HETATM 2223 C  C1  . DMS   E 4 .   ? 18.244 -2.151  23.069 1.00 76.87 ? 203 DMS   A C1  1 
HETATM 2224 C  C2  . DMS   E 4 .   ? 20.297 -3.494  24.181 1.00 77.11 ? 203 DMS   A C2  1 
HETATM 2225 ZN ZN  . ZN    F 3 .   ? 30.655 -31.110 26.776 1.00 10.54 2 201 ZN    C ZN  1 
HETATM 2226 S  S   . DMS   G 4 .   ? 20.847 -32.021 9.247  1.00 84.51 ? 202 DMS   C S   1 
HETATM 2227 O  O   . DMS   G 4 .   ? 22.064 -32.417 8.466  1.00 84.63 ? 202 DMS   C O   1 
HETATM 2228 C  C1  . DMS   G 4 .   ? 21.266 -32.049 11.001 1.00 84.44 ? 202 DMS   C C1  1 
HETATM 2229 C  C2  . DMS   G 4 .   ? 20.650 -30.223 9.128  1.00 84.45 ? 202 DMS   C C2  1 
HETATM 2230 O  O   . HOH   H 5 .   ? 35.317 -3.902  7.801  1.00 22.12 ? 301 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 2.233  22.689  21.841 1.00 24.83 ? 302 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 31.770 6.999   5.339  1.00 27.44 ? 303 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 2.979  9.439   9.241  1.00 26.93 ? 304 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 27.790 8.050   1.639  1.00 30.42 ? 305 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 11.169 9.201   4.541  1.00 20.43 ? 306 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 6.449  3.655   3.429  1.00 34.62 ? 307 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 0.431  -0.879  19.438 1.00 18.81 ? 308 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 0.994  12.017  21.353 1.00 33.20 ? 309 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 17.444 0.903   28.274 1.00 22.70 ? 310 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 12.385 -5.916  30.487 1.00 44.79 ? 311 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 37.656 14.983  13.906 1.00 40.67 ? 312 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 28.094 3.296   4.728  1.00 28.51 ? 313 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 33.824 14.091  9.650  1.00 29.07 ? 314 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 0.438  -1.498  9.282  1.00 38.34 ? 315 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 12.479 22.269  13.357 1.00 24.02 ? 316 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 10.633 10.133  31.488 1.00 22.32 ? 317 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 21.782 2.431   -0.934 1.00 30.97 ? 318 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 30.520 10.475  15.540 1.00 25.66 ? 319 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 12.319 16.643  27.993 1.00 27.41 ? 320 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 13.795 2.978   1.293  1.00 15.96 ? 321 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 4.653  -3.624  28.923 1.00 25.39 ? 322 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 25.068 4.920   21.396 1.00 27.64 ? 323 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 8.303  -2.829  31.922 1.00 23.99 ? 324 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 4.307  9.643   27.953 1.00 37.37 ? 325 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 33.867 -2.379  13.620 1.00 27.37 ? 326 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 29.646 22.170  19.461 1.00 20.35 ? 327 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 19.466 9.995   19.731 1.00 11.19 ? 328 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? -0.035 1.333   15.959 1.00 10.55 ? 329 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 14.457 13.676  24.216 1.00 21.52 ? 330 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 23.460 21.676  7.314  1.00 20.36 ? 331 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 16.001 23.936  15.078 1.00 33.89 ? 332 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 2.641  -2.927  20.845 1.00 21.98 ? 333 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 8.709  -2.877  0.556  1.00 29.23 ? 334 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 10.804 5.878   3.513  1.00 17.75 ? 335 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 1.020  9.499   9.540  1.00 31.98 ? 336 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 23.546 12.829  23.856 1.00 35.83 ? 337 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? -2.599 23.418  9.286  1.00 41.76 ? 338 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 10.759 17.126  25.793 1.00 27.03 ? 339 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 19.954 -4.190  10.881 1.00 30.37 ? 340 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 13.751 3.929   23.571 1.00 10.85 ? 341 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 22.652 0.796   17.373 1.00 13.71 ? 342 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 20.896 -4.177  14.199 1.00 13.81 ? 343 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 18.454 21.942  9.761  1.00 16.22 ? 344 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 7.489  20.029  17.778 1.00 18.64 ? 345 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 26.751 -1.197  8.721  1.00 20.78 ? 346 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 16.625 3.788   23.736 1.00 14.80 ? 347 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 17.878 17.785  4.534  1.00 31.55 ? 348 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 28.904 3.307   12.548 1.00 14.64 ? 349 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 12.326 11.065  29.762 1.00 19.16 ? 350 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 6.590  -6.944  23.764 1.00 22.86 ? 351 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 31.658 19.818  11.649 1.00 17.67 ? 352 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 30.024 11.487  18.423 1.00 23.56 ? 353 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 23.674 11.574  21.967 1.00 28.60 ? 354 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 33.723 11.073  15.460 1.00 34.30 ? 355 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 11.328 12.806  11.488 1.00 13.62 ? 356 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 20.510 -0.970  2.948  1.00 27.04 ? 357 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 1.528  5.304   27.128 1.00 29.11 ? 358 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 5.613  5.412   32.709 1.00 18.54 ? 359 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 30.562 2.847   14.686 1.00 20.82 ? 360 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 23.278 -6.546  11.929 1.00 23.46 ? 361 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 35.909 14.995  10.954 1.00 32.73 ? 362 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 3.927  12.904  17.753 1.00 23.59 ? 363 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 29.589 11.808  21.190 1.00 27.81 ? 364 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 17.270 -4.960  12.105 1.00 28.61 ? 365 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 17.752 19.944  17.187 1.00 15.44 ? 366 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 3.335  20.242  24.714 1.00 38.98 ? 367 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 8.600  24.548  24.185 1.00 26.55 ? 368 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 19.547 16.604  26.480 1.00 37.52 ? 369 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 29.196 6.724   19.953 1.00 39.22 ? 370 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 15.971 -6.758  10.793 1.00 35.80 ? 371 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 25.623 19.466  21.731 1.00 20.91 ? 372 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 36.608 17.811  14.336 1.00 25.60 ? 373 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 16.900 -3.613  27.799 1.00 31.43 ? 374 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 9.649  3.983   33.564 1.00 12.04 ? 375 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 9.135  3.719   3.085  1.00 20.08 ? 376 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 24.065 -3.480  16.054 1.00 29.24 ? 377 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 35.291 10.560  12.107 1.00 40.35 ? 378 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 28.850 15.828  4.296  1.00 28.86 ? 379 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 30.006 -1.490  8.537  1.00 32.09 ? 380 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 20.701 -2.552  16.814 1.00 12.57 ? 381 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 6.279  16.762  21.512 1.00 33.03 ? 382 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 21.901 4.792   24.674 1.00 31.87 ? 383 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 13.255 11.524  9.446  1.00 12.14 ? 384 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 13.982 24.713  26.203 1.00 38.83 ? 385 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 11.570 -7.062  24.706 1.00 23.07 ? 386 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 19.490 2.872   19.407 1.00 16.59 ? 387 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 27.179 -1.330  15.755 1.00 22.28 ? 388 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 17.119 6.024   26.997 1.00 25.70 ? 389 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 6.039  15.107  22.481 1.00 25.32 ? 390 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 14.416 -2.459  17.954 1.00 15.20 ? 391 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 22.718 -0.602  5.340  1.00 19.49 ? 392 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 31.199 15.497  22.708 1.00 20.39 ? 393 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 1.447  11.534  27.711 1.00 39.02 ? 394 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 25.170 17.833  4.628  1.00 28.82 ? 395 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 5.171  26.146  20.554 1.00 28.08 ? 396 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 17.773 10.503  26.263 1.00 19.93 ? 397 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 28.230 17.472  24.123 1.00 20.55 ? 398 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 2.449  15.978  19.410 1.00 25.99 ? 399 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 0.261  6.211   6.252  1.00 21.76 ? 400 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 3.176  7.565   24.635 1.00 19.36 ? 401 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 4.220  0.303   24.110 1.00 17.16 ? 402 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 31.976 8.722   7.513  1.00 21.13 ? 403 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 3.785  -3.740  6.066  1.00 25.25 ? 404 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 30.307 4.541   5.640  1.00 21.07 ? 405 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 32.834 16.512  9.201  1.00 26.84 ? 406 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 15.734 14.180  26.436 1.00 38.36 ? 407 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 15.360 15.392  3.822  1.00 28.69 ? 408 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 7.332  14.095  5.042  1.00 21.53 ? 409 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 36.320 -0.325  12.281 1.00 34.46 ? 410 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 16.657 21.240  19.355 1.00 30.11 ? 411 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 3.465  26.810  16.487 1.00 36.45 ? 412 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 5.192  8.278   2.455  1.00 34.02 ? 413 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 0.041  2.913   23.791 1.00 19.16 ? 414 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 0.503  -1.266  16.784 1.00 15.60 ? 415 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 17.430 0.582   20.194 1.00 16.00 ? 416 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 8.530  -6.408  9.653  1.00 22.70 ? 417 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 3.441  -0.299  21.507 1.00 18.50 ? 418 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 3.577  13.869  20.103 1.00 38.76 ? 419 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 34.092 18.660  10.602 1.00 23.05 ? 420 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 25.179 10.499  22.879 1.00 29.20 ? 421 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 7.395  26.782  15.350 1.00 29.88 ? 422 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 22.469 19.354  19.595 1.00 25.86 ? 423 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 8.210  16.512  25.984 1.00 31.99 ? 424 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 6.347  24.146  10.933 1.00 36.73 ? 425 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 30.923 -2.320  15.658 1.00 31.60 ? 426 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 34.010 5.088   16.536 1.00 29.79 ? 427 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 22.798 3.363   20.790 1.00 17.19 ? 428 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 8.411  6.530   33.865 1.00 16.80 ? 429 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 19.329 21.496  7.091  1.00 33.32 ? 430 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 23.164 19.089  6.394  1.00 17.15 ? 431 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 6.006  -3.549  31.484 1.00 27.19 ? 432 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 1.133  -5.020  17.641 1.00 30.79 ? 433 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 23.552 8.230   21.663 1.00 21.21 ? 434 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 17.826 24.490  10.614 1.00 29.32 ? 435 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 31.047 19.361  8.947  1.00 30.83 ? 436 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 13.088 -7.668  12.561 1.00 30.59 ? 437 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 36.705 16.016  16.591 1.00 30.05 ? 438 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 21.153 9.782   21.978 1.00 14.43 ? 439 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 19.663 13.353  2.242  1.00 29.30 ? 440 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 2.066  14.677  16.898 1.00 28.43 ? 441 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 16.737 -3.826  2.887  1.00 29.24 ? 442 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 17.124 -2.489  19.701 1.00 16.09 ? 443 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 15.842 21.532  7.550  1.00 20.13 ? 444 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 34.105 7.808   16.530 1.00 31.35 ? 445 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 19.316 9.398   -0.836 1.00 27.96 ? 446 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? -1.325 -3.015  15.754 1.00 27.43 ? 447 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 7.332  -4.330  2.681  1.00 30.22 ? 448 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 0.774  7.724   27.891 1.00 41.23 ? 449 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? -0.781 24.445  12.382 1.00 45.88 ? 450 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 31.775 9.096   17.288 1.00 38.91 ? 451 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 11.801 24.380  27.167 1.00 49.66 ? 452 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 18.546 2.094   22.709 1.00 34.34 ? 453 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 21.459 9.553   -1.856 1.00 45.81 ? 454 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 13.789 -6.672  25.708 1.00 41.75 ? 455 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 38.581 1.058   13.557 1.00 47.78 ? 456 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 27.902 10.045  22.965 1.00 42.18 ? 457 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 21.453 19.727  4.365  1.00 33.43 ? 458 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 16.775 -5.064  34.339 1.00 27.04 ? 459 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 23.690 6.174   23.171 1.00 41.05 ? 460 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 29.747 0.476   16.287 1.00 31.13 ? 461 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 31.117 12.749  22.990 1.00 38.10 ? 462 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 11.913 24.308  15.115 1.00 29.01 ? 463 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 0.148  0.084   23.244 1.00 25.13 ? 464 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 4.716  28.087  18.427 1.00 36.38 ? 465 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 8.776  12.200  31.637 1.00 35.55 ? 466 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 23.874 0.934   19.810 1.00 26.49 ? 467 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 9.466  8.222   2.487  1.00 32.47 ? 468 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 11.387 23.228  11.044 1.00 28.71 ? 469 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 12.530 -5.103  33.256 1.00 29.18 ? 470 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 37.848 -4.522  6.903  1.00 28.99 ? 471 HOH   A O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 30.440 6.893   17.743 1.00 33.33 ? 472 HOH   A O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 31.309 4.373   16.841 1.00 23.71 ? 473 HOH   A O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 21.644 10.961  24.412 1.00 27.07 ? 474 HOH   A O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 2.511  -1.702  22.901 1.00 33.19 ? 475 HOH   A O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? -0.378 13.655  17.070 1.00 26.93 ? 476 HOH   A O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 21.345 -1.081  18.915 1.00 26.86 ? 477 HOH   A O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 2.387  -5.059  22.617 1.00 32.28 ? 478 HOH   A O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 2.898  25.270  22.243 1.00 35.40 ? 479 HOH   A O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 32.076 11.246  6.402  1.00 28.35 ? 480 HOH   A O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 7.288  28.974  17.432 1.00 30.98 ? 481 HOH   A O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 28.926 1.485   18.858 1.00 41.37 ? 482 HOH   A O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 22.775 12.033  -1.929 1.00 39.31 ? 483 HOH   A O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 9.872  25.998  14.360 1.00 34.92 ? 484 HOH   A O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 26.634 0.268   19.756 1.00 45.15 ? 485 HOH   A O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 27.680 -20.635 1.304  1.00 32.15 ? 301 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 17.533 -33.424 24.188 1.00 39.28 ? 302 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 10.000 -20.135 28.910 1.00 32.23 ? 303 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 38.365 -18.459 21.603 1.00 23.01 ? 304 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 31.113 -23.585 -1.327 1.00 21.51 ? 305 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 38.327 -7.323  7.014  1.00 20.45 ? 306 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 36.184 -2.521  11.081 1.00 33.83 ? 307 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 31.120 -32.197 0.720  1.00 32.87 ? 308 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 24.498 -9.807  27.000 1.00 34.29 ? 309 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 24.653 -5.932  15.240 1.00 23.46 ? 310 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 27.016 -7.864  2.183  1.00 44.99 ? 311 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 19.696 -4.081  20.177 1.00 18.45 ? 312 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 30.778 -18.066 26.963 1.00 15.72 ? 313 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 14.642 -18.634 31.922 1.00 34.10 ? 314 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 42.640 -11.109 11.366 1.00 21.11 ? 315 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 22.864 -5.888  21.164 1.00 16.79 ? 316 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 36.153 -26.114 34.289 1.00 30.63 ? 317 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 36.147 -17.540 11.847 1.00 19.17 ? 318 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 22.616 -7.311  25.273 1.00 36.92 ? 319 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 43.257 -3.798  19.110 1.00 38.49 ? 320 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 14.568 -9.261  11.042 1.00 29.43 ? 321 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 10.221 -17.512 18.369 1.00 22.96 ? 322 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 16.720 -15.382 8.465  1.00 49.20 ? 323 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 20.744 -18.681 12.872 1.00 11.07 ? 324 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 17.908 -27.539 16.549 1.00 15.65 ? 325 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 17.804 -6.033  24.167 1.00 21.29 ? 326 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 18.513 -8.852  13.821 1.00 23.92 ? 327 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 37.291 -18.679 28.221 1.00 23.21 ? 328 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 37.476 -31.802 11.009 1.00 21.16 ? 329 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 40.178 -29.481 11.987 1.00 20.27 ? 330 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 7.350  -30.461 22.407 1.00 28.48 ? 331 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 21.743 -26.073 34.431 1.00 23.81 ? 332 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 14.786 -23.959 12.324 1.00 27.06 ? 333 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 24.754 -15.716 7.453  1.00 16.22 ? 334 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 32.482 -23.641 29.216 1.00 14.03 ? 335 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 27.949 -4.534  18.488 1.00 38.80 ? 336 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 40.584 -27.142 15.316 1.00 10.11 ? 337 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 30.934 -21.460 28.497 1.00 13.93 ? 338 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 22.118 -28.493 4.813  1.00 21.16 ? 339 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 3.309  -12.973 20.301 1.00 37.65 ? 340 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 16.789 -9.374  27.690 1.00 31.33 ? 341 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 26.528 -5.444  9.849  1.00 19.24 ? 342 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 26.356 -15.212 30.794 1.00 26.69 ? 343 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 37.373 -10.484 5.106  1.00 34.82 ? 344 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 26.077 -25.150 8.857  1.00 10.91 ? 345 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 35.242 -13.061 8.814  1.00 16.76 ? 346 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 41.236 -24.917 7.357  1.00 26.65 ? 347 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 11.133 -21.704 13.743 1.00 34.29 ? 348 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 34.808 -34.823 18.127 1.00 24.99 ? 349 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 9.180  -8.129  21.394 1.00 22.15 ? 350 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 31.361 -35.327 31.827 1.00 38.65 ? 351 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 35.308 -32.745 3.429  1.00 29.00 ? 352 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 32.046 -10.464 13.867 1.00 16.25 ? 353 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 45.381 -14.573 4.824  1.00 31.18 ? 354 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 20.783 -25.634 13.884 1.00 16.34 ? 355 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 11.887 -24.288 21.698 1.00 16.45 ? 356 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 29.868 -15.236 19.685 1.00 13.48 ? 357 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 9.790  -8.908  23.958 1.00 24.61 ? 358 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 13.271 -11.225 28.611 1.00 32.71 ? 359 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 26.024 -37.946 24.357 1.00 26.03 ? 360 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 36.623 -24.283 27.342 1.00 27.23 ? 361 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 13.817 -24.338 29.269 1.00 29.22 ? 362 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 6.727  -9.248  22.671 1.00 28.55 ? 363 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 10.445 -16.895 15.062 1.00 27.11 ? 364 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 23.868 -8.170  9.493  1.00 19.46 ? 365 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 10.565 -16.803 12.385 1.00 27.51 ? 366 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 29.933 -15.869 30.533 1.00 27.10 ? 367 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 23.656 -33.575 29.075 1.00 26.70 ? 368 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 17.492 -23.909 8.713  1.00 32.07 ? 369 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 22.917 -33.093 5.448  1.00 25.62 ? 370 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 38.276 -25.936 28.368 1.00 29.17 ? 371 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 9.372  -27.494 19.199 1.00 26.59 ? 372 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 14.603 -28.771 25.663 1.00 29.75 ? 373 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 19.239 -27.731 28.175 1.00 16.05 ? 374 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 13.261 -29.654 19.376 1.00 26.33 ? 375 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 28.871 -36.059 7.837  1.00 17.00 ? 376 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 20.216 -19.638 36.109 1.00 28.96 ? 377 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 27.298 -35.567 20.775 1.00 23.12 ? 378 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 29.785 -13.036 13.055 1.00 11.98 ? 379 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 4.214  -10.446 19.637 1.00 26.96 ? 380 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 10.931 -6.423  13.191 1.00 18.52 ? 381 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 34.311 -13.374 25.546 1.00 17.95 ? 382 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 22.918 -8.441  14.086 1.00 13.61 ? 383 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 32.221 -34.550 24.883 1.00 23.63 ? 384 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 23.796 -3.322  18.949 1.00 33.78 ? 385 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 36.201 -28.401 2.987  1.00 34.85 ? 386 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 22.161 -13.716 29.334 1.00 31.35 ? 387 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 33.566 -32.924 0.779  1.00 35.10 ? 388 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 32.979 -9.805  11.195 1.00 12.86 ? 389 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 20.240 -33.854 18.202 1.00 38.27 ? 390 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 33.491 -17.374 4.807  1.00 35.31 ? 391 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 23.239 -25.330 8.933  1.00 17.58 ? 392 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 28.095 -16.309 22.136 1.00 11.19 ? 393 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 29.929 -10.473 27.945 1.00 42.65 ? 394 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 8.801  -13.232 10.804 1.00 18.60 ? 395 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 10.006 -24.859 19.809 1.00 18.57 ? 396 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 42.250 -11.905 14.096 1.00 24.94 ? 397 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 31.221 -6.015  5.925  1.00 35.86 ? 398 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 11.442 -22.552 28.687 1.00 24.95 ? 399 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 31.282 -12.125 10.721 1.00 11.91 ? 400 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 34.560 -23.281 -0.702 1.00 28.49 ? 401 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 3.813  -8.174  14.717 1.00 23.51 ? 402 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 23.064 -28.208 12.646 1.00 16.72 ? 403 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 26.479 -31.163 14.867 1.00 16.23 ? 404 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 37.883 -31.168 26.076 1.00 27.60 ? 405 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 26.724 -12.041 27.755 1.00 22.47 ? 406 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 21.699 -18.893 5.943  1.00 23.85 ? 407 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 22.277 -23.607 6.003  1.00 30.85 ? 408 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 26.060 -30.985 30.908 1.00 15.22 ? 409 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 36.409 -21.188 7.129  1.00 19.91 ? 410 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 20.365 -23.660 34.791 1.00 27.53 ? 411 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 27.091 -19.035 1.757  1.00 22.26 ? 412 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 26.523 -6.006  22.088 1.00 24.38 ? 413 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 39.013 -15.962 4.196  1.00 34.27 ? 414 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 35.817 -28.385 7.831  1.00 16.04 ? 415 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 41.910 -12.532 20.767 1.00 32.72 ? 416 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 31.603 -13.531 4.570  1.00 27.03 ? 417 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 35.613 -24.590 24.719 1.00 14.54 ? 418 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 37.020 -29.130 10.178 1.00 17.58 ? 419 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 17.238 -25.250 12.772 1.00 20.55 ? 420 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 33.050 -30.231 31.762 1.00 16.44 ? 421 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 6.417  -22.811 18.367 1.00 30.58 ? 422 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 6.150  -18.641 25.182 1.00 44.03 ? 423 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 35.229 -13.583 6.137  1.00 30.18 ? 424 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 9.756  -18.472 26.716 1.00 26.10 ? 425 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 4.571  -27.827 23.311 1.00 31.91 ? 426 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 20.268 -32.232 22.263 1.00 28.91 ? 427 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 41.667 -13.614 10.296 1.00 24.78 ? 428 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 34.797 -4.014  17.803 1.00 23.90 ? 429 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 38.828 -12.893 25.913 1.00 23.94 ? 430 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 32.857 -14.284 9.559  1.00 12.79 ? 431 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 38.063 -23.576 4.648  1.00 28.50 ? 432 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 14.762 -18.324 10.375 1.00 29.77 ? 433 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 18.831 -19.144 10.880 1.00 15.52 ? 434 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 36.725 -32.015 25.299 1.00 28.52 ? 435 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 3.992  -12.729 17.275 1.00 33.00 ? 436 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 18.608 -8.330  25.584 1.00 18.54 ? 437 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 10.769 -11.871 8.993  1.00 26.37 ? 438 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 24.416 -13.767 5.587  1.00 31.47 ? 439 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 40.101 -29.797 14.735 1.00 14.96 ? 440 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 33.925 -35.824 8.855  1.00 29.75 ? 441 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 10.523 -30.981 25.510 1.00 30.84 ? 442 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 16.394 -20.491 11.573 1.00 21.35 ? 443 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 30.455 -17.804 8.372  1.00 23.81 ? 444 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 41.721 -12.299 18.159 1.00 23.80 ? 445 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 34.092 -15.477 27.266 1.00 33.91 ? 446 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 37.814 -20.318 4.899  1.00 35.85 ? 447 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 17.015 -31.687 28.659 1.00 46.25 ? 448 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 37.582 -13.742 10.088 1.00 24.68 ? 449 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 23.485 -31.111 13.191 1.00 28.50 ? 450 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 35.199 -22.859 29.117 1.00 23.65 ? 451 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 23.293 -17.594 33.379 1.00 19.85 ? 452 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 6.545  -20.040 18.091 1.00 29.11 ? 453 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 31.836 -15.642 7.074  1.00 28.63 ? 454 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 6.040  -11.989 23.306 1.00 39.95 ? 455 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 24.222 -16.506 3.288  1.00 34.36 ? 456 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 39.679 -14.130 8.461  1.00 24.63 ? 457 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 34.204 -31.775 29.626 1.00 21.59 ? 458 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 8.845  -19.186 16.879 1.00 31.41 ? 459 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 23.725 -15.560 31.488 1.00 28.57 ? 460 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 26.198 -35.220 7.486  1.00 21.24 ? 461 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 21.083 -17.497 34.672 1.00 26.19 ? 462 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 28.294 -12.445 30.084 1.00 42.63 ? 463 HOH   C O   1 
HETATM 2578 O  O   . HOH   I 5 .   ? 22.887 -16.678 5.555  1.00 35.18 ? 464 HOH   C O   1 
HETATM 2579 O  O   . HOH   I 5 .   ? 37.018 -29.102 5.622  1.00 37.30 ? 465 HOH   C O   1 
HETATM 2580 O  O   . HOH   I 5 .   ? 21.496 -26.890 10.296 1.00 32.60 ? 466 HOH   C O   1 
HETATM 2581 O  O   . HOH   I 5 .   ? 16.400 -27.529 14.212 1.00 27.23 ? 467 HOH   C O   1 
HETATM 2582 O  O   . HOH   I 5 .   ? 18.484 -26.023 10.164 1.00 32.50 ? 468 HOH   C O   1 
HETATM 2583 O  O   . HOH   I 5 .   ? 32.438 -19.239 29.219 1.00 26.45 ? 469 HOH   C O   1 
HETATM 2584 O  O   . HOH   I 5 .   ? 10.039 -21.306 16.231 1.00 29.22 ? 470 HOH   C O   1 
HETATM 2585 O  O   . HOH   I 5 .   ? 35.263 -20.163 29.502 1.00 30.83 ? 471 HOH   C O   1 
HETATM 2586 O  O   . HOH   I 5 .   ? 40.772 -28.473 7.798  1.00 44.76 ? 472 HOH   C O   1 
HETATM 2587 O  O   . HOH   I 5 .   ? 22.686 -11.905 6.165  1.00 36.11 ? 473 HOH   C O   1 
HETATM 2588 O  O   . HOH   I 5 .   ? 16.908 -28.820 28.890 1.00 35.82 ? 474 HOH   C O   1 
HETATM 2589 O  O   . HOH   I 5 .   ? 18.130 -17.947 8.344  1.00 29.61 ? 475 HOH   C O   1 
HETATM 2590 O  O   . HOH   I 5 .   ? 38.134 -31.547 5.006  1.00 38.05 ? 476 HOH   C O   1 
HETATM 2591 O  O   . HOH   I 5 .   ? 8.935  -23.562 17.658 1.00 25.07 ? 477 HOH   C O   1 
HETATM 2592 O  O   . HOH   I 5 .   ? 19.027 -29.664 15.058 1.00 33.15 ? 478 HOH   C O   1 
HETATM 2593 O  O   . HOH   I 5 .   ? 18.102 -16.646 38.156 1.00 29.20 ? 479 HOH   C O   1 
HETATM 2594 O  O   . HOH   I 5 .   ? 3.176  -8.511  22.080 1.00 38.69 ? 480 HOH   C O   1 
HETATM 2595 O  O   . HOH   I 5 .   ? 32.998 -17.226 2.211  1.00 36.32 ? 481 HOH   C O   1 
HETATM 2596 O  O   . HOH   I 5 .   ? 19.356 -17.692 5.874  1.00 35.59 ? 482 HOH   C O   1 
HETATM 2597 O  O   . HOH   I 5 .   ? 39.249 -2.701  10.751 1.00 32.34 ? 483 HOH   C O   1 
HETATM 2598 O  O   . HOH   I 5 .   ? 3.281  -9.496  17.045 1.00 29.75 ? 484 HOH   C O   1 
HETATM 2599 O  O   . HOH   I 5 .   ? 36.431 -35.496 8.383  1.00 50.42 ? 485 HOH   C O   1 
HETATM 2600 O  O   . HOH   I 5 .   ? 13.769 -28.218 14.318 1.00 41.27 ? 486 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   ? 0.1661 0.1693 0.1491 -0.0177 -0.0024 -0.0107 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1650 0.1701 0.1532 -0.0155 -0.0055 -0.0079 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1613 0.1670 0.1553 -0.0098 -0.0082 -0.0025 7   SER   A C   
4    O O   . SER   A 1   ? 0.1735 0.1793 0.1662 -0.0086 -0.0087 -0.0003 7   SER   A O   
5    C CB  . SER   A 1   ? 0.1907 0.2025 0.1749 -0.0218 -0.0093 -0.0065 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2298 0.2472 0.2117 -0.0233 -0.0138 -0.0007 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1469 0.1527 0.1469 -0.0070 -0.0092 -0.0009 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1439 0.1498 0.1498 -0.0028 -0.0103 0.0029  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1183 0.1220 0.1293 0.0000  -0.0086 0.0019  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1376 0.1390 0.1481 -0.0001 -0.0064 -0.0010 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1189 0.1233 0.1355 0.0021  -0.0089 0.0044  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1095 0.1124 0.1301 0.0036  -0.0070 0.0032  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1138 0.1155 0.1384 0.0052  -0.0049 0.0041  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1227 0.1246 0.1494 0.0058  -0.0050 0.0064  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1340 0.1397 0.1588 0.0026  -0.0086 0.0040  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1088 0.1092 0.1344 0.0051  -0.0024 0.0024  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1070 0.1061 0.1362 0.0050  0.0011  0.0016  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1032 0.1033 0.1397 0.0051  0.0021  0.0017  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1165 0.1176 0.1522 0.0045  0.0010  0.0010  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1048 0.1036 0.1294 0.0028  0.0034  -0.0005 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1291 0.1281 0.1480 0.0027  0.0022  0.0001  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1235 0.1208 0.1502 0.0007  0.0083  -0.0027 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1345 0.1357 0.1500 0.0002  0.0029  0.0002  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1071 0.1066 0.1519 0.0060  0.0046  0.0028  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1176 0.1180 0.1719 0.0064  0.0066  0.0031  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1226 0.1197 0.1805 0.0048  0.0136  -0.0007 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1391 0.1337 0.2037 0.0054  0.0176  -0.0004 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1280 0.1316 0.1926 0.0086  0.0041  0.0088  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1250 0.1332 0.1848 0.0081  -0.0026 0.0119  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1309 0.1422 0.1907 0.0070  -0.0050 0.0117  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1504 0.1597 0.2045 0.0077  -0.0058 0.0140  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1420 0.1571 0.1959 0.0048  -0.0100 0.0130  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1567 0.1701 0.2046 0.0054  -0.0108 0.0153  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1584 0.1745 0.2062 0.0037  -0.0126 0.0145  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1894 0.2091 0.2301 0.0001  -0.0163 0.0144  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1220 0.1188 0.1748 0.0017  0.0158  -0.0044 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1396 0.1340 0.1930 -0.0021 0.0230  -0.0093 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1381 0.1333 0.1969 -0.0033 0.0256  -0.0109 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1334 0.1312 0.1881 -0.0034 0.0215  -0.0098 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1525 0.1477 0.1931 -0.0067 0.0232  -0.0117 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1698 0.1684 0.2031 -0.0071 0.0176  -0.0095 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1720 0.1658 0.2110 -0.0130 0.0308  -0.0173 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1487 0.1413 0.2178 -0.0042 0.0330  -0.0137 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1560 0.1495 0.2316 -0.0053 0.0361  -0.0154 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1360 0.1334 0.2170 -0.0009 0.0292  -0.0099 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1372 0.1364 0.2246 0.0032  0.0251  -0.0047 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1341 0.1337 0.2112 -0.0027 0.0275  -0.0109 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1263 0.1297 0.2061 0.0001  0.0211  -0.0067 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1239 0.1282 0.1907 -0.0005 0.0150  -0.0058 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1332 0.1395 0.1988 -0.0007 0.0119  -0.0050 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1516 0.1566 0.2391 -0.0009 0.0238  -0.0078 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1878 0.1929 0.2930 0.0011  0.0290  -0.0067 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2259 0.2352 0.3419 0.0045  0.0252  -0.0010 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1775 0.1784 0.2864 -0.0013 0.0379  -0.0117 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1121 0.1151 0.1714 -0.0005 0.0137  -0.0056 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1132 0.1166 0.1630 -0.0005 0.0091  -0.0044 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1158 0.1193 0.1643 0.0019  0.0054  -0.0020 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1204 0.1230 0.1716 0.0030  0.0067  -0.0013 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1242 0.1270 0.1655 -0.0038 0.0109  -0.0060 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1312 0.1350 0.1712 -0.0080 0.0141  -0.0080 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1511 0.1562 0.1919 -0.0082 0.0123  -0.0070 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1652 0.1688 0.2024 -0.0127 0.0193  -0.0113 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1667 0.1732 0.2059 -0.0125 0.0152  -0.0084 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1877 0.1932 0.2222 -0.0180 0.0224  -0.0132 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1952 0.2022 0.2306 -0.0176 0.0200  -0.0113 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2333 0.2426 0.2657 -0.0234 0.0229  -0.0128 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.0997 0.1041 0.1438 0.0022  0.0015  -0.0010 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.0979 0.1023 0.1383 0.0032  -0.0015 0.0004  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.0986 0.1012 0.1322 0.0025  -0.0015 -0.0006 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1111 0.1134 0.1443 0.0017  -0.0015 -0.0010 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1162 0.1238 0.1586 0.0027  -0.0050 0.0019  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1269 0.1348 0.1631 0.0016  -0.0075 0.0020  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1409 0.1536 0.1781 -0.0010 -0.0110 0.0035  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1472 0.1592 0.1772 -0.0041 -0.0114 0.0006  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1562 0.1692 0.1805 -0.0064 -0.0126 0.0005  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1721 0.1870 0.1968 -0.0052 -0.0144 0.0040  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1608 0.1721 0.1791 -0.0101 -0.0112 -0.0036 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1007 0.1023 0.1307 0.0029  -0.0011 -0.0003 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1022 0.1031 0.1283 0.0026  -0.0009 0.0001  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1063 0.1062 0.1301 0.0034  -0.0022 -0.0002 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1133 0.1134 0.1355 0.0038  -0.0030 0.0001  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1102 0.1119 0.1337 0.0015  0.0006  0.0006  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1269 0.1296 0.1490 0.0011  0.0002  0.0028  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1294 0.1320 0.1538 -0.0009 0.0030  -0.0005 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.0965 0.0952 0.1206 0.0030  -0.0018 -0.0009 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.0986 0.0959 0.1203 0.0024  -0.0015 -0.0025 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1185 0.1159 0.1401 0.0024  -0.0016 -0.0025 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1030 0.0982 0.1270 0.0030  0.0012  -0.0025 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1175 0.1129 0.1458 0.0037  0.0021  -0.0002 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.0968 0.0947 0.1176 -0.0001 -0.0023 -0.0048 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1552 0.1533 0.1764 0.0000  -0.0026 -0.0046 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1177 0.1193 0.1378 -0.0008 -0.0056 -0.0032 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1575 0.1553 0.1743 -0.0029 -0.0021 -0.0072 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0641 0.0607 0.0887 -0.0007 -0.0009 -0.0058 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.1927 0.1943 0.2155 -0.0001 -0.0054 -0.0028 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1053 0.0987 0.1276 0.0023  0.0029  -0.0044 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1111 0.1018 0.1389 0.0029  0.0069  -0.0045 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1145 0.1027 0.1463 0.0016  0.0093  -0.0066 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1189 0.1067 0.1467 -0.0014 0.0090  -0.0103 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1170 0.1054 0.1423 0.0015  0.0097  -0.0079 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1181 0.1086 0.1398 0.0026  0.0079  -0.0061 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1256 0.1177 0.1407 0.0014  0.0050  -0.0067 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1279 0.1190 0.1549 0.0048  0.0093  -0.0030 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1171 0.1041 0.1574 0.0033  0.0117  -0.0035 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1200 0.1040 0.1655 0.0021  0.0146  -0.0052 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1335 0.1129 0.1778 -0.0012 0.0195  -0.0120 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1469 0.1250 0.1890 -0.0045 0.0203  -0.0160 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1231 0.1068 0.1800 0.0046  0.0168  0.0006  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1247 0.1052 0.1883 0.0037  0.0199  0.0000  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1404 0.1214 0.2174 0.0063  0.0221  0.0077  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1500 0.1283 0.2348 0.0058  0.0248  0.0088  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.1580 0.1293 0.2511 0.0050  0.0319  0.0049  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.1822 0.1486 0.2752 0.0038  0.0373  -0.0017 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.1744 0.1433 0.2758 0.0048  0.0344  0.0071  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1305 0.1078 0.1755 -0.0013 0.0230  -0.0139 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1525 0.1251 0.1959 -0.0061 0.0292  -0.0216 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.1617 0.1371 0.1918 -0.0117 0.0260  -0.0265 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.1941 0.1670 0.2204 -0.0178 0.0308  -0.0334 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.1655 0.1346 0.2148 -0.0052 0.0354  -0.0229 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1645 0.1371 0.2057 -0.0051 0.0319  -0.0223 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1590 0.1358 0.2018 -0.0004 0.0272  -0.0154 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.1772 0.1498 0.2085 -0.0099 0.0329  -0.0279 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.1722 0.1506 0.2070 -0.0018 0.0258  -0.0172 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.1833 0.1594 0.2111 -0.0073 0.0289  -0.0242 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1552 0.1364 0.1787 -0.0104 0.0185  -0.0226 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1513 0.1372 0.1647 -0.0151 0.0141  -0.0242 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1580 0.1477 0.1713 -0.0155 0.0095  -0.0221 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.1739 0.1691 0.1815 -0.0191 0.0051  -0.0214 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1522 0.1417 0.1604 -0.0139 0.0101  -0.0212 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.1609 0.1474 0.1680 -0.0146 0.0145  -0.0238 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.1720 0.1623 0.1739 -0.0132 0.0100  -0.0201 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.1933 0.1779 0.1949 -0.0224 0.0197  -0.0313 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1514 0.1390 0.1721 -0.0121 0.0105  -0.0202 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1456 0.1366 0.1671 -0.0123 0.0068  -0.0183 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1574 0.1501 0.1748 -0.0191 0.0073  -0.0228 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1672 0.1555 0.1840 -0.0231 0.0129  -0.0284 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1512 0.1394 0.1806 -0.0086 0.0086  -0.0160 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1530 0.1522 0.1685 -0.0207 0.0019  -0.0203 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1518 0.1553 0.1631 -0.0282 0.0010  -0.0234 24  THR   A CA  
140  C C   . THR   A 18  ? 0.1562 0.1579 0.1728 -0.0283 0.0026  -0.0246 24  THR   A C   
141  O O   . THR   A 18  ? 0.1469 0.1453 0.1702 -0.0225 0.0035  -0.0221 24  THR   A O   
142  C CB  . THR   A 18  ? 0.1738 0.1869 0.1830 -0.0298 -0.0063 -0.0180 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.1646 0.1792 0.1817 -0.0239 -0.0090 -0.0130 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.1932 0.2086 0.1981 -0.0294 -0.0085 -0.0154 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.1587 0.1639 0.1719 -0.0357 0.0025  -0.0280 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.1621 0.1666 0.1801 -0.0363 0.0036  -0.0289 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.1533 0.1625 0.1773 -0.0308 -0.0017 -0.0223 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1510 0.1566 0.1809 -0.0270 0.0001  -0.0215 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.1701 0.1797 0.1824 -0.0465 0.0034  -0.0333 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.2317 0.2434 0.2490 -0.0473 0.0024  -0.0327 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.2649 0.2683 0.2877 -0.0456 0.0084  -0.0361 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.2645 0.2856 0.2844 -0.0478 -0.0040 -0.0276 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.2687 0.2766 0.2945 -0.0471 0.0058  -0.0346 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.2803 0.2990 0.3053 -0.0478 -0.0017 -0.0293 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1484 0.1654 0.1718 -0.0302 -0.0076 -0.0171 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1454 0.1660 0.1765 -0.0251 -0.0109 -0.0116 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1320 0.1458 0.1666 -0.0180 -0.0081 -0.0106 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1361 0.1494 0.1763 -0.0152 -0.0075 -0.0092 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.1688 0.1981 0.2015 -0.0254 -0.0165 -0.0055 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2351 0.2677 0.2785 -0.0207 -0.0182 -0.0005 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.2815 0.3184 0.3298 -0.0227 -0.0193 0.0003  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.2478 0.2781 0.2954 -0.0150 -0.0175 0.0023  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1317 0.1412 0.1628 -0.0160 -0.0063 -0.0114 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1149 0.1195 0.1488 -0.0108 -0.0039 -0.0101 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1120 0.1122 0.1493 -0.0104 -0.0004 -0.0115 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1248 0.1247 0.1656 -0.0079 -0.0001 -0.0091 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1281 0.1295 0.1583 -0.0093 -0.0025 -0.0105 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1303 0.1352 0.1579 -0.0086 -0.0057 -0.0081 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1423 0.1505 0.1735 -0.0066 -0.0079 -0.0048 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1388 0.1430 0.1615 -0.0103 -0.0051 -0.0097 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1171 0.1136 0.1535 -0.0135 0.0029  -0.0153 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1230 0.1149 0.1647 -0.0131 0.0069  -0.0159 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1163 0.1110 0.1606 -0.0143 0.0054  -0.0154 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1265 0.1190 0.1753 -0.0126 0.0071  -0.0133 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1226 0.1093 0.1643 -0.0169 0.0122  -0.0211 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1268 0.1090 0.1702 -0.0146 0.0157  -0.0209 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1475 0.1288 0.1860 -0.0167 0.0171  -0.0242 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1221 0.1006 0.1735 -0.0101 0.0185  -0.0166 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1436 0.1205 0.1875 -0.0133 0.0210  -0.0228 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1316 0.1073 0.1840 -0.0092 0.0215  -0.0174 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1428 0.1212 0.2011 -0.0075 0.0185  -0.0114 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.1529 0.1262 0.2145 -0.0051 0.0243  -0.0124 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.1536 0.1304 0.2196 -0.0041 0.0205  -0.0059 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.1583 0.1326 0.2270 -0.0028 0.0235  -0.0063 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1157 0.1161 0.1579 -0.0175 0.0021  -0.0163 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1257 0.1296 0.1715 -0.0187 0.0007  -0.0156 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1313 0.1381 0.1811 -0.0147 -0.0012 -0.0115 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1445 0.1535 0.1985 -0.0151 -0.0013 -0.0109 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1523 0.1628 0.1959 -0.0242 -0.0023 -0.0171 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1240 0.1307 0.1725 -0.0114 -0.0020 -0.0093 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1243 0.1329 0.1762 -0.0086 -0.0023 -0.0067 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1218 0.1266 0.1711 -0.0064 -0.0003 -0.0057 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1285 0.1341 0.1772 -0.0047 -0.0004 -0.0045 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1393 0.1529 0.1936 -0.0077 -0.0051 -0.0046 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1492 0.1688 0.2080 -0.0104 -0.0077 -0.0037 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.1861 0.2081 0.2517 -0.0101 -0.0069 -0.0029 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.1624 0.1854 0.2177 -0.0140 -0.0105 -0.0040 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1266 0.1277 0.1751 -0.0067 0.0016  -0.0057 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1119 0.1110 0.1590 -0.0052 0.0028  -0.0033 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1260 0.1272 0.1730 -0.0056 0.0033  -0.0009 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1523 0.1544 0.2014 -0.0073 0.0042  -0.0006 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1231 0.1184 0.1731 -0.0055 0.0051  -0.0028 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1233 0.1177 0.1748 -0.0039 0.0061  0.0015  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1375 0.1315 0.1857 -0.0024 0.0054  0.0007  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1644 0.1549 0.2229 -0.0039 0.0094  0.0033  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1147 0.1170 0.1587 -0.0051 0.0031  0.0006  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1253 0.1302 0.1672 -0.0074 0.0040  0.0026  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1216 0.1275 0.1633 -0.0080 0.0036  0.0077  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1419 0.1507 0.1840 -0.0109 0.0039  0.0112  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1213 0.1275 0.1604 -0.0077 0.0048  0.0006  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1602 0.1694 0.1951 -0.0120 0.0066  0.0017  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1384 0.1443 0.1815 -0.0067 0.0055  -0.0026 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1277 0.1323 0.1697 -0.0057 0.0029  0.0089  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1265 0.1332 0.1709 -0.0059 0.0025  0.0149  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1258 0.1291 0.1732 -0.0026 0.0030  0.0144  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1248 0.1261 0.1685 -0.0013 0.0028  0.0099  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1430 0.1554 0.1816 -0.0093 0.0014  0.0172  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1540 0.1708 0.1950 -0.0099 0.0000  0.0243  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1798 0.2019 0.2248 -0.0125 -0.0012 0.0324  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1435 0.1608 0.1836 -0.0083 -0.0007 0.0250  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.1892 0.2159 0.2372 -0.0125 -0.0028 0.0386  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1638 0.1874 0.2083 -0.0100 -0.0024 0.0337  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1489 0.1628 0.1854 -0.0060 -0.0003 0.0198  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.1789 0.2053 0.2243 -0.0093 -0.0034 0.0367  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1668 0.1829 0.2031 -0.0055 -0.0011 0.0223  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.1794 0.2014 0.2206 -0.0068 -0.0025 0.0303  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1230 0.1258 0.1778 -0.0014 0.0042  0.0192  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1325 0.1319 0.1912 0.0013  0.0060  0.0184  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1341 0.1366 0.2022 0.0022  0.0065  0.0270  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1394 0.1450 0.2135 0.0010  0.0061  0.0336  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1545 0.1473 0.2162 0.0021  0.0094  0.0127  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1577 0.1479 0.2274 0.0016  0.0121  0.0145  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.1516 0.1400 0.2349 0.0034  0.0158  0.0205  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.1735 0.1618 0.2645 0.0030  0.0170  0.0252  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1578 0.1444 0.2457 0.0052  0.0183  0.0208  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1288 0.1312 0.1990 0.0040  0.0072  0.0277  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1289 0.1351 0.2104 0.0052  0.0077  0.0367  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1268 0.1281 0.2145 0.0082  0.0118  0.0341  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1309 0.1328 0.2116 0.0084  0.0108  0.0307  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1582 0.1741 0.2344 0.0022  0.0029  0.0429  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.1789 0.2021 0.2669 0.0023  0.0018  0.0545  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.1897 0.2097 0.2892 0.0061  0.0053  0.0561  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2299 0.2626 0.3155 -0.0019 -0.0023 0.0619  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1239 0.1202 0.2255 0.0103  0.0174  0.0353  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1244 0.1150 0.2334 0.0124  0.0233  0.0318  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.1418 0.1324 0.2501 0.0123  0.0231  0.0314  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1369 0.1331 0.2521 0.0141  0.0221  0.0385  36  SER   A C   
248  O O   . SER   A 30  ? 0.1509 0.1444 0.2632 0.0147  0.0244  0.0334  36  SER   A O   
249  C CB  A SER   A 30  ? 0.1277 0.1115 0.2528 0.0137  0.0308  0.0322  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.1918 0.1747 0.3144 0.0134  0.0309  0.0302  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.1109 0.0886 0.2441 0.0150  0.0381  0.0278  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2654 0.2524 0.4033 0.0149  0.0307  0.0417  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1423 0.1474 0.2654 0.0141  0.0184  0.0504  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1367 0.1492 0.2667 0.0150  0.0166  0.0584  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1327 0.1484 0.2457 0.0129  0.0122  0.0535  37  SER   A C   
256  O O   . SER   A 31  ? 0.1524 0.1714 0.2692 0.0139  0.0123  0.0561  37  SER   A O   
257  C CB  . SER   A 31  ? 0.1778 0.2016 0.3183 0.0137  0.0122  0.0733  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2116 0.2435 0.3372 0.0087  0.0051  0.0752  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1193 0.1338 0.2152 0.0102  0.0090  0.0466  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1240 0.1403 0.2050 0.0083  0.0058  0.0415  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1274 0.1351 0.2004 0.0095  0.0085  0.0306  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1273 0.1357 0.1897 0.0084  0.0065  0.0267  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1349 0.1562 0.2041 0.0041  0.0012  0.0417  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1587 0.1909 0.2324 0.0005  -0.0024 0.0527  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1473 0.1839 0.2086 -0.0050 -0.0055 0.0513  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1286 0.1655 0.1772 -0.0076 -0.0063 0.0450  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1320 0.1749 0.1707 -0.0141 -0.0081 0.0450  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1598 0.2101 0.1984 -0.0192 -0.0101 0.0510  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1513 0.1933 0.1805 -0.0162 -0.0076 0.0390  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1321 0.1325 0.2088 0.0107  0.0129  0.0256  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1242 0.1183 0.1920 0.0099  0.0147  0.0159  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1149 0.1105 0.1695 0.0080  0.0101  0.0125  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1219 0.1159 0.1680 0.0072  0.0093  0.0075  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1293 0.1213 0.1958 0.0105  0.0173  0.0125  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1311 0.1179 0.1882 0.0083  0.0191  0.0034  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1325 0.1152 0.1901 0.0066  0.0217  -0.0010 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1516 0.1389 0.2010 0.0075  0.0180  0.0006  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1123 0.1109 0.1665 0.0069  0.0076  0.0155  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1110 0.1106 0.1555 0.0052  0.0046  0.0122  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1087 0.1063 0.1540 0.0044  0.0050  0.0102  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1154 0.1129 0.1678 0.0045  0.0063  0.0137  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1117 0.1174 0.1530 0.0033  0.0018  0.0165  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1321 0.1406 0.1693 0.0029  0.0007  0.0171  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1413 0.1560 0.1741 -0.0010 -0.0013 0.0202  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1336 0.1383 0.1644 0.0037  0.0009  0.0112  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1034 0.1002 0.1424 0.0035  0.0036  0.0057  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1008 0.0970 0.1401 0.0023  0.0034  0.0040  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.0981 0.0965 0.1325 0.0016  0.0012  0.0024  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1059 0.1045 0.1368 0.0021  0.0003  0.0010  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1083 0.1006 0.1487 0.0016  0.0054  -0.0003 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1157 0.1078 0.1569 -0.0001 0.0052  -0.0023 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1421 0.1297 0.1872 -0.0016 0.0091  -0.0053 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1182 0.1128 0.1545 -0.0013 0.0023  -0.0047 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.0998 0.0998 0.1350 0.0004  0.0011  0.0029  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.0991 0.1007 0.1327 -0.0004 0.0006  0.0012  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.0971 0.0986 0.1337 -0.0009 0.0005  -0.0005 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1101 0.1112 0.1488 -0.0019 0.0013  0.0004  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1053 0.1095 0.1370 -0.0026 0.0017  0.0027  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1222 0.1268 0.1544 -0.0036 0.0032  -0.0001 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1143 0.1198 0.1428 -0.0029 0.0013  0.0047  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.0980 0.1004 0.1357 -0.0005 -0.0006 -0.0019 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1001 0.1040 0.1416 -0.0013 -0.0011 -0.0028 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1071 0.1131 0.1530 -0.0009 -0.0002 -0.0025 43  SER   A C   
304  O O   . SER   A 37  ? 0.1134 0.1191 0.1591 -0.0002 0.0010  -0.0023 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1143 0.1192 0.1552 -0.0022 -0.0033 -0.0036 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1237 0.1303 0.1634 -0.0015 -0.0052 -0.0024 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1196 0.1275 0.1707 -0.0017 0.0001  -0.0028 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1259 0.1356 0.1844 -0.0012 0.0023  -0.0026 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1441 0.1575 0.2091 0.0002  -0.0004 0.0002  44  SER   A C   
310  O O   . SER   A 38  ? 0.1747 0.1909 0.2382 -0.0008 -0.0044 0.0016  44  SER   A O   
311  C CB  . SER   A 38  ? 0.1482 0.1589 0.2108 -0.0028 0.0043  -0.0038 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.1841 0.1969 0.2480 -0.0035 0.0013  -0.0032 44  SER   A OG  
313  N N   . THR   A 39  ? 0.1453 0.1592 0.2183 0.0018  0.0021  0.0015  45  THR   A N   
314  C CA  . THR   A 39  ? 0.1647 0.1832 0.2468 0.0033  -0.0006 0.0064  45  THR   A CA  
315  C C   . THR   A 39  ? 0.1836 0.2049 0.2808 0.0044  0.0025  0.0082  45  THR   A C   
316  O O   . THR   A 39  ? 0.1742 0.1919 0.2745 0.0041  0.0086  0.0045  45  THR   A O   
317  C CB  . THR   A 39  ? 0.1702 0.1868 0.2520 0.0051  0.0000  0.0080  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.1778 0.1901 0.2636 0.0057  0.0066  0.0051  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.1807 0.1948 0.2492 0.0043  -0.0023 0.0062  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.1976 0.2258 0.3050 0.0050  -0.0014 0.0144  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2142 0.2460 0.3397 0.0066  0.0016  0.0178  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2120 0.2407 0.3489 0.0096  0.0071  0.0195  46  THR   A C   
323  O O   . THR   A 40  ? 0.2325 0.2579 0.3800 0.0105  0.0148  0.0167  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2670 0.3093 0.4000 0.0054  -0.0052 0.0250  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3257 0.3724 0.4570 0.0051  -0.0108 0.0309  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2822 0.3261 0.4042 0.0017  -0.0088 0.0217  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2142 0.2432 0.3484 0.0107  0.0041  0.0231  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2230 0.2484 0.3680 0.0134  0.0096  0.0247  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.1990 0.2150 0.3316 0.0123  0.0153  0.0164  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.1997 0.2140 0.3147 0.0103  0.0119  0.0128  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2529 0.2838 0.4016 0.0146  0.0035  0.0334  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.1785 0.1891 0.3206 0.0131  0.0239  0.0139  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.1952 0.1982 0.3261 0.0108  0.0296  0.0065  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.1872 0.1893 0.3133 0.0121  0.0264  0.0096  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.1969 0.2018 0.3356 0.0151  0.0247  0.0169  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2335 0.2308 0.3764 0.0096  0.0415  0.0014  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3156 0.3126 0.4600 0.0067  0.0465  -0.0040 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4004 0.3912 0.5566 0.0046  0.0596  -0.0100 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.3960 0.3865 0.5746 0.0081  0.0648  -0.0061 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4193 0.4055 0.5616 -0.0017 0.0656  -0.0192 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1609 0.1602 0.2693 0.0097  0.0250  0.0050  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1605 0.1587 0.2622 0.0104  0.0222  0.0069  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1537 0.1458 0.2589 0.0094  0.0303  0.0033  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1686 0.1565 0.2770 0.0067  0.0388  -0.0028 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1452 0.1366 0.2468 0.0105  0.0278  0.0061  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1436 0.1291 0.2490 0.0096  0.0353  0.0032  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1395 0.1225 0.2276 0.0058  0.0355  -0.0024 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1504 0.1286 0.2398 0.0037  0.0422  -0.0059 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1686 0.1551 0.2873 0.0136  0.0338  0.0115  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.1898 0.1800 0.3344 0.0177  0.0352  0.0198  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1340 0.1206 0.2075 0.0049  0.0284  -0.0024 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1379 0.1237 0.1973 0.0015  0.0281  -0.0061 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1500 0.1344 0.2039 -0.0044 0.0343  -0.0130 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.1722 0.1576 0.2283 -0.0056 0.0357  -0.0147 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1294 0.1193 0.1778 0.0024  0.0198  -0.0037 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1401 0.1319 0.1904 0.0060  0.0142  0.0020  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1494 0.1393 0.2037 0.0070  0.0158  0.0039  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1415 0.1367 0.1887 0.0070  0.0087  0.0042  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1631 0.1462 0.2093 -0.0089 0.0375  -0.0168 52  THR   A N   
360  C CA  . THR   A 46  ? 0.1828 0.1668 0.2202 -0.0168 0.0422  -0.0229 52  THR   A CA  
361  C C   . THR   A 46  ? 0.1692 0.1584 0.1927 -0.0195 0.0362  -0.0213 52  THR   A C   
362  O O   . THR   A 46  ? 0.1865 0.1760 0.2076 -0.0169 0.0324  -0.0184 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2536 0.2325 0.2947 -0.0219 0.0528  -0.0294 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.2983 0.2753 0.3380 -0.0209 0.0524  -0.0283 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.2722 0.2458 0.3308 -0.0189 0.0600  -0.0304 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1647 0.1586 0.1803 -0.0248 0.0352  -0.0223 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1526 0.1529 0.1583 -0.0274 0.0294  -0.0190 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1561 0.1590 0.1532 -0.0361 0.0331  -0.0224 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.1750 0.1778 0.1692 -0.0440 0.0400  -0.0282 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1574 0.1629 0.1602 -0.0286 0.0254  -0.0160 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1627 0.1655 0.1736 -0.0212 0.0226  -0.0137 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1588 0.1713 0.1554 -0.0299 0.0192  -0.0104 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1677 0.1689 0.1820 -0.0136 0.0173  -0.0096 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1436 0.1497 0.1362 -0.0359 0.0291  -0.0193 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1450 0.1559 0.1287 -0.0449 0.0312  -0.0213 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1512 0.1721 0.1269 -0.0530 0.0284  -0.0187 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1459 0.1711 0.1233 -0.0494 0.0222  -0.0123 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1472 0.1604 0.1296 -0.0416 0.0262  -0.0169 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.1740 0.1989 0.1411 -0.0648 0.0334  -0.0235 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.1872 0.2238 0.1454 -0.0748 0.0304  -0.0201 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2027 0.2471 0.1519 -0.0843 0.0301  -0.0199 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2200 0.2641 0.1617 -0.0951 0.0377  -0.0279 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2204 0.2559 0.1753 -0.0824 0.0371  -0.0266 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2126 0.2401 0.1777 -0.0729 0.0380  -0.0272 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.1959 0.2277 0.1649 -0.0660 0.0290  -0.0179 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.1835 0.2081 0.1614 -0.0582 0.0303  -0.0193 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.1802 0.2050 0.1639 -0.0501 0.0240  -0.0131 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.1748 0.2058 0.1578 -0.0482 0.0169  -0.0051 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2101 0.2289 0.2015 -0.0439 0.0253  -0.0147 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.1980 0.2498 0.1483 -0.0811 0.0220  -0.0108 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.1945 0.2529 0.1394 -0.0868 0.0207  -0.0094 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.1951 0.2631 0.1447 -0.0823 0.0112  0.0026  56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2074 0.2752 0.1651 -0.0739 0.0064  0.0092  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.1964 0.2430 0.1448 -0.0813 0.0261  -0.0163 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.1793 0.2182 0.1400 -0.0641 0.0208  -0.0108 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2126 0.2885 0.1583 -0.0879 0.0093  0.0052  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.2273 0.3119 0.1797 -0.0834 0.0015  0.0164  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.2113 0.2897 0.1666 -0.0776 0.0029  0.0137  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.2177 0.3049 0.1757 -0.0781 -0.0016 0.0208  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.2831 0.3869 0.2308 -0.0956 -0.0039 0.0256  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.3518 0.4619 0.2873 -0.1091 -0.0008 0.0204  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.3650 0.4633 0.2961 -0.1092 0.0068  0.0088  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.4045 0.5321 0.3353 -0.1205 -0.0058 0.0285  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.1852 0.2486 0.1417 -0.0711 0.0087  0.0048  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.1810 0.2385 0.1405 -0.0652 0.0095  0.0033  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.1720 0.2323 0.1408 -0.0562 0.0035  0.0118  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.1752 0.2351 0.1507 -0.0501 0.0005  0.0163  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.1852 0.2275 0.1475 -0.0584 0.0153  -0.0046 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2092 0.2449 0.1649 -0.0676 0.0254  -0.0160 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.1564 0.2183 0.1260 -0.0555 0.0028  0.0130  59  GLN   A N   
411  C CA  A GLN   A 53  ? 0.1421 0.2050 0.1208 -0.0473 -0.0009 0.0192  59  GLN   A CA  
412  C CA  B GLN   A 53  ? 0.1556 0.2183 0.1344 -0.0472 -0.0009 0.0192  59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.1345 0.1872 0.1136 -0.0415 0.0021  0.0142  59  GLN   A C   
414  O O   . GLN   A 53  ? 0.1437 0.1976 0.1286 -0.0368 0.0003  0.0179  59  GLN   A O   
415  C CB  A GLN   A 53  ? 0.1441 0.2219 0.1265 -0.0518 -0.0057 0.0287  59  GLN   A CB  
416  C CB  B GLN   A 53  ? 0.1910 0.2694 0.1734 -0.0521 -0.0060 0.0292  59  GLN   A CB  
417  C CG  A GLN   A 53  ? 0.1378 0.2266 0.1248 -0.0545 -0.0103 0.0377  59  GLN   A CG  
418  C CG  B GLN   A 53  ? 0.2354 0.3243 0.2182 -0.0577 -0.0096 0.0358  59  GLN   A CG  
419  C CD  A GLN   A 53  ? 0.1462 0.2508 0.1406 -0.0579 -0.0156 0.0494  59  GLN   A CD  
420  C CD  B GLN   A 53  ? 0.3115 0.3935 0.3007 -0.0500 -0.0098 0.0365  59  GLN   A CD  
421  O OE1 A GLN   A 53  ? 0.1827 0.3013 0.1716 -0.0692 -0.0184 0.0540  59  GLN   A OE1 
422  O OE1 B GLN   A 53  ? 0.3132 0.3872 0.3106 -0.0401 -0.0093 0.0364  59  GLN   A OE1 
423  N NE2 A GLN   A 53  ? 0.1087 0.2124 0.1161 -0.0493 -0.0166 0.0546  59  GLN   A NE2 
424  N NE2 B GLN   A 53  ? 0.3465 0.4314 0.3315 -0.0551 -0.0101 0.0367  59  GLN   A NE2 
425  N N   . THR   A 54  ? 0.1300 0.1732 0.1040 -0.0424 0.0072  0.0060  60  THR   A N   
426  C CA  . THR   A 54  ? 0.1373 0.1706 0.1127 -0.0367 0.0098  0.0023  60  THR   A CA  
427  C C   . THR   A 54  ? 0.1252 0.1482 0.1022 -0.0325 0.0129  -0.0021 60  THR   A C   
428  O O   . THR   A 54  ? 0.1489 0.1709 0.1237 -0.0365 0.0157  -0.0054 60  THR   A O   
429  C CB  . THR   A 54  ? 0.1787 0.2117 0.1492 -0.0420 0.0131  -0.0012 60  THR   A CB  
430  O OG1 . THR   A 54  ? 0.2619 0.2925 0.2270 -0.0492 0.0183  -0.0074 60  THR   A OG1 
431  C CG2 . THR   A 54  ? 0.1719 0.2163 0.1413 -0.0469 0.0099  0.0035  60  THR   A CG2 
432  N N   . GLY   A 55  ? 0.1283 0.1445 0.1093 -0.0249 0.0124  -0.0018 61  GLY   A N   
433  C CA  . GLY   A 55  ? 0.1240 0.1322 0.1082 -0.0207 0.0143  -0.0042 61  GLY   A CA  
434  C C   . GLY   A 55  ? 0.1067 0.1100 0.0938 -0.0144 0.0129  -0.0027 61  GLY   A C   
435  O O   . GLY   A 55  ? 0.1163 0.1205 0.1020 -0.0140 0.0122  -0.0016 61  GLY   A O   
436  N N   . VAL   A 56  ? 0.1088 0.1077 0.0995 -0.0101 0.0124  -0.0025 62  VAL   A N   
437  C CA  . VAL   A 56  ? 0.0993 0.0947 0.0919 -0.0057 0.0108  -0.0007 62  VAL   A CA  
438  C C   . VAL   A 56  ? 0.1015 0.0974 0.0963 -0.0025 0.0079  0.0008  62  VAL   A C   
439  O O   . VAL   A 56  ? 0.1120 0.1076 0.1091 -0.0025 0.0082  0.0002  62  VAL   A O   
440  C CB  . VAL   A 56  ? 0.1173 0.1072 0.1136 -0.0053 0.0140  -0.0012 62  VAL   A CB  
441  C CG1 . VAL   A 56  ? 0.1437 0.1318 0.1422 -0.0017 0.0115  0.0023  62  VAL   A CG1 
442  C CG2 . VAL   A 56  ? 0.1301 0.1185 0.1245 -0.0089 0.0180  -0.0035 62  VAL   A CG2 
443  N N   . TYR   A 57  ? 0.1002 0.0967 0.0940 -0.0004 0.0056  0.0022  63  TYR   A N   
444  C CA  . TYR   A 57  ? 0.0972 0.0937 0.0924 0.0015  0.0035  0.0028  63  TYR   A CA  
445  C C   . TYR   A 57  ? 0.1099 0.1050 0.1041 0.0023  0.0020  0.0040  63  TYR   A C   
446  O O   . TYR   A 57  ? 0.1206 0.1152 0.1122 0.0016  0.0022  0.0047  63  TYR   A O   
447  C CB  . TYR   A 57  ? 0.1097 0.1088 0.1056 0.0019  0.0029  0.0028  63  TYR   A CB  
448  C CG  . TYR   A 57  ? 0.1032 0.1024 0.0978 0.0022  0.0035  0.0025  63  TYR   A CG  
449  C CD1 . TYR   A 57  ? 0.1169 0.1174 0.1104 0.0013  0.0046  0.0028  63  TYR   A CD1 
450  C CD2 . TYR   A 57  ? 0.1164 0.1144 0.1107 0.0025  0.0035  0.0012  63  TYR   A CD2 
451  C CE1 . TYR   A 57  ? 0.1287 0.1291 0.1216 0.0013  0.0059  0.0021  63  TYR   A CE1 
452  C CE2 . TYR   A 57  ? 0.1281 0.1257 0.1212 0.0017  0.0055  -0.0003 63  TYR   A CE2 
453  C CZ  . TYR   A 57  ? 0.1351 0.1338 0.1279 0.0014  0.0068  0.0002  63  TYR   A CZ  
454  O OH  . TYR   A 57  ? 0.1728 0.1710 0.1650 0.0004  0.0095  -0.0016 63  TYR   A OH  
455  N N   . TYR   A 58  ? 0.1022 0.0976 0.0978 0.0029  0.0002  0.0046  64  TYR   A N   
456  C CA  . TYR   A 58  ? 0.1085 0.1049 0.1022 0.0019  -0.0021 0.0065  64  TYR   A CA  
457  C C   . TYR   A 58  ? 0.1070 0.1043 0.0963 0.0002  -0.0020 0.0040  64  TYR   A C   
458  O O   . TYR   A 58  ? 0.1087 0.1059 0.0994 0.0005  -0.0014 0.0019  64  TYR   A O   
459  C CB  . TYR   A 58  ? 0.1181 0.1157 0.1165 0.0024  -0.0041 0.0091  64  TYR   A CB  
460  C CG  . TYR   A 58  ? 0.1221 0.1230 0.1182 0.0000  -0.0074 0.0126  64  TYR   A CG  
461  C CD1 . TYR   A 58  ? 0.1297 0.1312 0.1253 -0.0008 -0.0081 0.0164  64  TYR   A CD1 
462  C CD2 . TYR   A 58  ? 0.1320 0.1359 0.1257 -0.0024 -0.0096 0.0122  64  TYR   A CD2 
463  C CE1 . TYR   A 58  ? 0.1508 0.1571 0.1435 -0.0044 -0.0117 0.0206  64  TYR   A CE1 
464  C CE2 . TYR   A 58  ? 0.1486 0.1573 0.1386 -0.0065 -0.0129 0.0156  64  TYR   A CE2 
465  C CZ  . TYR   A 58  ? 0.1408 0.1511 0.1302 -0.0076 -0.0143 0.0202  64  TYR   A CZ  
466  O OH  . TYR   A 58  ? 0.1805 0.1972 0.1655 -0.0129 -0.0181 0.0247  64  TYR   A OH  
467  N N   . CYS   A 59  ? 0.1133 0.1112 0.0976 -0.0021 -0.0021 0.0042  65  CYS   A N   
468  C CA  . CYS   A 59  ? 0.1199 0.1181 0.0995 -0.0051 -0.0004 0.0007  65  CYS   A CA  
469  C C   . CYS   A 59  ? 0.1250 0.1263 0.0992 -0.0098 -0.0030 0.0020  65  CYS   A C   
470  O O   . CYS   A 59  ? 0.1340 0.1374 0.1043 -0.0122 -0.0046 0.0049  65  CYS   A O   
471  C CB  . CYS   A 59  ? 0.1256 0.1228 0.1031 -0.0055 0.0024  -0.0008 65  CYS   A CB  
472  S SG  . CYS   A 59  ? 0.1401 0.1368 0.1131 -0.0099 0.0066  -0.0062 65  CYS   A SG  
473  N N   . SER   A 60  ? 0.1257 0.1283 0.0995 -0.0118 -0.0037 0.0005  66  SER   A N   
474  C CA  . SER   A 60  ? 0.1446 0.1523 0.1130 -0.0176 -0.0070 0.0026  66  SER   A CA  
475  C C   . SER   A 60  ? 0.1366 0.1458 0.0956 -0.0242 -0.0051 -0.0004 66  SER   A C   
476  O O   . SER   A 60  ? 0.1606 0.1755 0.1139 -0.0296 -0.0087 0.0036  66  SER   A O   
477  C CB  . SER   A 60  ? 0.1703 0.1794 0.1402 -0.0189 -0.0079 0.0011  66  SER   A CB  
478  O OG  . SER   A 60  ? 0.1963 0.2024 0.1637 -0.0214 -0.0031 -0.0060 66  SER   A OG  
479  N N   . SER   A 61  ? 0.1341 0.1388 0.0922 -0.0242 0.0008  -0.0069 67  SER   A N   
480  C CA  . SER   A 61  ? 0.1413 0.1465 0.0911 -0.0309 0.0045  -0.0113 67  SER   A CA  
481  C C   . SER   A 61  ? 0.1382 0.1445 0.0846 -0.0311 0.0033  -0.0078 67  SER   A C   
482  O O   . SER   A 61  ? 0.1505 0.1580 0.0889 -0.0375 0.0059  -0.0108 67  SER   A O   
483  C CB  . SER   A 61  ? 0.1607 0.1604 0.1134 -0.0309 0.0125  -0.0193 67  SER   A CB  
484  O OG  . SER   A 61  ? 0.1598 0.1560 0.1210 -0.0237 0.0145  -0.0183 67  SER   A OG  
485  N N   . ARG   A 62  ? 0.1423 0.1485 0.0946 -0.0251 -0.0003 -0.0017 68  ARG   A N   
486  C CA  . ARG   A 62  ? 0.1454 0.1527 0.0956 -0.0253 -0.0018 0.0026  68  ARG   A CA  
487  C C   . ARG   A 62  ? 0.1552 0.1662 0.1092 -0.0239 -0.0077 0.0114  68  ARG   A C   
488  O O   . ARG   A 62  ? 0.1629 0.1745 0.1172 -0.0236 -0.0090 0.0162  68  ARG   A O   
489  C CB  . ARG   A 62  ? 0.1499 0.1525 0.1056 -0.0195 0.0016  0.0009  68  ARG   A CB  
490  C CG  . ARG   A 62  ? 0.1548 0.1546 0.1097 -0.0206 0.0077  -0.0059 68  ARG   A CG  
491  C CD  . ARG   A 62  ? 0.1681 0.1693 0.1148 -0.0265 0.0099  -0.0078 68  ARG   A CD  
492  N NE  . ARG   A 62  ? 0.1845 0.1827 0.1327 -0.0275 0.0171  -0.0147 68  ARG   A NE  
493  C CZ  . ARG   A 62  ? 0.1728 0.1700 0.1186 -0.0324 0.0220  -0.0210 68  ARG   A CZ  
494  N NH1 . ARG   A 62  ? 0.1922 0.1918 0.1318 -0.0375 0.0198  -0.0216 68  ARG   A NH1 
495  N NH2 . ARG   A 62  ? 0.2073 0.2011 0.1574 -0.0328 0.0299  -0.0270 68  ARG   A NH2 
496  N N   . ARG   A 63  ? 0.1614 0.1742 0.1203 -0.0225 -0.0107 0.0140  69  ARG   A N   
497  C CA  . ARG   A 63  ? 0.1708 0.1860 0.1381 -0.0195 -0.0148 0.0225  69  ARG   A CA  
498  C C   . ARG   A 63  ? 0.1933 0.2035 0.1675 -0.0138 -0.0126 0.0239  69  ARG   A C   
499  O O   . ARG   A 63  ? 0.2156 0.2271 0.1944 -0.0133 -0.0143 0.0308  69  ARG   A O   
500  C CB  . ARG   A 63  ? 0.2130 0.2363 0.1776 -0.0252 -0.0200 0.0307  69  ARG   A CB  
501  C CG  . ARG   A 63  ? 0.2293 0.2591 0.1894 -0.0311 -0.0231 0.0308  69  ARG   A CG  
502  C CD  . ARG   A 63  ? 0.2339 0.2738 0.1952 -0.0360 -0.0297 0.0425  69  ARG   A CD  
503  N NE  . ARG   A 63  ? 0.2456 0.2937 0.1993 -0.0445 -0.0329 0.0423  69  ARG   A NE  
504  C CZ  . ARG   A 63  ? 0.2183 0.2722 0.1581 -0.0549 -0.0335 0.0403  69  ARG   A CZ  
505  N NH1 . ARG   A 63  ? 0.2308 0.2834 0.1634 -0.0576 -0.0315 0.0393  69  ARG   A NH1 
506  N NH2 . ARG   A 63  ? 0.2415 0.3029 0.1739 -0.0636 -0.0359 0.0392  69  ARG   A NH2 
507  N N   . LYS   A 64  ? 0.1628 0.1678 0.1380 -0.0103 -0.0086 0.0179  70  LYS   A N   
508  C CA  . LYS   A 64  ? 0.1677 0.1685 0.1473 -0.0067 -0.0060 0.0181  70  LYS   A CA  
509  C C   . LYS   A 64  ? 0.1531 0.1506 0.1372 -0.0031 -0.0035 0.0141  70  LYS   A C   
510  O O   . LYS   A 64  ? 0.1525 0.1502 0.1349 -0.0031 -0.0028 0.0101  70  LYS   A O   
511  C CB  . LYS   A 64  ? 0.2073 0.2071 0.1803 -0.0087 -0.0037 0.0152  70  LYS   A CB  
512  C CG  . LYS   A 64  ? 0.3212 0.3235 0.2906 -0.0121 -0.0055 0.0202  70  LYS   A CG  
513  C CD  . LYS   A 64  ? 0.4258 0.4263 0.3905 -0.0132 -0.0025 0.0174  70  LYS   A CD  
514  C CE  . LYS   A 64  ? 0.5120 0.5154 0.4722 -0.0174 -0.0044 0.0225  70  LYS   A CE  
515  N NZ  . LYS   A 64  ? 0.5721 0.5813 0.5248 -0.0235 -0.0074 0.0238  70  LYS   A NZ  
516  N N   . HIS   A 65  ? 0.1363 0.1310 0.1261 -0.0009 -0.0014 0.0151  71  HIS   A N   
517  C CA  . HIS   A 65  ? 0.1266 0.1191 0.1188 0.0006  0.0014  0.0112  71  HIS   A CA  
518  C C   . HIS   A 65  ? 0.1478 0.1394 0.1364 -0.0003 0.0038  0.0087  71  HIS   A C   
519  O O   . HIS   A 65  ? 0.1799 0.1702 0.1681 -0.0011 0.0049  0.0104  71  HIS   A O   
520  C CB  . HIS   A 65  ? 0.1287 0.1187 0.1291 0.0020  0.0034  0.0127  71  HIS   A CB  
521  C CG  . HIS   A 65  ? 0.1408 0.1322 0.1469 0.0033  0.0013  0.0156  71  HIS   A CG  
522  N ND1 . HIS   A 65  ? 0.1668 0.1581 0.1757 0.0042  0.0021  0.0131  71  HIS   A ND1 
523  C CD2 . HIS   A 65  ? 0.1366 0.1307 0.1467 0.0033  -0.0018 0.0216  71  HIS   A CD2 
524  C CE1 . HIS   A 65  ? 0.1396 0.1328 0.1545 0.0051  -0.0002 0.0171  71  HIS   A CE1 
525  N NE2 . HIS   A 65  ? 0.1728 0.1684 0.1888 0.0045  -0.0028 0.0226  71  HIS   A NE2 
526  N N   . TYR   A 66  ? 0.1248 0.1178 0.1120 -0.0004 0.0047  0.0056  72  TYR   A N   
527  C CA  . TYR   A 66  ? 0.1245 0.1186 0.1094 -0.0017 0.0065  0.0042  72  TYR   A CA  
528  C C   . TYR   A 66  ? 0.1181 0.1135 0.1047 -0.0029 0.0080  0.0028  72  TYR   A C   
529  O O   . TYR   A 66  ? 0.1225 0.1195 0.1109 -0.0025 0.0073  0.0024  72  TYR   A O   
530  C CB  . TYR   A 66  ? 0.1378 0.1343 0.1213 -0.0016 0.0063  0.0031  72  TYR   A CB  
531  C CG  . TYR   A 66  ? 0.1432 0.1391 0.1229 -0.0026 0.0059  0.0030  72  TYR   A CG  
532  C CD1 . TYR   A 66  ? 0.1702 0.1657 0.1464 -0.0042 0.0069  0.0034  72  TYR   A CD1 
533  C CD2 . TYR   A 66  ? 0.1559 0.1519 0.1345 -0.0029 0.0050  0.0022  72  TYR   A CD2 
534  C CE1 . TYR   A 66  ? 0.1804 0.1762 0.1517 -0.0065 0.0068  0.0031  72  TYR   A CE1 
535  C CE2 . TYR   A 66  ? 0.1680 0.1645 0.1415 -0.0058 0.0051  0.0014  72  TYR   A CE2 
536  C CZ  . TYR   A 66  ? 0.1745 0.1709 0.1439 -0.0078 0.0060  0.0019  72  TYR   A CZ  
537  O OH  . TYR   A 66  ? 0.2017 0.1993 0.1647 -0.0121 0.0064  0.0009  72  TYR   A OH  
538  N N   . PRO   A 67  ? 0.1200 0.1153 0.1052 -0.0052 0.0102  0.0019  73  PRO   A N   
539  C CA  . PRO   A 67  ? 0.1277 0.1263 0.1125 -0.0085 0.0115  0.0005  73  PRO   A CA  
540  C C   . PRO   A 67  ? 0.1270 0.1321 0.1123 -0.0088 0.0096  0.0021  73  PRO   A C   
541  O O   . PRO   A 67  ? 0.1568 0.1630 0.1420 -0.0079 0.0093  0.0030  73  PRO   A O   
542  C CB  . PRO   A 67  ? 0.1511 0.1480 0.1340 -0.0119 0.0148  -0.0012 73  PRO   A CB  
543  C CG  . PRO   A 67  ? 0.1802 0.1744 0.1625 -0.0097 0.0144  0.0004  73  PRO   A CG  
544  C CD  . PRO   A 67  ? 0.1360 0.1289 0.1196 -0.0059 0.0116  0.0024  73  PRO   A CD  
545  N N   . VAL   A 68  ? 0.1048 0.1145 0.0914 -0.0105 0.0086  0.0030  74  VAL   A N   
546  C CA  . VAL   A 68  ? 0.1230 0.1398 0.1134 -0.0105 0.0066  0.0066  74  VAL   A CA  
547  C C   . VAL   A 68  ? 0.1196 0.1440 0.1093 -0.0157 0.0057  0.0085  74  VAL   A C   
548  O O   . VAL   A 68  ? 0.1267 0.1503 0.1132 -0.0190 0.0067  0.0063  74  VAL   A O   
549  C CB  . VAL   A 68  ? 0.1591 0.1749 0.1543 -0.0063 0.0054  0.0079  74  VAL   A CB  
550  C CG1 . VAL   A 68  ? 0.1796 0.1905 0.1750 -0.0029 0.0063  0.0064  74  VAL   A CG1 
551  C CG2 . VAL   A 68  ? 0.1756 0.1890 0.1700 -0.0062 0.0049  0.0067  74  VAL   A CG2 
552  N N   A SER   A 69  ? 0.1209 0.1539 0.1149 -0.0171 0.0039  0.0133  75  SER   A N   
553  N N   B SER   A 69  ? 0.1226 0.1553 0.1164 -0.0171 0.0040  0.0132  75  SER   A N   
554  C CA  A SER   A 69  ? 0.1124 0.1560 0.1078 -0.0223 0.0014  0.0181  75  SER   A CA  
555  C CA  B SER   A 69  ? 0.1213 0.1649 0.1169 -0.0221 0.0015  0.0182  75  SER   A CA  
556  C C   A SER   A 69  ? 0.1028 0.1490 0.1074 -0.0181 -0.0006 0.0233  75  SER   A C   
557  C C   B SER   A 69  ? 0.1127 0.1584 0.1172 -0.0179 -0.0005 0.0231  75  SER   A C   
558  O O   A SER   A 69  ? 0.1046 0.1485 0.1165 -0.0128 0.0001  0.0247  75  SER   A O   
559  O O   B SER   A 69  ? 0.1184 0.1606 0.1296 -0.0122 0.0005  0.0237  75  SER   A O   
560  C CB  A SER   A 69  ? 0.1189 0.1721 0.1158 -0.0266 0.0002  0.0222  75  SER   A CB  
561  C CB  B SER   A 69  ? 0.1306 0.1828 0.1291 -0.0249 0.0004  0.0223  75  SER   A CB  
562  O OG  A SER   A 69  ? 0.1753 0.2252 0.1645 -0.0303 0.0027  0.0171  75  SER   A OG  
563  O OG  B SER   A 69  ? 0.1714 0.2361 0.1719 -0.0308 -0.0028 0.0287  75  SER   A OG  
564  N N   . PHE   A 70  ? 0.1121 0.1628 0.1168 -0.0209 -0.0024 0.0259  76  PHE   A N   
565  C CA  . PHE   A 70  ? 0.1087 0.1608 0.1225 -0.0169 -0.0038 0.0307  76  PHE   A CA  
566  C C   . PHE   A 70  ? 0.1191 0.1839 0.1368 -0.0221 -0.0074 0.0390  76  PHE   A C   
567  O O   . PHE   A 70  ? 0.1267 0.1982 0.1365 -0.0301 -0.0087 0.0392  76  PHE   A O   
568  C CB  . PHE   A 70  ? 0.1252 0.1673 0.1359 -0.0134 -0.0023 0.0252  76  PHE   A CB  
569  C CG  . PHE   A 70  ? 0.1150 0.1555 0.1167 -0.0181 -0.0017 0.0209  76  PHE   A CG  
570  C CD1 . PHE   A 70  ? 0.1192 0.1527 0.1138 -0.0190 0.0012  0.0142  76  PHE   A CD1 
571  C CD2 . PHE   A 70  ? 0.1224 0.1679 0.1237 -0.0218 -0.0032 0.0235  76  PHE   A CD2 
572  C CE1 . PHE   A 70  ? 0.1270 0.1582 0.1159 -0.0231 0.0034  0.0098  76  PHE   A CE1 
573  C CE2 . PHE   A 70  ? 0.1375 0.1807 0.1309 -0.0265 -0.0012 0.0184  76  PHE   A CE2 
574  C CZ  . PHE   A 70  ? 0.1333 0.1693 0.1211 -0.0272 0.0025  0.0113  76  PHE   A CZ  
575  N N   . SER   A 71  ? 0.1132 0.1819 0.1439 -0.0183 -0.0087 0.0465  77  SER   A N   
576  C CA  . SER   A 71  ? 0.1181 0.2005 0.1552 -0.0230 -0.0129 0.0571  77  SER   A CA  
577  C C   . SER   A 71  ? 0.1153 0.1982 0.1458 -0.0269 -0.0142 0.0563  77  SER   A C   
578  O O   . SER   A 71  ? 0.1329 0.2046 0.1572 -0.0241 -0.0115 0.0481  77  SER   A O   
579  C CB  . SER   A 71  ? 0.1304 0.2161 0.1869 -0.0170 -0.0128 0.0661  77  SER   A CB  
580  O OG  . SER   A 71  ? 0.1571 0.2319 0.2187 -0.0102 -0.0096 0.0624  77  SER   A OG  
581  N N   . LYS   A 72  ? 0.1208 0.2170 0.1526 -0.0338 -0.0182 0.0650  78  LYS   A N   
582  C CA  . LYS   A 72  ? 0.1291 0.2269 0.1554 -0.0381 -0.0194 0.0652  78  LYS   A CA  
583  C C   . LYS   A 72  ? 0.1344 0.2269 0.1730 -0.0302 -0.0188 0.0687  78  LYS   A C   
584  O O   . LYS   A 72  ? 0.1548 0.2479 0.2087 -0.0240 -0.0186 0.0750  78  LYS   A O   
585  C CB  . LYS   A 72  ? 0.1579 0.2738 0.1817 -0.0494 -0.0244 0.0750  78  LYS   A CB  
586  C CG  . LYS   A 72  ? 0.1852 0.3058 0.1951 -0.0588 -0.0240 0.0699  78  LYS   A CG  
587  C CD  . LYS   A 72  ? 0.2738 0.4125 0.2774 -0.0725 -0.0286 0.0775  78  LYS   A CD  
588  C CE  . LYS   A 72  ? 0.3548 0.4957 0.3426 -0.0828 -0.0263 0.0695  78  LYS   A CE  
589  N NZ  . LYS   A 72  ? 0.4170 0.5737 0.3934 -0.0989 -0.0291 0.0731  78  LYS   A NZ  
590  N N   . PRO   A 73  ? 0.1283 0.2154 0.1616 -0.0306 -0.0179 0.0646  79  PRO   A N   
591  C CA  . PRO   A 73  ? 0.1333 0.2148 0.1777 -0.0237 -0.0169 0.0670  79  PRO   A CA  
592  C C   . PRO   A 73  ? 0.1418 0.2347 0.2027 -0.0235 -0.0200 0.0817  79  PRO   A C   
593  O O   . PRO   A 73  ? 0.1597 0.2667 0.2195 -0.0314 -0.0246 0.0907  79  PRO   A O   
594  C CB  . PRO   A 73  ? 0.1571 0.2346 0.1910 -0.0270 -0.0162 0.0613  79  PRO   A CB  
595  C CG  . PRO   A 73  ? 0.1919 0.2669 0.2108 -0.0322 -0.0145 0.0521  79  PRO   A CG  
596  C CD  . PRO   A 73  ? 0.1586 0.2435 0.1759 -0.0374 -0.0166 0.0564  79  PRO   A CD  
597  N N   . SER   A 74  ? 0.1429 0.2301 0.2198 -0.0151 -0.0172 0.0841  80  SER   A N   
598  C CA  . SER   A 74  ? 0.1485 0.2452 0.2463 -0.0131 -0.0187 0.0985  80  SER   A CA  
599  C C   . SER   A 74  ? 0.1282 0.2149 0.2411 -0.0051 -0.0138 0.0985  80  SER   A C   
600  O O   . SER   A 74  ? 0.1230 0.1958 0.2300 -0.0009 -0.0093 0.0869  80  SER   A O   
601  C CB  . SER   A 74  ? 0.1959 0.2976 0.3027 -0.0115 -0.0183 0.1024  80  SER   A CB  
602  O OG  . SER   A 74  ? 0.2727 0.3785 0.3639 -0.0174 -0.0205 0.0978  80  SER   A OG  
603  N N   . LEU   A 75  ? 0.1360 0.2306 0.2710 -0.0029 -0.0142 0.1124  81  LEU   A N   
604  C CA  . LEU   A 75  ? 0.1460 0.2321 0.3000 0.0044  -0.0083 0.1141  81  LEU   A CA  
605  C C   . LEU   A 75  ? 0.1439 0.2263 0.3127 0.0100  -0.0027 0.1136  81  LEU   A C   
606  O O   . LEU   A 75  ? 0.1607 0.2551 0.3442 0.0095  -0.0049 0.1257  81  LEU   A O   
607  C CB  . LEU   A 75  ? 0.1542 0.2521 0.3258 0.0029  -0.0117 0.1311  81  LEU   A CB  
608  C CG  . LEU   A 75  ? 0.1951 0.2843 0.3880 0.0098  -0.0050 0.1338  81  LEU   A CG  
609  C CD1 . LEU   A 75  ? 0.2008 0.2759 0.3803 0.0107  -0.0018 0.1208  81  LEU   A CD1 
610  C CD2 . LEU   A 75  ? 0.2050 0.3083 0.4192 0.0085  -0.0089 0.1541  81  LEU   A CD2 
611  N N   . ILE   A 76  ? 0.1358 0.2027 0.3008 0.0144  0.0043  0.1000  82  ILE   A N   
612  C CA  . ILE   A 76  ? 0.1522 0.2136 0.3273 0.0187  0.0109  0.0962  82  ILE   A CA  
613  C C   . ILE   A 76  ? 0.1654 0.2137 0.3546 0.0240  0.0207  0.0907  82  ILE   A C   
614  O O   . ILE   A 76  ? 0.1607 0.1992 0.3402 0.0240  0.0228  0.0817  82  ILE   A O   
615  C CB  . ILE   A 76  ? 0.1870 0.2429 0.3389 0.0166  0.0101  0.0830  82  ILE   A CB  
616  C CG1 . ILE   A 76  ? 0.2124 0.2804 0.3501 0.0104  0.0016  0.0872  82  ILE   A CG1 
617  C CG2 . ILE   A 76  ? 0.2033 0.2523 0.3617 0.0200  0.0171  0.0769  82  ILE   A CG2 
618  C CD1 . ILE   A 76  ? 0.2119 0.2754 0.3292 0.0081  0.0009  0.0761  82  ILE   A CD1 
619  N N   . PHE   A 77  ? 0.1583 0.2060 0.3707 0.0281  0.0276  0.0953  83  PHE   A N   
620  C CA  . PHE   A 77  ? 0.1686 0.2030 0.3951 0.0322  0.0391  0.0884  83  PHE   A CA  
621  C C   . PHE   A 77  ? 0.2020 0.2246 0.4107 0.0311  0.0440  0.0713  83  PHE   A C   
622  O O   . PHE   A 77  ? 0.2469 0.2722 0.4496 0.0303  0.0431  0.0689  83  PHE   A O   
623  C CB  . PHE   A 77  ? 0.1751 0.2130 0.4344 0.0366  0.0460  0.0990  83  PHE   A CB  
624  C CG  . PHE   A 77  ? 0.2023 0.2266 0.4797 0.0401  0.0589  0.0935  83  PHE   A CG  
625  C CD1 . PHE   A 77  ? 0.2200 0.2420 0.5074 0.0412  0.0600  0.0983  83  PHE   A CD1 
626  C CD2 . PHE   A 77  ? 0.2446 0.2576 0.5266 0.0412  0.0704  0.0817  83  PHE   A CD2 
627  C CE1 . PHE   A 77  ? 0.2473 0.2557 0.5511 0.0436  0.0730  0.0920  83  PHE   A CE1 
628  C CE2 . PHE   A 77  ? 0.2575 0.2573 0.5552 0.0430  0.0837  0.0750  83  PHE   A CE2 
629  C CZ  . PHE   A 77  ? 0.2552 0.2526 0.5643 0.0443  0.0851  0.0801  83  PHE   A CZ  
630  N N   . VAL   A 78  ? 0.1860 0.1971 0.3845 0.0301  0.0481  0.0598  84  VAL   A N   
631  C CA  . VAL   A 78  ? 0.1758 0.1768 0.3557 0.0276  0.0519  0.0441  84  VAL   A CA  
632  C C   . VAL   A 78  ? 0.1727 0.1619 0.3659 0.0284  0.0650  0.0361  84  VAL   A C   
633  O O   . VAL   A 78  ? 0.1805 0.1654 0.3856 0.0295  0.0693  0.0377  84  VAL   A O   
634  C CB  . VAL   A 78  ? 0.1637 0.1626 0.3190 0.0243  0.0452  0.0373  84  VAL   A CB  
635  C CG1 . VAL   A 78  ? 0.1703 0.1605 0.3074 0.0211  0.0483  0.0229  84  VAL   A CG1 
636  C CG2 . VAL   A 78  ? 0.1772 0.1868 0.3201 0.0227  0.0340  0.0440  84  VAL   A CG2 
637  N N   . GLU   A 79  ? 0.1757 0.1591 0.3652 0.0268  0.0718  0.0266  85  GLU   A N   
638  C CA  . GLU   A 79  ? 0.1890 0.1607 0.3891 0.0257  0.0857  0.0168  85  GLU   A CA  
639  C C   . GLU   A 79  ? 0.1984 0.1616 0.3828 0.0212  0.0876  0.0055  85  GLU   A C   
640  O O   . GLU   A 79  ? 0.1961 0.1619 0.3587 0.0188  0.0781  0.0035  85  GLU   A O   
641  C CB  . GLU   A 79  ? 0.2252 0.1937 0.4225 0.0237  0.0924  0.0087  85  GLU   A CB  
642  C CG  . GLU   A 79  ? 0.2628 0.2389 0.4809 0.0282  0.0934  0.0194  85  GLU   A CG  
643  C CD  . GLU   A 79  ? 0.3362 0.3128 0.5887 0.0334  0.1007  0.0300  85  GLU   A CD  
644  O OE1 . GLU   A 79  ? 0.3729 0.3389 0.6381 0.0330  0.1128  0.0235  85  GLU   A OE1 
645  O OE2 . GLU   A 79  ? 0.3981 0.3865 0.6656 0.0374  0.0944  0.0453  85  GLU   A OE2 
646  N N   . ALA   A 80  ? 0.2104 0.1632 0.4072 0.0196  0.1007  -0.0020 86  ALA   A N   
647  C CA  . ALA   A 80  ? 0.2252 0.1699 0.4095 0.0142  0.1043  -0.0132 86  ALA   A CA  
648  C C   . ALA   A 80  ? 0.2411 0.1854 0.3964 0.0075  0.1002  -0.0243 86  ALA   A C   
649  O O   . ALA   A 80  ? 0.2595 0.2048 0.4075 0.0055  0.1012  -0.0282 86  ALA   A O   
650  C CB  . ALA   A 80  ? 0.2441 0.1773 0.4472 0.0123  0.1215  -0.0211 86  ALA   A CB  
651  N N   . SER   A 81  ? 0.2349 0.1783 0.3740 0.0038  0.0952  -0.0285 87  SER   A N   
652  C CA  . SER   A 81  ? 0.2504 0.1941 0.3638 -0.0034 0.0914  -0.0380 87  SER   A CA  
653  C C   . SER   A 81  ? 0.2721 0.2086 0.3807 -0.0102 0.0981  -0.0482 87  SER   A C   
654  O O   . SER   A 81  ? 0.2669 0.1975 0.3926 -0.0089 0.1065  -0.0484 87  SER   A O   
655  C CB  . SER   A 81  ? 0.2474 0.1999 0.3449 -0.0014 0.0764  -0.0314 87  SER   A CB  
656  O OG  . SER   A 81  ? 0.2360 0.1891 0.3337 -0.0003 0.0721  -0.0282 87  SER   A OG  
657  N N   . GLU   A 82  ? 0.2878 0.2260 0.3740 -0.0176 0.0938  -0.0554 88  GLU   A N   
658  C CA  . GLU   A 82  ? 0.2963 0.2302 0.3755 -0.0252 0.0981  -0.0642 88  GLU   A CA  
659  C C   . GLU   A 82  ? 0.2695 0.2052 0.3533 -0.0206 0.0915  -0.0572 88  GLU   A C   
660  O O   . GLU   A 82  ? 0.2864 0.2172 0.3724 -0.0245 0.0968  -0.0623 88  GLU   A O   
661  C CB  . GLU   A 82  ? 0.3615 0.3006 0.4152 -0.0339 0.0916  -0.0700 88  GLU   A CB  
662  C CG  . GLU   A 82  ? 0.4698 0.4073 0.5124 -0.0440 0.0945  -0.0791 88  GLU   A CG  
663  C CD  . GLU   A 82  ? 0.5911 0.5368 0.6101 -0.0522 0.0858  -0.0813 88  GLU   A CD  
664  O OE1 . GLU   A 82  ? 0.5721 0.5220 0.5830 -0.0527 0.0822  -0.0798 88  GLU   A OE1 
665  O OE2 . GLU   A 82  ? 0.6474 0.5960 0.6570 -0.0582 0.0824  -0.0837 88  GLU   A OE2 
666  N N   . TYR   A 83  ? 0.2428 0.1854 0.3287 -0.0129 0.0808  -0.0456 89  TYR   A N   
667  C CA  . TYR   A 83  ? 0.2173 0.1631 0.3038 -0.0095 0.0733  -0.0390 89  TYR   A CA  
668  C C   . TYR   A 83  ? 0.2024 0.1478 0.3102 -0.0021 0.0747  -0.0290 89  TYR   A C   
669  O O   . TYR   A 83  ? 0.2086 0.1543 0.3200 -0.0007 0.0721  -0.0252 89  TYR   A O   
670  C CB  . TYR   A 83  ? 0.2174 0.1720 0.2882 -0.0082 0.0601  -0.0341 89  TYR   A CB  
671  C CG  . TYR   A 83  ? 0.2412 0.1975 0.2929 -0.0158 0.0577  -0.0417 89  TYR   A CG  
672  C CD1 . TYR   A 83  ? 0.2719 0.2285 0.3150 -0.0213 0.0563  -0.0462 89  TYR   A CD1 
673  C CD2 . TYR   A 83  ? 0.2622 0.2206 0.3049 -0.0180 0.0568  -0.0438 89  TYR   A CD2 
674  C CE1 . TYR   A 83  ? 0.3028 0.2635 0.3291 -0.0289 0.0529  -0.0511 89  TYR   A CE1 
675  C CE2 . TYR   A 83  ? 0.2928 0.2544 0.3186 -0.0256 0.0539  -0.0490 89  TYR   A CE2 
676  C CZ  . TYR   A 83  ? 0.3301 0.2933 0.3479 -0.0312 0.0518  -0.0523 89  TYR   A CZ  
677  O OH  . TYR   A 83  ? 0.3783 0.3470 0.3803 -0.0392 0.0478  -0.0555 89  TYR   A OH  
678  N N   . TYR   A 84  ? 0.2121 0.1582 0.3337 0.0024  0.0778  -0.0236 90  TYR   A N   
679  C CA  . TYR   A 84  ? 0.1999 0.1477 0.3432 0.0089  0.0785  -0.0120 90  TYR   A CA  
680  C C   . TYR   A 84  ? 0.2045 0.1478 0.3690 0.0112  0.0897  -0.0114 90  TYR   A C   
681  O O   . TYR   A 84  ? 0.1994 0.1423 0.3596 0.0097  0.0924  -0.0160 90  TYR   A O   
682  C CB  . TYR   A 84  ? 0.1833 0.1420 0.3233 0.0133  0.0665  -0.0003 90  TYR   A CB  
683  C CG  . TYR   A 84  ? 0.1743 0.1381 0.2965 0.0119  0.0558  0.0006  90  TYR   A CG  
684  C CD1 . TYR   A 84  ? 0.1655 0.1299 0.2914 0.0126  0.0536  0.0047  90  TYR   A CD1 
685  C CD2 . TYR   A 84  ? 0.1732 0.1411 0.2762 0.0099  0.0487  -0.0025 90  TYR   A CD2 
686  C CE1 . TYR   A 84  ? 0.1606 0.1295 0.2717 0.0112  0.0448  0.0052  90  TYR   A CE1 
687  C CE2 . TYR   A 84  ? 0.1745 0.1466 0.2642 0.0089  0.0402  -0.0016 90  TYR   A CE2 
688  C CZ  . TYR   A 84  ? 0.1564 0.1288 0.2499 0.0094  0.0386  0.0017  90  TYR   A CZ  
689  O OH  . TYR   A 84  ? 0.1579 0.1340 0.2394 0.0082  0.0314  0.0019  90  TYR   A OH  
690  N N   . PRO   A 85  ? 0.2091 0.1496 0.3984 0.0151  0.0962  -0.0044 91  PRO   A N   
691  C CA  . PRO   A 85  ? 0.2108 0.1487 0.4250 0.0187  0.1064  -0.0008 91  PRO   A CA  
692  C C   . PRO   A 85  ? 0.2009 0.1507 0.4184 0.0236  0.0968  0.0121  91  PRO   A C   
693  O O   . PRO   A 85  ? 0.1957 0.1547 0.3977 0.0239  0.0836  0.0181  91  PRO   A O   
694  C CB  . PRO   A 85  ? 0.2332 0.1671 0.4733 0.0221  0.1132  0.0065  91  PRO   A CB  
695  C CG  . PRO   A 85  ? 0.2513 0.1921 0.4808 0.0228  0.1007  0.0139  91  PRO   A CG  
696  C CD  . PRO   A 85  ? 0.2154 0.1566 0.4128 0.0172  0.0936  0.0028  91  PRO   A CD  
697  N N   . ALA   A 86  ? 0.2100 0.1605 0.4482 0.0270  0.1035  0.0169  92  ALA   A N   
698  C CA  . ALA   A 86  ? 0.2056 0.1685 0.4497 0.0311  0.0949  0.0303  92  ALA   A CA  
699  C C   . ALA   A 86  ? 0.2119 0.1838 0.4667 0.0344  0.0866  0.0462  92  ALA   A C   
700  O O   . ALA   A 86  ? 0.2281 0.1957 0.5025 0.0364  0.0929  0.0505  92  ALA   A O   
701  C CB  . ALA   A 86  ? 0.2170 0.1784 0.4866 0.0343  0.1054  0.0333  92  ALA   A CB  
702  N N   . ARG   A 87  ? 0.2129 0.1964 0.4525 0.0338  0.0730  0.0534  93  ARG   A N   
703  C CA  . ARG   A 87  ? 0.2018 0.1948 0.4459 0.0348  0.0644  0.0670  93  ARG   A CA  
704  C C   . ARG   A 87  ? 0.1883 0.1950 0.4180 0.0331  0.0516  0.0744  93  ARG   A C   
705  O O   . ARG   A 87  ? 0.2032 0.2105 0.4172 0.0315  0.0493  0.0675  93  ARG   A O   
706  C CB  . ARG   A 87  ? 0.2229 0.2098 0.4513 0.0319  0.0626  0.0594  93  ARG   A CB  
707  C CG  . ARG   A 87  ? 0.2469 0.2346 0.4430 0.0278  0.0545  0.0494  93  ARG   A CG  
708  C CD  . ARG   A 87  ? 0.2449 0.2252 0.4256 0.0247  0.0549  0.0389  93  ARG   A CD  
709  N NE  . ARG   A 87  ? 0.2184 0.2038 0.3756 0.0220  0.0447  0.0369  93  ARG   A NE  
710  C CZ  . ARG   A 87  ? 0.2487 0.2362 0.3870 0.0199  0.0396  0.0314  93  ARG   A CZ  
711  N NH1 . ARG   A 87  ? 0.2316 0.2188 0.3697 0.0204  0.0420  0.0288  93  ARG   A NH1 
712  N NH2 . ARG   A 87  ? 0.2015 0.1920 0.3226 0.0176  0.0322  0.0296  93  ARG   A NH2 
713  N N   . TYR   A 88  ? 0.1805 0.1983 0.4142 0.0326  0.0434  0.0878  94  TYR   A N   
714  C CA  . TYR   A 88  ? 0.1841 0.2146 0.4013 0.0290  0.0318  0.0933  94  TYR   A CA  
715  C C   . TYR   A 88  ? 0.1719 0.1985 0.3612 0.0251  0.0268  0.0826  94  TYR   A C   
716  O O   . TYR   A 88  ? 0.1920 0.2140 0.3797 0.0247  0.0276  0.0807  94  TYR   A O   
717  C CB  . TYR   A 88  ? 0.1949 0.2400 0.4266 0.0282  0.0253  0.1121  94  TYR   A CB  
718  C CG  . TYR   A 88  ? 0.1915 0.2455 0.4483 0.0311  0.0270  0.1251  94  TYR   A CG  
719  C CD1 . TYR   A 88  ? 0.2024 0.2660 0.4525 0.0290  0.0219  0.1276  94  TYR   A CD1 
720  C CD2 . TYR   A 88  ? 0.1959 0.2472 0.4844 0.0361  0.0352  0.1335  94  TYR   A CD2 
721  C CE1 . TYR   A 88  ? 0.2122 0.2844 0.4860 0.0316  0.0235  0.1395  94  TYR   A CE1 
722  C CE2 . TYR   A 88  ? 0.1965 0.2558 0.5108 0.0393  0.0376  0.1456  94  TYR   A CE2 
723  C CZ  . TYR   A 88  ? 0.2126 0.2828 0.5192 0.0370  0.0314  0.1487  94  TYR   A CZ  
724  O OH  . TYR   A 88  ? 0.2390 0.3186 0.5708 0.0397  0.0330  0.1612  94  TYR   A OH  
725  N N   . GLN   A 89  ? 0.1509 0.1793 0.3192 0.0223  0.0221  0.0757  95  GLN   A N   
726  C CA  . GLN   A 89  ? 0.1349 0.1610 0.2788 0.0188  0.0173  0.0668  95  GLN   A CA  
727  C C   . GLN   A 89  ? 0.1296 0.1687 0.2647 0.0144  0.0086  0.0747  95  GLN   A C   
728  O O   . GLN   A 89  ? 0.1453 0.1925 0.2826 0.0134  0.0060  0.0801  95  GLN   A O   
729  C CB  . GLN   A 89  ? 0.1519 0.1692 0.2808 0.0186  0.0201  0.0531  95  GLN   A CB  
730  C CG  . GLN   A 89  ? 0.1585 0.1740 0.2659 0.0155  0.0154  0.0456  95  GLN   A CG  
731  C CD  . GLN   A 89  ? 0.1495 0.1559 0.2446 0.0152  0.0182  0.0331  95  GLN   A CD  
732  O OE1 . GLN   A 89  ? 0.1600 0.1670 0.2392 0.0130  0.0142  0.0285  95  GLN   A OE1 
733  N NE2 . GLN   A 89  ? 0.1276 0.1260 0.2287 0.0164  0.0252  0.0274  95  GLN   A NE2 
734  N N   . SER   A 90  ? 0.1211 0.1626 0.2463 0.0110  0.0043  0.0752  96  SER   A N   
735  C CA  . SER   A 90  ? 0.1210 0.1746 0.2365 0.0051  -0.0029 0.0814  96  SER   A CA  
736  C C   . SER   A 90  ? 0.1161 0.1666 0.2091 0.0017  -0.0048 0.0703  96  SER   A C   
737  O O   . SER   A 90  ? 0.1173 0.1571 0.2025 0.0041  -0.0017 0.0592  96  SER   A O   
738  C CB  . SER   A 90  ? 0.1443 0.2031 0.2626 0.0022  -0.0057 0.0888  96  SER   A CB  
739  O OG  . SER   A 90  ? 0.1789 0.2277 0.2873 0.0028  -0.0036 0.0786  96  SER   A OG  
740  N N   . HIS   A 91  ? 0.1154 0.1763 0.1995 -0.0044 -0.0097 0.0741  97  HIS   A N   
741  C CA  . HIS   A 91  ? 0.1203 0.1793 0.1855 -0.0085 -0.0107 0.0648  97  HIS   A CA  
742  C C   . HIS   A 91  ? 0.1124 0.1627 0.1735 -0.0045 -0.0076 0.0557  97  HIS   A C   
743  O O   . HIS   A 91  ? 0.1293 0.1724 0.1783 -0.0048 -0.0064 0.0461  97  HIS   A O   
744  C CB  . HIS   A 91  ? 0.1469 0.2009 0.2025 -0.0103 -0.0103 0.0586  97  HIS   A CB  
745  C CG  . HIS   A 91  ? 0.1428 0.2058 0.1998 -0.0156 -0.0134 0.0667  97  HIS   A CG  
746  N ND1 . HIS   A 91  ? 0.1626 0.2341 0.2078 -0.0243 -0.0161 0.0674  97  HIS   A ND1 
747  C CD2 . HIS   A 91  ? 0.1682 0.2334 0.2377 -0.0139 -0.0138 0.0750  97  HIS   A CD2 
748  C CE1 . HIS   A 91  ? 0.1798 0.2592 0.2291 -0.0282 -0.0186 0.0762  97  HIS   A CE1 
749  N NE2 . HIS   A 91  ? 0.1868 0.2626 0.2513 -0.0216 -0.0175 0.0814  97  HIS   A NE2 
750  N N   . LEU   A 92  ? 0.1064 0.1576 0.1777 -0.0013 -0.0061 0.0591  98  LEU   A N   
751  C CA  . LEU   A 92  ? 0.1086 0.1518 0.1773 0.0022  -0.0027 0.0514  98  LEU   A CA  
752  C C   . LEU   A 92  ? 0.1095 0.1594 0.1731 -0.0010 -0.0049 0.0529  98  LEU   A C   
753  O O   . LEU   A 92  ? 0.1106 0.1719 0.1815 -0.0037 -0.0077 0.0627  98  LEU   A O   
754  C CB  . LEU   A 92  ? 0.1198 0.1582 0.2045 0.0077  0.0023  0.0528  98  LEU   A CB  
755  C CG  . LEU   A 92  ? 0.1451 0.1750 0.2268 0.0104  0.0067  0.0442  98  LEU   A CG  
756  C CD1 . LEU   A 92  ? 0.1533 0.1739 0.2224 0.0104  0.0078  0.0338  98  LEU   A CD1 
757  C CD2 . LEU   A 92  ? 0.1791 0.2055 0.2789 0.0145  0.0131  0.0461  98  LEU   A CD2 
758  N N   . MET   A 93  ? 0.1055 0.1492 0.1580 -0.0009 -0.0035 0.0441  99  MET   A N   
759  C CA  . MET   A 93  ? 0.1090 0.1574 0.1559 -0.0039 -0.0048 0.0441  99  MET   A CA  
760  C C   . MET   A 93  ? 0.1062 0.1479 0.1555 0.0003  -0.0012 0.0397  99  MET   A C   
761  O O   . MET   A 93  ? 0.1250 0.1571 0.1705 0.0032  0.0015  0.0324  99  MET   A O   
762  C CB  . MET   A 93  ? 0.1191 0.1654 0.1506 -0.0083 -0.0055 0.0374  99  MET   A CB  
763  C CG  . MET   A 93  ? 0.1366 0.1889 0.1641 -0.0138 -0.0079 0.0403  99  MET   A CG  
764  S SD  . MET   A 93  ? 0.1714 0.2191 0.1836 -0.0188 -0.0063 0.0311  99  MET   A SD  
765  C CE  . MET   A 93  ? 0.1860 0.2204 0.1993 -0.0114 -0.0037 0.0241  99  MET   A CE  
766  N N   . LEU   A 94  ? 0.1007 0.1478 0.1558 0.0002  -0.0011 0.0437  100 LEU   A N   
767  C CA  . LEU   A 94  ? 0.1145 0.1556 0.1718 0.0035  0.0029  0.0391  100 LEU   A CA  
768  C C   . LEU   A 94  ? 0.1060 0.1476 0.1524 0.0007  0.0020  0.0354  100 LEU   A C   
769  O O   . LEU   A 94  ? 0.1274 0.1771 0.1697 -0.0040 -0.0012 0.0388  100 LEU   A O   
770  C CB  . LEU   A 94  ? 0.1341 0.1799 0.2097 0.0063  0.0053  0.0464  100 LEU   A CB  
771  C CG  . LEU   A 94  ? 0.1736 0.2175 0.2645 0.0100  0.0083  0.0501  100 LEU   A CG  
772  C CD1 . LEU   A 94  ? 0.1916 0.2390 0.3035 0.0133  0.0126  0.0567  100 LEU   A CD1 
773  C CD2 . LEU   A 94  ? 0.2218 0.2531 0.3077 0.0123  0.0127  0.0405  100 LEU   A CD2 
774  N N   . ALA   A 95  ? 0.1137 0.1471 0.1553 0.0027  0.0051  0.0285  101 ALA   A N   
775  C CA  . ALA   A 95  ? 0.1101 0.1427 0.1430 0.0008  0.0051  0.0250  101 ALA   A CA  
776  C C   . ALA   A 95  ? 0.1135 0.1411 0.1498 0.0035  0.0094  0.0217  101 ALA   A C   
777  O O   . ALA   A 95  ? 0.1142 0.1368 0.1563 0.0062  0.0128  0.0197  101 ALA   A O   
778  C CB  . ALA   A 95  ? 0.1264 0.1530 0.1459 -0.0008 0.0042  0.0189  101 ALA   A CB  
779  N N   . VAL   A 96  ? 0.1128 0.1411 0.1445 0.0020  0.0098  0.0202  102 VAL   A N   
780  C CA  . VAL   A 96  ? 0.1106 0.1338 0.1425 0.0033  0.0139  0.0161  102 VAL   A CA  
781  C C   . VAL   A 96  ? 0.1334 0.1489 0.1521 0.0025  0.0137  0.0097  102 VAL   A C   
782  O O   . VAL   A 96  ? 0.1627 0.1779 0.1727 0.0005  0.0113  0.0089  102 VAL   A O   
783  C CB  . VAL   A 96  ? 0.1082 0.1367 0.1420 0.0018  0.0143  0.0183  102 VAL   A CB  
784  C CG1 . VAL   A 96  ? 0.1281 0.1509 0.1597 0.0023  0.0189  0.0131  102 VAL   A CG1 
785  C CG2 . VAL   A 96  ? 0.1028 0.1411 0.1517 0.0024  0.0137  0.0267  102 VAL   A CG2 
786  N N   . GLY   A 97  ? 0.1410 0.1510 0.1597 0.0034  0.0167  0.0058  103 GLY   A N   
787  C CA  . GLY   A 97  ? 0.1586 0.1633 0.1662 0.0020  0.0159  0.0013  103 GLY   A CA  
788  C C   . GLY   A 97  ? 0.1743 0.1747 0.1824 0.0015  0.0194  -0.0028 103 GLY   A C   
789  O O   . GLY   A 97  ? 0.1853 0.1853 0.2028 0.0029  0.0229  -0.0029 103 GLY   A O   
790  N N   . HIS   A 98  ? 0.1952 0.1925 0.1931 -0.0012 0.0189  -0.0062 104 HIS   A N   
791  C CA  . HIS   A 98  ? 0.1991 0.1933 0.1945 -0.0039 0.0221  -0.0108 104 HIS   A CA  
792  C C   . HIS   A 98  ? 0.1910 0.1842 0.1872 -0.0034 0.0203  -0.0110 104 HIS   A C   
793  O O   . HIS   A 98  ? 0.1920 0.1864 0.1847 -0.0025 0.0152  -0.0083 104 HIS   A O   
794  C CB  . HIS   A 98  ? 0.2028 0.1963 0.1862 -0.0085 0.0213  -0.0131 104 HIS   A CB  
795  C CG  . HIS   A 98  ? 0.2110 0.2025 0.1901 -0.0135 0.0253  -0.0186 104 HIS   A CG  
796  N ND1 . HIS   A 98  ? 0.2132 0.2024 0.1967 -0.0154 0.0330  -0.0237 104 HIS   A ND1 
797  C CD2 . HIS   A 98  ? 0.2262 0.2181 0.1981 -0.0175 0.0231  -0.0200 104 HIS   A CD2 
798  C CE1 . HIS   A 98  ? 0.2228 0.2104 0.2001 -0.0212 0.0358  -0.0290 104 HIS   A CE1 
799  N NE2 . HIS   A 98  ? 0.2392 0.2290 0.2090 -0.0227 0.0294  -0.0266 104 HIS   A NE2 
800  N N   . SER   A 99  ? 0.1995 0.1903 0.2004 -0.0042 0.0249  -0.0144 105 SER   A N   
801  C CA  . SER   A 99  ? 0.2038 0.1932 0.2047 -0.0048 0.0242  -0.0157 105 SER   A CA  
802  C C   . SER   A 99  ? 0.2204 0.2060 0.2217 -0.0090 0.0313  -0.0224 105 SER   A C   
803  O O   . SER   A 99  ? 0.2591 0.2427 0.2669 -0.0092 0.0380  -0.0250 105 SER   A O   
804  C CB  . SER   A 99  ? 0.2055 0.1963 0.2155 -0.0002 0.0221  -0.0111 105 SER   A CB  
805  O OG  . SER   A 99  ? 0.2475 0.2386 0.2699 0.0023  0.0265  -0.0094 105 SER   A OG  
806  N N   . GLU   A 100 ? 0.1824 0.1673 0.1772 -0.0128 0.0301  -0.0253 106 GLU   A N   
807  C CA  . GLU   A 100 ? 0.2060 0.1876 0.1992 -0.0185 0.0363  -0.0325 106 GLU   A CA  
808  C C   . GLU   A 100 ? 0.2118 0.1930 0.2077 -0.0174 0.0339  -0.0316 106 GLU   A C   
809  O O   . GLU   A 100 ? 0.2020 0.1861 0.1983 -0.0133 0.0271  -0.0258 106 GLU   A O   
810  C CB  . GLU   A 100 ? 0.2363 0.2200 0.2144 -0.0270 0.0354  -0.0363 106 GLU   A CB  
811  C CG  . GLU   A 100 ? 0.2484 0.2323 0.2233 -0.0286 0.0381  -0.0375 106 GLU   A CG  
812  C CD  . GLU   A 100 ? 0.2557 0.2432 0.2152 -0.0377 0.0366  -0.0398 106 GLU   A CD  
813  O OE1 . GLU   A 100 ? 0.3237 0.3125 0.2750 -0.0454 0.0374  -0.0439 106 GLU   A OE1 
814  O OE2 . GLU   A 100 ? 0.2461 0.2357 0.2013 -0.0377 0.0346  -0.0372 106 GLU   A OE2 
815  N N   . PRO   A 101 ? 0.2212 0.1984 0.2201 -0.0210 0.0405  -0.0377 107 PRO   A N   
816  C CA  . PRO   A 101 ? 0.2088 0.1853 0.2119 -0.0194 0.0387  -0.0365 107 PRO   A CA  
817  C C   . PRO   A 101 ? 0.1990 0.1807 0.1931 -0.0203 0.0297  -0.0328 107 PRO   A C   
818  O O   . PRO   A 101 ? 0.1969 0.1797 0.1959 -0.0153 0.0253  -0.0279 107 PRO   A O   
819  C CB  . PRO   A 101 ? 0.2406 0.2118 0.2451 -0.0257 0.0482  -0.0454 107 PRO   A CB  
820  C CG  . PRO   A 101 ? 0.2687 0.2362 0.2789 -0.0263 0.0567  -0.0492 107 PRO   A CG  
821  C CD  . PRO   A 101 ? 0.2428 0.2150 0.2437 -0.0264 0.0513  -0.0461 107 PRO   A CD  
822  N N   . GLY   A 102 ? 0.1938 0.1792 0.1753 -0.0268 0.0267  -0.0343 108 GLY   A N   
823  C CA  . GLY   A 102 ? 0.1884 0.1798 0.1637 -0.0279 0.0183  -0.0296 108 GLY   A CA  
824  C C   . GLY   A 102 ? 0.1625 0.1566 0.1401 -0.0214 0.0118  -0.0218 108 GLY   A C   
825  O O   . GLY   A 102 ? 0.1692 0.1674 0.1454 -0.0209 0.0057  -0.0173 108 GLY   A O   
826  N N   . ASP   A 103 ? 0.1469 0.1387 0.1294 -0.0165 0.0136  -0.0204 109 ASP   A N   
827  C CA  . ASP   A 103 ? 0.1335 0.1272 0.1187 -0.0110 0.0088  -0.0142 109 ASP   A CA  
828  C C   . ASP   A 103 ? 0.1304 0.1234 0.1231 -0.0063 0.0075  -0.0117 109 ASP   A C   
829  O O   . ASP   A 103 ? 0.1277 0.1224 0.1219 -0.0032 0.0039  -0.0076 109 ASP   A O   
830  C CB  . ASP   A 103 ? 0.1363 0.1288 0.1233 -0.0087 0.0111  -0.0137 109 ASP   A CB  
831  C CG  . ASP   A 103 ? 0.1389 0.1329 0.1173 -0.0131 0.0109  -0.0146 109 ASP   A CG  
832  O OD1 . ASP   A 103 ? 0.1563 0.1538 0.1288 -0.0159 0.0063  -0.0120 109 ASP   A OD1 
833  O OD2 . ASP   A 103 ? 0.1488 0.1411 0.1275 -0.0139 0.0153  -0.0173 109 ASP   A OD2 
834  N N   . CYS   A 104 ? 0.1315 0.1222 0.1292 -0.0063 0.0107  -0.0143 110 CYS   A N   
835  C CA  . CYS   A 104 ? 0.1311 0.1219 0.1353 -0.0027 0.0092  -0.0114 110 CYS   A CA  
836  C C   . CYS   A 104 ? 0.1188 0.1125 0.1201 -0.0027 0.0040  -0.0089 110 CYS   A C   
837  O O   . CYS   A 104 ? 0.1336 0.1292 0.1300 -0.0063 0.0021  -0.0098 110 CYS   A O   
838  C CB  . CYS   A 104 ? 0.1311 0.1187 0.1409 -0.0035 0.0136  -0.0144 110 CYS   A CB  
839  S SG  . CYS   A 104 ? 0.1605 0.1447 0.1813 -0.0011 0.0206  -0.0147 110 CYS   A SG  
840  N N   . GLY   A 105 ? 0.1091 0.1038 0.1141 0.0007  0.0020  -0.0054 111 GLY   A N   
841  C CA  . GLY   A 105 ? 0.1180 0.1148 0.1229 0.0011  -0.0014 -0.0032 111 GLY   A CA  
842  C C   . GLY   A 105 ? 0.1135 0.1115 0.1171 0.0021  -0.0031 -0.0006 111 GLY   A C   
843  O O   . GLY   A 105 ? 0.1235 0.1224 0.1299 0.0031  -0.0044 0.0013  111 GLY   A O   
844  N N   . GLY   A 106 ? 0.1128 0.1103 0.1131 0.0017  -0.0023 -0.0008 112 GLY   A N   
845  C CA  . GLY   A 106 ? 0.1103 0.1082 0.1101 0.0025  -0.0031 0.0015  112 GLY   A CA  
846  C C   . GLY   A 106 ? 0.0929 0.0903 0.0958 0.0042  -0.0018 0.0020  112 GLY   A C   
847  O O   . GLY   A 106 ? 0.1051 0.1029 0.1091 0.0044  -0.0005 0.0015  112 GLY   A O   
848  N N   . ILE   A 107 ? 0.0985 0.0956 0.1035 0.0045  -0.0017 0.0033  113 ILE   A N   
849  C CA  . ILE   A 107 ? 0.0991 0.0959 0.1056 0.0042  0.0004  0.0025  113 ILE   A CA  
850  C C   . ILE   A 107 ? 0.0929 0.0899 0.0964 0.0031  0.0019  0.0022  113 ILE   A C   
851  O O   . ILE   A 107 ? 0.1016 0.0975 0.1038 0.0032  0.0020  0.0028  113 ILE   A O   
852  C CB  . ILE   A 107 ? 0.1053 0.1008 0.1168 0.0044  0.0018  0.0029  113 ILE   A CB  
853  C CG1 . ILE   A 107 ? 0.1256 0.1221 0.1407 0.0050  0.0008  0.0030  113 ILE   A CG1 
854  C CG2 . ILE   A 107 ? 0.1149 0.1091 0.1266 0.0024  0.0058  0.0008  113 ILE   A CG2 
855  C CD1 . ILE   A 107 ? 0.1526 0.1483 0.1753 0.0057  0.0022  0.0041  113 ILE   A CD1 
856  N N   . LEU   A 108 ? 0.0889 0.0882 0.0917 0.0013  0.0028  0.0019  114 LEU   A N   
857  C CA  . LEU   A 108 ? 0.0943 0.0954 0.0945 -0.0013 0.0043  0.0017  114 LEU   A CA  
858  C C   . LEU   A 108 ? 0.0930 0.0935 0.0930 -0.0046 0.0073  -0.0006 114 LEU   A C   
859  O O   . LEU   A 108 ? 0.0970 0.0986 0.0981 -0.0057 0.0076  -0.0010 114 LEU   A O   
860  C CB  . LEU   A 108 ? 0.0929 0.0990 0.0932 -0.0024 0.0030  0.0040  114 LEU   A CB  
861  C CG  . LEU   A 108 ? 0.1007 0.1115 0.0982 -0.0067 0.0037  0.0049  114 LEU   A CG  
862  C CD1 . LEU   A 108 ? 0.1232 0.1327 0.1189 -0.0063 0.0044  0.0044  114 LEU   A CD1 
863  C CD2 . LEU   A 108 ? 0.1214 0.1393 0.1219 -0.0080 0.0016  0.0096  114 LEU   A CD2 
864  N N   . ARG   A 109 ? 0.0986 0.0970 0.0976 -0.0065 0.0103  -0.0024 115 ARG   A N   
865  C CA  . ARG   A 109 ? 0.1094 0.1060 0.1089 -0.0106 0.0152  -0.0060 115 ARG   A CA  
866  C C   . ARG   A 109 ? 0.1144 0.1124 0.1091 -0.0159 0.0181  -0.0082 115 ARG   A C   
867  O O   . ARG   A 109 ? 0.1183 0.1167 0.1112 -0.0150 0.0168  -0.0068 115 ARG   A O   
868  C CB  . ARG   A 109 ? 0.1193 0.1100 0.1261 -0.0076 0.0181  -0.0067 115 ARG   A CB  
869  C CG  . ARG   A 109 ? 0.1281 0.1157 0.1370 -0.0054 0.0185  -0.0051 115 ARG   A CG  
870  C CD  . ARG   A 109 ? 0.1490 0.1325 0.1680 -0.0022 0.0204  -0.0032 115 ARG   A CD  
871  N NE  . ARG   A 109 ? 0.1466 0.1323 0.1679 0.0016  0.0152  0.0008  115 ARG   A NE  
872  C CZ  . ARG   A 109 ? 0.1303 0.1160 0.1590 0.0032  0.0153  0.0020  115 ARG   A CZ  
873  N NH1 . ARG   A 109 ? 0.1545 0.1376 0.1886 0.0015  0.0210  -0.0013 115 ARG   A NH1 
874  N NH2 . ARG   A 109 ? 0.1564 0.1450 0.1865 0.0057  0.0103  0.0059  115 ARG   A NH2 
875  N N   . CYS   A 110 ? 0.1472 0.1462 0.1393 -0.0223 0.0224  -0.0121 116 CYS   A N   
876  C CA  . CYS   A 110 ? 0.1744 0.1753 0.1608 -0.0296 0.0261  -0.0153 116 CYS   A CA  
877  C C   . CYS   A 110 ? 0.1971 0.1911 0.1868 -0.0328 0.0345  -0.0215 116 CYS   A C   
878  O O   . CYS   A 110 ? 0.1931 0.1813 0.1909 -0.0285 0.0370  -0.0220 116 CYS   A O   
879  C CB  . CYS   A 110 ? 0.1720 0.1825 0.1512 -0.0368 0.0238  -0.0140 116 CYS   A CB  
880  S SG  . CYS   A 110 ? 0.1720 0.1839 0.1496 -0.0425 0.0269  -0.0173 116 CYS   A SG  
881  N N   . GLN   A 111 ? 0.2055 0.2002 0.1897 -0.0413 0.0400  -0.0264 117 GLN   A N   
882  C CA  . GLN   A 111 ? 0.2308 0.2182 0.2186 -0.0459 0.0501  -0.0337 117 GLN   A CA  
883  C C   . GLN   A 111 ? 0.2504 0.2368 0.2406 -0.0483 0.0540  -0.0370 117 GLN   A C   
884  O O   . GLN   A 111 ? 0.2861 0.2645 0.2850 -0.0484 0.0627  -0.0419 117 GLN   A O   
885  C CB  . GLN   A 111 ? 0.2537 0.2430 0.2331 -0.0568 0.0558  -0.0395 117 GLN   A CB  
886  C CG  . GLN   A 111 ? 0.2859 0.2858 0.2535 -0.0673 0.0540  -0.0407 117 GLN   A CG  
887  C CD  . GLN   A 111 ? 0.3801 0.3826 0.3387 -0.0798 0.0599  -0.0469 117 GLN   A CD  
888  O OE1 . GLN   A 111 ? 0.4273 0.4373 0.3797 -0.0826 0.0551  -0.0435 117 GLN   A OE1 
889  N NE2 . GLN   A 111 ? 0.4020 0.3985 0.3604 -0.0879 0.0713  -0.0565 117 GLN   A NE2 
890  N N   . HIS   A 112 ? 0.2111 0.2052 0.1956 -0.0499 0.0483  -0.0342 118 HIS   A N   
891  C CA  . HIS   A 112 ? 0.2181 0.2121 0.2035 -0.0532 0.0519  -0.0375 118 HIS   A CA  
892  C C   . HIS   A 112 ? 0.2206 0.2113 0.2160 -0.0432 0.0485  -0.0334 118 HIS   A C   
893  O O   . HIS   A 112 ? 0.2574 0.2471 0.2556 -0.0449 0.0519  -0.0360 118 HIS   A O   
894  C CB  . HIS   A 112 ? 0.2148 0.2200 0.1885 -0.0615 0.0475  -0.0357 118 HIS   A CB  
895  C CG  . HIS   A 112 ? 0.2467 0.2578 0.2096 -0.0732 0.0500  -0.0390 118 HIS   A CG  
896  N ND1 . HIS   A 112 ? 0.2047 0.2249 0.1618 -0.0743 0.0425  -0.0328 118 HIS   A ND1 
897  C CD2 . HIS   A 112 ? 0.2786 0.2888 0.2354 -0.0853 0.0595  -0.0479 118 HIS   A CD2 
898  C CE1 . HIS   A 112 ? 0.2467 0.2713 0.1946 -0.0864 0.0468  -0.0374 118 HIS   A CE1 
899  N NE2 . HIS   A 112 ? 0.3035 0.3221 0.2502 -0.0937 0.0573  -0.0471 118 HIS   A NE2 
900  N N   . GLY   A 113 ? 0.1845 0.1748 0.1842 -0.0340 0.0414  -0.0269 119 GLY   A N   
901  C CA  . GLY   A 113 ? 0.1741 0.1629 0.1816 -0.0261 0.0375  -0.0229 119 GLY   A CA  
902  C C   . GLY   A 113 ? 0.1446 0.1380 0.1491 -0.0209 0.0283  -0.0165 119 GLY   A C   
903  O O   . GLY   A 113 ? 0.1476 0.1439 0.1471 -0.0213 0.0252  -0.0145 119 GLY   A O   
904  N N   . VAL   A 114 ? 0.1326 0.1267 0.1408 -0.0167 0.0247  -0.0138 120 VAL   A N   
905  C CA  . VAL   A 114 ? 0.1297 0.1272 0.1364 -0.0123 0.0175  -0.0088 120 VAL   A CA  
906  C C   . VAL   A 114 ? 0.1058 0.1099 0.1061 -0.0162 0.0147  -0.0070 120 VAL   A C   
907  O O   . VAL   A 114 ? 0.1249 0.1319 0.1230 -0.0209 0.0161  -0.0081 120 VAL   A O   
908  C CB  . VAL   A 114 ? 0.1289 0.1250 0.1417 -0.0075 0.0153  -0.0071 120 VAL   A CB  
909  C CG1 . VAL   A 114 ? 0.1397 0.1385 0.1506 -0.0045 0.0095  -0.0035 120 VAL   A CG1 
910  C CG2 . VAL   A 114 ? 0.1449 0.1367 0.1657 -0.0037 0.0167  -0.0064 120 VAL   A CG2 
911  N N   . VAL   A 115 ? 0.1101 0.1169 0.1084 -0.0147 0.0110  -0.0036 121 VAL   A N   
912  C CA  . VAL   A 115 ? 0.1061 0.1202 0.1017 -0.0175 0.0079  0.0003  121 VAL   A CA  
913  C C   . VAL   A 115 ? 0.1018 0.1169 0.1018 -0.0130 0.0042  0.0044  121 VAL   A C   
914  O O   . VAL   A 115 ? 0.1150 0.1356 0.1158 -0.0151 0.0023  0.0083  121 VAL   A O   
915  C CB  . VAL   A 115 ? 0.1172 0.1341 0.1102 -0.0186 0.0070  0.0020  121 VAL   A CB  
916  C CG1 . VAL   A 115 ? 0.1465 0.1722 0.1400 -0.0207 0.0032  0.0082  121 VAL   A CG1 
917  C CG2 . VAL   A 115 ? 0.1391 0.1553 0.1272 -0.0245 0.0113  -0.0025 121 VAL   A CG2 
918  N N   . GLY   A 116 ? 0.1037 0.1142 0.1070 -0.0073 0.0032  0.0042  122 GLY   A N   
919  C CA  . GLY   A 116 ? 0.1116 0.1221 0.1192 -0.0037 0.0011  0.0068  122 GLY   A CA  
920  C C   . GLY   A 116 ? 0.0953 0.1008 0.1040 0.0003  0.0009  0.0050  122 GLY   A C   
921  O O   . GLY   A 116 ? 0.1063 0.1091 0.1133 0.0008  0.0016  0.0030  122 GLY   A O   
922  N N   . ILE   A 117 ? 0.0975 0.1023 0.1096 0.0025  0.0003  0.0060  123 ILE   A N   
923  C CA  . ILE   A 117 ? 0.0948 0.0960 0.1063 0.0044  0.0004  0.0038  123 ILE   A CA  
924  C C   . ILE   A 117 ? 0.0981 0.0992 0.1122 0.0053  0.0017  0.0045  123 ILE   A C   
925  O O   . ILE   A 117 ? 0.1063 0.1095 0.1260 0.0057  0.0024  0.0073  123 ILE   A O   
926  C CB  . ILE   A 117 ? 0.1047 0.1040 0.1175 0.0049  -0.0002 0.0023  123 ILE   A CB  
927  C CG1 . ILE   A 117 ? 0.1243 0.1244 0.1418 0.0050  0.0004  0.0036  123 ILE   A CG1 
928  C CG2 . ILE   A 117 ? 0.1268 0.1260 0.1390 0.0045  -0.0009 0.0017  123 ILE   A CG2 
929  C CD1 . ILE   A 117 ? 0.1337 0.1317 0.1523 0.0049  0.0003  0.0015  123 ILE   A CD1 
930  N N   . VAL   A 118 ? 0.0991 0.0979 0.1104 0.0054  0.0024  0.0022  124 VAL   A N   
931  C CA  . VAL   A 118 ? 0.1037 0.1015 0.1178 0.0057  0.0051  0.0014  124 VAL   A CA  
932  C C   . VAL   A 118 ? 0.1075 0.1034 0.1276 0.0061  0.0075  0.0006  124 VAL   A C   
933  O O   . VAL   A 118 ? 0.1077 0.1019 0.1257 0.0051  0.0069  -0.0017 124 VAL   A O   
934  C CB  . VAL   A 118 ? 0.1093 0.1050 0.1175 0.0042  0.0058  -0.0019 124 VAL   A CB  
935  C CG1 . VAL   A 118 ? 0.1151 0.1087 0.1264 0.0036  0.0104  -0.0043 124 VAL   A CG1 
936  C CG2 . VAL   A 118 ? 0.1185 0.1154 0.1221 0.0040  0.0041  -0.0006 124 VAL   A CG2 
937  N N   . SER   A 119 ? 0.1079 0.1041 0.1367 0.0074  0.0105  0.0028  125 SER   A N   
938  C CA  . SER   A 119 ? 0.1202 0.1139 0.1578 0.0081  0.0142  0.0025  125 SER   A CA  
939  C C   . SER   A 119 ? 0.1374 0.1285 0.1832 0.0087  0.0202  0.0012  125 SER   A C   
940  O O   . SER   A 119 ? 0.1681 0.1544 0.2189 0.0078  0.0254  -0.0026 125 SER   A O   
941  C CB  . SER   A 119 ? 0.1224 0.1200 0.1667 0.0094  0.0121  0.0087  125 SER   A CB  
942  O OG  . SER   A 119 ? 0.1572 0.1524 0.2126 0.0105  0.0160  0.0099  125 SER   A OG  
943  N N   . THR   A 120 ? 0.1391 0.1329 0.1878 0.0097  0.0207  0.0039  126 THR   A N   
944  C CA  . THR   A 120 ? 0.1462 0.1376 0.2057 0.0105  0.0275  0.0029  126 THR   A CA  
945  C C   . THR   A 120 ? 0.1756 0.1672 0.2286 0.0092  0.0282  0.0002  126 THR   A C   
946  O O   . THR   A 120 ? 0.1458 0.1402 0.1880 0.0084  0.0228  0.0007  126 THR   A O   
947  C CB  . THR   A 120 ? 0.1416 0.1378 0.2182 0.0137  0.0282  0.0120  126 THR   A CB  
948  O OG1 . THR   A 120 ? 0.1457 0.1495 0.2200 0.0139  0.0231  0.0178  126 THR   A OG1 
949  C CG2 . THR   A 120 ? 0.1391 0.1366 0.2219 0.0147  0.0266  0.0166  126 THR   A CG2 
950  N N   . GLY   A 121 ? 0.2117 0.2002 0.2721 0.0090  0.0353  -0.0028 127 GLY   A N   
951  C CA  . GLY   A 121 ? 0.2534 0.2425 0.3086 0.0077  0.0363  -0.0050 127 GLY   A CA  
952  C C   . GLY   A 121 ? 0.2579 0.2432 0.3229 0.0071  0.0457  -0.0090 127 GLY   A C   
953  O O   . GLY   A 121 ? 0.2821 0.2635 0.3598 0.0078  0.0524  -0.0102 127 GLY   A O   
954  N N   . GLY   A 122 ? 0.2525 0.2384 0.3111 0.0052  0.0464  -0.0114 128 GLY   A N   
955  C CA  . GLY   A 122 ? 0.2301 0.2125 0.2954 0.0036  0.0557  -0.0164 128 GLY   A CA  
956  C C   . GLY   A 122 ? 0.2311 0.2184 0.3019 0.0057  0.0550  -0.0117 128 GLY   A C   
957  O O   . GLY   A 122 ? 0.2365 0.2306 0.3135 0.0093  0.0493  -0.0029 128 GLY   A O   
958  N N   . ASN   A 123 ? 0.2152 0.1996 0.2854 0.0029  0.0620  -0.0176 129 ASN   A N   
959  C CA  . ASN   A 123 ? 0.2271 0.2155 0.3048 0.0045  0.0636  -0.0143 129 ASN   A CA  
960  C C   . ASN   A 123 ? 0.2237 0.2194 0.2933 0.0059  0.0534  -0.0075 129 ASN   A C   
961  O O   . ASN   A 123 ? 0.2333 0.2353 0.3141 0.0087  0.0524  -0.0005 129 ASN   A O   
962  C CB  . ASN   A 123 ? 0.2422 0.2321 0.3460 0.0091  0.0701  -0.0087 129 ASN   A CB  
963  C CG  . ASN   A 123 ? 0.2825 0.2638 0.3972 0.0075  0.0826  -0.0163 129 ASN   A CG  
964  O OD1 . ASN   A 123 ? 0.3279 0.3039 0.4360 0.0025  0.0901  -0.0259 129 ASN   A OD1 
965  N ND2 . ASN   A 123 ? 0.2752 0.2552 0.4066 0.0109  0.0855  -0.0123 129 ASN   A ND2 
966  N N   . GLY   A 124 ? 0.1964 0.1917 0.2475 0.0034  0.0468  -0.0095 130 GLY   A N   
967  C CA  . GLY   A 124 ? 0.1933 0.1938 0.2362 0.0039  0.0389  -0.0047 130 GLY   A CA  
968  C C   . GLY   A 124 ? 0.1396 0.1452 0.1868 0.0065  0.0327  0.0025  130 GLY   A C   
969  O O   . GLY   A 124 ? 0.1770 0.1870 0.2185 0.0060  0.0275  0.0058  130 GLY   A O   
970  N N   . LEU   A 125 ? 0.1584 0.1630 0.2138 0.0083  0.0337  0.0040  131 LEU   A N   
971  C CA  . LEU   A 125 ? 0.1457 0.1550 0.2024 0.0097  0.0275  0.0102  131 LEU   A CA  
972  C C   . LEU   A 125 ? 0.1453 0.1499 0.1913 0.0086  0.0251  0.0061  131 LEU   A C   
973  O O   . LEU   A 125 ? 0.1773 0.1757 0.2198 0.0072  0.0289  -0.0002 131 LEU   A O   
974  C CB  . LEU   A 125 ? 0.1442 0.1575 0.2199 0.0126  0.0296  0.0172  131 LEU   A CB  
975  C CG  . LEU   A 125 ? 0.1496 0.1702 0.2389 0.0138  0.0309  0.0238  131 LEU   A CG  
976  C CD1 . LEU   A 125 ? 0.1793 0.2019 0.2920 0.0171  0.0359  0.0301  131 LEU   A CD1 
977  C CD2 . LEU   A 125 ? 0.1514 0.1816 0.2349 0.0117  0.0233  0.0301  131 LEU   A CD2 
978  N N   . VAL   A 126 ? 0.1115 0.1196 0.1528 0.0084  0.0192  0.0097  132 VAL   A N   
979  C CA  . VAL   A 126 ? 0.1119 0.1169 0.1463 0.0079  0.0167  0.0073  132 VAL   A CA  
980  C C   . VAL   A 126 ? 0.1155 0.1258 0.1558 0.0087  0.0134  0.0136  132 VAL   A C   
981  O O   . VAL   A 126 ? 0.1195 0.1364 0.1605 0.0077  0.0105  0.0185  132 VAL   A O   
982  C CB  . VAL   A 126 ? 0.1239 0.1269 0.1443 0.0059  0.0135  0.0039  132 VAL   A CB  
983  C CG1 . VAL   A 126 ? 0.1305 0.1376 0.1471 0.0050  0.0105  0.0067  132 VAL   A CG1 
984  C CG2 . VAL   A 126 ? 0.1262 0.1269 0.1419 0.0056  0.0111  0.0024  132 VAL   A CG2 
985  N N   . GLY   A 127 ? 0.1152 0.1232 0.1590 0.0096  0.0139  0.0135  133 GLY   A N   
986  C CA  . GLY   A 127 ? 0.1082 0.1213 0.1566 0.0095  0.0108  0.0194  133 GLY   A CA  
987  C C   . GLY   A 127 ? 0.1074 0.1179 0.1464 0.0083  0.0081  0.0163  133 GLY   A C   
988  O O   . GLY   A 127 ? 0.1241 0.1287 0.1589 0.0085  0.0096  0.0108  133 GLY   A O   
989  N N   . PHE   A 128 ? 0.0999 0.1157 0.1360 0.0063  0.0044  0.0197  134 PHE   A N   
990  C CA  . PHE   A 128 ? 0.1051 0.1189 0.1335 0.0049  0.0025  0.0169  134 PHE   A CA  
991  C C   . PHE   A 128 ? 0.1005 0.1183 0.1336 0.0039  0.0011  0.0215  134 PHE   A C   
992  O O   . PHE   A 128 ? 0.1007 0.1261 0.1382 0.0020  -0.0006 0.0280  134 PHE   A O   
993  C CB  . PHE   A 128 ? 0.1120 0.1278 0.1316 0.0019  0.0008  0.0155  134 PHE   A CB  
994  C CG  . PHE   A 128 ? 0.1006 0.1136 0.1159 0.0024  0.0019  0.0125  134 PHE   A CG  
995  C CD1 . PHE   A 128 ? 0.0997 0.1070 0.1102 0.0035  0.0025  0.0080  134 PHE   A CD1 
996  C CD2 . PHE   A 128 ? 0.1152 0.1325 0.1318 0.0013  0.0019  0.0151  134 PHE   A CD2 
997  C CE1 . PHE   A 128 ? 0.1043 0.1097 0.1110 0.0034  0.0032  0.0062  134 PHE   A CE1 
998  C CE2 . PHE   A 128 ? 0.1180 0.1327 0.1305 0.0015  0.0030  0.0123  134 PHE   A CE2 
999  C CZ  . PHE   A 128 ? 0.1107 0.1192 0.1180 0.0025  0.0037  0.0079  134 PHE   A CZ  
1000 N N   . ALA   A 129 ? 0.0970 0.1107 0.1291 0.0046  0.0014  0.0187  135 ALA   A N   
1001 C CA  . ALA   A 129 ? 0.1038 0.1208 0.1388 0.0032  0.0001  0.0223  135 ALA   A CA  
1002 C C   . ALA   A 129 ? 0.1019 0.1222 0.1281 -0.0010 -0.0018 0.0214  135 ALA   A C   
1003 O O   . ALA   A 129 ? 0.1096 0.1254 0.1295 -0.0010 -0.0012 0.0158  135 ALA   A O   
1004 C CB  . ALA   A 129 ? 0.1077 0.1189 0.1443 0.0050  0.0016  0.0188  135 ALA   A CB  
1005 N N   . ASP   A 130 ? 0.1045 0.1328 0.1309 -0.0051 -0.0037 0.0268  136 ASP   A N   
1006 C CA  . ASP   A 130 ? 0.1136 0.1451 0.1311 -0.0108 -0.0041 0.0248  136 ASP   A CA  
1007 C C   . ASP   A 130 ? 0.1097 0.1387 0.1252 -0.0118 -0.0034 0.0221  136 ASP   A C   
1008 O O   . ASP   A 130 ? 0.1260 0.1551 0.1475 -0.0101 -0.0040 0.0253  136 ASP   A O   
1009 C CB  . ASP   A 130 ? 0.1325 0.1753 0.1501 -0.0168 -0.0066 0.0322  136 ASP   A CB  
1010 C CG  . ASP   A 130 ? 0.1534 0.2004 0.1606 -0.0249 -0.0061 0.0294  136 ASP   A CG  
1011 O OD1 . ASP   A 130 ? 0.1815 0.2243 0.1824 -0.0260 -0.0036 0.0228  136 ASP   A OD1 
1012 O OD2 . ASP   A 130 ? 0.1956 0.2497 0.2012 -0.0306 -0.0076 0.0333  136 ASP   A OD2 
1013 N N   . VAL   A 131 ? 0.1055 0.1323 0.1141 -0.0150 -0.0013 0.0164  137 VAL   A N   
1014 C CA  . VAL   A 131 ? 0.1121 0.1373 0.1192 -0.0170 0.0001  0.0136  137 VAL   A CA  
1015 C C   . VAL   A 131 ? 0.1189 0.1487 0.1186 -0.0253 0.0021  0.0116  137 VAL   A C   
1016 O O   . VAL   A 131 ? 0.1188 0.1476 0.1170 -0.0280 0.0044  0.0086  137 VAL   A O   
1017 C CB  . VAL   A 131 ? 0.1200 0.1370 0.1286 -0.0124 0.0021  0.0079  137 VAL   A CB  
1018 C CG1 . VAL   A 131 ? 0.1336 0.1469 0.1476 -0.0063 0.0005  0.0092  137 VAL   A CG1 
1019 C CG2 . VAL   A 131 ? 0.1338 0.1472 0.1396 -0.0127 0.0048  0.0032  137 VAL   A CG2 
1020 N N   . ARG   A 132 ? 0.1190 0.1541 0.1140 -0.0303 0.0020  0.0127  138 ARG   A N   
1021 C CA  . ARG   A 132 ? 0.1255 0.1644 0.1121 -0.0398 0.0052  0.0090  138 ARG   A CA  
1022 C C   . ARG   A 132 ? 0.1474 0.1948 0.1305 -0.0475 0.0039  0.0128  138 ARG   A C   
1023 O O   . ARG   A 132 ? 0.1595 0.2085 0.1351 -0.0561 0.0080  0.0077  138 ARG   A O   
1024 C CB  . ARG   A 132 ? 0.1290 0.1724 0.1107 -0.0444 0.0051  0.0094  138 ARG   A CB  
1025 C CG  . ARG   A 132 ? 0.1211 0.1557 0.1047 -0.0386 0.0075  0.0045  138 ARG   A CG  
1026 C CD  . ARG   A 132 ? 0.1494 0.1889 0.1284 -0.0433 0.0073  0.0052  138 ARG   A CD  
1027 N NE  . ARG   A 132 ? 0.1426 0.1895 0.1260 -0.0409 0.0015  0.0140  138 ARG   A NE  
1028 C CZ  . ARG   A 132 ? 0.1606 0.2131 0.1432 -0.0430 -0.0002 0.0171  138 ARG   A CZ  
1029 N NH1 . ARG   A 132 ? 0.1716 0.2244 0.1469 -0.0492 0.0030  0.0121  138 ARG   A NH1 
1030 N NH2 . ARG   A 132 ? 0.1598 0.2175 0.1500 -0.0390 -0.0045 0.0252  138 ARG   A NH2 
1031 N N   . ASP   A 133 ? 0.1407 0.1937 0.1295 -0.0452 -0.0012 0.0218  139 ASP   A N   
1032 C CA  . ASP   A 133 ? 0.1509 0.2124 0.1375 -0.0522 -0.0030 0.0269  139 ASP   A CA  
1033 C C   . ASP   A 133 ? 0.1483 0.2037 0.1366 -0.0500 -0.0005 0.0230  139 ASP   A C   
1034 O O   . ASP   A 133 ? 0.1703 0.2321 0.1554 -0.0567 -0.0012 0.0261  139 ASP   A O   
1035 C CB  . ASP   A 133 ? 0.1733 0.2436 0.1685 -0.0503 -0.0090 0.0397  139 ASP   A CB  
1036 C CG  . ASP   A 133 ? 0.1984 0.2610 0.2057 -0.0390 -0.0097 0.0417  139 ASP   A CG  
1037 O OD1 . ASP   A 133 ? 0.1805 0.2333 0.1895 -0.0321 -0.0074 0.0353  139 ASP   A OD1 
1038 O OD2 . ASP   A 133 ? 0.2298 0.2966 0.2454 -0.0377 -0.0124 0.0501  139 ASP   A OD2 
1039 N N   . LEU   A 134 ? 0.1368 0.1812 0.1301 -0.0414 0.0018  0.0174  140 LEU   A N   
1040 C CA  . LEU   A 134 ? 0.1301 0.1695 0.1267 -0.0388 0.0034  0.0146  140 LEU   A CA  
1041 C C   . LEU   A 134 ? 0.1329 0.1692 0.1238 -0.0442 0.0095  0.0059  140 LEU   A C   
1042 O O   . LEU   A 134 ? 0.1396 0.1677 0.1338 -0.0396 0.0131  -0.0004 140 LEU   A O   
1043 C CB  . LEU   A 134 ? 0.1323 0.1632 0.1369 -0.0284 0.0028  0.0133  140 LEU   A CB  
1044 C CG  . LEU   A 134 ? 0.1477 0.1798 0.1593 -0.0230 -0.0012 0.0203  140 LEU   A CG  
1045 C CD1 . LEU   A 134 ? 0.1675 0.1911 0.1844 -0.0150 -0.0007 0.0169  140 LEU   A CD1 
1046 C CD2 . LEU   A 134 ? 0.1702 0.2078 0.1864 -0.0246 -0.0036 0.0280  140 LEU   A CD2 
1047 N N   . LEU   A 135 ? 0.1415 0.1850 0.1245 -0.0549 0.0112  0.0058  141 LEU   A N   
1048 C CA  . LEU   A 135 ? 0.1583 0.1988 0.1358 -0.0618 0.0188  -0.0037 141 LEU   A CA  
1049 C C   . LEU   A 135 ? 0.1610 0.1941 0.1444 -0.0579 0.0230  -0.0090 141 LEU   A C   
1050 O O   . LEU   A 135 ? 0.1817 0.2085 0.1670 -0.0586 0.0301  -0.0171 141 LEU   A O   
1051 C CB  . LEU   A 135 ? 0.1814 0.2323 0.1474 -0.0761 0.0201  -0.0032 141 LEU   A CB  
1052 C CG  . LEU   A 135 ? 0.1944 0.2557 0.1546 -0.0816 0.0150  0.0038  141 LEU   A CG  
1053 C CD1 . LEU   A 135 ? 0.2199 0.2922 0.1667 -0.0984 0.0172  0.0027  141 LEU   A CD1 
1054 C CD2 . LEU   A 135 ? 0.2129 0.2697 0.1739 -0.0779 0.0162  0.0004  141 LEU   A CD2 
1055 N N   . TRP   A 136 ? 0.1512 0.1850 0.1396 -0.0533 0.0188  -0.0038 142 TRP   A N   
1056 C CA  . TRP   A 136 ? 0.1581 0.1863 0.1526 -0.0497 0.0218  -0.0075 142 TRP   A CA  
1057 C C   . TRP   A 136 ? 0.1506 0.1702 0.1540 -0.0405 0.0233  -0.0112 142 TRP   A C   
1058 O O   . TRP   A 136 ? 0.1746 0.1900 0.1843 -0.0384 0.0270  -0.0151 142 TRP   A O   
1059 C CB  . TRP   A 136 ? 0.1669 0.1981 0.1644 -0.0475 0.0169  -0.0009 142 TRP   A CB  
1060 C CG  . TRP   A 136 ? 0.1464 0.1775 0.1491 -0.0400 0.0107  0.0060  142 TRP   A CG  
1061 C CD1 . TRP   A 136 ? 0.1486 0.1863 0.1503 -0.0416 0.0060  0.0142  142 TRP   A CD1 
1062 C CD2 . TRP   A 136 ? 0.1495 0.1738 0.1601 -0.0304 0.0092  0.0054  142 TRP   A CD2 
1063 N NE1 . TRP   A 136 ? 0.1610 0.1953 0.1705 -0.0331 0.0028  0.0179  142 TRP   A NE1 
1064 C CE2 . TRP   A 136 ? 0.1518 0.1779 0.1654 -0.0268 0.0047  0.0120  142 TRP   A CE2 
1065 C CE3 . TRP   A 136 ? 0.1545 0.1723 0.1705 -0.0253 0.0112  0.0005  142 TRP   A CE3 
1066 C CZ2 . TRP   A 136 ? 0.1654 0.1860 0.1855 -0.0192 0.0031  0.0122  142 TRP   A CZ2 
1067 C CZ3 . TRP   A 136 ? 0.1719 0.1860 0.1935 -0.0182 0.0083  0.0018  142 TRP   A CZ3 
1068 C CH2 . TRP   A 136 ? 0.1704 0.1856 0.1931 -0.0157 0.0048  0.0069  142 TRP   A CH2 
1069 N N   . LEU   A 137 ? 0.1425 0.1602 0.1476 -0.0352 0.0204  -0.0094 143 LEU   A N   
1070 C CA  . LEU   A 137 ? 0.1537 0.1647 0.1667 -0.0279 0.0217  -0.0120 143 LEU   A CA  
1071 C C   . LEU   A 137 ? 0.1804 0.1873 0.1966 -0.0306 0.0296  -0.0187 143 LEU   A C   
1072 O O   . LEU   A 137 ? 0.1931 0.1955 0.2191 -0.0250 0.0313  -0.0199 143 LEU   A O   
1073 C CB  . LEU   A 137 ? 0.1514 0.1616 0.1638 -0.0236 0.0180  -0.0093 143 LEU   A CB  
1074 C CG  . LEU   A 137 ? 0.1478 0.1596 0.1611 -0.0191 0.0117  -0.0035 143 LEU   A CG  
1075 C CD1 . LEU   A 137 ? 0.1638 0.1756 0.1756 -0.0166 0.0093  -0.0015 143 LEU   A CD1 
1076 C CD2 . LEU   A 137 ? 0.1654 0.1737 0.1857 -0.0132 0.0101  -0.0033 143 LEU   A CD2 
1077 N N   . ASP   A 138 ? 0.2058 0.2148 0.2146 -0.0398 0.0350  -0.0230 144 ASP   A N   
1078 C CA  . ASP   A 138 ? 0.2450 0.2492 0.2573 -0.0438 0.0448  -0.0309 144 ASP   A CA  
1079 C C   . ASP   A 138 ? 0.2961 0.2986 0.3133 -0.0467 0.0511  -0.0354 144 ASP   A C   
1080 O O   . ASP   A 138 ? 0.3227 0.3208 0.3446 -0.0505 0.0609  -0.0425 144 ASP   A O   
1081 C CB  . ASP   A 138 ? 0.2586 0.2659 0.2594 -0.0545 0.0490  -0.0349 144 ASP   A CB  
1082 C CG  . ASP   A 138 ? 0.2757 0.2844 0.2722 -0.0529 0.0446  -0.0318 144 ASP   A CG  
1083 O OD1 . ASP   A 138 ? 0.2978 0.3033 0.3011 -0.0433 0.0401  -0.0278 144 ASP   A OD1 
1084 O OD2 . ASP   A 138 ? 0.3606 0.3744 0.3465 -0.0621 0.0458  -0.0332 144 ASP   A OD2 
1085 N N   . GLU   A 139 ? 0.3090 0.3149 0.3256 -0.0458 0.0468  -0.0320 145 GLU   A N   
1086 C CA  . GLU   A 139 ? 0.3649 0.3699 0.3857 -0.0492 0.0530  -0.0363 145 GLU   A CA  
1087 C C   . GLU   A 139 ? 0.3999 0.4052 0.4279 -0.0422 0.0476  -0.0317 145 GLU   A C   
1088 O O   . GLU   A 139 ? 0.4021 0.4087 0.4303 -0.0359 0.0394  -0.0255 145 GLU   A O   
1089 C CB  . GLU   A 139 ? 0.4354 0.4462 0.4428 -0.0619 0.0560  -0.0391 145 GLU   A CB  
1090 C CG  . GLU   A 139 ? 0.5558 0.5738 0.5496 -0.0681 0.0507  -0.0351 145 GLU   A CG  
1091 C CD  . GLU   A 139 ? 0.7059 0.7331 0.6891 -0.0761 0.0464  -0.0303 145 GLU   A CD  
1092 O OE1 . GLU   A 139 ? 0.7311 0.7652 0.7077 -0.0777 0.0392  -0.0231 145 GLU   A OE1 
1093 O OE2 . GLU   A 139 ? 0.7673 0.7955 0.7495 -0.0816 0.0507  -0.0334 145 GLU   A OE2 
1094 N N   . GLU   A 140 ? 0.4252 0.4296 0.4590 -0.0442 0.0530  -0.0353 146 GLU   A N   
1095 C CA  . GLU   A 140 ? 0.4560 0.4616 0.4955 -0.0401 0.0492  -0.0320 146 GLU   A CA  
1096 C C   . GLU   A 140 ? 0.4719 0.4763 0.5195 -0.0300 0.0421  -0.0265 146 GLU   A C   
1097 O O   . GLU   A 140 ? 0.4763 0.4824 0.5259 -0.0269 0.0371  -0.0229 146 GLU   A O   
1098 C CB  . GLU   A 140 ? 0.5039 0.5153 0.5315 -0.0460 0.0450  -0.0288 146 GLU   A CB  
1099 C CG  . GLU   A 140 ? 0.5958 0.6089 0.6258 -0.0411 0.0379  -0.0229 146 GLU   A CG  
1100 C CD  . GLU   A 140 ? 0.7190 0.7319 0.7553 -0.0417 0.0410  -0.0249 146 GLU   A CD  
1101 O OE1 . GLU   A 140 ? 0.7397 0.7551 0.7737 -0.0418 0.0366  -0.0208 146 GLU   A OE1 
1102 O OE2 . GLU   A 140 ? 0.7602 0.7701 0.8049 -0.0419 0.0481  -0.0303 146 GLU   A OE2 
1103 N N   . SER   B 1   ? 0.1771 0.1918 0.1868 0.0056  -0.0121 0.0312  7   SER   C N   
1104 C CA  . SER   B 1   ? 0.1584 0.1739 0.1761 0.0037  -0.0130 0.0307  7   SER   C CA  
1105 C C   . SER   B 1   ? 0.1557 0.1691 0.1741 0.0021  -0.0124 0.0274  7   SER   C C   
1106 O O   . SER   B 1   ? 0.1869 0.1983 0.1994 0.0023  -0.0126 0.0252  7   SER   C O   
1107 C CB  . SER   B 1   ? 0.2013 0.2184 0.2205 0.0038  -0.0173 0.0313  7   SER   C CB  
1108 O OG  . SER   B 1   ? 0.2698 0.2854 0.2833 0.0039  -0.0206 0.0285  7   SER   C OG  
1109 N N   . GLY   B 2   ? 0.1593 0.1726 0.1845 0.0008  -0.0113 0.0271  8   GLY   C N   
1110 C CA  . GLY   B 2   ? 0.1546 0.1657 0.1806 -0.0002 -0.0102 0.0248  8   GLY   C CA  
1111 C C   . GLY   B 2   ? 0.1313 0.1417 0.1624 -0.0005 -0.0070 0.0252  8   GLY   C C   
1112 O O   . GLY   B 2   ? 0.1447 0.1559 0.1776 0.0001  -0.0055 0.0263  8   GLY   C O   
1113 N N   . ALA   B 3   ? 0.1266 0.1351 0.1601 -0.0012 -0.0058 0.0242  9   ALA   C N   
1114 C CA  . ALA   B 3   ? 0.1307 0.1376 0.1675 -0.0008 -0.0023 0.0245  9   ALA   C CA  
1115 C C   . ALA   B 3   ? 0.1175 0.1209 0.1512 -0.0004 0.0001  0.0231  9   ALA   C C   
1116 O O   . ALA   B 3   ? 0.1386 0.1411 0.1703 -0.0009 -0.0011 0.0221  9   ALA   C O   
1117 C CB  . ALA   B 3   ? 0.1505 0.1590 0.1962 -0.0015 -0.0021 0.0263  9   ALA   C CB  
1118 N N   . ILE   B 4   ? 0.1209 0.1220 0.1543 0.0009  0.0034  0.0230  10  ILE   C N   
1119 C CA  . ILE   B 4   ? 0.1262 0.1235 0.1568 0.0020  0.0065  0.0225  10  ILE   C CA  
1120 C C   . ILE   B 4   ? 0.1218 0.1184 0.1595 0.0020  0.0097  0.0244  10  ILE   C C   
1121 O O   . ILE   B 4   ? 0.1352 0.1327 0.1766 0.0023  0.0107  0.0252  10  ILE   C O   
1122 C CB  . ILE   B 4   ? 0.1218 0.1165 0.1451 0.0043  0.0081  0.0211  10  ILE   C CB  
1123 C CG1 . ILE   B 4   ? 0.1411 0.1372 0.1598 0.0044  0.0051  0.0195  10  ILE   C CG1 
1124 C CG2 . ILE   B 4   ? 0.1579 0.1482 0.1766 0.0061  0.0112  0.0211  10  ILE   C CG2 
1125 C CD1 . ILE   B 4   ? 0.1461 0.1403 0.1603 0.0066  0.0057  0.0177  10  ILE   C CD1 
1126 N N   . TYR   B 5   ? 0.1296 0.1242 0.1704 0.0018  0.0117  0.0251  11  TYR   C N   
1127 C CA  . TYR   B 5   ? 0.1371 0.1307 0.1861 0.0019  0.0155  0.0273  11  TYR   C CA  
1128 C C   . TYR   B 5   ? 0.1401 0.1286 0.1843 0.0044  0.0210  0.0280  11  TYR   C C   
1129 O O   . TYR   B 5   ? 0.1650 0.1515 0.2084 0.0044  0.0218  0.0281  11  TYR   C O   
1130 C CB  . TYR   B 5   ? 0.1490 0.1449 0.2086 -0.0006 0.0133  0.0280  11  TYR   C CB  
1131 C CG  . TYR   B 5   ? 0.1366 0.1373 0.2001 -0.0024 0.0079  0.0277  11  TYR   C CG  
1132 C CD1 . TYR   B 5   ? 0.1410 0.1440 0.2117 -0.0025 0.0082  0.0293  11  TYR   C CD1 
1133 C CD2 . TYR   B 5   ? 0.1534 0.1559 0.2124 -0.0033 0.0028  0.0259  11  TYR   C CD2 
1134 C CE1 . TYR   B 5   ? 0.1517 0.1589 0.2251 -0.0036 0.0034  0.0295  11  TYR   C CE1 
1135 C CE2 . TYR   B 5   ? 0.1681 0.1744 0.2287 -0.0041 -0.0018 0.0260  11  TYR   C CE2 
1136 C CZ  . TYR   B 5   ? 0.1583 0.1669 0.2261 -0.0042 -0.0016 0.0280  11  TYR   C CZ  
1137 O OH  . TYR   B 5   ? 0.1838 0.1960 0.2525 -0.0045 -0.0059 0.0286  11  TYR   C OH  
1138 N N   . VAL   B 6   ? 0.1639 0.1498 0.2036 0.0070  0.0246  0.0283  12  VAL   C N   
1139 C CA  . VAL   B 6   ? 0.1699 0.1503 0.2026 0.0105  0.0301  0.0292  12  VAL   C CA  
1140 C C   . VAL   B 6   ? 0.1756 0.1539 0.2130 0.0122  0.0357  0.0314  12  VAL   C C   
1141 O O   . VAL   B 6   ? 0.1645 0.1443 0.2037 0.0122  0.0352  0.0309  12  VAL   C O   
1142 C CB  . VAL   B 6   ? 0.1991 0.1774 0.2186 0.0131  0.0284  0.0265  12  VAL   C CB  
1143 C CG1 . VAL   B 6   ? 0.2041 0.1845 0.2229 0.0131  0.0259  0.0246  12  VAL   C CG1 
1144 C CG2 . VAL   B 6   ? 0.2185 0.1908 0.2290 0.0174  0.0334  0.0274  12  VAL   C CG2 
1145 N N   . GLY   B 7   ? 0.1924 0.1673 0.2331 0.0136  0.0418  0.0343  13  GLY   C N   
1146 C CA  . GLY   B 7   ? 0.2002 0.1730 0.2464 0.0154  0.0480  0.0369  13  GLY   C CA  
1147 C C   . GLY   B 7   ? 0.1941 0.1718 0.2539 0.0123  0.0459  0.0375  13  GLY   C C   
1148 O O   . GLY   B 7   ? 0.1976 0.1797 0.2666 0.0087  0.0414  0.0374  13  GLY   C O   
1149 N N   . ASN   B 8   ? 0.1823 0.1596 0.2425 0.0138  0.0482  0.0377  14  ASN   C N   
1150 C CA  . ASN   B 8   ? 0.1733 0.1555 0.2461 0.0111  0.0458  0.0383  14  ASN   C CA  
1151 C C   . ASN   B 8   ? 0.1564 0.1415 0.2239 0.0103  0.0400  0.0353  14  ASN   C C   
1152 O O   . ASN   B 8   ? 0.1561 0.1431 0.2294 0.0100  0.0400  0.0357  14  ASN   C O   
1153 C CB  . ASN   B 8   ? 0.2071 0.1874 0.2881 0.0129  0.0528  0.0412  14  ASN   C CB  
1154 C CG  . ASN   B 8   ? 0.2797 0.2590 0.3720 0.0125  0.0577  0.0447  14  ASN   C CG  
1155 O OD1 . ASN   B 8   ? 0.3121 0.2958 0.4196 0.0094  0.0552  0.0460  14  ASN   C OD1 
1156 N ND2 . ASN   B 8   ? 0.3225 0.2961 0.4076 0.0158  0.0640  0.0462  14  ASN   C ND2 
1157 N N   . TYR   B 9   ? 0.1375 0.1232 0.1961 0.0097  0.0352  0.0328  15  TYR   C N   
1158 C CA  . TYR   B 9   ? 0.1366 0.1250 0.1912 0.0089  0.0301  0.0303  15  TYR   C CA  
1159 C C   . TYR   B 9   ? 0.1314 0.1242 0.1877 0.0058  0.0240  0.0298  15  TYR   C C   
1160 O O   . TYR   B 9   ? 0.1436 0.1359 0.1982 0.0051  0.0231  0.0297  15  TYR   C O   
1161 C CB  . TYR   B 9   ? 0.1579 0.1425 0.1991 0.0118  0.0303  0.0274  15  TYR   C CB  
1162 C CG  . TYR   B 9   ? 0.1660 0.1455 0.2024 0.0156  0.0358  0.0272  15  TYR   C CG  
1163 C CD1 . TYR   B 9   ? 0.1881 0.1679 0.2296 0.0160  0.0373  0.0272  15  TYR   C CD1 
1164 C CD2 . TYR   B 9   ? 0.1992 0.1732 0.2250 0.0192  0.0393  0.0269  15  TYR   C CD2 
1165 C CE1 . TYR   B 9   ? 0.2367 0.2112 0.2727 0.0199  0.0426  0.0266  15  TYR   C CE1 
1166 C CE2 . TYR   B 9   ? 0.2394 0.2080 0.2586 0.0234  0.0443  0.0265  15  TYR   C CE2 
1167 C CZ  . TYR   B 9   ? 0.2729 0.2418 0.2970 0.0237  0.0458  0.0261  15  TYR   C CZ  
1168 O OH  . TYR   B 9   ? 0.3441 0.3073 0.3613 0.0282  0.0509  0.0253  15  TYR   C OH  
1169 N N   . ARG   B 10  ? 0.1176 0.1142 0.1769 0.0044  0.0201  0.0294  16  ARG   C N   
1170 C CA  . ARG   B 10  ? 0.1156 0.1159 0.1741 0.0024  0.0145  0.0288  16  ARG   C CA  
1171 C C   . ARG   B 10  ? 0.1082 0.1086 0.1604 0.0032  0.0129  0.0269  16  ARG   C C   
1172 O O   . ARG   B 10  ? 0.1196 0.1204 0.1748 0.0038  0.0137  0.0271  16  ARG   C O   
1173 C CB  . ARG   B 10  ? 0.1201 0.1248 0.1888 0.0004  0.0117  0.0308  16  ARG   C CB  
1174 C CG  . ARG   B 10  ? 0.1338 0.1421 0.2006 -0.0007 0.0063  0.0306  16  ARG   C CG  
1175 C CD  . ARG   B 10  ? 0.1325 0.1447 0.2086 -0.0020 0.0032  0.0327  16  ARG   C CD  
1176 N NE  . ARG   B 10  ? 0.1374 0.1527 0.2127 -0.0020 -0.0001 0.0337  16  ARG   C NE  
1177 C CZ  . ARG   B 10  ? 0.1453 0.1623 0.2159 -0.0022 -0.0043 0.0336  16  ARG   C CZ  
1178 N NH1 . ARG   B 10  ? 0.1739 0.1901 0.2399 -0.0027 -0.0064 0.0317  16  ARG   C NH1 
1179 N NH2 . ARG   B 10  ? 0.1553 0.1746 0.2254 -0.0015 -0.0060 0.0353  16  ARG   C NH2 
1180 N N   . VAL   B 11  ? 0.1100 0.1101 0.1549 0.0032  0.0106  0.0252  17  VAL   C N   
1181 C CA  . VAL   B 11  ? 0.1042 0.1046 0.1447 0.0039  0.0089  0.0234  17  VAL   C CA  
1182 C C   . VAL   B 11  ? 0.1105 0.1145 0.1522 0.0024  0.0054  0.0242  17  VAL   C C   
1183 O O   . VAL   B 11  ? 0.1200 0.1244 0.1587 0.0016  0.0036  0.0242  17  VAL   C O   
1184 C CB  . VAL   B 11  ? 0.1197 0.1167 0.1511 0.0057  0.0093  0.0209  17  VAL   C CB  
1185 C CG1 . VAL   B 11  ? 0.1430 0.1404 0.1725 0.0064  0.0075  0.0187  17  VAL   C CG1 
1186 C CG2 . VAL   B 11  ? 0.1406 0.1332 0.1685 0.0079  0.0132  0.0205  17  VAL   C CG2 
1187 N N   . VAL   B 12  ? 0.0999 0.1062 0.1455 0.0022  0.0046  0.0251  18  VAL   C N   
1188 C CA  A VAL   B 12  ? 0.0963 0.1056 0.1423 0.0014  0.0020  0.0266  18  VAL   C CA  
1189 C CA  B VAL   B 12  ? 0.1212 0.1306 0.1673 0.0014  0.0019  0.0266  18  VAL   C CA  
1190 C C   . VAL   B 12  ? 0.1070 0.1169 0.1537 0.0021  0.0021  0.0262  18  VAL   C C   
1191 O O   . VAL   B 12  ? 0.1151 0.1234 0.1638 0.0028  0.0035  0.0245  18  VAL   C O   
1192 C CB  A VAL   B 12  ? 0.0921 0.1044 0.1446 0.0007  0.0008  0.0296  18  VAL   C CB  
1193 C CB  B VAL   B 12  ? 0.1719 0.1841 0.2251 0.0006  0.0011  0.0296  18  VAL   C CB  
1194 C CG1 A VAL   B 12  ? 0.1059 0.1185 0.1589 -0.0002 -0.0006 0.0299  18  VAL   C CG1 
1195 C CG1 B VAL   B 12  ? 0.1822 0.1972 0.2345 0.0005  -0.0018 0.0315  18  VAL   C CG1 
1196 C CG2 A VAL   B 12  ? 0.0608 0.0734 0.1207 0.0010  0.0029  0.0307  18  VAL   C CG2 
1197 C CG2 B VAL   B 12  ? 0.2087 0.2204 0.2644 -0.0001 0.0012  0.0298  18  VAL   C CG2 
1198 N N   . ASN   B 13  ? 0.1040 0.1159 0.1498 0.0019  0.0007  0.0276  19  ASN   C N   
1199 C CA  . ASN   B 13  ? 0.0976 0.1105 0.1469 0.0025  0.0014  0.0280  19  ASN   C CA  
1200 C C   . ASN   B 13  ? 0.1034 0.1175 0.1608 0.0024  0.0025  0.0302  19  ASN   C C   
1201 O O   . ASN   B 13  ? 0.1014 0.1172 0.1608 0.0021  0.0018  0.0329  19  ASN   C O   
1202 C CB  . ASN   B 13  ? 0.0982 0.1129 0.1454 0.0028  0.0007  0.0303  19  ASN   C CB  
1203 C CG  . ASN   B 13  ? 0.1037 0.1171 0.1435 0.0030  -0.0001 0.0284  19  ASN   C CG  
1204 O OD1 . ASN   B 13  ? 0.1188 0.1320 0.1534 0.0027  -0.0014 0.0282  19  ASN   C OD1 
1205 N ND2 . ASN   B 13  ? 0.1181 0.1308 0.1585 0.0035  0.0006  0.0266  19  ASN   C ND2 
1206 N N   . ARG   B 14  ? 0.0963 0.1094 0.1588 0.0028  0.0038  0.0288  20  ARG   C N   
1207 C CA  . ARG   B 14  ? 0.0989 0.1129 0.1698 0.0028  0.0052  0.0307  20  ARG   C CA  
1208 C C   . ARG   B 14  ? 0.1019 0.1189 0.1762 0.0029  0.0051  0.0354  20  ARG   C C   
1209 O O   . ARG   B 14  ? 0.1037 0.1221 0.1823 0.0029  0.0052  0.0382  20  ARG   C O   
1210 C CB  . ARG   B 14  ? 0.1053 0.1177 0.1815 0.0033  0.0062  0.0280  20  ARG   C CB  
1211 C CG  . ARG   B 14  ? 0.1072 0.1196 0.1922 0.0034  0.0080  0.0291  20  ARG   C CG  
1212 C CD  . ARG   B 14  ? 0.1038 0.1143 0.1944 0.0039  0.0084  0.0257  20  ARG   C CD  
1213 N NE  . ARG   B 14  ? 0.1057 0.1153 0.2048 0.0042  0.0103  0.0257  20  ARG   C NE  
1214 C CZ  . ARG   B 14  ? 0.0930 0.1044 0.2016 0.0040  0.0117  0.0293  20  ARG   C CZ  
1215 N NH1 . ARG   B 14  ? 0.1214 0.1357 0.2315 0.0037  0.0118  0.0337  20  ARG   C NH1 
1216 N NH2 . ARG   B 14  ? 0.1095 0.1195 0.2260 0.0043  0.0134  0.0285  20  ARG   C NH2 
1217 N N   . HIS   B 15  ? 0.1004 0.1183 0.1721 0.0033  0.0049  0.0368  21  HIS   C N   
1218 C CA  . HIS   B 15  ? 0.1142 0.1345 0.1878 0.0042  0.0053  0.0418  21  HIS   C CA  
1219 C C   . HIS   B 15  ? 0.1124 0.1340 0.1800 0.0045  0.0029  0.0439  21  HIS   C C   
1220 O O   . HIS   B 15  ? 0.1413 0.1647 0.2097 0.0058  0.0028  0.0481  21  HIS   C O   
1221 C CB  . HIS   B 15  ? 0.1256 0.1460 0.1988 0.0051  0.0069  0.0431  21  HIS   C CB  
1222 C CG  . HIS   B 15  ? 0.1155 0.1354 0.1790 0.0054  0.0057  0.0420  21  HIS   C CG  
1223 N ND1 . HIS   B 15  ? 0.1213 0.1396 0.1816 0.0047  0.0050  0.0376  21  HIS   C ND1 
1224 C CD2 . HIS   B 15  ? 0.1256 0.1462 0.1819 0.0067  0.0051  0.0446  21  HIS   C CD2 
1225 C CE1 . HIS   B 15  ? 0.1361 0.1543 0.1883 0.0053  0.0043  0.0378  21  HIS   C CE1 
1226 N NE2 . HIS   B 15  ? 0.1294 0.1488 0.1787 0.0065  0.0043  0.0418  21  HIS   C NE2 
1227 N N   . LEU   B 16  ? 0.1013 0.1220 0.1638 0.0036  0.0009  0.0411  22  LEU   C N   
1228 C CA  . LEU   B 16  ? 0.1180 0.1399 0.1767 0.0036  -0.0021 0.0421  22  LEU   C CA  
1229 C C   . LEU   B 16  ? 0.1223 0.1445 0.1868 0.0026  -0.0027 0.0417  22  LEU   C C   
1230 O O   . LEU   B 16  ? 0.1342 0.1575 0.1978 0.0023  -0.0056 0.0419  22  LEU   C O   
1231 C CB  . LEU   B 16  ? 0.1190 0.1396 0.1687 0.0034  -0.0039 0.0396  22  LEU   C CB  
1232 C CG  . LEU   B 16  ? 0.1334 0.1538 0.1773 0.0047  -0.0030 0.0404  22  LEU   C CG  
1233 C CD1 . LEU   B 16  ? 0.1515 0.1703 0.1870 0.0045  -0.0046 0.0375  22  LEU   C CD1 
1234 C CD2 . LEU   B 16  ? 0.1522 0.1742 0.1946 0.0067  -0.0035 0.0448  22  LEU   C CD2 
1235 N N   . ALA   B 17  ? 0.1245 0.1456 0.1953 0.0022  0.0000  0.0407  23  ALA   C N   
1236 C CA  . ALA   B 17  ? 0.1166 0.1375 0.1930 0.0016  0.0005  0.0404  23  ALA   C CA  
1237 C C   . ALA   B 17  ? 0.1219 0.1458 0.2043 0.0019  -0.0013 0.0442  23  ALA   C C   
1238 O O   . ALA   B 17  ? 0.1354 0.1610 0.2199 0.0030  -0.0013 0.0474  23  ALA   C O   
1239 C CB  . ALA   B 17  ? 0.1359 0.1546 0.2167 0.0018  0.0040  0.0387  23  ALA   C CB  
1240 N N   . THR   B 18  ? 0.1271 0.1518 0.2131 0.0012  -0.0026 0.0441  24  THR   C N   
1241 C CA  . THR   B 18  ? 0.1301 0.1578 0.2229 0.0016  -0.0052 0.0474  24  THR   C CA  
1242 C C   . THR   B 18  ? 0.1170 0.1447 0.2203 0.0016  -0.0019 0.0487  24  THR   C C   
1243 O O   . THR   B 18  ? 0.1234 0.1485 0.2280 0.0014  0.0021  0.0467  24  THR   C O   
1244 C CB  . THR   B 18  ? 0.1365 0.1652 0.2298 0.0007  -0.0088 0.0463  24  THR   C CB  
1245 O OG1 . THR   B 18  ? 0.1416 0.1682 0.2391 -0.0004 -0.0056 0.0443  24  THR   C OG1 
1246 C CG2 . THR   B 18  ? 0.1583 0.1863 0.2411 0.0007  -0.0120 0.0443  24  THR   C CG2 
1247 N N   . HIS   B 19  ? 0.1343 0.1651 0.2454 0.0022  -0.0039 0.0522  25  HIS   C N   
1248 C CA  . HIS   B 19  ? 0.1355 0.1665 0.2577 0.0022  -0.0009 0.0537  25  HIS   C CA  
1249 C C   . HIS   B 19  ? 0.1073 0.1364 0.2327 0.0012  0.0016  0.0511  25  HIS   C C   
1250 O O   . HIS   B 19  ? 0.1351 0.1615 0.2637 0.0015  0.0064  0.0502  25  HIS   C O   
1251 C CB  . HIS   B 19  ? 0.1460 0.1810 0.2765 0.0030  -0.0044 0.0578  25  HIS   C CB  
1252 C CG  . HIS   B 19  ? 0.1441 0.1795 0.2875 0.0030  -0.0015 0.0592  25  HIS   C CG  
1253 N ND1 . HIS   B 19  ? 0.1682 0.2021 0.3165 0.0036  0.0033  0.0601  25  HIS   C ND1 
1254 C CD2 . HIS   B 19  ? 0.1673 0.2037 0.3192 0.0022  -0.0017 0.0591  25  HIS   C CD2 
1255 C CE1 . HIS   B 19  ? 0.1609 0.1954 0.3204 0.0036  0.0053  0.0612  25  HIS   C CE1 
1256 N NE2 . HIS   B 19  ? 0.1617 0.1977 0.3240 0.0027  0.0028  0.0607  25  HIS   C NE2 
1257 N N   . ASN   B 20  ? 0.1193 0.1490 0.2433 0.0002  -0.0013 0.0499  26  ASN   C N   
1258 C CA  . ASN   B 20  ? 0.1333 0.1607 0.2609 -0.0005 0.0020  0.0482  26  ASN   C CA  
1259 C C   . ASN   B 20  ? 0.1225 0.1453 0.2419 -0.0001 0.0067  0.0452  26  ASN   C C   
1260 O O   . ASN   B 20  ? 0.1214 0.1414 0.2437 0.0004  0.0116  0.0445  26  ASN   C O   
1261 C CB  . ASN   B 20  ? 0.1583 0.1869 0.2867 -0.0017 -0.0019 0.0473  26  ASN   C CB  
1262 C CG  . ASN   B 20  ? 0.2339 0.2603 0.3689 -0.0023 0.0023  0.0465  26  ASN   C CG  
1263 O OD1 . ASN   B 20  ? 0.2667 0.2943 0.4138 -0.0022 0.0044  0.0486  26  ASN   C OD1 
1264 N ND2 . ASN   B 20  ? 0.2546 0.2777 0.3822 -0.0026 0.0044  0.0440  26  ASN   C ND2 
1265 N N   . ASP   B 21  ? 0.1105 0.1322 0.2192 0.0000  0.0053  0.0433  27  ASP   C N   
1266 C CA  . ASP   B 21  ? 0.1134 0.1311 0.2146 0.0006  0.0088  0.0403  27  ASP   C CA  
1267 C C   . ASP   B 21  ? 0.1066 0.1224 0.2114 0.0018  0.0127  0.0400  27  ASP   C C   
1268 O O   . ASP   B 21  ? 0.1190 0.1310 0.2219 0.0028  0.0167  0.0380  27  ASP   C O   
1269 C CB  . ASP   B 21  ? 0.1122 0.1296 0.2036 0.0006  0.0064  0.0387  27  ASP   C CB  
1270 C CG  . ASP   B 21  ? 0.1255 0.1432 0.2109 -0.0002 0.0034  0.0376  27  ASP   C CG  
1271 O OD1 . ASP   B 21  ? 0.1424 0.1585 0.2285 -0.0006 0.0047  0.0367  27  ASP   C OD1 
1272 O OD2 . ASP   B 21  ? 0.1312 0.1504 0.2116 -0.0003 0.0002  0.0379  27  ASP   C OD2 
1273 N N   . TRP   B 22  ? 0.1034 0.1215 0.2130 0.0020  0.0116  0.0422  28  TRP   C N   
1274 C CA  . TRP   B 22  ? 0.1079 0.1241 0.2220 0.0030  0.0151  0.0417  28  TRP   C CA  
1275 C C   . TRP   B 22  ? 0.1057 0.1211 0.2285 0.0036  0.0187  0.0429  28  TRP   C C   
1276 O O   . TRP   B 22  ? 0.1230 0.1348 0.2459 0.0048  0.0227  0.0408  28  TRP   C O   
1277 C CB  . TRP   B 22  ? 0.1095 0.1284 0.2281 0.0031  0.0135  0.0444  28  TRP   C CB  
1278 C CG  . TRP   B 22  ? 0.1157 0.1340 0.2278 0.0031  0.0123  0.0428  28  TRP   C CG  
1279 C CD1 . TRP   B 22  ? 0.1341 0.1546 0.2410 0.0028  0.0092  0.0442  28  TRP   C CD1 
1280 C CD2 . TRP   B 22  ? 0.0918 0.1070 0.2023 0.0037  0.0142  0.0393  28  TRP   C CD2 
1281 N NE1 . TRP   B 22  ? 0.1282 0.1473 0.2317 0.0030  0.0096  0.0423  28  TRP   C NE1 
1282 C CE2 . TRP   B 22  ? 0.1149 0.1310 0.2213 0.0034  0.0123  0.0392  28  TRP   C CE2 
1283 C CE3 . TRP   B 22  ? 0.1300 0.1416 0.2430 0.0046  0.0173  0.0362  28  TRP   C CE3 
1284 C CZ2 . TRP   B 22  ? 0.1088 0.1228 0.2150 0.0038  0.0130  0.0361  28  TRP   C CZ2 
1285 C CZ3 . TRP   B 22  ? 0.1469 0.1561 0.2583 0.0051  0.0174  0.0326  28  TRP   C CZ3 
1286 C CH2 . TRP   B 22  ? 0.1347 0.1453 0.2436 0.0045  0.0151  0.0326  28  TRP   C CH2 
1287 N N   . ALA   B 23  ? 0.1087 0.1271 0.2379 0.0028  0.0172  0.0457  29  ALA   C N   
1288 C CA  . ALA   B 23  ? 0.1072 0.1253 0.2465 0.0033  0.0208  0.0473  29  ALA   C CA  
1289 C C   . ALA   B 23  ? 0.1273 0.1412 0.2628 0.0040  0.0252  0.0451  29  ALA   C C   
1290 O O   . ALA   B 23  ? 0.1427 0.1551 0.2853 0.0049  0.0299  0.0461  29  ALA   C O   
1291 C CB  . ALA   B 23  ? 0.1299 0.1529 0.2790 0.0023  0.0171  0.0509  29  ALA   C CB  
1292 N N   . ASN   B 24  ? 0.1294 0.1412 0.2539 0.0038  0.0242  0.0425  30  ASN   C N   
1293 C CA  . ASN   B 24  ? 0.1271 0.1346 0.2460 0.0048  0.0283  0.0407  30  ASN   C CA  
1294 C C   . ASN   B 24  ? 0.1354 0.1390 0.2408 0.0061  0.0286  0.0368  30  ASN   C C   
1295 O O   . ASN   B 24  ? 0.1399 0.1411 0.2372 0.0065  0.0290  0.0353  30  ASN   C O   
1296 C CB  . ASN   B 24  ? 0.1447 0.1542 0.2655 0.0033  0.0260  0.0418  30  ASN   C CB  
1297 C CG  . ASN   B 24  ? 0.1512 0.1640 0.2866 0.0023  0.0258  0.0451  30  ASN   C CG  
1298 O OD1 . ASN   B 24  ? 0.1843 0.1952 0.3269 0.0033  0.0313  0.0465  30  ASN   C OD1 
1299 N ND2 . ASN   B 24  ? 0.1611 0.1790 0.3020 0.0008  0.0198  0.0467  30  ASN   C ND2 
1300 N N   . LEU   B 25  ? 0.1403 0.1432 0.2443 0.0068  0.0282  0.0352  31  LEU   C N   
1301 C CA  . LEU   B 25  ? 0.1351 0.1351 0.2283 0.0078  0.0271  0.0313  31  LEU   C CA  
1302 C C   . LEU   B 25  ? 0.1522 0.1463 0.2367 0.0106  0.0311  0.0283  31  LEU   C C   
1303 O O   . LEU   B 25  ? 0.1658 0.1568 0.2527 0.0125  0.0358  0.0283  31  LEU   C O   
1304 C CB  . LEU   B 25  ? 0.1485 0.1493 0.2458 0.0079  0.0260  0.0304  31  LEU   C CB  
1305 C CG  . LEU   B 25  ? 0.1477 0.1463 0.2370 0.0085  0.0240  0.0263  31  LEU   C CG  
1306 C CD1 . LEU   B 25  ? 0.1476 0.1489 0.2320 0.0070  0.0198  0.0266  31  LEU   C CD1 
1307 C CD2 . LEU   B 25  ? 0.1707 0.1694 0.2663 0.0087  0.0237  0.0253  31  LEU   C CD2 
1308 N N   . VAL   B 26  ? 0.1378 0.1299 0.2116 0.0112  0.0294  0.0257  32  VAL   C N   
1309 C CA  . VAL   B 26  ? 0.1494 0.1354 0.2124 0.0145  0.0323  0.0224  32  VAL   C CA  
1310 C C   . VAL   B 26  ? 0.1548 0.1392 0.2122 0.0155  0.0292  0.0179  32  VAL   C C   
1311 O O   . VAL   B 26  ? 0.1918 0.1717 0.2451 0.0184  0.0310  0.0146  32  VAL   C O   
1312 C CB  . VAL   B 26  ? 0.1650 0.1496 0.2203 0.0149  0.0328  0.0230  32  VAL   C CB  
1313 C CG1 . VAL   B 26  ? 0.1986 0.1768 0.2408 0.0189  0.0351  0.0197  32  VAL   C CG1 
1314 C CG2 . VAL   B 26  ? 0.1704 0.1562 0.2334 0.0140  0.0362  0.0271  32  VAL   C CG2 
1315 N N   . TRP   B 27  ? 0.1420 0.1298 0.1995 0.0135  0.0243  0.0173  33  TRP   C N   
1316 C CA  . TRP   B 27  ? 0.1492 0.1359 0.2032 0.0142  0.0210  0.0130  33  TRP   C CA  
1317 C C   . TRP   B 27  ? 0.1398 0.1316 0.1991 0.0113  0.0170  0.0145  33  TRP   C C   
1318 O O   . TRP   B 27  ? 0.1429 0.1377 0.2023 0.0096  0.0161  0.0175  33  TRP   C O   
1319 C CB  . TRP   B 27  ? 0.1677 0.1500 0.2086 0.0169  0.0204  0.0095  33  TRP   C CB  
1320 C CG  . TRP   B 27  ? 0.1746 0.1566 0.2124 0.0175  0.0157  0.0051  33  TRP   C CG  
1321 C CD1 . TRP   B 27  ? 0.2058 0.1846 0.2424 0.0196  0.0142  0.0001  33  TRP   C CD1 
1322 C CD2 . TRP   B 27  ? 0.1629 0.1476 0.1990 0.0160  0.0119  0.0050  33  TRP   C CD2 
1323 N NE1 . TRP   B 27  ? 0.2184 0.1982 0.2539 0.0193  0.0093  -0.0030 33  TRP   C NE1 
1324 C CE2 . TRP   B 27  ? 0.1932 0.1764 0.2280 0.0172  0.0082  0.0001  33  TRP   C CE2 
1325 C CE3 . TRP   B 27  ? 0.1616 0.1494 0.1973 0.0139  0.0112  0.0082  33  TRP   C CE3 
1326 C CZ2 . TRP   B 27  ? 0.1814 0.1666 0.2152 0.0165  0.0043  -0.0011 33  TRP   C CZ2 
1327 C CZ3 . TRP   B 27  ? 0.1677 0.1570 0.2010 0.0133  0.0076  0.0069  33  TRP   C CZ3 
1328 C CH2 . TRP   B 27  ? 0.1734 0.1618 0.2068 0.0145  0.0044  0.0026  33  TRP   C CH2 
1329 N N   . GLU   B 28  ? 0.1288 0.1212 0.1925 0.0111  0.0149  0.0124  34  GLU   C N   
1330 C CA  . GLU   B 28  ? 0.1407 0.1374 0.2092 0.0089  0.0120  0.0140  34  GLU   C CA  
1331 C C   . GLU   B 28  ? 0.1403 0.1359 0.2104 0.0095  0.0095  0.0098  34  GLU   C C   
1332 O O   . GLU   B 28  ? 0.1497 0.1420 0.2213 0.0111  0.0099  0.0061  34  GLU   C O   
1333 C CB  . GLU   B 28  ? 0.1468 0.1475 0.2251 0.0071  0.0128  0.0188  34  GLU   C CB  
1334 C CG  . GLU   B 28  ? 0.1541 0.1539 0.2410 0.0076  0.0149  0.0187  34  GLU   C CG  
1335 C CD  . GLU   B 28  ? 0.1653 0.1651 0.2591 0.0075  0.0137  0.0166  34  GLU   C CD  
1336 O OE1 . GLU   B 28  ? 0.2014 0.1988 0.3004 0.0085  0.0153  0.0145  34  GLU   C OE1 
1337 O OE2 . GLU   B 28  ? 0.1598 0.1619 0.2553 0.0065  0.0117  0.0174  34  GLU   C OE2 
1338 N N   . ASP   B 29  ? 0.1302 0.1282 0.2007 0.0084  0.0070  0.0102  35  ASP   C N   
1339 C CA  . ASP   B 29  ? 0.1309 0.1285 0.2056 0.0087  0.0045  0.0065  35  ASP   C CA  
1340 C C   . ASP   B 29  ? 0.1246 0.1264 0.2056 0.0069  0.0038  0.0099  35  ASP   C C   
1341 O O   . ASP   B 29  ? 0.1237 0.1269 0.1992 0.0064  0.0028  0.0112  35  ASP   C O   
1342 C CB  . ASP   B 29  ? 0.1537 0.1480 0.2185 0.0108  0.0020  0.0015  35  ASP   C CB  
1343 C CG  . ASP   B 29  ? 0.1847 0.1784 0.2538 0.0114  -0.0017 -0.0032 35  ASP   C CG  
1344 O OD1 . ASP   B 29  ? 0.1873 0.1841 0.2660 0.0097  -0.0023 -0.0016 35  ASP   C OD1 
1345 O OD2 . ASP   B 29  ? 0.2309 0.2208 0.2933 0.0139  -0.0040 -0.0084 35  ASP   C OD2 
1346 N N   . SER   B 30  ? 0.1254 0.1289 0.2180 0.0061  0.0047  0.0115  36  SER   C N   
1347 C CA  A SER   B 30  ? 0.1208 0.1278 0.2199 0.0049  0.0052  0.0154  36  SER   C CA  
1348 C CA  B SER   B 30  ? 0.1286 0.1356 0.2272 0.0049  0.0052  0.0155  36  SER   C CA  
1349 C C   . SER   B 30  ? 0.1272 0.1344 0.2262 0.0050  0.0029  0.0127  36  SER   C C   
1350 O O   . SER   B 30  ? 0.1280 0.1375 0.2254 0.0045  0.0033  0.0159  36  SER   C O   
1351 C CB  A SER   B 30  ? 0.1215 0.1294 0.2339 0.0044  0.0071  0.0175  36  SER   C CB  
1352 C CB  B SER   B 30  ? 0.1502 0.1585 0.2615 0.0044  0.0073  0.0183  36  SER   C CB  
1353 O OG  A SER   B 30  ? 0.1179 0.1285 0.2371 0.0038  0.0081  0.0210  36  SER   C OG  
1354 O OG  B SER   B 30  ? 0.1647 0.1705 0.2833 0.0048  0.0064  0.0134  36  SER   C OG  
1355 N N   . SER   B 31  ? 0.1237 0.1283 0.2240 0.0060  0.0003  0.0068  37  SER   C N   
1356 C CA  . SER   B 31  ? 0.1323 0.1373 0.2343 0.0062  -0.0025 0.0040  37  SER   C CA  
1357 C C   . SER   B 31  ? 0.1179 0.1230 0.2076 0.0066  -0.0035 0.0044  37  SER   C C   
1358 O O   . SER   B 31  ? 0.1318 0.1385 0.2236 0.0064  -0.0045 0.0045  37  SER   C O   
1359 C CB  . SER   B 31  ? 0.1787 0.1808 0.2838 0.0075  -0.0061 -0.0031 37  SER   C CB  
1360 O OG  . SER   B 31  ? 0.2345 0.2331 0.3265 0.0095  -0.0083 -0.0072 37  SER   C OG  
1361 N N   . ARG   B 32  ? 0.1140 0.1176 0.1924 0.0071  -0.0027 0.0051  38  ARG   C N   
1362 C CA  . ARG   B 32  ? 0.1143 0.1178 0.1818 0.0075  -0.0033 0.0057  38  ARG   C CA  
1363 C C   . ARG   B 32  ? 0.1133 0.1193 0.1786 0.0061  -0.0010 0.0112  38  ARG   C C   
1364 O O   . ARG   B 32  ? 0.1130 0.1190 0.1704 0.0062  -0.0013 0.0120  38  ARG   C O   
1365 C CB  . ARG   B 32  ? 0.1422 0.1419 0.1990 0.0092  -0.0037 0.0030  38  ARG   C CB  
1366 C CG  . ARG   B 32  ? 0.1612 0.1576 0.2168 0.0115  -0.0068 -0.0030 38  ARG   C CG  
1367 C CD  . ARG   B 32  ? 0.1367 0.1288 0.1802 0.0140  -0.0064 -0.0052 38  ARG   C CD  
1368 N NE  . ARG   B 32  ? 0.1363 0.1279 0.1699 0.0146  -0.0063 -0.0037 38  ARG   C NE  
1369 C CZ  . ARG   B 32  ? 0.1380 0.1256 0.1605 0.0176  -0.0069 -0.0061 38  ARG   C CZ  
1370 N NH1 . ARG   B 32  ? 0.1624 0.1459 0.1806 0.0204  -0.0079 -0.0101 38  ARG   C NH1 
1371 N NH2 . ARG   B 32  ? 0.1538 0.1412 0.1690 0.0180  -0.0066 -0.0044 38  ARG   C NH2 
1372 N N   . ASP   B 33  ? 0.1059 0.1139 0.1778 0.0051  0.0012  0.0150  39  ASP   C N   
1373 C CA  . ASP   B 33  ? 0.1011 0.1112 0.1701 0.0043  0.0027  0.0198  39  ASP   C CA  
1374 C C   . ASP   B 33  ? 0.0983 0.1068 0.1588 0.0044  0.0025  0.0195  39  ASP   C C   
1375 O O   . ASP   B 33  ? 0.1033 0.1129 0.1587 0.0039  0.0024  0.0218  39  ASP   C O   
1376 C CB  . ASP   B 33  ? 0.0996 0.1116 0.1670 0.0041  0.0028  0.0223  39  ASP   C CB  
1377 C CG  . ASP   B 33  ? 0.1139 0.1278 0.1780 0.0038  0.0037  0.0269  39  ASP   C CG  
1378 O OD1 . ASP   B 33  ? 0.1156 0.1306 0.1840 0.0036  0.0047  0.0296  39  ASP   C OD1 
1379 O OD2 . ASP   B 33  ? 0.1126 0.1269 0.1701 0.0039  0.0032  0.0277  39  ASP   C OD2 
1380 N N   . LEU   B 34  ? 0.0986 0.1046 0.1580 0.0052  0.0030  0.0171  40  LEU   C N   
1381 C CA  . LEU   B 34  ? 0.1035 0.1079 0.1564 0.0054  0.0039  0.0174  40  LEU   C CA  
1382 C C   . LEU   B 34  ? 0.1042 0.1082 0.1616 0.0054  0.0060  0.0188  40  LEU   C C   
1383 O O   . LEU   B 34  ? 0.1039 0.1070 0.1668 0.0059  0.0067  0.0174  40  LEU   C O   
1384 C CB  . LEU   B 34  ? 0.1181 0.1187 0.1631 0.0072  0.0033  0.0134  40  LEU   C CB  
1385 C CG  . LEU   B 34  ? 0.1194 0.1199 0.1584 0.0074  0.0014  0.0123  40  LEU   C CG  
1386 C CD1 . LEU   B 34  ? 0.1494 0.1459 0.1802 0.0098  0.0009  0.0088  40  LEU   C CD1 
1387 C CD2 . LEU   B 34  ? 0.1269 0.1291 0.1629 0.0061  0.0018  0.0154  40  LEU   C CD2 
1388 N N   . LEU   B 35  ? 0.1003 0.1047 0.1562 0.0048  0.0069  0.0211  41  LEU   C N   
1389 C CA  . LEU   B 35  ? 0.1074 0.1112 0.1677 0.0050  0.0093  0.0224  41  LEU   C CA  
1390 C C   . LEU   B 35  ? 0.0999 0.1022 0.1557 0.0052  0.0105  0.0229  41  LEU   C C   
1391 O O   . LEU   B 35  ? 0.1146 0.1181 0.1672 0.0043  0.0090  0.0238  41  LEU   C O   
1392 C CB  . LEU   B 35  ? 0.1098 0.1175 0.1783 0.0037  0.0089  0.0264  41  LEU   C CB  
1393 C CG  . LEU   B 35  ? 0.1142 0.1220 0.1895 0.0038  0.0111  0.0283  41  LEU   C CG  
1394 C CD1 . LEU   B 35  ? 0.1320 0.1425 0.2163 0.0035  0.0111  0.0310  41  LEU   C CD1 
1395 C CD2 . LEU   B 35  ? 0.1290 0.1381 0.2045 0.0030  0.0109  0.0305  41  LEU   C CD2 
1396 N N   . VAL   B 36  ? 0.1054 0.1047 0.1613 0.0066  0.0137  0.0223  42  VAL   C N   
1397 C CA  . VAL   B 36  ? 0.1132 0.1106 0.1669 0.0071  0.0162  0.0233  42  VAL   C CA  
1398 C C   . VAL   B 36  ? 0.1085 0.1067 0.1709 0.0068  0.0190  0.0259  42  VAL   C C   
1399 O O   . VAL   B 36  ? 0.1256 0.1225 0.1913 0.0079  0.0210  0.0253  42  VAL   C O   
1400 C CB  . VAL   B 36  ? 0.1264 0.1185 0.1706 0.0099  0.0185  0.0204  42  VAL   C CB  
1401 C CG1 . VAL   B 36  ? 0.1540 0.1437 0.1968 0.0108  0.0222  0.0222  42  VAL   C CG1 
1402 C CG2 . VAL   B 36  ? 0.1428 0.1345 0.1793 0.0103  0.0152  0.0178  42  VAL   C CG2 
1403 N N   . SER   B 37  ? 0.1152 0.1154 0.1823 0.0054  0.0190  0.0286  43  SER   C N   
1404 C CA  . SER   B 37  ? 0.1157 0.1170 0.1929 0.0051  0.0214  0.0313  43  SER   C CA  
1405 C C   . SER   B 37  ? 0.1237 0.1223 0.2010 0.0057  0.0251  0.0322  43  SER   C C   
1406 O O   . SER   B 37  ? 0.1340 0.1306 0.2042 0.0061  0.0251  0.0312  43  SER   C O   
1407 C CB  . SER   B 37  ? 0.1199 0.1265 0.2053 0.0028  0.0174  0.0339  43  SER   C CB  
1408 O OG  . SER   B 37  ? 0.1239 0.1322 0.2068 0.0014  0.0139  0.0340  43  SER   C OG  
1409 N N   . SER   B 38  ? 0.1341 0.1323 0.2199 0.0063  0.0291  0.0344  44  SER   C N   
1410 C CA  . SER   B 38  ? 0.1509 0.1466 0.2397 0.0070  0.0337  0.0361  44  SER   C CA  
1411 C C   . SER   B 38  ? 0.1633 0.1631 0.2625 0.0043  0.0308  0.0382  44  SER   C C   
1412 O O   . SER   B 38  ? 0.1803 0.1848 0.2872 0.0024  0.0264  0.0392  44  SER   C O   
1413 C CB  . SER   B 38  ? 0.1784 0.1711 0.2716 0.0093  0.0403  0.0374  44  SER   C CB  
1414 O OG  . SER   B 38  ? 0.2190 0.2157 0.3247 0.0079  0.0391  0.0394  44  SER   C OG  
1415 N N   . THR   B 39  ? 0.1619 0.1598 0.2620 0.0043  0.0331  0.0389  45  THR   C N   
1416 C CA  . THR   B 39  ? 0.1762 0.1775 0.2870 0.0017  0.0300  0.0402  45  THR   C CA  
1417 C C   . THR   B 39  ? 0.1963 0.1959 0.3189 0.0023  0.0361  0.0431  45  THR   C C   
1418 O O   . THR   B 39  ? 0.2000 0.1946 0.3183 0.0050  0.0432  0.0439  45  THR   C O   
1419 C CB  . THR   B 39  ? 0.1863 0.1868 0.2893 0.0008  0.0267  0.0382  45  THR   C CB  
1420 O OG1 . THR   B 39  ? 0.2001 0.1953 0.2961 0.0030  0.0324  0.0383  45  THR   C OG1 
1421 C CG2 . THR   B 39  ? 0.1974 0.1993 0.2890 0.0004  0.0213  0.0356  45  THR   C CG2 
1422 N N   . THR   B 40  ? 0.2209 0.2244 0.3582 -0.0001 0.0331  0.0444  46  THR   C N   
1423 C CA  . THR   B 40  ? 0.2462 0.2486 0.3977 0.0001  0.0387  0.0473  46  THR   C CA  
1424 C C   . THR   B 40  ? 0.2487 0.2479 0.3980 0.0000  0.0408  0.0470  46  THR   C C   
1425 O O   . THR   B 40  ? 0.2792 0.2739 0.4304 0.0021  0.0490  0.0494  46  THR   C O   
1426 C CB  . THR   B 40  ? 0.2873 0.2954 0.4569 -0.0023 0.0341  0.0486  46  THR   C CB  
1427 O OG1 . THR   B 40  ? 0.3271 0.3389 0.4962 -0.0048 0.0250  0.0462  46  THR   C OG1 
1428 C CG2 . THR   B 40  ? 0.2811 0.2918 0.4529 -0.0018 0.0331  0.0495  46  THR   C CG2 
1429 N N   . ALA   B 41  ? 0.2210 0.2219 0.3654 -0.0020 0.0340  0.0443  47  ALA   C N   
1430 C CA  . ALA   B 41  ? 0.2381 0.2360 0.3807 -0.0022 0.0354  0.0438  47  ALA   C CA  
1431 C C   . ALA   B 41  ? 0.2309 0.2240 0.3543 0.0003  0.0381  0.0426  47  ALA   C C   
1432 O O   . ALA   B 41  ? 0.2364 0.2303 0.3481 0.0009  0.0349  0.0406  47  ALA   C O   
1433 C CB  . ALA   B 41  ? 0.2637 0.2655 0.4107 -0.0053 0.0266  0.0412  47  ALA   C CB  
1434 N N   . GLN   B 42  ? 0.2262 0.2147 0.3473 0.0019  0.0436  0.0438  48  GLN   C N   
1435 C CA  . GLN   B 42  ? 0.2367 0.2208 0.3405 0.0044  0.0455  0.0427  48  GLN   C CA  
1436 C C   . GLN   B 42  ? 0.2180 0.2040 0.3158 0.0023  0.0383  0.0394  48  GLN   C C   
1437 O O   . GLN   B 42  ? 0.2298 0.2178 0.3368 -0.0003 0.0348  0.0387  48  GLN   C O   
1438 C CB  . GLN   B 42  ? 0.3101 0.2883 0.4137 0.0073  0.0543  0.0458  48  GLN   C CB  
1439 C CG  . GLN   B 42  ? 0.4253 0.3997 0.5276 0.0110  0.0627  0.0488  48  GLN   C CG  
1440 C CD  . GLN   B 42  ? 0.5556 0.5237 0.6551 0.0145  0.0715  0.0522  48  GLN   C CD  
1441 O OE1 . GLN   B 42  ? 0.5991 0.5666 0.7124 0.0134  0.0751  0.0550  48  GLN   C OE1 
1442 N NE2 . GLN   B 42  ? 0.5899 0.5527 0.6715 0.0190  0.0751  0.0521  48  GLN   C NE2 
1443 N N   . GLY   B 43  ? 0.1918 0.1769 0.2743 0.0037  0.0361  0.0372  49  GLY   C N   
1444 C CA  . GLY   B 43  ? 0.1940 0.1802 0.2690 0.0024  0.0304  0.0344  49  GLY   C CA  
1445 C C   . GLY   B 43  ? 0.1889 0.1702 0.2549 0.0047  0.0340  0.0346  49  GLY   C C   
1446 O O   . GLY   B 43  ? 0.2297 0.2065 0.2924 0.0078  0.0408  0.0370  49  GLY   C O   
1447 N N   . CYS   B 44  ? 0.1740 0.1558 0.2357 0.0035  0.0298  0.0324  50  CYS   C N   
1448 C CA  . CYS   B 44  ? 0.1858 0.1633 0.2410 0.0052  0.0325  0.0328  50  CYS   C CA  
1449 C C   . CYS   B 44  ? 0.1903 0.1673 0.2317 0.0064  0.0294  0.0304  50  CYS   C C   
1450 O O   . CYS   B 44  ? 0.2252 0.1990 0.2616 0.0078  0.0309  0.0305  50  CYS   C O   
1451 C CB  . CYS   B 44  ? 0.2011 0.1789 0.2670 0.0027  0.0313  0.0326  50  CYS   C CB  
1452 S SG  . CYS   B 44  ? 0.2536 0.2317 0.3388 0.0013  0.0356  0.0357  50  CYS   C SG  
1453 N N   . ASP   B 45  ? 0.1681 0.1482 0.2044 0.0060  0.0251  0.0283  51  ASP   C N   
1454 C CA  . ASP   B 45  ? 0.1787 0.1586 0.2038 0.0071  0.0222  0.0261  51  ASP   C CA  
1455 C C   . ASP   B 45  ? 0.1903 0.1657 0.2059 0.0112  0.0263  0.0269  51  ASP   C C   
1456 O O   . ASP   B 45  ? 0.2266 0.2004 0.2427 0.0130  0.0301  0.0283  51  ASP   C O   
1457 C CB  . ASP   B 45  ? 0.1762 0.1602 0.2000 0.0058  0.0173  0.0241  51  ASP   C CB  
1458 C CG  . ASP   B 45  ? 0.2087 0.1966 0.2382 0.0027  0.0126  0.0231  51  ASP   C CG  
1459 O OD1 . ASP   B 45  ? 0.2417 0.2287 0.2720 0.0017  0.0116  0.0223  51  ASP   C OD1 
1460 O OD2 . ASP   B 45  ? 0.1884 0.1798 0.2204 0.0015  0.0098  0.0228  51  ASP   C OD2 
1461 N N   . THR   B 46  ? 0.1743 0.1476 0.1811 0.0131  0.0256  0.0259  52  THR   C N   
1462 C CA  . THR   B 46  ? 0.1817 0.1510 0.1777 0.0175  0.0280  0.0260  52  THR   C CA  
1463 C C   . THR   B 46  ? 0.1699 0.1414 0.1597 0.0178  0.0229  0.0228  52  THR   C C   
1464 O O   . THR   B 46  ? 0.1745 0.1486 0.1645 0.0160  0.0189  0.0211  52  THR   C O   
1465 C CB  . THR   B 46  ? 0.2100 0.1752 0.2011 0.0197  0.0305  0.0275  52  THR   C CB  
1466 O OG1 . THR   B 46  ? 0.2324 0.1951 0.2309 0.0195  0.0361  0.0309  52  THR   C OG1 
1467 C CG2 . THR   B 46  ? 0.2437 0.2046 0.2217 0.0249  0.0318  0.0273  52  THR   C CG2 
1468 N N   . ILE   B 47  ? 0.1724 0.1426 0.1570 0.0203  0.0231  0.0216  53  ILE   C N   
1469 C CA  . ILE   B 47  ? 0.1675 0.1396 0.1478 0.0209  0.0183  0.0183  53  ILE   C CA  
1470 C C   . ILE   B 47  ? 0.1733 0.1421 0.1434 0.0245  0.0174  0.0173  53  ILE   C C   
1471 O O   . ILE   B 47  ? 0.1920 0.1558 0.1547 0.0285  0.0210  0.0187  53  ILE   C O   
1472 C CB  . ILE   B 47  ? 0.1837 0.1553 0.1633 0.0222  0.0186  0.0170  53  ILE   C CB  
1473 C CG1 . ILE   B 47  ? 0.1924 0.1668 0.1823 0.0192  0.0202  0.0187  53  ILE   C CG1 
1474 C CG2 . ILE   B 47  ? 0.1850 0.1587 0.1626 0.0224  0.0134  0.0133  53  ILE   C CG2 
1475 C CD1 . ILE   B 47  ? 0.2106 0.1906 0.2084 0.0149  0.0162  0.0184  53  ILE   C CD1 
1476 N N   . ALA   B 48  ? 0.1639 0.1352 0.1335 0.0237  0.0128  0.0152  54  ALA   C N   
1477 C CA  . ALA   B 48  ? 0.1598 0.1285 0.1207 0.0272  0.0110  0.0139  54  ALA   C CA  
1478 C C   . ALA   B 48  ? 0.1561 0.1224 0.1099 0.0311  0.0095  0.0114  54  ALA   C C   
1479 O O   . ALA   B 48  ? 0.1599 0.1283 0.1174 0.0299  0.0075  0.0092  54  ALA   C O   
1480 C CB  . ALA   B 48  ? 0.1546 0.1273 0.1190 0.0251  0.0064  0.0120  54  ALA   C CB  
1481 N N   . ARG   B 49  ? 0.1688 0.1304 0.1120 0.0359  0.0101  0.0115  55  ARG   C N   
1482 C CA  . ARG   B 49  ? 0.1725 0.1311 0.1068 0.0405  0.0078  0.0085  55  ARG   C CA  
1483 C C   . ARG   B 49  ? 0.1783 0.1361 0.1065 0.0433  0.0034  0.0069  55  ARG   C C   
1484 O O   . ARG   B 49  ? 0.1963 0.1500 0.1161 0.0471  0.0058  0.0092  55  ARG   C O   
1485 C CB  . ARG   B 49  ? 0.1948 0.1475 0.1205 0.0448  0.0134  0.0106  55  ARG   C CB  
1486 C CG  . ARG   B 49  ? 0.1839 0.1376 0.1177 0.0417  0.0181  0.0127  55  ARG   C CG  
1487 C CD  . ARG   B 49  ? 0.1990 0.1559 0.1389 0.0395  0.0151  0.0093  55  ARG   C CD  
1488 N NE  . ARG   B 49  ? 0.1915 0.1493 0.1391 0.0370  0.0198  0.0119  55  ARG   C NE  
1489 C CZ  . ARG   B 49  ? 0.1867 0.1484 0.1435 0.0336  0.0182  0.0105  55  ARG   C CZ  
1490 N NH1 . ARG   B 49  ? 0.1884 0.1530 0.1475 0.0325  0.0126  0.0067  55  ARG   C NH1 
1491 N NH2 . ARG   B 49  ? 0.2016 0.1643 0.1661 0.0314  0.0223  0.0132  55  ARG   C NH2 
1492 N N   . CYS   B 50  ? 0.1632 0.1252 0.0970 0.0415  -0.0026 0.0034  56  CYS   C N   
1493 C CA  . CYS   B 50  ? 0.1665 0.1295 0.0990 0.0429  -0.0071 0.0020  56  CYS   C CA  
1494 C C   . CYS   B 50  ? 0.1665 0.1342 0.1075 0.0407  -0.0131 -0.0021 56  CYS   C C   
1495 O O   . CYS   B 50  ? 0.1667 0.1368 0.1147 0.0380  -0.0134 -0.0034 56  CYS   C O   
1496 C CB  . CYS   B 50  ? 0.1585 0.1231 0.0956 0.0400  -0.0043 0.0056  56  CYS   C CB  
1497 S SG  . CYS   B 50  ? 0.1599 0.1307 0.1111 0.0331  -0.0042 0.0058  56  CYS   C SG  
1498 N N   . ASP   B 51  ? 0.1749 0.1438 0.1164 0.0421  -0.0177 -0.0037 57  ASP   C N   
1499 C CA  . ASP   B 51  ? 0.1856 0.1592 0.1374 0.0400  -0.0229 -0.0069 57  ASP   C CA  
1500 C C   . ASP   B 51  ? 0.1652 0.1422 0.1240 0.0372  -0.0221 -0.0047 57  ASP   C C   
1501 O O   . ASP   B 51  ? 0.1836 0.1636 0.1492 0.0369  -0.0264 -0.0068 57  ASP   C O   
1502 C CB  . ASP   B 51  ? 0.2155 0.1878 0.1637 0.0443  -0.0297 -0.0116 57  ASP   C CB  
1503 C CG  . ASP   B 51  ? 0.2742 0.2440 0.2141 0.0487  -0.0319 -0.0111 57  ASP   C CG  
1504 O OD1 . ASP   B 51  ? 0.2586 0.2272 0.1951 0.0485  -0.0275 -0.0069 57  ASP   C OD1 
1505 O OD2 . ASP   B 51  ? 0.3446 0.3137 0.2820 0.0524  -0.0385 -0.0152 57  ASP   C OD2 
1506 N N   . CYS   B 52  ? 0.1585 0.1352 0.1170 0.0348  -0.0168 -0.0007 58  CYS   C N   
1507 C CA  . CYS   B 52  ? 0.1575 0.1372 0.1224 0.0322  -0.0161 0.0008  58  CYS   C CA  
1508 C C   . CYS   B 52  ? 0.1415 0.1261 0.1177 0.0290  -0.0180 -0.0006 58  CYS   C C   
1509 O O   . CYS   B 52  ? 0.1446 0.1307 0.1252 0.0272  -0.0179 -0.0015 58  CYS   C O   
1510 C CB  . CYS   B 52  ? 0.1559 0.1346 0.1200 0.0297  -0.0107 0.0044  58  CYS   C CB  
1511 S SG  . CYS   B 52  ? 0.1678 0.1408 0.1217 0.0331  -0.0071 0.0072  58  CYS   C SG  
1512 N N   . GLN   B 53  ? 0.1311 0.1179 0.1124 0.0284  -0.0189 -0.0004 59  GLN   C N   
1513 C CA  . GLN   B 53  ? 0.1415 0.1326 0.1337 0.0255  -0.0191 -0.0005 59  GLN   C CA  
1514 C C   . GLN   B 53  ? 0.1281 0.1201 0.1216 0.0236  -0.0156 0.0021  59  GLN   C C   
1515 O O   . GLN   B 53  ? 0.1351 0.1302 0.1365 0.0222  -0.0152 0.0024  59  GLN   C O   
1516 C CB  . GLN   B 53  ? 0.1503 0.1437 0.1499 0.0271  -0.0240 -0.0034 59  GLN   C CB  
1517 C CG  . GLN   B 53  ? 0.1905 0.1836 0.1913 0.0284  -0.0280 -0.0069 59  GLN   C CG  
1518 C CD  . GLN   B 53  ? 0.1998 0.1956 0.2106 0.0295  -0.0332 -0.0101 59  GLN   C CD  
1519 O OE1 . GLN   B 53  ? 0.2380 0.2321 0.2451 0.0330  -0.0385 -0.0133 59  GLN   C OE1 
1520 N NE2 . GLN   B 53  ? 0.1822 0.1819 0.2060 0.0267  -0.0321 -0.0094 59  GLN   C NE2 
1521 N N   . THR   B 54  ? 0.1302 0.1192 0.1165 0.0237  -0.0127 0.0040  60  THR   C N   
1522 C CA  . THR   B 54  ? 0.1326 0.1219 0.1198 0.0217  -0.0095 0.0059  60  THR   C CA  
1523 C C   . THR   B 54  ? 0.1310 0.1185 0.1141 0.0201  -0.0066 0.0074  60  THR   C C   
1524 O O   . THR   B 54  ? 0.1484 0.1331 0.1265 0.0213  -0.0061 0.0077  60  THR   C O   
1525 C CB  . THR   B 54  ? 0.1790 0.1667 0.1642 0.0235  -0.0093 0.0063  60  THR   C CB  
1526 O OG1 . THR   B 54  ? 0.2408 0.2247 0.2186 0.0256  -0.0088 0.0070  60  THR   C OG1 
1527 C CG2 . THR   B 54  ? 0.1814 0.1711 0.1716 0.0254  -0.0125 0.0049  60  THR   C CG2 
1528 N N   . GLY   B 55  ? 0.1249 0.1137 0.1104 0.0175  -0.0046 0.0083  61  GLY   C N   
1529 C CA  . GLY   B 55  ? 0.1266 0.1141 0.1100 0.0157  -0.0026 0.0094  61  GLY   C CA  
1530 C C   . GLY   B 55  ? 0.1127 0.1016 0.0980 0.0135  -0.0016 0.0098  61  GLY   C C   
1531 O O   . GLY   B 55  ? 0.1219 0.1117 0.1084 0.0139  -0.0014 0.0096  61  GLY   C O   
1532 N N   . VAL   B 56  ? 0.1054 0.0943 0.0907 0.0117  -0.0008 0.0104  62  VAL   C N   
1533 C CA  . VAL   B 56  ? 0.1066 0.0963 0.0920 0.0101  -0.0005 0.0105  62  VAL   C CA  
1534 C C   . VAL   B 56  ? 0.1042 0.0961 0.0920 0.0086  -0.0011 0.0113  62  VAL   C C   
1535 O O   . VAL   B 56  ? 0.1138 0.1053 0.1027 0.0081  -0.0010 0.0117  62  VAL   C O   
1536 C CB  . VAL   B 56  ? 0.1108 0.0975 0.0941 0.0095  0.0003  0.0101  62  VAL   C CB  
1537 C CG1 . VAL   B 56  ? 0.1328 0.1199 0.1154 0.0081  -0.0004 0.0094  62  VAL   C CG1 
1538 C CG2 . VAL   B 56  ? 0.1279 0.1122 0.1091 0.0112  0.0011  0.0096  62  VAL   C CG2 
1539 N N   . TYR   B 57  ? 0.1060 0.1001 0.0946 0.0081  -0.0012 0.0119  63  TYR   C N   
1540 C CA  . TYR   B 57  ? 0.1006 0.0969 0.0915 0.0070  -0.0018 0.0131  63  TYR   C CA  
1541 C C   . TYR   B 57  ? 0.1077 0.1040 0.0958 0.0064  -0.0024 0.0132  63  TYR   C C   
1542 O O   . TYR   B 57  ? 0.1161 0.1113 0.1005 0.0072  -0.0019 0.0125  63  TYR   C O   
1543 C CB  . TYR   B 57  ? 0.1041 0.1032 0.0993 0.0074  -0.0015 0.0142  63  TYR   C CB  
1544 C CG  . TYR   B 57  ? 0.1053 0.1058 0.1007 0.0081  -0.0003 0.0154  63  TYR   C CG  
1545 C CD1 . TYR   B 57  ? 0.1227 0.1227 0.1178 0.0094  0.0009  0.0150  63  TYR   C CD1 
1546 C CD2 . TYR   B 57  ? 0.1063 0.1084 0.1021 0.0079  0.0001  0.0174  63  TYR   C CD2 
1547 C CE1 . TYR   B 57  ? 0.1255 0.1266 0.1212 0.0104  0.0030  0.0166  63  TYR   C CE1 
1548 C CE2 . TYR   B 57  ? 0.1187 0.1217 0.1141 0.0092  0.0020  0.0192  63  TYR   C CE2 
1549 C CZ  . TYR   B 57  ? 0.1208 0.1231 0.1162 0.0104  0.0038  0.0188  63  TYR   C CZ  
1550 O OH  . TYR   B 57  ? 0.1513 0.1542 0.1467 0.0120  0.0068  0.0210  63  TYR   C OH  
1551 N N   . TYR   B 58  ? 0.1027 0.1002 0.0925 0.0053  -0.0036 0.0139  64  TYR   C N   
1552 C CA  . TYR   B 58  ? 0.1105 0.1082 0.0974 0.0051  -0.0053 0.0138  64  TYR   C CA  
1553 C C   . TYR   B 58  ? 0.1141 0.1141 0.1005 0.0061  -0.0048 0.0161  64  TYR   C C   
1554 O O   . TYR   B 58  ? 0.1155 0.1176 0.1064 0.0058  -0.0044 0.0179  64  TYR   C O   
1555 C CB  . TYR   B 58  ? 0.1213 0.1190 0.1112 0.0036  -0.0074 0.0135  64  TYR   C CB  
1556 C CG  . TYR   B 58  ? 0.1355 0.1333 0.1221 0.0037  -0.0102 0.0128  64  TYR   C CG  
1557 C CD1 . TYR   B 58  ? 0.1434 0.1387 0.1245 0.0044  -0.0111 0.0104  64  TYR   C CD1 
1558 C CD2 . TYR   B 58  ? 0.1427 0.1428 0.1310 0.0036  -0.0122 0.0142  64  TYR   C CD2 
1559 C CE1 . TYR   B 58  ? 0.1611 0.1561 0.1379 0.0051  -0.0143 0.0091  64  TYR   C CE1 
1560 C CE2 . TYR   B 58  ? 0.1535 0.1535 0.1377 0.0043  -0.0157 0.0133  64  TYR   C CE2 
1561 C CZ  . TYR   B 58  ? 0.1542 0.1515 0.1322 0.0051  -0.0168 0.0105  64  TYR   C CZ  
1562 O OH  . TYR   B 58  ? 0.1903 0.1868 0.1624 0.0064  -0.0206 0.0089  64  TYR   C OH  
1563 N N   . CYS   B 59  ? 0.1169 0.1161 0.0974 0.0076  -0.0045 0.0160  65  CYS   C N   
1564 C CA  . CYS   B 59  ? 0.1230 0.1236 0.1015 0.0093  -0.0033 0.0187  65  CYS   C CA  
1565 C C   . CYS   B 59  ? 0.1214 0.1215 0.0939 0.0101  -0.0061 0.0185  65  CYS   C C   
1566 O O   . CYS   B 59  ? 0.1428 0.1405 0.1081 0.0114  -0.0068 0.0165  65  CYS   C O   
1567 C CB  . CYS   B 59  ? 0.1296 0.1293 0.1058 0.0112  0.0000  0.0192  65  CYS   C CB  
1568 S SG  . CYS   B 59  ? 0.1491 0.1498 0.1225 0.0139  0.0031  0.0232  65  CYS   C SG  
1569 N N   . SER   B 60  ? 0.1321 0.1342 0.1076 0.0095  -0.0080 0.0200  66  SER   C N   
1570 C CA  A SER   B 60  ? 0.1550 0.1568 0.1253 0.0104  -0.0118 0.0195  66  SER   C CA  
1571 C CA  B SER   B 60  ? 0.1458 0.1478 0.1163 0.0104  -0.0117 0.0196  66  SER   C CA  
1572 C C   . SER   B 60  ? 0.1600 0.1606 0.1206 0.0139  -0.0108 0.0209  66  SER   C C   
1573 O O   . SER   B 60  ? 0.1786 0.1773 0.1317 0.0152  -0.0140 0.0186  66  SER   C O   
1574 C CB  A SER   B 60  ? 0.1888 0.1933 0.1652 0.0093  -0.0140 0.0212  66  SER   C CB  
1575 C CB  B SER   B 60  ? 0.1505 0.1553 0.1269 0.0096  -0.0134 0.0219  66  SER   C CB  
1576 O OG  A SER   B 60  ? 0.2222 0.2288 0.2009 0.0104  -0.0113 0.0252  66  SER   C OG  
1577 O OG  B SER   B 60  ? 0.1584 0.1631 0.1306 0.0105  -0.0180 0.0211  66  SER   C OG  
1578 N N   . SER   B 61  ? 0.1487 0.1502 0.1100 0.0155  -0.0062 0.0245  67  SER   C N   
1579 C CA  . SER   B 61  ? 0.1616 0.1615 0.1136 0.0194  -0.0037 0.0268  67  SER   C CA  
1580 C C   . SER   B 61  ? 0.1716 0.1682 0.1160 0.0209  -0.0023 0.0242  67  SER   C C   
1581 O O   . SER   B 61  ? 0.1940 0.1885 0.1291 0.0246  0.0000  0.0257  67  SER   C O   
1582 C CB  . SER   B 61  ? 0.1714 0.1732 0.1286 0.0206  0.0015  0.0318  67  SER   C CB  
1583 O OG  . SER   B 61  ? 0.1746 0.1768 0.1388 0.0193  0.0051  0.0315  67  SER   C OG  
1584 N N   . ARG   B 62  ? 0.1586 0.1541 0.1060 0.0186  -0.0033 0.0204  68  ARG   C N   
1585 C CA  . ARG   B 62  ? 0.1713 0.1632 0.1119 0.0198  -0.0025 0.0174  68  ARG   C CA  
1586 C C   . ARG   B 62  ? 0.1703 0.1604 0.1098 0.0179  -0.0076 0.0124  68  ARG   C C   
1587 O O   . ARG   B 62  ? 0.1933 0.1802 0.1281 0.0186  -0.0074 0.0093  68  ARG   C O   
1588 C CB  . ARG   B 62  ? 0.1742 0.1663 0.1207 0.0192  0.0019  0.0179  68  ARG   C CB  
1589 C CG  . ARG   B 62  ? 0.2110 0.2047 0.1606 0.0210  0.0072  0.0224  68  ARG   C CG  
1590 C CD  . ARG   B 62  ? 0.2282 0.2190 0.1676 0.0251  0.0106  0.0237  68  ARG   C CD  
1591 N NE  . ARG   B 62  ? 0.2384 0.2307 0.1823 0.0271  0.0166  0.0286  68  ARG   C NE  
1592 C CZ  . ARG   B 62  ? 0.2497 0.2432 0.1936 0.0288  0.0185  0.0329  68  ARG   C CZ  
1593 N NH1 . ARG   B 62  ? 0.2690 0.2626 0.2068 0.0293  0.0145  0.0331  68  ARG   C NH1 
1594 N NH2 . ARG   B 62  ? 0.2996 0.2940 0.2490 0.0306  0.0247  0.0374  68  ARG   C NH2 
1595 N N   . ARG   B 63  ? 0.1728 0.1648 0.1182 0.0155  -0.0115 0.0118  69  ARG   C N   
1596 C CA  . ARG   B 63  ? 0.1924 0.1831 0.1409 0.0131  -0.0157 0.0076  69  ARG   C CA  
1597 C C   . ARG   B 63  ? 0.2020 0.1906 0.1532 0.0119  -0.0133 0.0056  69  ARG   C C   
1598 O O   . ARG   B 63  ? 0.2326 0.2182 0.1815 0.0117  -0.0150 0.0019  69  ARG   C O   
1599 C CB  . ARG   B 63  ? 0.2202 0.2083 0.1603 0.0148  -0.0205 0.0040  69  ARG   C CB  
1600 C CG  . ARG   B 63  ? 0.2639 0.2537 0.2005 0.0164  -0.0241 0.0056  69  ARG   C CG  
1601 C CD  . ARG   B 63  ? 0.3157 0.3086 0.2629 0.0134  -0.0273 0.0060  69  ARG   C CD  
1602 N NE  . ARG   B 63  ? 0.3429 0.3369 0.2869 0.0149  -0.0327 0.0060  69  ARG   C NE  
1603 C CZ  . ARG   B 63  ? 0.3580 0.3547 0.3020 0.0162  -0.0323 0.0102  69  ARG   C CZ  
1604 N NH1 . ARG   B 63  ? 0.3520 0.3507 0.2996 0.0160  -0.0266 0.0147  69  ARG   C NH1 
1605 N NH2 . ARG   B 63  ? 0.3573 0.3549 0.2985 0.0178  -0.0379 0.0100  69  ARG   C NH2 
1606 N N   . LYS   B 64  ? 0.1740 0.1643 0.1306 0.0112  -0.0094 0.0081  70  LYS   C N   
1607 C CA  . LYS   B 64  ? 0.1782 0.1667 0.1368 0.0107  -0.0070 0.0068  70  LYS   C CA  
1608 C C   . LYS   B 64  ? 0.1524 0.1429 0.1191 0.0091  -0.0055 0.0085  70  LYS   C C   
1609 O O   . LYS   B 64  ? 0.1641 0.1574 0.1341 0.0090  -0.0047 0.0112  70  LYS   C O   
1610 C CB  . LYS   B 64  ? 0.2379 0.2253 0.1914 0.0133  -0.0032 0.0078  70  LYS   C CB  
1611 C CG  . LYS   B 64  ? 0.3692 0.3528 0.3136 0.0154  -0.0038 0.0049  70  LYS   C CG  
1612 C CD  . LYS   B 64  ? 0.4722 0.4542 0.4135 0.0177  0.0008  0.0057  70  LYS   C CD  
1613 C CE  . LYS   B 64  ? 0.5443 0.5221 0.4754 0.0202  0.0006  0.0027  70  LYS   C CE  
1614 N NZ  . LYS   B 64  ? 0.5907 0.5682 0.5132 0.0224  -0.0014 0.0031  70  LYS   C NZ  
1615 N N   . HIS   B 65  ? 0.1398 0.1284 0.1090 0.0082  -0.0050 0.0070  71  HIS   C N   
1616 C CA  . HIS   B 65  ? 0.1401 0.1297 0.1147 0.0075  -0.0035 0.0083  71  HIS   C CA  
1617 C C   . HIS   B 65  ? 0.1696 0.1585 0.1433 0.0091  -0.0009 0.0085  71  HIS   C C   
1618 O O   . HIS   B 65  ? 0.2098 0.1962 0.1802 0.0100  -0.0002 0.0069  71  HIS   C O   
1619 C CB  . HIS   B 65  ? 0.1459 0.1334 0.1236 0.0062  -0.0041 0.0070  71  HIS   C CB  
1620 C CG  . HIS   B 65  ? 0.1373 0.1257 0.1186 0.0045  -0.0063 0.0070  71  HIS   C CG  
1621 N ND1 . HIS   B 65  ? 0.1710 0.1608 0.1571 0.0036  -0.0059 0.0087  71  HIS   C ND1 
1622 C CD2 . HIS   B 65  ? 0.1339 0.1215 0.1147 0.0037  -0.0092 0.0051  71  HIS   C CD2 
1623 C CE1 . HIS   B 65  ? 0.1413 0.1316 0.1309 0.0022  -0.0080 0.0082  71  HIS   C CE1 
1624 N NE2 . HIS   B 65  ? 0.1808 0.1699 0.1676 0.0022  -0.0104 0.0060  71  HIS   C NE2 
1625 N N   . TYR   B 66  ? 0.1391 0.1304 0.1166 0.0096  0.0004  0.0103  72  TYR   C N   
1626 C CA  . TYR   B 66  ? 0.1265 0.1178 0.1050 0.0112  0.0024  0.0106  72  TYR   C CA  
1627 C C   . TYR   B 66  ? 0.1240 0.1155 0.1065 0.0112  0.0019  0.0105  72  TYR   C C   
1628 O O   . TYR   B 66  ? 0.1181 0.1111 0.1036 0.0106  0.0009  0.0111  72  TYR   C O   
1629 C CB  . TYR   B 66  ? 0.1365 0.1306 0.1178 0.0120  0.0040  0.0128  72  TYR   C CB  
1630 C CG  . TYR   B 66  ? 0.1448 0.1384 0.1208 0.0132  0.0053  0.0137  72  TYR   C CG  
1631 C CD1 . TYR   B 66  ? 0.1759 0.1675 0.1478 0.0150  0.0077  0.0133  72  TYR   C CD1 
1632 C CD2 . TYR   B 66  ? 0.1580 0.1530 0.1328 0.0129  0.0045  0.0152  72  TYR   C CD2 
1633 C CE1 . TYR   B 66  ? 0.1902 0.1808 0.1557 0.0168  0.0093  0.0142  72  TYR   C CE1 
1634 C CE2 . TYR   B 66  ? 0.1699 0.1642 0.1385 0.0146  0.0056  0.0162  72  TYR   C CE2 
1635 C CZ  . TYR   B 66  ? 0.1712 0.1630 0.1344 0.0167  0.0080  0.0156  72  TYR   C CZ  
1636 O OH  . TYR   B 66  ? 0.2089 0.1995 0.1644 0.0192  0.0095  0.0168  72  TYR   C OH  
1637 N N   . PRO   B 67  ? 0.1210 0.1107 0.1030 0.0124  0.0027  0.0097  73  PRO   C N   
1638 C CA  . PRO   B 67  ? 0.1352 0.1251 0.1201 0.0132  0.0019  0.0096  73  PRO   C CA  
1639 C C   . PRO   B 67  ? 0.1313 0.1242 0.1218 0.0141  0.0018  0.0104  73  PRO   C C   
1640 O O   . PRO   B 67  ? 0.1557 0.1496 0.1480 0.0148  0.0036  0.0110  73  PRO   C O   
1641 C CB  . PRO   B 67  ? 0.1599 0.1470 0.1428 0.0145  0.0028  0.0089  73  PRO   C CB  
1642 C CG  . PRO   B 67  ? 0.1882 0.1745 0.1689 0.0146  0.0045  0.0084  73  PRO   C CG  
1643 C CD  . PRO   B 67  ? 0.1438 0.1311 0.1224 0.0133  0.0042  0.0087  73  PRO   C CD  
1644 N N   . VAL   B 68  ? 0.1141 0.1082 0.1076 0.0142  -0.0001 0.0101  74  VAL   C N   
1645 C CA  . VAL   B 68  ? 0.1228 0.1199 0.1235 0.0148  -0.0008 0.0103  74  VAL   C CA  
1646 C C   . VAL   B 68  ? 0.1219 0.1189 0.1244 0.0161  -0.0038 0.0088  74  VAL   C C   
1647 O O   . VAL   B 68  ? 0.1285 0.1234 0.1261 0.0166  -0.0049 0.0081  74  VAL   C O   
1648 C CB  . VAL   B 68  ? 0.1441 0.1435 0.1480 0.0134  -0.0005 0.0113  74  VAL   C CB  
1649 C CG1 . VAL   B 68  ? 0.1603 0.1602 0.1629 0.0129  0.0023  0.0132  74  VAL   C CG1 
1650 C CG2 . VAL   B 68  ? 0.1562 0.1546 0.1569 0.0124  -0.0018 0.0109  74  VAL   C CG2 
1651 N N   . SER   B 69  ? 0.1147 0.1140 0.1248 0.0172  -0.0050 0.0082  75  SER   C N   
1652 C CA  . SER   B 69  ? 0.1134 0.1133 0.1270 0.0184  -0.0089 0.0062  75  SER   C CA  
1653 C C   . SER   B 69  ? 0.1034 0.1055 0.1228 0.0171  -0.0094 0.0060  75  SER   C C   
1654 O O   . SER   B 69  ? 0.1150 0.1191 0.1398 0.0158  -0.0068 0.0077  75  SER   C O   
1655 C CB  . SER   B 69  ? 0.1405 0.1420 0.1615 0.0201  -0.0106 0.0053  75  SER   C CB  
1656 O OG  . SER   B 69  ? 0.2114 0.2108 0.2271 0.0215  -0.0099 0.0056  75  SER   C OG  
1657 N N   . PHE   B 70  ? 0.1030 0.1044 0.1211 0.0177  -0.0122 0.0040  76  PHE   C N   
1658 C CA  . PHE   B 70  ? 0.1070 0.1100 0.1308 0.0165  -0.0127 0.0036  76  PHE   C CA  
1659 C C   . PHE   B 70  ? 0.1101 0.1130 0.1373 0.0181  -0.0174 0.0001  76  PHE   C C   
1660 O O   . PHE   B 70  ? 0.1223 0.1229 0.1435 0.0205  -0.0203 -0.0019 76  PHE   C O   
1661 C CB  . PHE   B 70  ? 0.1139 0.1156 0.1316 0.0149  -0.0105 0.0051  76  PHE   C CB  
1662 C CG  . PHE   B 70  ? 0.1106 0.1089 0.1185 0.0161  -0.0111 0.0044  76  PHE   C CG  
1663 C CD1 . PHE   B 70  ? 0.1139 0.1100 0.1148 0.0162  -0.0092 0.0058  76  PHE   C CD1 
1664 C CD2 . PHE   B 70  ? 0.1230 0.1198 0.1290 0.0173  -0.0131 0.0024  76  PHE   C CD2 
1665 C CE1 . PHE   B 70  ? 0.1169 0.1097 0.1103 0.0174  -0.0090 0.0057  76  PHE   C CE1 
1666 C CE2 . PHE   B 70  ? 0.1232 0.1164 0.1200 0.0188  -0.0125 0.0024  76  PHE   C CE2 
1667 C CZ  . PHE   B 70  ? 0.1236 0.1149 0.1146 0.0189  -0.0104 0.0042  76  PHE   C CZ  
1668 N N   . SER   B 71  ? 0.1033 0.1084 0.1403 0.0172  -0.0182 -0.0008 77  SER   C N   
1669 C CA  . SER   B 71  ? 0.1088 0.1141 0.1514 0.0187  -0.0232 -0.0049 77  SER   C CA  
1670 C C   . SER   B 71  ? 0.1180 0.1202 0.1522 0.0198  -0.0251 -0.0072 77  SER   C C   
1671 O O   . SER   B 71  ? 0.1404 0.1408 0.1662 0.0191  -0.0220 -0.0051 77  SER   C O   
1672 C CB  . SER   B 71  ? 0.1177 0.1263 0.1760 0.0172  -0.0232 -0.0052 77  SER   C CB  
1673 O OG  . SER   B 71  ? 0.1394 0.1485 0.1995 0.0151  -0.0197 -0.0029 77  SER   C OG  
1674 N N   . LYS   B 72  ? 0.1488 0.1503 0.1854 0.0218  -0.0302 -0.0116 78  LYS   C N   
1675 C CA  . LYS   B 72  ? 0.1471 0.1451 0.1752 0.0236  -0.0320 -0.0142 78  LYS   C CA  
1676 C C   . LYS   B 72  ? 0.1436 0.1426 0.1783 0.0213  -0.0300 -0.0140 78  LYS   C C   
1677 O O   . LYS   B 72  ? 0.1633 0.1654 0.2114 0.0193  -0.0298 -0.0137 78  LYS   C O   
1678 C CB  . LYS   B 72  ? 0.1932 0.1899 0.2217 0.0270  -0.0391 -0.0197 78  LYS   C CB  
1679 C CG  . LYS   B 72  ? 0.2368 0.2329 0.2600 0.0295  -0.0416 -0.0198 78  LYS   C CG  
1680 C CD  . LYS   B 72  ? 0.3487 0.3437 0.3724 0.0333  -0.0496 -0.0255 78  LYS   C CD  
1681 C CE  . LYS   B 72  ? 0.4299 0.4199 0.4399 0.0367  -0.0515 -0.0284 78  LYS   C CE  
1682 N NZ  . LYS   B 72  ? 0.5077 0.4943 0.5027 0.0376  -0.0460 -0.0242 78  LYS   C NZ  
1683 N N   . PRO   B 73  ? 0.1439 0.1400 0.1702 0.0217  -0.0282 -0.0138 79  PRO   C N   
1684 C CA  . PRO   B 73  ? 0.1410 0.1381 0.1742 0.0195  -0.0259 -0.0131 79  PRO   C CA  
1685 C C   . PRO   B 73  ? 0.1412 0.1393 0.1860 0.0197  -0.0300 -0.0175 79  PRO   C C   
1686 O O   . PRO   B 73  ? 0.1739 0.1696 0.2158 0.0226  -0.0352 -0.0226 79  PRO   C O   
1687 C CB  . PRO   B 73  ? 0.1722 0.1654 0.1939 0.0209  -0.0241 -0.0132 79  PRO   C CB  
1688 C CG  . PRO   B 73  ? 0.2185 0.2093 0.2280 0.0228  -0.0231 -0.0116 79  PRO   C CG  
1689 C CD  . PRO   B 73  ? 0.1689 0.1608 0.1802 0.0242  -0.0272 -0.0134 79  PRO   C CD  
1690 N N   . SER   B 74  ? 0.1387 0.1401 0.1971 0.0169  -0.0280 -0.0156 80  SER   C N   
1691 C CA  A SER   B 74  ? 0.1452 0.1479 0.2180 0.0167  -0.0315 -0.0194 80  SER   C CA  
1692 C CA  B SER   B 74  ? 0.1451 0.1478 0.2178 0.0168  -0.0315 -0.0195 80  SER   C CA  
1693 C C   . SER   B 74  ? 0.1344 0.1392 0.2190 0.0140  -0.0275 -0.0166 80  SER   C C   
1694 O O   . SER   B 74  ? 0.1399 0.1455 0.2209 0.0124  -0.0224 -0.0115 80  SER   C O   
1695 C CB  A SER   B 74  ? 0.1649 0.1704 0.2474 0.0168  -0.0341 -0.0201 80  SER   C CB  
1696 C CB  B SER   B 74  ? 0.1609 0.1660 0.2428 0.0171  -0.0347 -0.0208 80  SER   C CB  
1697 O OG  A SER   B 74  ? 0.1918 0.1957 0.2639 0.0194  -0.0375 -0.0220 80  SER   C OG  
1698 O OG  B SER   B 74  ? 0.1674 0.1760 0.2570 0.0148  -0.0300 -0.0155 80  SER   C OG  
1699 N N   . LEU   B 75  ? 0.1430 0.1487 0.2423 0.0136  -0.0301 -0.0199 81  LEU   C N   
1700 C CA  . LEU   B 75  ? 0.1412 0.1487 0.2541 0.0113  -0.0265 -0.0173 81  LEU   C CA  
1701 C C   . LEU   B 75  ? 0.1476 0.1590 0.2735 0.0098  -0.0239 -0.0134 81  LEU   C C   
1702 O O   . LEU   B 75  ? 0.1705 0.1832 0.3073 0.0103  -0.0275 -0.0165 81  LEU   C O   
1703 C CB  . LEU   B 75  ? 0.1548 0.1607 0.2775 0.0120  -0.0310 -0.0236 81  LEU   C CB  
1704 C CG  . LEU   B 75  ? 0.1870 0.1941 0.3244 0.0099  -0.0275 -0.0215 81  LEU   C CG  
1705 C CD1 . LEU   B 75  ? 0.1874 0.1931 0.3156 0.0094  -0.0230 -0.0178 81  LEU   C CD1 
1706 C CD2 . LEU   B 75  ? 0.2200 0.2255 0.3697 0.0105  -0.0328 -0.0287 81  LEU   C CD2 
1707 N N   . ILE   B 76  ? 0.1590 0.1721 0.2837 0.0084  -0.0177 -0.0067 82  ILE   C N   
1708 C CA  A ILE   B 76  ? 0.1614 0.1774 0.2936 0.0077  -0.0137 -0.0018 82  ILE   C CA  
1709 C CA  B ILE   B 76  ? 0.1663 0.1824 0.3005 0.0077  -0.0140 -0.0022 82  ILE   C CA  
1710 C C   . ILE   B 76  ? 0.1597 0.1773 0.3033 0.0063  -0.0083 0.0032  82  ILE   C C   
1711 O O   . ILE   B 76  ? 0.1452 0.1619 0.2819 0.0059  -0.0059 0.0056  82  ILE   C O   
1712 C CB  A ILE   B 76  ? 0.1630 0.1787 0.2788 0.0081  -0.0111 0.0020  82  ILE   C CB  
1713 C CB  B ILE   B 76  ? 0.1726 0.1887 0.2928 0.0082  -0.0120 0.0010  82  ILE   C CB  
1714 C CG1 A ILE   B 76  ? 0.1741 0.1880 0.2784 0.0096  -0.0157 -0.0022 82  ILE   C CG1 
1715 C CG1 B ILE   B 76  ? 0.1674 0.1820 0.2789 0.0098  -0.0172 -0.0037 82  ILE   C CG1 
1716 C CG2 A ILE   B 76  ? 0.1753 0.1933 0.2954 0.0077  -0.0058 0.0077  82  ILE   C CG2 
1717 C CG2 B ILE   B 76  ? 0.1955 0.2142 0.3227 0.0078  -0.0069 0.0063  82  ILE   C CG2 
1718 C CD1 A ILE   B 76  ? 0.1768 0.1921 0.2886 0.0106  -0.0185 -0.0042 82  ILE   C CD1 
1719 C CD1 B ILE   B 76  ? 0.1317 0.1454 0.2276 0.0102  -0.0152 -0.0010 82  ILE   C CD1 
1720 N N   . PHE   B 77  ? 0.1517 0.1715 0.3118 0.0059  -0.0057 0.0054  83  PHE   C N   
1721 C CA  . PHE   B 77  ? 0.1541 0.1752 0.3234 0.0052  0.0005  0.0114  83  PHE   C CA  
1722 C C   . PHE   B 77  ? 0.1624 0.1840 0.3197 0.0058  0.0058  0.0180  83  PHE   C C   
1723 O O   . PHE   B 77  ? 0.1872 0.2096 0.3424 0.0065  0.0069  0.0192  83  PHE   C O   
1724 C CB  . PHE   B 77  ? 0.1494 0.1724 0.3414 0.0048  0.0021  0.0120  83  PHE   C CB  
1725 C CG  . PHE   B 77  ? 0.1490 0.1726 0.3514 0.0044  0.0086  0.0181  83  PHE   C CG  
1726 C CD1 . PHE   B 77  ? 0.1613 0.1838 0.3687 0.0036  0.0078  0.0166  83  PHE   C CD1 
1727 C CD2 . PHE   B 77  ? 0.1709 0.1958 0.3763 0.0052  0.0159  0.0257  83  PHE   C CD2 
1728 C CE1 . PHE   B 77  ? 0.1785 0.2014 0.3950 0.0035  0.0140  0.0227  83  PHE   C CE1 
1729 C CE2 . PHE   B 77  ? 0.1854 0.2106 0.3991 0.0054  0.0221  0.0318  83  PHE   C CE2 
1730 C CZ  . PHE   B 77  ? 0.1718 0.1961 0.3919 0.0044  0.0210  0.0303  83  PHE   C CZ  
1731 N N   . VAL   B 78  ? 0.1318 0.1529 0.2814 0.0057  0.0089  0.0220  84  VAL   C N   
1732 C CA  . VAL   B 78  ? 0.1369 0.1581 0.2737 0.0065  0.0130  0.0277  84  VAL   C CA  
1733 C C   . VAL   B 78  ? 0.1200 0.1421 0.2659 0.0072  0.0195  0.0345  84  VAL   C C   
1734 O O   . VAL   B 78  ? 0.1379 0.1600 0.2918 0.0066  0.0202  0.0354  84  VAL   C O   
1735 C CB  . VAL   B 78  ? 0.1437 0.1634 0.2646 0.0062  0.0107  0.0267  84  VAL   C CB  
1736 C CG1 . VAL   B 78  ? 0.1526 0.1723 0.2609 0.0072  0.0138  0.0317  84  VAL   C CG1 
1737 C CG2 . VAL   B 78  ? 0.1549 0.1731 0.2679 0.0060  0.0051  0.0204  84  VAL   C CG2 
1738 N N   . GLU   B 79  ? 0.1219 0.1445 0.2652 0.0087  0.0244  0.0397  85  GLU   C N   
1739 C CA  . GLU   B 79  ? 0.1314 0.1543 0.2803 0.0102  0.0312  0.0470  85  GLU   C CA  
1740 C C   . GLU   B 79  ? 0.1274 0.1496 0.2643 0.0107  0.0316  0.0502  85  GLU   C C   
1741 O O   . GLU   B 79  ? 0.1243 0.1459 0.2478 0.0101  0.0274  0.0473  85  GLU   C O   
1742 C CB  . GLU   B 79  ? 0.1562 0.1792 0.3032 0.0124  0.0367  0.0517  85  GLU   C CB  
1743 C CG  . GLU   B 79  ? 0.1994 0.2235 0.3625 0.0121  0.0375  0.0498  85  GLU   C CG  
1744 C CD  . GLU   B 79  ? 0.2395 0.2647 0.4255 0.0112  0.0392  0.0503  85  GLU   C CD  
1745 O OE1 . GLU   B 79  ? 0.2659 0.2909 0.4571 0.0119  0.0438  0.0556  85  GLU   C OE1 
1746 O OE2 . GLU   B 79  ? 0.2891 0.3154 0.4887 0.0098  0.0355  0.0452  85  GLU   C OE2 
1747 N N   . ALA   B 80  ? 0.1397 0.1621 0.2825 0.0121  0.0369  0.0566  86  ALA   C N   
1748 C CA  . ALA   B 80  ? 0.1573 0.1793 0.2906 0.0130  0.0373  0.0601  86  ALA   C CA  
1749 C C   . ALA   B 80  ? 0.1529 0.1741 0.2661 0.0145  0.0362  0.0612  86  ALA   C C   
1750 O O   . ALA   B 80  ? 0.1779 0.1985 0.2853 0.0161  0.0385  0.0625  86  ALA   C O   
1751 C CB  . ALA   B 80  ? 0.1749 0.1970 0.3175 0.0151  0.0441  0.0679  86  ALA   C CB  
1752 N N   . SER   B 81  ? 0.1474 0.1684 0.2508 0.0139  0.0324  0.0600  87  SER   C N   
1753 C CA  . SER   B 81  ? 0.1619 0.1822 0.2479 0.0152  0.0307  0.0607  87  SER   C CA  
1754 C C   . SER   B 81  ? 0.1685 0.1890 0.2504 0.0169  0.0315  0.0657  87  SER   C C   
1755 O O   . SER   B 81  ? 0.1772 0.1983 0.2702 0.0169  0.0339  0.0688  87  SER   C O   
1756 C CB  . SER   B 81  ? 0.1540 0.1740 0.2326 0.0129  0.0246  0.0541  87  SER   C CB  
1757 O OG  . SER   B 81  ? 0.1411 0.1616 0.2234 0.0113  0.0219  0.0526  87  SER   C OG  
1758 N N   . GLU   B 82  ? 0.1812 0.2011 0.2478 0.0181  0.0289  0.0661  88  GLU   C N   
1759 C CA  . GLU   B 82  ? 0.2059 0.2263 0.2689 0.0199  0.0286  0.0705  88  GLU   C CA  
1760 C C   . GLU   B 82  ? 0.1867 0.2083 0.2567 0.0173  0.0252  0.0682  88  GLU   C C   
1761 O O   . GLU   B 82  ? 0.2049 0.2272 0.2768 0.0186  0.0257  0.0724  88  GLU   C O   
1762 C CB  . GLU   B 82  ? 0.2816 0.3010 0.3272 0.0222  0.0261  0.0712  88  GLU   C CB  
1763 C CG  . GLU   B 82  ? 0.3966 0.4163 0.4350 0.0200  0.0196  0.0659  88  GLU   C CG  
1764 C CD  . GLU   B 82  ? 0.4669 0.4857 0.4900 0.0226  0.0167  0.0668  88  GLU   C CD  
1765 O OE1 . GLU   B 82  ? 0.4748 0.4919 0.4895 0.0260  0.0197  0.0698  88  GLU   C OE1 
1766 O OE2 . GLU   B 82  ? 0.4663 0.4857 0.4858 0.0214  0.0113  0.0643  88  GLU   C OE2 
1767 N N   . TYR   B 83  ? 0.1561 0.1778 0.2303 0.0142  0.0222  0.0621  89  TYR   C N   
1768 C CA  . TYR   B 83  ? 0.1454 0.1677 0.2244 0.0122  0.0193  0.0596  89  TYR   C CA  
1769 C C   . TYR   B 83  ? 0.1573 0.1793 0.2501 0.0102  0.0201  0.0564  89  TYR   C C   
1770 O O   . TYR   B 83  ? 0.1731 0.1953 0.2706 0.0090  0.0186  0.0549  89  TYR   C O   
1771 C CB  . TYR   B 83  ? 0.1477 0.1697 0.2165 0.0108  0.0144  0.0552  89  TYR   C CB  
1772 C CG  . TYR   B 83  ? 0.1382 0.1590 0.2018 0.0099  0.0132  0.0507  89  TYR   C CG  
1773 C CD1 . TYR   B 83  ? 0.1445 0.1646 0.1982 0.0114  0.0135  0.0516  89  TYR   C CD1 
1774 C CD2 . TYR   B 83  ? 0.1318 0.1519 0.2002 0.0080  0.0120  0.0456  89  TYR   C CD2 
1775 C CE1 . TYR   B 83  ? 0.1469 0.1660 0.1964 0.0107  0.0126  0.0477  89  TYR   C CE1 
1776 C CE2 . TYR   B 83  ? 0.1337 0.1528 0.1976 0.0075  0.0109  0.0419  89  TYR   C CE2 
1777 C CZ  . TYR   B 83  ? 0.1361 0.1547 0.1909 0.0087  0.0113  0.0430  89  TYR   C CZ  
1778 O OH  . TYR   B 83  ? 0.1508 0.1684 0.2017 0.0085  0.0106  0.0398  89  TYR   C OH  
1779 N N   . TYR   B 84  ? 0.1331 0.1548 0.2331 0.0099  0.0221  0.0551  90  TYR   C N   
1780 C CA  . TYR   B 84  ? 0.1359 0.1573 0.2501 0.0084  0.0224  0.0520  90  TYR   C CA  
1781 C C   . TYR   B 84  ? 0.1320 0.1537 0.2577 0.0094  0.0269  0.0550  90  TYR   C C   
1782 O O   . TYR   B 84  ? 0.1391 0.1609 0.2601 0.0108  0.0292  0.0574  90  TYR   C O   
1783 C CB  . TYR   B 84  ? 0.1239 0.1442 0.2362 0.0067  0.0184  0.0445  90  TYR   C CB  
1784 C CG  . TYR   B 84  ? 0.1192 0.1387 0.2241 0.0057  0.0146  0.0408  90  TYR   C CG  
1785 C CD1 . TYR   B 84  ? 0.1267 0.1459 0.2367 0.0052  0.0145  0.0407  90  TYR   C CD1 
1786 C CD2 . TYR   B 84  ? 0.1172 0.1360 0.2104 0.0054  0.0119  0.0378  90  TYR   C CD2 
1787 C CE1 . TYR   B 84  ? 0.1324 0.1506 0.2364 0.0045  0.0119  0.0375  90  TYR   C CE1 
1788 C CE2 . TYR   B 84  ? 0.1168 0.1345 0.2042 0.0046  0.0093  0.0348  90  TYR   C CE2 
1789 C CZ  . TYR   B 84  ? 0.1239 0.1413 0.2167 0.0043  0.0094  0.0347  90  TYR   C CZ  
1790 O OH  . TYR   B 84  ? 0.1161 0.1322 0.2039 0.0038  0.0078  0.0322  90  TYR   C OH  
1791 N N   . PRO   B 85  ? 0.1366 0.1583 0.2783 0.0087  0.0287  0.0549  91  PRO   C N   
1792 C CA  . PRO   B 85  ? 0.1382 0.1602 0.2935 0.0092  0.0326  0.0567  91  PRO   C CA  
1793 C C   . PRO   B 85  ? 0.1352 0.1570 0.2919 0.0079  0.0294  0.0504  91  PRO   C C   
1794 O O   . PRO   B 85  ? 0.1259 0.1471 0.2735 0.0068  0.0242  0.0445  91  PRO   C O   
1795 C CB  . PRO   B 85  ? 0.1532 0.1750 0.3255 0.0083  0.0338  0.0566  91  PRO   C CB  
1796 C CG  . PRO   B 85  ? 0.1518 0.1727 0.3194 0.0066  0.0285  0.0505  91  PRO   C CG  
1797 C CD  . PRO   B 85  ? 0.1425 0.1636 0.2910 0.0072  0.0264  0.0515  91  PRO   C CD  
1798 N N   . ALA   B 86  ? 0.1287 0.1511 0.2983 0.0082  0.0325  0.0515  92  ALA   C N   
1799 C CA  . ALA   B 86  ? 0.1432 0.1658 0.3181 0.0071  0.0291  0.0455  92  ALA   C CA  
1800 C C   . ALA   B 86  ? 0.1578 0.1795 0.3401 0.0053  0.0237  0.0383  92  ALA   C C   
1801 O O   . ALA   B 86  ? 0.1679 0.1893 0.3618 0.0048  0.0250  0.0389  92  ALA   C O   
1802 C CB  . ALA   B 86  ? 0.1466 0.1701 0.3380 0.0078  0.0340  0.0487  92  ALA   C CB  
1803 N N   . ARG   B 87  ? 0.1474 0.1685 0.3214 0.0046  0.0179  0.0316  93  ARG   C N   
1804 C CA  . ARG   B 87  ? 0.1496 0.1691 0.3261 0.0036  0.0127  0.0246  93  ARG   C CA  
1805 C C   . ARG   B 87  ? 0.1468 0.1655 0.3147 0.0037  0.0069  0.0181  93  ARG   C C   
1806 O O   . ARG   B 87  ? 0.1384 0.1576 0.2962 0.0043  0.0071  0.0194  93  ARG   C O   
1807 C CB  . ARG   B 87  ? 0.1491 0.1674 0.3155 0.0036  0.0125  0.0255  93  ARG   C CB  
1808 C CG  . ARG   B 87  ? 0.1429 0.1609 0.2894 0.0040  0.0110  0.0257  93  ARG   C CG  
1809 C CD  . ARG   B 87  ? 0.1507 0.1680 0.2896 0.0039  0.0115  0.0276  93  ARG   C CD  
1810 N NE  . ARG   B 87  ? 0.1408 0.1573 0.2633 0.0041  0.0090  0.0258  93  ARG   C NE  
1811 C CZ  . ARG   B 87  ? 0.1374 0.1523 0.2525 0.0039  0.0069  0.0231  93  ARG   C CZ  
1812 N NH1 . ARG   B 87  ? 0.1626 0.1764 0.2840 0.0037  0.0071  0.0219  93  ARG   C NH1 
1813 N NH2 . ARG   B 87  ? 0.1551 0.1692 0.2571 0.0041  0.0051  0.0218  93  ARG   C NH2 
1814 N N   . TYR   B 88  ? 0.1563 0.1731 0.3265 0.0035  0.0018  0.0111  94  TYR   C N   
1815 C CA  . TYR   B 88  ? 0.1657 0.1811 0.3247 0.0042  -0.0037 0.0051  94  TYR   C CA  
1816 C C   . TYR   B 88  ? 0.1473 0.1609 0.2876 0.0047  -0.0039 0.0055  94  TYR   C C   
1817 O O   . TYR   B 88  ? 0.1625 0.1750 0.3019 0.0044  -0.0029 0.0060  94  TYR   C O   
1818 C CB  . TYR   B 88  ? 0.1847 0.1982 0.3518 0.0046  -0.0094 -0.0028 94  TYR   C CB  
1819 C CG  . TYR   B 88  ? 0.2020 0.2174 0.3866 0.0043  -0.0110 -0.0046 94  TYR   C CG  
1820 C CD1 . TYR   B 88  ? 0.2093 0.2256 0.3915 0.0050  -0.0140 -0.0067 94  TYR   C CD1 
1821 C CD2 . TYR   B 88  ? 0.2030 0.2193 0.4081 0.0032  -0.0087 -0.0036 94  TYR   C CD2 
1822 C CE1 . TYR   B 88  ? 0.2262 0.2445 0.4262 0.0047  -0.0152 -0.0079 94  TYR   C CE1 
1823 C CE2 . TYR   B 88  ? 0.2150 0.2333 0.4385 0.0028  -0.0095 -0.0047 94  TYR   C CE2 
1824 C CZ  . TYR   B 88  ? 0.2278 0.2472 0.4490 0.0036  -0.0129 -0.0070 94  TYR   C CZ  
1825 O OH  . TYR   B 88  ? 0.2463 0.2678 0.4878 0.0031  -0.0136 -0.0080 94  TYR   C OH  
1826 N N   . GLN   B 89  ? 0.1249 0.1383 0.2517 0.0053  -0.0051 0.0054  95  GLN   C N   
1827 C CA  . GLN   B 89  ? 0.1206 0.1321 0.2312 0.0058  -0.0056 0.0053  95  GLN   C CA  
1828 C C   . GLN   B 89  ? 0.1218 0.1309 0.2242 0.0072  -0.0104 -0.0007 95  GLN   C C   
1829 O O   . GLN   B 89  ? 0.1378 0.1476 0.2417 0.0078  -0.0128 -0.0025 95  GLN   C O   
1830 C CB  . GLN   B 89  ? 0.1344 0.1474 0.2361 0.0055  -0.0024 0.0108  95  GLN   C CB  
1831 C CG  . GLN   B 89  ? 0.1459 0.1571 0.2330 0.0057  -0.0027 0.0108  95  GLN   C CG  
1832 C CD  . GLN   B 89  ? 0.1234 0.1360 0.2043 0.0052  0.0002  0.0162  95  GLN   C CD  
1833 O OE1 . GLN   B 89  ? 0.1312 0.1457 0.2179 0.0049  0.0032  0.0207  95  GLN   C OE1 
1834 N NE2 . GLN   B 89  ? 0.1283 0.1397 0.1975 0.0054  -0.0006 0.0157  95  GLN   C NE2 
1835 N N   . SER   B 90  ? 0.1137 0.1199 0.2078 0.0082  -0.0119 -0.0037 96  SER   C N   
1836 C CA  . SER   B 90  ? 0.1166 0.1196 0.2010 0.0104  -0.0162 -0.0091 96  SER   C CA  
1837 C C   . SER   B 90  ? 0.1167 0.1186 0.1858 0.0112  -0.0151 -0.0071 96  SER   C C   
1838 O O   . SER   B 90  ? 0.1156 0.1185 0.1809 0.0099  -0.0114 -0.0023 96  SER   C O   
1839 C CB  . SER   B 90  ? 0.1388 0.1384 0.2226 0.0118  -0.0180 -0.0137 96  SER   C CB  
1840 O OG  . SER   B 90  ? 0.1494 0.1479 0.2264 0.0115  -0.0143 -0.0107 96  SER   C OG  
1841 N N   . HIS   B 91  ? 0.1244 0.1239 0.1850 0.0134  -0.0186 -0.0109 97  HIS   C N   
1842 C CA  . HIS   B 91  ? 0.1296 0.1274 0.1762 0.0146  -0.0176 -0.0095 97  HIS   C CA  
1843 C C   . HIS   B 91  ? 0.1151 0.1157 0.1616 0.0127  -0.0148 -0.0045 97  HIS   C C   
1844 O O   . HIS   B 91  ? 0.1335 0.1333 0.1716 0.0124  -0.0122 -0.0016 97  HIS   C O   
1845 C CB  . HIS   B 91  ? 0.1409 0.1356 0.1789 0.0154  -0.0150 -0.0088 97  HIS   C CB  
1846 C CG  . HIS   B 91  ? 0.1580 0.1489 0.1933 0.0180  -0.0174 -0.0138 97  HIS   C CG  
1847 N ND1 . HIS   B 91  ? 0.1903 0.1770 0.2130 0.0216  -0.0193 -0.0168 97  HIS   C ND1 
1848 C CD2 . HIS   B 91  ? 0.1728 0.1632 0.2162 0.0178  -0.0182 -0.0165 97  HIS   C CD2 
1849 C CE1 . HIS   B 91  ? 0.2001 0.1837 0.2225 0.0237  -0.0213 -0.0214 97  HIS   C CE1 
1850 N NE2 . HIS   B 91  ? 0.1953 0.1810 0.2303 0.0214  -0.0207 -0.0216 97  HIS   C NE2 
1851 N N   . LEU   B 92  ? 0.1097 0.1132 0.1654 0.0117  -0.0153 -0.0037 98  LEU   C N   
1852 C CA  . LEU   B 92  ? 0.1146 0.1205 0.1705 0.0104  -0.0123 0.0007  98  LEU   C CA  
1853 C C   . LEU   B 92  ? 0.1158 0.1218 0.1689 0.0115  -0.0143 -0.0006 98  LEU   C C   
1854 O O   . LEU   B 92  ? 0.1184 0.1243 0.1763 0.0128  -0.0181 -0.0043 98  LEU   C O   
1855 C CB  . LEU   B 92  ? 0.1184 0.1275 0.1874 0.0088  -0.0100 0.0035  98  LEU   C CB  
1856 C CG  . LEU   B 92  ? 0.1321 0.1432 0.2005 0.0079  -0.0064 0.0085  98  LEU   C CG  
1857 C CD1 . LEU   B 92  ? 0.1431 0.1538 0.2027 0.0072  -0.0041 0.0116  98  LEU   C CD1 
1858 C CD2 . LEU   B 92  ? 0.1627 0.1764 0.2446 0.0072  -0.0037 0.0113  98  LEU   C CD2 
1859 N N   . MET   B 93  ? 0.1107 0.1167 0.1568 0.0112  -0.0122 0.0023  99  MET   C N   
1860 C CA  . MET   B 93  ? 0.1048 0.1108 0.1480 0.0123  -0.0133 0.0018  99  MET   C CA  
1861 C C   . MET   B 93  ? 0.1086 0.1169 0.1553 0.0111  -0.0099 0.0056  99  MET   C C   
1862 O O   . MET   B 93  ? 0.1228 0.1313 0.1659 0.0100  -0.0069 0.0087  99  MET   C O   
1863 C CB  . MET   B 93  ? 0.1256 0.1285 0.1558 0.0134  -0.0134 0.0016  99  MET   C CB  
1864 C CG  . MET   B 93  ? 0.1436 0.1436 0.1683 0.0153  -0.0158 -0.0016 99  MET   C CG  
1865 S SD  . MET   B 93  ? 0.1608 0.1569 0.1715 0.0168  -0.0143 -0.0007 99  MET   C SD  
1866 C CE  . MET   B 93  ? 0.1688 0.1659 0.1799 0.0138  -0.0098 0.0035  99  MET   C CE  
1867 N N   . LEU   B 94  ? 0.1015 0.1112 0.1543 0.0117  -0.0102 0.0054  100 LEU   C N   
1868 C CA  . LEU   B 94  ? 0.1051 0.1164 0.1604 0.0112  -0.0062 0.0091  100 LEU   C CA  
1869 C C   . LEU   B 94  ? 0.0971 0.1073 0.1453 0.0121  -0.0059 0.0093  100 LEU   C C   
1870 O O   . LEU   B 94  ? 0.1121 0.1213 0.1587 0.0135  -0.0092 0.0065  100 LEU   C O   
1871 C CB  . LEU   B 94  ? 0.1171 0.1311 0.1875 0.0112  -0.0054 0.0097  100 LEU   C CB  
1872 C CG  . LEU   B 94  ? 0.1341 0.1494 0.2151 0.0102  -0.0049 0.0100  100 LEU   C CG  
1873 C CD1 . LEU   B 94  ? 0.1611 0.1790 0.2586 0.0103  -0.0033 0.0111  100 LEU   C CD1 
1874 C CD2 . LEU   B 94  ? 0.1360 0.1512 0.2124 0.0092  -0.0012 0.0139  100 LEU   C CD2 
1875 N N   . ALA   B 95  ? 0.1102 0.1205 0.1547 0.0118  -0.0022 0.0124  101 ALA   C N   
1876 C CA  . ALA   B 95  ? 0.1098 0.1191 0.1494 0.0128  -0.0009 0.0129  101 ALA   C CA  
1877 C C   . ALA   B 95  ? 0.1076 0.1181 0.1508 0.0130  0.0037  0.0164  101 ALA   C C   
1878 O O   . ALA   B 95  ? 0.1051 0.1167 0.1508 0.0125  0.0061  0.0189  101 ALA   C O   
1879 C CB  . ALA   B 95  ? 0.1226 0.1292 0.1495 0.0125  -0.0011 0.0127  101 ALA   C CB  
1880 N N   . VAL   B 96  ? 0.1041 0.1141 0.1463 0.0142  0.0054  0.0168  102 VAL   C N   
1881 C CA  . VAL   B 96  ? 0.1153 0.1255 0.1580 0.0151  0.0106  0.0202  102 VAL   C CA  
1882 C C   . VAL   B 96  ? 0.1225 0.1302 0.1514 0.0151  0.0117  0.0210  102 VAL   C C   
1883 O O   . VAL   B 96  ? 0.1457 0.1513 0.1667 0.0151  0.0101  0.0190  102 VAL   C O   
1884 C CB  . VAL   B 96  ? 0.1252 0.1357 0.1734 0.0166  0.0120  0.0200  102 VAL   C CB  
1885 C CG1 . VAL   B 96  ? 0.1625 0.1724 0.2095 0.0181  0.0181  0.0236  102 VAL   C CG1 
1886 C CG2 . VAL   B 96  ? 0.1330 0.1462 0.1963 0.0166  0.0097  0.0187  102 VAL   C CG2 
1887 N N   . GLY   B 97  ? 0.1381 0.1460 0.1648 0.0151  0.0141  0.0237  103 GLY   C N   
1888 C CA  . GLY   B 97  ? 0.1515 0.1573 0.1658 0.0152  0.0142  0.0240  103 GLY   C CA  
1889 C C   . GLY   B 97  ? 0.1459 0.1524 0.1588 0.0155  0.0159  0.0271  103 GLY   C C   
1890 O O   . GLY   B 97  ? 0.1775 0.1861 0.1995 0.0154  0.0173  0.0292  103 GLY   C O   
1891 N N   . HIS   B 98  ? 0.1524 0.1571 0.1545 0.0161  0.0156  0.0274  104 HIS   C N   
1892 C CA  . HIS   B 98  ? 0.1558 0.1609 0.1547 0.0170  0.0168  0.0304  104 HIS   C CA  
1893 C C   . HIS   B 98  ? 0.1417 0.1480 0.1420 0.0150  0.0132  0.0300  104 HIS   C C   
1894 O O   . HIS   B 98  ? 0.1424 0.1479 0.1394 0.0133  0.0095  0.0270  104 HIS   C O   
1895 C CB  . HIS   B 98  ? 0.1883 0.1905 0.1743 0.0190  0.0174  0.0305  104 HIS   C CB  
1896 C CG  . HIS   B 98  ? 0.1982 0.2005 0.1797 0.0209  0.0188  0.0341  104 HIS   C CG  
1897 N ND1 . HIS   B 98  ? 0.2328 0.2358 0.2186 0.0231  0.0242  0.0387  104 HIS   C ND1 
1898 C CD2 . HIS   B 98  ? 0.2210 0.2229 0.1952 0.0210  0.0155  0.0339  104 HIS   C CD2 
1899 C CE1 . HIS   B 98  ? 0.2606 0.2634 0.2403 0.0247  0.0240  0.0414  104 HIS   C CE1 
1900 N NE2 . HIS   B 98  ? 0.2583 0.2605 0.2307 0.0235  0.0185  0.0384  104 HIS   C NE2 
1901 N N   . SER   B 99  ? 0.1464 0.1544 0.1514 0.0153  0.0147  0.0333  105 SER   C N   
1902 C CA  . SER   B 99  ? 0.1547 0.1641 0.1616 0.0137  0.0119  0.0334  105 SER   C CA  
1903 C C   . SER   B 99  ? 0.1659 0.1763 0.1740 0.0154  0.0145  0.0382  105 SER   C C   
1904 O O   . SER   B 99  ? 0.1881 0.1996 0.2045 0.0162  0.0183  0.0410  105 SER   C O   
1905 C CB  . SER   B 99  ? 0.1566 0.1674 0.1739 0.0118  0.0106  0.0315  105 SER   C CB  
1906 O OG  . SER   B 99  ? 0.1628 0.1746 0.1826 0.0105  0.0088  0.0319  105 SER   C OG  
1907 N N   . GLU   B 100 ? 0.1611 0.1713 0.1626 0.0158  0.0124  0.0391  106 GLU   C N   
1908 C CA  . GLU   B 100 ? 0.1825 0.1936 0.1840 0.0176  0.0141  0.0437  106 GLU   C CA  
1909 C C   . GLU   B 100 ? 0.1605 0.1731 0.1663 0.0156  0.0106  0.0432  106 GLU   C C   
1910 O O   . GLU   B 100 ? 0.1504 0.1631 0.1569 0.0132  0.0072  0.0393  106 GLU   C O   
1911 C CB  . GLU   B 100 ? 0.2300 0.2391 0.2176 0.0205  0.0132  0.0447  106 GLU   C CB  
1912 C CG  . GLU   B 100 ? 0.3034 0.3102 0.2847 0.0233  0.0173  0.0458  106 GLU   C CG  
1913 C CD  . GLU   B 100 ? 0.3384 0.3425 0.3043 0.0265  0.0158  0.0457  106 GLU   C CD  
1914 O OE1 . GLU   B 100 ? 0.4530 0.4574 0.4138 0.0276  0.0129  0.0471  106 GLU   C OE1 
1915 O OE2 . GLU   B 100 ? 0.3521 0.3537 0.3112 0.0280  0.0175  0.0442  106 GLU   C OE2 
1916 N N   . PRO   B 101 ? 0.1704 0.1844 0.1797 0.0166  0.0119  0.0473  107 PRO   C N   
1917 C CA  . PRO   B 101 ? 0.1649 0.1805 0.1799 0.0146  0.0090  0.0468  107 PRO   C CA  
1918 C C   . PRO   B 101 ? 0.1588 0.1741 0.1677 0.0134  0.0039  0.0437  107 PRO   C C   
1919 O O   . PRO   B 101 ? 0.1563 0.1722 0.1707 0.0110  0.0020  0.0412  107 PRO   C O   
1920 C CB  . PRO   B 101 ? 0.1921 0.2088 0.2093 0.0169  0.0113  0.0525  107 PRO   C CB  
1921 C CG  . PRO   B 101 ? 0.2185 0.2346 0.2384 0.0188  0.0167  0.0555  107 PRO   C CG  
1922 C CD  . PRO   B 101 ? 0.1969 0.2109 0.2077 0.0196  0.0169  0.0530  107 PRO   C CD  
1923 N N   . GLY   B 102 ? 0.1622 0.1762 0.1602 0.0152  0.0018  0.0434  108 GLY   C N   
1924 C CA  . GLY   B 102 ? 0.1685 0.1823 0.1628 0.0139  -0.0035 0.0402  108 GLY   C CA  
1925 C C   . GLY   B 102 ? 0.1473 0.1599 0.1427 0.0113  -0.0046 0.0355  108 GLY   C C   
1926 O O   . GLY   B 102 ? 0.1674 0.1798 0.1626 0.0098  -0.0082 0.0329  108 GLY   C O   
1927 N N   . ASP   B 103 ? 0.1386 0.1503 0.1353 0.0111  -0.0015 0.0345  109 ASP   C N   
1928 C CA  . ASP   B 103 ? 0.1297 0.1400 0.1271 0.0092  -0.0024 0.0304  109 ASP   C CA  
1929 C C   . ASP   B 103 ? 0.1205 0.1317 0.1261 0.0071  -0.0025 0.0294  109 ASP   C C   
1930 O O   . ASP   B 103 ? 0.1149 0.1248 0.1206 0.0059  -0.0034 0.0265  109 ASP   C O   
1931 C CB  . ASP   B 103 ? 0.1419 0.1510 0.1378 0.0102  0.0006  0.0299  109 ASP   C CB  
1932 C CG  . ASP   B 103 ? 0.1579 0.1653 0.1442 0.0124  0.0009  0.0301  109 ASP   C CG  
1933 O OD1 . ASP   B 103 ? 0.1690 0.1752 0.1491 0.0124  -0.0024 0.0282  109 ASP   C OD1 
1934 O OD2 . ASP   B 103 ? 0.1668 0.1737 0.1520 0.0143  0.0046  0.0320  109 ASP   C OD2 
1935 N N   . CYS   B 104 ? 0.1128 0.1258 0.1253 0.0070  -0.0014 0.0318  110 CYS   C N   
1936 C CA  . CYS   B 104 ? 0.1059 0.1192 0.1254 0.0055  -0.0014 0.0304  110 CYS   C CA  
1937 C C   . CYS   B 104 ? 0.1057 0.1184 0.1242 0.0042  -0.0038 0.0286  110 CYS   C C   
1938 O O   . CYS   B 104 ? 0.1271 0.1404 0.1437 0.0042  -0.0060 0.0295  110 CYS   C O   
1939 C CB  . CYS   B 104 ? 0.1178 0.1329 0.1447 0.0056  -0.0001 0.0333  110 CYS   C CB  
1940 S SG  . CYS   B 104 ? 0.1354 0.1512 0.1684 0.0067  0.0035  0.0350  110 CYS   C SG  
1941 N N   . GLY   B 105 ? 0.0983 0.1094 0.1182 0.0033  -0.0034 0.0261  111 GLY   C N   
1942 C CA  . GLY   B 105 ? 0.1087 0.1188 0.1290 0.0022  -0.0045 0.0248  111 GLY   C CA  
1943 C C   . GLY   B 105 ? 0.1107 0.1185 0.1256 0.0021  -0.0051 0.0225  111 GLY   C C   
1944 O O   . GLY   B 105 ? 0.1233 0.1297 0.1393 0.0014  -0.0051 0.0214  111 GLY   C O   
1945 N N   . GLY   B 106 ? 0.1127 0.1201 0.1225 0.0029  -0.0052 0.0220  112 GLY   C N   
1946 C CA  . GLY   B 106 ? 0.1196 0.1246 0.1246 0.0029  -0.0055 0.0198  112 GLY   C CA  
1947 C C   . GLY   B 106 ? 0.1082 0.1113 0.1139 0.0030  -0.0040 0.0183  112 GLY   C C   
1948 O O   . GLY   B 106 ? 0.1081 0.1117 0.1158 0.0037  -0.0030 0.0184  112 GLY   C O   
1949 N N   . ILE   B 107 ? 0.1075 0.1083 0.1117 0.0027  -0.0039 0.0170  113 ILE   C N   
1950 C CA  . ILE   B 107 ? 0.1070 0.1056 0.1106 0.0035  -0.0023 0.0161  113 ILE   C CA  
1951 C C   . ILE   B 107 ? 0.1016 0.0990 0.1011 0.0047  -0.0021 0.0149  113 ILE   C C   
1952 O O   . ILE   B 107 ? 0.1051 0.1020 0.1017 0.0047  -0.0025 0.0144  113 ILE   C O   
1953 C CB  . ILE   B 107 ? 0.1343 0.1306 0.1387 0.0029  -0.0016 0.0160  113 ILE   C CB  
1954 C CG1 . ILE   B 107 ? 0.1807 0.1780 0.1908 0.0022  -0.0008 0.0174  113 ILE   C CG1 
1955 C CG2 . ILE   B 107 ? 0.1350 0.1279 0.1361 0.0044  0.0004  0.0153  113 ILE   C CG2 
1956 C CD1 . ILE   B 107 ? 0.2340 0.2298 0.2484 0.0014  0.0004  0.0181  113 ILE   C CD1 
1957 N N   . LEU   B 108 ? 0.0964 0.0931 0.0957 0.0061  -0.0016 0.0142  114 LEU   C N   
1958 C CA  . LEU   B 108 ? 0.0923 0.0875 0.0885 0.0077  -0.0016 0.0129  114 LEU   C CA  
1959 C C   . LEU   B 108 ? 0.0994 0.0911 0.0923 0.0089  -0.0005 0.0126  114 LEU   C C   
1960 O O   . LEU   B 108 ? 0.1034 0.0943 0.0968 0.0094  0.0003  0.0129  114 LEU   C O   
1961 C CB  . LEU   B 108 ? 0.1006 0.0972 0.0994 0.0087  -0.0026 0.0121  114 LEU   C CB  
1962 C CG  . LEU   B 108 ? 0.1088 0.1041 0.1054 0.0107  -0.0035 0.0105  114 LEU   C CG  
1963 C CD1 . LEU   B 108 ? 0.1269 0.1226 0.1227 0.0107  -0.0032 0.0107  114 LEU   C CD1 
1964 C CD2 . LEU   B 108 ? 0.1243 0.1212 0.1254 0.0116  -0.0052 0.0091  114 LEU   C CD2 
1965 N N   . ARG   B 109 ? 0.1059 0.0954 0.0955 0.0095  0.0001  0.0124  115 ARG   C N   
1966 C CA  . ARG   B 109 ? 0.1104 0.0963 0.0970 0.0110  0.0019  0.0129  115 ARG   C CA  
1967 C C   . ARG   B 109 ? 0.1158 0.0998 0.0981 0.0133  0.0016  0.0122  115 ARG   C C   
1968 O O   . ARG   B 109 ? 0.1236 0.1086 0.1061 0.0130  0.0006  0.0115  115 ARG   C O   
1969 C CB  . ARG   B 109 ? 0.1492 0.1338 0.1379 0.0094  0.0035  0.0139  115 ARG   C CB  
1970 C CG  . ARG   B 109 ? 0.1800 0.1645 0.1684 0.0083  0.0026  0.0131  115 ARG   C CG  
1971 C CD  . ARG   B 109 ? 0.2189 0.2020 0.2107 0.0067  0.0033  0.0133  115 ARG   C CD  
1972 N NE  . ARG   B 109 ? 0.2756 0.2615 0.2715 0.0046  0.0016  0.0132  115 ARG   C NE  
1973 C CZ  . ARG   B 109 ? 0.3659 0.3517 0.3670 0.0034  0.0022  0.0141  115 ARG   C CZ  
1974 N NH1 . ARG   B 109 ? 0.4170 0.3999 0.4201 0.0041  0.0053  0.0154  115 ARG   C NH1 
1975 N NH2 . ARG   B 109 ? 0.4044 0.3931 0.4093 0.0018  0.0000  0.0140  115 ARG   C NH2 
1976 N N   . CYS   B 110 ? 0.1282 0.1090 0.1062 0.0160  0.0028  0.0126  116 CYS   C N   
1977 C CA  . CYS   B 110 ? 0.1428 0.1213 0.1161 0.0187  0.0025  0.0124  116 CYS   C CA  
1978 C C   . CYS   B 110 ? 0.1528 0.1269 0.1232 0.0200  0.0061  0.0146  116 CYS   C C   
1979 O O   . CYS   B 110 ? 0.1576 0.1311 0.1313 0.0183  0.0086  0.0159  116 CYS   C O   
1980 C CB  . CYS   B 110 ? 0.1407 0.1189 0.1104 0.0217  0.0001  0.0109  116 CYS   C CB  
1981 S SG  . CYS   B 110 ? 0.1460 0.1211 0.1110 0.0241  0.0020  0.0115  116 CYS   C SG  
1982 N N   . GLN   B 111 ? 0.1619 0.1330 0.1271 0.0232  0.0066  0.0152  117 GLN   C N   
1983 C CA  . GLN   B 111 ? 0.1887 0.1553 0.1515 0.0249  0.0108  0.0179  117 GLN   C CA  
1984 C C   . GLN   B 111 ? 0.1877 0.1520 0.1483 0.0264  0.0138  0.0195  117 GLN   C C   
1985 O O   . GLN   B 111 ? 0.2145 0.1756 0.1763 0.0269  0.0183  0.0222  117 GLN   C O   
1986 C CB  . GLN   B 111 ? 0.2073 0.1707 0.1639 0.0289  0.0110  0.0188  117 GLN   C CB  
1987 C CG  . GLN   B 111 ? 0.2204 0.1828 0.1693 0.0331  0.0085  0.0179  117 GLN   C CG  
1988 C CD  . GLN   B 111 ? 0.3650 0.3244 0.3076 0.0373  0.0080  0.0189  117 GLN   C CD  
1989 O OE1 . GLN   B 111 ? 0.4118 0.3734 0.3554 0.0377  0.0042  0.0171  117 GLN   C OE1 
1990 N NE2 . GLN   B 111 ? 0.3764 0.3309 0.3130 0.0408  0.0121  0.0220  117 GLN   C NE2 
1991 N N   . HIS   B 112 ? 0.1674 0.1330 0.1257 0.0273  0.0118  0.0179  118 HIS   C N   
1992 C CA  . HIS   B 112 ? 0.1803 0.1432 0.1357 0.0292  0.0150  0.0193  118 HIS   C CA  
1993 C C   . HIS   B 112 ? 0.1823 0.1475 0.1456 0.0257  0.0165  0.0197  118 HIS   C C   
1994 O O   . HIS   B 112 ? 0.2048 0.1679 0.1673 0.0270  0.0200  0.0212  118 HIS   C O   
1995 C CB  . HIS   B 112 ? 0.1869 0.1491 0.1348 0.0328  0.0120  0.0170  118 HIS   C CB  
1996 C CG  . HIS   B 112 ? 0.1816 0.1417 0.1216 0.0368  0.0096  0.0164  118 HIS   C CG  
1997 N ND1 . HIS   B 112 ? 0.1655 0.1288 0.1071 0.0364  0.0041  0.0134  118 HIS   C ND1 
1998 C CD2 . HIS   B 112 ? 0.2140 0.1689 0.1450 0.0417  0.0121  0.0186  118 HIS   C CD2 
1999 C CE1 . HIS   B 112 ? 0.1851 0.1457 0.1194 0.0406  0.0029  0.0136  118 HIS   C CE1 
2000 N NE2 . HIS   B 112 ? 0.2249 0.1803 0.1520 0.0440  0.0075  0.0168  118 HIS   C NE2 
2001 N N   . GLY   B 113 ? 0.1608 0.1305 0.1314 0.0215  0.0138  0.0184  119 GLY   C N   
2002 C CA  . GLY   B 113 ? 0.1574 0.1297 0.1355 0.0183  0.0143  0.0187  119 GLY   C CA  
2003 C C   . GLY   B 113 ? 0.1380 0.1150 0.1193 0.0160  0.0101  0.0165  119 GLY   C C   
2004 O O   . GLY   B 113 ? 0.1373 0.1161 0.1174 0.0158  0.0071  0.0149  119 GLY   C O   
2005 N N   . VAL   B 114 ? 0.1371 0.1161 0.1232 0.0144  0.0103  0.0168  120 VAL   C N   
2006 C CA  . VAL   B 114 ? 0.1274 0.1108 0.1176 0.0123  0.0072  0.0155  120 VAL   C CA  
2007 C C   . VAL   B 114 ? 0.1183 0.1017 0.1052 0.0143  0.0053  0.0135  120 VAL   C C   
2008 O O   . VAL   B 114 ? 0.1364 0.1176 0.1205 0.0165  0.0066  0.0132  120 VAL   C O   
2009 C CB  . VAL   B 114 ? 0.1341 0.1193 0.1311 0.0102  0.0081  0.0168  120 VAL   C CB  
2010 C CG1 . VAL   B 114 ? 0.1430 0.1323 0.1438 0.0086  0.0054  0.0160  120 VAL   C CG1 
2011 C CG2 . VAL   B 114 ? 0.1516 0.1370 0.1534 0.0080  0.0089  0.0181  120 VAL   C CG2 
2012 N N   . VAL   B 115 ? 0.1082 0.0941 0.0961 0.0137  0.0023  0.0120  121 VAL   C N   
2013 C CA  . VAL   B 115 ? 0.1164 0.1030 0.1038 0.0153  -0.0003 0.0097  121 VAL   C CA  
2014 C C   . VAL   B 115 ? 0.1195 0.1091 0.1134 0.0136  -0.0010 0.0094  121 VAL   C C   
2015 O O   . VAL   B 115 ? 0.1257 0.1149 0.1202 0.0149  -0.0022 0.0075  121 VAL   C O   
2016 C CB  . VAL   B 115 ? 0.1167 0.1046 0.1040 0.0155  -0.0027 0.0086  121 VAL   C CB  
2017 C CG1 . VAL   B 115 ? 0.1359 0.1251 0.1255 0.0167  -0.0058 0.0060  121 VAL   C CG1 
2018 C CG2 . VAL   B 115 ? 0.1432 0.1280 0.1241 0.0175  -0.0019 0.0090  121 VAL   C CG2 
2019 N N   . GLY   B 116 ? 0.1121 0.1047 0.1111 0.0108  -0.0008 0.0111  122 GLY   C N   
2020 C CA  . GLY   B 116 ? 0.1274 0.1229 0.1329 0.0094  -0.0012 0.0116  122 GLY   C CA  
2021 C C   . GLY   B 116 ? 0.0978 0.0960 0.1062 0.0072  -0.0011 0.0138  122 GLY   C C   
2022 O O   . GLY   B 116 ? 0.1129 0.1104 0.1186 0.0066  -0.0008 0.0145  122 GLY   C O   
2023 N N   . ILE   B 117 ? 0.0944 0.0954 0.1084 0.0062  -0.0014 0.0149  123 ILE   C N   
2024 C CA  . ILE   B 117 ? 0.0944 0.0978 0.1101 0.0048  -0.0015 0.0171  123 ILE   C CA  
2025 C C   . ILE   B 117 ? 0.0917 0.0972 0.1106 0.0049  -0.0017 0.0179  123 ILE   C C   
2026 O O   . ILE   B 117 ? 0.1034 0.1095 0.1270 0.0054  -0.0017 0.0171  123 ILE   C O   
2027 C CB  . ILE   B 117 ? 0.1045 0.1090 0.1240 0.0037  -0.0011 0.0190  123 ILE   C CB  
2028 C CG1 . ILE   B 117 ? 0.1224 0.1272 0.1471 0.0041  -0.0004 0.0189  123 ILE   C CG1 
2029 C CG2 . ILE   B 117 ? 0.1343 0.1368 0.1519 0.0033  -0.0006 0.0189  123 ILE   C CG2 
2030 C CD1 . ILE   B 117 ? 0.1311 0.1376 0.1612 0.0031  0.0001  0.0212  123 ILE   C CD1 
2031 N N   . VAL   B 118 ? 0.0907 0.0974 0.1076 0.0047  -0.0016 0.0195  124 VAL   C N   
2032 C CA  . VAL   B 118 ? 0.0962 0.1049 0.1163 0.0052  -0.0007 0.0212  124 VAL   C CA  
2033 C C   . VAL   B 118 ? 0.0968 0.1072 0.1238 0.0049  0.0000  0.0231  124 VAL   C C   
2034 O O   . VAL   B 118 ? 0.0975 0.1084 0.1250 0.0043  -0.0003 0.0245  124 VAL   C O   
2035 C CB  . VAL   B 118 ? 0.1005 0.1094 0.1154 0.0055  -0.0004 0.0230  124 VAL   C CB  
2036 C CG1 . VAL   B 118 ? 0.1099 0.1204 0.1275 0.0066  0.0016  0.0256  124 VAL   C CG1 
2037 C CG2 . VAL   B 118 ? 0.1121 0.1190 0.1209 0.0059  -0.0009 0.0210  124 VAL   C CG2 
2038 N N   . SER   B 119 ? 0.0919 0.1033 0.1253 0.0054  0.0010  0.0233  125 SER   C N   
2039 C CA  . SER   B 119 ? 0.0962 0.1091 0.1378 0.0052  0.0021  0.0251  125 SER   C CA  
2040 C C   . SER   B 119 ? 0.1043 0.1187 0.1519 0.0059  0.0044  0.0278  125 SER   C C   
2041 O O   . SER   B 119 ? 0.1071 0.1228 0.1602 0.0060  0.0060  0.0308  125 SER   C O   
2042 C CB  . SER   B 119 ? 0.1162 0.1280 0.1624 0.0050  0.0010  0.0218  125 SER   C CB  
2043 O OG  . SER   B 119 ? 0.1203 0.1332 0.1756 0.0048  0.0020  0.0229  125 SER   C OG  
2044 N N   . THR   B 120 ? 0.0987 0.1130 0.1465 0.0066  0.0051  0.0271  126 THR   C N   
2045 C CA  . THR   B 120 ? 0.0994 0.1151 0.1545 0.0075  0.0082  0.0300  126 THR   C CA  
2046 C C   . THR   B 120 ? 0.0937 0.1089 0.1424 0.0088  0.0100  0.0315  126 THR   C C   
2047 O O   . THR   B 120 ? 0.0987 0.1126 0.1393 0.0087  0.0082  0.0291  126 THR   C O   
2048 C CB  . THR   B 120 ? 0.0993 0.1155 0.1663 0.0072  0.0078  0.0276  126 THR   C CB  
2049 O OG1 . THR   B 120 ? 0.1079 0.1233 0.1726 0.0075  0.0058  0.0241  126 THR   C OG1 
2050 C CG2 . THR   B 120 ? 0.1189 0.1348 0.1915 0.0063  0.0057  0.0251  126 THR   C CG2 
2051 N N   . GLY   B 121 ? 0.0993 0.1153 0.1520 0.0102  0.0139  0.0353  127 GLY   C N   
2052 C CA  . GLY   B 121 ? 0.1307 0.1460 0.1785 0.0119  0.0166  0.0369  127 GLY   C CA  
2053 C C   . GLY   B 121 ? 0.1583 0.1746 0.2158 0.0134  0.0217  0.0411  127 GLY   C C   
2054 O O   . GLY   B 121 ? 0.1974 0.2144 0.2599 0.0138  0.0240  0.0448  127 GLY   C O   
2055 N N   . GLY   B 122 ? 0.2004 0.2166 0.2612 0.0143  0.0241  0.0411  128 GLY   C N   
2056 C CA  . GLY   B 122 ? 0.2192 0.2362 0.2905 0.0160  0.0299  0.0456  128 GLY   C CA  
2057 C C   . GLY   B 122 ? 0.2271 0.2442 0.3043 0.0164  0.0311  0.0441  128 GLY   C C   
2058 O O   . GLY   B 122 ? 0.2199 0.2372 0.2984 0.0149  0.0266  0.0392  128 GLY   C O   
2059 N N   . ASN   B 123 ? 0.2025 0.2194 0.2840 0.0187  0.0375  0.0486  129 ASN   C N   
2060 C CA  . ASN   B 123 ? 0.1999 0.2173 0.2902 0.0194  0.0396  0.0480  129 ASN   C CA  
2061 C C   . ASN   B 123 ? 0.1832 0.1994 0.2632 0.0191  0.0359  0.0436  129 ASN   C C   
2062 O O   . ASN   B 123 ? 0.2196 0.2369 0.3080 0.0184  0.0340  0.0406  129 ASN   C O   
2063 C CB  . ASN   B 123 ? 0.2232 0.2433 0.3346 0.0175  0.0379  0.0459  129 ASN   C CB  
2064 C CG  . ASN   B 123 ? 0.2833 0.3045 0.4113 0.0187  0.0446  0.0512  129 ASN   C CG  
2065 O OD1 . ASN   B 123 ? 0.3093 0.3294 0.4352 0.0214  0.0518  0.0567  129 ASN   C OD1 
2066 N ND2 . ASN   B 123 ? 0.2774 0.3005 0.4229 0.0168  0.0426  0.0495  129 ASN   C ND2 
2067 N N   . GLY   B 124 ? 0.1679 0.1819 0.2303 0.0196  0.0345  0.0430  130 GLY   C N   
2068 C CA  . GLY   B 124 ? 0.1700 0.1825 0.2231 0.0194  0.0313  0.0390  130 GLY   C CA  
2069 C C   . GLY   B 124 ? 0.1447 0.1579 0.1986 0.0169  0.0246  0.0337  130 GLY   C C   
2070 O O   . GLY   B 124 ? 0.1511 0.1632 0.2006 0.0168  0.0223  0.0307  130 GLY   C O   
2071 N N   . LEU   B 125 ? 0.1248 0.1392 0.1836 0.0152  0.0218  0.0328  131 LEU   C N   
2072 C CA  . LEU   B 125 ? 0.1272 0.1418 0.1857 0.0134  0.0159  0.0282  131 LEU   C CA  
2073 C C   . LEU   B 125 ? 0.1209 0.1345 0.1700 0.0123  0.0136  0.0279  131 LEU   C C   
2074 O O   . LEU   B 125 ? 0.1607 0.1747 0.2095 0.0125  0.0158  0.0311  131 LEU   C O   
2075 C CB  . LEU   B 125 ? 0.1447 0.1613 0.2185 0.0125  0.0140  0.0264  131 LEU   C CB  
2076 C CG  . LEU   B 125 ? 0.1691 0.1870 0.2549 0.0134  0.0154  0.0263  131 LEU   C CG  
2077 C CD1 . LEU   B 125 ? 0.2125 0.2327 0.3167 0.0128  0.0155  0.0264  131 LEU   C CD1 
2078 C CD2 . LEU   B 125 ? 0.1788 0.1959 0.2608 0.0137  0.0116  0.0225  131 LEU   C CD2 
2079 N N   . VAL   B 126 ? 0.0984 0.1108 0.1411 0.0114  0.0097  0.0244  132 VAL   C N   
2080 C CA  . VAL   B 126 ? 0.1009 0.1125 0.1370 0.0102  0.0075  0.0238  132 VAL   C CA  
2081 C C   . VAL   B 126 ? 0.0910 0.1028 0.1320 0.0093  0.0041  0.0205  132 VAL   C C   
2082 O O   . VAL   B 126 ? 0.1026 0.1137 0.1442 0.0098  0.0018  0.0175  132 VAL   C O   
2083 C CB  . VAL   B 126 ? 0.1075 0.1170 0.1313 0.0102  0.0064  0.0228  132 VAL   C CB  
2084 C CG1 . VAL   B 126 ? 0.1392 0.1472 0.1603 0.0107  0.0051  0.0200  132 VAL   C CG1 
2085 C CG2 . VAL   B 126 ? 0.1191 0.1280 0.1386 0.0090  0.0041  0.0221  132 VAL   C CG2 
2086 N N   . GLY   B 127 ? 0.0886 0.1009 0.1318 0.0085  0.0035  0.0209  133 GLY   C N   
2087 C CA  . GLY   B 127 ? 0.0953 0.1071 0.1417 0.0080  0.0005  0.0176  133 GLY   C CA  
2088 C C   . GLY   B 127 ? 0.0946 0.1048 0.1330 0.0074  -0.0007 0.0169  133 GLY   C C   
2089 O O   . GLY   B 127 ? 0.1022 0.1128 0.1379 0.0068  0.0006  0.0196  133 GLY   C O   
2090 N N   . PHE   B 128 ? 0.0941 0.1024 0.1294 0.0078  -0.0031 0.0137  134 PHE   C N   
2091 C CA  . PHE   B 128 ? 0.0983 0.1046 0.1267 0.0076  -0.0036 0.0130  134 PHE   C CA  
2092 C C   . PHE   B 128 ? 0.0934 0.0987 0.1248 0.0080  -0.0049 0.0107  134 PHE   C C   
2093 O O   . PHE   B 128 ? 0.1071 0.1118 0.1410 0.0092  -0.0070 0.0077  134 PHE   C O   
2094 C CB  . PHE   B 128 ? 0.0962 0.1002 0.1165 0.0085  -0.0044 0.0115  134 PHE   C CB  
2095 C CG  . PHE   B 128 ? 0.0987 0.1030 0.1161 0.0084  -0.0034 0.0129  134 PHE   C CG  
2096 C CD1 . PHE   B 128 ? 0.1005 0.1047 0.1136 0.0075  -0.0023 0.0148  134 PHE   C CD1 
2097 C CD2 . PHE   B 128 ? 0.1049 0.1096 0.1243 0.0094  -0.0039 0.0120  134 PHE   C CD2 
2098 C CE1 . PHE   B 128 ? 0.1079 0.1118 0.1174 0.0077  -0.0015 0.0154  134 PHE   C CE1 
2099 C CE2 . PHE   B 128 ? 0.1149 0.1196 0.1314 0.0096  -0.0025 0.0131  134 PHE   C CE2 
2100 C CZ  . PHE   B 128 ? 0.1168 0.1207 0.1277 0.0088  -0.0013 0.0147  134 PHE   C CZ  
2101 N N   . ALA   B 129 ? 0.0990 0.1041 0.1301 0.0073  -0.0038 0.0119  135 ALA   C N   
2102 C CA  . ALA   B 129 ? 0.1022 0.1056 0.1345 0.0080  -0.0044 0.0098  135 ALA   C CA  
2103 C C   . ALA   B 129 ? 0.1043 0.1042 0.1275 0.0096  -0.0048 0.0079  135 ALA   C C   
2104 O O   . ALA   B 129 ? 0.1103 0.1093 0.1286 0.0092  -0.0032 0.0097  135 ALA   C O   
2105 C CB  . ALA   B 129 ? 0.1067 0.1110 0.1424 0.0068  -0.0025 0.0123  135 ALA   C CB  
2106 N N   . ASP   B 130 ? 0.1062 0.1040 0.1272 0.0117  -0.0070 0.0043  136 ASP   C N   
2107 C CA  . ASP   B 130 ? 0.1150 0.1090 0.1263 0.0140  -0.0071 0.0028  136 ASP   C CA  
2108 C C   . ASP   B 130 ? 0.1272 0.1189 0.1359 0.0145  -0.0045 0.0035  136 ASP   C C   
2109 O O   . ASP   B 130 ? 0.1287 0.1207 0.1425 0.0141  -0.0042 0.0029  136 ASP   C O   
2110 C CB  . ASP   B 130 ? 0.1346 0.1268 0.1443 0.0167  -0.0107 -0.0015 136 ASP   C CB  
2111 C CG  . ASP   B 130 ? 0.1491 0.1370 0.1474 0.0200  -0.0111 -0.0028 136 ASP   C CG  
2112 O OD1 . ASP   B 130 ? 0.1595 0.1467 0.1526 0.0200  -0.0095 -0.0005 136 ASP   C OD1 
2113 O OD2 . ASP   B 130 ? 0.1936 0.1784 0.1875 0.0228  -0.0124 -0.0058 136 ASP   C OD2 
2114 N N   . VAL   B 131 ? 0.1272 0.1161 0.1284 0.0157  -0.0024 0.0047  137 VAL   C N   
2115 C CA  . VAL   B 131 ? 0.1250 0.1109 0.1231 0.0169  0.0007  0.0055  137 VAL   C CA  
2116 C C   . VAL   B 131 ? 0.1418 0.1227 0.1293 0.0209  0.0014  0.0040  137 VAL   C C   
2117 O O   . VAL   B 131 ? 0.1537 0.1313 0.1375 0.0226  0.0049  0.0049  137 VAL   C O   
2118 C CB  . VAL   B 131 ? 0.1319 0.1190 0.1332 0.0146  0.0040  0.0093  137 VAL   C CB  
2119 C CG1 . VAL   B 131 ? 0.1345 0.1262 0.1451 0.0115  0.0031  0.0108  137 VAL   C CG1 
2120 C CG2 . VAL   B 131 ? 0.1479 0.1345 0.1456 0.0143  0.0046  0.0110  137 VAL   C CG2 
2121 N N   . ARG   B 132 ? 0.1390 0.1190 0.1214 0.0227  -0.0014 0.0022  138 ARG   C N   
2122 C CA  . ARG   B 132 ? 0.1449 0.1198 0.1159 0.0270  -0.0006 0.0016  138 ARG   C CA  
2123 C C   . ARG   B 132 ? 0.1542 0.1252 0.1190 0.0308  -0.0014 -0.0016 138 ARG   C C   
2124 O O   . ARG   B 132 ? 0.1823 0.1483 0.1365 0.0349  0.0009  -0.0011 138 ARG   C O   
2125 C CB  . ARG   B 132 ? 0.1461 0.1215 0.1142 0.0280  -0.0040 0.0006  138 ARG   C CB  
2126 C CG  . ARG   B 132 ? 0.1449 0.1229 0.1168 0.0249  -0.0026 0.0037  138 ARG   C CG  
2127 C CD  . ARG   B 132 ? 0.1424 0.1207 0.1118 0.0263  -0.0058 0.0025  138 ARG   C CD  
2128 N NE  . ARG   B 132 ? 0.1400 0.1217 0.1163 0.0252  -0.0101 -0.0003 138 ARG   C NE  
2129 C CZ  . ARG   B 132 ? 0.1440 0.1273 0.1222 0.0257  -0.0134 -0.0017 138 ARG   C CZ  
2130 N NH1 . ARG   B 132 ? 0.1509 0.1323 0.1230 0.0277  -0.0133 -0.0007 138 ARG   C NH1 
2131 N NH2 . ARG   B 132 ? 0.1472 0.1339 0.1343 0.0243  -0.0164 -0.0037 138 ARG   C NH2 
2132 N N   . ASP   B 133 ? 0.1524 0.1250 0.1230 0.0301  -0.0042 -0.0048 139 ASP   C N   
2133 C CA  . ASP   B 133 ? 0.1681 0.1365 0.1330 0.0338  -0.0052 -0.0086 139 ASP   C CA  
2134 C C   . ASP   B 133 ? 0.1787 0.1451 0.1439 0.0339  0.0002  -0.0067 139 ASP   C C   
2135 O O   . ASP   B 133 ? 0.2033 0.1653 0.1620 0.0375  0.0006  -0.0095 139 ASP   C O   
2136 C CB  . ASP   B 133 ? 0.1861 0.1569 0.1588 0.0329  -0.0108 -0.0134 139 ASP   C CB  
2137 C CG  . ASP   B 133 ? 0.1877 0.1631 0.1742 0.0283  -0.0095 -0.0117 139 ASP   C CG  
2138 O OD1 . ASP   B 133 ? 0.1837 0.1625 0.1752 0.0250  -0.0069 -0.0073 139 ASP   C OD1 
2139 O OD2 . ASP   B 133 ? 0.2198 0.1952 0.2122 0.0282  -0.0113 -0.0149 139 ASP   C OD2 
2140 N N   . LEU   B 134 ? 0.1650 0.1344 0.1378 0.0301  0.0042  -0.0021 140 LEU   C N   
2141 C CA  . LEU   B 134 ? 0.1720 0.1401 0.1476 0.0298  0.0091  -0.0001 140 LEU   C CA  
2142 C C   . LEU   B 134 ? 0.1718 0.1354 0.1389 0.0328  0.0146  0.0029  140 LEU   C C   
2143 O O   . LEU   B 134 ? 0.1775 0.1425 0.1489 0.0307  0.0182  0.0072  140 LEU   C O   
2144 C CB  . LEU   B 134 ? 0.1721 0.1459 0.1605 0.0247  0.0099  0.0031  140 LEU   C CB  
2145 C CG  . LEU   B 134 ? 0.1654 0.1437 0.1630 0.0219  0.0055  0.0013  140 LEU   C CG  
2146 C CD1 . LEU   B 134 ? 0.1679 0.1513 0.1757 0.0176  0.0066  0.0053  140 LEU   C CD1 
2147 C CD2 . LEU   B 134 ? 0.1878 0.1645 0.1876 0.0234  0.0043  -0.0025 140 LEU   C CD2 
2148 N N   . LEU   B 135 ? 0.1912 0.1489 0.1457 0.0382  0.0151  0.0006  141 LEU   C N   
2149 C CA  . LEU   B 135 ? 0.2033 0.1559 0.1480 0.0420  0.0206  0.0039  141 LEU   C CA  
2150 C C   . LEU   B 135 ? 0.2059 0.1572 0.1551 0.0416  0.0280  0.0079  141 LEU   C C   
2151 O O   . LEU   B 135 ? 0.2213 0.1705 0.1690 0.0426  0.0334  0.0122  141 LEU   C O   
2152 C CB  . LEU   B 135 ? 0.2208 0.1670 0.1496 0.0487  0.0196  0.0005  141 LEU   C CB  
2153 C CG  . LEU   B 135 ? 0.2366 0.1838 0.1612 0.0497  0.0113  -0.0042 141 LEU   C CG  
2154 C CD1 . LEU   B 135 ? 0.2634 0.2038 0.1708 0.0571  0.0096  -0.0075 141 LEU   C CD1 
2155 C CD2 . LEU   B 135 ? 0.2337 0.1848 0.1621 0.0469  0.0095  -0.0017 141 LEU   C CD2 
2156 N N   . TRP   B 136 ? 0.1977 0.1502 0.1539 0.0402  0.0284  0.0066  142 TRP   C N   
2157 C CA  . TRP   B 136 ? 0.2102 0.1620 0.1726 0.0398  0.0352  0.0102  142 TRP   C CA  
2158 C C   . TRP   B 136 ? 0.2118 0.1684 0.1866 0.0349  0.0369  0.0149  142 TRP   C C   
2159 O O   . TRP   B 136 ? 0.2209 0.1766 0.2012 0.0348  0.0428  0.0186  142 TRP   C O   
2160 C CB  . TRP   B 136 ? 0.2125 0.1648 0.1804 0.0393  0.0346  0.0075  142 TRP   C CB  
2161 C CG  . TRP   B 136 ? 0.2028 0.1613 0.1808 0.0347  0.0282  0.0053  142 TRP   C CG  
2162 C CD1 . TRP   B 136 ? 0.2070 0.1660 0.1831 0.0350  0.0221  0.0003  142 TRP   C CD1 
2163 C CD2 . TRP   B 136 ? 0.1932 0.1579 0.1856 0.0294  0.0277  0.0083  142 TRP   C CD2 
2164 N NE1 . TRP   B 136 ? 0.2145 0.1797 0.2033 0.0302  0.0187  0.0005  142 TRP   C NE1 
2165 C CE2 . TRP   B 136 ? 0.2004 0.1689 0.1982 0.0269  0.0220  0.0054  142 TRP   C CE2 
2166 C CE3 . TRP   B 136 ? 0.1940 0.1613 0.1955 0.0268  0.0315  0.0131  142 TRP   C CE3 
2167 C CZ2 . TRP   B 136 ? 0.1942 0.1687 0.2044 0.0224  0.0204  0.0076  142 TRP   C CZ2 
2168 C CZ3 . TRP   B 136 ? 0.1904 0.1637 0.2042 0.0222  0.0290  0.0146  142 TRP   C CZ3 
2169 C CH2 . TRP   B 136 ? 0.1878 0.1645 0.2049 0.0203  0.0237  0.0121  142 TRP   C CH2 
2170 N N   . LEU   B 137 ? 0.1912 0.1530 0.1712 0.0309  0.0318  0.0147  143 LEU   C N   
2171 C CA  . LEU   B 137 ? 0.1936 0.1593 0.1839 0.0268  0.0329  0.0186  143 LEU   C CA  
2172 C C   . LEU   B 137 ? 0.2333 0.1952 0.2204 0.0289  0.0385  0.0222  143 LEU   C C   
2173 O O   . LEU   B 137 ? 0.2549 0.2189 0.2520 0.0261  0.0409  0.0255  143 LEU   C O   
2174 C CB  . LEU   B 137 ? 0.1788 0.1495 0.1723 0.0232  0.0269  0.0175  143 LEU   C CB  
2175 C CG  . LEU   B 137 ? 0.1690 0.1442 0.1690 0.0205  0.0223  0.0154  143 LEU   C CG  
2176 C CD1 . LEU   B 137 ? 0.1883 0.1670 0.1886 0.0183  0.0171  0.0142  143 LEU   C CD1 
2177 C CD2 . LEU   B 137 ? 0.1837 0.1626 0.1959 0.0174  0.0237  0.0181  143 LEU   C CD2 
2178 N N   . ASP   B 138 ? 0.2255 0.1818 0.1991 0.0338  0.0402  0.0215  144 ASP   C N   
2179 C CA  . ASP   B 138 ? 0.2570 0.2092 0.2267 0.0363  0.0459  0.0253  144 ASP   C CA  
2180 C C   . ASP   B 138 ? 0.2888 0.2364 0.2587 0.0395  0.0543  0.0287  144 ASP   C C   
2181 O O   . ASP   B 138 ? 0.3160 0.2598 0.2840 0.0418  0.0602  0.0326  144 ASP   C O   
2182 C CB  . ASP   B 138 ? 0.2658 0.2136 0.2202 0.0409  0.0444  0.0238  144 ASP   C CB  
2183 C CG  . ASP   B 138 ? 0.2596 0.2113 0.2140 0.0383  0.0372  0.0213  144 ASP   C CG  
2184 O OD1 . ASP   B 138 ? 0.2607 0.2179 0.2260 0.0331  0.0343  0.0215  144 ASP   C OD1 
2185 O OD2 . ASP   B 138 ? 0.3177 0.2667 0.2607 0.0419  0.0346  0.0194  144 ASP   C OD2 
2186 N N   . GLU   B 139 ? 0.2888 0.2363 0.2614 0.0398  0.0556  0.0276  145 GLU   C N   
2187 C CA  . GLU   B 139 ? 0.3471 0.2897 0.3195 0.0434  0.0644  0.0307  145 GLU   C CA  
2188 C C   . GLU   B 139 ? 0.3923 0.3383 0.3779 0.0406  0.0655  0.0311  145 GLU   C C   
2189 O O   . GLU   B 139 ? 0.3986 0.3504 0.3922 0.0361  0.0594  0.0288  145 GLU   C O   
2190 C CB  . GLU   B 139 ? 0.4190 0.3543 0.3729 0.0505  0.0662  0.0283  145 GLU   C CB  
2191 C CG  . GLU   B 139 ? 0.5063 0.4434 0.4549 0.0502  0.0580  0.0220  145 GLU   C CG  
2192 C CD  . GLU   B 139 ? 0.6324 0.5630 0.5623 0.0567  0.0565  0.0178  145 GLU   C CD  
2193 O OE1 . GLU   B 139 ? 0.6727 0.6054 0.5994 0.0561  0.0484  0.0125  145 GLU   C OE1 
2194 O OE2 . GLU   B 139 ? 0.6531 0.5767 0.5722 0.0627  0.0634  0.0198  145 GLU   C OE2 
2195 N N   . GLU   B 140 ? 0.4313 0.3733 0.4189 0.0435  0.0739  0.0342  146 GLU   C N   
2196 C CA  . GLU   B 140 ? 0.4613 0.4049 0.4595 0.0423  0.0763  0.0346  146 GLU   C CA  
2197 C C   . GLU   B 140 ? 0.4780 0.4298 0.4938 0.0356  0.0714  0.0352  146 GLU   C C   
2198 O O   . GLU   B 140 ? 0.4839 0.4383 0.5087 0.0340  0.0712  0.0349  146 GLU   C O   
2199 C CB  . GLU   B 140 ? 0.4994 0.4398 0.4864 0.0457  0.0743  0.0296  146 GLU   C CB  
2200 C CG  . GLU   B 140 ? 0.6026 0.5464 0.5998 0.0433  0.0726  0.0278  146 GLU   C CG  
2201 C CD  . GLU   B 140 ? 0.7162 0.6571 0.7198 0.0454  0.0809  0.0306  146 GLU   C CD  
2202 O OE1 . GLU   B 140 ? 0.7609 0.7024 0.7677 0.0452  0.0798  0.0280  146 GLU   C OE1 
2203 O OE2 . GLU   B 140 ? 0.7415 0.6799 0.7483 0.0471  0.0887  0.0355  146 GLU   C OE2 
2204 N N1  . A1B04 C .   ? 0.2822 0.2504 0.3755 0.0080  0.0529  -0.0100 201 A1B04 A N1  
2205 C C4  . A1B04 C .   ? 0.2886 0.2690 0.3749 0.0118  0.0379  0.0026  201 A1B04 A C4  
2206 C C5  . A1B04 C .   ? 0.2783 0.2501 0.3875 0.0126  0.0529  -0.0007 201 A1B04 A C5  
2207 C C6  . A1B04 C .   ? 0.2912 0.2661 0.3332 -0.0022 0.0433  -0.0229 201 A1B04 A C6  
2208 C C7  . A1B04 C .   ? 0.3062 0.2865 0.3395 -0.0005 0.0343  -0.0180 201 A1B04 A C7  
2209 C C8  . A1B04 C .   ? 0.3195 0.3021 0.3467 -0.0008 0.0323  -0.0173 201 A1B04 A C8  
2210 C C10 . A1B04 C .   ? 0.3058 0.2809 0.3433 -0.0047 0.0480  -0.0266 201 A1B04 A C10 
2211 O O   . A1B04 C .   ? 0.3240 0.2900 0.3711 -0.0079 0.0542  -0.0330 201 A1B04 A O   
2212 C C   . A1B04 C .   ? 0.2989 0.2701 0.3458 -0.0032 0.0465  -0.0253 201 A1B04 A C   
2213 C C11 . A1B04 C .   ? 0.3043 0.2764 0.3488 -0.0043 0.0505  -0.0274 201 A1B04 A C11 
2214 C C9  . A1B04 C .   ? 0.3112 0.2915 0.3403 -0.0028 0.0388  -0.0213 201 A1B04 A C9  
2215 N N   . A1B04 C .   ? 0.2764 0.2502 0.3263 0.0003  0.0410  -0.0195 201 A1B04 A N   
2216 C C1  . A1B04 C .   ? 0.2757 0.2464 0.3283 -0.0012 0.0430  -0.0218 201 A1B04 A C1  
2217 C C2  . A1B04 C .   ? 0.2798 0.2534 0.3412 0.0035  0.0390  -0.0138 201 A1B04 A C2  
2218 C C3  . A1B04 C .   ? 0.2832 0.2573 0.3626 0.0080  0.0427  -0.0071 201 A1B04 A C3  
2219 O O1  . A1B04 C .   ? 0.2848 0.2648 0.3903 0.0147  0.0436  0.0077  201 A1B04 A O1  
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