data_7I4M
# 
_entry.id   7I4M 
# 
_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   7I4M         pdb_00007i4m 10.2210/pdb7i4m/pdb 
WWPDB D_1001408309 ?            ?                   
# 
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                        7I4M 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                        15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '1-(3-hydroxyazetidin-1-yl)-2-[2-(methylsulfanyl)phenyl]ethan-1-one' 237.318   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    422 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-(3-hydroxyazetidin-1-yl)-2-[2-(methylsulfanyl)phenyl]ethan-1-one' A1B22 
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 
A1B22 non-polymer         . '1-(3-hydroxyazetidin-1-yl)-2-[2-(methylsulfanyl)phenyl]ethan-1-one' ? 'C12 H15 N O2 S' 237.318 
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        A1B22 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B22 
_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 A1B22 1   201 201 A1B22 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   301 405 HOH   HOH A . 
H 5 HOH   2   302 67  HOH   HOH A . 
H 5 HOH   3   303 77  HOH   HOH A . 
H 5 HOH   4   304 81  HOH   HOH A . 
H 5 HOH   5   305 435 HOH   HOH A . 
H 5 HOH   6   306 353 HOH   HOH A . 
H 5 HOH   7   307 266 HOH   HOH A . 
H 5 HOH   8   308 359 HOH   HOH A . 
H 5 HOH   9   309 383 HOH   HOH A . 
H 5 HOH   10  310 354 HOH   HOH A . 
H 5 HOH   11  311 376 HOH   HOH A . 
H 5 HOH   12  312 142 HOH   HOH A . 
H 5 HOH   13  313 275 HOH   HOH A . 
H 5 HOH   14  314 101 HOH   HOH A . 
H 5 HOH   15  315 111 HOH   HOH A . 
H 5 HOH   16  316 348 HOH   HOH A . 
H 5 HOH   17  317 177 HOH   HOH A . 
H 5 HOH   18  318 169 HOH   HOH A . 
H 5 HOH   19  319 209 HOH   HOH A . 
H 5 HOH   20  320 158 HOH   HOH A . 
H 5 HOH   21  321 102 HOH   HOH A . 
H 5 HOH   22  322 118 HOH   HOH A . 
H 5 HOH   23  323 127 HOH   HOH A . 
H 5 HOH   24  324 386 HOH   HOH A . 
H 5 HOH   25  325 187 HOH   HOH A . 
H 5 HOH   26  326 202 HOH   HOH A . 
H 5 HOH   27  327 224 HOH   HOH A . 
H 5 HOH   28  328 17  HOH   HOH A . 
H 5 HOH   29  329 125 HOH   HOH A . 
H 5 HOH   30  330 54  HOH   HOH A . 
H 5 HOH   31  331 176 HOH   HOH A . 
H 5 HOH   32  332 375 HOH   HOH A . 
H 5 HOH   33  333 403 HOH   HOH A . 
H 5 HOH   34  334 148 HOH   HOH A . 
H 5 HOH   35  335 263 HOH   HOH A . 
H 5 HOH   36  336 112 HOH   HOH A . 
H 5 HOH   37  337 16  HOH   HOH A . 
H 5 HOH   38  338 385 HOH   HOH A . 
H 5 HOH   39  339 404 HOH   HOH A . 
H 5 HOH   40  340 42  HOH   HOH A . 
H 5 HOH   41  341 293 HOH   HOH A . 
H 5 HOH   42  342 61  HOH   HOH A . 
H 5 HOH   43  343 161 HOH   HOH A . 
H 5 HOH   44  344 328 HOH   HOH A . 
H 5 HOH   45  345 221 HOH   HOH A . 
H 5 HOH   46  346 93  HOH   HOH A . 
H 5 HOH   47  347 349 HOH   HOH A . 
H 5 HOH   48  348 103 HOH   HOH A . 
H 5 HOH   49  349 128 HOH   HOH A . 
H 5 HOH   50  350 408 HOH   HOH A . 
H 5 HOH   51  351 71  HOH   HOH A . 
H 5 HOH   52  352 7   HOH   HOH A . 
H 5 HOH   53  353 400 HOH   HOH A . 
H 5 HOH   54  354 36  HOH   HOH A . 
H 5 HOH   55  355 164 HOH   HOH A . 
H 5 HOH   56  356 133 HOH   HOH A . 
H 5 HOH   57  357 32  HOH   HOH A . 
H 5 HOH   58  358 108 HOH   HOH A . 
H 5 HOH   59  359 5   HOH   HOH A . 
H 5 HOH   60  360 91  HOH   HOH A . 
H 5 HOH   61  361 85  HOH   HOH A . 
H 5 HOH   62  362 257 HOH   HOH A . 
H 5 HOH   63  363 281 HOH   HOH A . 
H 5 HOH   64  364 283 HOH   HOH A . 
H 5 HOH   65  365 252 HOH   HOH A . 
H 5 HOH   66  366 130 HOH   HOH A . 
H 5 HOH   67  367 424 HOH   HOH A . 
H 5 HOH   68  368 104 HOH   HOH A . 
H 5 HOH   69  369 8   HOH   HOH A . 
H 5 HOH   70  370 431 HOH   HOH A . 
H 5 HOH   71  371 356 HOH   HOH A . 
H 5 HOH   72  372 303 HOH   HOH A . 
H 5 HOH   73  373 113 HOH   HOH A . 
H 5 HOH   74  374 235 HOH   HOH A . 
H 5 HOH   75  375 371 HOH   HOH A . 
H 5 HOH   76  376 41  HOH   HOH A . 
H 5 HOH   77  377 341 HOH   HOH A . 
H 5 HOH   78  378 56  HOH   HOH A . 
H 5 HOH   79  379 45  HOH   HOH A . 
H 5 HOH   80  380 170 HOH   HOH A . 
H 5 HOH   81  381 140 HOH   HOH A . 
H 5 HOH   82  382 342 HOH   HOH A . 
H 5 HOH   83  383 427 HOH   HOH A . 
H 5 HOH   84  384 20  HOH   HOH A . 
H 5 HOH   85  385 139 HOH   HOH A . 
H 5 HOH   86  386 12  HOH   HOH A . 
H 5 HOH   87  387 62  HOH   HOH A . 
H 5 HOH   88  388 273 HOH   HOH A . 
H 5 HOH   89  389 106 HOH   HOH A . 
H 5 HOH   90  390 203 HOH   HOH A . 
H 5 HOH   91  391 277 HOH   HOH A . 
H 5 HOH   92  392 351 HOH   HOH A . 
H 5 HOH   93  393 415 HOH   HOH A . 
H 5 HOH   94  394 390 HOH   HOH A . 
H 5 HOH   95  395 192 HOH   HOH A . 
H 5 HOH   96  396 39  HOH   HOH A . 
H 5 HOH   97  397 194 HOH   HOH A . 
H 5 HOH   98  398 232 HOH   HOH A . 
H 5 HOH   99  399 301 HOH   HOH A . 
H 5 HOH   100 400 362 HOH   HOH A . 
H 5 HOH   101 401 255 HOH   HOH A . 
H 5 HOH   102 402 188 HOH   HOH A . 
H 5 HOH   103 403 48  HOH   HOH A . 
H 5 HOH   104 404 432 HOH   HOH A . 
H 5 HOH   105 405 157 HOH   HOH A . 
H 5 HOH   106 406 65  HOH   HOH A . 
H 5 HOH   107 407 250 HOH   HOH A . 
H 5 HOH   108 408 254 HOH   HOH A . 
H 5 HOH   109 409 96  HOH   HOH A . 
H 5 HOH   110 410 94  HOH   HOH A . 
H 5 HOH   111 411 183 HOH   HOH A . 
H 5 HOH   112 412 165 HOH   HOH A . 
H 5 HOH   113 413 90  HOH   HOH A . 
H 5 HOH   114 414 227 HOH   HOH A . 
H 5 HOH   115 415 279 HOH   HOH A . 
H 5 HOH   116 416 76  HOH   HOH A . 
H 5 HOH   117 417 213 HOH   HOH A . 
H 5 HOH   118 418 60  HOH   HOH A . 
H 5 HOH   119 419 14  HOH   HOH A . 
H 5 HOH   120 420 144 HOH   HOH A . 
H 5 HOH   121 421 141 HOH   HOH A . 
H 5 HOH   122 422 25  HOH   HOH A . 
H 5 HOH   123 423 381 HOH   HOH A . 
H 5 HOH   124 424 29  HOH   HOH A . 
H 5 HOH   125 425 78  HOH   HOH A . 
H 5 HOH   126 426 47  HOH   HOH A . 
H 5 HOH   127 427 66  HOH   HOH A . 
H 5 HOH   128 428 402 HOH   HOH A . 
H 5 HOH   129 429 217 HOH   HOH A . 
H 5 HOH   130 430 166 HOH   HOH A . 
H 5 HOH   131 431 58  HOH   HOH A . 
H 5 HOH   132 432 38  HOH   HOH A . 
H 5 HOH   133 433 145 HOH   HOH A . 
H 5 HOH   134 434 306 HOH   HOH A . 
H 5 HOH   135 435 197 HOH   HOH A . 
H 5 HOH   136 436 136 HOH   HOH A . 
H 5 HOH   137 437 6   HOH   HOH A . 
H 5 HOH   138 438 22  HOH   HOH A . 
H 5 HOH   139 439 123 HOH   HOH A . 
H 5 HOH   140 440 178 HOH   HOH A . 
H 5 HOH   141 441 272 HOH   HOH A . 
H 5 HOH   142 442 198 HOH   HOH A . 
H 5 HOH   143 443 9   HOH   HOH A . 
H 5 HOH   144 444 30  HOH   HOH A . 
H 5 HOH   145 445 369 HOH   HOH A . 
H 5 HOH   146 446 182 HOH   HOH A . 
H 5 HOH   147 447 350 HOH   HOH A . 
H 5 HOH   148 448 100 HOH   HOH A . 
H 5 HOH   149 449 150 HOH   HOH A . 
H 5 HOH   150 450 428 HOH   HOH A . 
H 5 HOH   151 451 167 HOH   HOH A . 
H 5 HOH   152 452 63  HOH   HOH A . 
H 5 HOH   153 453 330 HOH   HOH A . 
H 5 HOH   154 454 37  HOH   HOH A . 
H 5 HOH   155 455 151 HOH   HOH A . 
H 5 HOH   156 456 75  HOH   HOH A . 
H 5 HOH   157 457 389 HOH   HOH A . 
H 5 HOH   158 458 44  HOH   HOH A . 
H 5 HOH   159 459 347 HOH   HOH A . 
H 5 HOH   160 460 308 HOH   HOH A . 
H 5 HOH   161 461 380 HOH   HOH A . 
H 5 HOH   162 462 325 HOH   HOH A . 
H 5 HOH   163 463 329 HOH   HOH A . 
H 5 HOH   164 464 240 HOH   HOH A . 
H 5 HOH   165 465 367 HOH   HOH A . 
H 5 HOH   166 466 339 HOH   HOH A . 
H 5 HOH   167 467 196 HOH   HOH A . 
H 5 HOH   168 468 97  HOH   HOH A . 
H 5 HOH   169 469 394 HOH   HOH A . 
H 5 HOH   170 470 243 HOH   HOH A . 
H 5 HOH   171 471 280 HOH   HOH A . 
H 5 HOH   172 472 241 HOH   HOH A . 
H 5 HOH   173 473 336 HOH   HOH A . 
H 5 HOH   174 474 234 HOH   HOH A . 
H 5 HOH   175 475 285 HOH   HOH A . 
H 5 HOH   176 476 316 HOH   HOH A . 
H 5 HOH   177 477 422 HOH   HOH A . 
H 5 HOH   178 478 249 HOH   HOH A . 
H 5 HOH   179 479 186 HOH   HOH A . 
H 5 HOH   180 480 74  HOH   HOH A . 
H 5 HOH   181 481 265 HOH   HOH A . 
H 5 HOH   182 482 261 HOH   HOH A . 
H 5 HOH   183 483 331 HOH   HOH A . 
H 5 HOH   184 484 425 HOH   HOH A . 
H 5 HOH   185 485 290 HOH   HOH A . 
H 5 HOH   186 486 314 HOH   HOH A . 
H 5 HOH   187 487 298 HOH   HOH A . 
H 5 HOH   188 488 246 HOH   HOH A . 
H 5 HOH   189 489 421 HOH   HOH A . 
H 5 HOH   190 490 320 HOH   HOH A . 
H 5 HOH   191 491 195 HOH   HOH A . 
H 5 HOH   192 492 229 HOH   HOH A . 
H 5 HOH   193 493 271 HOH   HOH A . 
H 5 HOH   194 494 238 HOH   HOH A . 
H 5 HOH   195 495 206 HOH   HOH A . 
H 5 HOH   196 496 267 HOH   HOH A . 
H 5 HOH   197 497 310 HOH   HOH A . 
H 5 HOH   198 498 414 HOH   HOH A . 
H 5 HOH   199 499 344 HOH   HOH A . 
H 5 HOH   200 500 242 HOH   HOH A . 
H 5 HOH   201 501 114 HOH   HOH A . 
H 5 HOH   202 502 87  HOH   HOH A . 
H 5 HOH   203 503 117 HOH   HOH A . 
H 5 HOH   204 504 401 HOH   HOH A . 
H 5 HOH   205 505 364 HOH   HOH A . 
H 5 HOH   206 506 395 HOH   HOH A . 
H 5 HOH   207 507 326 HOH   HOH A . 
H 5 HOH   208 508 426 HOH   HOH A . 
H 5 HOH   209 509 311 HOH   HOH A . 
H 5 HOH   210 510 185 HOH   HOH A . 
H 5 HOH   211 511 413 HOH   HOH A . 
H 5 HOH   212 512 409 HOH   HOH A . 
H 5 HOH   213 513 264 HOH   HOH A . 
H 5 HOH   214 514 407 HOH   HOH A . 
H 5 HOH   215 515 269 HOH   HOH A . 
I 5 HOH   1   301 377 HOH   HOH C . 
I 5 HOH   2   302 105 HOH   HOH C . 
I 5 HOH   3   303 396 HOH   HOH C . 
I 5 HOH   4   304 358 HOH   HOH C . 
I 5 HOH   5   305 346 HOH   HOH C . 
I 5 HOH   6   306 345 HOH   HOH C . 
I 5 HOH   7   307 89  HOH   HOH C . 
I 5 HOH   8   308 226 HOH   HOH C . 
I 5 HOH   9   309 417 HOH   HOH C . 
I 5 HOH   10  310 199 HOH   HOH C . 
I 5 HOH   11  311 433 HOH   HOH C . 
I 5 HOH   12  312 68  HOH   HOH C . 
I 5 HOH   13  313 361 HOH   HOH C . 
I 5 HOH   14  314 399 HOH   HOH C . 
I 5 HOH   15  315 135 HOH   HOH C . 
I 5 HOH   16  316 200 HOH   HOH C . 
I 5 HOH   17  317 244 HOH   HOH C . 
I 5 HOH   18  318 430 HOH   HOH C . 
I 5 HOH   19  319 3   HOH   HOH C . 
I 5 HOH   20  320 191 HOH   HOH C . 
I 5 HOH   21  321 286 HOH   HOH C . 
I 5 HOH   22  322 149 HOH   HOH C . 
I 5 HOH   23  323 210 HOH   HOH C . 
I 5 HOH   24  324 49  HOH   HOH C . 
I 5 HOH   25  325 19  HOH   HOH C . 
I 5 HOH   26  326 215 HOH   HOH C . 
I 5 HOH   27  327 374 HOH   HOH C . 
I 5 HOH   28  328 337 HOH   HOH C . 
I 5 HOH   29  329 355 HOH   HOH C . 
I 5 HOH   30  330 318 HOH   HOH C . 
I 5 HOH   31  331 126 HOH   HOH C . 
I 5 HOH   32  332 57  HOH   HOH C . 
I 5 HOH   33  333 171 HOH   HOH C . 
I 5 HOH   34  334 83  HOH   HOH C . 
I 5 HOH   35  335 143 HOH   HOH C . 
I 5 HOH   36  336 13  HOH   HOH C . 
I 5 HOH   37  337 296 HOH   HOH C . 
I 5 HOH   38  338 317 HOH   HOH C . 
I 5 HOH   39  339 107 HOH   HOH C . 
I 5 HOH   40  340 1   HOH   HOH C . 
I 5 HOH   41  341 131 HOH   HOH C . 
I 5 HOH   42  342 288 HOH   HOH C . 
I 5 HOH   43  343 223 HOH   HOH C . 
I 5 HOH   44  344 340 HOH   HOH C . 
I 5 HOH   45  345 324 HOH   HOH C . 
I 5 HOH   46  346 26  HOH   HOH C . 
I 5 HOH   47  347 88  HOH   HOH C . 
I 5 HOH   48  348 53  HOH   HOH C . 
I 5 HOH   49  349 366 HOH   HOH C . 
I 5 HOH   50  350 92  HOH   HOH C . 
I 5 HOH   51  351 23  HOH   HOH C . 
I 5 HOH   52  352 222 HOH   HOH C . 
I 5 HOH   53  353 73  HOH   HOH C . 
I 5 HOH   54  354 40  HOH   HOH C . 
I 5 HOH   55  355 378 HOH   HOH C . 
I 5 HOH   56  356 95  HOH   HOH C . 
I 5 HOH   57  357 24  HOH   HOH C . 
I 5 HOH   58  358 59  HOH   HOH C . 
I 5 HOH   59  359 129 HOH   HOH C . 
I 5 HOH   60  360 159 HOH   HOH C . 
I 5 HOH   61  361 50  HOH   HOH C . 
I 5 HOH   62  362 382 HOH   HOH C . 
I 5 HOH   63  363 80  HOH   HOH C . 
I 5 HOH   64  364 220 HOH   HOH C . 
I 5 HOH   65  365 10  HOH   HOH C . 
I 5 HOH   66  366 179 HOH   HOH C . 
I 5 HOH   67  367 204 HOH   HOH C . 
I 5 HOH   68  368 180 HOH   HOH C . 
I 5 HOH   69  369 120 HOH   HOH C . 
I 5 HOH   70  370 72  HOH   HOH C . 
I 5 HOH   71  371 237 HOH   HOH C . 
I 5 HOH   72  372 119 HOH   HOH C . 
I 5 HOH   73  373 363 HOH   HOH C . 
I 5 HOH   74  374 236 HOH   HOH C . 
I 5 HOH   75  375 268 HOH   HOH C . 
I 5 HOH   76  376 334 HOH   HOH C . 
I 5 HOH   77  377 55  HOH   HOH C . 
I 5 HOH   78  378 323 HOH   HOH C . 
I 5 HOH   79  379 51  HOH   HOH C . 
I 5 HOH   80  380 219 HOH   HOH C . 
I 5 HOH   81  381 365 HOH   HOH C . 
I 5 HOH   82  382 15  HOH   HOH C . 
I 5 HOH   83  383 258 HOH   HOH C . 
I 5 HOH   84  384 319 HOH   HOH C . 
I 5 HOH   85  385 302 HOH   HOH C . 
I 5 HOH   86  386 262 HOH   HOH C . 
I 5 HOH   87  387 43  HOH   HOH C . 
I 5 HOH   88  388 34  HOH   HOH C . 
I 5 HOH   89  389 260 HOH   HOH C . 
I 5 HOH   90  390 205 HOH   HOH C . 
I 5 HOH   91  391 86  HOH   HOH C . 
I 5 HOH   92  392 370 HOH   HOH C . 
I 5 HOH   93  393 315 HOH   HOH C . 
I 5 HOH   94  394 21  HOH   HOH C . 
I 5 HOH   95  395 338 HOH   HOH C . 
I 5 HOH   96  396 434 HOH   HOH C . 
I 5 HOH   97  397 218 HOH   HOH C . 
I 5 HOH   98  398 193 HOH   HOH C . 
I 5 HOH   99  399 239 HOH   HOH C . 
I 5 HOH   100 400 2   HOH   HOH C . 
I 5 HOH   101 401 207 HOH   HOH C . 
I 5 HOH   102 402 69  HOH   HOH C . 
I 5 HOH   103 403 18  HOH   HOH C . 
I 5 HOH   104 404 35  HOH   HOH C . 
I 5 HOH   105 405 251 HOH   HOH C . 
I 5 HOH   106 406 327 HOH   HOH C . 
I 5 HOH   107 407 304 HOH   HOH C . 
I 5 HOH   108 408 214 HOH   HOH C . 
I 5 HOH   109 409 291 HOH   HOH C . 
I 5 HOH   110 410 398 HOH   HOH C . 
I 5 HOH   111 411 163 HOH   HOH C . 
I 5 HOH   112 412 357 HOH   HOH C . 
I 5 HOH   113 413 27  HOH   HOH C . 
I 5 HOH   114 414 429 HOH   HOH C . 
I 5 HOH   115 415 116 HOH   HOH C . 
I 5 HOH   116 416 289 HOH   HOH C . 
I 5 HOH   117 417 384 HOH   HOH C . 
I 5 HOH   118 418 160 HOH   HOH C . 
I 5 HOH   119 419 153 HOH   HOH C . 
I 5 HOH   120 420 155 HOH   HOH C . 
I 5 HOH   121 421 79  HOH   HOH C . 
I 5 HOH   122 422 156 HOH   HOH C . 
I 5 HOH   123 423 98  HOH   HOH C . 
I 5 HOH   124 424 391 HOH   HOH C . 
I 5 HOH   125 425 189 HOH   HOH C . 
I 5 HOH   126 426 110 HOH   HOH C . 
I 5 HOH   127 427 134 HOH   HOH C . 
I 5 HOH   128 428 46  HOH   HOH C . 
I 5 HOH   129 429 124 HOH   HOH C . 
I 5 HOH   130 430 216 HOH   HOH C . 
I 5 HOH   131 431 138 HOH   HOH C . 
I 5 HOH   132 432 82  HOH   HOH C . 
I 5 HOH   133 433 299 HOH   HOH C . 
I 5 HOH   134 434 321 HOH   HOH C . 
I 5 HOH   135 435 352 HOH   HOH C . 
I 5 HOH   136 436 28  HOH   HOH C . 
I 5 HOH   137 437 84  HOH   HOH C . 
I 5 HOH   138 438 99  HOH   HOH C . 
I 5 HOH   139 439 11  HOH   HOH C . 
I 5 HOH   140 440 175 HOH   HOH C . 
I 5 HOH   141 441 146 HOH   HOH C . 
I 5 HOH   142 442 418 HOH   HOH C . 
I 5 HOH   143 443 154 HOH   HOH C . 
I 5 HOH   144 444 225 HOH   HOH C . 
I 5 HOH   145 445 208 HOH   HOH C . 
I 5 HOH   146 446 31  HOH   HOH C . 
I 5 HOH   147 447 253 HOH   HOH C . 
I 5 HOH   148 448 4   HOH   HOH C . 
I 5 HOH   149 449 52  HOH   HOH C . 
I 5 HOH   150 450 115 HOH   HOH C . 
I 5 HOH   151 451 368 HOH   HOH C . 
I 5 HOH   152 452 201 HOH   HOH C . 
I 5 HOH   153 453 174 HOH   HOH C . 
I 5 HOH   154 454 173 HOH   HOH C . 
I 5 HOH   155 455 33  HOH   HOH C . 
I 5 HOH   156 456 419 HOH   HOH C . 
I 5 HOH   157 457 64  HOH   HOH C . 
I 5 HOH   158 458 230 HOH   HOH C . 
I 5 HOH   159 459 387 HOH   HOH C . 
I 5 HOH   160 460 109 HOH   HOH C . 
I 5 HOH   161 461 228 HOH   HOH C . 
I 5 HOH   162 462 70  HOH   HOH C . 
I 5 HOH   163 463 292 HOH   HOH C . 
I 5 HOH   164 464 190 HOH   HOH C . 
I 5 HOH   165 465 360 HOH   HOH C . 
I 5 HOH   166 466 332 HOH   HOH C . 
I 5 HOH   167 467 379 HOH   HOH C . 
I 5 HOH   168 468 233 HOH   HOH C . 
I 5 HOH   169 469 132 HOH   HOH C . 
I 5 HOH   170 470 122 HOH   HOH C . 
I 5 HOH   171 471 333 HOH   HOH C . 
I 5 HOH   172 472 256 HOH   HOH C . 
I 5 HOH   173 473 373 HOH   HOH C . 
I 5 HOH   174 474 397 HOH   HOH C . 
I 5 HOH   175 475 410 HOH   HOH C . 
I 5 HOH   176 476 147 HOH   HOH C . 
I 5 HOH   177 477 322 HOH   HOH C . 
I 5 HOH   178 478 420 HOH   HOH C . 
I 5 HOH   179 479 392 HOH   HOH C . 
I 5 HOH   180 480 300 HOH   HOH C . 
I 5 HOH   181 481 411 HOH   HOH C . 
I 5 HOH   182 482 393 HOH   HOH C . 
I 5 HOH   183 483 231 HOH   HOH C . 
I 5 HOH   184 484 287 HOH   HOH C . 
I 5 HOH   185 485 168 HOH   HOH C . 
I 5 HOH   186 486 137 HOH   HOH C . 
I 5 HOH   187 487 248 HOH   HOH C . 
I 5 HOH   188 488 247 HOH   HOH C . 
I 5 HOH   189 489 423 HOH   HOH C . 
I 5 HOH   190 490 152 HOH   HOH C . 
I 5 HOH   191 491 245 HOH   HOH C . 
I 5 HOH   192 492 282 HOH   HOH C . 
I 5 HOH   193 493 212 HOH   HOH C . 
I 5 HOH   194 494 412 HOH   HOH C . 
I 5 HOH   195 495 294 HOH   HOH C . 
I 5 HOH   196 496 305 HOH   HOH C . 
I 5 HOH   197 497 406 HOH   HOH C . 
I 5 HOH   198 498 259 HOH   HOH C . 
I 5 HOH   199 499 181 HOH   HOH C . 
I 5 HOH   200 500 162 HOH   HOH C . 
I 5 HOH   201 501 184 HOH   HOH C . 
I 5 HOH   202 502 343 HOH   HOH C . 
I 5 HOH   203 503 416 HOH   HOH C . 
I 5 HOH   204 504 309 HOH   HOH C . 
I 5 HOH   205 505 278 HOH   HOH C . 
I 5 HOH   206 506 335 HOH   HOH C . 
I 5 HOH   207 507 274 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           7I4M 
_cell.length_a           86.889 
_cell.length_b           57.070 
_cell.length_c           64.893 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.59 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4M 
_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          7I4M 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.25 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-17 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I4M 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.70 
_reflns.d_resolution_high            1.23 
_reflns.number_obs                   80768 
_reflns.percent_possible_obs         88.0 
_reflns.pdbx_Rmerge_I_obs            0.088 
_reflns.pdbx_netI_over_sigmaI        11.6 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.097 
_reflns.pdbx_Rpim_I_all              0.039 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     445376 
_reflns.pdbx_chi_squared             0.84 
_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                  1.23 
_reflns_shell.d_res_low                   1.25 
_reflns_shell.number_measured_all         3254 
_reflns_shell.number_unique_obs           1662 
_reflns_shell.Rmerge_I_obs                1.119 
_reflns_shell.pdbx_chi_squared            0.34 
_reflns_shell.pdbx_redundancy             2.0 
_reflns_shell.percent_possible_obs        36.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.489 
_reflns_shell.pdbx_Rpim_I_all             0.970 
_reflns_shell.pdbx_CC_half                0.336 
_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                                 7I4M 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     80690 
_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                             17.94 
_refine.ls_d_res_high                            1.230 
_refine.ls_percent_reflns_obs                    88.0 
_refine.ls_R_factor_obs                          0.1768 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1763 
_refine.ls_R_factor_R_free                       0.1872 
_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                  4041 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.968 
_refine.B_iso_mean                               17.69 
_refine.aniso_B[1][1]                            -0.96510 
_refine.aniso_B[2][2]                            0.48160 
_refine.aniso_B[3][3]                            0.48350 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.88300 
_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             0.044 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.043 
_refine.pdbx_overall_SU_R_Blow_DPI               0.047 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.046 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4M 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             422 
_refine_hist.number_atoms_total               2614 
_refine_hist.d_res_high                       1.230 
_refine_hist.d_res_low                        17.94 
# 
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                  0.013 ? 2.00  2291 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3125 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  773  '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 2257 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.89  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.14 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  281  '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  2185 '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                       1.23 
_refine_ls_shell.d_res_low                        1.25 
_refine_ls_shell.number_reflns_R_work             1542 
_refine_ls_shell.R_factor_R_work                  0.3335 
_refine_ls_shell.percent_reflns_obs               36.01 
_refine_ls_shell.R_factor_R_free                  0.3279 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.46 
_refine_ls_shell.number_reflns_R_free             72 
_refine_ls_shell.number_reflns_all                1614 
_refine_ls_shell.R_factor_all                     0.3332 
# 
_struct.entry_id                  7I4M 
_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-0036643-001 (A71EV2A-x4715)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4M 
_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 7I4M A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I4M 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 ? ? ? ? ? ? ? 2.362 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
# 
_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_555 110.5 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.7 ? 
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_555 104.5 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.4 ? 
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_555 116.5 ? 
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_555 109.9 ? 
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_555 107.4 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.4 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.8 ? 
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_555 101.0 ? 
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_555 113.5 ? 
# 
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                   7I4M 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 394 ? ? O A HOH 458 ? ? 1.57 
2 1 O A HOH 400 ? ? O C HOH 491 ? ? 1.79 
3 1 O C HOH 417 ? ? O C HOH 439 ? ? 1.82 
4 1 O A HOH 332 ? ? O A HOH 451 ? ? 2.08 
5 1 O C HOH 346 ? ? O C HOH 459 ? ? 2.12 
6 1 O C HOH 301 ? ? O C HOH 422 ? ? 2.13 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     308 
_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    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     414 
_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              2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -134.56 
_pdbx_validate_torsion.psi             -32.45 
# 
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 14.8622 8.1867   14.4911 -0.0214 -0.0076 -0.0041 0.0028 -0.0068 0.0039 0.7700 0.4883 0.3271 0.3228 
-0.3459 -0.0648 -0.0030 0.0395 0.0550 0.0056 0.0244 -0.0123 0.0093 -0.0394 -0.0214 
'X-RAY DIFFRACTION' 2 ? refined 25.9984 -20.1947 17.8073 -0.0209 -0.0106 0.0052  0.0035 -0.0064 0.0097 0.4821 0.6094 0.1842 
-0.0655 -0.0683 -0.1025 0.0116  0.0111 0.0695 0.0171 0.0245 0.0385  0.0163 0.0114  -0.0361 
# 
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 
A1B22 C4   C  Y N 1   
A1B22 C5   C  Y N 2   
A1B22 C6   C  Y N 3   
A1B22 C7   C  N N 4   
A1B22 C8   C  N N 5   
A1B22 C10  C  N N 6   
A1B22 O    O  N N 7   
A1B22 N    N  N N 8   
A1B22 C11  C  N N 9   
A1B22 O1   O  N N 10  
A1B22 C9   C  N N 11  
A1B22 C1   C  Y N 12  
A1B22 S    S  N N 13  
A1B22 C    C  N N 14  
A1B22 C3   C  Y N 15  
A1B22 C2   C  Y N 16  
A1B22 H5   H  N N 17  
A1B22 H6   H  N N 18  
A1B22 H7   H  N N 19  
A1B22 H8   H  N N 20  
A1B22 H11  H  N N 21  
A1B22 H14  H  N N 22  
A1B22 H13  H  N N 23  
A1B22 H12  H  N N 24  
A1B22 H10  H  N N 25  
A1B22 H9   H  N N 26  
A1B22 H1   H  N N 27  
A1B22 H    H  N N 28  
A1B22 H2   H  N N 29  
A1B22 H4   H  N N 30  
A1B22 H3   H  N N 31  
ALA   N    N  N N 32  
ALA   CA   C  N S 33  
ALA   C    C  N N 34  
ALA   O    O  N N 35  
ALA   CB   C  N N 36  
ALA   OXT  O  N N 37  
ALA   H    H  N N 38  
ALA   H2   H  N N 39  
ALA   HA   H  N N 40  
ALA   HB1  H  N N 41  
ALA   HB2  H  N N 42  
ALA   HB3  H  N N 43  
ALA   HXT  H  N N 44  
ARG   N    N  N N 45  
ARG   CA   C  N S 46  
ARG   C    C  N N 47  
ARG   O    O  N N 48  
ARG   CB   C  N N 49  
ARG   CG   C  N N 50  
ARG   CD   C  N N 51  
ARG   NE   N  N N 52  
ARG   CZ   C  N N 53  
ARG   NH1  N  N N 54  
ARG   NH2  N  N N 55  
ARG   OXT  O  N N 56  
ARG   H    H  N N 57  
ARG   H2   H  N N 58  
ARG   HA   H  N N 59  
ARG   HB2  H  N N 60  
ARG   HB3  H  N N 61  
ARG   HG2  H  N N 62  
ARG   HG3  H  N N 63  
ARG   HD2  H  N N 64  
ARG   HD3  H  N N 65  
ARG   HE   H  N N 66  
ARG   HH11 H  N N 67  
ARG   HH12 H  N N 68  
ARG   HH21 H  N N 69  
ARG   HH22 H  N N 70  
ARG   HXT  H  N N 71  
ASN   N    N  N N 72  
ASN   CA   C  N S 73  
ASN   C    C  N N 74  
ASN   O    O  N N 75  
ASN   CB   C  N N 76  
ASN   CG   C  N N 77  
ASN   OD1  O  N N 78  
ASN   ND2  N  N N 79  
ASN   OXT  O  N N 80  
ASN   H    H  N N 81  
ASN   H2   H  N N 82  
ASN   HA   H  N N 83  
ASN   HB2  H  N N 84  
ASN   HB3  H  N N 85  
ASN   HD21 H  N N 86  
ASN   HD22 H  N N 87  
ASN   HXT  H  N N 88  
ASP   N    N  N N 89  
ASP   CA   C  N S 90  
ASP   C    C  N N 91  
ASP   O    O  N N 92  
ASP   CB   C  N N 93  
ASP   CG   C  N N 94  
ASP   OD1  O  N N 95  
ASP   OD2  O  N N 96  
ASP   OXT  O  N N 97  
ASP   H    H  N N 98  
ASP   H2   H  N N 99  
ASP   HA   H  N N 100 
ASP   HB2  H  N N 101 
ASP   HB3  H  N N 102 
ASP   HD2  H  N N 103 
ASP   HXT  H  N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
DMS   S    S  N N 119 
DMS   O    O  N N 120 
DMS   C1   C  N N 121 
DMS   C2   C  N N 122 
DMS   H11  H  N N 123 
DMS   H12  H  N N 124 
DMS   H13  H  N N 125 
DMS   H21  H  N N 126 
DMS   H22  H  N N 127 
DMS   H23  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TRP   N    N  N N 362 
TRP   CA   C  N S 363 
TRP   C    C  N N 364 
TRP   O    O  N N 365 
TRP   CB   C  N N 366 
TRP   CG   C  Y N 367 
TRP   CD1  C  Y N 368 
TRP   CD2  C  Y N 369 
TRP   NE1  N  Y N 370 
TRP   CE2  C  Y N 371 
TRP   CE3  C  Y N 372 
TRP   CZ2  C  Y N 373 
TRP   CZ3  C  Y N 374 
TRP   CH2  C  Y N 375 
TRP   OXT  O  N N 376 
TRP   H    H  N N 377 
TRP   H2   H  N N 378 
TRP   HA   H  N N 379 
TRP   HB2  H  N N 380 
TRP   HB3  H  N N 381 
TRP   HD1  H  N N 382 
TRP   HE1  H  N N 383 
TRP   HE3  H  N N 384 
TRP   HZ2  H  N N 385 
TRP   HZ3  H  N N 386 
TRP   HH2  H  N N 387 
TRP   HXT  H  N N 388 
TYR   N    N  N N 389 
TYR   CA   C  N S 390 
TYR   C    C  N N 391 
TYR   O    O  N N 392 
TYR   CB   C  N N 393 
TYR   CG   C  Y N 394 
TYR   CD1  C  Y N 395 
TYR   CD2  C  Y N 396 
TYR   CE1  C  Y N 397 
TYR   CE2  C  Y N 398 
TYR   CZ   C  Y N 399 
TYR   OH   O  N N 400 
TYR   OXT  O  N N 401 
TYR   H    H  N N 402 
TYR   H2   H  N N 403 
TYR   HA   H  N N 404 
TYR   HB2  H  N N 405 
TYR   HB3  H  N N 406 
TYR   HD1  H  N N 407 
TYR   HD2  H  N N 408 
TYR   HE1  H  N N 409 
TYR   HE2  H  N N 410 
TYR   HH   H  N N 411 
TYR   HXT  H  N N 412 
VAL   N    N  N N 413 
VAL   CA   C  N S 414 
VAL   C    C  N N 415 
VAL   O    O  N N 416 
VAL   CB   C  N N 417 
VAL   CG1  C  N N 418 
VAL   CG2  C  N N 419 
VAL   OXT  O  N N 420 
VAL   H    H  N N 421 
VAL   H2   H  N N 422 
VAL   HA   H  N N 423 
VAL   HB   H  N N 424 
VAL   HG11 H  N N 425 
VAL   HG12 H  N N 426 
VAL   HG13 H  N N 427 
VAL   HG21 H  N N 428 
VAL   HG22 H  N N 429 
VAL   HG23 H  N N 430 
VAL   HXT  H  N N 431 
ZN    ZN   ZN N N 432 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1B22 C   S    sing N N 1   
A1B22 S   C1   sing N N 2   
A1B22 C1  C2   doub Y N 3   
A1B22 C2  C3   sing Y N 4   
A1B22 C3  C4   doub Y N 5   
A1B22 C4  C5   sing Y N 6   
A1B22 C5  C6   doub Y N 7   
A1B22 C1  C6   sing Y N 8   
A1B22 C6  C7   sing N N 9   
A1B22 C7  C8   sing N N 10  
A1B22 C8  O    doub N N 11  
A1B22 N   C8   sing N N 12  
A1B22 N   C9   sing N N 13  
A1B22 C9  C10  sing N N 14  
A1B22 O1  C10  sing N N 15  
A1B22 C10 C11  sing N N 16  
A1B22 C11 N    sing N N 17  
A1B22 C4  H5   sing N N 18  
A1B22 C5  H6   sing N N 19  
A1B22 C7  H7   sing N N 20  
A1B22 C7  H8   sing N N 21  
A1B22 C10 H11  sing N N 22  
A1B22 C11 H14  sing N N 23  
A1B22 C11 H13  sing N N 24  
A1B22 O1  H12  sing N N 25  
A1B22 C9  H10  sing N N 26  
A1B22 C9  H9   sing N N 27  
A1B22 C   H1   sing N N 28  
A1B22 C   H    sing N N 29  
A1B22 C   H2   sing N N 30  
A1B22 C3  H4   sing N N 31  
A1B22 C2  H3   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
DMS   S   O    doub N N 115 
DMS   S   C1   sing N N 116 
DMS   S   C2   sing N N 117 
DMS   C1  H11  sing N N 118 
DMS   C1  H12  sing N N 119 
DMS   C1  H13  sing N N 120 
DMS   C2  H21  sing N N 121 
DMS   C2  H22  sing N N 122 
DMS   C2  H23  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
_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                    7I4M 
_atom_sites.fract_transf_matrix[1][1]   0.011509 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000924 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017522 
_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]   0.015460 
_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   ? 17.616 8.167   24.834 1.00 13.13 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.882 8.227   24.071 1.00 14.11 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.008 7.043   23.148 1.00 14.21 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.302 6.036   23.302 1.00 15.36 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.066 8.307   25.046 1.00 17.23 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.146 7.083   25.751 1.00 20.43 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.932 7.136   22.187 1.00 12.65 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.199 6.014   21.291 1.00 12.35 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.654 6.447   19.910 1.00 12.20 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.355 7.571   19.503 1.00 13.48 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.345 5.577   19.198 1.00 11.21 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.857 5.920   17.875 1.00 11.55 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.858 4.697   16.976 1.00 11.40 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.745 3.556   17.449 1.00 12.38 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.289 6.462   18.008 1.00 12.59 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.944 4.934   15.650 1.00 10.65 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.161 3.874   14.631 1.00 10.16 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.623 3.957   14.218 1.00 11.42 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.126 5.071   13.974 1.00 11.25 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.289 4.080   13.376 1.00 10.47 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.790 4.232   13.743 1.00 11.91 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.462 2.874   12.420 1.00 11.70 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.993 4.768   12.511 1.00 13.63 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.319 2.825   14.213 1.00 10.99 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.735 2.816   13.814 1.00 12.04 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.833 1.979   12.543 1.00 12.05 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.842 0.744   12.625 1.00 12.19 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.613 2.227   14.956 1.00 12.69 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.666 3.126   16.171 1.00 11.93 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.529 4.215   16.218 1.00 13.38 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.824 2.915   17.252 1.00 13.29 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.531 5.084   17.301 1.00 13.68 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.833 3.775   18.353 1.00 14.41 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.665 4.868   18.351 1.00 14.53 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.676 5.738   19.434 1.00 16.91 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.924 2.621   11.378 1.00 11.89 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.992 1.992   10.063 1.00 12.12 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.208 2.489   9.345  1.00 13.68 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.458 3.705   9.308  1.00 12.55 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.681 2.245   9.241  1.00 13.53 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.344 3.742   9.146  1.00 14.44 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.816 1.621   7.842  1.00 15.00 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.047 1.581   8.881  1.00 13.82 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.298 1.980   8.228  1.00 13.71 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.141 2.868   9.131  1.00 13.32 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.244 2.590   10.329 1.00 13.30 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.606 4.026   8.607  1.00 13.10 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.307 5.007   9.442  1.00 12.86 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.412 6.214   9.772  1.00 12.69 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.901 7.361   9.886  1.00 12.75 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.658 5.442   8.866  1.00 13.43 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.725 4.370   8.989  1.00 18.13 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.484 4.306   9.982  1.00 20.47 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.764 3.508   8.010  1.00 18.96 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.131 5.935   9.997  1.00 11.46 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.144 6.963   10.384 1.00 11.19 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.472 6.645   11.720 1.00 10.90 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.226 5.453   12.037 1.00 11.32 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.039 7.042   9.292  1.00 10.73 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.566 7.413   7.932  1.00 12.30 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.179 8.635   7.717  1.00 13.45 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.367 6.584   6.844  1.00 14.98 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.626 9.006   6.447  1.00 14.12 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.791 6.952   5.571  1.00 16.14 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.389 8.174   5.375  1.00 16.29 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.859 8.526   4.121  1.00 19.29 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.150 7.694   12.456 1.00 10.19 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.353 7.624   13.685 1.00 10.18 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.106 8.502   13.435 1.00 10.66 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.251 9.710   13.133 1.00 10.62 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.176 8.205   14.884 1.00 11.28 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.355 8.497   16.159 1.00 11.75 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.295 8.909   17.329 1.00 12.99 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.742 9.988   18.162 1.00 13.45 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.083 9.795   19.303 1.00 15.36 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.797 8.559   19.716 1.00 15.70 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.644 10.836  20.004 1.00 14.81 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.904 7.904   13.498 1.00 10.17 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.629 8.624   13.266 1.00 10.11 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.962 8.825   14.610 1.00 11.29 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.684 7.850   15.328 1.00 11.30 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.699 7.815   12.363 1.00 10.55 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.472 8.662   11.979 1.00 12.42 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.424 7.330   11.111 1.00 11.72 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.712 10.085  14.973 1.00 10.09 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.076 10.406  16.270 0.50 9.75  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.108 10.394  16.279 0.50 10.99 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.971 11.408  16.075 1.00 10.35 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.852 12.056  15.015 1.00 11.97 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.106 11.020  17.281 0.50 9.91  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.254 11.013  17.168 0.50 13.54 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.025 9.949   17.853 0.50 11.52 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.818 11.284  18.589 0.50 13.00 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.858 12.237  16.686 0.50 7.32  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.470 10.117  17.209 0.50 16.16 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.126 11.586  17.118 1.00 9.80  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.130 12.672  17.058 1.00 10.15 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.926 13.987  17.073 1.00 10.52 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.888 14.149  17.871 1.00 11.24 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.280 12.679  18.335 1.00 10.11 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.392 11.451  18.433 1.00 10.99 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.808 10.430  19.012 1.00 12.53 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.202 11.488  17.794 1.00 11.34 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.576 14.926  16.167 1.00 10.54 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.329 16.209  16.129 1.00 11.05 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.306 16.902  17.497 1.00 12.08 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.321 17.447  17.933 1.00 12.62 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.706 17.114  15.082 1.00 11.18 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.514 18.438  14.891 1.00 11.57 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.774 19.294  13.870 1.00 12.59 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.488 20.501  13.425 1.00 14.37 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.498 21.661  14.083 1.00 16.70 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.924 21.759  15.286 1.00 14.99 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.064 22.747  13.532 1.00 17.65 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.160 16.780  18.227 1.00 10.43 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.054 17.481  19.521 1.00 12.04 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.921 16.861  20.632 1.00 13.14 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.056 17.467  21.712 1.00 14.20 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.574 17.616  19.954 1.00 12.83 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.926 16.356  20.445 1.00 11.57 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.265 15.501  19.579 1.00 12.55 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.764 15.898  21.713 1.00 12.17 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.736 14.531  20.339 1.00 12.94 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.005 14.729  21.630 1.00 12.53 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.466 15.644  20.408 1.00 12.38 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.345 14.997  21.382 1.00 11.84 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.811 14.928  20.903 1.00 12.88 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.649 14.301  21.551 1.00 13.85 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.841 13.587  21.675 1.00 12.33 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.440 13.555  22.290 1.00 13.04 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.984 12.113  22.516 1.00 14.15 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.384 14.347  23.633 1.00 14.83 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.128 15.594  19.777 1.00 12.68 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.503 15.561  19.277 1.00 13.33 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.483 16.200  20.272 1.00 14.68 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.189 17.227  20.881 1.00 14.65 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.585 16.249  17.921 1.00 12.76 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.674 15.608  20.361 1.00 13.89 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.735 16.106  21.259 1.00 13.96 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.667 17.104  20.544 1.00 14.82 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.607 17.243  19.313 1.00 13.12 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.583 14.915  21.750 1.00 15.03 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.295 14.368  20.623 1.00 14.85 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.751 13.827  22.435 1.00 16.83 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.599 17.761  21.281 1.00 14.32 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.575 18.610  20.667 1.00 14.46 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.417 17.781  19.685 1.00 13.95 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.693 18.265  18.583 1.00 14.37 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.495 19.277  21.727 1.00 16.46 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.767 19.860  21.141 1.00 24.87 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.766 21.061  20.453 1.00 29.48 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.007 19.306  21.037 1.00 28.24 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 33.021 21.283  20.088 1.00 30.30 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.802 20.224  20.358 1.00 30.78 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.778 16.515  20.043 1.00 13.42 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.567 15.723  19.118 1.00 13.75 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.811 15.445  17.812 1.00 12.51 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.409 15.464  16.740 1.00 13.17 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.029 14.401  19.728 1.00 14.66 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.993 13.691  18.821 1.00 22.63 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.148 14.145  18.657 1.00 24.75 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.543 12.612  18.172 1.00 23.98 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.491 15.244  17.896 1.00 11.97 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.673 15.062  16.706 1.00 12.11 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.726 16.310  15.808 1.00 10.97 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.956 16.194  14.599 1.00 11.79 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.204 14.787  17.065 1.00 10.94 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.933 13.422  17.651 1.00 13.40 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.565 12.441  17.201 1.00 12.81 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.093 13.330  18.583 1.00 12.87 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.559 17.499  16.386 1.00 10.96 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.590 18.738  15.601 1.00 12.12 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.993 19.000  15.031 1.00 12.35 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.091 19.561  13.942 1.00 13.67 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.145 19.946  16.457 1.00 12.88 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.641 19.994  16.619 1.00 12.37 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.925 19.710  17.741 1.00 13.95 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.684 20.437  15.637 1.00 12.63 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.584 19.938  17.518 1.00 13.38 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.409 20.374  16.225 1.00 13.22 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.804 20.882  14.319 1.00 13.63 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.244 20.744  15.519 1.00 13.73 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.674 21.203  13.616 1.00 14.03 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.422 21.179  14.215 1.00 14.58 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.057 18.596  15.759 1.00 11.69 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.412 18.810  15.272 1.00 12.51 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.838 17.795  14.193 1.00 13.91 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.893 17.944  13.578 1.00 14.47 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.381 18.760  16.461 1.00 13.47 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.035 16.731  13.978 1.00 12.84 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.273 15.686  12.980 1.00 13.28 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.010 15.505  12.131 1.00 12.50 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.646 14.385  11.757 1.00 12.64 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.659 14.374  13.680 1.00 13.42 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.036 14.534  14.304 1.00 14.90 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.061 14.470  13.605 1.00 17.35 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.082 14.832  15.611 1.00 16.72 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.393 16.585  11.776 1.00 11.90 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.078 16.576  11.114 1.00 11.74 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.118 16.130  9.687  1.00 13.39 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.974 16.572  8.899  1.00 15.03 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.470 18.004  11.175 1.00 11.85 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.076 18.127  10.601 1.00 11.80 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.062 17.409  11.483 1.00 13.05 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.666 19.605  10.553 1.00 15.76 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.185 15.233  9.307  1.00 12.47 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.038 14.837  7.914  1.00 12.59 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.771 15.526  7.329  1.00 12.55 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.814 16.083  6.225  1.00 14.11 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.899 13.291  7.827  1.00 12.16 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.526 12.854  6.405  1.00 14.12 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.209 12.620  8.284  1.00 14.15 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.637 15.473  8.065  1.00 11.59 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.372 16.027  7.551  1.00 12.36 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.389 16.226  8.701  1.00 12.42 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.450 15.456  9.667  1.00 12.37 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.760 15.020  6.525  1.00 12.78 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.335 15.289  6.086  1.00 14.14 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.918 16.190  5.145  1.00 17.08 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.144 14.676  6.612  1.00 14.16 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.546 16.128  5.010  1.00 17.42 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.044 15.222  5.920  1.00 15.82 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.908 13.731  7.601  1.00 14.21 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.726 14.787  6.142  1.00 17.43 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.619 13.282  7.793  1.00 15.29 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.542 13.835  7.099  1.00 16.31 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.577 17.304  8.665  1.00 12.51 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.568 17.479  9.697  1.00 12.45 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.339 18.122  9.084  1.00 13.79 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.448 18.901  8.124  1.00 14.06 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.103 18.316  10.858 1.00 13.75 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.691 19.681  10.507 1.00 14.52 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.730 20.843  10.327 1.00 16.34 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.078 21.822  9.623  1.00 17.88 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.623 20.800  10.919 1.00 16.22 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.169 17.826  9.658  1.00 13.15 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.924 18.406  9.155  1.00 13.11 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.980 18.568  10.319 1.00 13.33 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.458 17.577  10.859 1.00 13.10 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.328 17.503  8.047  1.00 15.36 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.073 18.036  7.392  1.00 19.98 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.228 18.599  8.106  1.00 20.52 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.895 17.808  6.187  1.00 22.53 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.758 19.833  10.750 1.00 13.07 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.880 20.149  11.876 0.50 13.03 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.897 20.081  11.896 0.50 14.55 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.443 19.681  11.635 1.00 14.06 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.797 19.171  12.562 1.00 13.46 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.910 21.657  12.139 0.50 12.61 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.014 21.536  12.339 0.50 18.82 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.094 22.029  13.237 0.50 10.83 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.676 22.387  11.261 0.50 25.66 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.927 19.844  10.406 1.00 13.89 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.545 19.426  10.107 1.00 13.75 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.346 17.920  10.244 1.00 13.72 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.225 17.499  10.440 1.00 13.92 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.131 19.877  8.706  1.00 16.40 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.657 19.056  7.686  1.00 22.73 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.412 17.127  10.202 1.00 12.74 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.307 15.660  10.376 1.00 12.00 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.769 15.206  11.777 1.00 11.66 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.680 14.015  12.089 1.00 11.34 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.187 14.933  9.316  1.00 13.41 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.644 15.107  7.908  1.00 13.68 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.514 14.451  6.835  1.00 12.99 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.466 12.991  6.962  1.00 12.67 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.610 12.146  5.946  1.00 12.93 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.909 12.603  4.728  1.00 15.39 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.503 10.827  6.145  1.00 13.21 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.366 16.113  12.593 1.00 10.99 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.951 15.768  13.875 1.00 10.55 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.095 14.784  13.725 1.00 10.89 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.306 13.935  14.602 1.00 10.86 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.924 15.293  14.918 1.00 12.04 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.517 15.063  16.310 1.00 11.81 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.382 15.884  16.768 1.00 12.47 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.136 14.054  16.974 1.00 12.09 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.876 14.906  12.618 1.00 10.57 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.987 13.961  12.414 1.00 10.60 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.333 14.659  12.272 1.00 11.04 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.419 15.770  11.699 1.00 10.99 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.788 13.113  11.147 1.00 10.96 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.698 12.005  11.180 1.00 12.61 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.643 11.283  9.830  1.00 13.07 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.952 10.990  12.322 1.00 12.93 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.370 14.007  12.764 1.00 10.61 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.760 14.454  12.542 1.00 10.71 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.606 13.223  12.402 1.00 10.73 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.428 12.204  13.109 1.00 10.82 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.227 15.317  13.739 1.00 11.26 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.660 15.875  13.639 1.00 11.29 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.784 17.231  14.349 1.00 12.90 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.691 14.942  14.278 1.00 11.81 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.563 13.301  11.442 1.00 10.57 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.505 12.210  11.201 1.00 10.24 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.932 12.722  11.354 1.00 10.18 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.263 13.775  10.770 1.00 10.87 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.296 11.641  9.774  1.00 9.89  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.294 10.503  9.505  1.00 11.52 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.840 11.109  9.631  1.00 11.43 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.754 12.019  12.135 1.00 10.35 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.171 12.365  12.306 1.00 11.26 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.044 11.206  11.854 1.00 11.52 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.569 10.066  11.628 1.00 11.19 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.459 12.743  13.759 1.00 12.97 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.160 11.678  14.644 1.00 12.76 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.347 11.481  11.646 1.00 12.25 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.269 10.432  11.214 1.00 13.08 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.922 9.737   12.414 1.00 14.95 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.130 10.356  13.471 1.00 16.85 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.352 11.005  10.297 1.00 15.79 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.021 12.018  11.034 1.00 18.34 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.249 8.442   12.249 1.00 14.74 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.845 7.626   13.303 1.00 16.53 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.180 7.039   12.855 1.00 17.54 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.415 6.788   11.666 1.00 16.69 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.921 6.424   13.647 1.00 18.01 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.816 5.510   12.546 1.00 19.06 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.523 6.871   14.109 1.00 17.86 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 35.041 6.769   13.836 1.00 18.96 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.321 6.137   13.554 1.00 20.34 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.107 4.612   13.333 1.00 20.24 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.637 4.056   12.371 1.00 21.78 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.315 6.455   14.683 1.00 25.45 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.824 5.913   15.894 1.00 30.53 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.516 7.934   14.872 1.00 25.93 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.284 3.983   14.168 1.00 19.89 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 35.032 2.543   14.041 1.00 21.03 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.804 2.251   13.158 1.00 20.40 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.859 3.044   13.146 1.00 20.14 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.786 1.956   15.422 1.00 23.50 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.786 1.081   12.504 1.00 18.56 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.655 0.679   11.666 1.00 18.59 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.567 0.078   12.526 1.00 18.69 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.849 -0.713  13.430 1.00 20.33 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.087 -0.364  10.629 1.00 20.44 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.962 0.216   9.507  1.00 26.33 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.338 -0.829  8.493  1.00 31.71 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.174 -1.699  8.754  1.00 32.23 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.742 -0.753  7.309  1.00 33.57 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.328 0.419   12.208 1.00 15.02 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.176 -0.073  12.942 1.00 14.84 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.575 -1.323  12.336 1.00 14.31 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.906 -1.686  11.204 1.00 15.41 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.631 -1.942  13.080 1.00 13.17 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 27.034 -3.240  12.693 1.00 13.69 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.590 -3.178  12.282 1.00 14.45 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.046 -4.200  11.883 1.00 14.60 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.215 -4.256  13.817 1.00 15.01 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.934 -4.682  14.166 1.00 18.11 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.937 -2.027  12.429 1.00 12.34 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.538 -1.912  12.023 1.00 12.21 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.454 -1.853  10.479 1.00 13.36 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.335 -1.303  9.828  1.00 15.58 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.930 -0.634  12.609 1.00 11.98 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.782 -0.700  14.126 1.00 13.37 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.444 -1.817  14.643 1.00 13.62 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.976 0.345   14.806 1.00 13.57 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.380 -2.409  9.914  1.00 14.53 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.116 -2.289  8.455  1.00 15.76 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.765 -1.596  8.271  1.00 14.34 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.853 -1.776  9.108  1.00 15.03 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 22.096 -3.629  7.779  1.00 19.99 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 21.109 -4.402  8.429  1.00 24.29 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.467 -4.323  7.898  1.00 22.05 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.644 -0.747  7.256  1.00 13.73 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.408 -0.000  7.032  1.00 13.37 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.460 -0.772  6.132  1.00 13.62 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.863 -1.286  5.066  1.00 14.59 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.736 1.385   6.400  1.00 13.24 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.834 2.146   7.171  1.00 14.10 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.470 2.261   6.259  1.00 13.47 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.464 2.417   8.664  1.00 15.37 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.193 -0.800  6.502  1.00 12.05 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.131 -1.415  5.703  1.00 11.98 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.885 -0.565  4.447  1.00 13.21 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.875 0.684   4.491  1.00 12.49 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.847 -1.448  6.530  1.00 11.48 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.646 -1.244  3.296  1.00 14.48 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.321 -0.555  2.038  1.00 15.23 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.029 -1.230  1.550  1.00 17.88 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.073 -2.209  0.804  1.00 18.71 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.483 -0.644  1.016  1.00 15.19 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.810 -0.089  1.564  1.00 14.74 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.821 1.441   1.817  1.00 14.54 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.150 1.877   2.326  1.00 14.70 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.361 3.031   2.960  1.00 16.48 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.367 3.885   3.149  1.00 17.16 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.573 3.332   3.429  1.00 17.34 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.897 -0.689  1.990  1.00 17.23 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.574 -1.337  1.872  1.00 17.42 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.434 -0.363  2.187  1.00 17.80 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.650 0.772   2.581  1.00 20.01 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.559 -2.486  2.877  1.00 17.09 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.478 -1.913  4.603  1.00 15.86 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.149  -0.876  2.100  1.00 19.64 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.995  -0.084  2.492  1.00 21.80 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.207  -0.823  3.594  1.00 20.78 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.987  -0.664  3.694  1.00 21.98 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.075  0.266   1.304  1.00 28.25 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.426  -0.927  0.645  1.00 37.47 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.815  -2.080  0.972  1.00 38.25 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.528  -0.715  -0.218 1.00 42.84 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.902  -1.550  4.473  1.00 17.63 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.237  -2.195  5.636  1.00 16.62 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.508  -1.180  6.464  1.00 17.26 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.939  -0.023  6.626  1.00 17.38 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.256  -2.913  6.522  1.00 17.64 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.926  -4.475  5.862  1.00 18.02 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.381  -1.626  7.007  1.00 15.27 ? 59  GLN   A N   1 
ATOM   411  C  CA  A GLN   A 1 53  ? 4.547  -0.839  7.927  0.50 14.35 ? 59  GLN   A CA  1 
ATOM   412  C  CA  B GLN   A 1 53  ? 4.632  -0.803  7.930  0.50 15.22 ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.329  -1.590  9.242  1.00 13.79 ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.456  -1.225  10.028 1.00 14.09 ? 59  GLN   A O   1 
ATOM   415  C  CB  A GLN   A 1 53  ? 3.194  -0.417  7.302  0.50 14.95 ? 59  GLN   A CB  1 
ATOM   416  C  CB  B GLN   A 1 53  ? 3.420  -0.177  7.223  0.50 18.47 ? 59  GLN   A CB  1 
ATOM   417  C  CG  A GLN   A 1 53  ? 3.259  0.885   6.472  0.50 14.94 ? 59  GLN   A CG  1 
ATOM   418  C  CG  B GLN   A 1 53  ? 3.851  0.677   5.978  0.50 22.74 ? 59  GLN   A CG  1 
ATOM   419  C  CD  A GLN   A 1 53  ? 1.898  1.359   6.036  0.50 17.29 ? 59  GLN   A CD  1 
ATOM   420  C  CD  B GLN   A 1 53  ? 4.884  1.774   6.277  0.50 26.67 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 A GLN   A 1 53  ? 1.444  1.112   4.903  0.50 18.77 ? 59  GLN   A OE1 1 
ATOM   422  O  OE1 B GLN   A 1 53  ? 5.877  2.050   5.537  0.50 27.45 ? 59  GLN   A OE1 1 
ATOM   423  N  NE2 A GLN   A 1 53  ? 1.209  2.066   6.917  0.50 12.91 ? 59  GLN   A NE2 1 
ATOM   424  N  NE2 B GLN   A 1 53  ? 4.708  2.423   7.393  0.50 26.64 ? 59  GLN   A NE2 1 
ATOM   425  N  N   . THR   A 1 54  ? 5.096  -2.693  9.466  1.00 12.09 ? 60  THR   A N   1 
ATOM   426  C  CA  . THR   A 1 54  ? 5.074  -3.446  10.720 1.00 12.78 ? 60  THR   A CA  1 
ATOM   427  C  C   . THR   A 1 54  ? 6.543  -3.658  11.123 1.00 11.82 ? 60  THR   A C   1 
ATOM   428  O  O   . THR   A 1 54  ? 7.413  -3.841  10.254 1.00 13.32 ? 60  THR   A O   1 
ATOM   429  C  CB  . THR   A 1 54  ? 4.298  -4.750  10.695 1.00 16.51 ? 60  THR   A CB  1 
ATOM   430  O  OG1 . THR   A 1 54  ? 4.929  -5.633  9.815  1.00 22.27 ? 60  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A 1 54  ? 2.878  -4.570  10.251 1.00 15.91 ? 60  THR   A CG2 1 
ATOM   432  N  N   . GLY   A 1 55  ? 6.806  -3.585  12.404 1.00 10.96 ? 61  GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 55  ? 8.176  -3.754  12.909 1.00 11.37 ? 61  GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 55  ? 8.184  -3.828  14.418 1.00 10.16 ? 61  GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 55  ? 7.153  -4.092  15.046 1.00 10.95 ? 61  GLY   A O   1 
ATOM   436  N  N   . VAL   A 1 56  ? 9.350  -3.601  15.031 1.00 10.15 ? 62  VAL   A N   1 
ATOM   437  C  CA  . VAL   A 1 56  ? 9.548  -3.689  16.476 1.00 9.07  ? 62  VAL   A CA  1 
ATOM   438  C  C   . VAL   A 1 56  ? 10.382 -2.517  16.894 1.00 9.45  ? 62  VAL   A C   1 
ATOM   439  O  O   . VAL   A 1 56  ? 11.368 -2.215  16.211 1.00 10.72 ? 62  VAL   A O   1 
ATOM   440  C  CB  . VAL   A 1 56  ? 10.275 -5.030  16.822 1.00 10.64 ? 62  VAL   A CB  1 
ATOM   441  C  CG1 . VAL   A 1 56  ? 10.673 -5.088  18.297 1.00 13.00 ? 62  VAL   A CG1 1 
ATOM   442  C  CG2 . VAL   A 1 56  ? 9.379  -6.231  16.460 1.00 11.69 ? 62  VAL   A CG2 1 
ATOM   443  N  N   . TYR   A 1 57  ? 10.005 -1.849  18.003 1.00 9.28  ? 63  TYR   A N   1 
ATOM   444  C  CA  . TYR   A 1 57  ? 10.847 -0.735  18.481 1.00 9.14  ? 63  TYR   A CA  1 
ATOM   445  C  C   . TYR   A 1 57  ? 11.295 -0.970  19.907 1.00 9.77  ? 63  TYR   A C   1 
ATOM   446  O  O   . TYR   A 1 57  ? 10.596 -1.609  20.699 1.00 10.66 ? 63  TYR   A O   1 
ATOM   447  C  CB  . TYR   A 1 57  ? 10.143 0.662   18.355 1.00 9.51  ? 63  TYR   A CB  1 
ATOM   448  C  CG  . TYR   A 1 57  ? 9.134  1.002   19.421 1.00 8.90  ? 63  TYR   A CG  1 
ATOM   449  C  CD1 . TYR   A 1 57  ? 7.858  0.451   19.400 1.00 10.74 ? 63  TYR   A CD1 1 
ATOM   450  C  CD2 . TYR   A 1 57  ? 9.434  1.923   20.427 1.00 9.16  ? 63  TYR   A CD2 1 
ATOM   451  C  CE1 . TYR   A 1 57  ? 6.918  0.758   20.386 1.00 10.84 ? 63  TYR   A CE1 1 
ATOM   452  C  CE2 . TYR   A 1 57  ? 8.502  2.230   21.418 1.00 9.56  ? 63  TYR   A CE2 1 
ATOM   453  C  CZ  . TYR   A 1 57  ? 7.242  1.658   21.374 1.00 10.31 ? 63  TYR   A CZ  1 
ATOM   454  O  OH  . TYR   A 1 57  ? 6.269  1.899   22.348 1.00 11.71 ? 63  TYR   A OH  1 
ATOM   455  N  N   . TYR   A 1 58  ? 12.413 -0.327  20.285 1.00 9.51  ? 64  TYR   A N   1 
ATOM   456  C  CA  . TYR   A 1 58  ? 12.874 -0.390  21.678 1.00 9.38  ? 64  TYR   A CA  1 
ATOM   457  C  C   . TYR   A 1 58  ? 12.387 0.811   22.463 1.00 9.57  ? 64  TYR   A C   1 
ATOM   458  O  O   . TYR   A 1 58  ? 12.607 1.985   22.066 1.00 10.02 ? 64  TYR   A O   1 
ATOM   459  C  CB  . TYR   A 1 58  ? 14.427 -0.412  21.737 1.00 11.17 ? 64  TYR   A CB  1 
ATOM   460  C  CG  . TYR   A 1 58  ? 14.897 -0.544  23.163 1.00 11.90 ? 64  TYR   A CG  1 
ATOM   461  C  CD1 . TYR   A 1 58  ? 14.586 -1.668  23.905 1.00 12.30 ? 64  TYR   A CD1 1 
ATOM   462  C  CD2 . TYR   A 1 58  ? 15.613 0.482   23.779 1.00 11.56 ? 64  TYR   A CD2 1 
ATOM   463  C  CE1 . TYR   A 1 58  ? 14.963 -1.774  25.237 1.00 12.70 ? 64  TYR   A CE1 1 
ATOM   464  C  CE2 . TYR   A 1 58  ? 16.014 0.384   25.104 1.00 12.03 ? 64  TYR   A CE2 1 
ATOM   465  C  CZ  . TYR   A 1 58  ? 15.711 -0.759  25.816 1.00 13.21 ? 64  TYR   A CZ  1 
ATOM   466  O  OH  . TYR   A 1 58  ? 16.093 -0.900  27.144 1.00 16.06 ? 64  TYR   A OH  1 
ATOM   467  N  N   . CYS   A 1 59  ? 11.797 0.513   23.609 1.00 9.81  ? 65  CYS   A N   1 
ATOM   468  C  CA  . CYS   A 1 59  ? 11.237 1.515   24.543 1.00 10.66 ? 65  CYS   A CA  1 
ATOM   469  C  C   . CYS   A 1 59  ? 12.053 1.523   25.858 1.00 11.71 ? 65  CYS   A C   1 
ATOM   470  O  O   . CYS   A 1 59  ? 11.858 0.614   26.719 1.00 11.50 ? 65  CYS   A O   1 
ATOM   471  C  CB  . CYS   A 1 59  ? 9.769  1.190   24.803 1.00 10.53 ? 65  CYS   A CB  1 
ATOM   472  S  SG  . CYS   A 1 59  ? 8.970  2.286   26.036 1.00 11.64 ? 65  CYS   A SG  1 
ATOM   473  N  N   . SER   A 1 60  ? 12.947 2.515   26.033 1.00 11.44 ? 66  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 60  ? 13.818 2.520   27.234 1.00 11.80 ? 66  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 60  ? 13.046 2.711   28.551 1.00 11.81 ? 66  SER   A C   1 
ATOM   476  O  O   . SER   A 1 60  ? 13.427 2.145   29.567 1.00 13.16 ? 66  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 60  ? 14.922 3.579   27.129 1.00 13.27 ? 66  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 60  ? 14.436 4.911   27.156 1.00 14.99 ? 66  SER   A OG  1 
ATOM   479  N  N   . SER   A 1 61  ? 11.907 3.425   28.500 1.00 10.00 ? 67  SER   A N   1 
ATOM   480  C  CA  . SER   A 1 61  ? 11.074 3.632   29.683 1.00 10.46 ? 67  SER   A CA  1 
ATOM   481  C  C   . SER   A 1 61  ? 10.291 2.404   30.150 1.00 10.73 ? 67  SER   A C   1 
ATOM   482  O  O   . SER   A 1 61  ? 9.622  2.439   31.182 1.00 10.82 ? 67  SER   A O   1 
ATOM   483  C  CB  . SER   A 1 61  ? 10.144 4.826   29.475 1.00 10.58 ? 67  SER   A CB  1 
ATOM   484  O  OG  . SER   A 1 61  ? 9.157  4.610   28.471 1.00 12.25 ? 67  SER   A OG  1 
ATOM   485  N  N   . ARG   A 1 62  ? 10.393 1.299   29.403 1.00 10.76 ? 68  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? 9.856  -0.001  29.782 1.00 10.86 ? 68  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? 10.922 -1.109  29.748 1.00 12.21 ? 68  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? 10.585 -2.288  30.013 1.00 12.54 ? 68  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? 8.680  -0.375  28.840 1.00 10.72 ? 68  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? 7.484  0.560   28.987 1.00 11.65 ? 68  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? 6.736  0.223   30.263 1.00 11.05 ? 68  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? 5.569  1.114   30.428 1.00 12.91 ? 68  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? 5.582  2.275   31.079 1.00 12.63 ? 68  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? 6.725  2.759   31.587 1.00 13.19 ? 68  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? 4.458  2.985   31.210 1.00 12.94 ? 68  ARG   A NH2 1 
ATOM   496  N  N   . ARG   A 1 63  ? 12.164 -0.794  29.281 1.00 13.33 ? 69  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 63  ? 13.237 -1.784  29.047 1.00 14.39 ? 69  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 63  ? 12.661 -2.965  28.210 1.00 15.78 ? 69  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 63  ? 12.905 -4.162  28.511 1.00 17.47 ? 69  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 63  ? 13.753 -2.306  30.402 1.00 18.87 ? 69  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 63  ? 15.212 -2.370  30.545 1.00 22.86 ? 69  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 63  ? 15.531 -2.818  31.935 1.00 20.71 ? 69  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 63  ? 16.194 -1.725  32.614 1.00 21.03 ? 69  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 63  ? 15.873 -1.276  33.821 1.00 17.66 ? 69  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 63  ? 14.808 -1.764  34.462 1.00 17.98 ? 69  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 63  ? 16.547 -0.267  34.356 1.00 16.97 ? 69  ARG   A NH2 1 
ATOM   507  N  N   . LYS   A 1 64  ? 11.878 -2.647  27.163 1.00 13.23 ? 70  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 64  ? 11.195 -3.655  26.364 1.00 13.44 ? 70  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 64  ? 11.139 -3.293  24.887 1.00 13.20 ? 70  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 64  ? 11.049 -2.108  24.550 1.00 12.70 ? 70  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 64  ? 9.735  -3.824  26.845 1.00 16.16 ? 70  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 64  ? 9.612  -4.798  28.027 1.00 26.35 ? 70  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 64  ? 8.195  -5.241  28.287 1.00 34.51 ? 70  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 64  ? 8.114  -6.008  29.592 1.00 40.81 ? 70  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 64  ? 8.672  -5.228  30.735 1.00 45.51 ? 70  LYS   A NZ  1 
ATOM   516  N  N   . HIS   A 1 65  ? 11.125 -4.316  24.019 1.00 12.12 ? 71  HIS   A N   1 
ATOM   517  C  CA  . HIS   A 1 65  ? 10.895 -4.159  22.566 1.00 11.72 ? 71  HIS   A CA  1 
ATOM   518  C  C   . HIS   A 1 65  ? 9.438  -4.521  22.280 1.00 13.29 ? 71  HIS   A C   1 
ATOM   519  O  O   . HIS   A 1 65  ? 8.955  -5.566  22.727 1.00 16.94 ? 71  HIS   A O   1 
ATOM   520  C  CB  . HIS   A 1 65  ? 11.818 -5.109  21.773 1.00 11.51 ? 71  HIS   A CB  1 
ATOM   521  C  CG  . HIS   A 1 65  ? 13.267 -4.769  21.902 1.00 12.37 ? 71  HIS   A CG  1 
ATOM   522  N  ND1 . HIS   A 1 65  ? 13.962 -4.081  20.918 1.00 15.75 ? 71  HIS   A ND1 1 
ATOM   523  C  CD2 . HIS   A 1 65  ? 14.113 -5.070  22.913 1.00 12.10 ? 71  HIS   A CD2 1 
ATOM   524  C  CE1 . HIS   A 1 65  ? 15.232 -4.030  21.341 1.00 12.98 ? 71  HIS   A CE1 1 
ATOM   525  N  NE2 . HIS   A 1 65  ? 15.354 -4.584  22.542 1.00 15.06 ? 71  HIS   A NE2 1 
ATOM   526  N  N   . TYR   A 1 66  ? 8.715  -3.643  21.550 1.00 11.01 ? 72  TYR   A N   1 
ATOM   527  C  CA  . TYR   A 1 66  ? 7.295  -3.881  21.273 1.00 11.79 ? 72  TYR   A CA  1 
ATOM   528  C  C   . TYR   A 1 66  ? 7.050  -3.982  19.786 1.00 10.93 ? 72  TYR   A C   1 
ATOM   529  O  O   . TYR   A 1 66  ? 7.552  -3.144  19.031 1.00 10.93 ? 72  TYR   A O   1 
ATOM   530  C  CB  . TYR   A 1 66  ? 6.449  -2.663  21.770 1.00 11.80 ? 72  TYR   A CB  1 
ATOM   531  C  CG  . TYR   A 1 66  ? 6.388  -2.511  23.276 1.00 11.60 ? 72  TYR   A CG  1 
ATOM   532  C  CD1 . TYR   A 1 66  ? 5.601  -3.355  24.050 1.00 13.14 ? 72  TYR   A CD1 1 
ATOM   533  C  CD2 . TYR   A 1 66  ? 7.097  -1.512  23.911 1.00 11.85 ? 72  TYR   A CD2 1 
ATOM   534  C  CE1 . TYR   A 1 66  ? 5.534  -3.233  25.438 1.00 12.76 ? 72  TYR   A CE1 1 
ATOM   535  C  CE2 . TYR   A 1 66  ? 7.014  -1.345  25.301 1.00 13.88 ? 72  TYR   A CE2 1 
ATOM   536  C  CZ  . TYR   A 1 66  ? 6.229  -2.207  26.058 1.00 13.63 ? 72  TYR   A CZ  1 
ATOM   537  O  OH  . TYR   A 1 66  ? 6.140  -2.048  27.430 1.00 16.23 ? 72  TYR   A OH  1 
ATOM   538  N  N   . PRO   A 1 67  ? 6.217  -4.929  19.359 1.00 11.35 ? 73  PRO   A N   1 
ATOM   539  C  CA  . PRO   A 1 67  ? 5.814  -4.944  17.935 1.00 12.05 ? 73  PRO   A CA  1 
ATOM   540  C  C   . PRO   A 1 67  ? 4.811  -3.808  17.668 1.00 13.53 ? 73  PRO   A C   1 
ATOM   541  O  O   . PRO   A 1 67  ? 3.936  -3.537  18.527 1.00 17.26 ? 73  PRO   A O   1 
ATOM   542  C  CB  . PRO   A 1 67  ? 5.154  -6.321  17.734 1.00 13.84 ? 73  PRO   A CB  1 
ATOM   543  C  CG  . PRO   A 1 67  ? 4.738  -6.762  19.115 1.00 15.31 ? 73  PRO   A CG  1 
ATOM   544  C  CD  . PRO   A 1 67  ? 5.618  -6.027  20.142 1.00 12.32 ? 73  PRO   A CD  1 
ATOM   545  N  N   . VAL   A 1 68  ? 4.896  -3.184  16.509 1.00 11.35 ? 74  VAL   A N   1 
ATOM   546  C  CA  . VAL   A 1 68  ? 3.999  -2.073  16.170 1.00 13.35 ? 74  VAL   A CA  1 
ATOM   547  C  C   . VAL   A 1 68  ? 3.661  -2.065  14.698 1.00 12.94 ? 74  VAL   A C   1 
ATOM   548  O  O   . VAL   A 1 68  ? 4.436  -2.461  13.859 1.00 12.38 ? 74  VAL   A O   1 
ATOM   549  C  CB  . VAL   A 1 68  ? 4.587  -0.699  16.528 1.00 17.27 ? 74  VAL   A CB  1 
ATOM   550  C  CG1 . VAL   A 1 68  ? 4.532  -0.479  18.020 1.00 19.28 ? 74  VAL   A CG1 1 
ATOM   551  C  CG2 . VAL   A 1 68  ? 5.984  -0.521  15.967 1.00 17.27 ? 74  VAL   A CG2 1 
ATOM   552  N  N   . SER   A 1 69  ? 2.475  -1.511  14.394 1.00 12.19 ? 75  SER   A N   1 
ATOM   553  C  CA  A SER   A 1 69  ? 2.077  -1.133  13.043 0.50 12.42 ? 75  SER   A CA  1 
ATOM   554  C  CA  B SER   A 1 69  ? 2.013  -1.135  13.066 0.50 12.82 ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 2.281  0.388   12.972 1.00 12.05 ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 1.938  1.100   13.923 1.00 13.12 ? 75  SER   A O   1 
ATOM   557  C  CB  A SER   A 1 69  ? 0.608  -1.459  12.801 0.50 13.94 ? 75  SER   A CB  1 
ATOM   558  C  CB  B SER   A 1 69  ? 0.505  -1.362  12.971 0.50 15.32 ? 75  SER   A CB  1 
ATOM   559  O  OG  A SER   A 1 69  ? 0.445  -2.861  12.871 0.50 15.97 ? 75  SER   A OG  1 
ATOM   560  O  OG  B SER   A 1 69  ? 0.028  -0.890  11.725 0.50 19.48 ? 75  SER   A OG  1 
ATOM   561  N  N   . PHE   A 1 70  ? 2.879  0.898   11.893 1.00 11.69 ? 76  PHE   A N   1 
ATOM   562  C  CA  . PHE   A 1 70  ? 3.181  2.330   11.795 1.00 12.55 ? 76  PHE   A CA  1 
ATOM   563  C  C   . PHE   A 1 70  ? 2.788  2.915   10.457 1.00 12.83 ? 76  PHE   A C   1 
ATOM   564  O  O   . PHE   A 1 70  ? 2.686  2.190   9.454  1.00 13.76 ? 76  PHE   A O   1 
ATOM   565  C  CB  . PHE   A 1 70  ? 4.691  2.575   12.155 1.00 13.19 ? 76  PHE   A CB  1 
ATOM   566  C  CG  . PHE   A 1 70  ? 5.718  1.775   11.362 1.00 11.75 ? 76  PHE   A CG  1 
ATOM   567  C  CD1 . PHE   A 1 70  ? 6.136  0.512   11.787 1.00 11.75 ? 76  PHE   A CD1 1 
ATOM   568  C  CD2 . PHE   A 1 70  ? 6.283  2.293   10.210 1.00 12.23 ? 76  PHE   A CD2 1 
ATOM   569  C  CE1 . PHE   A 1 70  ? 7.074  -0.201  11.076 1.00 12.10 ? 76  PHE   A CE1 1 
ATOM   570  C  CE2 . PHE   A 1 70  ? 7.252  1.578   9.505  1.00 13.17 ? 76  PHE   A CE2 1 
ATOM   571  C  CZ  . PHE   A 1 70  ? 7.619  0.324   9.939  1.00 12.35 ? 76  PHE   A CZ  1 
ATOM   572  N  N   . SER   A 1 71  ? 2.520  4.219   10.428 1.00 13.17 ? 77  SER   A N   1 
ATOM   573  C  CA  . SER   A 1 71  ? 2.114  4.895   9.197  1.00 13.51 ? 77  SER   A CA  1 
ATOM   574  C  C   . SER   A 1 71  ? 3.273  5.095   8.222  1.00 13.50 ? 77  SER   A C   1 
ATOM   575  O  O   . SER   A 1 71  ? 4.441  4.948   8.614  1.00 13.66 ? 77  SER   A O   1 
ATOM   576  C  CB  . SER   A 1 71  ? 1.408  6.216   9.534  1.00 15.19 ? 77  SER   A CB  1 
ATOM   577  O  OG  . SER   A 1 71  ? 2.312  7.122   10.164 1.00 18.24 ? 77  SER   A OG  1 
ATOM   578  N  N   . LYS   A 1 72  ? 2.984  5.460   6.991  1.00 12.74 ? 78  LYS   A N   1 
ATOM   579  C  CA  . LYS   A 1 72  ? 4.040  5.764   6.028  1.00 13.04 ? 78  LYS   A CA  1 
ATOM   580  C  C   . LYS   A 1 72  ? 4.658  7.138   6.362  1.00 14.30 ? 78  LYS   A C   1 
ATOM   581  O  O   . LYS   A 1 72  ? 3.985  7.994   6.935  1.00 15.22 ? 78  LYS   A O   1 
ATOM   582  C  CB  . LYS   A 1 72  ? 3.418  5.768   4.632  1.00 14.59 ? 78  LYS   A CB  1 
ATOM   583  C  CG  . LYS   A 1 72  ? 3.021  4.360   4.209  1.00 18.10 ? 78  LYS   A CG  1 
ATOM   584  C  CD  . LYS   A 1 72  ? 2.573  4.340   2.742  1.00 26.11 ? 78  LYS   A CD  1 
ATOM   585  C  CE  . LYS   A 1 72  ? 2.200  2.954   2.281  1.00 33.08 ? 78  LYS   A CE  1 
ATOM   586  N  NZ  . LYS   A 1 72  ? 2.224  2.867   0.796  1.00 37.47 ? 78  LYS   A NZ  1 
ATOM   587  N  N   . PRO   A 1 73  ? 5.931  7.375   6.027  1.00 13.70 ? 79  PRO   A N   1 
ATOM   588  C  CA  . PRO   A 1 73  ? 6.560  8.684   6.347  1.00 13.88 ? 79  PRO   A CA  1 
ATOM   589  C  C   . PRO   A 1 73  ? 5.755  9.858   5.785  1.00 15.23 ? 79  PRO   A C   1 
ATOM   590  O  O   . PRO   A 1 73  ? 5.385  9.867   4.588  1.00 16.80 ? 79  PRO   A O   1 
ATOM   591  C  CB  . PRO   A 1 73  ? 7.961  8.596   5.706  1.00 16.31 ? 79  PRO   A CB  1 
ATOM   592  C  CG  . PRO   A 1 73  ? 8.163  7.151   5.373  1.00 19.58 ? 79  PRO   A CG  1 
ATOM   593  C  CD  . PRO   A 1 73  ? 6.849  6.460   5.315  1.00 16.20 ? 79  PRO   A CD  1 
ATOM   594  N  N   . SER   A 1 74  ? 5.459  10.807  6.671  1.00 14.71 ? 80  SER   A N   1 
ATOM   595  C  CA  . SER   A 1 74  ? 4.575  11.916  6.288  1.00 15.65 ? 80  SER   A CA  1 
ATOM   596  C  C   . SER   A 1 74  ? 4.952  13.208  7.039  1.00 14.51 ? 80  SER   A C   1 
ATOM   597  O  O   . SER   A 1 74  ? 5.788  13.210  7.934  1.00 13.95 ? 80  SER   A O   1 
ATOM   598  C  CB  . SER   A 1 74  ? 3.101  11.555  6.562  1.00 22.23 ? 80  SER   A CB  1 
ATOM   599  O  OG  . SER   A 1 74  ? 2.739  10.198  6.780  1.00 27.46 ? 80  SER   A OG  1 
ATOM   600  N  N   . LEU   A 1 75  ? 4.269  14.316  6.661  1.00 15.04 ? 81  LEU   A N   1 
ATOM   601  C  CA  . LEU   A 1 75  ? 4.435  15.650  7.244  1.00 15.62 ? 81  LEU   A CA  1 
ATOM   602  C  C   . LEU   A 1 75  ? 3.337  15.812  8.310  1.00 16.04 ? 81  LEU   A C   1 
ATOM   603  O  O   . LEU   A 1 75  ? 2.138  15.816  7.975  1.00 18.11 ? 81  LEU   A O   1 
ATOM   604  C  CB  . LEU   A 1 75  ? 4.250  16.723  6.151  1.00 16.80 ? 81  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A 1 75  ? 4.558  18.140  6.611  1.00 19.07 ? 81  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A 1 75  ? 6.029  18.298  6.937  1.00 19.46 ? 81  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A 1 75  ? 4.177  19.152  5.497  1.00 22.09 ? 81  LEU   A CD2 1 
ATOM   608  N  N   . ILE   A 1 76  ? 3.725  15.791  9.596  1.00 14.31 ? 82  ILE   A N   1 
ATOM   609  C  CA  . ILE   A 1 76  ? 2.810  15.801  10.745 1.00 14.59 ? 82  ILE   A CA  1 
ATOM   610  C  C   . ILE   A 1 76  ? 3.096  16.951  11.690 1.00 16.54 ? 82  ILE   A C   1 
ATOM   611  O  O   . ILE   A 1 76  ? 4.265  17.242  11.985 1.00 15.92 ? 82  ILE   A O   1 
ATOM   612  C  CB  . ILE   A 1 76  ? 3.010  14.449  11.489 1.00 15.96 ? 82  ILE   A CB  1 
ATOM   613  C  CG1 . ILE   A 1 76  ? 2.615  13.283  10.587 1.00 18.71 ? 82  ILE   A CG1 1 
ATOM   614  C  CG2 . ILE   A 1 76  ? 2.238  14.408  12.848 1.00 17.30 ? 82  ILE   A CG2 1 
ATOM   615  C  CD1 . ILE   A 1 76  ? 2.806  11.938  11.154 1.00 19.09 ? 82  ILE   A CD1 1 
ATOM   616  N  N   . PHE   A 1 77  ? 2.042  17.620  12.207 1.00 16.38 ? 83  PHE   A N   1 
ATOM   617  C  CA  . PHE   A 1 77  ? 2.241  18.707  13.174 1.00 16.95 ? 83  PHE   A CA  1 
ATOM   618  C  C   . PHE   A 1 77  ? 2.560  18.066  14.509 1.00 18.42 ? 83  PHE   A C   1 
ATOM   619  O  O   . PHE   A 1 77  ? 1.778  17.249  15.015 1.00 20.81 ? 83  PHE   A O   1 
ATOM   620  C  CB  . PHE   A 1 77  ? 0.954  19.574  13.304 1.00 17.69 ? 83  PHE   A CB  1 
ATOM   621  C  CG  . PHE   A 1 77  ? 1.223  20.917  13.949 1.00 20.11 ? 83  PHE   A CG  1 
ATOM   622  C  CD1 . PHE   A 1 77  ? 2.001  21.866  13.312 1.00 21.17 ? 83  PHE   A CD1 1 
ATOM   623  C  CD2 . PHE   A 1 77  ? 0.689  21.225  15.192 1.00 22.23 ? 83  PHE   A CD2 1 
ATOM   624  C  CE1 . PHE   A 1 77  ? 2.264  23.097  13.914 1.00 22.93 ? 83  PHE   A CE1 1 
ATOM   625  C  CE2 . PHE   A 1 77  ? 0.945  22.449  15.786 1.00 23.20 ? 83  PHE   A CE2 1 
ATOM   626  C  CZ  . PHE   A 1 77  ? 1.726  23.382  15.139 1.00 23.18 ? 83  PHE   A CZ  1 
ATOM   627  N  N   . VAL   A 1 78  ? 3.688  18.442  15.098 1.00 15.77 ? 84  VAL   A N   1 
ATOM   628  C  CA  . VAL   A 1 78  ? 4.197  17.901  16.356 1.00 14.79 ? 84  VAL   A CA  1 
ATOM   629  C  C   . VAL   A 1 78  ? 4.138  19.021  17.405 1.00 14.57 ? 84  VAL   A C   1 
ATOM   630  O  O   . VAL   A 1 78  ? 4.619  20.132  17.140 1.00 15.62 ? 84  VAL   A O   1 
ATOM   631  C  CB  . VAL   A 1 78  ? 5.642  17.417  16.163 1.00 14.71 ? 84  VAL   A CB  1 
ATOM   632  C  CG1 . VAL   A 1 78  ? 6.245  17.018  17.525 1.00 15.27 ? 84  VAL   A CG1 1 
ATOM   633  C  CG2 . VAL   A 1 78  ? 5.664  16.235  15.195 1.00 15.28 ? 84  VAL   A CG2 1 
ATOM   634  N  N   . GLU   A 1 79  ? 3.540  18.724  18.568 1.00 14.36 ? 85  GLU   A N   1 
ATOM   635  C  CA  . GLU   A 1 79  ? 3.384  19.719  19.628 1.00 15.44 ? 85  GLU   A CA  1 
ATOM   636  C  C   . GLU   A 1 79  ? 4.714  20.181  20.189 1.00 15.73 ? 85  GLU   A C   1 
ATOM   637  O  O   . GLU   A 1 79  ? 5.721  19.472  20.111 1.00 15.30 ? 85  GLU   A O   1 
ATOM   638  C  CB  . GLU   A 1 79  ? 2.577  19.104  20.792 1.00 17.70 ? 85  GLU   A CB  1 
ATOM   639  C  CG  . GLU   A 1 79  ? 1.115  18.801  20.428 1.00 22.92 ? 85  GLU   A CG  1 
ATOM   640  C  CD  . GLU   A 1 79  ? 0.391  20.061  19.971 1.00 30.10 ? 85  GLU   A CD  1 
ATOM   641  O  OE1 . GLU   A 1 79  ? 0.390  21.044  20.746 1.00 35.91 ? 85  GLU   A OE1 1 
ATOM   642  O  OE2 . GLU   A 1 79  ? -0.082 20.104  18.812 1.00 32.37 ? 85  GLU   A OE2 1 
ATOM   643  N  N   . ALA   A 1 80  ? 4.718  21.359  20.810 1.00 16.17 ? 86  ALA   A N   1 
ATOM   644  C  CA  . ALA   A 1 80  ? 5.923  21.900  21.438 1.00 15.89 ? 86  ALA   A CA  1 
ATOM   645  C  C   . ALA   A 1 80  ? 6.485  20.971  22.481 1.00 16.14 ? 86  ALA   A C   1 
ATOM   646  O  O   . ALA   A 1 80  ? 5.741  20.263  23.192 1.00 17.01 ? 86  ALA   A O   1 
ATOM   647  C  CB  . ALA   A 1 80  ? 5.618  23.247  22.096 1.00 16.84 ? 86  ALA   A CB  1 
ATOM   648  N  N   . SER   A 1 81  ? 7.839  20.932  22.532 1.00 16.04 ? 87  SER   A N   1 
ATOM   649  C  CA  . SER   A 1 81  ? 8.548  20.127  23.528 1.00 16.60 ? 87  SER   A CA  1 
ATOM   650  C  C   . SER   A 1 81  ? 9.658  20.995  24.128 1.00 17.54 ? 87  SER   A C   1 
ATOM   651  O  O   . SER   A 1 81  ? 9.753  22.183  23.832 1.00 19.43 ? 87  SER   A O   1 
ATOM   652  C  CB  . SER   A 1 81  ? 9.161  18.877  22.884 1.00 16.68 ? 87  SER   A CB  1 
ATOM   653  O  OG  . SER   A 1 81  ? 10.173 19.266  21.972 1.00 16.08 ? 87  SER   A OG  1 
ATOM   654  N  N   . GLU   A 1 82  ? 10.534 20.396  24.954 1.00 17.57 ? 88  GLU   A N   1 
ATOM   655  C  CA  . GLU   A 1 82  ? 11.699 21.134  25.487 1.00 18.62 ? 88  GLU   A CA  1 
ATOM   656  C  C   . GLU   A 1 82  ? 12.669 21.533  24.338 1.00 18.04 ? 88  GLU   A C   1 
ATOM   657  O  O   . GLU   A 1 82  ? 13.480 22.456  24.470 1.00 19.04 ? 88  GLU   A O   1 
ATOM   658  C  CB  . GLU   A 1 82  ? 12.446 20.183  26.455 1.00 22.92 ? 88  GLU   A CB  1 
ATOM   659  C  CG  . GLU   A 1 82  ? 13.716 20.734  27.055 1.00 29.70 ? 88  GLU   A CG  1 
ATOM   660  C  CD  . GLU   A 1 82  ? 14.425 19.791  28.004 1.00 36.25 ? 88  GLU   A CD  1 
ATOM   661  O  OE1 . GLU   A 1 82  ? 15.615 20.051  28.296 1.00 39.03 ? 88  GLU   A OE1 1 
ATOM   662  O  OE2 . GLU   A 1 82  ? 13.805 18.794  28.449 1.00 35.49 ? 88  GLU   A OE2 1 
ATOM   663  N  N   . TYR   A 1 83  ? 12.594 20.822  23.205 1.00 16.54 ? 89  TYR   A N   1 
ATOM   664  C  CA  . TYR   A 1 83  ? 13.578 20.961  22.140 1.00 15.71 ? 89  TYR   A CA  1 
ATOM   665  C  C   . TYR   A 1 83  ? 13.156 21.691  20.895 1.00 14.41 ? 89  TYR   A C   1 
ATOM   666  O  O   . TYR   A 1 83  ? 14.022 22.155  20.144 1.00 15.13 ? 89  TYR   A O   1 
ATOM   667  C  CB  . TYR   A 1 83  ? 14.061 19.548  21.756 1.00 16.33 ? 89  TYR   A CB  1 
ATOM   668  C  CG  . TYR   A 1 83  ? 14.661 18.823  22.937 1.00 18.83 ? 89  TYR   A CG  1 
ATOM   669  C  CD1 . TYR   A 1 83  ? 15.943 19.119  23.377 1.00 21.25 ? 89  TYR   A CD1 1 
ATOM   670  C  CD2 . TYR   A 1 83  ? 13.919 17.893  23.657 1.00 22.05 ? 89  TYR   A CD2 1 
ATOM   671  C  CE1 . TYR   A 1 83  ? 16.516 18.427  24.445 1.00 24.33 ? 89  TYR   A CE1 1 
ATOM   672  C  CE2 . TYR   A 1 83  ? 14.472 17.221  24.741 1.00 24.08 ? 89  TYR   A CE2 1 
ATOM   673  C  CZ  . TYR   A 1 83  ? 15.748 17.537  25.166 1.00 25.68 ? 89  TYR   A CZ  1 
ATOM   674  O  OH  . TYR   A 1 83  ? 16.312 16.826  26.203 1.00 30.01 ? 89  TYR   A OH  1 
ATOM   675  N  N   . TYR   A 1 84  ? 11.842 21.776  20.641 1.00 15.38 ? 90  TYR   A N   1 
ATOM   676  C  CA  . TYR   A 1 84  ? 11.345 22.453  19.455 1.00 14.70 ? 90  TYR   A CA  1 
ATOM   677  C  C   . TYR   A 1 84  ? 10.003 23.113  19.799 1.00 14.96 ? 90  TYR   A C   1 
ATOM   678  O  O   . TYR   A 1 84  ? 9.234  22.542  20.584 1.00 14.30 ? 90  TYR   A O   1 
ATOM   679  C  CB  . TYR   A 1 84  ? 11.026 21.430  18.342 1.00 14.95 ? 90  TYR   A CB  1 
ATOM   680  C  CG  . TYR   A 1 84  ? 12.197 20.629  17.790 1.00 13.14 ? 90  TYR   A CG  1 
ATOM   681  C  CD1 . TYR   A 1 84  ? 13.105 21.199  16.915 1.00 14.08 ? 90  TYR   A CD1 1 
ATOM   682  C  CD2 . TYR   A 1 84  ? 12.407 19.301  18.169 1.00 12.22 ? 90  TYR   A CD2 1 
ATOM   683  C  CE1 . TYR   A 1 84  ? 14.170 20.469  16.395 1.00 13.42 ? 90  TYR   A CE1 1 
ATOM   684  C  CE2 . TYR   A 1 84  ? 13.466 18.564  17.660 1.00 13.61 ? 90  TYR   A CE2 1 
ATOM   685  C  CZ  . TYR   A 1 84  ? 14.344 19.152  16.782 1.00 13.06 ? 90  TYR   A CZ  1 
ATOM   686  O  OH  . TYR   A 1 84  ? 15.418 18.434  16.304 1.00 13.56 ? 90  TYR   A OH  1 
ATOM   687  N  N   . PRO   A 1 85  ? 9.697  24.260  19.165 1.00 16.18 ? 91  PRO   A N   1 
ATOM   688  C  CA  . PRO   A 1 85  ? 8.317  24.779  19.267 1.00 16.91 ? 91  PRO   A CA  1 
ATOM   689  C  C   . PRO   A 1 85  ? 7.377  23.850  18.469 1.00 17.35 ? 91  PRO   A C   1 
ATOM   690  O  O   . PRO   A 1 85  ? 7.842  22.956  17.719 1.00 17.22 ? 91  PRO   A O   1 
ATOM   691  C  CB  . PRO   A 1 85  ? 8.426  26.184  18.621 1.00 18.68 ? 91  PRO   A CB  1 
ATOM   692  C  CG  . PRO   A 1 85  ? 9.507  26.036  17.593 1.00 18.94 ? 91  PRO   A CG  1 
ATOM   693  C  CD  . PRO   A 1 85  ? 10.517 25.016  18.183 1.00 16.35 ? 91  PRO   A CD  1 
ATOM   694  N  N   . ALA   A 1 86  ? 6.055  24.075  18.561 1.00 18.05 ? 92  ALA   A N   1 
ATOM   695  C  CA  . ALA   A 1 86  ? 5.106  23.278  17.766 1.00 17.22 ? 92  ALA   A CA  1 
ATOM   696  C  C   . ALA   A 1 86  ? 5.386  23.588  16.281 1.00 17.37 ? 92  ALA   A C   1 
ATOM   697  O  O   . ALA   A 1 86  ? 5.587  24.757  15.918 1.00 18.30 ? 92  ALA   A O   1 
ATOM   698  C  CB  . ALA   A 1 86  ? 3.659  23.637  18.135 1.00 17.56 ? 92  ALA   A CB  1 
ATOM   699  N  N   . ARG   A 1 87  ? 5.563  22.560  15.458 1.00 16.45 ? 93  ARG   A N   1 
ATOM   700  C  CA  . ARG   A 1 87  ? 5.935  22.753  14.051 1.00 15.73 ? 93  ARG   A CA  1 
ATOM   701  C  C   . ARG   A 1 87  ? 5.562  21.496  13.265 1.00 15.78 ? 93  ARG   A C   1 
ATOM   702  O  O   . ARG   A 1 87  ? 5.308  20.450  13.881 1.00 17.11 ? 93  ARG   A O   1 
ATOM   703  C  CB  . ARG   A 1 87  ? 7.471  22.985  13.933 1.00 17.55 ? 93  ARG   A CB  1 
ATOM   704  C  CG  . ARG   A 1 87  ? 8.306  21.671  13.816 1.00 21.75 ? 93  ARG   A CG  1 
ATOM   705  C  CD  . ARG   A 1 87  ? 9.457  21.676  14.705 1.00 22.51 ? 93  ARG   A CD  1 
ATOM   706  N  NE  . ARG   A 1 87  ? 10.425 20.654  14.313 1.00 17.63 ? 93  ARG   A NE  1 
ATOM   707  C  CZ  . ARG   A 1 87  ? 10.491 19.426  14.826 1.00 19.41 ? 93  ARG   A CZ  1 
ATOM   708  N  NH1 . ARG   A 1 87  ? 9.582  19.013  15.723 1.00 17.39 ? 93  ARG   A NH1 1 
ATOM   709  N  NH2 . ARG   A 1 87  ? 11.491 18.618  14.488 1.00 16.58 ? 93  ARG   A NH2 1 
ATOM   710  N  N   . TYR   A 1 88  ? 5.698  21.551  11.919 1.00 16.42 ? 94  TYR   A N   1 
ATOM   711  C  CA  . TYR   A 1 88  ? 5.522  20.377  11.079 1.00 17.03 ? 94  TYR   A CA  1 
ATOM   712  C  C   . TYR   A 1 88  ? 6.852  19.636  10.941 1.00 16.43 ? 94  TYR   A C   1 
ATOM   713  O  O   . TYR   A 1 88  ? 7.875  20.215  10.572 1.00 17.21 ? 94  TYR   A O   1 
ATOM   714  C  CB  . TYR   A 1 88  ? 5.036  20.763  9.681  1.00 18.14 ? 94  TYR   A CB  1 
ATOM   715  C  CG  . TYR   A 1 88  ? 3.552  21.041  9.663  1.00 19.09 ? 94  TYR   A CG  1 
ATOM   716  C  CD1 . TYR   A 1 88  ? 2.638  20.007  9.596  1.00 19.93 ? 94  TYR   A CD1 1 
ATOM   717  C  CD2 . TYR   A 1 88  ? 3.065  22.331  9.804  1.00 20.54 ? 94  TYR   A CD2 1 
ATOM   718  C  CE1 . TYR   A 1 88  ? 1.282  20.234  9.689  1.00 21.25 ? 94  TYR   A CE1 1 
ATOM   719  C  CE2 . TYR   A 1 88  ? 1.700  22.581  9.837  1.00 21.21 ? 94  TYR   A CE2 1 
ATOM   720  C  CZ  . TYR   A 1 88  ? 0.812  21.528  9.763  1.00 21.94 ? 94  TYR   A CZ  1 
ATOM   721  O  OH  . TYR   A 1 88  ? -0.540 21.730  9.811  1.00 24.62 ? 94  TYR   A OH  1 
ATOM   722  N  N   . GLN   A 1 89  ? 6.828  18.342  11.287 1.00 14.48 ? 95  GLN   A N   1 
ATOM   723  C  CA  . GLN   A 1 89  ? 8.008  17.457  11.173 1.00 14.31 ? 95  GLN   A CA  1 
ATOM   724  C  C   . GLN   A 1 89  ? 7.786  16.583  9.946  1.00 14.16 ? 95  GLN   A C   1 
ATOM   725  O  O   . GLN   A 1 89  ? 6.684  16.036  9.754  1.00 14.31 ? 95  GLN   A O   1 
ATOM   726  C  CB  . GLN   A 1 89  ? 8.195  16.611  12.437 1.00 14.38 ? 95  GLN   A CB  1 
ATOM   727  C  CG  . GLN   A 1 89  ? 9.444  15.705  12.378 1.00 14.09 ? 95  GLN   A CG  1 
ATOM   728  C  CD  . GLN   A 1 89  ? 9.865  15.178  13.735 1.00 14.48 ? 95  GLN   A CD  1 
ATOM   729  O  OE1 . GLN   A 1 89  ? 9.523  15.732  14.775 1.00 16.54 ? 95  GLN   A OE1 1 
ATOM   730  N  NE2 . GLN   A 1 89  ? 10.534 14.042  13.759 1.00 12.80 ? 95  GLN   A NE2 1 
ATOM   731  N  N   . SER   A 1 90  ? 8.807  16.474  9.088  1.00 12.81 ? 96  SER   A N   1 
ATOM   732  C  CA  . SER   A 1 90  ? 8.714  15.655  7.900  1.00 13.14 ? 96  SER   A CA  1 
ATOM   733  C  C   . SER   A 1 90  ? 9.309  14.258  8.098  1.00 12.79 ? 96  SER   A C   1 
ATOM   734  O  O   . SER   A 1 90  ? 10.109 14.036  9.034  1.00 12.56 ? 96  SER   A O   1 
ATOM   735  C  CB  . SER   A 1 90  ? 9.405  16.377  6.742  1.00 14.85 ? 96  SER   A CB  1 
ATOM   736  O  OG  . SER   A 1 90  ? 10.806 16.493  7.003  1.00 18.10 ? 96  SER   A OG  1 
ATOM   737  N  N   . HIS   A 1 91  ? 8.923  13.327  7.167  1.00 12.49 ? 97  HIS   A N   1 
ATOM   738  C  CA  . HIS   A 1 91  ? 9.409  11.940  7.146  1.00 12.26 ? 97  HIS   A CA  1 
ATOM   739  C  C   . HIS   A 1 91  ? 9.149  11.254  8.512  1.00 11.80 ? 97  HIS   A C   1 
ATOM   740  O  O   . HIS   A 1 91  ? 9.977  10.413  8.929  1.00 12.58 ? 97  HIS   A O   1 
ATOM   741  C  CB  . HIS   A 1 91  ? 10.936 11.924  6.800  1.00 14.14 ? 97  HIS   A CB  1 
ATOM   742  C  CG  . HIS   A 1 91  ? 11.242 12.502  5.444  1.00 15.84 ? 97  HIS   A CG  1 
ATOM   743  N  ND1 . HIS   A 1 91  ? 11.355 11.697  4.334  1.00 17.98 ? 97  HIS   A ND1 1 
ATOM   744  C  CD2 . HIS   A 1 91  ? 11.414 13.788  5.066  1.00 16.78 ? 97  HIS   A CD2 1 
ATOM   745  C  CE1 . HIS   A 1 91  ? 11.626 12.508  3.312  1.00 18.49 ? 97  HIS   A CE1 1 
ATOM   746  N  NE2 . HIS   A 1 91  ? 11.665 13.768  3.694  1.00 18.50 ? 97  HIS   A NE2 1 
ATOM   747  N  N   . LEU   A 1 92  ? 8.022  11.542  9.123  1.00 11.15 ? 98  LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 92  ? 7.671  11.021  10.438 1.00 11.35 ? 98  LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 92  ? 6.597  9.921   10.275 1.00 11.28 ? 98  LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 92  ? 5.653  10.078  9.491  1.00 12.27 ? 98  LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 92  ? 7.114  12.167  11.330 1.00 12.57 ? 98  LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 92  ? 6.764  11.790  12.792 1.00 13.82 ? 98  LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 92  ? 8.005  11.410  13.551 1.00 13.65 ? 98  LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 92  ? 6.037  12.976  13.511 1.00 16.47 ? 98  LEU   A CD2 1 
ATOM   755  N  N   . MET   A 1 93  ? 6.723  8.836   11.065 1.00 11.78 ? 99  MET   A N   1 
ATOM   756  C  CA  . MET   A 1 93  ? 5.763  7.718   11.032 1.00 11.35 ? 99  MET   A CA  1 
ATOM   757  C  C   . MET   A 1 93  ? 5.184  7.554   12.431 1.00 12.47 ? 99  MET   A C   1 
ATOM   758  O  O   . MET   A 1 93  ? 5.953  7.499   13.388 1.00 13.13 ? 99  MET   A O   1 
ATOM   759  C  CB  . MET   A 1 93  ? 6.532  6.438   10.697 1.00 12.25 ? 99  MET   A CB  1 
ATOM   760  C  CG  . MET   A 1 93  ? 7.166  6.540   9.305  1.00 14.06 ? 99  MET   A CG  1 
ATOM   761  S  SD  . MET   A 1 93  ? 8.296  5.177   8.843  1.00 16.03 ? 99  MET   A SD  1 
ATOM   762  C  CE  . MET   A 1 93  ? 9.556  5.359   10.087 1.00 19.34 ? 99  MET   A CE  1 
ATOM   763  N  N   . LEU   A 1 94  ? 3.869  7.430   12.571 1.00 11.65 ? 100 LEU   A N   1 
ATOM   764  C  CA  . LEU   A 1 94  ? 3.246  7.264   13.895 1.00 12.43 ? 100 LEU   A CA  1 
ATOM   765  C  C   . LEU   A 1 94  ? 2.773  5.838   14.151 1.00 13.12 ? 100 LEU   A C   1 
ATOM   766  O  O   . LEU   A 1 94  ? 2.345  5.135   13.220 1.00 12.98 ? 100 LEU   A O   1 
ATOM   767  C  CB  . LEU   A 1 94  ? 2.036  8.213   14.076 1.00 14.55 ? 100 LEU   A CB  1 
ATOM   768  C  CG  . LEU   A 1 94  ? 2.283  9.690   14.024 1.00 18.86 ? 100 LEU   A CG  1 
ATOM   769  C  CD1 . LEU   A 1 94  ? 1.013  10.481  14.471 1.00 19.99 ? 100 LEU   A CD1 1 
ATOM   770  C  CD2 . LEU   A 1 94  ? 3.420  10.103  14.949 1.00 21.54 ? 100 LEU   A CD2 1 
ATOM   771  N  N   . ALA   A 1 95  ? 2.759  5.453   15.427 1.00 13.22 ? 101 ALA   A N   1 
ATOM   772  C  CA  . ALA   A 1 95  ? 2.268  4.142   15.846 1.00 12.57 ? 101 ALA   A CA  1 
ATOM   773  C  C   . ALA   A 1 95  ? 1.644  4.302   17.238 1.00 10.72 ? 101 ALA   A C   1 
ATOM   774  O  O   . ALA   A 1 95  ? 1.927  5.288   17.968 1.00 11.61 ? 101 ALA   A O   1 
ATOM   775  C  CB  . ALA   A 1 95  ? 3.432  3.113   15.937 1.00 13.88 ? 101 ALA   A CB  1 
ATOM   776  N  N   . VAL   A 1 96  ? 0.849  3.314   17.613 1.00 10.94 ? 102 VAL   A N   1 
ATOM   777  C  CA  . VAL   A 1 96  ? 0.354  3.219   18.945 1.00 10.29 ? 102 VAL   A CA  1 
ATOM   778  C  C   . VAL   A 1 96  ? 1.365  2.402   19.778 1.00 11.84 ? 102 VAL   A C   1 
ATOM   779  O  O   . VAL   A 1 96  ? 1.696  1.258   19.440 1.00 14.36 ? 102 VAL   A O   1 
ATOM   780  C  CB  . VAL   A 1 96  ? -1.007 2.499   18.937 1.00 10.75 ? 102 VAL   A CB  1 
ATOM   781  C  CG1 . VAL   A 1 96  ? -1.491 2.307   20.373 1.00 11.20 ? 102 VAL   A CG1 1 
ATOM   782  C  CG2 . VAL   A 1 96  ? -2.023 3.324   18.143 1.00 12.09 ? 102 VAL   A CG2 1 
ATOM   783  N  N   . GLY   A 1 97  ? 1.910  3.050   20.786 1.00 11.20 ? 103 GLY   A N   1 
ATOM   784  C  CA  . GLY   A 1 97  ? 2.926  2.450   21.643 1.00 12.12 ? 103 GLY   A CA  1 
ATOM   785  C  C   . GLY   A 1 97  ? 3.308  3.421   22.734 1.00 11.36 ? 103 GLY   A C   1 
ATOM   786  O  O   . GLY   A 1 97  ? 3.181  4.638   22.569 1.00 12.15 ? 103 GLY   A O   1 
ATOM   787  N  N   . HIS   A 1 98  ? 3.820  2.904   23.866 1.00 11.90 ? 104 HIS   A N   1 
ATOM   788  C  CA  . HIS   A 1 98  ? 4.236  3.787   24.938 1.00 11.87 ? 104 HIS   A CA  1 
ATOM   789  C  C   . HIS   A 1 98  ? 5.523  4.546   24.564 1.00 11.01 ? 104 HIS   A C   1 
ATOM   790  O  O   . HIS   A 1 98  ? 6.459  3.968   24.008 1.00 11.33 ? 104 HIS   A O   1 
ATOM   791  C  CB  . HIS   A 1 98  ? 4.508  2.976   26.228 1.00 12.02 ? 104 HIS   A CB  1 
ATOM   792  C  CG  . HIS   A 1 98  ? 4.907  3.857   27.364 1.00 13.21 ? 104 HIS   A CG  1 
ATOM   793  N  ND1 . HIS   A 1 98  ? 3.999  4.725   27.960 1.00 13.90 ? 104 HIS   A ND1 1 
ATOM   794  C  CD2 . HIS   A 1 98  ? 6.125  4.019   27.956 1.00 12.46 ? 104 HIS   A CD2 1 
ATOM   795  C  CE1 . HIS   A 1 98  ? 4.717  5.441   28.845 1.00 13.65 ? 104 HIS   A CE1 1 
ATOM   796  N  NE2 . HIS   A 1 98  ? 5.981  5.023   28.903 1.00 14.12 ? 104 HIS   A NE2 1 
ATOM   797  N  N   . SER   A 1 99  ? 5.564  5.823   24.955 1.00 11.39 ? 105 SER   A N   1 
ATOM   798  C  CA  . SER   A 1 99  ? 6.783  6.607   24.865 1.00 10.80 ? 105 SER   A CA  1 
ATOM   799  C  C   . SER   A 1 99  ? 6.779  7.770   25.841 1.00 12.15 ? 105 SER   A C   1 
ATOM   800  O  O   . SER   A 1 99  ? 5.710  8.282   26.198 1.00 13.56 ? 105 SER   A O   1 
ATOM   801  C  CB  . SER   A 1 99  ? 7.104  7.065   23.428 1.00 12.46 ? 105 SER   A CB  1 
ATOM   802  O  OG  . SER   A 1 99  ? 6.164  8.061   22.990 1.00 12.96 ? 105 SER   A OG  1 
ATOM   803  N  N   . GLU   A 1 100 ? 8.001  8.115   26.302 1.00 11.42 ? 106 GLU   A N   1 
ATOM   804  C  CA  . GLU   A 1 100 ? 8.326  9.278   27.143 1.00 12.66 ? 106 GLU   A CA  1 
ATOM   805  C  C   . GLU   A 1 100 ? 9.482  10.023  26.476 1.00 13.32 ? 106 GLU   A C   1 
ATOM   806  O  O   . GLU   A 1 100 ? 10.158 9.481   25.576 1.00 12.01 ? 106 GLU   A O   1 
ATOM   807  C  CB  . GLU   A 1 100 ? 8.694  8.830   28.573 1.00 14.38 ? 106 GLU   A CB  1 
ATOM   808  C  CG  . GLU   A 1 100 ? 7.512  8.121   29.211 1.00 15.11 ? 106 GLU   A CG  1 
ATOM   809  C  CD  . GLU   A 1 100 ? 7.782  7.471   30.559 1.00 18.03 ? 106 GLU   A CD  1 
ATOM   810  O  OE1 . GLU   A 1 100 ? 8.545  8.071   31.343 1.00 23.31 ? 106 GLU   A OE1 1 
ATOM   811  O  OE2 . GLU   A 1 100 ? 7.237  6.390   30.841 1.00 16.36 ? 106 GLU   A OE2 1 
ATOM   812  N  N   . PRO   A 1 101 ? 9.719  11.298  26.814 1.00 13.31 ? 107 PRO   A N   1 
ATOM   813  C  CA  . PRO   A 1 101 ? 10.721 12.078  26.052 1.00 13.42 ? 107 PRO   A CA  1 
ATOM   814  C  C   . PRO   A 1 101 ? 12.089 11.411  25.902 1.00 13.27 ? 107 PRO   A C   1 
ATOM   815  O  O   . PRO   A 1 101 ? 12.670 11.392  24.792 1.00 13.56 ? 107 PRO   A O   1 
ATOM   816  C  CB  . PRO   A 1 101 ? 10.764 13.413  26.832 1.00 14.90 ? 107 PRO   A CB  1 
ATOM   817  C  CG  . PRO   A 1 101 ? 9.352  13.549  27.389 1.00 15.30 ? 107 PRO   A CG  1 
ATOM   818  C  CD  . PRO   A 1 101 ? 8.955  12.130  27.773 1.00 13.66 ? 107 PRO   A CD  1 
ATOM   819  N  N   . GLY   A 1 102 ? 12.619 10.825  26.970 1.00 12.66 ? 108 GLY   A N   1 
ATOM   820  C  CA  . GLY   A 1 102 ? 13.920 10.150  26.941 1.00 12.57 ? 108 GLY   A CA  1 
ATOM   821  C  C   . GLY   A 1 102 ? 13.971 8.829   26.158 1.00 12.44 ? 108 GLY   A C   1 
ATOM   822  O  O   . GLY   A 1 102 ? 15.051 8.234   26.002 1.00 12.71 ? 108 GLY   A O   1 
ATOM   823  N  N   . ASP   A 1 103 ? 12.827 8.397   25.614 1.00 10.53 ? 109 ASP   A N   1 
ATOM   824  C  CA  . ASP   A 1 103 ? 12.820 7.224   24.727 1.00 11.02 ? 109 ASP   A CA  1 
ATOM   825  C  C   . ASP   A 1 103 ? 13.348 7.570   23.328 1.00 10.97 ? 109 ASP   A C   1 
ATOM   826  O  O   . ASP   A 1 103 ? 13.625 6.661   22.528 1.00 11.54 ? 109 ASP   A O   1 
ATOM   827  C  CB  . ASP   A 1 103 ? 11.397 6.632   24.575 1.00 11.08 ? 109 ASP   A CB  1 
ATOM   828  C  CG  . ASP   A 1 103 ? 11.003 5.882   25.833 1.00 12.00 ? 109 ASP   A CG  1 
ATOM   829  O  OD1 . ASP   A 1 103 ? 11.882 5.243   26.423 1.00 12.00 ? 109 ASP   A OD1 1 
ATOM   830  O  OD2 . ASP   A 1 103 ? 9.788  5.925   26.212 1.00 11.85 ? 109 ASP   A OD2 1 
ATOM   831  N  N   . CYS   A 1 104 ? 13.549 8.876   23.011 1.00 10.22 ? 110 CYS   A N   1 
ATOM   832  C  CA  . CYS   A 1 104 ? 14.105 9.252   21.697 1.00 10.88 ? 110 CYS   A CA  1 
ATOM   833  C  C   . CYS   A 1 104 ? 15.432 8.554   21.472 1.00 11.22 ? 110 CYS   A C   1 
ATOM   834  O  O   . CYS   A 1 104 ? 16.276 8.463   22.394 1.00 11.83 ? 110 CYS   A O   1 
ATOM   835  C  CB  . CYS   A 1 104 ? 14.250 10.769  21.606 1.00 11.53 ? 110 CYS   A CB  1 
ATOM   836  S  SG  . CYS   A 1 104 ? 12.659 11.628  21.383 1.00 12.42 ? 110 CYS   A SG  1 
ATOM   837  N  N   . GLY   A 1 105 ? 15.600 8.020   20.280 1.00 10.68 ? 111 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 105 ? 16.822 7.322   19.898 1.00 11.16 ? 111 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 105 ? 16.666 5.801   19.847 1.00 11.18 ? 111 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 105 ? 17.540 5.124   19.302 1.00 11.58 ? 111 GLY   A O   1 
ATOM   841  N  N   . GLY   A 1 106 ? 15.589 5.276   20.441 1.00 10.66 ? 112 GLY   A N   1 
ATOM   842  C  CA  . GLY   A 1 106 ? 15.347 3.833   20.356 1.00 10.13 ? 112 GLY   A CA  1 
ATOM   843  C  C   . GLY   A 1 106 ? 15.119 3.402   18.900 1.00 10.38 ? 112 GLY   A C   1 
ATOM   844  O  O   . GLY   A 1 106 ? 14.436 4.109   18.129 1.00 10.14 ? 112 GLY   A O   1 
ATOM   845  N  N   . ILE   A 1 107 ? 15.641 2.238   18.507 1.00 9.62  ? 113 ILE   A N   1 
ATOM   846  C  CA  . ILE   A 1 107 ? 15.508 1.814   17.097 1.00 9.41  ? 113 ILE   A CA  1 
ATOM   847  C  C   . ILE   A 1 107 ? 14.182 1.143   16.802 1.00 9.66  ? 113 ILE   A C   1 
ATOM   848  O  O   . ILE   A 1 107 ? 13.693 0.351   17.601 1.00 10.39 ? 113 ILE   A O   1 
ATOM   849  C  CB  . ILE   A 1 107 ? 16.688 0.847   16.774 1.00 9.95  ? 113 ILE   A CB  1 
ATOM   850  C  CG1 . ILE   A 1 107 ? 17.958 1.703   16.525 1.00 11.45 ? 113 ILE   A CG1 1 
ATOM   851  C  CG2 . ILE   A 1 107 ? 16.420 -0.048  15.530 1.00 10.65 ? 113 ILE   A CG2 1 
ATOM   852  C  CD1 . ILE   A 1 107 ? 19.213 0.822   16.394 1.00 15.53 ? 113 ILE   A CD1 1 
ATOM   853  N  N   . LEU   A 1 108 ? 13.615 1.480   15.633 1.00 8.92  ? 114 LEU   A N   1 
ATOM   854  C  CA  . LEU   A 1 108 ? 12.501 0.752   15.035 1.00 8.80  ? 114 LEU   A CA  1 
ATOM   855  C  C   . LEU   A 1 108 ? 13.144 -0.094  13.904 1.00 9.16  ? 114 LEU   A C   1 
ATOM   856  O  O   . LEU   A 1 108 ? 13.904 0.439   13.066 1.00 10.16 ? 114 LEU   A O   1 
ATOM   857  C  CB  . LEU   A 1 108 ? 11.498 1.767   14.381 1.00 9.59  ? 114 LEU   A CB  1 
ATOM   858  C  CG  . LEU   A 1 108 ? 10.423 1.136   13.486 1.00 10.44 ? 114 LEU   A CG  1 
ATOM   859  C  CD1 . LEU   A 1 108 ? 9.448  0.339   14.355 1.00 10.99 ? 114 LEU   A CD1 1 
ATOM   860  C  CD2 . LEU   A 1 108 ? 9.641  2.239   12.696 1.00 12.12 ? 114 LEU   A CD2 1 
ATOM   861  N  N   . ARG   A 1 109 ? 12.823 -1.393  13.883 1.00 9.39  ? 115 ARG   A N   1 
ATOM   862  C  CA  . ARG   A 1 109 ? 13.390 -2.296  12.851 1.00 10.22 ? 115 ARG   A CA  1 
ATOM   863  C  C   . ARG   A 1 109 ? 12.332 -3.215  12.304 1.00 11.01 ? 115 ARG   A C   1 
ATOM   864  O  O   . ARG   A 1 109 ? 11.317 -3.494  12.942 1.00 11.32 ? 115 ARG   A O   1 
ATOM   865  C  CB  . ARG   A 1 109 ? 14.562 -3.128  13.446 1.00 11.59 ? 115 ARG   A CB  1 
ATOM   866  C  CG  . ARG   A 1 109 ? 14.110 -4.065  14.555 1.00 12.48 ? 115 ARG   A CG  1 
ATOM   867  C  CD  . ARG   A 1 109 ? 15.307 -4.807  15.115 1.00 12.81 ? 115 ARG   A CD  1 
ATOM   868  N  NE  . ARG   A 1 109 ? 16.091 -3.926  15.969 1.00 13.81 ? 115 ARG   A NE  1 
ATOM   869  C  CZ  . ARG   A 1 109 ? 17.402 -3.754  15.913 1.00 13.65 ? 115 ARG   A CZ  1 
ATOM   870  N  NH1 . ARG   A 1 109 ? 18.091 -4.160  14.847 1.00 15.33 ? 115 ARG   A NH1 1 
ATOM   871  N  NH2 . ARG   A 1 109 ? 18.008 -2.985  16.800 1.00 13.97 ? 115 ARG   A NH2 1 
ATOM   872  N  N   . CYS   A 1 110 ? 12.554 -3.652  11.083 1.00 12.03 ? 116 CYS   A N   1 
ATOM   873  C  CA  . CYS   A 1 110 ? 11.665 -4.599  10.390 1.00 14.44 ? 116 CYS   A CA  1 
ATOM   874  C  C   . CYS   A 1 110 ? 12.492 -5.816  9.982  1.00 16.42 ? 116 CYS   A C   1 
ATOM   875  O  O   . CYS   A 1 110 ? 13.689 -5.904  10.305 1.00 16.20 ? 116 CYS   A O   1 
ATOM   876  C  CB  . CYS   A 1 110 ? 10.996 -3.924  9.192  1.00 13.26 ? 116 CYS   A CB  1 
ATOM   877  S  SG  . CYS   A 1 110 ? 12.157 -3.573  7.831  1.00 13.93 ? 116 CYS   A SG  1 
ATOM   878  N  N   . GLN   A 1 111 ? 11.881 -6.771  9.220  1.00 18.26 ? 117 GLN   A N   1 
ATOM   879  C  CA  . GLN   A 1 111 ? 12.645 -7.911  8.741  1.00 20.44 ? 117 GLN   A CA  1 
ATOM   880  C  C   . GLN   A 1 111 ? 13.860 -7.538  7.868  1.00 20.82 ? 117 GLN   A C   1 
ATOM   881  O  O   . GLN   A 1 111 ? 14.782 -8.335  7.784  1.00 23.02 ? 117 GLN   A O   1 
ATOM   882  C  CB  . GLN   A 1 111 ? 11.737 -8.929  7.990  1.00 23.50 ? 117 GLN   A CB  1 
ATOM   883  C  CG  . GLN   A 1 111 ? 11.248 -8.376  6.646  1.00 28.68 ? 117 GLN   A CG  1 
ATOM   884  C  CD  . GLN   A 1 111 ? 10.302 -9.311  5.922  1.00 35.88 ? 117 GLN   A CD  1 
ATOM   885  O  OE1 . GLN   A 1 111 ? 9.073  -9.169  5.999  1.00 36.58 ? 117 GLN   A OE1 1 
ATOM   886  N  NE2 . GLN   A 1 111 ? 10.860 -10.246 5.174  1.00 36.14 ? 117 GLN   A NE2 1 
ATOM   887  N  N   . HIS   A 1 112 ? 13.887 -6.336  7.253  1.00 18.01 ? 118 HIS   A N   1 
ATOM   888  C  CA  . HIS   A 1 112 ? 14.988 -5.931  6.353  1.00 17.77 ? 118 HIS   A CA  1 
ATOM   889  C  C   . HIS   A 1 112 ? 16.131 -5.179  7.053  1.00 17.95 ? 118 HIS   A C   1 
ATOM   890  O  O   . HIS   A 1 112 ? 17.198 -4.978  6.468  1.00 19.83 ? 118 HIS   A O   1 
ATOM   891  C  CB  . HIS   A 1 112 ? 14.403 -5.056  5.235  1.00 17.34 ? 118 HIS   A CB  1 
ATOM   892  C  CG  . HIS   A 1 112 ? 13.279 -5.759  4.499  1.00 19.27 ? 118 HIS   A CG  1 
ATOM   893  N  ND1 . HIS   A 1 112 ? 11.955 -5.369  4.635  1.00 20.15 ? 118 HIS   A ND1 1 
ATOM   894  C  CD2 . HIS   A 1 112 ? 13.328 -6.812  3.631  1.00 23.11 ? 118 HIS   A CD2 1 
ATOM   895  C  CE1 . HIS   A 1 112 ? 11.237 -6.177  3.865  1.00 23.79 ? 118 HIS   A CE1 1 
ATOM   896  N  NE2 . HIS   A 1 112 ? 12.025 -7.054  3.222  1.00 24.89 ? 118 HIS   A NE2 1 
ATOM   897  N  N   . GLY   A 1 113 ? 15.895 -4.708  8.283  1.00 15.93 ? 119 GLY   A N   1 
ATOM   898  C  CA  . GLY   A 1 113 ? 16.929 -3.957  8.987  1.00 14.98 ? 119 GLY   A CA  1 
ATOM   899  C  C   . GLY   A 1 113 ? 16.331 -2.767  9.739  1.00 12.47 ? 119 GLY   A C   1 
ATOM   900  O  O   . GLY   A 1 113 ? 15.134 -2.767  10.066 1.00 12.42 ? 119 GLY   A O   1 
ATOM   901  N  N   . VAL   A 1 114 ? 17.176 -1.755  10.024 1.00 10.96 ? 120 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 114 ? 16.732 -0.559  10.767 1.00 11.28 ? 120 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 114 ? 15.903 0.378   9.906  1.00 10.32 ? 120 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 114 ? 16.311 0.711   8.793  1.00 11.34 ? 120 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 114 ? 17.963 0.172   11.375 1.00 12.20 ? 120 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 114 ? 17.560 1.509   12.022 1.00 13.04 ? 120 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 114 ? 18.714 -0.739  12.350 1.00 12.47 ? 120 VAL   A CG2 1 
ATOM   908  N  N   . VAL   A 1 115 ? 14.750 0.784   10.434 1.00 10.53 ? 121 VAL   A N   1 
ATOM   909  C  CA  . VAL   A 1 115 ? 13.814 1.637   9.727  1.00 10.35 ? 121 VAL   A CA  1 
ATOM   910  C  C   . VAL   A 1 115 ? 13.955 3.086   10.145 1.00 10.96 ? 121 VAL   A C   1 
ATOM   911  O  O   . VAL   A 1 115 ? 13.786 4.001   9.323  1.00 11.99 ? 121 VAL   A O   1 
ATOM   912  C  CB  . VAL   A 1 115 ? 12.354 1.132   10.001 1.00 11.50 ? 121 VAL   A CB  1 
ATOM   913  C  CG1 . VAL   A 1 115 ? 11.290 2.091   9.434  1.00 13.23 ? 121 VAL   A CG1 1 
ATOM   914  C  CG2 . VAL   A 1 115 ? 12.164 -0.268  9.430  1.00 12.35 ? 121 VAL   A CG2 1 
ATOM   915  N  N   . GLY   A 1 116 ? 14.158 3.323   11.447 1.00 10.75 ? 122 GLY   A N   1 
ATOM   916  C  CA  . GLY   A 1 116 ? 14.236 4.693   11.951 1.00 11.22 ? 122 GLY   A CA  1 
ATOM   917  C  C   . GLY   A 1 116 ? 14.415 4.697   13.445 1.00 10.20 ? 122 GLY   A C   1 
ATOM   918  O  O   . GLY   A 1 116 ? 14.760 3.662   14.023 1.00 10.08 ? 122 GLY   A O   1 
ATOM   919  N  N   . ILE   A 1 117 ? 14.309 5.897   14.065 1.00 10.20 ? 123 ILE   A N   1 
ATOM   920  C  CA  . ILE   A 1 117 ? 14.522 6.052   15.515 1.00 9.53  ? 123 ILE   A CA  1 
ATOM   921  C  C   . ILE   A 1 117 ? 13.379 6.801   16.139 1.00 9.72  ? 123 ILE   A C   1 
ATOM   922  O  O   . ILE   A 1 117 ? 12.777 7.690   15.494 1.00 9.67  ? 123 ILE   A O   1 
ATOM   923  C  CB  . ILE   A 1 117 ? 15.872 6.753   15.880 1.00 10.70 ? 123 ILE   A CB  1 
ATOM   924  C  CG1 . ILE   A 1 117 ? 16.009 8.067   15.121 1.00 12.54 ? 123 ILE   A CG1 1 
ATOM   925  C  CG2 . ILE   A 1 117 ? 17.034 5.789   15.667 1.00 12.39 ? 123 ILE   A CG2 1 
ATOM   926  C  CD1 . ILE   A 1 117 ? 17.291 8.859   15.629 1.00 13.15 ? 123 ILE   A CD1 1 
ATOM   927  N  N   . VAL   A 1 118 ? 13.080 6.513   17.401 1.00 9.62  ? 124 VAL   A N   1 
ATOM   928  C  CA  . VAL   A 1 118 ? 12.029 7.249   18.133 1.00 9.42  ? 124 VAL   A CA  1 
ATOM   929  C  C   . VAL   A 1 118 ? 12.350 8.750   18.148 1.00 9.43  ? 124 VAL   A C   1 
ATOM   930  O  O   . VAL   A 1 118 ? 13.511 9.109   18.443 1.00 10.01 ? 124 VAL   A O   1 
ATOM   931  C  CB  . VAL   A 1 118 ? 11.924 6.739   19.582 1.00 9.78  ? 124 VAL   A CB  1 
ATOM   932  C  CG1 . VAL   A 1 118 ? 10.949 7.581   20.399 1.00 10.10 ? 124 VAL   A CG1 1 
ATOM   933  C  CG2 . VAL   A 1 118 ? 11.485 5.263   19.609 1.00 10.28 ? 124 VAL   A CG2 1 
ATOM   934  N  N   . SER   A 1 119 ? 11.353 9.602   17.829 1.00 9.31  ? 125 SER   A N   1 
ATOM   935  C  CA  . SER   A 1 119 ? 11.533 11.063  17.762 1.00 10.16 ? 125 SER   A CA  1 
ATOM   936  C  C   . SER   A 1 119 ? 10.401 11.826  18.460 1.00 11.87 ? 125 SER   A C   1 
ATOM   937  O  O   . SER   A 1 119 ? 10.656 12.954  18.906 1.00 12.77 ? 125 SER   A O   1 
ATOM   938  C  CB  . SER   A 1 119 ? 11.701 11.492  16.303 1.00 11.49 ? 125 SER   A CB  1 
ATOM   939  O  OG  . SER   A 1 119 ? 11.779 12.901  16.127 1.00 12.52 ? 125 SER   A OG  1 
ATOM   940  N  N   . THR   A 1 120 ? 9.154  11.335  18.470 1.00 11.01 ? 126 THR   A N   1 
ATOM   941  C  CA  . THR   A 1 120 ? 8.022  12.112  19.032 1.00 11.42 ? 126 THR   A CA  1 
ATOM   942  C  C   . THR   A 1 120 ? 7.107  11.155  19.814 1.00 12.15 ? 126 THR   A C   1 
ATOM   943  O  O   . THR   A 1 120 ? 7.312  9.908   19.782 1.00 10.49 ? 126 THR   A O   1 
ATOM   944  C  CB  . THR   A 1 120 ? 7.185  12.788  17.906 1.00 11.38 ? 126 THR   A CB  1 
ATOM   945  O  OG1 . THR   A 1 120 ? 6.394  11.813  17.215 1.00 13.00 ? 126 THR   A OG1 1 
ATOM   946  C  CG2 . THR   A 1 120 ? 8.019  13.602  16.934 1.00 12.11 ? 126 THR   A CG2 1 
ATOM   947  N  N   . GLY   A 1 121 ? 6.084  11.694  20.493 1.00 12.52 ? 127 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 121 ? 5.116  10.824  21.125 1.00 13.34 ? 127 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 121 ? 4.253  11.534  22.133 1.00 13.82 ? 127 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 121 ? 4.269  12.768  22.235 1.00 14.62 ? 127 GLY   A O   1 
ATOM   951  N  N   . GLY   A 1 122 ? 3.537  10.705  22.897 1.00 13.83 ? 128 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 122 ? 2.674  11.113  24.006 1.00 14.60 ? 128 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 122 ? 1.321  10.432  23.924 1.00 15.22 ? 128 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 122 ? 0.852  10.083  22.826 1.00 15.14 ? 128 GLY   A O   1 
ATOM   955  N  N   . ASN   A 1 123 ? 0.658  10.295  25.074 1.00 14.40 ? 129 ASN   A N   1 
ATOM   956  C  CA  . ASN   A 1 123 ? -0.716 9.742   25.148 1.00 14.34 ? 129 ASN   A CA  1 
ATOM   957  C  C   . ASN   A 1 123 ? -0.895 8.433   24.397 1.00 14.24 ? 129 ASN   A C   1 
ATOM   958  O  O   . ASN   A 1 123 ? -1.961 8.187   23.818 1.00 15.39 ? 129 ASN   A O   1 
ATOM   959  C  CB  . ASN   A 1 123 ? -1.713 10.812  24.653 1.00 15.43 ? 129 ASN   A CB  1 
ATOM   960  C  CG  . ASN   A 1 123 ? -1.678 12.049  25.501 1.00 18.46 ? 129 ASN   A CG  1 
ATOM   961  O  OD1 . ASN   A 1 123 ? -1.910 11.973  26.715 1.00 19.93 ? 129 ASN   A OD1 1 
ATOM   962  N  ND2 . ASN   A 1 123 ? -1.367 13.190  24.885 1.00 19.61 ? 129 ASN   A ND2 1 
ATOM   963  N  N   . GLY   A 1 124 ? 0.077  7.545   24.530 1.00 12.93 ? 130 GLY   A N   1 
ATOM   964  C  CA  . GLY   A 1 124 ? -0.025 6.240   23.907 1.00 11.86 ? 130 GLY   A CA  1 
ATOM   965  C  C   . GLY   A 1 124 ? 0.331  6.229   22.450 1.00 11.40 ? 130 GLY   A C   1 
ATOM   966  O  O   . GLY   A 1 124 ? 0.146  5.175   21.847 1.00 12.74 ? 130 GLY   A O   1 
ATOM   967  N  N   . LEU   A 1 125 ? 0.920  7.297   21.923 1.00 11.65 ? 131 LEU   A N   1 
ATOM   968  C  CA  . LEU   A 1 125 ? 1.464  7.285   20.572 1.00 11.81 ? 131 LEU   A CA  1 
ATOM   969  C  C   . LEU   A 1 125 ? 3.000  7.372   20.640 1.00 12.15 ? 131 LEU   A C   1 
ATOM   970  O  O   . LEU   A 1 125 ? 3.586  7.882   21.627 1.00 12.68 ? 131 LEU   A O   1 
ATOM   971  C  CB  . LEU   A 1 125 ? 0.946  8.490   19.790 1.00 12.01 ? 131 LEU   A CB  1 
ATOM   972  C  CG  . LEU   A 1 125 ? -0.544 8.450   19.501 1.00 13.87 ? 131 LEU   A CG  1 
ATOM   973  C  CD1 . LEU   A 1 125 ? -1.078 9.847   19.180 1.00 16.90 ? 131 LEU   A CD1 1 
ATOM   974  C  CD2 . LEU   A 1 125 ? -0.913 7.367   18.429 1.00 14.75 ? 131 LEU   A CD2 1 
ATOM   975  N  N   . VAL   A 1 126 ? 3.656  6.867   19.583 1.00 10.71 ? 132 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 126 ? 5.114  7.021   19.460 1.00 10.84 ? 132 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 126 ? 5.370  7.366   17.948 1.00 10.63 ? 132 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 126 ? 4.731  6.765   17.078 1.00 10.98 ? 132 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 126 ? 5.847  5.762   19.951 1.00 11.01 ? 132 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 126 ? 5.351  4.514   19.230 1.00 11.97 ? 132 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 126 ? 7.361  5.941   19.774 1.00 11.97 ? 132 VAL   A CG2 1 
ATOM   982  N  N   . GLY   A 1 127 ? 6.234  8.325   17.666 1.00 10.40 ? 133 GLY   A N   1 
ATOM   983  C  CA  . GLY   A 1 127 ? 6.568  8.683   16.298 1.00 10.45 ? 133 GLY   A CA  1 
ATOM   984  C  C   . GLY   A 1 127 ? 8.031  8.396   16.040 1.00 10.74 ? 133 GLY   A C   1 
ATOM   985  O  O   . GLY   A 1 127 ? 8.895  8.586   16.916 1.00 11.01 ? 133 GLY   A O   1 
ATOM   986  N  N   . PHE   A 1 128 ? 8.324  7.963   14.807 1.00 9.70  ? 134 PHE   A N   1 
ATOM   987  C  CA  . PHE   A 1 128 ? 9.687  7.569   14.406 1.00 9.45  ? 134 PHE   A CA  1 
ATOM   988  C  C   . PHE   A 1 128 ? 10.137 8.364   13.208 1.00 10.38 ? 134 PHE   A C   1 
ATOM   989  O  O   . PHE   A 1 128 ? 9.380  8.521   12.241 1.00 10.92 ? 134 PHE   A O   1 
ATOM   990  C  CB  . PHE   A 1 128 ? 9.675  6.072   13.983 1.00 9.93  ? 134 PHE   A CB  1 
ATOM   991  C  CG  . PHE   A 1 128 ? 9.042  5.144   15.018 1.00 10.10 ? 134 PHE   A CG  1 
ATOM   992  C  CD1 . PHE   A 1 128 ? 9.793  4.652   16.093 1.00 10.16 ? 134 PHE   A CD1 1 
ATOM   993  C  CD2 . PHE   A 1 128 ? 7.733  4.714   14.873 1.00 12.06 ? 134 PHE   A CD2 1 
ATOM   994  C  CE1 . PHE   A 1 128 ? 9.236  3.773   17.024 1.00 10.19 ? 134 PHE   A CE1 1 
ATOM   995  C  CE2 . PHE   A 1 128 ? 7.180  3.844   15.823 1.00 11.69 ? 134 PHE   A CE2 1 
ATOM   996  C  CZ  . PHE   A 1 128 ? 7.942  3.380   16.874 1.00 10.87 ? 134 PHE   A CZ  1 
ATOM   997  N  N   . ALA   A 1 129 ? 11.385 8.851   13.284 1.00 9.87  ? 135 ALA   A N   1 
ATOM   998  C  CA  . ALA   A 1 129 ? 12.009 9.556   12.148 1.00 10.50 ? 135 ALA   A CA  1 
ATOM   999  C  C   . ALA   A 1 129 ? 12.529 8.477   11.162 1.00 10.10 ? 135 ALA   A C   1 
ATOM   1000 O  O   . ALA   A 1 129 ? 13.384 7.671   11.533 1.00 10.28 ? 135 ALA   A O   1 
ATOM   1001 C  CB  . ALA   A 1 129 ? 13.143 10.420  12.698 1.00 10.52 ? 135 ALA   A CB  1 
ATOM   1002 N  N   . ASP   A 1 130 ? 11.982 8.412   9.949  1.00 10.55 ? 136 ASP   A N   1 
ATOM   1003 C  CA  . ASP   A 1 130 ? 12.424 7.412   8.959  1.00 11.14 ? 136 ASP   A CA  1 
ATOM   1004 C  C   . ASP   A 1 130 ? 13.852 7.716   8.462  1.00 11.45 ? 136 ASP   A C   1 
ATOM   1005 O  O   . ASP   A 1 130 ? 14.230 8.900   8.310  1.00 12.08 ? 136 ASP   A O   1 
ATOM   1006 C  CB  . ASP   A 1 130 ? 11.471 7.474   7.734  1.00 12.66 ? 136 ASP   A CB  1 
ATOM   1007 C  CG  . ASP   A 1 130 ? 11.721 6.439   6.675  1.00 19.51 ? 136 ASP   A CG  1 
ATOM   1008 O  OD1 . ASP   A 1 130 ? 11.835 5.261   7.027  1.00 15.89 ? 136 ASP   A OD1 1 
ATOM   1009 O  OD2 . ASP   A 1 130 ? 11.917 6.830   5.483  1.00 24.56 ? 136 ASP   A OD2 1 
ATOM   1010 N  N   . VAL   A 1 131 ? 14.618 6.645   8.206  1.00 10.81 ? 137 VAL   A N   1 
ATOM   1011 C  CA  . VAL   A 1 131 ? 15.936 6.776   7.583  1.00 10.31 ? 137 VAL   A CA  1 
ATOM   1012 C  C   . VAL   A 1 131 ? 16.041 5.944   6.292  1.00 11.53 ? 137 VAL   A C   1 
ATOM   1013 O  O   . VAL   A 1 131 ? 17.106 5.953   5.672  1.00 11.32 ? 137 VAL   A O   1 
ATOM   1014 C  CB  . VAL   A 1 131 ? 17.109 6.445   8.510  1.00 11.42 ? 137 VAL   A CB  1 
ATOM   1015 C  CG1 . VAL   A 1 131 ? 17.147 7.365   9.744  1.00 12.19 ? 137 VAL   A CG1 1 
ATOM   1016 C  CG2 . VAL   A 1 131 ? 17.114 4.978   8.922  1.00 11.56 ? 137 VAL   A CG2 1 
ATOM   1017 N  N   . ARG   A 1 132 ? 14.972 5.251   5.856  1.00 11.97 ? 138 ARG   A N   1 
ATOM   1018 C  CA  . ARG   A 1 132 ? 15.059 4.358   4.702  1.00 12.21 ? 138 ARG   A CA  1 
ATOM   1019 C  C   . ARG   A 1 132 ? 15.309 5.057   3.397  1.00 13.01 ? 138 ARG   A C   1 
ATOM   1020 O  O   . ARG   A 1 132 ? 15.786 4.404   2.430  1.00 13.01 ? 138 ARG   A O   1 
ATOM   1021 C  CB  . ARG   A 1 132 ? 13.792 3.488   4.613  1.00 11.61 ? 138 ARG   A CB  1 
ATOM   1022 C  CG  . ARG   A 1 132 ? 13.648 2.524   5.808  1.00 11.90 ? 138 ARG   A CG  1 
ATOM   1023 C  CD  . ARG   A 1 132 ? 12.343 1.752   5.633  1.00 12.87 ? 138 ARG   A CD  1 
ATOM   1024 N  NE  . ARG   A 1 132 ? 11.201 2.657   5.870  1.00 12.14 ? 138 ARG   A NE  1 
ATOM   1025 C  CZ  . ARG   A 1 132 ? 9.937  2.258   5.991  1.00 14.43 ? 138 ARG   A CZ  1 
ATOM   1026 N  NH1 . ARG   A 1 132 ? 9.605  0.994   5.734  1.00 15.38 ? 138 ARG   A NH1 1 
ATOM   1027 N  NH2 . ARG   A 1 132 ? 8.982  3.140   6.284  1.00 14.93 ? 138 ARG   A NH2 1 
ATOM   1028 N  N   . ASP   A 1 133 ? 15.002 6.368   3.297  1.00 12.49 ? 139 ASP   A N   1 
ATOM   1029 C  CA  . ASP   A 1 133 ? 15.272 7.092   2.059  1.00 13.51 ? 139 ASP   A CA  1 
ATOM   1030 C  C   . ASP   A 1 133 ? 16.708 7.632   1.958  1.00 13.44 ? 139 ASP   A C   1 
ATOM   1031 O  O   . ASP   A 1 133 ? 17.083 8.118   0.883  1.00 15.04 ? 139 ASP   A O   1 
ATOM   1032 C  CB  . ASP   A 1 133 ? 14.281 8.261   1.937  1.00 15.55 ? 139 ASP   A CB  1 
ATOM   1033 C  CG  . ASP   A 1 133 ? 14.530 9.322   2.999  1.00 18.68 ? 139 ASP   A CG  1 
ATOM   1034 O  OD1 . ASP   A 1 133 ? 14.630 8.958   4.197  1.00 16.97 ? 139 ASP   A OD1 1 
ATOM   1035 O  OD2 . ASP   A 1 133 ? 14.569 10.522  2.649  1.00 20.62 ? 139 ASP   A OD2 1 
ATOM   1036 N  N   . LEU   A 1 134 ? 17.513 7.546   3.022  1.00 12.09 ? 140 LEU   A N   1 
ATOM   1037 C  CA  . LEU   A 1 134 ? 18.897 8.080   3.043  1.00 12.23 ? 140 LEU   A CA  1 
ATOM   1038 C  C   . LEU   A 1 134 ? 19.823 7.028   2.502  1.00 12.47 ? 140 LEU   A C   1 
ATOM   1039 O  O   . LEU   A 1 134 ? 20.522 6.329   3.246  1.00 12.73 ? 140 LEU   A O   1 
ATOM   1040 C  CB  . LEU   A 1 134 ? 19.267 8.472   4.497  1.00 12.12 ? 140 LEU   A CB  1 
ATOM   1041 C  CG  . LEU   A 1 134 ? 18.294 9.472   5.135  1.00 14.12 ? 140 LEU   A CG  1 
ATOM   1042 C  CD1 . LEU   A 1 134 ? 18.677 9.730   6.597  1.00 15.58 ? 140 LEU   A CD1 1 
ATOM   1043 C  CD2 . LEU   A 1 134 ? 18.276 10.782  4.399  1.00 16.79 ? 140 LEU   A CD2 1 
ATOM   1044 N  N   . LEU   A 1 135 ? 19.839 6.894   1.174  1.00 12.65 ? 141 LEU   A N   1 
ATOM   1045 C  CA  . LEU   A 1 135 ? 20.578 5.804   0.529  1.00 13.64 ? 141 LEU   A CA  1 
ATOM   1046 C  C   . LEU   A 1 135 ? 22.080 5.907   0.711  1.00 14.19 ? 141 LEU   A C   1 
ATOM   1047 O  O   . LEU   A 1 135 ? 22.756 4.876   0.770  1.00 14.35 ? 141 LEU   A O   1 
ATOM   1048 C  CB  . LEU   A 1 135 ? 20.213 5.701   -0.974 1.00 14.41 ? 141 LEU   A CB  1 
ATOM   1049 C  CG  . LEU   A 1 135 ? 18.715 5.668   -1.313 1.00 16.07 ? 141 LEU   A CG  1 
ATOM   1050 C  CD1 . LEU   A 1 135 ? 18.558 5.371   -2.812 1.00 16.88 ? 141 LEU   A CD1 1 
ATOM   1051 C  CD2 . LEU   A 1 135 ? 17.932 4.642   -0.494 1.00 16.48 ? 141 LEU   A CD2 1 
ATOM   1052 N  N   . TRP   A 1 136 ? 22.581 7.134   0.890  1.00 12.83 ? 142 TRP   A N   1 
ATOM   1053 C  CA  . TRP   A 1 136 ? 24.001 7.384   1.066  1.00 12.98 ? 142 TRP   A CA  1 
ATOM   1054 C  C   . TRP   A 1 136 ? 24.551 6.782   2.369  1.00 13.87 ? 142 TRP   A C   1 
ATOM   1055 O  O   . TRP   A 1 136 ? 25.776 6.643   2.504  1.00 15.10 ? 142 TRP   A O   1 
ATOM   1056 C  CB  . TRP   A 1 136 ? 24.289 8.903   0.947  1.00 12.71 ? 142 TRP   A CB  1 
ATOM   1057 C  CG  . TRP   A 1 136 ? 23.468 9.742   1.892  1.00 12.90 ? 142 TRP   A CG  1 
ATOM   1058 C  CD1 . TRP   A 1 136 ? 22.316 10.404  1.593  1.00 14.29 ? 142 TRP   A CD1 1 
ATOM   1059 C  CD2 . TRP   A 1 136 ? 23.783 10.073  3.260  1.00 13.25 ? 142 TRP   A CD2 1 
ATOM   1060 N  NE1 . TRP   A 1 136 ? 21.852 11.071  2.704  1.00 14.95 ? 142 TRP   A NE1 1 
ATOM   1061 C  CE2 . TRP   A 1 136 ? 22.756 10.911  3.730  1.00 13.97 ? 142 TRP   A CE2 1 
ATOM   1062 C  CE3 . TRP   A 1 136 ? 24.836 9.744   4.127  1.00 13.65 ? 142 TRP   A CE3 1 
ATOM   1063 C  CZ2 . TRP   A 1 136 ? 22.751 11.422  5.034  1.00 15.12 ? 142 TRP   A CZ2 1 
ATOM   1064 C  CZ3 . TRP   A 1 136 ? 24.846 10.279  5.406  1.00 15.67 ? 142 TRP   A CZ3 1 
ATOM   1065 C  CH2 . TRP   A 1 136 ? 23.818 11.112  5.837  1.00 15.30 ? 142 TRP   A CH2 1 
ATOM   1066 N  N   . LEU   A 1 137 ? 23.670 6.429   3.353  1.00 12.32 ? 143 LEU   A N   1 
ATOM   1067 C  CA  . LEU   A 1 137 ? 24.165 5.755   4.561  1.00 14.45 ? 143 LEU   A CA  1 
ATOM   1068 C  C   . LEU   A 1 137 ? 24.845 4.419   4.245  1.00 16.26 ? 143 LEU   A C   1 
ATOM   1069 O  O   . LEU   A 1 137 ? 25.688 3.968   5.053  1.00 16.20 ? 143 LEU   A O   1 
ATOM   1070 C  CB  . LEU   A 1 137 ? 23.022 5.508   5.563  1.00 14.10 ? 143 LEU   A CB  1 
ATOM   1071 C  CG  . LEU   A 1 137 ? 22.488 6.759   6.256  1.00 13.42 ? 143 LEU   A CG  1 
ATOM   1072 C  CD1 . LEU   A 1 137 ? 21.211 6.407   7.045  1.00 14.65 ? 143 LEU   A CD1 1 
ATOM   1073 C  CD2 . LEU   A 1 137 ? 23.574 7.389   7.224  1.00 14.05 ? 143 LEU   A CD2 1 
ATOM   1074 N  N   . ASP   A 1 138 ? 24.544 3.818   3.064  1.00 18.11 ? 144 ASP   A N   1 
ATOM   1075 C  CA  . ASP   A 1 138 ? 25.079 2.497   2.669  1.00 21.33 ? 144 ASP   A CA  1 
ATOM   1076 C  C   . ASP   A 1 138 ? 26.433 2.563   1.967  1.00 25.32 ? 144 ASP   A C   1 
ATOM   1077 O  O   . ASP   A 1 138 ? 26.995 1.512   1.637  1.00 26.19 ? 144 ASP   A O   1 
ATOM   1078 C  CB  . ASP   A 1 138 ? 24.086 1.752   1.718  1.00 21.88 ? 144 ASP   A CB  1 
ATOM   1079 C  CG  . ASP   A 1 138 ? 22.745 1.395   2.302  1.00 27.27 ? 144 ASP   A CG  1 
ATOM   1080 O  OD1 . ASP   A 1 138 ? 22.608 1.450   3.524  1.00 29.30 ? 144 ASP   A OD1 1 
ATOM   1081 O  OD2 . ASP   A 1 138 ? 21.807 1.055   1.515  1.00 32.97 ? 144 ASP   A OD2 1 
ATOM   1082 N  N   . GLU   A 1 139 ? 26.962 3.775   1.705  1.00 27.23 ? 145 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 139 ? 28.223 3.892   0.967  1.00 30.94 ? 145 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 139 ? 29.207 4.880   1.603  1.00 33.03 ? 145 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 139 ? 28.864 5.576   2.552  1.00 32.12 ? 145 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 139 ? 27.892 4.308   -0.473 1.00 35.24 ? 145 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 139 ? 27.288 5.698   -0.532 1.00 42.31 ? 145 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 139 ? 26.477 6.017   -1.773 1.00 50.87 ? 145 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 139 ? 26.185 7.216   -1.997 1.00 50.68 ? 145 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 139 ? 26.135 5.071   -2.522 1.00 54.83 ? 145 GLU   A OE2 1 
ATOM   1091 N  N   . GLU   A 1 140 ? 30.428 4.950   1.043  1.00 35.89 ? 146 GLU   A N   1 
ATOM   1092 C  CA  . GLU   A 1 140 ? 31.523 5.841   1.419  1.00 39.52 ? 146 GLU   A CA  1 
ATOM   1093 C  C   . GLU   A 1 140 ? 32.201 5.374   2.690  1.00 41.91 ? 146 GLU   A C   1 
ATOM   1094 O  O   . GLU   A 1 140 ? 33.431 5.238   2.693  1.00 43.22 ? 146 GLU   A O   1 
ATOM   1095 C  CB  . GLU   A 1 140 ? 31.085 7.319   1.468  1.00 42.89 ? 146 GLU   A CB  1 
ATOM   1096 C  CG  . GLU   A 1 140 ? 32.010 8.262   2.225  1.00 49.44 ? 146 GLU   A CG  1 
ATOM   1097 C  CD  . GLU   A 1 140 ? 32.799 9.223   1.354  1.00 57.95 ? 146 GLU   A CD  1 
ATOM   1098 O  OE1 . GLU   A 1 140 ? 32.223 10.249  0.923  1.00 60.57 ? 146 GLU   A OE1 1 
ATOM   1099 O  OE2 . GLU   A 1 140 ? 33.997 8.953   1.111  1.00 59.38 ? 146 GLU   A OE2 1 
ATOM   1100 N  N   . SER   B 1 1   ? 21.981 -21.245 7.739  1.00 16.45 ? 7   SER   C N   1 
ATOM   1101 C  CA  . SER   B 1 1   ? 20.846 -21.075 8.678  1.00 16.08 ? 7   SER   C CA  1 
ATOM   1102 C  C   . SER   B 1 1   ? 20.833 -22.157 9.750  1.00 16.20 ? 7   SER   C C   1 
ATOM   1103 O  O   . SER   B 1 1   ? 21.494 -23.200 9.616  1.00 17.32 ? 7   SER   C O   1 
ATOM   1104 C  CB  . SER   B 1 1   ? 19.521 -21.076 7.908  1.00 19.25 ? 7   SER   C CB  1 
ATOM   1105 O  OG  . SER   B 1 1   ? 19.338 -22.357 7.332  1.00 23.09 ? 7   SER   C OG  1 
ATOM   1106 N  N   . GLY   B 1 2   ? 20.071 -21.919 10.835 1.00 14.74 ? 8   GLY   C N   1 
ATOM   1107 C  CA  . GLY   B 1 2   ? 19.934 -22.924 11.882 1.00 14.56 ? 8   GLY   C CA  1 
ATOM   1108 C  C   . GLY   B 1 2   ? 19.675 -22.324 13.248 1.00 13.51 ? 8   GLY   C C   1 
ATOM   1109 O  O   . GLY   B 1 2   ? 20.037 -21.183 13.494 1.00 13.86 ? 8   GLY   C O   1 
ATOM   1110 N  N   . ALA   B 1 3   ? 19.018 -23.069 14.128 1.00 12.98 ? 9   ALA   C N   1 
ATOM   1111 C  CA  . ALA   B 1 3   ? 18.691 -22.587 15.463 1.00 12.91 ? 9   ALA   C CA  1 
ATOM   1112 C  C   . ALA   B 1 3   ? 18.817 -23.704 16.474 1.00 11.74 ? 9   ALA   C C   1 
ATOM   1113 O  O   . ALA   B 1 3   ? 18.877 -24.905 16.110 1.00 12.53 ? 9   ALA   C O   1 
ATOM   1114 C  CB  . ALA   B 1 3   ? 17.255 -22.044 15.469 1.00 14.77 ? 9   ALA   C CB  1 
ATOM   1115 N  N   . ILE   B 1 4   ? 18.873 -23.328 17.771 1.00 11.14 ? 10  ILE   C N   1 
ATOM   1116 C  CA  . ILE   B 1 4   ? 18.784 -24.288 18.910 1.00 10.46 ? 10  ILE   C CA  1 
ATOM   1117 C  C   . ILE   B 1 4   ? 17.388 -24.105 19.530 1.00 11.20 ? 10  ILE   C C   1 
ATOM   1118 O  O   . ILE   B 1 4   ? 16.937 -22.949 19.703 1.00 12.11 ? 10  ILE   C O   1 
ATOM   1119 C  CB  . ILE   B 1 4   ? 19.825 -23.966 19.978 1.00 10.99 ? 10  ILE   C CB  1 
ATOM   1120 C  CG1 . ILE   B 1 4   ? 21.242 -23.836 19.361 1.00 11.76 ? 10  ILE   C CG1 1 
ATOM   1121 C  CG2 . ILE   B 1 4   ? 19.790 -25.076 21.082 1.00 13.69 ? 10  ILE   C CG2 1 
ATOM   1122 C  CD1 . ILE   B 1 4   ? 22.287 -23.228 20.399 1.00 13.12 ? 10  ILE   C CD1 1 
ATOM   1123 N  N   . TYR   B 1 5   ? 16.693 -25.214 19.785 1.00 11.02 ? 11  TYR   C N   1 
ATOM   1124 C  CA  . TYR   B 1 5   ? 15.354 -25.161 20.389 1.00 12.40 ? 11  TYR   C CA  1 
ATOM   1125 C  C   . TYR   B 1 5   ? 15.458 -25.839 21.760 1.00 13.16 ? 11  TYR   C C   1 
ATOM   1126 O  O   . TYR   B 1 5   ? 15.495 -27.070 21.830 1.00 14.63 ? 11  TYR   C O   1 
ATOM   1127 C  CB  . TYR   B 1 5   ? 14.284 -25.833 19.476 1.00 13.41 ? 11  TYR   C CB  1 
ATOM   1128 C  CG  . TYR   B 1 5   ? 14.106 -25.067 18.182 1.00 14.39 ? 11  TYR   C CG  1 
ATOM   1129 C  CD1 . TYR   B 1 5   ? 13.264 -23.956 18.113 1.00 14.34 ? 11  TYR   C CD1 1 
ATOM   1130 C  CD2 . TYR   B 1 5   ? 14.802 -25.429 17.035 1.00 14.76 ? 11  TYR   C CD2 1 
ATOM   1131 C  CE1 . TYR   B 1 5   ? 13.135 -23.228 16.942 1.00 14.93 ? 11  TYR   C CE1 1 
ATOM   1132 C  CE2 . TYR   B 1 5   ? 14.671 -24.711 15.852 1.00 16.38 ? 11  TYR   C CE2 1 
ATOM   1133 C  CZ  . TYR   B 1 5   ? 13.844 -23.608 15.814 1.00 16.74 ? 11  TYR   C CZ  1 
ATOM   1134 O  OH  . TYR   B 1 5   ? 13.741 -22.863 14.650 1.00 18.44 ? 11  TYR   C OH  1 
ATOM   1135 N  N   . VAL   B 1 6   ? 15.472 -25.084 22.849 1.00 13.33 ? 12  VAL   C N   1 
ATOM   1136 C  CA  . VAL   B 1 6   ? 15.584 -25.625 24.203 1.00 14.20 ? 12  VAL   C CA  1 
ATOM   1137 C  C   . VAL   B 1 6   ? 14.471 -25.006 25.057 1.00 14.65 ? 12  VAL   C C   1 
ATOM   1138 O  O   . VAL   B 1 6   ? 14.283 -23.790 25.047 1.00 13.76 ? 12  VAL   C O   1 
ATOM   1139 C  CB  . VAL   B 1 6   ? 17.001 -25.333 24.789 1.00 15.18 ? 12  VAL   C CB  1 
ATOM   1140 C  CG1 . VAL   B 1 6   ? 17.359 -23.838 24.698 1.00 15.91 ? 12  VAL   C CG1 1 
ATOM   1141 C  CG2 . VAL   B 1 6   ? 17.086 -25.845 26.228 1.00 17.14 ? 12  VAL   C CG2 1 
ATOM   1142 N  N   . GLY   B 1 7   ? 13.654 -25.826 25.742 1.00 15.39 ? 13  GLY   C N   1 
ATOM   1143 C  CA  . GLY   B 1 7   ? 12.535 -25.297 26.533 1.00 15.45 ? 13  GLY   C CA  1 
ATOM   1144 C  C   . GLY   B 1 7   ? 11.601 -24.469 25.670 1.00 15.77 ? 13  GLY   C C   1 
ATOM   1145 O  O   . GLY   B 1 7   ? 11.305 -24.858 24.534 1.00 16.44 ? 13  GLY   C O   1 
ATOM   1146 N  N   . ASN   B 1 8   ? 11.258 -23.275 26.112 1.00 14.95 ? 14  ASN   C N   1 
ATOM   1147 C  CA  . ASN   B 1 8   ? 10.458 -22.374 25.287 1.00 15.43 ? 14  ASN   C CA  1 
ATOM   1148 C  C   . ASN   B 1 8   ? 11.321 -21.252 24.706 1.00 14.03 ? 14  ASN   C C   1 
ATOM   1149 O  O   . ASN   B 1 8   ? 10.854 -20.133 24.531 1.00 14.18 ? 14  ASN   C O   1 
ATOM   1150 C  CB  . ASN   B 1 8   ? 9.219  -21.827 26.036 1.00 17.60 ? 14  ASN   C CB  1 
ATOM   1151 C  CG  . ASN   B 1 8   ? 8.127  -22.884 26.189 1.00 24.65 ? 14  ASN   C CG  1 
ATOM   1152 O  OD1 . ASN   B 1 8   ? 7.236  -23.018 25.340 1.00 26.50 ? 14  ASN   C OD1 1 
ATOM   1153 N  ND2 . ASN   B 1 8   ? 8.236  -23.682 27.229 1.00 26.64 ? 14  ASN   C ND2 1 
ATOM   1154 N  N   . TYR   B 1 9   ? 12.540 -21.597 24.312 1.00 12.84 ? 15  TYR   C N   1 
ATOM   1155 C  CA  . TYR   B 1 9   ? 13.496 -20.652 23.703 1.00 12.75 ? 15  TYR   C CA  1 
ATOM   1156 C  C   . TYR   B 1 9   ? 13.966 -21.117 22.313 1.00 11.44 ? 15  TYR   C C   1 
ATOM   1157 O  O   . TYR   B 1 9   ? 14.139 -22.336 22.089 1.00 11.94 ? 15  TYR   C O   1 
ATOM   1158 C  CB  . TYR   B 1 9   ? 14.749 -20.488 24.591 1.00 12.61 ? 15  TYR   C CB  1 
ATOM   1159 C  CG  . TYR   B 1 9   ? 14.450 -19.985 25.991 1.00 13.36 ? 15  TYR   C CG  1 
ATOM   1160 C  CD1 . TYR   B 1 9   ? 13.884 -18.735 26.192 1.00 15.39 ? 15  TYR   C CD1 1 
ATOM   1161 C  CD2 . TYR   B 1 9   ? 14.788 -20.741 27.105 1.00 16.24 ? 15  TYR   C CD2 1 
ATOM   1162 C  CE1 . TYR   B 1 9   ? 13.626 -18.264 27.483 1.00 17.29 ? 15  TYR   C CE1 1 
ATOM   1163 C  CE2 . TYR   B 1 9   ? 14.553 -20.273 28.395 1.00 18.94 ? 15  TYR   C CE2 1 
ATOM   1164 C  CZ  . TYR   B 1 9   ? 14.012 -19.019 28.572 1.00 20.83 ? 15  TYR   C CZ  1 
ATOM   1165 O  OH  . TYR   B 1 9   ? 13.760 -18.595 29.863 1.00 25.61 ? 15  TYR   C OH  1 
ATOM   1166 N  N   . ARG   B 1 10  ? 14.204 -20.168 21.430 1.00 11.28 ? 16  ARG   C N   1 
ATOM   1167 C  CA  . ARG   B 1 10  ? 14.801 -20.392 20.103 1.00 11.43 ? 16  ARG   C CA  1 
ATOM   1168 C  C   . ARG   B 1 10  ? 16.076 -19.498 20.079 1.00 11.58 ? 16  ARG   C C   1 
ATOM   1169 O  O   . ARG   B 1 10  ? 15.994 -18.275 20.307 1.00 11.46 ? 16  ARG   C O   1 
ATOM   1170 C  CB  . ARG   B 1 10  ? 13.824 -19.922 18.987 1.00 12.37 ? 16  ARG   C CB  1 
ATOM   1171 C  CG  . ARG   B 1 10  ? 14.469 -19.757 17.578 1.00 13.01 ? 16  ARG   C CG  1 
ATOM   1172 C  CD  . ARG   B 1 10  ? 13.390 -19.465 16.523 1.00 14.23 ? 16  ARG   C CD  1 
ATOM   1173 N  NE  . ARG   B 1 10  ? 13.800 -18.504 15.500 1.00 14.50 ? 16  ARG   C NE  1 
ATOM   1174 C  CZ  . ARG   B 1 10  ? 14.300 -18.822 14.304 1.00 15.30 ? 16  ARG   C CZ  1 
ATOM   1175 N  NH1 . ARG   B 1 10  ? 14.524 -20.099 13.981 1.00 15.83 ? 16  ARG   C NH1 1 
ATOM   1176 N  NH2 . ARG   B 1 10  ? 14.612 -17.867 13.434 1.00 16.60 ? 16  ARG   C NH2 1 
ATOM   1177 N  N   . VAL   B 1 11  ? 17.246 -20.101 19.872 1.00 12.13 ? 17  VAL   C N   1 
ATOM   1178 C  CA  . VAL   B 1 11  ? 18.536 -19.390 19.817 1.00 10.69 ? 17  VAL   C CA  1 
ATOM   1179 C  C   . VAL   B 1 11  ? 19.002 -19.334 18.387 1.00 10.87 ? 17  VAL   C C   1 
ATOM   1180 O  O   . VAL   B 1 11  ? 19.150 -20.400 17.735 1.00 11.88 ? 17  VAL   C O   1 
ATOM   1181 C  CB  . VAL   B 1 11  ? 19.607 -20.127 20.669 1.00 11.25 ? 17  VAL   C CB  1 
ATOM   1182 C  CG1 . VAL   B 1 11  ? 20.877 -19.270 20.761 1.00 13.45 ? 17  VAL   C CG1 1 
ATOM   1183 C  CG2 . VAL   B 1 11  ? 19.055 -20.478 22.061 1.00 13.30 ? 17  VAL   C CG2 1 
ATOM   1184 N  N   . VAL   B 1 12  ? 19.249 -18.116 17.858 1.00 10.51 ? 18  VAL   C N   1 
ATOM   1185 C  CA  A VAL   B 1 12  ? 19.689 -17.961 16.459 0.50 10.10 ? 18  VAL   C CA  1 
ATOM   1186 C  CA  B VAL   B 1 12  ? 19.656 -17.972 16.456 0.50 11.57 ? 18  VAL   C CA  1 
ATOM   1187 C  C   . VAL   B 1 12  ? 20.827 -16.956 16.383 1.00 10.73 ? 18  VAL   C C   1 
ATOM   1188 O  O   . VAL   B 1 12  ? 21.077 -16.186 17.341 1.00 10.93 ? 18  VAL   C O   1 
ATOM   1189 C  CB  A VAL   B 1 12  ? 18.530 -17.447 15.546 0.50 10.04 ? 18  VAL   C CB  1 
ATOM   1190 C  CB  B VAL   B 1 12  ? 18.397 -17.438 15.685 0.50 14.53 ? 18  VAL   C CB  1 
ATOM   1191 C  CG1 A VAL   B 1 12  ? 17.538 -18.548 15.224 0.50 11.94 ? 18  VAL   C CG1 1 
ATOM   1192 C  CG1 B VAL   B 1 12  ? 18.629 -17.310 14.199 0.50 14.61 ? 18  VAL   C CG1 1 
ATOM   1193 C  CG2 A VAL   B 1 12  ? 17.871 -16.163 16.099 0.50 7.22  ? 18  VAL   C CG2 1 
ATOM   1194 C  CG2 B VAL   B 1 12  ? 17.189 -18.324 15.916 0.50 17.18 ? 18  VAL   C CG2 1 
ATOM   1195 N  N   . ASN   B 1 13  ? 21.519 -16.900 15.226 1.00 9.83  ? 19  ASN   C N   1 
ATOM   1196 C  CA  . ASN   B 1 13  ? 22.500 -15.834 15.014 1.00 10.19 ? 19  ASN   C CA  1 
ATOM   1197 C  C   . ASN   B 1 13  ? 21.701 -14.501 14.973 1.00 10.86 ? 19  ASN   C C   1 
ATOM   1198 O  O   . ASN   B 1 13  ? 20.668 -14.406 14.296 1.00 10.61 ? 19  ASN   C O   1 
ATOM   1199 C  CB  . ASN   B 1 13  ? 23.174 -15.991 13.636 1.00 11.79 ? 19  ASN   C CB  1 
ATOM   1200 C  CG  . ASN   B 1 13  ? 24.025 -17.258 13.544 1.00 11.19 ? 19  ASN   C CG  1 
ATOM   1201 O  OD1 . ASN   B 1 13  ? 23.558 -18.342 13.152 1.00 12.82 ? 19  ASN   C OD1 1 
ATOM   1202 N  ND2 . ASN   B 1 13  ? 25.277 -17.171 13.996 1.00 12.25 ? 19  ASN   C ND2 1 
ATOM   1203 N  N   . ARG   B 1 14  ? 22.190 -13.465 15.690 1.00 10.61 ? 20  ARG   C N   1 
ATOM   1204 C  CA  . ARG   B 1 14  ? 21.454 -12.181 15.699 1.00 10.88 ? 20  ARG   C CA  1 
ATOM   1205 C  C   . ARG   B 1 14  ? 21.290 -11.632 14.284 1.00 12.06 ? 20  ARG   C C   1 
ATOM   1206 O  O   . ARG   B 1 14  ? 20.219 -11.099 13.936 1.00 12.27 ? 20  ARG   C O   1 
ATOM   1207 C  CB  . ARG   B 1 14  ? 22.200 -11.173 16.561 1.00 10.80 ? 20  ARG   C CB  1 
ATOM   1208 C  CG  . ARG   B 1 14  ? 21.417 -9.847  16.745 1.00 11.06 ? 20  ARG   C CG  1 
ATOM   1209 C  CD  . ARG   B 1 14  ? 22.267 -8.911  17.555 1.00 12.37 ? 20  ARG   C CD  1 
ATOM   1210 N  NE  . ARG   B 1 14  ? 21.609 -7.635  17.997 1.00 12.86 ? 20  ARG   C NE  1 
ATOM   1211 C  CZ  . ARG   B 1 14  ? 21.484 -6.547  17.249 1.00 14.04 ? 20  ARG   C CZ  1 
ATOM   1212 N  NH1 . ARG   B 1 14  ? 21.847 -6.564  15.966 1.00 14.53 ? 20  ARG   C NH1 1 
ATOM   1213 N  NH2 . ARG   B 1 14  ? 20.997 -5.426  17.774 1.00 13.21 ? 20  ARG   C NH2 1 
ATOM   1214 N  N   . HIS   B 1 15  ? 22.302 -11.840 13.416 1.00 11.41 ? 21  HIS   C N   1 
ATOM   1215 C  CA  . HIS   B 1 15  ? 22.217 -11.312 12.035 1.00 11.68 ? 21  HIS   C CA  1 
ATOM   1216 C  C   . HIS   B 1 15  ? 21.195 -12.047 11.142 1.00 12.73 ? 21  HIS   C C   1 
ATOM   1217 O  O   . HIS   B 1 15  ? 20.867 -11.518 10.059 1.00 14.74 ? 21  HIS   C O   1 
ATOM   1218 C  CB  . HIS   B 1 15  ? 23.613 -11.233 11.365 1.00 13.01 ? 21  HIS   C CB  1 
ATOM   1219 C  CG  . HIS   B 1 15  ? 24.163 -12.555 10.909 1.00 12.54 ? 21  HIS   C CG  1 
ATOM   1220 N  ND1 . HIS   B 1 15  ? 24.915 -13.364 11.768 1.00 14.37 ? 21  HIS   C ND1 1 
ATOM   1221 C  CD2 . HIS   B 1 15  ? 24.129 -13.142 9.682  1.00 13.12 ? 21  HIS   C CD2 1 
ATOM   1222 C  CE1 . HIS   B 1 15  ? 25.301 -14.419 11.042 1.00 15.97 ? 21  HIS   C CE1 1 
ATOM   1223 N  NE2 . HIS   B 1 15  ? 24.856 -14.334 9.783  1.00 14.08 ? 21  HIS   C NE2 1 
ATOM   1224 N  N   . LEU   B 1 16  ? 20.674 -13.213 11.593 1.00 12.01 ? 22  LEU   C N   1 
ATOM   1225 C  CA  . LEU   B 1 16  ? 19.645 -13.939 10.836 1.00 13.14 ? 22  LEU   C CA  1 
ATOM   1226 C  C   . LEU   B 1 16  ? 18.276 -13.889 11.538 1.00 13.95 ? 22  LEU   C C   1 
ATOM   1227 O  O   . LEU   B 1 16  ? 17.341 -14.597 11.107 1.00 15.66 ? 22  LEU   C O   1 
ATOM   1228 C  CB  . LEU   B 1 16  ? 20.093 -15.396 10.668 1.00 13.02 ? 22  LEU   C CB  1 
ATOM   1229 C  CG  . LEU   B 1 16  ? 21.379 -15.534 9.853  1.00 13.98 ? 22  LEU   C CG  1 
ATOM   1230 C  CD1 . LEU   B 1 16  ? 21.782 -17.036 9.752  1.00 15.04 ? 22  LEU   C CD1 1 
ATOM   1231 C  CD2 . LEU   B 1 16  ? 21.242 -14.917 8.451  1.00 14.53 ? 22  LEU   C CD2 1 
ATOM   1232 N  N   . ALA   B 1 17  ? 18.131 -13.111 12.651 1.00 13.81 ? 23  ALA   C N   1 
ATOM   1233 C  CA  . ALA   B 1 17  ? 16.847 -13.083 13.369 1.00 13.52 ? 23  ALA   C CA  1 
ATOM   1234 C  C   . ALA   B 1 17  ? 15.741 -12.530 12.480 1.00 14.85 ? 23  ALA   C C   1 
ATOM   1235 O  O   . ALA   B 1 17  ? 15.957 -11.593 11.684 1.00 15.70 ? 23  ALA   C O   1 
ATOM   1236 C  CB  . ALA   B 1 17  ? 16.995 -12.226 14.616 1.00 14.61 ? 23  ALA   C CB  1 
ATOM   1237 N  N   . THR   B 1 18  ? 14.542 -13.088 12.651 1.00 14.27 ? 24  THR   C N   1 
ATOM   1238 C  CA  . THR   B 1 18  ? 13.377 -12.661 11.874 1.00 14.64 ? 24  THR   C CA  1 
ATOM   1239 C  C   . THR   B 1 18  ? 12.561 -11.597 12.634 1.00 15.22 ? 24  THR   C C   1 
ATOM   1240 O  O   . THR   B 1 18  ? 12.796 -11.314 13.818 1.00 15.08 ? 24  THR   C O   1 
ATOM   1241 C  CB  . THR   B 1 18  ? 12.451 -13.912 11.629 1.00 16.12 ? 24  THR   C CB  1 
ATOM   1242 O  OG1 . THR   B 1 18  ? 11.920 -14.332 12.877 1.00 16.72 ? 24  THR   C OG1 1 
ATOM   1243 C  CG2 . THR   B 1 18  ? 13.172 -15.077 10.915 1.00 17.85 ? 24  THR   C CG2 1 
ATOM   1244 N  N   . HIS   B 1 19  ? 11.518 -11.001 11.945 1.00 15.75 ? 25  HIS   C N   1 
ATOM   1245 C  CA  . HIS   B 1 19  ? 10.623 -10.082 12.638 1.00 16.46 ? 25  HIS   C CA  1 
ATOM   1246 C  C   . HIS   B 1 19  ? 9.934  -10.833 13.788 1.00 15.07 ? 25  HIS   C C   1 
ATOM   1247 O  O   . HIS   B 1 19  ? 9.817  -10.268 14.861 1.00 16.01 ? 25  HIS   C O   1 
ATOM   1248 C  CB  . HIS   B 1 19  ? 9.525  -9.573  11.665 1.00 17.20 ? 25  HIS   C CB  1 
ATOM   1249 C  CG  . HIS   B 1 19  ? 8.359  -8.902  12.359 1.00 20.00 ? 25  HIS   C CG  1 
ATOM   1250 N  ND1 . HIS   B 1 19  ? 8.469  -7.629  12.882 1.00 22.20 ? 25  HIS   C ND1 1 
ATOM   1251 C  CD2 . HIS   B 1 19  ? 7.156  -9.414  12.713 1.00 22.14 ? 25  HIS   C CD2 1 
ATOM   1252 C  CE1 . HIS   B 1 19  ? 7.280  -7.338  13.397 1.00 22.40 ? 25  HIS   C CE1 1 
ATOM   1253 N  NE2 . HIS   B 1 19  ? 6.472  -8.404  13.376 1.00 22.18 ? 25  HIS   C NE2 1 
ATOM   1254 N  N   . ASN   B 1 20  ? 9.515  -12.112 13.600 1.00 15.51 ? 26  ASN   C N   1 
ATOM   1255 C  CA  . ASN   B 1 20  ? 8.865  -12.832 14.712 1.00 16.67 ? 26  ASN   C CA  1 
ATOM   1256 C  C   . ASN   B 1 20  ? 9.818  -13.005 15.909 1.00 15.38 ? 26  ASN   C C   1 
ATOM   1257 O  O   . ASN   B 1 20  ? 9.391  -12.917 17.051 1.00 15.72 ? 26  ASN   C O   1 
ATOM   1258 C  CB  . ASN   B 1 20  ? 8.342  -14.198 14.283 1.00 17.63 ? 26  ASN   C CB  1 
ATOM   1259 C  CG  . ASN   B 1 20  ? 7.540  -14.852 15.391 1.00 24.67 ? 26  ASN   C CG  1 
ATOM   1260 O  OD1 . ASN   B 1 20  ? 6.426  -14.420 15.686 1.00 27.48 ? 26  ASN   C OD1 1 
ATOM   1261 N  ND2 . ASN   B 1 20  ? 8.099  -15.881 16.069 1.00 27.59 ? 26  ASN   C ND2 1 
ATOM   1262 N  N   . ASP   B 1 21  ? 11.124 -13.214 15.645 1.00 13.88 ? 27  ASP   C N   1 
ATOM   1263 C  CA  . ASP   B 1 21  ? 12.089 -13.302 16.729 1.00 14.43 ? 27  ASP   C CA  1 
ATOM   1264 C  C   . ASP   B 1 21  ? 12.158 -11.977 17.524 1.00 13.91 ? 27  ASP   C C   1 
ATOM   1265 O  O   . ASP   B 1 21  ? 12.099 -11.982 18.754 1.00 14.18 ? 27  ASP   C O   1 
ATOM   1266 C  CB  . ASP   B 1 21  ? 13.496 -13.608 16.174 1.00 14.31 ? 27  ASP   C CB  1 
ATOM   1267 C  CG  . ASP   B 1 21  ? 13.696 -15.028 15.691 1.00 14.68 ? 27  ASP   C CG  1 
ATOM   1268 O  OD1 . ASP   B 1 21  ? 13.144 -15.956 16.330 1.00 15.66 ? 27  ASP   C OD1 1 
ATOM   1269 O  OD2 . ASP   B 1 21  ? 14.401 -15.207 14.655 1.00 13.88 ? 27  ASP   C OD2 1 
ATOM   1270 N  N   . TRP   B 1 22  ? 12.245 -10.819 16.817 1.00 13.65 ? 28  TRP   C N   1 
ATOM   1271 C  CA  . TRP   B 1 22  ? 12.292 -9.533  17.484 1.00 14.38 ? 28  TRP   C CA  1 
ATOM   1272 C  C   . TRP   B 1 22  ? 10.968 -9.199  18.211 1.00 14.72 ? 28  TRP   C C   1 
ATOM   1273 O  O   . TRP   B 1 22  ? 10.985 -8.559  19.268 1.00 15.79 ? 28  TRP   C O   1 
ATOM   1274 C  CB  . TRP   B 1 22  ? 12.648 -8.426  16.499 1.00 14.08 ? 28  TRP   C CB  1 
ATOM   1275 C  CG  . TRP   B 1 22  ? 14.126 -8.373  16.212 1.00 13.58 ? 28  TRP   C CG  1 
ATOM   1276 C  CD1 . TRP   B 1 22  ? 14.759 -8.863  15.106 1.00 13.92 ? 28  TRP   C CD1 1 
ATOM   1277 C  CD2 . TRP   B 1 22  ? 15.156 -7.793  17.040 1.00 12.50 ? 28  TRP   C CD2 1 
ATOM   1278 N  NE1 . TRP   B 1 22  ? 16.116 -8.615  15.186 1.00 13.99 ? 28  TRP   C NE1 1 
ATOM   1279 C  CE2 . TRP   B 1 22  ? 16.374 -7.921  16.345 1.00 13.32 ? 28  TRP   C CE2 1 
ATOM   1280 C  CE3 . TRP   B 1 22  ? 15.144 -7.086  18.253 1.00 14.93 ? 28  TRP   C CE3 1 
ATOM   1281 C  CZ2 . TRP   B 1 22  ? 17.562 -7.386  16.822 1.00 13.78 ? 28  TRP   C CZ2 1 
ATOM   1282 C  CZ3 . TRP   B 1 22  ? 16.351 -6.603  18.759 1.00 15.62 ? 28  TRP   C CZ3 1 
ATOM   1283 C  CH2 . TRP   B 1 22  ? 17.536 -6.733  18.027 1.00 15.18 ? 28  TRP   C CH2 1 
ATOM   1284 N  N   . ALA   B 1 23  ? 9.846  -9.654  17.649 1.00 13.74 ? 29  ALA   C N   1 
ATOM   1285 C  CA  . ALA   B 1 23  ? 8.534  -9.426  18.286 1.00 15.20 ? 29  ALA   C CA  1 
ATOM   1286 C  C   . ALA   B 1 23  ? 8.290  -10.318 19.524 1.00 17.04 ? 29  ALA   C C   1 
ATOM   1287 O  O   . ALA   B 1 23  ? 7.318  -10.101 20.277 1.00 18.51 ? 29  ALA   C O   1 
ATOM   1288 C  CB  . ALA   B 1 23  ? 7.416  -9.663  17.265 1.00 16.30 ? 29  ALA   C CB  1 
ATOM   1289 N  N   . ASN   B 1 24  ? 9.139  -11.344 19.729 1.00 16.36 ? 30  ASN   C N   1 
ATOM   1290 C  CA  . ASN   B 1 24  ? 9.050  -12.241 20.872 1.00 15.49 ? 30  ASN   C CA  1 
ATOM   1291 C  C   . ASN   B 1 24  ? 10.439 -12.322 21.565 1.00 14.47 ? 30  ASN   C C   1 
ATOM   1292 O  O   . ASN   B 1 24  ? 10.868 -13.374 22.030 1.00 14.71 ? 30  ASN   C O   1 
ATOM   1293 C  CB  . ASN   B 1 24  ? 8.605  -13.631 20.368 1.00 16.14 ? 30  ASN   C CB  1 
ATOM   1294 C  CG  . ASN   B 1 24  ? 7.161  -13.579 19.917 1.00 17.97 ? 30  ASN   C CG  1 
ATOM   1295 O  OD1 . ASN   B 1 24  ? 6.214  -13.568 20.758 1.00 21.01 ? 30  ASN   C OD1 1 
ATOM   1296 N  ND2 . ASN   B 1 24  ? 6.967  -13.463 18.608 1.00 19.77 ? 30  ASN   C ND2 1 
ATOM   1297 N  N   . LEU   B 1 25  ? 11.118 -11.212 21.664 1.00 15.30 ? 31  LEU   C N   1 
ATOM   1298 C  CA  . LEU   B 1 25  ? 12.515 -11.161 22.132 1.00 14.45 ? 31  LEU   C CA  1 
ATOM   1299 C  C   . LEU   B 1 25  ? 12.666 -11.471 23.601 1.00 15.55 ? 31  LEU   C C   1 
ATOM   1300 O  O   . LEU   B 1 25  ? 11.884 -10.992 24.447 1.00 16.94 ? 31  LEU   C O   1 
ATOM   1301 C  CB  . LEU   B 1 25  ? 13.079 -9.751  21.858 1.00 15.11 ? 31  LEU   C CB  1 
ATOM   1302 C  CG  . LEU   B 1 25  ? 14.549 -9.591  22.207 1.00 15.39 ? 31  LEU   C CG  1 
ATOM   1303 C  CD1 . LEU   B 1 25  ? 15.433 -10.440 21.247 1.00 15.85 ? 31  LEU   C CD1 1 
ATOM   1304 C  CD2 . LEU   B 1 25  ? 14.956 -8.126  22.122 1.00 17.63 ? 31  LEU   C CD2 1 
ATOM   1305 N  N   . VAL   B 1 26  ? 13.654 -12.323 23.928 1.00 14.40 ? 32  VAL   C N   1 
ATOM   1306 C  CA  . VAL   B 1 26  ? 14.001 -12.596 25.312 1.00 15.27 ? 32  VAL   C CA  1 
ATOM   1307 C  C   . VAL   B 1 26  ? 15.334 -11.891 25.636 1.00 15.60 ? 32  VAL   C C   1 
ATOM   1308 O  O   . VAL   B 1 26  ? 15.452 -11.227 26.670 1.00 16.55 ? 32  VAL   C O   1 
ATOM   1309 C  CB  . VAL   B 1 26  ? 14.159 -14.129 25.524 1.00 16.08 ? 32  VAL   C CB  1 
ATOM   1310 C  CG1 . VAL   B 1 26  ? 14.756 -14.437 26.910 1.00 17.01 ? 32  VAL   C CG1 1 
ATOM   1311 C  CG2 . VAL   B 1 26  ? 12.809 -14.838 25.349 1.00 17.50 ? 32  VAL   C CG2 1 
ATOM   1312 N  N   . TRP   B 1 27  ? 16.355 -12.015 24.751 1.00 14.37 ? 33  TRP   C N   1 
ATOM   1313 C  CA  . TRP   B 1 27  ? 17.691 -11.458 25.022 1.00 13.82 ? 33  TRP   C CA  1 
ATOM   1314 C  C   . TRP   B 1 27  ? 18.490 -11.411 23.699 1.00 14.01 ? 33  TRP   C C   1 
ATOM   1315 O  O   . TRP   B 1 27  ? 18.280 -12.277 22.850 1.00 13.98 ? 33  TRP   C O   1 
ATOM   1316 C  CB  . TRP   B 1 27  ? 18.441 -12.367 26.046 1.00 14.55 ? 33  TRP   C CB  1 
ATOM   1317 C  CG  . TRP   B 1 27  ? 19.917 -12.085 26.228 1.00 15.59 ? 33  TRP   C CG  1 
ATOM   1318 C  CD1 . TRP   B 1 27  ? 20.489 -11.101 26.991 1.00 17.85 ? 33  TRP   C CD1 1 
ATOM   1319 C  CD2 . TRP   B 1 27  ? 21.002 -12.770 25.580 1.00 14.49 ? 33  TRP   C CD2 1 
ATOM   1320 N  NE1 . TRP   B 1 27  ? 21.872 -11.175 26.899 1.00 17.99 ? 33  TRP   C NE1 1 
ATOM   1321 C  CE2 . TRP   B 1 27  ? 22.205 -12.191 26.040 1.00 16.00 ? 33  TRP   C CE2 1 
ATOM   1322 C  CE3 . TRP   B 1 27  ? 21.070 -13.819 24.655 1.00 14.66 ? 33  TRP   C CE3 1 
ATOM   1323 C  CZ2 . TRP   B 1 27  ? 23.463 -12.677 25.658 1.00 15.62 ? 33  TRP   C CZ2 1 
ATOM   1324 C  CZ3 . TRP   B 1 27  ? 22.317 -14.314 24.308 1.00 14.64 ? 33  TRP   C CZ3 1 
ATOM   1325 C  CH2 . TRP   B 1 27  ? 23.490 -13.713 24.765 1.00 15.06 ? 33  TRP   C CH2 1 
ATOM   1326 N  N   . GLU   B 1 28  ? 19.312 -10.384 23.502 1.00 12.91 ? 34  GLU   C N   1 
ATOM   1327 C  CA  . GLU   B 1 28  ? 20.160 -10.322 22.319 1.00 13.55 ? 34  GLU   C CA  1 
ATOM   1328 C  C   . GLU   B 1 28  ? 21.460 -9.645  22.673 1.00 14.16 ? 34  GLU   C C   1 
ATOM   1329 O  O   . GLU   B 1 28  ? 21.484 -8.755  23.546 1.00 14.47 ? 34  GLU   C O   1 
ATOM   1330 C  CB  . GLU   B 1 28  ? 19.441 -9.618  21.160 1.00 14.93 ? 34  GLU   C CB  1 
ATOM   1331 C  CG  . GLU   B 1 28  ? 18.905 -8.235  21.442 1.00 15.06 ? 34  GLU   C CG  1 
ATOM   1332 C  CD  . GLU   B 1 28  ? 19.879 -7.080  21.364 1.00 17.32 ? 34  GLU   C CD  1 
ATOM   1333 O  OE1 . GLU   B 1 28  ? 19.643 -6.045  22.035 1.00 20.20 ? 34  GLU   C OE1 1 
ATOM   1334 O  OE2 . GLU   B 1 28  ? 20.884 -7.201  20.624 1.00 15.78 ? 34  GLU   C OE2 1 
ATOM   1335 N  N   . ASP   B 1 29  ? 22.542 -10.000 21.949 1.00 13.64 ? 35  ASP   C N   1 
ATOM   1336 C  CA  . ASP   B 1 29  ? 23.829 -9.372  22.180 1.00 13.58 ? 35  ASP   C CA  1 
ATOM   1337 C  C   . ASP   B 1 29  ? 24.583 -9.323  20.856 1.00 13.26 ? 35  ASP   C C   1 
ATOM   1338 O  O   . ASP   B 1 29  ? 24.995 -10.361 20.343 1.00 13.25 ? 35  ASP   C O   1 
ATOM   1339 C  CB  . ASP   B 1 29  ? 24.579 -10.158 23.263 1.00 14.43 ? 35  ASP   C CB  1 
ATOM   1340 C  CG  . ASP   B 1 29  ? 25.928 -9.588  23.657 1.00 19.19 ? 35  ASP   C CG  1 
ATOM   1341 O  OD1 . ASP   B 1 29  ? 26.674 -9.149  22.762 1.00 20.08 ? 35  ASP   C OD1 1 
ATOM   1342 O  OD2 . ASP   B 1 29  ? 26.284 -9.681  24.849 1.00 21.66 ? 35  ASP   C OD2 1 
ATOM   1343 N  N   . SER   B 1 30  ? 24.721 -8.121  20.276 1.00 12.91 ? 36  SER   C N   1 
ATOM   1344 C  CA  A SER   B 1 30  ? 25.429 -7.933  18.998 0.50 12.69 ? 36  SER   C CA  1 
ATOM   1345 C  CA  B SER   B 1 30  ? 25.406 -7.999  18.989 0.50 13.32 ? 36  SER   C CA  1 
ATOM   1346 C  C   . SER   B 1 30  ? 26.892 -8.401  19.076 1.00 13.42 ? 36  SER   C C   1 
ATOM   1347 O  O   . SER   B 1 30  ? 27.399 -9.014  18.111 1.00 12.31 ? 36  SER   C O   1 
ATOM   1348 C  CB  A SER   B 1 30  ? 25.374 -6.469  18.561 0.50 13.43 ? 36  SER   C CB  1 
ATOM   1349 C  CB  B SER   B 1 30  ? 25.225 -6.604  18.412 0.50 15.72 ? 36  SER   C CB  1 
ATOM   1350 O  OG  A SER   B 1 30  ? 26.229 -6.202  17.453 0.50 12.26 ? 36  SER   C OG  1 
ATOM   1351 O  OG  B SER   B 1 30  ? 25.717 -5.650  19.333 0.50 17.35 ? 36  SER   C OG  1 
ATOM   1352 N  N   . SER   B 1 31  ? 27.582 -8.119  20.204 1.00 13.21 ? 37  SER   C N   1 
ATOM   1353 C  CA  . SER   B 1 31  ? 28.993 -8.532  20.293 1.00 12.75 ? 37  SER   C CA  1 
ATOM   1354 C  C   . SER   B 1 31  ? 29.162 -10.034 20.246 1.00 12.38 ? 37  SER   C C   1 
ATOM   1355 O  O   . SER   B 1 31  ? 30.253 -10.486 19.864 1.00 13.14 ? 37  SER   C O   1 
ATOM   1356 C  CB  . SER   B 1 31  ? 29.637 -7.969  21.549 1.00 16.32 ? 37  SER   C CB  1 
ATOM   1357 O  OG  . SER   B 1 31  ? 29.255 -8.665  22.716 1.00 21.67 ? 37  SER   C OG  1 
ATOM   1358 N  N   . ARG   B 1 32  ? 28.130 -10.814 20.575 1.00 11.50 ? 38  ARG   C N   1 
ATOM   1359 C  CA  . ARG   B 1 32  ? 28.215 -12.296 20.515 1.00 11.06 ? 38  ARG   C CA  1 
ATOM   1360 C  C   . ARG   B 1 32  ? 27.552 -12.863 19.253 1.00 10.62 ? 38  ARG   C C   1 
ATOM   1361 O  O   . ARG   B 1 32  ? 27.584 -14.090 19.033 1.00 11.53 ? 38  ARG   C O   1 
ATOM   1362 C  CB  . ARG   B 1 32  ? 27.477 -12.916 21.749 1.00 13.09 ? 38  ARG   C CB  1 
ATOM   1363 C  CG  . ARG   B 1 32  ? 28.181 -12.575 23.049 1.00 13.97 ? 38  ARG   C CG  1 
ATOM   1364 C  CD  . ARG   B 1 32  ? 27.451 -13.108 24.300 1.00 12.37 ? 38  ARG   C CD  1 
ATOM   1365 N  NE  . ARG   B 1 32  ? 27.475 -14.584 24.344 1.00 11.72 ? 38  ARG   C NE  1 
ATOM   1366 C  CZ  . ARG   B 1 32  ? 27.490 -15.320 25.462 1.00 12.82 ? 38  ARG   C CZ  1 
ATOM   1367 N  NH1 . ARG   B 1 32  ? 27.376 -14.742 26.655 1.00 13.28 ? 38  ARG   C NH1 1 
ATOM   1368 N  NH2 . ARG   B 1 32  ? 27.612 -16.646 25.393 1.00 12.65 ? 38  ARG   C NH2 1 
ATOM   1369 N  N   . ASP   B 1 33  ? 26.849 -12.020 18.466 1.00 10.72 ? 39  ASP   C N   1 
ATOM   1370 C  CA  . ASP   B 1 33  ? 26.066 -12.480 17.334 1.00 10.99 ? 39  ASP   C CA  1 
ATOM   1371 C  C   . ASP   B 1 33  ? 24.977 -13.451 17.770 1.00 10.83 ? 39  ASP   C C   1 
ATOM   1372 O  O   . ASP   B 1 33  ? 24.674 -14.383 17.021 1.00 11.03 ? 39  ASP   C O   1 
ATOM   1373 C  CB  . ASP   B 1 33  ? 26.911 -13.075 16.198 1.00 10.99 ? 39  ASP   C CB  1 
ATOM   1374 C  CG  . ASP   B 1 33  ? 26.125 -13.412 14.937 1.00 13.19 ? 39  ASP   C CG  1 
ATOM   1375 O  OD1 . ASP   B 1 33  ? 25.209 -12.620 14.568 1.00 13.20 ? 39  ASP   C OD1 1 
ATOM   1376 O  OD2 . ASP   B 1 33  ? 26.433 -14.458 14.297 1.00 11.90 ? 39  ASP   C OD2 1 
ATOM   1377 N  N   . LEU   B 1 34  ? 24.337 -13.209 18.951 1.00 10.65 ? 40  LEU   C N   1 
ATOM   1378 C  CA  . LEU   B 1 34  ? 23.258 -14.114 19.413 1.00 11.86 ? 40  LEU   C CA  1 
ATOM   1379 C  C   . LEU   B 1 34  ? 21.962 -13.374 19.691 1.00 11.96 ? 40  LEU   C C   1 
ATOM   1380 O  O   . LEU   B 1 34  ? 21.993 -12.204 20.133 1.00 11.43 ? 40  LEU   C O   1 
ATOM   1381 C  CB  . LEU   B 1 34  ? 23.654 -14.853 20.707 1.00 12.44 ? 40  LEU   C CB  1 
ATOM   1382 C  CG  . LEU   B 1 34  ? 24.729 -15.954 20.605 1.00 12.20 ? 40  LEU   C CG  1 
ATOM   1383 C  CD1 . LEU   B 1 34  ? 24.980 -16.548 22.024 1.00 13.46 ? 40  LEU   C CD1 1 
ATOM   1384 C  CD2 . LEU   B 1 34  ? 24.279 -17.057 19.635 1.00 13.21 ? 40  LEU   C CD2 1 
ATOM   1385 N  N   . LEU   B 1 35  ? 20.857 -14.031 19.418 1.00 11.41 ? 41  LEU   C N   1 
ATOM   1386 C  CA  . LEU   B 1 35  ? 19.534 -13.538 19.805 1.00 11.58 ? 41  LEU   C CA  1 
ATOM   1387 C  C   . LEU   B 1 35  ? 18.703 -14.765 20.225 1.00 11.41 ? 41  LEU   C C   1 
ATOM   1388 O  O   . LEU   B 1 35  ? 18.766 -15.834 19.601 1.00 12.34 ? 41  LEU   C O   1 
ATOM   1389 C  CB  . LEU   B 1 35  ? 18.881 -12.796 18.609 1.00 11.66 ? 41  LEU   C CB  1 
ATOM   1390 C  CG  . LEU   B 1 35  ? 17.486 -12.223 18.881 1.00 11.56 ? 41  LEU   C CG  1 
ATOM   1391 C  CD1 . LEU   B 1 35  ? 17.280 -10.903 18.125 1.00 14.26 ? 41  LEU   C CD1 1 
ATOM   1392 C  CD2 . LEU   B 1 35  ? 16.371 -13.221 18.524 1.00 12.36 ? 41  LEU   C CD2 1 
ATOM   1393 N  N   . VAL   B 1 36  ? 17.929 -14.601 21.314 1.00 11.77 ? 42  VAL   C N   1 
ATOM   1394 C  CA  . VAL   B 1 36  ? 17.015 -15.605 21.832 1.00 11.91 ? 42  VAL   C CA  1 
ATOM   1395 C  C   . VAL   B 1 36  ? 15.584 -15.078 21.831 1.00 11.62 ? 42  VAL   C C   1 
ATOM   1396 O  O   . VAL   B 1 36  ? 15.354 -13.968 22.334 1.00 12.33 ? 42  VAL   C O   1 
ATOM   1397 C  CB  . VAL   B 1 36  ? 17.450 -16.047 23.246 1.00 12.20 ? 42  VAL   C CB  1 
ATOM   1398 C  CG1 . VAL   B 1 36  ? 16.502 -17.130 23.777 1.00 13.75 ? 42  VAL   C CG1 1 
ATOM   1399 C  CG2 . VAL   B 1 36  ? 18.902 -16.582 23.205 1.00 13.10 ? 42  VAL   C CG2 1 
ATOM   1400 N  N   . SER   B 1 37  ? 14.655 -15.849 21.258 1.00 11.19 ? 43  SER   C N   1 
ATOM   1401 C  CA  . SER   B 1 37  ? 13.240 -15.480 21.255 1.00 12.28 ? 43  SER   C CA  1 
ATOM   1402 C  C   . SER   B 1 37  ? 12.436 -16.570 21.974 1.00 13.31 ? 43  SER   C C   1 
ATOM   1403 O  O   . SER   B 1 37  ? 12.929 -17.695 22.205 1.00 12.95 ? 43  SER   C O   1 
ATOM   1404 C  CB  . SER   B 1 37  ? 12.763 -15.265 19.826 1.00 14.26 ? 43  SER   C CB  1 
ATOM   1405 O  OG  . SER   B 1 37  ? 12.886 -16.439 19.034 1.00 13.78 ? 43  SER   C OG  1 
ATOM   1406 N  N   . SER   B 1 38  ? 11.191 -16.252 22.335 1.00 13.36 ? 44  SER   C N   1 
ATOM   1407 C  CA  . SER   B 1 38  ? 10.327 -17.231 23.000 1.00 15.18 ? 44  SER   C CA  1 
ATOM   1408 C  C   . SER   B 1 38  ? 9.493  -18.006 21.983 1.00 16.93 ? 44  SER   C C   1 
ATOM   1409 O  O   . SER   B 1 38  ? 9.140  -17.481 20.916 1.00 17.99 ? 44  SER   C O   1 
ATOM   1410 C  CB  . SER   B 1 38  ? 9.435  -16.535 24.026 1.00 17.41 ? 44  SER   C CB  1 
ATOM   1411 O  OG  . SER   B 1 38  ? 8.641  -15.574 23.350 1.00 21.15 ? 44  SER   C OG  1 
ATOM   1412 N  N   . THR   B 1 39  ? 9.161  -19.254 22.325 1.00 16.94 ? 45  THR   C N   1 
ATOM   1413 C  CA  . THR   B 1 39  ? 8.386  -20.128 21.456 1.00 17.68 ? 45  THR   C CA  1 
ATOM   1414 C  C   . THR   B 1 39  ? 7.100  -20.574 22.168 1.00 19.48 ? 45  THR   C C   1 
ATOM   1415 O  O   . THR   B 1 39  ? 7.058  -20.687 23.390 1.00 19.60 ? 45  THR   C O   1 
ATOM   1416 C  CB  . THR   B 1 39  ? 9.215  -21.407 21.107 1.00 18.17 ? 45  THR   C CB  1 
ATOM   1417 O  OG1 . THR   B 1 39  ? 9.476  -22.181 22.279 1.00 19.30 ? 45  THR   C OG1 1 
ATOM   1418 C  CG2 . THR   B 1 39  ? 10.559 -21.087 20.382 1.00 18.38 ? 45  THR   C CG2 1 
ATOM   1419 N  N   . THR   B 1 40  ? 6.098  -20.946 21.368 1.00 21.28 ? 46  THR   C N   1 
ATOM   1420 C  CA  . THR   B 1 40  ? 4.856  -21.497 21.913 1.00 23.48 ? 46  THR   C CA  1 
ATOM   1421 C  C   . THR   B 1 40  ? 5.064  -22.977 22.266 1.00 23.29 ? 46  THR   C C   1 
ATOM   1422 O  O   . THR   B 1 40  ? 4.697  -23.412 23.359 1.00 25.00 ? 46  THR   C O   1 
ATOM   1423 C  CB  . THR   B 1 40  ? 3.716  -21.248 20.915 1.00 27.92 ? 46  THR   C CB  1 
ATOM   1424 O  OG1 . THR   B 1 40  ? 4.046  -21.899 19.685 1.00 32.27 ? 46  THR   C OG1 1 
ATOM   1425 C  CG2 . THR   B 1 40  ? 3.536  -19.762 20.617 1.00 27.45 ? 46  THR   C CG2 1 
ATOM   1426 N  N   . ALA   B 1 41  ? 5.733  -23.727 21.379 1.00 21.29 ? 47  ALA   C N   1 
ATOM   1427 C  CA  . ALA   B 1 41  ? 5.977  -25.140 21.627 1.00 21.73 ? 47  ALA   C CA  1 
ATOM   1428 C  C   . ALA   B 1 41  ? 7.311  -25.395 22.318 1.00 20.05 ? 47  ALA   C C   1 
ATOM   1429 O  O   . ALA   B 1 41  ? 8.249  -24.623 22.132 1.00 20.39 ? 47  ALA   C O   1 
ATOM   1430 C  CB  . ALA   B 1 41  ? 5.924  -25.913 20.315 1.00 23.34 ? 47  ALA   C CB  1 
ATOM   1431 N  N   . GLN   B 1 42  ? 7.420  -26.488 23.062 1.00 18.74 ? 48  GLN   C N   1 
ATOM   1432 C  CA  . GLN   B 1 42  ? 8.660  -26.837 23.748 1.00 19.05 ? 48  GLN   C CA  1 
ATOM   1433 C  C   . GLN   B 1 42  ? 9.630  -27.497 22.780 1.00 18.34 ? 48  GLN   C C   1 
ATOM   1434 O  O   . GLN   B 1 42  ? 9.218  -28.299 21.953 1.00 19.41 ? 48  GLN   C O   1 
ATOM   1435 C  CB  . GLN   B 1 42  ? 8.388  -27.796 24.924 1.00 23.74 ? 48  GLN   C CB  1 
ATOM   1436 C  CG  . GLN   B 1 42  ? 7.738  -27.102 26.121 1.00 33.47 ? 48  GLN   C CG  1 
ATOM   1437 C  CD  . GLN   B 1 42  ? 7.604  -28.077 27.263 1.00 43.63 ? 48  GLN   C CD  1 
ATOM   1438 O  OE1 . GLN   B 1 42  ? 6.804  -29.019 27.221 1.00 48.09 ? 48  GLN   C OE1 1 
ATOM   1439 N  NE2 . GLN   B 1 42  ? 8.391  -27.895 28.309 1.00 46.50 ? 48  GLN   C NE2 1 
ATOM   1440 N  N   . GLY   B 1 43  ? 10.905 -27.163 22.923 1.00 16.57 ? 49  GLY   C N   1 
ATOM   1441 C  CA  . GLY   B 1 43  ? 12.001 -27.733 22.127 1.00 15.95 ? 49  GLY   C CA  1 
ATOM   1442 C  C   . GLY   B 1 43  ? 12.671 -28.866 22.880 1.00 16.46 ? 49  GLY   C C   1 
ATOM   1443 O  O   . GLY   B 1 43  ? 12.438 -29.051 24.084 1.00 18.97 ? 49  GLY   C O   1 
ATOM   1444 N  N   . CYS   B 1 44  ? 13.500 -29.609 22.201 1.00 14.90 ? 50  CYS   C N   1 
ATOM   1445 C  CA  . CYS   B 1 44  ? 14.079 -30.827 22.775 1.00 14.60 ? 50  CYS   C CA  1 
ATOM   1446 C  C   . CYS   B 1 44  ? 15.564 -30.860 22.801 1.00 15.76 ? 50  CYS   C C   1 
ATOM   1447 O  O   . CYS   B 1 44  ? 16.132 -31.904 23.152 1.00 17.68 ? 50  CYS   C O   1 
ATOM   1448 C  CB  . CYS   B 1 44  ? 13.527 -32.043 22.032 1.00 14.94 ? 50  CYS   C CB  1 
ATOM   1449 S  SG  . CYS   B 1 44  ? 11.714 -32.124 22.089 1.00 19.32 ? 50  CYS   C SG  1 
ATOM   1450 N  N   . ASP   B 1 45  ? 16.241 -29.785 22.396 1.00 13.00 ? 51  ASP   C N   1 
ATOM   1451 C  CA  . ASP   B 1 45  ? 17.700 -29.779 22.419 1.00 13.02 ? 51  ASP   C CA  1 
ATOM   1452 C  C   . ASP   B 1 45  ? 18.148 -29.575 23.871 1.00 14.43 ? 51  ASP   C C   1 
ATOM   1453 O  O   . ASP   B 1 45  ? 17.441 -28.929 24.688 1.00 16.25 ? 51  ASP   C O   1 
ATOM   1454 C  CB  . ASP   B 1 45  ? 18.254 -28.607 21.568 1.00 14.23 ? 51  ASP   C CB  1 
ATOM   1455 C  CG  . ASP   B 1 45  ? 18.088 -28.781 20.073 1.00 17.84 ? 51  ASP   C CG  1 
ATOM   1456 O  OD1 . ASP   B 1 45  ? 18.058 -29.936 19.606 1.00 18.39 ? 51  ASP   C OD1 1 
ATOM   1457 O  OD2 . ASP   B 1 45  ? 17.936 -27.746 19.361 1.00 15.28 ? 51  ASP   C OD2 1 
ATOM   1458 N  N   . THR   B 1 46  ? 19.297 -30.178 24.212 1.00 13.66 ? 52  THR   C N   1 
ATOM   1459 C  CA  . THR   B 1 46  ? 19.914 -30.003 25.533 1.00 12.97 ? 52  THR   C CA  1 
ATOM   1460 C  C   . THR   B 1 46  ? 21.190 -29.174 25.359 1.00 13.83 ? 52  THR   C C   1 
ATOM   1461 O  O   . THR   B 1 46  ? 21.974 -29.463 24.450 1.00 13.96 ? 52  THR   C O   1 
ATOM   1462 C  CB  . THR   B 1 46  ? 20.349 -31.380 26.098 1.00 15.08 ? 52  THR   C CB  1 
ATOM   1463 O  OG1 . THR   B 1 46  ? 19.185 -32.218 26.306 1.00 18.14 ? 52  THR   C OG1 1 
ATOM   1464 C  CG2 . THR   B 1 46  ? 21.155 -31.246 27.444 1.00 15.78 ? 52  THR   C CG2 1 
ATOM   1465 N  N   . ILE   B 1 47  ? 21.373 -28.128 26.162 1.00 12.81 ? 53  ILE   C N   1 
ATOM   1466 C  CA  . ILE   B 1 47  ? 22.592 -27.328 26.113 1.00 12.78 ? 53  ILE   C CA  1 
ATOM   1467 C  C   . ILE   B 1 47  ? 23.673 -28.010 26.942 1.00 11.08 ? 53  ILE   C C   1 
ATOM   1468 O  O   . ILE   B 1 47  ? 23.443 -28.432 28.075 1.00 11.92 ? 53  ILE   C O   1 
ATOM   1469 C  CB  . ILE   B 1 47  ? 22.341 -25.937 26.701 1.00 13.78 ? 53  ILE   C CB  1 
ATOM   1470 C  CG1 . ILE   B 1 47  ? 21.114 -25.248 26.084 1.00 13.77 ? 53  ILE   C CG1 1 
ATOM   1471 C  CG2 . ILE   B 1 47  ? 23.600 -25.062 26.607 1.00 13.66 ? 53  ILE   C CG2 1 
ATOM   1472 C  CD1 . ILE   B 1 47  ? 21.295 -25.123 24.525 1.00 16.29 ? 53  ILE   C CD1 1 
ATOM   1473 N  N   . ALA   B 1 48  ? 24.879 -28.071 26.393 1.00 10.73 ? 54  ALA   C N   1 
ATOM   1474 C  CA  . ALA   B 1 48  ? 26.018 -28.630 27.119 1.00 10.40 ? 54  ALA   C CA  1 
ATOM   1475 C  C   . ALA   B 1 48  ? 26.404 -27.716 28.274 1.00 10.43 ? 54  ALA   C C   1 
ATOM   1476 O  O   . ALA   B 1 48  ? 26.391 -26.473 28.137 1.00 11.17 ? 54  ALA   C O   1 
ATOM   1477 C  CB  . ALA   B 1 48  ? 27.199 -28.737 26.158 1.00 10.96 ? 54  ALA   C CB  1 
ATOM   1478 N  N   . ARG   B 1 49  ? 26.790 -28.336 29.421 1.00 10.70 ? 55  ARG   C N   1 
ATOM   1479 C  CA  . ARG   B 1 49  ? 27.252 -27.568 30.590 1.00 11.14 ? 55  ARG   C CA  1 
ATOM   1480 C  C   . ARG   B 1 49  ? 28.573 -28.222 30.964 1.00 11.78 ? 55  ARG   C C   1 
ATOM   1481 O  O   . ARG   B 1 49  ? 28.614 -29.254 31.643 1.00 12.74 ? 55  ARG   C O   1 
ATOM   1482 C  CB  . ARG   B 1 49  ? 26.227 -27.605 31.751 1.00 11.26 ? 55  ARG   C CB  1 
ATOM   1483 C  CG  . ARG   B 1 49  ? 24.855 -27.062 31.345 1.00 10.63 ? 55  ARG   C CG  1 
ATOM   1484 C  CD  . ARG   B 1 49  ? 24.856 -25.554 30.993 1.00 12.94 ? 55  ARG   C CD  1 
ATOM   1485 N  NE  . ARG   B 1 49  ? 23.496 -25.117 30.607 1.00 12.84 ? 55  ARG   C NE  1 
ATOM   1486 C  CZ  . ARG   B 1 49  ? 23.224 -24.001 29.918 1.00 13.33 ? 55  ARG   C CZ  1 
ATOM   1487 N  NH1 . ARG   B 1 49  ? 24.200 -23.186 29.537 1.00 13.44 ? 55  ARG   C NH1 1 
ATOM   1488 N  NH2 . ARG   B 1 49  ? 21.964 -23.713 29.567 1.00 14.68 ? 55  ARG   C NH2 1 
ATOM   1489 N  N   . CYS   B 1 50  ? 29.659 -27.628 30.437 1.00 11.06 ? 56  CYS   C N   1 
ATOM   1490 C  CA  . CYS   B 1 50  ? 30.984 -28.264 30.448 1.00 10.58 ? 56  CYS   C CA  1 
ATOM   1491 C  C   . CYS   B 1 50  ? 32.046 -27.306 29.902 1.00 11.06 ? 56  CYS   C C   1 
ATOM   1492 O  O   . CYS   B 1 50  ? 31.718 -26.200 29.436 1.00 11.50 ? 56  CYS   C O   1 
ATOM   1493 C  CB  . CYS   B 1 50  ? 30.912 -29.486 29.516 1.00 11.12 ? 56  CYS   C CB  1 
ATOM   1494 S  SG  . CYS   B 1 50  ? 30.762 -29.041 27.735 1.00 11.54 ? 56  CYS   C SG  1 
ATOM   1495 N  N   . ASP   B 1 51  ? 33.327 -27.753 29.934 1.00 11.95 ? 57  ASP   C N   1 
ATOM   1496 C  CA  . ASP   B 1 51  ? 34.446 -27.049 29.313 1.00 12.44 ? 57  ASP   C CA  1 
ATOM   1497 C  C   . ASP   B 1 51  ? 35.116 -27.882 28.210 1.00 12.90 ? 57  ASP   C C   1 
ATOM   1498 O  O   . ASP   B 1 51  ? 36.309 -27.736 27.943 1.00 13.30 ? 57  ASP   C O   1 
ATOM   1499 C  CB  . ASP   B 1 51  ? 35.465 -26.602 30.362 1.00 14.32 ? 57  ASP   C CB  1 
ATOM   1500 C  CG  . ASP   B 1 51  ? 36.149 -27.720 31.097 1.00 18.58 ? 57  ASP   C CG  1 
ATOM   1501 O  OD1 . ASP   B 1 51  ? 35.820 -28.879 30.855 1.00 18.25 ? 57  ASP   C OD1 1 
ATOM   1502 O  OD2 . ASP   B 1 51  ? 37.090 -27.429 31.904 1.00 23.78 ? 57  ASP   C OD2 1 
ATOM   1503 N  N   . CYS   B 1 52  ? 34.338 -28.723 27.528 1.00 11.90 ? 58  CYS   C N   1 
ATOM   1504 C  CA  . CYS   B 1 52  ? 34.879 -29.504 26.381 1.00 11.42 ? 58  CYS   C CA  1 
ATOM   1505 C  C   . CYS   B 1 52  ? 35.541 -28.624 25.355 1.00 11.03 ? 58  CYS   C C   1 
ATOM   1506 O  O   . CYS   B 1 52  ? 35.112 -27.465 25.118 1.00 11.39 ? 58  CYS   C O   1 
ATOM   1507 C  CB  . CYS   B 1 52  ? 33.772 -30.305 25.684 1.00 11.72 ? 58  CYS   C CB  1 
ATOM   1508 S  SG  . CYS   B 1 52  ? 33.180 -31.766 26.610 1.00 12.03 ? 58  CYS   C SG  1 
ATOM   1509 N  N   . GLN   B 1 53  ? 36.576 -29.182 24.725 1.00 10.75 ? 59  GLN   C N   1 
ATOM   1510 C  CA  . GLN   B 1 53  ? 37.253 -28.578 23.576 1.00 11.94 ? 59  GLN   C CA  1 
ATOM   1511 C  C   . GLN   B 1 53  ? 37.255 -29.516 22.378 1.00 10.79 ? 59  GLN   C C   1 
ATOM   1512 O  O   . GLN   B 1 53  ? 38.027 -29.293 21.424 1.00 10.94 ? 59  GLN   C O   1 
ATOM   1513 C  CB  . GLN   B 1 53  ? 38.685 -28.140 23.917 1.00 11.05 ? 59  GLN   C CB  1 
ATOM   1514 C  CG  . GLN   B 1 53  ? 38.711 -26.922 24.828 1.00 14.21 ? 59  GLN   C CG  1 
ATOM   1515 C  CD  . GLN   B 1 53  ? 40.095 -26.339 25.019 1.00 18.32 ? 59  GLN   C CD  1 
ATOM   1516 O  OE1 . GLN   B 1 53  ? 40.645 -26.325 26.146 1.00 18.94 ? 59  GLN   C OE1 1 
ATOM   1517 N  NE2 . GLN   B 1 53  ? 40.635 -25.748 23.964 1.00 15.36 ? 59  GLN   C NE2 1 
ATOM   1518 N  N   . THR   B 1 54  ? 36.459 -30.602 22.404 1.00 11.51 ? 60  THR   C N   1 
ATOM   1519 C  CA  . THR   B 1 54  ? 36.338 -31.469 21.242 1.00 12.59 ? 60  THR   C CA  1 
ATOM   1520 C  C   . THR   B 1 54  ? 34.855 -31.724 21.027 1.00 11.84 ? 60  THR   C C   1 
ATOM   1521 O  O   . THR   B 1 54  ? 34.085 -31.830 21.984 1.00 12.21 ? 60  THR   C O   1 
ATOM   1522 C  CB  . THR   B 1 54  ? 37.079 -32.795 21.362 1.00 15.41 ? 60  THR   C CB  1 
ATOM   1523 O  OG1 . THR   B 1 54  ? 36.551 -33.500 22.423 1.00 20.24 ? 60  THR   C OG1 1 
ATOM   1524 C  CG2 . THR   B 1 54  ? 38.543 -32.623 21.633 1.00 15.40 ? 60  THR   C CG2 1 
ATOM   1525 N  N   . GLY   B 1 55  ? 34.453 -31.760 19.759 1.00 10.48 ? 61  GLY   C N   1 
ATOM   1526 C  CA  . GLY   B 1 55  ? 33.047 -31.981 19.425 1.00 10.43 ? 61  GLY   C CA  1 
ATOM   1527 C  C   . GLY   B 1 55  ? 32.893 -32.189 17.924 1.00 9.45  ? 61  GLY   C C   1 
ATOM   1528 O  O   . GLY   B 1 55  ? 33.876 -32.491 17.222 1.00 10.98 ? 61  GLY   C O   1 
ATOM   1529 N  N   . VAL   B 1 56  ? 31.657 -32.056 17.450 1.00 9.49  ? 62  VAL   C N   1 
ATOM   1530 C  CA  . VAL   B 1 56  ? 31.332 -32.252 16.021 1.00 9.54  ? 62  VAL   C CA  1 
ATOM   1531 C  C   . VAL   B 1 56  ? 30.442 -31.124 15.594 1.00 9.72  ? 62  VAL   C C   1 
ATOM   1532 O  O   . VAL   B 1 56  ? 29.494 -30.828 16.313 1.00 10.68 ? 62  VAL   C O   1 
ATOM   1533 C  CB  . VAL   B 1 56  ? 30.600 -33.621 15.861 1.00 10.25 ? 62  VAL   C CB  1 
ATOM   1534 C  CG1 . VAL   B 1 56  ? 30.054 -33.820 14.428 1.00 12.21 ? 62  VAL   C CG1 1 
ATOM   1535 C  CG2 . VAL   B 1 56  ? 31.516 -34.797 16.275 1.00 11.38 ? 62  VAL   C CG2 1 
ATOM   1536 N  N   . TYR   B 1 57  ? 30.690 -30.546 14.415 1.00 9.77  ? 63  TYR   C N   1 
ATOM   1537 C  CA  . TYR   B 1 57  ? 29.803 -29.472 13.926 1.00 8.47  ? 63  TYR   C CA  1 
ATOM   1538 C  C   . TYR   B 1 57  ? 29.227 -29.808 12.568 1.00 9.99  ? 63  TYR   C C   1 
ATOM   1539 O  O   . TYR   B 1 57  ? 29.888 -30.504 11.781 1.00 10.58 ? 63  TYR   C O   1 
ATOM   1540 C  CB  . TYR   B 1 57  ? 30.493 -28.055 13.892 1.00 9.32  ? 63  TYR   C CB  1 
ATOM   1541 C  CG  . TYR   B 1 57  ? 31.357 -27.764 12.682 1.00 9.34  ? 63  TYR   C CG  1 
ATOM   1542 C  CD1 . TYR   B 1 57  ? 32.657 -28.244 12.597 1.00 10.59 ? 63  TYR   C CD1 1 
ATOM   1543 C  CD2 . TYR   B 1 57  ? 30.903 -26.913 11.668 1.00 9.91  ? 63  TYR   C CD2 1 
ATOM   1544 C  CE1 . TYR   B 1 57  ? 33.464 -27.969 11.483 1.00 11.29 ? 63  TYR   C CE1 1 
ATOM   1545 C  CE2 . TYR   B 1 57  ? 31.713 -26.610 10.560 1.00 10.81 ? 63  TYR   C CE2 1 
ATOM   1546 C  CZ  . TYR   B 1 57  ? 32.991 -27.124 10.487 1.00 11.19 ? 63  TYR   C CZ  1 
ATOM   1547 O  OH  . TYR   B 1 57  ? 33.814 -26.843 9.409  1.00 13.10 ? 63  TYR   C OH  1 
ATOM   1548 N  N   . TYR   B 1 58  ? 28.063 -29.237 12.277 1.00 9.66  ? 64  TYR   C N   1 
ATOM   1549 C  CA  . TYR   B 1 58  ? 27.435 -29.410 10.959 1.00 10.20 ? 64  TYR   C CA  1 
ATOM   1550 C  C   . TYR   B 1 58  ? 27.804 -28.275 10.034 1.00 10.16 ? 64  TYR   C C   1 
ATOM   1551 O  O   . TYR   B 1 58  ? 27.577 -27.084 10.356 1.00 11.07 ? 64  TYR   C O   1 
ATOM   1552 C  CB  . TYR   B 1 58  ? 25.922 -29.501 11.055 1.00 10.68 ? 64  TYR   C CB  1 
ATOM   1553 C  CG  . TYR   B 1 58  ? 25.298 -29.789 9.690  1.00 12.04 ? 64  TYR   C CG  1 
ATOM   1554 C  CD1 . TYR   B 1 58  ? 25.633 -30.938 8.981  1.00 12.57 ? 64  TYR   C CD1 1 
ATOM   1555 C  CD2 . TYR   B 1 58  ? 24.449 -28.875 9.086  1.00 11.88 ? 64  TYR   C CD2 1 
ATOM   1556 C  CE1 . TYR   B 1 58  ? 25.122 -31.185 7.699  1.00 12.17 ? 64  TYR   C CE1 1 
ATOM   1557 C  CE2 . TYR   B 1 58  ? 23.886 -29.136 7.831  1.00 12.84 ? 64  TYR   C CE2 1 
ATOM   1558 C  CZ  . TYR   B 1 58  ? 24.249 -30.284 7.138  1.00 12.84 ? 64  TYR   C CZ  1 
ATOM   1559 O  OH  . TYR   B 1 58  ? 23.746 -30.548 5.861  1.00 15.47 ? 64  TYR   C OH  1 
ATOM   1560 N  N   . CYS   B 1 59  ? 28.305 -28.646 8.848  1.00 10.03 ? 65  CYS   C N   1 
ATOM   1561 C  CA  . CYS   B 1 59  ? 28.703 -27.702 7.789  1.00 10.35 ? 65  CYS   C CA  1 
ATOM   1562 C  C   . CYS   B 1 59  ? 27.756 -27.870 6.586  1.00 10.90 ? 65  CYS   C C   1 
ATOM   1563 O  O   . CYS   B 1 59  ? 27.920 -28.826 5.797  1.00 11.96 ? 65  CYS   C O   1 
ATOM   1564 C  CB  . CYS   B 1 59  ? 30.157 -27.944 7.403  1.00 10.73 ? 65  CYS   C CB  1 
ATOM   1565 S  SG  . CYS   B 1 59  ? 30.738 -26.889 6.033  1.00 13.08 ? 65  CYS   C SG  1 
ATOM   1566 N  N   . SER   B 1 60  ? 26.764 -26.966 6.448  1.00 11.83 ? 66  SER   C N   1 
ATOM   1567 C  CA  A SER   B 1 60  ? 25.772 -27.184 5.395  0.50 12.85 ? 66  SER   C CA  1 
ATOM   1568 C  CA  B SER   B 1 60  ? 25.766 -27.139 5.397  0.50 12.04 ? 66  SER   C CA  1 
ATOM   1569 C  C   . SER   B 1 60  ? 26.380 -27.069 3.998  1.00 13.31 ? 66  SER   C C   1 
ATOM   1570 O  O   . SER   B 1 60  ? 25.936 -27.788 3.100  1.00 14.98 ? 66  SER   C O   1 
ATOM   1571 C  CB  A SER   B 1 60  ? 24.587 -26.250 5.562  0.50 15.96 ? 66  SER   C CB  1 
ATOM   1572 C  CB  B SER   B 1 60  ? 24.709 -26.055 5.509  0.50 12.57 ? 66  SER   C CB  1 
ATOM   1573 O  OG  A SER   B 1 60  ? 25.012 -24.903 5.648  0.50 19.12 ? 66  SER   C OG  1 
ATOM   1574 O  OG  B SER   B 1 60  ? 23.712 -26.275 4.524  0.50 12.38 ? 66  SER   C OG  1 
ATOM   1575 N  N   . SER   B 1 61  ? 27.398 -26.216 3.825  1.00 11.68 ? 67  SER   C N   1 
ATOM   1576 C  CA  . SER   B 1 61  ? 28.020 -26.077 2.483  1.00 13.25 ? 67  SER   C CA  1 
ATOM   1577 C  C   . SER   B 1 61  ? 28.820 -27.280 2.046  1.00 14.23 ? 67  SER   C C   1 
ATOM   1578 O  O   . SER   B 1 61  ? 29.269 -27.319 0.896  1.00 14.64 ? 67  SER   C O   1 
ATOM   1579 C  CB  . SER   B 1 61  ? 28.861 -24.812 2.429  1.00 13.42 ? 67  SER   C CB  1 
ATOM   1580 O  OG  . SER   B 1 61  ? 29.977 -24.918 3.278  1.00 14.53 ? 67  SER   C OG  1 
ATOM   1581 N  N   . ARG   B 1 62  ? 29.018 -28.274 2.902  1.00 12.34 ? 68  ARG   C N   1 
ATOM   1582 C  CA  . ARG   B 1 62  ? 29.665 -29.540 2.556  1.00 13.09 ? 68  ARG   C CA  1 
ATOM   1583 C  C   . ARG   B 1 62  ? 28.726 -30.719 2.781  1.00 13.73 ? 68  ARG   C C   1 
ATOM   1584 O  O   . ARG   B 1 62  ? 29.141 -31.875 2.608  1.00 14.87 ? 68  ARG   C O   1 
ATOM   1585 C  CB  . ARG   B 1 62  ? 30.963 -29.726 3.360  1.00 14.19 ? 68  ARG   C CB  1 
ATOM   1586 C  CG  . ARG   B 1 62  ? 31.992 -28.623 3.085  1.00 16.75 ? 68  ARG   C CG  1 
ATOM   1587 C  CD  . ARG   B 1 62  ? 32.657 -28.883 1.762  1.00 16.06 ? 68  ARG   C CD  1 
ATOM   1588 N  NE  . ARG   B 1 62  ? 33.685 -27.872 1.462  1.00 19.21 ? 68  ARG   C NE  1 
ATOM   1589 C  CZ  . ARG   B 1 62  ? 33.465 -26.732 0.834  1.00 22.86 ? 68  ARG   C CZ  1 
ATOM   1590 N  NH1 . ARG   B 1 62  ? 32.245 -26.436 0.378  1.00 25.00 ? 68  ARG   C NH1 1 
ATOM   1591 N  NH2 . ARG   B 1 62  ? 34.481 -25.911 0.555  1.00 24.22 ? 68  ARG   C NH2 1 
ATOM   1592 N  N   . ARG   B 1 63  ? 27.510 -30.466 3.328  1.00 13.73 ? 69  ARG   C N   1 
ATOM   1593 C  CA  . ARG   B 1 63  ? 26.563 -31.524 3.753  1.00 15.63 ? 69  ARG   C CA  1 
ATOM   1594 C  C   . ARG   B 1 63  ? 27.262 -32.562 4.635  1.00 16.50 ? 69  ARG   C C   1 
ATOM   1595 O  O   . ARG   B 1 63  ? 27.111 -33.777 4.434  1.00 18.46 ? 69  ARG   C O   1 
ATOM   1596 C  CB  . ARG   B 1 63  ? 25.921 -32.217 2.537  1.00 17.18 ? 69  ARG   C CB  1 
ATOM   1597 C  CG  . ARG   B 1 63  ? 25.116 -31.315 1.670  1.00 19.49 ? 69  ARG   C CG  1 
ATOM   1598 C  CD  . ARG   B 1 63  ? 23.920 -30.772 2.368  1.00 23.64 ? 69  ARG   C CD  1 
ATOM   1599 N  NE  . ARG   B 1 63  ? 22.896 -30.360 1.413  1.00 28.22 ? 69  ARG   C NE  1 
ATOM   1600 C  CZ  . ARG   B 1 63  ? 22.637 -29.103 1.083  1.00 28.81 ? 69  ARG   C CZ  1 
ATOM   1601 N  NH1 . ARG   B 1 63  ? 23.352 -28.109 1.602  1.00 26.87 ? 69  ARG   C NH1 1 
ATOM   1602 N  NH2 . ARG   B 1 63  ? 21.660 -28.827 0.236  1.00 29.09 ? 69  ARG   C NH2 1 
ATOM   1603 N  N   . LYS   B 1 64  ? 28.106 -32.073 5.571  1.00 13.91 ? 70  LYS   C N   1 
ATOM   1604 C  CA  . LYS   B 1 64  ? 28.920 -32.981 6.368  1.00 14.71 ? 70  LYS   C CA  1 
ATOM   1605 C  C   . LYS   B 1 64  ? 29.041 -32.522 7.804  1.00 13.00 ? 70  LYS   C C   1 
ATOM   1606 O  O   . LYS   B 1 64  ? 29.043 -31.314 8.073  1.00 13.12 ? 70  LYS   C O   1 
ATOM   1607 C  CB  . LYS   B 1 64  ? 30.344 -33.047 5.780  1.00 18.54 ? 70  LYS   C CB  1 
ATOM   1608 C  CG  . LYS   B 1 64  ? 30.480 -34.110 4.683  1.00 30.15 ? 70  LYS   C CG  1 
ATOM   1609 C  CD  . LYS   B 1 64  ? 31.916 -34.460 4.352  1.00 39.32 ? 70  LYS   C CD  1 
ATOM   1610 C  CE  . LYS   B 1 64  ? 31.960 -35.335 3.126  1.00 44.91 ? 70  LYS   C CE  1 
ATOM   1611 N  NZ  . LYS   B 1 64  ? 31.265 -34.695 1.979  1.00 48.63 ? 70  LYS   C NZ  1 
ATOM   1612 N  N   . HIS   B 1 65  ? 29.153 -33.497 8.711  1.00 12.22 ? 71  HIS   C N   1 
ATOM   1613 C  CA  . HIS   B 1 65  ? 29.454 -33.225 10.130 1.00 12.64 ? 71  HIS   C CA  1 
ATOM   1614 C  C   . HIS   B 1 65  ? 30.938 -33.495 10.306 1.00 13.27 ? 71  HIS   C C   1 
ATOM   1615 O  O   . HIS   B 1 65  ? 31.410 -34.578 9.936  1.00 16.24 ? 71  HIS   C O   1 
ATOM   1616 C  CB  . HIS   B 1 65  ? 28.623 -34.133 11.055 1.00 12.48 ? 71  HIS   C CB  1 
ATOM   1617 C  CG  . HIS   B 1 65  ? 27.167 -33.837 11.005 1.00 10.91 ? 71  HIS   C CG  1 
ATOM   1618 N  ND1 . HIS   B 1 65  ? 26.526 -33.086 11.991 1.00 14.56 ? 71  HIS   C ND1 1 
ATOM   1619 C  CD2 . HIS   B 1 65  ? 26.256 -34.243 10.110 1.00 11.00 ? 71  HIS   C CD2 1 
ATOM   1620 C  CE1 . HIS   B 1 65  ? 25.235 -33.088 11.671 1.00 12.71 ? 71  HIS   C CE1 1 
ATOM   1621 N  NE2 . HIS   B 1 65  ? 25.016 -33.778 10.572 1.00 14.60 ? 71  HIS   C NE2 1 
ATOM   1622 N  N   . TYR   B 1 66  ? 31.692 -32.543 10.892 1.00 11.02 ? 72  TYR   C N   1 
ATOM   1623 C  CA  . TYR   B 1 66  ? 33.140 -32.742 11.020 1.00 11.57 ? 72  TYR   C CA  1 
ATOM   1624 C  C   . TYR   B 1 66  ? 33.502 -32.808 12.487 1.00 11.08 ? 72  TYR   C C   1 
ATOM   1625 O  O   . TYR   B 1 66  ? 33.099 -31.900 13.241 1.00 10.68 ? 72  TYR   C O   1 
ATOM   1626 C  CB  . TYR   B 1 66  ? 33.858 -31.495 10.435 1.00 12.72 ? 72  TYR   C CB  1 
ATOM   1627 C  CG  . TYR   B 1 66  ? 33.823 -31.390 8.916  1.00 13.71 ? 72  TYR   C CG  1 
ATOM   1628 C  CD1 . TYR   B 1 66  ? 34.657 -32.160 8.129  1.00 15.46 ? 72  TYR   C CD1 1 
ATOM   1629 C  CD2 . TYR   B 1 66  ? 33.014 -30.459 8.280  1.00 14.70 ? 72  TYR   C CD2 1 
ATOM   1630 C  CE1 . TYR   B 1 66  ? 34.639 -32.055 6.731  1.00 16.07 ? 72  TYR   C CE1 1 
ATOM   1631 C  CE2 . TYR   B 1 66  ? 32.995 -30.332 6.891  1.00 15.94 ? 72  TYR   C CE2 1 
ATOM   1632 C  CZ  . TYR   B 1 66  ? 33.809 -31.132 6.119  1.00 16.60 ? 72  TYR   C CZ  1 
ATOM   1633 O  OH  . TYR   B 1 66  ? 33.792 -30.984 4.732  1.00 18.02 ? 72  TYR   C OH  1 
ATOM   1634 N  N   . PRO   B 1 67  ? 34.335 -33.772 12.888 1.00 10.26 ? 73  PRO   C N   1 
ATOM   1635 C  CA  . PRO   B 1 67  ? 34.867 -33.736 14.260 1.00 10.97 ? 73  PRO   C CA  1 
ATOM   1636 C  C   . PRO   B 1 67  ? 35.968 -32.665 14.369 1.00 12.27 ? 73  PRO   C C   1 
ATOM   1637 O  O   . PRO   B 1 67  ? 36.824 -32.593 13.455 1.00 13.42 ? 73  PRO   C O   1 
ATOM   1638 C  CB  . PRO   B 1 67  ? 35.453 -35.144 14.457 1.00 13.52 ? 73  PRO   C CB  1 
ATOM   1639 C  CG  . PRO   B 1 67  ? 35.769 -35.635 13.070 1.00 14.59 ? 73  PRO   C CG  1 
ATOM   1640 C  CD  . PRO   B 1 67  ? 34.844 -34.926 12.101 1.00 11.68 ? 73  PRO   C CD  1 
ATOM   1641 N  N   . VAL   B 1 68  ? 35.962 -31.857 15.420 1.00 10.55 ? 74  VAL   C N   1 
ATOM   1642 C  CA  . VAL   B 1 68  ? 36.953 -30.770 15.533 1.00 10.91 ? 74  VAL   C CA  1 
ATOM   1643 C  C   . VAL   B 1 68  ? 37.347 -30.597 16.977 1.00 10.73 ? 74  VAL   C C   1 
ATOM   1644 O  O   . VAL   B 1 68  ? 36.581 -30.844 17.910 1.00 10.50 ? 74  VAL   C O   1 
ATOM   1645 C  CB  . VAL   B 1 68  ? 36.344 -29.386 15.051 1.00 12.75 ? 74  VAL   C CB  1 
ATOM   1646 C  CG1 . VAL   B 1 68  ? 36.226 -29.301 13.509 1.00 15.34 ? 74  VAL   C CG1 1 
ATOM   1647 C  CG2 . VAL   B 1 68  ? 34.994 -29.078 15.734 1.00 13.74 ? 74  VAL   C CG2 1 
ATOM   1648 N  N   . SER   B 1 69  ? 38.564 -30.055 17.145 1.00 9.80  ? 75  SER   C N   1 
ATOM   1649 C  CA  . SER   B 1 69  ? 39.045 -29.426 18.382 1.00 10.49 ? 75  SER   C CA  1 
ATOM   1650 C  C   . SER   B 1 69  ? 38.738 -27.928 18.276 1.00 10.27 ? 75  SER   C C   1 
ATOM   1651 O  O   . SER   B 1 69  ? 38.834 -27.326 17.198 1.00 10.40 ? 75  SER   C O   1 
ATOM   1652 C  CB  . SER   B 1 69  ? 40.544 -29.578 18.541 1.00 12.23 ? 75  SER   C CB  1 
ATOM   1653 O  OG  . SER   B 1 69  ? 40.860 -30.958 18.729 1.00 16.19 ? 75  SER   C OG  1 
ATOM   1654 N  N   . PHE   B 1 70  ? 38.281 -27.322 19.373 1.00 9.53  ? 76  PHE   C N   1 
ATOM   1655 C  CA  . PHE   B 1 70  ? 37.923 -25.895 19.351 1.00 9.86  ? 76  PHE   C CA  1 
ATOM   1656 C  C   . PHE   B 1 70  ? 38.450 -25.178 20.588 1.00 10.52 ? 76  PHE   C C   1 
ATOM   1657 O  O   . PHE   B 1 70  ? 38.638 -25.801 21.649 1.00 11.18 ? 76  PHE   C O   1 
ATOM   1658 C  CB  . PHE   B 1 70  ? 36.411 -25.682 19.114 1.00 10.71 ? 76  PHE   C CB  1 
ATOM   1659 C  CG  . PHE   B 1 70  ? 35.516 -26.374 20.124 1.00 9.60  ? 76  PHE   C CG  1 
ATOM   1660 C  CD1 . PHE   B 1 70  ? 35.075 -27.683 19.909 1.00 11.02 ? 76  PHE   C CD1 1 
ATOM   1661 C  CD2 . PHE   B 1 70  ? 35.082 -25.712 21.252 1.00 9.98  ? 76  PHE   C CD2 1 
ATOM   1662 C  CE1 . PHE   B 1 70  ? 34.264 -28.314 20.837 1.00 10.38 ? 76  PHE   C CE1 1 
ATOM   1663 C  CE2 . PHE   B 1 70  ? 34.209 -26.329 22.148 1.00 10.81 ? 76  PHE   C CE2 1 
ATOM   1664 C  CZ  . PHE   B 1 70  ? 33.843 -27.638 21.960 1.00 10.95 ? 76  PHE   C CZ  1 
ATOM   1665 N  N   . SER   B 1 71  ? 38.677 -23.873 20.458 1.00 9.97  ? 77  SER   C N   1 
ATOM   1666 C  CA  . SER   B 1 71  ? 39.316 -23.103 21.539 1.00 11.43 ? 77  SER   C CA  1 
ATOM   1667 C  C   . SER   B 1 71  ? 38.342 -22.743 22.661 1.00 11.37 ? 77  SER   C C   1 
ATOM   1668 O  O   . SER   B 1 71  ? 37.145 -23.030 22.579 1.00 11.82 ? 77  SER   C O   1 
ATOM   1669 C  CB  . SER   B 1 71  ? 40.032 -21.882 20.952 1.00 12.40 ? 77  SER   C CB  1 
ATOM   1670 O  OG  . SER   B 1 71  ? 39.098 -20.991 20.356 1.00 13.17 ? 77  SER   C OG  1 
ATOM   1671 N  N   . LYS   B 1 72  ? 38.849 -22.059 23.680 1.00 11.54 ? 78  LYS   C N   1 
ATOM   1672 C  CA  . LYS   B 1 72  ? 37.999 -21.637 24.816 1.00 11.42 ? 78  LYS   C CA  1 
ATOM   1673 C  C   . LYS   B 1 72  ? 37.302 -20.318 24.423 1.00 13.27 ? 78  LYS   C C   1 
ATOM   1674 O  O   . LYS   B 1 72  ? 37.885 -19.499 23.710 1.00 14.50 ? 78  LYS   C O   1 
ATOM   1675 C  CB  . LYS   B 1 72  ? 38.920 -21.370 26.020 1.00 13.09 ? 78  LYS   C CB  1 
ATOM   1676 C  CG  . LYS   B 1 72  ? 39.613 -22.634 26.499 1.00 15.86 ? 78  LYS   C CG  1 
ATOM   1677 C  CD  . LYS   B 1 72  ? 40.553 -22.314 27.670 1.00 23.63 ? 78  LYS   C CD  1 
ATOM   1678 C  CE  . LYS   B 1 72  ? 41.448 -23.443 28.080 1.00 34.17 ? 78  LYS   C CE  1 
ATOM   1679 N  NZ  . LYS   B 1 72  ? 42.416 -22.985 29.126 1.00 39.45 ? 78  LYS   C NZ  1 
ATOM   1680 N  N   . PRO   B 1 73  ? 36.069 -20.067 24.881 1.00 11.83 ? 79  PRO   C N   1 
ATOM   1681 C  CA  . PRO   B 1 73  ? 35.342 -18.805 24.481 1.00 12.31 ? 79  PRO   C CA  1 
ATOM   1682 C  C   . PRO   B 1 73  ? 36.133 -17.563 24.841 1.00 13.57 ? 79  PRO   C C   1 
ATOM   1683 O  O   . PRO   B 1 73  ? 36.593 -17.409 25.998 1.00 14.72 ? 79  PRO   C O   1 
ATOM   1684 C  CB  . PRO   B 1 73  ? 34.037 -18.831 25.286 1.00 13.44 ? 79  PRO   C CB  1 
ATOM   1685 C  CG  . PRO   B 1 73  ? 33.913 -20.238 25.772 1.00 15.64 ? 79  PRO   C CG  1 
ATOM   1686 C  CD  . PRO   B 1 73  ? 35.273 -20.919 25.792 1.00 12.85 ? 79  PRO   C CD  1 
ATOM   1687 N  N   . SER   B 1 74  ? 36.329 -16.682 23.853 1.00 11.74 ? 80  SER   C N   1 
ATOM   1688 C  CA  . SER   B 1 74  ? 37.160 -15.507 24.096 1.00 12.23 ? 80  SER   C CA  1 
ATOM   1689 C  C   . SER   B 1 74  ? 36.798 -14.370 23.148 1.00 12.60 ? 80  SER   C C   1 
ATOM   1690 O  O   . SER   B 1 74  ? 35.938 -14.530 22.277 1.00 12.57 ? 80  SER   C O   1 
ATOM   1691 C  CB  . SER   B 1 74  ? 38.638 -15.872 23.942 1.00 14.76 ? 80  SER   C CB  1 
ATOM   1692 O  OG  . SER   B 1 74  ? 39.023 -16.138 22.601 1.00 18.25 ? 80  SER   C OG  1 
ATOM   1693 N  N   . LEU   B 1 75  ? 37.441 -13.203 23.340 1.00 13.54 ? 81  LEU   C N   1 
ATOM   1694 C  CA  . LEU   B 1 75  ? 37.231 -12.000 22.529 1.00 14.06 ? 81  LEU   C CA  1 
ATOM   1695 C  C   . LEU   B 1 75  ? 38.251 -12.037 21.388 1.00 14.11 ? 81  LEU   C C   1 
ATOM   1696 O  O   . LEU   B 1 75  ? 39.474 -11.948 21.640 1.00 15.95 ? 81  LEU   C O   1 
ATOM   1697 C  CB  . LEU   B 1 75  ? 37.462 -10.741 23.416 1.00 15.31 ? 81  LEU   C CB  1 
ATOM   1698 C  CG  . LEU   B 1 75  ? 37.234 -9.416  22.751 1.00 17.55 ? 81  LEU   C CG  1 
ATOM   1699 C  CD1 . LEU   B 1 75  ? 35.751 -9.232  22.464 1.00 17.52 ? 81  LEU   C CD1 1 
ATOM   1700 C  CD2 . LEU   B 1 75  ? 37.762 -8.273  23.674 1.00 20.13 ? 81  LEU   C CD2 1 
ATOM   1701 N  N   . ILE   B 1 76  ? 37.778 -12.236 20.146 1.00 13.44 ? 82  ILE   C N   1 
ATOM   1702 C  CA  . ILE   B 1 76  ? 38.611 -12.471 18.954 1.00 13.31 ? 82  ILE   C CA  1 
ATOM   1703 C  C   . ILE   B 1 76  ? 38.323 -11.433 17.894 1.00 13.56 ? 82  ILE   C C   1 
ATOM   1704 O  O   . ILE   B 1 76  ? 37.149 -11.101 17.652 1.00 13.26 ? 82  ILE   C O   1 
ATOM   1705 C  CB  . ILE   B 1 76  ? 38.294 -13.875 18.409 1.00 16.47 ? 82  ILE   C CB  1 
ATOM   1706 C  CG1 . ILE   B 1 76  ? 38.746 -14.923 19.436 1.00 20.47 ? 82  ILE   C CG1 1 
ATOM   1707 C  CG2 . ILE   B 1 76  ? 38.908 -14.111 16.992 1.00 18.22 ? 82  ILE   C CG2 1 
ATOM   1708 C  CD1 . ILE   B 1 76  ? 38.482 -16.278 19.076 1.00 22.19 ? 82  ILE   C CD1 1 
ATOM   1709 N  N   . PHE   B 1 77  ? 39.396 -10.974 17.222 1.00 14.23 ? 83  PHE   C N   1 
ATOM   1710 C  CA  . PHE   B 1 77  ? 39.205 -10.036 16.130 1.00 14.63 ? 83  PHE   C CA  1 
ATOM   1711 C  C   . PHE   B 1 77  ? 38.834 -10.885 14.893 1.00 16.21 ? 83  PHE   C C   1 
ATOM   1712 O  O   . PHE   B 1 77  ? 39.600 -11.797 14.470 1.00 17.95 ? 83  PHE   C O   1 
ATOM   1713 C  CB  . PHE   B 1 77  ? 40.498 -9.249  15.857 1.00 15.21 ? 83  PHE   C CB  1 
ATOM   1714 C  CG  . PHE   B 1 77  ? 40.211 -8.118  14.889 1.00 16.35 ? 83  PHE   C CG  1 
ATOM   1715 C  CD1 . PHE   B 1 77  ? 39.532 -6.988  15.303 1.00 17.19 ? 83  PHE   C CD1 1 
ATOM   1716 C  CD2 . PHE   B 1 77  ? 40.552 -8.225  13.542 1.00 17.93 ? 83  PHE   C CD2 1 
ATOM   1717 C  CE1 . PHE   B 1 77  ? 39.217 -5.969  14.403 1.00 19.09 ? 83  PHE   C CE1 1 
ATOM   1718 C  CE2 . PHE   B 1 77  ? 40.253 -7.196  12.648 1.00 19.43 ? 83  PHE   C CE2 1 
ATOM   1719 C  CZ  . PHE   B 1 77  ? 39.595 -6.076  13.082 1.00 19.36 ? 83  PHE   C CZ  1 
ATOM   1720 N  N   . VAL   B 1 78  ? 37.678 -10.547 14.293 1.00 13.22 ? 84  VAL   C N   1 
ATOM   1721 C  CA  . VAL   B 1 78  ? 37.158 -11.280 13.136 1.00 14.14 ? 84  VAL   C CA  1 
ATOM   1722 C  C   . VAL   B 1 78  ? 37.226 -10.342 11.935 1.00 13.57 ? 84  VAL   C C   1 
ATOM   1723 O  O   . VAL   B 1 78  ? 36.789 -9.180  12.037 1.00 14.16 ? 84  VAL   C O   1 
ATOM   1724 C  CB  . VAL   B 1 78  ? 35.700 -11.713 13.431 1.00 14.11 ? 84  VAL   C CB  1 
ATOM   1725 C  CG1 . VAL   B 1 78  ? 35.122 -12.531 12.274 1.00 14.50 ? 84  VAL   C CG1 1 
ATOM   1726 C  CG2 . VAL   B 1 78  ? 35.597 -12.503 14.742 1.00 15.24 ? 84  VAL   C CG2 1 
ATOM   1727 N  N   . GLU   B 1 79  ? 37.727 -10.833 10.784 1.00 12.63 ? 85  GLU   C N   1 
ATOM   1728 C  CA  . GLU   B 1 79  ? 37.753 -10.007 9.573  1.00 13.21 ? 85  GLU   C CA  1 
ATOM   1729 C  C   . GLU   B 1 79  ? 36.347 -9.786  9.015  1.00 13.62 ? 85  GLU   C C   1 
ATOM   1730 O  O   . GLU   B 1 79  ? 35.379 -10.438 9.432  1.00 13.99 ? 85  GLU   C O   1 
ATOM   1731 C  CB  . GLU   B 1 79  ? 38.652 -10.603 8.476  1.00 14.87 ? 85  GLU   C CB  1 
ATOM   1732 C  CG  . GLU   B 1 79  ? 40.128 -10.644 8.893  1.00 16.99 ? 85  GLU   C CG  1 
ATOM   1733 C  CD  . GLU   B 1 79  ? 40.723 -9.263  9.130  1.00 22.94 ? 85  GLU   C CD  1 
ATOM   1734 O  OE1 . GLU   B 1 79  ? 40.342 -8.267  8.458  1.00 26.92 ? 85  GLU   C OE1 1 
ATOM   1735 O  OE2 . GLU   B 1 79  ? 41.636 -9.177  9.983  1.00 24.66 ? 85  GLU   C OE2 1 
ATOM   1736 N  N   . ALA   B 1 80  ? 36.204 -8.778  8.110  1.00 14.69 ? 86  ALA   C N   1 
ATOM   1737 C  CA  . ALA   B 1 80  ? 34.892 -8.477  7.560  1.00 15.32 ? 86  ALA   C CA  1 
ATOM   1738 C  C   . ALA   B 1 80  ? 34.280 -9.684  6.867  1.00 15.78 ? 86  ALA   C C   1 
ATOM   1739 O  O   . ALA   B 1 80  ? 34.994 -10.468 6.231  1.00 16.55 ? 86  ALA   C O   1 
ATOM   1740 C  CB  . ALA   B 1 80  ? 35.032 -7.338  6.555  1.00 16.37 ? 86  ALA   C CB  1 
ATOM   1741 N  N   . SER   B 1 81  ? 32.956 -9.815  6.999  1.00 14.25 ? 87  SER   C N   1 
ATOM   1742 C  CA  . SER   B 1 81  ? 32.231 -10.843 6.301  1.00 15.55 ? 87  SER   C CA  1 
ATOM   1743 C  C   . SER   B 1 81  ? 31.088 -10.183 5.517  1.00 15.74 ? 87  SER   C C   1 
ATOM   1744 O  O   . SER   B 1 81  ? 30.926 -8.934  5.522  1.00 16.18 ? 87  SER   C O   1 
ATOM   1745 C  CB  . SER   B 1 81  ? 31.643 -11.828 7.310  1.00 15.40 ? 87  SER   C CB  1 
ATOM   1746 O  OG  . SER   B 1 81  ? 30.625 -11.188 8.091  1.00 14.99 ? 87  SER   C OG  1 
ATOM   1747 N  N   . GLU   B 1 82  ? 30.255 -11.005 4.885  1.00 17.23 ? 88  GLU   C N   1 
ATOM   1748 C  CA  . GLU   B 1 82  ? 29.142 -10.394 4.150  1.00 18.38 ? 88  GLU   C CA  1 
ATOM   1749 C  C   . GLU   B 1 82  ? 28.094 -9.720  5.093  1.00 18.44 ? 88  GLU   C C   1 
ATOM   1750 O  O   . GLU   B 1 82  ? 27.301 -8.873  4.645  1.00 20.23 ? 88  GLU   C O   1 
ATOM   1751 C  CB  . GLU   B 1 82  ? 28.507 -11.383 3.167  1.00 23.14 ? 88  GLU   C CB  1 
ATOM   1752 C  CG  . GLU   B 1 82  ? 27.595 -12.415 3.769  1.00 32.37 ? 88  GLU   C CG  1 
ATOM   1753 C  CD  . GLU   B 1 82  ? 26.833 -13.188 2.704  1.00 40.45 ? 88  GLU   C CD  1 
ATOM   1754 O  OE1 . GLU   B 1 82  ? 27.407 -13.415 1.612  1.00 41.21 ? 88  GLU   C OE1 1 
ATOM   1755 O  OE2 . GLU   B 1 82  ? 25.666 -13.567 2.966  1.00 41.83 ? 88  GLU   C OE2 1 
ATOM   1756 N  N   . TYR   B 1 83  ? 28.116 -10.050 6.392  1.00 15.65 ? 89  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 83  ? 27.094 -9.555  7.316  1.00 14.95 ? 89  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 83  ? 27.610 -8.673  8.491  1.00 15.12 ? 89  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 83  ? 26.771 -8.112  9.200  1.00 16.35 ? 89  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 83  ? 26.242 -10.737 7.841  1.00 15.03 ? 89  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 83  ? 27.076 -11.931 8.299  1.00 14.49 ? 89  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 83  ? 27.438 -12.940 7.409  1.00 15.77 ? 89  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 83  ? 27.512 -12.041 9.613  1.00 13.96 ? 89  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 83  ? 28.230 -14.016 7.816  1.00 14.62 ? 89  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 83  ? 28.290 -13.120 10.037 1.00 14.76 ? 89  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 83  ? 28.673 -14.093 9.125  1.00 14.55 ? 89  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 83  ? 29.464 -15.173 9.492  1.00 15.20 ? 89  TYR   C OH  1 
ATOM   1768 N  N   . TYR   B 1 84  ? 28.933 -8.573  8.748  1.00 13.89 ? 90  TYR   C N   1 
ATOM   1769 C  CA  . TYR   B 1 84  ? 29.499 -7.680  9.762  1.00 13.49 ? 90  TYR   C CA  1 
ATOM   1770 C  C   . TYR   B 1 84  ? 30.816 -7.087  9.230  1.00 13.79 ? 90  TYR   C C   1 
ATOM   1771 O  O   . TYR   B 1 84  ? 31.538 -7.737  8.457  1.00 14.06 ? 90  TYR   C O   1 
ATOM   1772 C  CB  . TYR   B 1 84  ? 29.868 -8.451  11.071 1.00 13.46 ? 90  TYR   C CB  1 
ATOM   1773 C  CG  . TYR   B 1 84  ? 28.703 -8.858  11.943 1.00 12.96 ? 90  TYR   C CG  1 
ATOM   1774 C  CD1 . TYR   B 1 84  ? 27.800 -7.918  12.442 1.00 13.87 ? 90  TYR   C CD1 1 
ATOM   1775 C  CD2 . TYR   B 1 84  ? 28.509 -10.173 12.282 1.00 12.56 ? 90  TYR   C CD2 1 
ATOM   1776 C  CE1 . TYR   B 1 84  ? 26.745 -8.298  13.293 1.00 12.90 ? 90  TYR   C CE1 1 
ATOM   1777 C  CE2 . TYR   B 1 84  ? 27.434 -10.571 13.083 1.00 12.83 ? 90  TYR   C CE2 1 
ATOM   1778 C  CZ  . TYR   B 1 84  ? 26.575 -9.631  13.626 1.00 12.80 ? 90  TYR   C CZ  1 
ATOM   1779 O  OH  . TYR   B 1 84  ? 25.512 -10.002 14.465 1.00 12.97 ? 90  TYR   C OH  1 
ATOM   1780 N  N   . PRO   B 1 85  ? 31.166 -5.865  9.664  1.00 14.43 ? 91  PRO   C N   1 
ATOM   1781 C  CA  . PRO   B 1 85  ? 32.509 -5.348  9.357  1.00 13.73 ? 91  PRO   C CA  1 
ATOM   1782 C  C   . PRO   B 1 85  ? 33.549 -6.115  10.198 1.00 14.20 ? 91  PRO   C C   1 
ATOM   1783 O  O   . PRO   B 1 85  ? 33.188 -6.944  11.097 1.00 14.43 ? 91  PRO   C O   1 
ATOM   1784 C  CB  . PRO   B 1 85  ? 32.409 -3.881  9.822  1.00 14.35 ? 91  PRO   C CB  1 
ATOM   1785 C  CG  . PRO   B 1 85  ? 31.437 -3.942  11.031 1.00 15.55 ? 91  PRO   C CG  1 
ATOM   1786 C  CD  . PRO   B 1 85  ? 30.418 -5.014  10.634 1.00 15.08 ? 91  PRO   C CD  1 
ATOM   1787 N  N   . ALA   B 1 86  ? 34.845 -5.825  9.953  1.00 14.61 ? 92  ALA   C N   1 
ATOM   1788 C  CA  . ALA   B 1 86  ? 35.910 -6.369  10.798 1.00 15.17 ? 92  ALA   C CA  1 
ATOM   1789 C  C   . ALA   B 1 86  ? 35.715 -5.812  12.227 1.00 15.57 ? 92  ALA   C C   1 
ATOM   1790 O  O   . ALA   B 1 86  ? 35.456 -4.599  12.374 1.00 17.68 ? 92  ALA   C O   1 
ATOM   1791 C  CB  . ALA   B 1 86  ? 37.284 -5.973  10.242 1.00 15.65 ? 92  ALA   C CB  1 
ATOM   1792 N  N   . ARG   B 1 87  ? 35.757 -6.686  13.238 1.00 14.78 ? 93  ARG   C N   1 
ATOM   1793 C  CA  . ARG   B 1 87  ? 35.433 -6.245  14.597 1.00 13.81 ? 93  ARG   C CA  1 
ATOM   1794 C  C   . ARG   B 1 87  ? 35.846 -7.316  15.602 1.00 14.50 ? 93  ARG   C C   1 
ATOM   1795 O  O   . ARG   B 1 87  ? 36.099 -8.480  15.245 1.00 14.38 ? 93  ARG   C O   1 
ATOM   1796 C  CB  . ARG   B 1 87  ? 33.881 -5.983  14.733 1.00 15.16 ? 93  ARG   C CB  1 
ATOM   1797 C  CG  . ARG   B 1 87  ? 33.087 -7.294  14.648 1.00 14.52 ? 93  ARG   C CG  1 
ATOM   1798 C  CD  . ARG   B 1 87  ? 31.571 -7.058  14.740 1.00 15.08 ? 93  ARG   C CD  1 
ATOM   1799 N  NE  . ARG   B 1 87  ? 30.904 -8.343  14.990 1.00 15.01 ? 93  ARG   C NE  1 
ATOM   1800 C  CZ  . ARG   B 1 87  ? 29.850 -8.522  15.781 1.00 16.99 ? 93  ARG   C CZ  1 
ATOM   1801 N  NH1 . ARG   B 1 87  ? 29.228 -7.477  16.323 1.00 17.58 ? 93  ARG   C NH1 1 
ATOM   1802 N  NH2 . ARG   B 1 87  ? 29.399 -9.753  16.024 1.00 15.90 ? 93  ARG   C NH2 1 
ATOM   1803 N  N   . TYR   B 1 88  ? 35.809 -6.952  16.888 1.00 14.77 ? 94  TYR   C N   1 
ATOM   1804 C  CA  . TYR   B 1 88  ? 35.971 -7.946  17.952 1.00 15.28 ? 94  TYR   C CA  1 
ATOM   1805 C  C   . TYR   B 1 88  ? 34.618 -8.580  18.210 1.00 13.74 ? 94  TYR   C C   1 
ATOM   1806 O  O   . TYR   B 1 88  ? 33.599 -7.883  18.334 1.00 16.00 ? 94  TYR   C O   1 
ATOM   1807 C  CB  . TYR   B 1 88  ? 36.472 -7.242  19.249 1.00 16.71 ? 94  TYR   C CB  1 
ATOM   1808 C  CG  . TYR   B 1 88  ? 37.946 -6.925  19.142 1.00 17.79 ? 94  TYR   C CG  1 
ATOM   1809 C  CD1 . TYR   B 1 88  ? 38.899 -7.897  19.378 1.00 18.83 ? 94  TYR   C CD1 1 
ATOM   1810 C  CD2 . TYR   B 1 88  ? 38.383 -5.642  18.812 1.00 18.68 ? 94  TYR   C CD2 1 
ATOM   1811 C  CE1 . TYR   B 1 88  ? 40.262 -7.626  19.241 1.00 20.09 ? 94  TYR   C CE1 1 
ATOM   1812 C  CE2 . TYR   B 1 88  ? 39.738 -5.366  18.649 1.00 20.05 ? 94  TYR   C CE2 1 
ATOM   1813 C  CZ  . TYR   B 1 88  ? 40.676 -6.348  18.913 1.00 20.86 ? 94  TYR   C CZ  1 
ATOM   1814 O  OH  . TYR   B 1 88  ? 42.030 -6.087  18.786 1.00 23.17 ? 94  TYR   C OH  1 
ATOM   1815 N  N   . GLN   B 1 89  ? 34.602 -9.917  18.315 1.00 12.64 ? 95  GLN   C N   1 
ATOM   1816 C  CA  . GLN   B 1 89  ? 33.389 -10.664 18.678 1.00 13.14 ? 95  GLN   C CA  1 
ATOM   1817 C  C   . GLN   B 1 89  ? 33.719 -11.396 19.968 1.00 12.82 ? 95  GLN   C C   1 
ATOM   1818 O  O   . GLN   B 1 89  ? 34.813 -11.994 20.087 1.00 13.85 ? 95  GLN   C O   1 
ATOM   1819 C  CB  . GLN   B 1 89  ? 33.002 -11.635 17.558 1.00 12.99 ? 95  GLN   C CB  1 
ATOM   1820 C  CG  . GLN   B 1 89  ? 31.739 -12.440 17.885 1.00 14.27 ? 95  GLN   C CG  1 
ATOM   1821 C  CD  . GLN   B 1 89  ? 31.054 -13.023 16.659 1.00 12.62 ? 95  GLN   C CD  1 
ATOM   1822 O  OE1 . GLN   B 1 89  ? 31.032 -12.428 15.542 1.00 14.31 ? 95  GLN   C OE1 1 
ATOM   1823 N  NE2 . GLN   B 1 89  ? 30.471 -14.189 16.851 1.00 13.85 ? 95  GLN   C NE2 1 
ATOM   1824 N  N   . SER   B 1 90  ? 32.819 -11.366 20.938 1.00 11.39 ? 96  SER   C N   1 
ATOM   1825 C  CA  . SER   B 1 90  ? 33.036 -12.014 22.230 1.00 12.32 ? 96  SER   C CA  1 
ATOM   1826 C  C   . SER   B 1 90  ? 32.422 -13.430 22.304 1.00 11.94 ? 96  SER   C C   1 
ATOM   1827 O  O   . SER   B 1 90  ? 31.552 -13.779 21.501 1.00 11.52 ? 96  SER   C O   1 
ATOM   1828 C  CB  . SER   B 1 90  ? 32.504 -11.139 23.385 1.00 13.97 ? 96  SER   C CB  1 
ATOM   1829 O  OG  . SER   B 1 90  ? 31.090 -11.069 23.299 1.00 15.00 ? 96  SER   C OG  1 
ATOM   1830 N  N   . HIS   B 1 91  ? 32.893 -14.223 23.315 1.00 11.30 ? 97  HIS   C N   1 
ATOM   1831 C  CA  . HIS   B 1 91  ? 32.413 -15.578 23.570 1.00 11.35 ? 97  HIS   C CA  1 
ATOM   1832 C  C   . HIS   B 1 91  ? 32.496 -16.454 22.316 1.00 11.83 ? 97  HIS   C C   1 
ATOM   1833 O  O   . HIS   B 1 91  ? 31.609 -17.284 22.071 1.00 12.30 ? 97  HIS   C O   1 
ATOM   1834 C  CB  . HIS   B 1 91  ? 30.961 -15.538 24.130 1.00 12.36 ? 97  HIS   C CB  1 
ATOM   1835 C  CG  . HIS   B 1 91  ? 30.846 -14.786 25.448 1.00 13.96 ? 97  HIS   C CG  1 
ATOM   1836 N  ND1 . HIS   B 1 91  ? 30.867 -15.451 26.667 1.00 16.78 ? 97  HIS   C ND1 1 
ATOM   1837 C  CD2 . HIS   B 1 91  ? 30.769 -13.443 25.681 1.00 15.18 ? 97  HIS   C CD2 1 
ATOM   1838 C  CE1 . HIS   B 1 91  ? 30.774 -14.509 27.604 1.00 16.84 ? 97  HIS   C CE1 1 
ATOM   1839 N  NE2 . HIS   B 1 91  ? 30.659 -13.287 27.062 1.00 16.68 ? 97  HIS   C NE2 1 
ATOM   1840 N  N   . LEU   B 1 92  ? 33.558 -16.260 21.540 1.00 10.59 ? 98  LEU   C N   1 
ATOM   1841 C  CA  . LEU   B 1 92  ? 33.769 -16.963 20.284 1.00 10.44 ? 98  LEU   C CA  1 
ATOM   1842 C  C   . LEU   B 1 92  ? 34.833 -18.047 20.465 1.00 10.40 ? 98  LEU   C C   1 
ATOM   1843 O  O   . LEU   B 1 92  ? 35.828 -17.831 21.175 1.00 11.31 ? 98  LEU   C O   1 
ATOM   1844 C  CB  . LEU   B 1 92  ? 34.224 -15.952 19.174 1.00 11.58 ? 98  LEU   C CB  1 
ATOM   1845 C  CG  . LEU   B 1 92  ? 34.308 -16.484 17.749 1.00 12.31 ? 98  LEU   C CG  1 
ATOM   1846 C  CD1 . LEU   B 1 92  ? 32.934 -16.861 17.206 1.00 12.15 ? 98  LEU   C CD1 1 
ATOM   1847 C  CD2 . LEU   B 1 92  ? 34.990 -15.446 16.786 1.00 14.40 ? 98  LEU   C CD2 1 
ATOM   1848 N  N   . MET   B 1 93  ? 34.641 -19.203 19.822 1.00 10.58 ? 99  MET   C N   1 
ATOM   1849 C  CA  . MET   B 1 93  ? 35.595 -20.316 19.868 1.00 10.25 ? 99  MET   C CA  1 
ATOM   1850 C  C   . MET   B 1 93  ? 35.982 -20.655 18.432 1.00 10.52 ? 99  MET   C C   1 
ATOM   1851 O  O   . MET   B 1 93  ? 35.092 -20.728 17.593 1.00 11.08 ? 99  MET   C O   1 
ATOM   1852 C  CB  . MET   B 1 93  ? 34.895 -21.543 20.436 1.00 11.80 ? 99  MET   C CB  1 
ATOM   1853 C  CG  . MET   B 1 93  ? 34.441 -21.271 21.862 1.00 12.64 ? 99  MET   C CG  1 
ATOM   1854 S  SD  . MET   B 1 93  ? 33.397 -22.590 22.552 1.00 13.34 ? 99  MET   C SD  1 
ATOM   1855 C  CE  . MET   B 1 93  ? 31.960 -22.503 21.455 1.00 14.08 ? 99  MET   C CE  1 
ATOM   1856 N  N   . LEU   B 1 94  ? 37.258 -20.882 18.130 1.00 10.22 ? 100 LEU   C N   1 
ATOM   1857 C  CA  . LEU   B 1 94  ? 37.676 -21.200 16.767 1.00 11.19 ? 100 LEU   C CA  1 
ATOM   1858 C  C   . LEU   B 1 94  ? 38.087 -22.667 16.638 1.00 10.71 ? 100 LEU   C C   1 
ATOM   1859 O  O   . LEU   B 1 94  ? 38.607 -23.273 17.579 1.00 11.33 ? 100 LEU   C O   1 
ATOM   1860 C  CB  . LEU   B 1 94  ? 38.910 -20.347 16.372 1.00 11.81 ? 100 LEU   C CB  1 
ATOM   1861 C  CG  . LEU   B 1 94  ? 38.753 -18.851 16.330 1.00 12.14 ? 100 LEU   C CG  1 
ATOM   1862 C  CD1 . LEU   B 1 94  ? 40.097 -18.208 15.848 1.00 15.16 ? 100 LEU   C CD1 1 
ATOM   1863 C  CD2 . LEU   B 1 94  ? 37.532 -18.416 15.469 1.00 13.60 ? 100 LEU   C CD2 1 
ATOM   1864 N  N   . ALA   B 1 95  ? 37.952 -23.197 15.423 1.00 11.18 ? 101 ALA   C N   1 
ATOM   1865 C  CA  . ALA   B 1 95  ? 38.475 -24.506 15.024 1.00 11.16 ? 101 ALA   C CA  1 
ATOM   1866 C  C   . ALA   B 1 95  ? 39.023 -24.379 13.587 1.00 10.53 ? 101 ALA   C C   1 
ATOM   1867 O  O   . ALA   B 1 95  ? 38.640 -23.444 12.873 1.00 10.50 ? 101 ALA   C O   1 
ATOM   1868 C  CB  . ALA   B 1 95  ? 37.373 -25.570 15.050 1.00 11.72 ? 101 ALA   C CB  1 
ATOM   1869 N  N   . VAL   B 1 96  ? 39.861 -25.322 13.162 1.00 10.75 ? 102 VAL   C N   1 
ATOM   1870 C  CA  . VAL   B 1 96  ? 40.308 -25.369 11.778 1.00 11.31 ? 102 VAL   C CA  1 
ATOM   1871 C  C   . VAL   B 1 96  ? 39.245 -26.119 10.978 1.00 12.15 ? 102 VAL   C C   1 
ATOM   1872 O  O   . VAL   B 1 96  ? 38.972 -27.310 11.238 1.00 13.70 ? 102 VAL   C O   1 
ATOM   1873 C  CB  . VAL   B 1 96  ? 41.666 -26.103 11.703 1.00 13.36 ? 102 VAL   C CB  1 
ATOM   1874 C  CG1 . VAL   B 1 96  ? 42.094 -26.205 10.238 1.00 14.94 ? 102 VAL   C CG1 1 
ATOM   1875 C  CG2 . VAL   B 1 96  ? 42.713 -25.352 12.535 1.00 14.72 ? 102 VAL   C CG2 1 
ATOM   1876 N  N   . GLY   B 1 97  ? 38.614 -25.411 10.045 1.00 12.82 ? 103 GLY   C N   1 
ATOM   1877 C  CA  . GLY   B 1 97  ? 37.532 -26.033 9.280  1.00 13.54 ? 103 GLY   C CA  1 
ATOM   1878 C  C   . GLY   B 1 97  ? 36.891 -25.064 8.350  1.00 13.92 ? 103 GLY   C C   1 
ATOM   1879 O  O   . GLY   B 1 97  ? 37.131 -23.840 8.412  1.00 15.53 ? 103 GLY   C O   1 
ATOM   1880 N  N   . HIS   B 1 98  ? 36.010 -25.600 7.513  1.00 13.74 ? 104 HIS   C N   1 
ATOM   1881 C  CA  . HIS   B 1 98  ? 35.321 -24.789 6.537  1.00 13.93 ? 104 HIS   C CA  1 
ATOM   1882 C  C   . HIS   B 1 98  ? 34.052 -24.115 7.081  1.00 12.97 ? 104 HIS   C C   1 
ATOM   1883 O  O   . HIS   B 1 98  ? 33.259 -24.740 7.807  1.00 13.26 ? 104 HIS   C O   1 
ATOM   1884 C  CB  . HIS   B 1 98  ? 34.943 -25.679 5.365  1.00 16.15 ? 104 HIS   C CB  1 
ATOM   1885 C  CG  . HIS   B 1 98  ? 34.376 -24.888 4.255  1.00 19.55 ? 104 HIS   C CG  1 
ATOM   1886 N  ND1 . HIS   B 1 98  ? 35.148 -23.947 3.553  1.00 21.51 ? 104 HIS   C ND1 1 
ATOM   1887 C  CD2 . HIS   B 1 98  ? 33.114 -24.870 3.787  1.00 21.73 ? 104 HIS   C CD2 1 
ATOM   1888 C  CE1 . HIS   B 1 98  ? 34.320 -23.384 2.691  1.00 23.29 ? 104 HIS   C CE1 1 
ATOM   1889 N  NE2 . HIS   B 1 98  ? 33.089 -23.918 2.773  1.00 23.64 ? 104 HIS   C NE2 1 
ATOM   1890 N  N   . SER   B 1 99  ? 33.815 -22.846 6.699  1.00 13.06 ? 105 SER   C N   1 
ATOM   1891 C  CA  . SER   B 1 99  ? 32.618 -22.077 7.082  1.00 14.21 ? 105 SER   C CA  1 
ATOM   1892 C  C   . SER   B 1 99  ? 32.395 -20.926 6.105  1.00 16.01 ? 105 SER   C C   1 
ATOM   1893 O  O   . SER   B 1 99  ? 33.267 -20.057 5.970  1.00 18.30 ? 105 SER   C O   1 
ATOM   1894 C  CB  . SER   B 1 99  ? 32.874 -21.490 8.467  1.00 16.43 ? 105 SER   C CB  1 
ATOM   1895 O  OG  . SER   B 1 99  ? 31.780 -20.688 8.898  1.00 17.73 ? 105 SER   C OG  1 
ATOM   1896 N  N   . GLU   B 1 100 ? 31.240 -20.929 5.425  1.00 15.47 ? 106 GLU   C N   1 
ATOM   1897 C  CA  . GLU   B 1 100 ? 30.797 -19.859 4.527  1.00 16.15 ? 106 GLU   C CA  1 
ATOM   1898 C  C   . GLU   B 1 100 ? 29.615 -19.186 5.196  1.00 15.13 ? 106 GLU   C C   1 
ATOM   1899 O  O   . GLU   B 1 100 ? 29.041 -19.701 6.161  1.00 15.06 ? 106 GLU   C O   1 
ATOM   1900 C  CB  . GLU   B 1 100 ? 30.291 -20.494 3.216  1.00 20.54 ? 106 GLU   C CB  1 
ATOM   1901 C  CG  . GLU   B 1 100 ? 31.408 -20.954 2.322  1.00 31.30 ? 106 GLU   C CG  1 
ATOM   1902 C  CD  . GLU   B 1 100 ? 30.916 -21.853 1.214  1.00 35.19 ? 106 GLU   C CD  1 
ATOM   1903 O  OE1 . GLU   B 1 100 ? 29.722 -21.789 0.831  1.00 39.13 ? 106 GLU   C OE1 1 
ATOM   1904 O  OE2 . GLU   B 1 100 ? 31.743 -22.673 0.765  1.00 37.59 ? 106 GLU   C OE2 1 
ATOM   1905 N  N   . PRO   B 1 101 ? 29.209 -17.991 4.722  1.00 15.60 ? 107 PRO   C N   1 
ATOM   1906 C  CA  . PRO   B 1 101 ? 28.088 -17.313 5.373  1.00 15.55 ? 107 PRO   C CA  1 
ATOM   1907 C  C   . PRO   B 1 101 ? 26.840 -18.167 5.579  1.00 15.57 ? 107 PRO   C C   1 
ATOM   1908 O  O   . PRO   B 1 101 ? 26.240 -18.127 6.659  1.00 15.52 ? 107 PRO   C O   1 
ATOM   1909 C  CB  . PRO   B 1 101 ? 27.810 -16.097 4.454  1.00 17.29 ? 107 PRO   C CB  1 
ATOM   1910 C  CG  . PRO   B 1 101 ? 29.092 -15.848 3.790  1.00 20.28 ? 107 PRO   C CG  1 
ATOM   1911 C  CD  . PRO   B 1 101 ? 29.821 -17.163 3.650  1.00 17.98 ? 107 PRO   C CD  1 
ATOM   1912 N  N   . GLY   B 1 102 ? 26.487 -19.002 4.601  1.00 13.99 ? 108 GLY   C N   1 
ATOM   1913 C  CA  . GLY   B 1 102 ? 25.290 -19.847 4.716  1.00 13.93 ? 108 GLY   C CA  1 
ATOM   1914 C  C   . GLY   B 1 102 ? 25.398 -20.957 5.754  1.00 13.23 ? 108 GLY   C C   1 
ATOM   1915 O  O   . GLY   B 1 102 ? 24.404 -21.622 6.066  1.00 14.54 ? 108 GLY   C O   1 
ATOM   1916 N  N   . ASP   B 1 103 ? 26.612 -21.201 6.281  1.00 11.94 ? 109 ASP   C N   1 
ATOM   1917 C  CA  . ASP   B 1 103 ? 26.794 -22.227 7.309  1.00 11.61 ? 109 ASP   C CA  1 
ATOM   1918 C  C   . ASP   B 1 103 ? 26.429 -21.737 8.707  1.00 11.09 ? 109 ASP   C C   1 
ATOM   1919 O  O   . ASP   B 1 103 ? 26.322 -22.521 9.644  1.00 11.43 ? 109 ASP   C O   1 
ATOM   1920 C  CB  . ASP   B 1 103 ? 28.262 -22.695 7.339  1.00 13.44 ? 109 ASP   C CB  1 
ATOM   1921 C  CG  . ASP   B 1 103 ? 28.577 -23.497 6.104  1.00 14.12 ? 109 ASP   C CG  1 
ATOM   1922 O  OD1 . ASP   B 1 103 ? 27.720 -24.266 5.666  1.00 13.69 ? 109 ASP   C OD1 1 
ATOM   1923 O  OD2 . ASP   B 1 103 ? 29.696 -23.361 5.571  1.00 15.00 ? 109 ASP   C OD2 1 
ATOM   1924 N  N   . CYS   B 1 104 ? 26.224 -20.409 8.896  1.00 9.85  ? 110 CYS   C N   1 
ATOM   1925 C  CA  . CYS   B 1 104 ? 25.847 -19.868 10.217 1.00 10.62 ? 110 CYS   C CA  1 
ATOM   1926 C  C   . CYS   B 1 104 ? 24.600 -20.551 10.712 1.00 11.11 ? 110 CYS   C C   1 
ATOM   1927 O  O   . CYS   B 1 104 ? 23.644 -20.761 9.958  1.00 12.84 ? 110 CYS   C O   1 
ATOM   1928 C  CB  . CYS   B 1 104 ? 25.630 -18.352 10.130 1.00 11.40 ? 110 CYS   C CB  1 
ATOM   1929 S  SG  . CYS   B 1 104 ? 27.161 -17.403 9.986  1.00 13.24 ? 110 CYS   C SG  1 
ATOM   1930 N  N   . GLY   B 1 105 ? 24.630 -20.911 11.975 1.00 10.02 ? 111 GLY   C N   1 
ATOM   1931 C  CA  . GLY   B 1 105 ? 23.495 -21.576 12.617 1.00 10.98 ? 111 GLY   C CA  1 
ATOM   1932 C  C   . GLY   B 1 105 ? 23.671 -23.095 12.759 1.00 10.84 ? 111 GLY   C C   1 
ATOM   1933 O  O   . GLY   B 1 105 ? 22.895 -23.738 13.477 1.00 12.40 ? 111 GLY   C O   1 
ATOM   1934 N  N   . GLY   B 1 106 ? 24.675 -23.670 12.082 1.00 11.12 ? 112 GLY   C N   1 
ATOM   1935 C  CA  . GLY   B 1 106 ? 24.984 -25.107 12.232 1.00 11.16 ? 112 GLY   C CA  1 
ATOM   1936 C  C   . GLY   B 1 106 ? 25.391 -25.404 13.678 1.00 11.20 ? 112 GLY   C C   1 
ATOM   1937 O  O   . GLY   B 1 106 ? 26.126 -24.606 14.300 1.00 10.78 ? 112 GLY   C O   1 
ATOM   1938 N  N   . ILE   B 1 107 ? 24.954 -26.538 14.218 1.00 10.77 ? 113 ILE   C N   1 
ATOM   1939 C  CA  . ILE   B 1 107 ? 25.261 -26.841 15.620 1.00 10.99 ? 113 ILE   C CA  1 
ATOM   1940 C  C   . ILE   B 1 107 ? 26.623 -27.471 15.799 1.00 10.24 ? 113 ILE   C C   1 
ATOM   1941 O  O   . ILE   B 1 107 ? 27.029 -28.336 15.028 1.00 10.36 ? 113 ILE   C O   1 
ATOM   1942 C  CB  . ILE   B 1 107 ? 24.112 -27.770 16.175 1.00 13.65 ? 113 ILE   C CB  1 
ATOM   1943 C  CG1 . ILE   B 1 107 ? 22.865 -26.826 16.573 1.00 16.70 ? 113 ILE   C CG1 1 
ATOM   1944 C  CG2 . ILE   B 1 107 ? 24.575 -28.628 17.410 1.00 13.11 ? 113 ILE   C CG2 1 
ATOM   1945 C  CD1 . ILE   B 1 107 ? 21.584 -27.599 16.976 1.00 20.17 ? 113 ILE   C CD1 1 
ATOM   1946 N  N   . LEU   B 1 108 ? 27.316 -27.031 16.887 1.00 9.42  ? 114 LEU   C N   1 
ATOM   1947 C  CA  . LEU   B 1 108 ? 28.517 -27.694 17.410 1.00 9.78  ? 114 LEU   C CA  1 
ATOM   1948 C  C   . LEU   B 1 108 ? 28.029 -28.453 18.659 1.00 9.16  ? 114 LEU   C C   1 
ATOM   1949 O  O   . LEU   B 1 108 ? 27.400 -27.862 19.543 1.00 9.49  ? 114 LEU   C O   1 
ATOM   1950 C  CB  . LEU   B 1 108 ? 29.566 -26.625 17.812 1.00 8.93  ? 114 LEU   C CB  1 
ATOM   1951 C  CG  . LEU   B 1 108 ? 30.767 -27.173 18.594 1.00 9.94  ? 114 LEU   C CG  1 
ATOM   1952 C  CD1 . LEU   B 1 108 ? 31.630 -28.085 17.683 1.00 10.71 ? 114 LEU   C CD1 1 
ATOM   1953 C  CD2 . LEU   B 1 108 ? 31.606 -25.994 19.133 1.00 10.97 ? 114 LEU   C CD2 1 
ATOM   1954 N  N   . ARG   B 1 109 ? 28.287 -29.787 18.706 1.00 9.50  ? 115 ARG   C N   1 
ATOM   1955 C  CA  . ARG   B 1 109 ? 27.836 -30.573 19.887 1.00 10.64 ? 115 ARG   C CA  1 
ATOM   1956 C  C   . ARG   B 1 109 ? 28.966 -31.430 20.427 1.00 11.20 ? 115 ARG   C C   1 
ATOM   1957 O  O   . ARG   B 1 109 ? 29.883 -31.840 19.698 1.00 11.83 ? 115 ARG   C O   1 
ATOM   1958 C  CB  . ARG   B 1 109 ? 26.651 -31.457 19.482 1.00 14.58 ? 115 ARG   C CB  1 
ATOM   1959 C  CG  . ARG   B 1 109 ? 27.043 -32.493 18.466 1.00 19.30 ? 115 ARG   C CG  1 
ATOM   1960 C  CD  . ARG   B 1 109 ? 25.850 -33.342 17.999 1.00 25.59 ? 115 ARG   C CD  1 
ATOM   1961 N  NE  . ARG   B 1 109 ? 24.982 -32.604 17.070 1.00 31.52 ? 115 ARG   C NE  1 
ATOM   1962 C  CZ  . ARG   B 1 109 ? 23.689 -32.365 17.283 1.00 39.11 ? 115 ARG   C CZ  1 
ATOM   1963 N  NH1 . ARG   B 1 109 ? 23.116 -32.738 18.421 1.00 41.40 ? 115 ARG   C NH1 1 
ATOM   1964 N  NH2 . ARG   B 1 109 ? 22.977 -31.687 16.390 1.00 39.82 ? 115 ARG   C NH2 1 
ATOM   1965 N  N   . CYS   B 1 110 ? 28.912 -31.670 21.719 1.00 10.60 ? 116 CYS   C N   1 
ATOM   1966 C  CA  . CYS   B 1 110 ? 29.884 -32.557 22.416 1.00 10.92 ? 116 CYS   C CA  1 
ATOM   1967 C  C   . CYS   B 1 110 ? 29.055 -33.658 23.122 1.00 11.88 ? 116 CYS   C C   1 
ATOM   1968 O  O   . CYS   B 1 110 ? 27.836 -33.742 22.927 1.00 12.46 ? 116 CYS   C O   1 
ATOM   1969 C  CB  . CYS   B 1 110 ? 30.703 -31.747 23.423 1.00 10.60 ? 116 CYS   C CB  1 
ATOM   1970 S  SG  . CYS   B 1 110 ? 29.689 -31.120 24.804 1.00 10.72 ? 116 CYS   C SG  1 
ATOM   1971 N  N   . GLN   B 1 111 ? 29.701 -34.515 23.950 1.00 12.49 ? 117 GLN   C N   1 
ATOM   1972 C  CA  . GLN   B 1 111 ? 28.923 -35.546 24.655 1.00 14.35 ? 117 GLN   C CA  1 
ATOM   1973 C  C   . GLN   B 1 111 ? 27.867 -34.988 25.600 1.00 14.48 ? 117 GLN   C C   1 
ATOM   1974 O  O   . GLN   B 1 111 ? 26.921 -35.708 25.939 1.00 16.03 ? 117 GLN   C O   1 
ATOM   1975 C  CB  . GLN   B 1 111 ? 29.848 -36.522 25.451 1.00 15.93 ? 117 GLN   C CB  1 
ATOM   1976 C  CG  . GLN   B 1 111 ? 30.523 -35.841 26.638 1.00 19.28 ? 117 GLN   C CG  1 
ATOM   1977 C  CD  . GLN   B 1 111 ? 31.507 -36.714 27.384 1.00 30.94 ? 117 GLN   C CD  1 
ATOM   1978 O  OE1 . GLN   B 1 111 ? 32.721 -36.658 27.147 1.00 34.02 ? 117 GLN   C OE1 1 
ATOM   1979 N  NE2 . GLN   B 1 111 ? 30.991 -37.461 28.348 1.00 31.90 ? 117 GLN   C NE2 1 
ATOM   1980 N  N   . HIS   B 1 112 ? 27.981 -33.698 26.023 1.00 12.51 ? 118 HIS   C N   1 
ATOM   1981 C  CA  . HIS   B 1 112 ? 27.023 -33.134 26.966 1.00 12.65 ? 118 HIS   C CA  1 
ATOM   1982 C  C   . HIS   B 1 112 ? 25.851 -32.453 26.292 1.00 13.24 ? 118 HIS   C C   1 
ATOM   1983 O  O   . HIS   B 1 112 ? 24.893 -32.085 26.995 1.00 14.39 ? 118 HIS   C O   1 
ATOM   1984 C  CB  . HIS   B 1 112 ? 27.757 -32.153 27.875 1.00 12.76 ? 118 HIS   C CB  1 
ATOM   1985 C  CG  . HIS   B 1 112 ? 28.936 -32.773 28.577 1.00 12.81 ? 118 HIS   C CG  1 
ATOM   1986 N  ND1 . HIS   B 1 112 ? 30.243 -32.517 28.181 1.00 11.08 ? 118 HIS   C ND1 1 
ATOM   1987 C  CD2 . HIS   B 1 112 ? 28.976 -33.645 29.626 1.00 14.68 ? 118 HIS   C CD2 1 
ATOM   1988 C  CE1 . HIS   B 1 112 ? 31.040 -33.206 28.982 1.00 13.75 ? 118 HIS   C CE1 1 
ATOM   1989 N  NE2 . HIS   B 1 112 ? 30.325 -33.887 29.891 1.00 15.34 ? 118 HIS   C NE2 1 
ATOM   1990 N  N   . GLY   B 1 113 ? 25.916 -32.197 24.987 1.00 11.74 ? 119 GLY   C N   1 
ATOM   1991 C  CA  . GLY   B 1 113 ? 24.821 -31.522 24.299 1.00 11.60 ? 119 GLY   C CA  1 
ATOM   1992 C  C   . GLY   B 1 113 ? 25.326 -30.450 23.354 1.00 10.30 ? 119 GLY   C C   1 
ATOM   1993 O  O   . GLY   B 1 113 ? 26.460 -30.525 22.843 1.00 10.28 ? 119 GLY   C O   1 
ATOM   1994 N  N   . VAL   B 1 114 ? 24.456 -29.464 23.074 1.00 10.28 ? 120 VAL   C N   1 
ATOM   1995 C  CA  . VAL   B 1 114 ? 24.791 -28.370 22.148 1.00 10.71 ? 120 VAL   C CA  1 
ATOM   1996 C  C   . VAL   B 1 114 ? 25.742 -27.352 22.807 1.00 10.60 ? 120 VAL   C C   1 
ATOM   1997 O  O   . VAL   B 1 114 ? 25.439 -26.811 23.882 1.00 11.22 ? 120 VAL   C O   1 
ATOM   1998 C  CB  . VAL   B 1 114 ? 23.485 -27.674 21.691 1.00 12.26 ? 120 VAL   C CB  1 
ATOM   1999 C  CG1 . VAL   B 1 114 ? 23.818 -26.443 20.836 1.00 13.11 ? 120 VAL   C CG1 1 
ATOM   2000 C  CG2 . VAL   B 1 114 ? 22.578 -28.667 20.930 1.00 14.19 ? 120 VAL   C CG2 1 
ATOM   2001 N  N   . VAL   B 1 115 ? 26.891 -27.095 22.168 1.00 9.44  ? 121 VAL   C N   1 
ATOM   2002 C  CA  . VAL   B 1 115 ? 27.901 -26.167 22.671 1.00 9.50  ? 121 VAL   C CA  1 
ATOM   2003 C  C   . VAL   B 1 115 ? 27.677 -24.758 22.153 1.00 10.89 ? 121 VAL   C C   1 
ATOM   2004 O  O   . VAL   B 1 115 ? 27.935 -23.773 22.878 1.00 10.92 ? 121 VAL   C O   1 
ATOM   2005 C  CB  . VAL   B 1 115 ? 29.305 -26.702 22.254 1.00 10.42 ? 121 VAL   C CB  1 
ATOM   2006 C  CG1 . VAL   B 1 115 ? 30.388 -25.697 22.643 1.00 12.21 ? 121 VAL   C CG1 1 
ATOM   2007 C  CG2 . VAL   B 1 115 ? 29.550 -28.082 22.890 1.00 11.98 ? 121 VAL   C CG2 1 
ATOM   2008 N  N   . GLY   B 1 116 ? 27.310 -24.660 20.887 1.00 10.24 ? 122 GLY   C N   1 
ATOM   2009 C  CA  . GLY   B 1 116 ? 27.118 -23.363 20.272 1.00 11.58 ? 122 GLY   C CA  1 
ATOM   2010 C  C   . GLY   B 1 116 ? 26.763 -23.538 18.806 1.00 10.38 ? 122 GLY   C C   1 
ATOM   2011 O  O   . GLY   B 1 116 ? 26.407 -24.654 18.385 1.00 10.57 ? 122 GLY   C O   1 
ATOM   2012 N  N   . ILE   B 1 117 ? 26.729 -22.378 18.081 1.00 10.62 ? 123 ILE   C N   1 
ATOM   2013 C  CA  . ILE   B 1 117 ? 26.354 -22.397 16.667 1.00 9.62  ? 123 ILE   C CA  1 
ATOM   2014 C  C   . ILE   B 1 117 ? 27.395 -21.683 15.831 1.00 9.88  ? 123 ILE   C C   1 
ATOM   2015 O  O   . ILE   B 1 117 ? 28.040 -20.718 16.308 1.00 10.27 ? 123 ILE   C O   1 
ATOM   2016 C  CB  . ILE   B 1 117 ? 24.959 -21.754 16.410 1.00 11.18 ? 123 ILE   C CB  1 
ATOM   2017 C  CG1 . ILE   B 1 117 ? 24.850 -20.365 17.062 1.00 11.75 ? 123 ILE   C CG1 1 
ATOM   2018 C  CG2 . ILE   B 1 117 ? 23.829 -22.676 16.880 1.00 11.94 ? 123 ILE   C CG2 1 
ATOM   2019 C  CD1 . ILE   B 1 117 ? 23.475 -19.596 16.628 1.00 11.87 ? 123 ILE   C CD1 1 
ATOM   2020 N  N   . VAL   B 1 118 ? 27.546 -22.100 14.558 1.00 9.75  ? 124 VAL   C N   1 
ATOM   2021 C  CA  . VAL   B 1 118 ? 28.470 -21.430 13.646 1.00 10.38 ? 124 VAL   C CA  1 
ATOM   2022 C  C   . VAL   B 1 118 ? 28.109 -19.956 13.525 1.00 9.43  ? 124 VAL   C C   1 
ATOM   2023 O  O   . VAL   B 1 118 ? 26.919 -19.621 13.349 1.00 10.18 ? 124 VAL   C O   1 
ATOM   2024 C  CB  . VAL   B 1 118 ? 28.424 -22.100 12.256 1.00 9.96  ? 124 VAL   C CB  1 
ATOM   2025 C  CG1 . VAL   B 1 118 ? 29.279 -21.363 11.241 1.00 10.84 ? 124 VAL   C CG1 1 
ATOM   2026 C  CG2 . VAL   B 1 118 ? 28.885 -23.555 12.358 1.00 10.54 ? 124 VAL   C CG2 1 
ATOM   2027 N  N   . SER   B 1 119 ? 29.147 -19.065 13.631 1.00 9.34  ? 125 SER   C N   1 
ATOM   2028 C  CA  . SER   B 1 119 ? 28.947 -17.612 13.533 1.00 9.88  ? 125 SER   C CA  1 
ATOM   2029 C  C   . SER   B 1 119 ? 29.945 -16.921 12.595 1.00 11.09 ? 125 SER   C C   1 
ATOM   2030 O  O   . SER   B 1 119 ? 29.615 -15.848 12.053 1.00 10.70 ? 125 SER   C O   1 
ATOM   2031 C  CB  . SER   B 1 119 ? 28.982 -17.019 14.937 1.00 10.78 ? 125 SER   C CB  1 
ATOM   2032 O  OG  . SER   B 1 119 ? 28.866 -15.597 14.912 1.00 12.40 ? 125 SER   C OG  1 
ATOM   2033 N  N   . THR   B 1 120 ? 31.175 -17.458 12.455 1.00 10.86 ? 126 THR   C N   1 
ATOM   2034 C  CA  . THR   B 1 120 ? 32.195 -16.786 11.617 1.00 10.99 ? 126 THR   C CA  1 
ATOM   2035 C  C   . THR   B 1 120 ? 32.921 -17.803 10.759 1.00 10.69 ? 126 THR   C C   1 
ATOM   2036 O  O   . THR   B 1 120 ? 32.869 -19.039 10.989 1.00 10.70 ? 126 THR   C O   1 
ATOM   2037 C  CB  . THR   B 1 120 ? 33.253 -16.034 12.534 1.00 11.01 ? 126 THR   C CB  1 
ATOM   2038 O  OG1 . THR   B 1 120 ? 34.109 -16.997 13.176 1.00 12.26 ? 126 THR   C OG1 1 
ATOM   2039 C  CG2 . THR   B 1 120 ? 32.630 -15.129 13.592 1.00 13.09 ? 126 THR   C CG2 1 
ATOM   2040 N  N   . GLY   B 1 121 ? 33.603 -17.285 9.762  1.00 12.06 ? 127 GLY   C N   1 
ATOM   2041 C  CA  . GLY   B 1 121 ? 34.417 -18.106 8.870  1.00 13.76 ? 127 GLY   C CA  1 
ATOM   2042 C  C   . GLY   B 1 121 ? 35.449 -17.259 8.146  1.00 16.53 ? 127 GLY   C C   1 
ATOM   2043 O  O   . GLY   B 1 121 ? 35.141 -16.143 7.710  1.00 18.81 ? 127 GLY   C O   1 
ATOM   2044 N  N   . GLY   B 1 122 ? 36.647 -17.760 8.017  1.00 19.06 ? 128 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 122 ? 37.691 -17.014 7.304  1.00 20.13 ? 128 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 122 ? 39.033 -17.627 7.517  1.00 20.36 ? 128 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 122 ? 39.295 -18.137 8.596  1.00 20.37 ? 128 GLY   C O   1 
ATOM   2048 N  N   . ASN   B 1 123 ? 39.933 -17.534 6.505  1.00 18.90 ? 129 ASN   C N   1 
ATOM   2049 C  CA  . ASN   B 1 123 ? 41.310 -18.004 6.667  1.00 18.62 ? 129 ASN   C CA  1 
ATOM   2050 C  C   . ASN   B 1 123 ? 41.366 -19.485 7.054  1.00 17.37 ? 129 ASN   C C   1 
ATOM   2051 O  O   . ASN   B 1 123 ? 42.312 -19.883 7.735  1.00 19.77 ? 129 ASN   C O   1 
ATOM   2052 C  CB  . ASN   B 1 123 ? 42.101 -17.107 7.692  1.00 21.47 ? 129 ASN   C CB  1 
ATOM   2053 C  CG  . ASN   B 1 123 ? 42.879 -15.956 7.075  1.00 27.03 ? 129 ASN   C CG  1 
ATOM   2054 O  OD1 . ASN   B 1 123 ? 43.242 -15.974 5.891  1.00 27.41 ? 129 ASN   C OD1 1 
ATOM   2055 N  ND2 . ASN   B 1 123 ? 43.187 -14.915 7.861  1.00 29.13 ? 129 ASN   C ND2 1 
ATOM   2056 N  N   . GLY   B 1 124 ? 40.391 -20.306 6.622  1.00 15.63 ? 130 GLY   C N   1 
ATOM   2057 C  CA  . GLY   B 1 124 ? 40.385 -21.736 6.975  1.00 15.31 ? 130 GLY   C CA  1 
ATOM   2058 C  C   . GLY   B 1 124 ? 39.977 -22.062 8.404  1.00 14.83 ? 130 GLY   C C   1 
ATOM   2059 O  O   . GLY   B 1 124 ? 40.219 -23.183 8.897  1.00 15.24 ? 130 GLY   C O   1 
ATOM   2060 N  N   . LEU   B 1 125 ? 39.404 -21.069 9.083  1.00 13.51 ? 131 LEU   C N   1 
ATOM   2061 C  CA  . LEU   B 1 125 ? 38.935 -21.203 10.449 1.00 12.56 ? 131 LEU   C CA  1 
ATOM   2062 C  C   . LEU   B 1 125 ? 37.424 -21.076 10.482 1.00 13.53 ? 131 LEU   C C   1 
ATOM   2063 O  O   . LEU   B 1 125 ? 36.844 -20.303 9.706  1.00 16.04 ? 131 LEU   C O   1 
ATOM   2064 C  CB  . LEU   B 1 125 ? 39.581 -20.140 11.376 1.00 14.62 ? 131 LEU   C CB  1 
ATOM   2065 C  CG  . LEU   B 1 125 ? 41.131 -20.214 11.449 1.00 17.23 ? 131 LEU   C CG  1 
ATOM   2066 C  CD1 . LEU   B 1 125 ? 41.759 -18.890 11.894 1.00 21.00 ? 131 LEU   C CD1 1 
ATOM   2067 C  CD2 . LEU   B 1 125 ? 41.603 -21.365 12.276 1.00 18.49 ? 131 LEU   C CD2 1 
ATOM   2068 N  N   . VAL   B 1 126 ? 36.781 -21.796 11.374 1.00 11.00 ? 132 VAL   C N   1 
ATOM   2069 C  CA  . VAL   B 1 126 ? 35.342 -21.656 11.613 1.00 10.63 ? 132 VAL   C CA  1 
ATOM   2070 C  C   . VAL   B 1 126 ? 35.179 -21.222 13.080 1.00 10.13 ? 132 VAL   C C   1 
ATOM   2071 O  O   . VAL   B 1 126 ? 35.879 -21.746 13.966 1.00 10.49 ? 132 VAL   C O   1 
ATOM   2072 C  CB  . VAL   B 1 126 ? 34.598 -22.989 11.357 1.00 10.74 ? 132 VAL   C CB  1 
ATOM   2073 C  CG1 . VAL   B 1 126 ? 35.211 -24.172 12.068 1.00 11.83 ? 132 VAL   C CG1 1 
ATOM   2074 C  CG2 . VAL   B 1 126 ? 33.095 -22.853 11.724 1.00 10.86 ? 132 VAL   C CG2 1 
ATOM   2075 N  N   . GLY   B 1 127 ? 34.330 -20.245 13.316 1.00 9.69  ? 133 GLY   C N   1 
ATOM   2076 C  CA  . GLY   B 1 127 ? 34.099 -19.777 14.664 1.00 9.30  ? 133 GLY   C CA  1 
ATOM   2077 C  C   . GLY   B 1 127 ? 32.670 -20.077 15.104 1.00 10.32 ? 133 GLY   C C   1 
ATOM   2078 O  O   . GLY   B 1 127 ? 31.702 -19.950 14.314 1.00 10.77 ? 133 GLY   C O   1 
ATOM   2079 N  N   . PHE   B 1 128 ? 32.549 -20.402 16.384 1.00 8.69  ? 134 PHE   C N   1 
ATOM   2080 C  CA  . PHE   B 1 128 ? 31.274 -20.780 17.017 1.00 9.36  ? 134 PHE   C CA  1 
ATOM   2081 C  C   . PHE   B 1 128 ? 30.955 -19.838 18.158 1.00 9.39  ? 134 PHE   C C   1 
ATOM   2082 O  O   . PHE   B 1 128 ? 31.806 -19.581 19.025 1.00 9.94  ? 134 PHE   C O   1 
ATOM   2083 C  CB  . PHE   B 1 128 ? 31.353 -22.229 17.592 1.00 9.73  ? 134 PHE   C CB  1 
ATOM   2084 C  CG  . PHE   B 1 128 ? 31.873 -23.239 16.592 1.00 10.36 ? 134 PHE   C CG  1 
ATOM   2085 C  CD1 . PHE   B 1 128 ? 31.015 -23.825 15.672 1.00 10.46 ? 134 PHE   C CD1 1 
ATOM   2086 C  CD2 . PHE   B 1 128 ? 33.207 -23.640 16.618 1.00 11.85 ? 134 PHE   C CD2 1 
ATOM   2087 C  CE1 . PHE   B 1 128 ? 31.484 -24.796 14.795 1.00 11.27 ? 134 PHE   C CE1 1 
ATOM   2088 C  CE2 . PHE   B 1 128 ? 33.685 -24.594 15.711 1.00 11.95 ? 134 PHE   C CE2 1 
ATOM   2089 C  CZ  . PHE   B 1 128 ? 32.829 -25.170 14.819 1.00 11.32 ? 134 PHE   C CZ  1 
ATOM   2090 N  N   . ALA   B 1 129 ? 29.690 -19.366 18.191 1.00 9.97  ? 135 ALA   C N   1 
ATOM   2091 C  CA  . ALA   B 1 129 ? 29.208 -18.554 19.313 1.00 10.18 ? 135 ALA   C CA  1 
ATOM   2092 C  C   . ALA   B 1 129 ? 28.812 -19.520 20.468 1.00 10.53 ? 135 ALA   C C   1 
ATOM   2093 O  O   . ALA   B 1 129 ? 27.926 -20.352 20.298 1.00 10.61 ? 135 ALA   C O   1 
ATOM   2094 C  CB  . ALA   B 1 129 ? 27.982 -17.758 18.841 1.00 11.61 ? 135 ALA   C CB  1 
ATOM   2095 N  N   . ASP   B 1 130 ? 29.547 -19.459 21.580 1.00 9.76  ? 136 ASP   C N   1 
ATOM   2096 C  CA  . ASP   B 1 130 ? 29.260 -20.348 22.726 1.00 9.68  ? 136 ASP   C CA  1 
ATOM   2097 C  C   . ASP   B 1 130 ? 27.912 -19.985 23.365 1.00 10.51 ? 136 ASP   C C   1 
ATOM   2098 O  O   . ASP   B 1 130 ? 27.534 -18.796 23.448 1.00 10.46 ? 136 ASP   C O   1 
ATOM   2099 C  CB  . ASP   B 1 130 ? 30.360 -20.122 23.794 1.00 11.03 ? 136 ASP   C CB  1 
ATOM   2100 C  CG  . ASP   B 1 130 ? 30.273 -21.053 24.990 1.00 15.03 ? 136 ASP   C CG  1 
ATOM   2101 O  OD1 . ASP   B 1 130 ? 30.131 -22.267 24.786 1.00 14.10 ? 136 ASP   C OD1 1 
ATOM   2102 O  OD2 . ASP   B 1 130 ? 30.249 -20.539 26.154 1.00 17.79 ? 136 ASP   C OD2 1 
ATOM   2103 N  N   . VAL   B 1 131 ? 27.206 -21.002 23.844 1.00 10.20 ? 137 VAL   C N   1 
ATOM   2104 C  CA  . VAL   B 1 131 ? 25.980 -20.793 24.636 1.00 9.53  ? 137 VAL   C CA  1 
ATOM   2105 C  C   . VAL   B 1 131 ? 26.064 -21.505 25.992 1.00 11.17 ? 137 VAL   C C   1 
ATOM   2106 O  O   . VAL   B 1 131 ? 25.083 -21.441 26.758 1.00 11.39 ? 137 VAL   C O   1 
ATOM   2107 C  CB  . VAL   B 1 131 ? 24.701 -21.234 23.895 1.00 11.29 ? 137 VAL   C CB  1 
ATOM   2108 C  CG1 . VAL   B 1 131 ? 24.491 -20.434 22.603 1.00 11.97 ? 137 VAL   C CG1 1 
ATOM   2109 C  CG2 . VAL   B 1 131 ? 24.694 -22.732 23.613 1.00 11.73 ? 137 VAL   C CG2 1 
ATOM   2110 N  N   . ARG   B 1 132 ? 27.197 -22.158 26.330 1.00 10.93 ? 138 ARG   C N   1 
ATOM   2111 C  CA  . ARG   B 1 132 ? 27.252 -22.935 27.575 1.00 11.26 ? 138 ARG   C CA  1 
ATOM   2112 C  C   . ARG   B 1 132 ? 27.205 -22.120 28.837 1.00 11.63 ? 138 ARG   C C   1 
ATOM   2113 O  O   . ARG   B 1 132 ? 26.887 -22.683 29.914 1.00 13.21 ? 138 ARG   C O   1 
ATOM   2114 C  CB  . ARG   B 1 132 ? 28.517 -23.795 27.574 1.00 10.29 ? 138 ARG   C CB  1 
ATOM   2115 C  CG  . ARG   B 1 132 ? 28.516 -24.839 26.421 1.00 10.05 ? 138 ARG   C CG  1 
ATOM   2116 C  CD  . ARG   B 1 132 ? 29.831 -25.604 26.482 1.00 10.68 ? 138 ARG   C CD  1 
ATOM   2117 N  NE  . ARG   B 1 132 ? 30.916 -24.704 26.061 1.00 10.35 ? 138 ARG   C NE  1 
ATOM   2118 C  CZ  . ARG   B 1 132 ? 32.168 -25.098 25.857 1.00 11.78 ? 138 ARG   C CZ  1 
ATOM   2119 N  NH1 . ARG   B 1 132 ? 32.549 -26.324 26.185 1.00 10.34 ? 138 ARG   C NH1 1 
ATOM   2120 N  NH2 . ARG   B 1 132 ? 33.070 -24.245 25.397 1.00 11.72 ? 138 ARG   C NH2 1 
ATOM   2121 N  N   . ASP   B 1 133 ? 27.515 -20.812 28.756 1.00 11.09 ? 139 ASP   C N   1 
ATOM   2122 C  CA  . ASP   B 1 133 ? 27.457 -19.950 29.931 1.00 12.17 ? 139 ASP   C CA  1 
ATOM   2123 C  C   . ASP   B 1 133 ? 26.050 -19.379 30.191 1.00 12.40 ? 139 ASP   C C   1 
ATOM   2124 O  O   . ASP   B 1 133 ? 25.853 -18.785 31.265 1.00 13.77 ? 139 ASP   C O   1 
ATOM   2125 C  CB  . ASP   B 1 133 ? 28.442 -18.775 29.785 1.00 13.87 ? 139 ASP   C CB  1 
ATOM   2126 C  CG  . ASP   B 1 133 ? 28.054 -17.828 28.660 1.00 15.19 ? 139 ASP   C CG  1 
ATOM   2127 O  OD1 . ASP   B 1 133 ? 27.713 -18.326 27.556 1.00 15.63 ? 139 ASP   C OD1 1 
ATOM   2128 O  OD2 . ASP   B 1 133 ? 28.075 -16.574 28.886 1.00 17.22 ? 139 ASP   C OD2 1 
ATOM   2129 N  N   . LEU   B 1 134 ? 25.093 -19.580 29.266 1.00 11.69 ? 140 LEU   C N   1 
ATOM   2130 C  CA  . LEU   B 1 134 ? 23.727 -19.017 29.390 1.00 11.80 ? 140 LEU   C CA  1 
ATOM   2131 C  C   . LEU   B 1 134 ? 22.875 -19.989 30.177 1.00 12.26 ? 140 LEU   C C   1 
ATOM   2132 O  O   . LEU   B 1 134 ? 22.058 -20.730 29.622 1.00 12.27 ? 140 LEU   C O   1 
ATOM   2133 C  CB  . LEU   B 1 134 ? 23.142 -18.751 27.991 1.00 11.72 ? 140 LEU   C CB  1 
ATOM   2134 C  CG  . LEU   B 1 134 ? 24.021 -17.828 27.124 1.00 13.15 ? 140 LEU   C CG  1 
ATOM   2135 C  CD1 . LEU   B 1 134 ? 23.437 -17.709 25.693 1.00 14.30 ? 140 LEU   C CD1 1 
ATOM   2136 C  CD2 . LEU   B 1 134 ? 24.137 -16.425 27.752 1.00 14.60 ? 140 LEU   C CD2 1 
ATOM   2137 N  N   . LEU   B 1 135 ? 23.080 -20.033 31.505 1.00 13.14 ? 141 LEU   C N   1 
ATOM   2138 C  CA  . LEU   B 1 135 ? 22.446 -21.070 32.335 1.00 13.96 ? 141 LEU   C CA  1 
ATOM   2139 C  C   . LEU   B 1 135 ? 20.925 -20.972 32.396 1.00 13.41 ? 141 LEU   C C   1 
ATOM   2140 O  O   . LEU   B 1 135 ? 20.253 -21.992 32.551 1.00 14.95 ? 141 LEU   C O   1 
ATOM   2141 C  CB  . LEU   B 1 135 ? 23.041 -21.090 33.758 1.00 13.55 ? 141 LEU   C CB  1 
ATOM   2142 C  CG  . LEU   B 1 135 ? 24.577 -21.061 33.834 1.00 14.14 ? 141 LEU   C CG  1 
ATOM   2143 C  CD1 . LEU   B 1 135 ? 25.065 -21.065 35.326 1.00 14.99 ? 141 LEU   C CD1 1 
ATOM   2144 C  CD2 . LEU   B 1 135 ? 25.216 -22.234 33.051 1.00 14.22 ? 141 LEU   C CD2 1 
ATOM   2145 N  N   . TRP   B 1 136 ? 20.404 -19.740 32.184 1.00 13.10 ? 142 TRP   C N   1 
ATOM   2146 C  CA  . TRP   B 1 136 ? 18.957 -19.481 32.218 1.00 14.51 ? 142 TRP   C CA  1 
ATOM   2147 C  C   . TRP   B 1 136 ? 18.223 -20.205 31.074 1.00 14.90 ? 142 TRP   C C   1 
ATOM   2148 O  O   . TRP   B 1 136 ? 16.996 -20.346 31.144 1.00 16.50 ? 142 TRP   C O   1 
ATOM   2149 C  CB  . TRP   B 1 136 ? 18.706 -17.962 32.195 1.00 14.50 ? 142 TRP   C CB  1 
ATOM   2150 C  CG  . TRP   B 1 136 ? 19.405 -17.237 31.086 1.00 14.43 ? 142 TRP   C CG  1 
ATOM   2151 C  CD1 . TRP   B 1 136 ? 20.575 -16.544 31.175 1.00 15.35 ? 142 TRP   C CD1 1 
ATOM   2152 C  CD2 . TRP   B 1 136 ? 18.894 -17.000 29.760 1.00 14.46 ? 142 TRP   C CD2 1 
ATOM   2153 N  NE1 . TRP   B 1 136 ? 20.891 -15.988 29.939 1.00 15.89 ? 142 TRP   C NE1 1 
ATOM   2154 C  CE2 . TRP   B 1 136 ? 19.850 -16.227 29.069 1.00 15.26 ? 142 TRP   C CE2 1 
ATOM   2155 C  CE3 . TRP   B 1 136 ? 17.727 -17.390 29.093 1.00 14.58 ? 142 TRP   C CE3 1 
ATOM   2156 C  CZ2 . TRP   B 1 136 ? 19.663 -15.819 27.734 1.00 15.06 ? 142 TRP   C CZ2 1 
ATOM   2157 C  CZ3 . TRP   B 1 136 ? 17.528 -16.959 27.789 1.00 15.05 ? 142 TRP   C CZ3 1 
ATOM   2158 C  CH2 . TRP   B 1 136 ? 18.490 -16.198 27.126 1.00 15.25 ? 142 TRP   C CH2 1 
ATOM   2159 N  N   . LEU   B 1 137 ? 18.935 -20.647 30.014 1.00 13.95 ? 143 LEU   C N   1 
ATOM   2160 C  CA  . LEU   B 1 137 ? 18.266 -21.426 28.959 1.00 14.49 ? 143 LEU   C CA  1 
ATOM   2161 C  C   . LEU   B 1 137 ? 17.662 -22.723 29.503 1.00 16.58 ? 143 LEU   C C   1 
ATOM   2162 O  O   . LEU   B 1 137 ? 16.746 -23.277 28.876 1.00 18.42 ? 143 LEU   C O   1 
ATOM   2163 C  CB  . LEU   B 1 137 ? 19.228 -21.762 27.792 1.00 14.05 ? 143 LEU   C CB  1 
ATOM   2164 C  CG  . LEU   B 1 137 ? 19.657 -20.569 26.912 1.00 14.46 ? 143 LEU   C CG  1 
ATOM   2165 C  CD1 . LEU   B 1 137 ? 20.799 -21.007 25.980 1.00 14.23 ? 143 LEU   C CD1 1 
ATOM   2166 C  CD2 . LEU   B 1 137 ? 18.461 -20.037 26.057 1.00 14.13 ? 143 LEU   C CD2 1 
ATOM   2167 N  N   . ASP   B 1 138 ? 18.161 -23.234 30.670 1.00 15.64 ? 144 ASP   C N   1 
ATOM   2168 C  CA  . ASP   B 1 138 ? 17.725 -24.522 31.244 1.00 16.49 ? 144 ASP   C CA  1 
ATOM   2169 C  C   . ASP   B 1 138 ? 16.477 -24.382 32.130 1.00 19.17 ? 144 ASP   C C   1 
ATOM   2170 O  O   . ASP   B 1 138 ? 15.990 -25.414 32.632 1.00 20.87 ? 144 ASP   C O   1 
ATOM   2171 C  CB  . ASP   B 1 138 ? 18.848 -25.189 32.108 1.00 16.30 ? 144 ASP   C CB  1 
ATOM   2172 C  CG  . ASP   B 1 138 ? 20.080 -25.605 31.318 1.00 17.78 ? 144 ASP   C CG  1 
ATOM   2173 O  OD1 . ASP   B 1 138 ? 20.003 -25.642 30.078 1.00 18.16 ? 144 ASP   C OD1 1 
ATOM   2174 O  OD2 . ASP   B 1 138 ? 21.142 -25.927 31.968 1.00 18.98 ? 144 ASP   C OD2 1 
ATOM   2175 N  N   . GLU   B 1 139 ? 15.966 -23.153 32.332 1.00 20.73 ? 145 GLU   C N   1 
ATOM   2176 C  CA  . GLU   B 1 139 ? 14.828 -22.975 33.241 1.00 25.17 ? 145 GLU   C CA  1 
ATOM   2177 C  C   . GLU   B 1 139 ? 13.745 -22.046 32.660 1.00 29.76 ? 145 GLU   C C   1 
ATOM   2178 O  O   . GLU   B 1 139 ? 13.933 -21.448 31.610 1.00 30.53 ? 145 GLU   C O   1 
ATOM   2179 C  CB  . GLU   B 1 139 ? 15.365 -22.413 34.574 1.00 29.03 ? 145 GLU   C CB  1 
ATOM   2180 C  CG  . GLU   B 1 139 ? 15.939 -21.019 34.410 1.00 37.25 ? 145 GLU   C CG  1 
ATOM   2181 C  CD  . GLU   B 1 139 ? 16.912 -20.558 35.477 1.00 46.26 ? 145 GLU   C CD  1 
ATOM   2182 O  OE1 . GLU   B 1 139 ? 17.221 -19.342 35.516 1.00 47.24 ? 145 GLU   C OE1 1 
ATOM   2183 O  OE2 . GLU   B 1 139 ? 17.354 -21.410 36.280 1.00 48.36 ? 145 GLU   C OE2 1 
ATOM   2184 N  N   . GLU   B 1 140 ? 12.627 -21.897 33.395 1.00 32.93 ? 146 GLU   C N   1 
ATOM   2185 C  CA  . GLU   B 1 140 ? 11.498 -21.008 33.110 1.00 36.67 ? 146 GLU   C CA  1 
ATOM   2186 C  C   . GLU   B 1 140 ? 10.635 -21.537 31.988 1.00 40.30 ? 146 GLU   C C   1 
ATOM   2187 O  O   . GLU   B 1 140 ? 9.410  -21.597 32.156 1.00 42.77 ? 146 GLU   C O   1 
ATOM   2188 C  CB  . GLU   B 1 140 ? 11.943 -19.548 32.894 1.00 38.21 ? 146 GLU   C CB  1 
ATOM   2189 C  CG  . GLU   B 1 140 ? 10.938 -18.617 32.239 1.00 43.93 ? 146 GLU   C CG  1 
ATOM   2190 C  CD  . GLU   B 1 140 ? 10.349 -17.587 33.188 1.00 49.90 ? 146 GLU   C CD  1 
ATOM   2191 O  OE1 . GLU   B 1 140 ? 10.998 -16.536 33.393 1.00 51.54 ? 146 GLU   C OE1 1 
ATOM   2192 O  OE2 . GLU   B 1 140 ? 9.241  -17.825 33.724 1.00 51.10 ? 146 GLU   C OE2 1 
HETATM 2193 C  C4  A A1B22 C 2 .   ? 5.903  12.845  25.459 0.47 14.24 ? 201 A1B22 A C4  1 
HETATM 2194 C  C4  B A1B22 C 2 .   ? 5.776  12.848  25.319 0.47 14.25 ? 201 A1B22 A C4  1 
HETATM 2195 C  C5  A A1B22 C 2 .   ? 6.711  13.846  24.947 0.47 15.87 ? 201 A1B22 A C5  1 
HETATM 2196 C  C5  B A1B22 C 2 .   ? 6.287  13.822  24.477 0.47 15.87 ? 201 A1B22 A C5  1 
HETATM 2197 C  C6  A A1B22 C 2 .   ? 7.734  13.555  24.048 0.47 15.48 ? 201 A1B22 A C6  1 
HETATM 2198 C  C6  B A1B22 C 2 .   ? 7.264  13.516  23.533 0.47 15.48 ? 201 A1B22 A C6  1 
HETATM 2199 C  C7  A A1B22 C 2 .   ? 8.682  14.651  23.613 0.47 19.61 ? 201 A1B22 A C7  1 
HETATM 2200 C  C7  B A1B22 C 2 .   ? 7.645  14.545  22.491 0.47 19.59 ? 201 A1B22 A C7  1 
HETATM 2201 C  C8  A A1B22 C 2 .   ? 8.523  15.000  22.146 0.47 20.72 ? 201 A1B22 A C8  1 
HETATM 2202 C  C8  B A1B22 C 2 .   ? 9.045  15.083  22.708 0.47 20.76 ? 201 A1B22 A C8  1 
HETATM 2203 C  C10 A A1B22 C 2 .   ? 11.119 16.084  20.188 0.47 14.92 ? 201 A1B22 A C10 1 
HETATM 2204 C  C10 B A1B22 C 2 .   ? 10.998 16.129  20.094 0.47 14.93 ? 201 A1B22 A C10 1 
HETATM 2205 O  O   A A1B22 C 2 .   ? 7.433  14.952  21.602 0.47 23.33 ? 201 A1B22 A O   1 
HETATM 2206 O  O   B A1B22 C 2 .   ? 9.479  15.254  23.831 0.47 23.43 ? 201 A1B22 A O   1 
HETATM 2207 N  N   A A1B22 C 2 .   ? 9.640  15.352  21.478 0.47 15.98 ? 201 A1B22 A N   1 
HETATM 2208 N  N   B A1B22 C 2 .   ? 9.784  15.334  21.606 0.47 15.99 ? 201 A1B22 A N   1 
HETATM 2209 C  C11 A A1B22 C 2 .   ? 11.103 15.407  21.568 0.47 15.26 ? 201 A1B22 A C11 1 
HETATM 2210 C  C11 B A1B22 C 2 .   ? 11.220 15.615  21.524 0.47 15.29 ? 201 A1B22 A C11 1 
HETATM 2211 O  O1  A A1B22 C 2 .   ? 11.908 15.456  19.174 0.47 14.72 ? 201 A1B22 A O1  1 
HETATM 2212 O  O1  B A1B22 C 2 .   ? 11.785 15.477  19.093 0.47 14.71 ? 201 A1B22 A O1  1 
HETATM 2213 C  C9  A A1B22 C 2 .   ? 9.613  15.803  20.083 0.47 16.15 ? 201 A1B22 A C9  1 
HETATM 2214 C  C9  B A1B22 C 2 .   ? 9.530  15.686  20.206 0.47 16.14 ? 201 A1B22 A C9  1 
HETATM 2215 C  C1  A A1B22 C 2 .   ? 7.900  12.223  23.651 0.47 11.57 ? 201 A1B22 A C1  1 
HETATM 2216 C  C1  B A1B22 C 2 .   ? 7.764  12.209  23.506 0.47 11.61 ? 201 A1B22 A C1  1 
HETATM 2217 S  S   A A1B22 C 2 .   ? 9.168  11.875  22.473 0.47 11.22 ? 201 A1B22 A S   1 
HETATM 2218 S  S   B A1B22 C 2 .   ? 9.143  11.875  22.457 0.47 11.25 ? 201 A1B22 A S   1 
HETATM 2219 C  C   A A1B22 C 2 .   ? 9.210  10.077  22.468 0.47 10.97 ? 201 A1B22 A C   1 
HETATM 2220 C  C   B A1B22 C 2 .   ? 9.213  10.078  22.469 0.47 10.98 ? 201 A1B22 A C   1 
HETATM 2221 C  C3  A A1B22 C 2 .   ? 6.096  11.539  25.083 0.47 12.57 ? 201 A1B22 A C3  1 
HETATM 2222 C  C3  B A1B22 C 2 .   ? 6.228  11.555  25.234 0.47 12.60 ? 201 A1B22 A C3  1 
HETATM 2223 C  C2  A A1B22 C 2 .   ? 7.087  11.219  24.174 0.47 11.38 ? 201 A1B22 A C2  1 
HETATM 2224 C  C2  B A1B22 C 2 .   ? 7.225  11.227  24.335 0.47 11.41 ? 201 A1B22 A C2  1 
HETATM 2225 ZN ZN  . ZN    D 3 .   ? 11.153 -3.910  5.821  1.00 16.80 2 202 ZN    A ZN  1 
HETATM 2226 S  S   . DMS   E 4 .   ? 19.240 -2.183  23.989 1.00 87.75 ? 203 DMS   A S   1 
HETATM 2227 O  O   . DMS   E 4 .   ? 18.485 -3.217  24.782 1.00 87.68 ? 203 DMS   A O   1 
HETATM 2228 C  C1  . DMS   E 4 .   ? 19.488 -0.730  25.046 1.00 87.67 ? 203 DMS   A C1  1 
HETATM 2229 C  C2  . DMS   E 4 .   ? 20.984 -2.677  24.025 1.00 87.79 ? 203 DMS   A C2  1 
HETATM 2230 ZN ZN  . ZN    F 3 .   ? 30.947 -31.152 26.749 1.00 11.71 2 201 ZN    C ZN  1 
HETATM 2231 S  S   . DMS   G 4 .   ? 21.188 -31.151 9.666  1.00 77.10 ? 202 DMS   C S   1 
HETATM 2232 O  O   . DMS   G 4 .   ? 19.986 -30.318 10.006 1.00 77.15 ? 202 DMS   C O   1 
HETATM 2233 C  C1  . DMS   G 4 .   ? 21.357 -32.383 10.971 1.00 76.92 ? 202 DMS   C C1  1 
HETATM 2234 C  C2  . DMS   G 4 .   ? 20.697 -32.295 8.348  1.00 77.18 ? 202 DMS   C C2  1 
HETATM 2235 O  O   . HOH   H 5 .   ? 3.100  9.320   9.031  1.00 34.61 ? 301 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 11.311 8.877   4.282  1.00 19.49 ? 302 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 35.466 -3.924  7.769  1.00 18.49 ? 303 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 10.933 16.547  16.611 1.00 18.18 ? 304 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 38.525 4.748   10.914 1.00 45.37 ? 305 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 0.177  18.193  17.213 1.00 26.93 ? 306 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 14.134 17.475  4.435  1.00 40.72 ? 307 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 8.998  -3.348  0.614  1.00 36.42 ? 308 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 15.951 -6.760  11.118 1.00 41.59 ? 309 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 2.901  -3.324  20.863 1.00 32.19 ? 310 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 23.237 13.229  23.833 1.00 39.30 ? 311 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 28.136 3.134   4.927  1.00 30.30 ? 312 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 37.619 14.818  13.859 1.00 51.86 ? 313 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 17.444 0.993   28.339 1.00 22.55 ? 314 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 2.186  22.852  21.339 1.00 21.19 ? 315 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 5.772  16.939  21.207 1.00 34.51 ? 316 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 14.093 2.794   1.232  1.00 20.56 ? 317 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 0.640  -1.440  9.229  1.00 37.70 ? 318 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 36.357 -2.531  10.954 1.00 24.17 ? 319 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 27.916 7.975   1.725  1.00 30.93 ? 320 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 10.441 9.909   31.390 1.00 23.52 ? 321 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 4.795  -3.726  28.975 1.00 24.93 ? 322 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 12.467 22.267  12.954 1.00 21.92 ? 323 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 12.997 -5.836  30.578 1.00 35.81 ? 324 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 30.559 10.578  15.612 1.00 25.54 ? 325 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 33.882 14.094  9.599  1.00 32.60 ? 326 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 29.607 22.220  19.394 1.00 26.75 ? 327 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 19.373 10.070  19.672 1.00 11.73 ? 328 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 23.449 21.688  7.332  1.00 21.81 ? 329 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 7.602  20.300  17.480 1.00 16.77 ? 330 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 33.756 11.167  15.453 1.00 34.51 ? 331 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 19.973 19.852  5.654  1.00 43.87 ? 332 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 0.454  -1.131  19.447 1.00 27.02 ? 333 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 25.048 5.106   21.494 1.00 32.35 ? 334 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 14.536 11.377  0.087  1.00 34.38 ? 335 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 5.088  14.551  20.322 1.00 20.31 ? 336 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? -0.067 1.261   15.731 1.00 12.00 ? 337 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 16.049 23.977  14.852 1.00 34.23 ? 338 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? -2.987 9.872   28.048 1.00 26.43 ? 339 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 14.303 13.596  23.993 1.00 17.81 ? 340 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 29.275 11.065  3.247  1.00 52.33 ? 341 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 8.628  19.081  19.740 1.00 18.08 ? 342 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 0.759  12.253  21.185 1.00 26.54 ? 343 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 12.158 16.722  27.804 1.00 26.82 ? 344 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 21.953 2.432   -0.832 1.00 32.53 ? 345 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 3.365  20.709  24.452 1.00 29.34 ? 346 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 21.541 4.942   24.785 1.00 37.25 ? 347 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 10.876 5.499   3.336  1.00 22.63 ? 348 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 4.159  9.526   28.073 1.00 26.02 ? 349 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 6.641  3.346   3.249  1.00 34.38 ? 350 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 16.618 3.908   23.700 1.00 16.75 ? 351 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 22.729 0.906   17.486 1.00 15.49 ? 352 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 20.752 -0.998  3.039  1.00 28.80 ? 353 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 11.440 12.687  11.051 1.00 14.48 ? 354 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 26.949 -1.231  8.918  1.00 21.87 ? 355 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 8.575  24.690  23.885 1.00 21.61 ? 356 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 21.016 -4.163  14.242 1.00 15.15 ? 357 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 18.424 21.893  9.625  1.00 17.48 ? 358 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 13.734 4.044   23.550 1.00 11.67 ? 359 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 31.689 19.918  11.699 1.00 19.38 ? 360 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 1.353  5.240   27.288 1.00 22.18 ? 361 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 34.069 -2.377  13.606 1.00 29.61 ? 362 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 17.170 -3.381  27.803 1.00 33.12 ? 363 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 31.061 -2.128  15.698 1.00 43.53 ? 364 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 2.954  14.724  23.725 1.00 40.29 ? 365 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 7.333  26.425  14.521 1.00 28.83 ? 366 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 15.332 -5.154  27.538 1.00 40.85 ? 367 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 5.434  5.328   32.699 1.00 18.30 ? 368 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 28.995 3.392   12.714 1.00 14.29 ? 369 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? -0.713 3.821   5.877  1.00 34.41 ? 370 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 5.232  8.369   2.224  1.00 32.49 ? 371 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 11.684 18.170  4.933  1.00 45.14 ? 372 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 28.900 15.918  4.354  1.00 29.35 ? 373 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 17.615 -5.153  12.265 1.00 34.32 ? 374 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 23.500 11.652  21.929 1.00 32.62 ? 375 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 20.931 -2.585  16.885 1.00 14.56 ? 376 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 3.220  0.278   29.127 1.00 32.49 ? 377 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 29.468 11.883  21.235 1.00 30.76 ? 378 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 13.316 11.419  9.180  1.00 12.19 ? 379 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 35.302 10.770  12.126 1.00 39.84 ? 380 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 3.802  12.841  17.661 1.00 27.28 ? 381 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 29.936 11.568  18.470 1.00 26.80 ? 382 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? -3.825 13.809  27.702 1.00 43.77 ? 383 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 9.529  4.036   33.518 1.00 12.07 ? 384 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 5.830  17.495  23.787 1.00 27.00 ? 385 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 17.649 20.018  17.129 1.00 15.36 ? 386 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 22.898 -0.668  5.391  1.00 20.08 ? 387 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 35.976 14.913  10.953 1.00 43.02 ? 388 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 6.723  -6.939  23.823 1.00 24.31 ? 389 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? -2.640 23.401  8.878  1.00 51.31 ? 390 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 3.777  26.918  16.282 1.00 34.00 ? 391 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 34.901 16.524  20.024 1.00 42.31 ? 392 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 29.198 6.828   20.185 1.00 42.40 ? 393 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 14.996 21.839  8.546  1.00 24.76 ? 394 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 36.645 17.936  14.331 1.00 27.00 ? 395 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 11.975 11.093  29.737 1.00 16.58 ? 396 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 9.297  3.264   2.917  1.00 25.36 ? 397 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 32.818 16.623  9.189  1.00 31.53 ? 398 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 3.325  -0.723  20.710 1.00 36.75 ? 399 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 23.428 -6.551  12.170 1.00 28.26 ? 400 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 32.261 1.853   6.204  1.00 34.56 ? 401 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 18.084 17.927  4.328  1.00 36.29 ? 402 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 19.443 2.972   19.460 1.00 18.58 ? 403 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 3.240  -0.363  2.889  1.00 38.35 ? 404 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 16.954 6.368   27.094 1.00 23.30 ? 405 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 30.559 2.982   14.880 1.00 20.23 ? 406 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 24.283 -3.474  16.124 1.00 30.39 ? 407 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 25.589 19.598  21.741 1.00 24.31 ? 408 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 17.633 10.732  26.159 1.00 17.75 ? 409 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 15.289 15.142  3.406  1.00 27.76 ? 410 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 25.271 17.865  4.554  1.00 36.43 ? 411 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 11.491 -7.035  24.926 1.00 31.70 ? 412 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 30.490 4.463   5.747  1.00 21.49 ? 413 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 30.243 -1.377  8.653  1.00 28.23 ? 414 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 36.949 2.317   10.074 1.00 36.47 ? 415 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 2.858  15.961  19.119 1.00 20.24 ? 416 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 31.059 15.593  22.777 1.00 23.07 ? 417 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 2.117  11.340  27.351 1.00 25.10 ? 418 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 4.112  0.030   24.136 1.00 15.77 ? 419 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 16.642 21.232  19.292 1.00 22.83 ? 420 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 32.045 8.689   7.565  1.00 20.84 ? 421 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 14.500 -2.427  17.924 1.00 17.06 ? 422 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 23.586 3.671   -2.378 1.00 46.09 ? 423 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 27.314 -1.347  15.919 1.00 25.79 ? 424 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 3.950  -3.963  6.004  1.00 25.44 ? 425 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 33.942 18.594  10.729 1.00 26.01 ? 426 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 8.237  6.602   33.851 1.00 18.28 ? 427 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 0.256  6.055   6.108  1.00 25.03 ? 428 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 36.366 -0.303  12.404 1.00 35.34 ? 429 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 28.133 17.532  24.167 1.00 22.72 ? 430 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 7.341  13.868  4.751  1.00 19.79 ? 431 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 0.117  2.802   23.580 1.00 15.93 ? 432 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 20.531 -4.554  11.333 1.00 29.91 ? 433 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 8.682  -6.464  9.700  1.00 26.97 ? 434 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 22.684 19.567  19.767 1.00 32.85 ? 435 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 5.205  26.437  20.144 1.00 23.73 ? 436 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 17.539 0.807   20.293 1.00 17.95 ? 437 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 3.142  7.774   24.590 1.00 17.27 ? 438 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 19.868 13.302  2.318  1.00 31.59 ? 439 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 6.400  24.194  10.652 1.00 28.56 ? 440 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 19.446 -0.578  33.580 1.00 40.53 ? 441 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 31.096 19.378  8.835  1.00 42.15 ? 442 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 21.065 9.935   21.900 1.00 15.68 ? 443 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 23.265 19.155  6.361  1.00 18.28 ? 444 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 8.515  20.970  7.703  1.00 45.07 ? 445 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 33.982 5.162   16.659 1.00 32.86 ? 446 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 36.708 16.004  16.593 1.00 34.16 ? 447 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 22.776 3.492   20.899 1.00 20.63 ? 448 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 2.188  14.704  16.653 1.00 26.86 ? 449 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 15.413 -4.927  0.395  1.00 40.63 ? 450 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 19.405 21.468  6.829  1.00 37.50 ? 451 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 17.273 -2.385  19.710 1.00 18.68 ? 452 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 10.463 17.360  25.833 1.00 27.25 ? 453 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 0.758  -0.998  16.886 1.00 22.93 ? 454 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 16.861 -4.039  2.906  1.00 26.16 ? 455 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 23.443 8.305   21.683 1.00 24.94 ? 456 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 14.359 24.509  18.185 1.00 38.79 ? 457 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 15.891 21.500  7.299  1.00 24.33 ? 458 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 17.883 24.429  10.557 1.00 33.54 ? 459 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 25.148 10.698  23.058 1.00 36.55 ? 460 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 11.248 -9.664  1.735  1.00 48.35 ? 461 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 7.867  11.115  31.591 1.00 30.65 ? 462 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 34.173 7.869   16.669 1.00 29.89 ? 463 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 6.066  -3.638  31.563 1.00 27.15 ? 464 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 17.358 23.561  17.371 1.00 35.21 ? 465 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 19.793 9.283   -0.942 1.00 28.23 ? 466 HOH   A O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? -1.331 -3.010  15.532 1.00 29.13 ? 467 HOH   A O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 1.024  7.973   27.639 1.00 24.65 ? 468 HOH   A O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 7.842  16.984  26.088 1.00 35.05 ? 469 HOH   A O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 1.240  -4.960  17.286 1.00 37.71 ? 470 HOH   A O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 20.499 20.750  18.580 1.00 39.17 ? 471 HOH   A O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 2.189  -5.245  14.499 1.00 45.31 ? 472 HOH   A O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 17.414 8.976   28.445 1.00 29.17 ? 473 HOH   A O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? -0.876 24.322  12.123 1.00 42.51 ? 474 HOH   A O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 19.030 -3.556  33.685 1.00 44.56 ? 475 HOH   A O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 31.848 7.020   5.387  1.00 29.00 ? 476 HOH   A O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 31.838 9.179   17.354 1.00 42.06 ? 477 HOH   A O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 14.582 13.417  28.638 1.00 37.93 ? 478 HOH   A O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 1.597  15.136  21.402 1.00 38.04 ? 479 HOH   A O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 15.966 13.165  26.116 1.00 23.50 ? 480 HOH   A O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 13.857 -6.643  25.882 1.00 49.05 ? 481 HOH   A O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 2.804  -0.454  26.611 1.00 28.15 ? 482 HOH   A O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 16.801 -5.065  34.356 1.00 32.83 ? 483 HOH   A O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 30.959 12.873  22.960 1.00 39.54 ? 484 HOH   A O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 21.632 19.729  4.204  1.00 36.50 ? 485 HOH   A O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 29.881 0.678   16.500 1.00 31.32 ? 486 HOH   A O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 11.882 24.296  14.897 1.00 31.49 ? 487 HOH   A O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 18.564 2.091   22.750 1.00 36.64 ? 488 HOH   A O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 36.809 20.483  17.683 1.00 34.05 ? 489 HOH   A O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 0.232  0.092   23.071 1.00 22.06 ? 490 HOH   A O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 23.903 1.048   19.890 1.00 33.29 ? 491 HOH   A O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 2.401  14.181  26.340 1.00 35.32 ? 492 HOH   A O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 30.352 7.033   17.905 1.00 32.51 ? 493 HOH   A O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 11.445 23.314  10.845 1.00 34.95 ? 494 HOH   A O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 12.345 -5.031  33.160 1.00 33.17 ? 495 HOH   A O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 21.394 11.355  24.426 1.00 35.29 ? 496 HOH   A O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 21.406 2.993   23.222 1.00 34.24 ? 497 HOH   A O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 13.921 25.209  16.030 1.00 31.92 ? 498 HOH   A O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 4.909  28.407  18.285 1.00 27.95 ? 499 HOH   A O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 37.893 -4.550  6.741  1.00 26.60 ? 500 HOH   A O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 31.346 4.534   17.029 1.00 23.58 ? 501 HOH   A O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 2.595  -1.617  22.711 1.00 25.31 ? 502 HOH   A O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 21.347 -1.029  19.008 1.00 26.54 ? 503 HOH   A O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? -0.356 13.784  16.869 1.00 26.33 ? 504 HOH   A O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 1.277  1.177   27.753 1.00 34.13 ? 505 HOH   A O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 1.390  18.770  24.558 1.00 37.00 ? 506 HOH   A O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 39.254 -2.673  10.607 1.00 33.42 ? 507 HOH   A O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 6.026  11.681  29.560 1.00 30.15 ? 508 HOH   A O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 1.170  -3.758  6.638  1.00 57.60 ? 509 HOH   A O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 1.356  12.281  18.333 1.00 38.81 ? 510 HOH   A O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 38.119 19.809  15.342 1.00 38.75 ? 511 HOH   A O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 9.903  25.936  13.812 1.00 33.39 ? 512 HOH   A O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 4.229  -6.867  23.543 1.00 41.81 ? 513 HOH   A O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 1.205  26.488  17.511 1.00 37.58 ? 514 HOH   A O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 26.486 0.403   20.238 1.00 52.12 ? 515 HOH   A O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 27.615 -21.159 1.445  1.00 40.75 ? 301 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 38.684 -18.574 21.612 1.00 24.78 ? 302 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 31.064 -23.809 -1.292 1.00 23.04 ? 303 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 17.940 -33.342 24.232 1.00 37.20 ? 304 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 31.132 -32.464 0.745  1.00 34.41 ? 305 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 15.020 -18.636 32.117 1.00 36.39 ? 306 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 38.436 -7.351  6.967  1.00 18.17 ? 307 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 24.830 -5.918  15.290 1.00 23.98 ? 308 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 16.546 -17.068 11.278 1.00 35.67 ? 309 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 22.086 -26.030 34.399 1.00 24.68 ? 310 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 41.207 -10.717 23.183 1.00 41.55 ? 311 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 31.051 -18.166 26.964 1.00 16.82 ? 312 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 16.427 -15.985 9.063  1.00 38.22 ? 313 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 18.107 -5.955  24.176 1.00 25.76 ? 314 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 19.896 -4.103  20.263 1.00 20.83 ? 315 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 24.856 -9.856  27.066 1.00 37.99 ? 316 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 43.334 -3.791  18.914 1.00 40.28 ? 317 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 25.722 -35.641 3.147  1.00 42.55 ? 318 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 20.880 -18.721 12.945 1.00 13.34 ? 319 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 29.808 -31.333 32.795 1.00 26.74 ? 320 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 35.116 -32.807 3.310  1.00 34.28 ? 321 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 14.887 -23.900 12.474 1.00 29.45 ? 322 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 37.360 -10.464 4.972  1.00 36.10 ? 323 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 23.158 -5.906  21.252 1.00 17.78 ? 324 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 37.458 -31.838 10.945 1.00 23.88 ? 325 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 14.309 -24.303 29.414 1.00 31.15 ? 326 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 13.093 -14.831 33.230 1.00 46.15 ? 327 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 36.308 -17.690 11.758 1.00 20.65 ? 328 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 34.527 -33.617 24.219 1.00 38.23 ? 329 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 5.269  -12.156 14.737 1.00 46.85 ? 330 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 26.825 -15.234 30.895 1.00 26.95 ? 331 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 18.069 -27.541 16.647 1.00 17.77 ? 332 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 10.440 -17.522 18.503 1.00 24.19 ? 333 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 24.816 -15.756 7.455  1.00 17.70 ? 334 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 18.811 -8.760  13.890 1.00 25.41 ? 335 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 31.319 -21.481 28.485 1.00 15.24 ? 336 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 28.508 -5.166  18.549 1.00 40.64 ? 337 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 36.008 -28.477 2.770  1.00 36.20 ? 338 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 37.602 -18.722 28.174 1.00 19.00 ? 339 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 40.662 -27.312 15.159 1.00 11.05 ? 340 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 26.007 -37.783 24.398 1.00 32.89 ? 341 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 3.533  -12.995 20.663 1.00 43.49 ? 342 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 10.753 -16.805 12.652 1.00 31.52 ? 343 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 10.123 -8.905  24.075 1.00 30.25 ? 344 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 7.558  -30.476 22.276 1.00 25.05 ? 345 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 13.431 -29.620 19.445 1.00 24.14 ? 346 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 40.353 -29.612 11.874 1.00 23.27 ? 347 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 19.477 -27.708 28.320 1.00 17.13 ? 348 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 22.018 -21.646 4.671  1.00 40.24 ? 349 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 42.825 -11.362 11.192 1.00 17.98 ? 350 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 26.106 -25.258 8.881  1.00 12.09 ? 351 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 36.403 -26.316 34.346 1.00 30.76 ? 352 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 24.030 -8.143  9.601  1.00 21.20 ? 353 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 32.833 -23.669 29.200 1.00 14.25 ? 354 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 17.097 -9.303  27.812 1.00 32.53 ? 355 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 40.219 -25.283 7.076  1.00 31.01 ? 356 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 30.085 -15.273 19.670 1.00 13.62 ? 357 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 20.943 -25.670 13.921 1.00 18.64 ? 358 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 26.705 -5.437  9.985  1.00 20.36 ? 359 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 13.527 -11.158 28.688 1.00 30.28 ? 360 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 12.155 -24.286 21.848 1.00 16.09 ? 361 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 6.200  -16.775 22.719 1.00 45.48 ? 362 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 32.212 -10.515 13.807 1.00 16.08 ? 363 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 31.240 -6.159  5.733  1.00 37.21 ? 364 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 35.371 -13.154 8.737  1.00 16.41 ? 365 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 7.238  -9.333  22.973 1.00 39.08 ? 366 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 4.028  -8.406  14.756 1.00 27.42 ? 367 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 10.631 -16.888 15.382 1.00 32.67 ? 368 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 9.556  -8.209  21.663 1.00 28.92 ? 369 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 23.267 -25.301 9.029  1.00 19.18 ? 370 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 17.603 -23.963 8.855  1.00 39.07 ? 371 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 22.015 -28.536 4.915  1.00 24.07 ? 372 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 24.479 -13.831 5.509  1.00 40.22 ? 373 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 14.802 -28.751 25.692 1.00 34.08 ? 374 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 45.493 -14.775 4.664  1.00 27.41 ? 375 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 23.901 -33.648 29.151 1.00 27.81 ? 376 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 29.940 -13.121 13.011 1.00 14.43 ? 377 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 22.872 -33.247 5.564  1.00 29.01 ? 378 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 23.124 -8.475  14.142 1.00 14.30 ? 379 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 32.120 -34.887 31.872 1.00 36.45 ? 380 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 4.916  -25.150 25.616 1.00 37.72 ? 381 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 33.175 -9.844  11.155 1.00 13.17 ? 382 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 28.508 -8.230  25.911 1.00 46.07 ? 383 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 19.888 -32.123 19.852 1.00 42.19 ? 384 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 24.094 -3.307  19.039 1.00 40.26 ? 385 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 34.906 -35.048 18.012 1.00 26.74 ? 386 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 10.221 -24.869 20.064 1.00 19.07 ? 387 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 31.433 -12.167 10.664 1.00 14.44 ? 388 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 38.595 -26.044 28.328 1.00 28.30 ? 389 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 11.232 -21.698 13.885 1.00 35.75 ? 390 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 27.072 -12.076 27.692 1.00 22.94 ? 391 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 5.993  -12.376 23.367 1.00 45.80 ? 392 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 20.269 -32.378 15.700 1.00 53.03 ? 393 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 28.367 -16.357 22.160 1.00 11.71 ? 394 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 9.533  -27.443 19.218 1.00 26.99 ? 395 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 39.535 -33.256 14.181 1.00 43.27 ? 396 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 11.066 -6.445  13.301 1.00 23.33 ? 397 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 21.755 -18.974 5.974  1.00 27.33 ? 398 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 32.466 -34.531 24.798 1.00 28.60 ? 399 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 23.128 -28.219 12.726 1.00 20.93 ? 400 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 27.311 -35.710 20.867 1.00 24.05 ? 401 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 26.590 -31.201 14.957 1.00 18.06 ? 402 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 34.609 -13.426 25.513 1.00 17.21 ? 403 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 35.858 -24.669 24.708 1.00 14.19 ? 404 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 30.393 -15.982 30.531 1.00 29.57 ? 405 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 42.101 -12.755 20.701 1.00 28.98 ? 406 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 39.341 -15.896 4.175  1.00 43.04 ? 407 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 11.792 -22.624 28.897 1.00 25.49 ? 408 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 40.173 -13.788 12.424 1.00 24.58 ? 409 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 41.712 -15.204 21.984 1.00 28.25 ? 410 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 42.461 -12.068 13.975 1.00 24.00 ? 411 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 22.377 -23.719 6.159  1.00 35.12 ? 412 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 28.959 -36.276 7.841  1.00 18.58 ? 413 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 33.440 -33.048 0.919  1.00 40.74 ? 414 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 26.878 -5.963  22.056 1.00 25.90 ? 415 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 6.535  -17.072 19.630 1.00 45.09 ? 416 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 38.238 -31.201 26.060 1.00 28.71 ? 417 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 35.349 -13.782 5.973  1.00 29.52 ? 418 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 41.793 -13.798 10.196 1.00 23.61 ? 419 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 35.181 -4.168  17.607 1.00 23.87 ? 420 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 37.141 -29.290 10.057 1.00 20.15 ? 421 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 27.040 -19.130 1.712  1.00 22.88 ? 422 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 4.417  -10.386 19.862 1.00 33.77 ? 423 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 23.185 -7.449  25.573 1.00 38.92 ? 424 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 20.674 -23.632 34.974 1.00 26.55 ? 425 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 36.429 -21.264 6.937  1.00 22.92 ? 426 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 31.611 -13.609 4.461  1.00 30.39 ? 427 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 26.378 -31.038 30.856 1.00 16.42 ? 428 HOH   C O   1 
HETATM 2578 O  O   . HOH   I 5 .   ? 8.920  -13.321 10.943 1.00 21.70 ? 429 HOH   C O   1 
HETATM 2579 O  O   . HOH   I 5 .   ? 4.856  -27.965 23.412 1.00 30.97 ? 430 HOH   C O   1 
HETATM 2580 O  O   . HOH   I 5 .   ? 22.820 -13.726 29.715 1.00 32.56 ? 431 HOH   C O   1 
HETATM 2581 O  O   . HOH   I 5 .   ? 35.894 -28.571 7.744  1.00 19.16 ? 432 HOH   C O   1 
HETATM 2582 O  O   . HOH   I 5 .   ? 37.815 -20.025 5.134  1.00 34.00 ? 433 HOH   C O   1 
HETATM 2583 O  O   . HOH   I 5 .   ? 33.346 -30.333 31.729 1.00 17.10 ? 434 HOH   C O   1 
HETATM 2584 O  O   . HOH   I 5 .   ? 10.023 -18.508 26.917 1.00 28.65 ? 435 HOH   C O   1 
HETATM 2585 O  O   . HOH   I 5 .   ? 17.369 -25.285 12.927 1.00 22.94 ? 436 HOH   C O   1 
HETATM 2586 O  O   . HOH   I 5 .   ? 42.000 -12.239 18.056 1.00 19.42 ? 437 HOH   C O   1 
HETATM 2587 O  O   . HOH   I 5 .   ? 20.451 -32.333 22.449 1.00 28.41 ? 438 HOH   C O   1 
HETATM 2588 O  O   . HOH   I 5 .   ? 36.955 -32.140 25.170 1.00 31.90 ? 439 HOH   C O   1 
HETATM 2589 O  O   . HOH   I 5 .   ? 34.577 -23.212 -0.788 1.00 37.16 ? 440 HOH   C O   1 
HETATM 2590 O  O   . HOH   I 5 .   ? 6.690  -22.875 18.607 1.00 30.94 ? 441 HOH   C O   1 
HETATM 2591 O  O   . HOH   I 5 .   ? 18.736 -11.789 7.935  1.00 41.24 ? 442 HOH   C O   1 
HETATM 2592 O  O   . HOH   I 5 .   ? 16.530 -20.506 11.756 1.00 26.27 ? 443 HOH   C O   1 
HETATM 2593 O  O   . HOH   I 5 .   ? 30.208 -10.336 27.560 1.00 41.28 ? 444 HOH   C O   1 
HETATM 2594 O  O   . HOH   I 5 .   ? 10.918 -11.955 9.136  1.00 27.49 ? 445 HOH   C O   1 
HETATM 2595 O  O   . HOH   I 5 .   ? 32.965 -14.340 9.471  1.00 14.36 ? 446 HOH   C O   1 
HETATM 2596 O  O   . HOH   I 5 .   ? 10.546 -31.025 25.412 1.00 29.68 ? 447 HOH   C O   1 
HETATM 2597 O  O   . HOH   I 5 .   ? 40.187 -30.008 14.575 1.00 15.58 ? 448 HOH   C O   1 
HETATM 2598 O  O   . HOH   I 5 .   ? 18.864 -8.267  25.644 1.00 18.22 ? 449 HOH   C O   1 
HETATM 2599 O  O   . HOH   I 5 .   ? 39.086 -12.933 25.888 1.00 21.82 ? 450 HOH   C O   1 
HETATM 2600 O  O   . HOH   I 5 .   ? 9.933  -24.629 29.574 1.00 43.49 ? 451 HOH   C O   1 
HETATM 2601 O  O   . HOH   I 5 .   ? 4.182  -12.710 17.608 1.00 41.04 ? 452 HOH   C O   1 
HETATM 2602 O  O   . HOH   I 5 .   ? 14.722 -18.388 10.425 1.00 37.26 ? 453 HOH   C O   1 
HETATM 2603 O  O   . HOH   I 5 .   ? 34.402 -15.667 27.226 1.00 31.81 ? 454 HOH   C O   1 
HETATM 2604 O  O   . HOH   I 5 .   ? 18.882 -19.099 11.007 1.00 17.60 ? 455 HOH   C O   1 
HETATM 2605 O  O   . HOH   I 5 .   ? 42.650 -19.935 29.386 1.00 33.54 ? 456 HOH   C O   1 
HETATM 2606 O  O   . HOH   I 5 .   ? 37.726 -13.824 10.039 1.00 24.36 ? 457 HOH   C O   1 
HETATM 2607 O  O   . HOH   I 5 .   ? 33.911 -36.047 8.837  1.00 36.13 ? 458 HOH   C O   1 
HETATM 2608 O  O   . HOH   I 5 .   ? 15.211 -30.010 18.354 1.00 47.26 ? 459 HOH   C O   1 
HETATM 2609 O  O   . HOH   I 5 .   ? 30.494 -17.892 8.356  1.00 27.34 ? 460 HOH   C O   1 
HETATM 2610 O  O   . HOH   I 5 .   ? 23.550 -31.117 13.347 1.00 30.45 ? 461 HOH   C O   1 
HETATM 2611 O  O   . HOH   I 5 .   ? 43.665 -25.414 26.148 1.00 23.82 ? 462 HOH   C O   1 
HETATM 2612 O  O   . HOH   I 5 .   ? 4.770  -16.265 17.655 1.00 39.97 ? 463 HOH   C O   1 
HETATM 2613 O  O   . HOH   I 5 .   ? 6.644  -20.040 18.348 1.00 32.03 ? 464 HOH   C O   1 
HETATM 2614 O  O   . HOH   I 5 .   ? 38.182 -23.576 4.517  1.00 40.00 ? 465 HOH   C O   1 
HETATM 2615 O  O   . HOH   I 5 .   ? 23.810 -17.564 33.464 1.00 19.44 ? 466 HOH   C O   1 
HETATM 2616 O  O   . HOH   I 5 .   ? 24.410 -16.537 3.292  1.00 40.77 ? 467 HOH   C O   1 
HETATM 2617 O  O   . HOH   I 5 .   ? 31.997 -15.691 6.966  1.00 32.06 ? 468 HOH   C O   1 
HETATM 2618 O  O   . HOH   I 5 .   ? 22.443 -11.558 7.172  1.00 40.49 ? 469 HOH   C O   1 
HETATM 2619 O  O   . HOH   I 5 .   ? 36.868 -24.533 27.235 1.00 29.75 ? 470 HOH   C O   1 
HETATM 2620 O  O   . HOH   I 5 .   ? 21.468 -17.504 34.658 1.00 22.38 ? 471 HOH   C O   1 
HETATM 2621 O  O   . HOH   I 5 .   ? 39.778 -14.229 8.358  1.00 24.34 ? 472 HOH   C O   1 
HETATM 2622 O  O   . HOH   I 5 .   ? 34.944 -30.359 33.934 1.00 37.01 ? 473 HOH   C O   1 
HETATM 2623 O  O   . HOH   I 5 .   ? 34.498 -31.868 29.510 1.00 21.43 ? 474 HOH   C O   1 
HETATM 2624 O  O   . HOH   I 5 .   ? 39.092 -33.671 17.308 1.00 45.42 ? 475 HOH   C O   1 
HETATM 2625 O  O   . HOH   I 5 .   ? 26.209 -35.317 7.490  1.00 22.88 ? 476 HOH   C O   1 
HETATM 2626 O  O   . HOH   I 5 .   ? 24.112 -15.703 31.532 1.00 27.81 ? 477 HOH   C O   1 
HETATM 2627 O  O   . HOH   I 5 .   ? 9.043  -19.131 17.151 1.00 37.77 ? 478 HOH   C O   1 
HETATM 2628 O  O   . HOH   I 5 .   ? 10.417 -19.996 29.132 1.00 34.95 ? 479 HOH   C O   1 
HETATM 2629 O  O   . HOH   I 5 .   ? 24.729 -11.800 28.984 1.00 41.76 ? 480 HOH   C O   1 
HETATM 2630 O  O   . HOH   I 5 .   ? 21.579 -26.857 10.447 1.00 30.30 ? 481 HOH   C O   1 
HETATM 2631 O  O   . HOH   I 5 .   ? 22.916 -16.762 5.473  1.00 38.12 ? 482 HOH   C O   1 
HETATM 2632 O  O   . HOH   I 5 .   ? 16.573 -27.515 14.356 1.00 30.24 ? 483 HOH   C O   1 
HETATM 2633 O  O   . HOH   I 5 .   ? 20.882 -12.159 30.724 1.00 37.41 ? 484 HOH   C O   1 
HETATM 2634 O  O   . HOH   I 5 .   ? 18.303 -16.607 38.264 1.00 31.06 ? 485 HOH   C O   1 
HETATM 2635 O  O   . HOH   I 5 .   ? 28.330 -12.674 30.353 1.00 41.48 ? 486 HOH   C O   1 
HETATM 2636 O  O   . HOH   I 5 .   ? 33.605 -20.510 -2.150 1.00 39.31 ? 487 HOH   C O   1 
HETATM 2637 O  O   . HOH   I 5 .   ? 18.479 -25.928 10.289 1.00 41.29 ? 488 HOH   C O   1 
HETATM 2638 O  O   . HOH   I 5 .   ? 22.287 -2.923  20.806 1.00 43.65 ? 489 HOH   C O   1 
HETATM 2639 O  O   . HOH   I 5 .   ? 32.920 -19.438 29.182 1.00 30.24 ? 490 HOH   C O   1 
HETATM 2640 O  O   . HOH   I 5 .   ? 22.450 -7.899  11.518 1.00 29.07 ? 491 HOH   C O   1 
HETATM 2641 O  O   . HOH   I 5 .   ? 40.494 -27.984 7.240  1.00 42.59 ? 492 HOH   C O   1 
HETATM 2642 O  O   . HOH   I 5 .   ? 18.112 -17.943 8.545  1.00 31.24 ? 493 HOH   C O   1 
HETATM 2643 O  O   . HOH   I 5 .   ? 38.024 -15.594 12.064 1.00 27.93 ? 494 HOH   C O   1 
HETATM 2644 O  O   . HOH   I 5 .   ? 17.241 -28.924 29.013 1.00 38.95 ? 495 HOH   C O   1 
HETATM 2645 O  O   . HOH   I 5 .   ? 10.257 -21.208 16.644 1.00 32.49 ? 496 HOH   C O   1 
HETATM 2646 O  O   . HOH   I 5 .   ? 27.472 -15.359 33.646 1.00 32.00 ? 497 HOH   C O   1 
HETATM 2647 O  O   . HOH   I 5 .   ? 9.267  -23.420 17.896 1.00 29.48 ? 498 HOH   C O   1 
HETATM 2648 O  O   . HOH   I 5 .   ? 35.790 -20.373 29.407 1.00 29.55 ? 499 HOH   C O   1 
HETATM 2649 O  O   . HOH   I 5 .   ? 35.514 -23.011 29.057 1.00 23.95 ? 500 HOH   C O   1 
HETATM 2650 O  O   . HOH   I 5 .   ? 3.206  -8.524  21.968 1.00 40.35 ? 501 HOH   C O   1 
HETATM 2651 O  O   . HOH   I 5 .   ? 7.329  -27.673 17.657 1.00 36.71 ? 502 HOH   C O   1 
HETATM 2652 O  O   . HOH   I 5 .   ? 33.098 -17.126 2.093  1.00 43.98 ? 503 HOH   C O   1 
HETATM 2653 O  O   . HOH   I 5 .   ? 19.466 -17.588 5.837  1.00 40.74 ? 504 HOH   C O   1 
HETATM 2654 O  O   . HOH   I 5 .   ? 3.472  -9.551  17.118 1.00 33.72 ? 505 HOH   C O   1 
HETATM 2655 O  O   . HOH   I 5 .   ? 19.990 -15.217 34.784 1.00 31.87 ? 506 HOH   C O   1 
HETATM 2656 O  O   . HOH   I 5 .   ? 36.444 -35.390 8.021  1.00 57.15 ? 507 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   ? 0.1625 0.1721 0.1642 -0.0028 -0.0136 -0.0052 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1732 0.1839 0.1792 -0.0018 -0.0149 -0.0045 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1740 0.1840 0.1818 0.0003  -0.0155 -0.0018 7   SER   A C   
4    O O   . SER   A 1   ? 0.1899 0.1988 0.1951 0.0006  -0.0155 -0.0003 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2119 0.2257 0.2169 -0.0034 -0.0176 -0.0047 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2531 0.2680 0.2551 -0.0034 -0.0199 -0.0019 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1528 0.1631 0.1649 0.0014  -0.0157 -0.0014 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1485 0.1580 0.1627 0.0029  -0.0156 0.0004  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1453 0.1545 0.1635 0.0037  -0.0142 -0.0001 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1614 0.1705 0.1803 0.0033  -0.0129 -0.0013 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1320 0.1409 0.1530 0.0045  -0.0140 0.0009  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1353 0.1439 0.1595 0.0048  -0.0124 0.0003  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1335 0.1408 0.1587 0.0052  -0.0108 0.0008  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1465 0.1527 0.1712 0.0055  -0.0111 0.0019  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1465 0.1569 0.1751 0.0050  -0.0134 -0.0001 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1239 0.1309 0.1500 0.0047  -0.0088 0.0000  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1176 0.1234 0.1450 0.0043  -0.0066 -0.0004 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1317 0.1377 0.1644 0.0048  -0.0059 -0.0008 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1287 0.1360 0.1628 0.0047  -0.0061 -0.0012 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1225 0.1286 0.1468 0.0027  -0.0047 -0.0012 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1419 0.1487 0.1619 0.0022  -0.0055 -0.0005 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1383 0.1431 0.1631 0.0014  -0.0019 -0.0024 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1638 0.1727 0.1816 0.0007  -0.0045 -0.0004 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1254 0.1303 0.1619 0.0055  -0.0048 -0.0006 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1365 0.1418 0.1793 0.0061  -0.0038 -0.0009 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1369 0.1401 0.1808 0.0050  0.0003  -0.0026 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1387 0.1398 0.1848 0.0054  0.0020  -0.0025 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1426 0.1490 0.1906 0.0080  -0.0059 0.0013  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1325 0.1418 0.1790 0.0083  -0.0099 0.0024  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1491 0.1610 0.1983 0.0080  -0.0110 0.0016  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1512 0.1605 0.1932 0.0083  -0.0120 0.0037  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1527 0.1671 0.2000 0.0075  -0.0140 0.0018  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1652 0.1773 0.2051 0.0077  -0.0151 0.0040  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1651 0.1796 0.2074 0.0072  -0.0160 0.0029  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1952 0.2123 0.2352 0.0060  -0.0185 0.0024  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1352 0.1388 0.1777 0.0034  0.0023  -0.0043 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1388 0.1409 0.1810 0.0013  0.0065  -0.0066 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1568 0.1595 0.2034 0.0010  0.0084  -0.0076 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1421 0.1466 0.1882 0.0012  0.0068  -0.0070 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1590 0.1619 0.1934 -0.0013 0.0070  -0.0073 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1706 0.1760 0.2022 -0.0013 0.0048  -0.0059 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1782 0.1803 0.2115 -0.0044 0.0115  -0.0101 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1575 0.1584 0.2094 0.0009  0.0119  -0.0091 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1541 0.1555 0.2113 0.0007  0.0142  -0.0103 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1467 0.1506 0.2088 0.0030  0.0107  -0.0084 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1452 0.1500 0.2102 0.0052  0.0076  -0.0062 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1435 0.1490 0.2054 0.0021  0.0109  -0.0089 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1383 0.1463 0.2039 0.0036  0.0077  -0.0076 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1380 0.1468 0.1973 0.0031  0.0049  -0.0067 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1377 0.1480 0.1986 0.0030  0.0040  -0.0067 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1430 0.1520 0.2153 0.0033  0.0099  -0.0089 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1993 0.2084 0.2810 0.0047  0.0118  -0.0090 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2259 0.2377 0.3143 0.0067  0.0090  -0.0073 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2106 0.2170 0.2928 0.0035  0.0165  -0.0110 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1247 0.1327 0.1778 0.0029  0.0037  -0.0060 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1228 0.1315 0.1708 0.0027  0.0015  -0.0049 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1196 0.1286 0.1659 0.0039  -0.0017 -0.0038 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1253 0.1333 0.1715 0.0045  -0.0017 -0.0035 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1193 0.1275 0.1610 0.0009  0.0032  -0.0048 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1391 0.1473 0.1808 -0.0009 0.0063  -0.0056 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1528 0.1617 0.1967 -0.0009 0.0065  -0.0052 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1741 0.1819 0.2131 -0.0030 0.0092  -0.0069 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1615 0.1704 0.2048 -0.0028 0.0095  -0.0056 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1891 0.1973 0.2269 -0.0053 0.0122  -0.0076 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1902 0.1990 0.2299 -0.0051 0.0122  -0.0067 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2284 0.2376 0.2669 -0.0074 0.0153  -0.0072 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1108 0.1207 0.1557 0.0041  -0.0038 -0.0034 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1115 0.1217 0.1535 0.0046  -0.0064 -0.0026 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1193 0.1290 0.1568 0.0040  -0.0060 -0.0023 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1184 0.1282 0.1569 0.0037  -0.0052 -0.0025 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1238 0.1361 0.1688 0.0049  -0.0088 -0.0028 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1309 0.1436 0.1720 0.0047  -0.0111 -0.0027 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1446 0.1604 0.1884 0.0041  -0.0136 -0.0031 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1514 0.1674 0.1921 0.0027  -0.0141 -0.0046 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1769 0.1934 0.2134 0.0021  -0.0158 -0.0045 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1817 0.1985 0.2164 0.0029  -0.0173 -0.0025 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1706 0.1871 0.2049 0.0005  -0.0154 -0.0065 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1147 0.1238 0.1480 0.0039  -0.0062 -0.0016 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1149 0.1242 0.1449 0.0036  -0.0059 -0.0008 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1305 0.1396 0.1589 0.0040  -0.0075 -0.0008 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1313 0.1401 0.1579 0.0042  -0.0086 -0.0008 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1216 0.1311 0.1482 0.0027  -0.0048 -0.0002 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1455 0.1563 0.1701 0.0024  -0.0047 0.0014  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1361 0.1456 0.1635 0.0016  -0.0028 -0.0008 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1150 0.1241 0.1442 0.0040  -0.0073 -0.0010 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1113 0.1201 0.1389 0.0039  -0.0081 -0.0018 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1270 0.1359 0.1547 0.0039  -0.0081 -0.0018 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1190 0.1275 0.1469 0.0041  -0.0065 -0.0011 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1388 0.1475 0.1686 0.0043  -0.0052 0.0003  18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1125 0.1218 0.1421 0.0033  -0.0090 -0.0036 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1584 0.1677 0.1884 0.0033  -0.0090 -0.0036 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1325 0.1431 0.1622 0.0033  -0.0112 -0.0035 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1522 0.1617 0.1799 0.0024  -0.0098 -0.0049 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0785 0.0876 0.1122 0.0030  -0.0074 -0.0043 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.1905 0.2011 0.2223 0.0035  -0.0105 -0.0035 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1127 0.1208 0.1390 0.0038  -0.0066 -0.0018 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1166 0.1242 0.1448 0.0042  -0.0045 -0.0013 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1203 0.1267 0.1526 0.0039  -0.0029 -0.0024 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1295 0.1356 0.1618 0.0028  -0.0035 -0.0049 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1170 0.1239 0.1432 0.0036  -0.0042 -0.0028 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1292 0.1369 0.1517 0.0037  -0.0054 -0.0017 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1497 0.1574 0.1689 0.0032  -0.0071 -0.0023 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1329 0.1417 0.1564 0.0044  -0.0045 0.0002  19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1194 0.1255 0.1555 0.0048  -0.0009 -0.0004 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1249 0.1293 0.1655 0.0045  0.0013  -0.0014 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1383 0.1409 0.1796 0.0032  0.0027  -0.0050 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1449 0.1468 0.1877 0.0018  0.0033  -0.0077 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1253 0.1295 0.1701 0.0058  0.0035  0.0021  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1292 0.1312 0.1793 0.0056  0.0062  0.0015  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1406 0.1425 0.1952 0.0072  0.0083  0.0061  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1621 0.1618 0.2221 0.0072  0.0112  0.0067  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.1910 0.1872 0.2562 0.0070  0.0148  0.0048  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.1698 0.1647 0.2351 0.0065  0.0159  0.0016  20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2020 0.1959 0.2726 0.0072  0.0178  0.0061  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1180 0.1204 0.1580 0.0032  0.0034  -0.0055 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1389 0.1394 0.1791 0.0015  0.0055  -0.0094 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.1540 0.1558 0.1893 -0.0009 0.0030  -0.0127 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.1679 0.1689 0.2026 -0.0033 0.0046  -0.0165 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.1489 0.1486 0.1898 0.0021  0.0076  -0.0090 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1343 0.1358 0.1696 0.0019  0.0051  -0.0087 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1463 0.1497 0.1806 0.0036  0.0033  -0.0051 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.1436 0.1450 0.1740 -0.0001 0.0047  -0.0116 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.1527 0.1568 0.1821 0.0028  0.0020  -0.0059 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.1488 0.1516 0.1756 0.0007  0.0027  -0.0095 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1448 0.1489 0.1766 -0.0005 -0.0007 -0.0112 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1386 0.1447 0.1667 -0.0024 -0.0035 -0.0130 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1504 0.1581 0.1808 -0.0025 -0.0052 -0.0129 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.1624 0.1727 0.1910 -0.0036 -0.0081 -0.0134 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1459 0.1532 0.1692 -0.0018 -0.0061 -0.0112 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.1562 0.1623 0.1769 -0.0020 -0.0045 -0.0116 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.1715 0.1786 0.1877 -0.0015 -0.0068 -0.0096 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.1796 0.1853 0.1985 -0.0049 -0.0028 -0.0155 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1467 0.1533 0.1817 -0.0014 -0.0034 -0.0119 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1536 0.1616 0.1913 -0.0015 -0.0045 -0.0120 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1698 0.1793 0.2085 -0.0043 -0.0049 -0.0155 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1698 0.1778 0.2091 -0.0061 -0.0024 -0.0183 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1456 0.1518 0.1875 -0.0002 -0.0021 -0.0102 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1585 0.1713 0.1981 -0.0047 -0.0077 -0.0154 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1579 0.1737 0.1987 -0.0077 -0.0088 -0.0184 24  THR   A CA  
140  C C   . THR   A 18  ? 0.1670 0.1823 0.2137 -0.0083 -0.0066 -0.0198 24  THR   A C   
141  O O   . THR   A 18  ? 0.1454 0.1581 0.1949 -0.0062 -0.0047 -0.0178 24  THR   A O   
142  C CB  . THR   A 18  ? 0.1701 0.1908 0.2101 -0.0077 -0.0133 -0.0168 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.1663 0.1872 0.2107 -0.0054 -0.0136 -0.0144 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.1947 0.2158 0.2292 -0.0070 -0.0155 -0.0148 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.1592 0.1771 0.2077 -0.0114 -0.0069 -0.0232 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.1591 0.1769 0.2134 -0.0123 -0.0050 -0.0246 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.1509 0.1705 0.2085 -0.0099 -0.0067 -0.0216 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1559 0.1730 0.2173 -0.0089 -0.0040 -0.0209 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.1828 0.2045 0.2382 -0.0167 -0.0057 -0.0290 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.2867 0.3098 0.3486 -0.0176 -0.0047 -0.0302 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3452 0.3636 0.4112 -0.0179 0.0001  -0.0318 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3264 0.3547 0.3919 -0.0178 -0.0079 -0.0294 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3530 0.3741 0.4242 -0.0190 -0.0001 -0.0327 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3570 0.3841 0.4284 -0.0187 -0.0048 -0.0311 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1434 0.1670 0.1997 -0.0091 -0.0108 -0.0195 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1457 0.1705 0.2060 -0.0069 -0.0116 -0.0170 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1320 0.1521 0.1913 -0.0042 -0.0090 -0.0146 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1393 0.1587 0.2024 -0.0034 -0.0073 -0.0139 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.1557 0.1851 0.2160 -0.0061 -0.0158 -0.0148 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2544 0.2850 0.3206 -0.0042 -0.0159 -0.0128 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.2783 0.3118 0.3504 -0.0053 -0.0157 -0.0141 26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.2725 0.3009 0.3377 -0.0016 -0.0155 -0.0102 26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1277 0.1451 0.1820 -0.0033 -0.0085 -0.0136 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1310 0.1450 0.1840 -0.0013 -0.0064 -0.0113 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1166 0.1279 0.1724 -0.0016 -0.0028 -0.0116 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1267 0.1372 0.1840 -0.0007 -0.0013 -0.0100 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1186 0.1308 0.1663 -0.0006 -0.0065 -0.0103 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1502 0.1641 0.1947 0.0001  -0.0094 -0.0091 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1419 0.1569 0.1879 0.0011  -0.0104 -0.0077 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1449 0.1586 0.1854 -0.0004 -0.0102 -0.0095 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1165 0.1266 0.1735 -0.0031 -0.0011 -0.0138 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1309 0.1379 0.1915 -0.0032 0.0028  -0.0136 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1319 0.1401 0.1973 -0.0041 0.0035  -0.0145 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1485 0.1546 0.2161 -0.0036 0.0063  -0.0129 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1409 0.1458 0.2026 -0.0049 0.0051  -0.0163 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1361 0.1387 0.1950 -0.0036 0.0061  -0.0147 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1572 0.1603 0.2125 -0.0043 0.0049  -0.0164 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1399 0.1398 0.2000 -0.0015 0.0086  -0.0111 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1510 0.1516 0.2057 -0.0027 0.0068  -0.0143 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1484 0.1474 0.2063 -0.0008 0.0088  -0.0108 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1521 0.1507 0.2149 -0.0003 0.0105  -0.0079 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.1551 0.1524 0.2143 0.0012  0.0107  -0.0070 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.1576 0.1548 0.2209 0.0015  0.0121  -0.0038 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.1650 0.1618 0.2272 0.0024  0.0122  -0.0034 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1217 0.1338 0.1887 -0.0055 0.0010  -0.0167 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1296 0.1435 0.2021 -0.0064 0.0017  -0.0177 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1469 0.1614 0.2201 -0.0046 0.0014  -0.0152 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1521 0.1676 0.2301 -0.0051 0.0027  -0.0157 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1394 0.1581 0.2141 -0.0088 -0.0011 -0.0206 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1349 0.1490 0.2039 -0.0028 0.0000  -0.0129 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1405 0.1548 0.2095 -0.0014 0.0004  -0.0111 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1333 0.1446 0.1970 -0.0004 0.0018  -0.0087 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1359 0.1474 0.1970 0.0005  0.0011  -0.0075 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1408 0.1583 0.2106 -0.0006 -0.0029 -0.0109 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1562 0.1778 0.2322 -0.0017 -0.0043 -0.0125 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.1851 0.2077 0.2665 -0.0018 -0.0028 -0.0128 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.1784 0.2028 0.2540 -0.0030 -0.0071 -0.0137 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1268 0.1358 0.1897 -0.0006 0.0038  -0.0079 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1268 0.1341 0.1852 0.0002  0.0046  -0.0051 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1483 0.1555 0.2050 0.0001  0.0062  -0.0031 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1683 0.1752 0.2277 -0.0007 0.0085  -0.0032 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1285 0.1335 0.1883 0.0001  0.0068  -0.0042 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1292 0.1333 0.1857 0.0012  0.0073  -0.0007 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1460 0.1508 0.1989 0.0020  0.0049  -0.0010 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1791 0.1807 0.2392 0.0014  0.0101  0.0007  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1380 0.1458 0.1899 0.0006  0.0053  -0.0015 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1404 0.1486 0.1894 -0.0003 0.0070  0.0002  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1409 0.1491 0.1868 -0.0001 0.0074  0.0039  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1608 0.1693 0.2061 -0.0010 0.0093  0.0062  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1356 0.1447 0.1817 -0.0004 0.0060  -0.0008 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1616 0.1715 0.2034 -0.0021 0.0078  0.0005  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1591 0.1685 0.2099 -0.0002 0.0059  -0.0035 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1292 0.1376 0.1734 0.0009  0.0056  0.0047  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1393 0.1486 0.1817 0.0013  0.0057  0.0086  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1400 0.1488 0.1830 0.0027  0.0044  0.0085  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1398 0.1484 0.1818 0.0029  0.0028  0.0057  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1456 0.1577 0.1824 0.0000  0.0051  0.0101  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1626 0.1773 0.1972 0.0002  0.0043  0.0142  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1991 0.2155 0.2341 0.0000  0.0052  0.0189  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1632 0.1794 0.1956 0.0008  0.0023  0.0145  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2029 0.2226 0.2364 0.0004  0.0036  0.0222  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1832 0.2026 0.2151 0.0008  0.0020  0.0193  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1644 0.1798 0.1955 0.0012  0.0009  0.0116  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2033 0.2255 0.2336 0.0011  0.0002  0.0208  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1782 0.1957 0.2070 0.0013  -0.0006 0.0128  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.1900 0.2109 0.2188 0.0013  -0.0009 0.0172  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1404 0.1488 0.1859 0.0037  0.0055  0.0114  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1396 0.1475 0.1860 0.0049  0.0048  0.0112  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1556 0.1650 0.2035 0.0059  0.0055  0.0161  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1581 0.1680 0.2081 0.0060  0.0070  0.0198  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1557 0.1604 0.2062 0.0050  0.0062  0.0080  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1645 0.1670 0.2204 0.0050  0.0093  0.0088  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.1864 0.1876 0.2469 0.0064  0.0117  0.0125  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2051 0.2049 0.2696 0.0066  0.0143  0.0150  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1847 0.1861 0.2454 0.0074  0.0114  0.0130  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1473 0.1578 0.1945 0.0067  0.0044  0.0166  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1451 0.1580 0.1950 0.0080  0.0048  0.0217  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1474 0.1592 0.1997 0.0092  0.0052  0.0205  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1454 0.1584 0.1939 0.0087  0.0033  0.0185  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1736 0.1916 0.2184 0.0068  0.0025  0.0248  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2298 0.2520 0.2774 0.0078  0.0022  0.0309  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2353 0.2568 0.2878 0.0097  0.0030  0.0319  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2617 0.2883 0.3062 0.0065  0.0009  0.0346  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1429 0.1519 0.2020 0.0105  0.0082  0.0213  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1417 0.1491 0.2041 0.0114  0.0097  0.0197  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.1611 0.1686 0.2232 0.0114  0.0095  0.0195  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1534 0.1650 0.2158 0.0124  0.0082  0.0233  36  SER   A C   
248  O O   . SER   A 30  ? 0.1464 0.1578 0.2073 0.0123  0.0078  0.0206  36  SER   A O   
249  C CB  A SER   A 30  ? 0.1350 0.1386 0.2057 0.0126  0.0140  0.0203  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2140 0.2173 0.2839 0.0123  0.0139  0.0192  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.1119 0.1134 0.1863 0.0132  0.0164  0.0182  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2983 0.3027 0.3738 0.0139  0.0153  0.0255  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1493 0.1651 0.2132 0.0131  0.0072  0.0293  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1456 0.1667 0.2100 0.0138  0.0054  0.0331  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1471 0.1707 0.2035 0.0119  0.0023  0.0302  37  SER   A C   
256  O O   . SER   A 31  ? 0.1484 0.1752 0.2052 0.0122  0.0013  0.0313  37  SER   A O   
257  C CB  . SER   A 31  ? 0.1766 0.2029 0.2436 0.0144  0.0045  0.0407  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2581 0.2878 0.3176 0.0120  0.0018  0.0412  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1374 0.1594 0.1874 0.0101  0.0011  0.0264  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1299 0.1533 0.1729 0.0084  -0.0012 0.0234  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1276 0.1466 0.1687 0.0082  -0.0008 0.0178  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1251 0.1445 0.1613 0.0070  -0.0024 0.0155  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1490 0.1739 0.1867 0.0063  -0.0025 0.0231  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1507 0.1812 0.1880 0.0055  -0.0035 0.0284  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1434 0.1753 0.1751 0.0029  -0.0041 0.0276  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1411 0.1733 0.1670 0.0009  -0.0051 0.0238  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1452 0.1804 0.1657 -0.0021 -0.0057 0.0233  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1757 0.2140 0.1950 -0.0036 -0.0054 0.0263  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1501 0.1851 0.1665 -0.0039 -0.0060 0.0196  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1193 0.1341 0.1639 0.0089  0.0013  0.0156  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1157 0.1272 0.1579 0.0082  0.0013  0.0107  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1217 0.1329 0.1591 0.0069  -0.0006 0.0085  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1228 0.1332 0.1568 0.0062  -0.0018 0.0057  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1350 0.1465 0.1759 0.0081  0.0013  0.0091  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1341 0.1426 0.1722 0.0070  0.0014  0.0044  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1426 0.1486 0.1827 0.0065  0.0028  0.0022  39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1389 0.1478 0.1726 0.0063  0.0000  0.0030  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1173 0.1293 0.1549 0.0066  -0.0006 0.0100  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1189 0.1306 0.1532 0.0055  -0.0019 0.0079  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1242 0.1341 0.1612 0.0053  -0.0008 0.0067  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1226 0.1320 0.1631 0.0057  0.0010  0.0087  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1236 0.1381 0.1546 0.0045  -0.0027 0.0097  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1451 0.1618 0.1724 0.0039  -0.0040 0.0100  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1510 0.1706 0.1749 0.0020  -0.0043 0.0112  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1506 0.1651 0.1756 0.0038  -0.0049 0.0067  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1194 0.1284 0.1552 0.0047  -0.0017 0.0038  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1201 0.1282 0.1586 0.0042  -0.0010 0.0025  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1207 0.1295 0.1575 0.0037  -0.0022 0.0012  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1226 0.1316 0.1571 0.0037  -0.0039 0.0002  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1267 0.1332 0.1680 0.0040  -0.0005 -0.0001 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1260 0.1320 0.1708 0.0032  0.0003  -0.0018 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1458 0.1500 0.1943 0.0026  0.0023  -0.0036 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1323 0.1397 0.1766 0.0026  -0.0019 -0.0040 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1181 0.1270 0.1565 0.0031  -0.0011 0.0013  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1137 0.1231 0.1522 0.0027  -0.0014 -0.0001 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1115 0.1206 0.1546 0.0025  -0.0008 -0.0017 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1197 0.1283 0.1650 0.0021  0.0010  -0.0012 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1099 0.1200 0.1457 0.0017  0.0000  0.0011  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1303 0.1402 0.1672 0.0011  0.0007  -0.0008 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1306 0.1418 0.1619 0.0014  -0.0008 0.0025  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1128 0.1226 0.1578 0.0027  -0.0023 -0.0033 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1222 0.1330 0.1725 0.0024  -0.0021 -0.0048 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1246 0.1361 0.1773 0.0026  -0.0018 -0.0052 43  SER   A C   
304  O O   . SER   A 37  ? 0.1213 0.1323 0.1716 0.0030  -0.0018 -0.0046 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1430 0.1551 0.1947 0.0022  -0.0044 -0.0062 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1408 0.1539 0.1904 0.0027  -0.0069 -0.0058 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1315 0.1441 0.1897 0.0022  -0.0009 -0.0062 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1405 0.1537 0.2027 0.0026  0.0001  -0.0066 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1620 0.1778 0.2284 0.0037  -0.0029 -0.0064 44  SER   A C   
310  O O   . SER   A 38  ? 0.1850 0.2030 0.2523 0.0034  -0.0054 -0.0067 44  SER   A O   
311  C CB  . SER   A 38  ? 0.1733 0.1867 0.2400 0.0017  0.0029  -0.0077 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2037 0.2188 0.2742 0.0013  0.0016  -0.0085 44  SER   A OG  
313  N N   . THR   A 39  ? 0.1584 0.1741 0.2275 0.0047  -0.0023 -0.0058 45  THR   A N   
314  C CA  . THR   A 39  ? 0.1786 0.1970 0.2525 0.0060  -0.0050 -0.0045 45  THR   A CA  
315  C C   . THR   A 39  ? 0.1879 0.2078 0.2708 0.0068  -0.0033 -0.0046 45  THR   A C   
316  O O   . THR   A 39  ? 0.1774 0.1950 0.2617 0.0063  0.0008  -0.0059 45  THR   A O   
317  C CB  . THR   A 39  ? 0.1991 0.2158 0.2694 0.0070  -0.0057 -0.0030 45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2132 0.2269 0.2840 0.0071  -0.0018 -0.0036 45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2005 0.2158 0.2624 0.0064  -0.0072 -0.0028 45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2023 0.2264 0.2916 0.0078  -0.0063 -0.0030 46  THR   A N   
321  C CA  . THR   A 40  ? 0.2156 0.2418 0.3152 0.0090  -0.0049 -0.0024 46  THR   A CA  
322  C C   . THR   A 40  ? 0.2144 0.2380 0.3164 0.0108  -0.0029 -0.0009 46  THR   A C   
323  O O   . THR   A 40  ? 0.2329 0.2545 0.3402 0.0110  0.0015  -0.0020 46  THR   A O   
324  C CB  . THR   A 40  ? 0.2760 0.3088 0.3820 0.0092  -0.0092 -0.0009 46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3405 0.3754 0.4439 0.0100  -0.0134 0.0020  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2822 0.3171 0.3861 0.0069  -0.0104 -0.0031 46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2116 0.2347 0.3095 0.0116  -0.0054 0.0013  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2262 0.2464 0.3266 0.0132  -0.0033 0.0029  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2228 0.2374 0.3148 0.0119  0.0002  0.0006  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2228 0.2366 0.3059 0.0104  -0.0010 -0.0006 47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2566 0.2793 0.3571 0.0148  -0.0078 0.0069  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.1997 0.2107 0.2949 0.0123  0.0044  0.0000  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2041 0.2105 0.2917 0.0105  0.0078  -0.0023 48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2075 0.2127 0.2900 0.0111  0.0054  -0.0003 48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2263 0.2322 0.3139 0.0133  0.0038  0.0029  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2269 0.2298 0.3200 0.0100  0.0140  -0.0045 48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3003 0.3036 0.3965 0.0085  0.0176  -0.0075 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.3681 0.3675 0.4691 0.0075  0.0244  -0.0103 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.3712 0.3702 0.4831 0.0097  0.0264  -0.0091 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.3949 0.3919 0.4885 0.0040  0.0282  -0.0140 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1648 0.1684 0.2376 0.0092  0.0054  -0.0018 49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1647 0.1671 0.2320 0.0094  0.0035  -0.0004 49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1596 0.1579 0.2262 0.0085  0.0078  -0.0018 49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1735 0.1697 0.2422 0.0070  0.0124  -0.0046 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1468 0.1438 0.2098 0.0088  0.0064  -0.0002 50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1549 0.1476 0.2178 0.0079  0.0105  -0.0013 50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1679 0.1597 0.2215 0.0052  0.0110  -0.0035 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1711 0.1596 0.2241 0.0037  0.0145  -0.0051 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1702 0.1617 0.2384 0.0105  0.0095  0.0025  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2046 0.1974 0.2863 0.0138  0.0098  0.0057  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1424 0.1371 0.1895 0.0045  0.0075  -0.0033 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1434 0.1381 0.1825 0.0020  0.0077  -0.0048 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1587 0.1534 0.1954 -0.0011 0.0114  -0.0083 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.1856 0.1813 0.2248 -0.0014 0.0124  -0.0092 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1410 0.1389 0.1753 0.0025  0.0035  -0.0034 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1584 0.1566 0.1929 0.0046  0.0001  -0.0006 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1622 0.1580 0.1973 0.0050  0.0009  0.0004  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1605 0.1611 0.1943 0.0054  -0.0031 0.0006  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1753 0.1695 0.2072 -0.0040 0.0133  -0.0102 52  THR   A N   
360  C CA  . THR   A 46  ? 0.1919 0.1874 0.2196 -0.0079 0.0162  -0.0134 52  THR   A CA  
361  C C   . THR   A 46  ? 0.1751 0.1744 0.1954 -0.0096 0.0135  -0.0127 52  THR   A C   
362  O O   . THR   A 46  ? 0.1844 0.1838 0.2030 -0.0088 0.0114  -0.0112 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2461 0.2384 0.2749 -0.0106 0.0215  -0.0169 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3017 0.2925 0.3288 -0.0108 0.0212  -0.0165 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.2705 0.2590 0.3083 -0.0086 0.0249  -0.0174 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1674 0.1701 0.1841 -0.0118 0.0133  -0.0131 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1633 0.1704 0.1744 -0.0131 0.0106  -0.0115 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1675 0.1765 0.1736 -0.0177 0.0127  -0.0140 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.1802 0.1890 0.1850 -0.0211 0.0164  -0.0171 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1609 0.1713 0.1709 -0.0131 0.0091  -0.0097 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1706 0.1792 0.1860 -0.0093 0.0076  -0.0081 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1635 0.1787 0.1696 -0.0137 0.0060  -0.0070 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1864 0.1942 0.2035 -0.0060 0.0043  -0.0060 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1477 0.1591 0.1509 -0.0182 0.0105  -0.0128 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1475 0.1621 0.1458 -0.0228 0.0118  -0.0148 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1624 0.1832 0.1562 -0.0259 0.0108  -0.0139 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1523 0.1758 0.1465 -0.0237 0.0078  -0.0102 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1409 0.1572 0.1382 -0.0219 0.0091  -0.0130 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.1793 0.2024 0.1687 -0.0314 0.0137  -0.0173 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.1882 0.2183 0.1723 -0.0353 0.0127  -0.0162 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2216 0.2568 0.2008 -0.0403 0.0126  -0.0178 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2334 0.2683 0.2092 -0.0454 0.0165  -0.0226 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.1886 0.2172 0.1715 -0.0379 0.0165  -0.0190 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.1826 0.2060 0.1714 -0.0331 0.0169  -0.0178 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.1787 0.2050 0.1688 -0.0294 0.0126  -0.0124 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.1804 0.2019 0.1762 -0.0255 0.0134  -0.0121 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2019 0.2234 0.2008 -0.0215 0.0104  -0.0084 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2097 0.2351 0.2073 -0.0205 0.0068  -0.0045 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2123 0.2299 0.2165 -0.0185 0.0111  -0.0086 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2119 0.2518 0.1910 -0.0388 0.0084  -0.0140 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2137 0.2584 0.1899 -0.0425 0.0077  -0.0151 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2159 0.2673 0.1932 -0.0405 0.0027  -0.0095 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2429 0.2942 0.2234 -0.0360 0.0002  -0.0051 56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2108 0.2484 0.1901 -0.0412 0.0103  -0.0184 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.1947 0.2278 0.1800 -0.0336 0.0073  -0.0143 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2380 0.2949 0.2134 -0.0437 0.0016  -0.0100 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.2624 0.3254 0.2403 -0.0416 -0.0026 -0.0050 57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.2497 0.3098 0.2302 -0.0403 -0.0022 -0.0066 57  ASP   A C   
399  O O   . ASP   A 51  ? 0.2623 0.3288 0.2438 -0.0411 -0.0046 -0.0044 57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3415 0.4163 0.3156 -0.0464 -0.0054 -0.0023 57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.4586 0.5376 0.4277 -0.0535 -0.0037 -0.0071 57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.4710 0.5428 0.4394 -0.0550 0.0005  -0.0130 57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5238 0.6138 0.4900 -0.0579 -0.0065 -0.0048 57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2123 0.2630 0.1946 -0.0381 0.0007  -0.0098 58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.1999 0.2470 0.1847 -0.0364 0.0013  -0.0107 58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2058 0.2555 0.1944 -0.0322 -0.0022 -0.0060 58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2066 0.2563 0.1974 -0.0285 -0.0041 -0.0025 58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2156 0.2524 0.2024 -0.0336 0.0044  -0.0132 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2227 0.2544 0.2074 -0.0383 0.0101  -0.0196 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.1797 0.2312 0.1692 -0.0329 -0.0025 -0.0063 59  GLN   A N   
411  C CA  A GLN   A 53  ? 0.1661 0.2195 0.1598 -0.0293 -0.0048 -0.0027 59  GLN   A CA  
412  C CA  B GLN   A 53  ? 0.1772 0.2303 0.1709 -0.0291 -0.0048 -0.0026 59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.1608 0.2076 0.1556 -0.0276 -0.0030 -0.0046 59  GLN   A C   
414  O O   . GLN   A 53  ? 0.1631 0.2114 0.1609 -0.0257 -0.0040 -0.0027 59  GLN   A O   
415  C CB  A GLN   A 53  ? 0.1697 0.2338 0.1644 -0.0317 -0.0075 0.0001  59  GLN   A CB  
416  C CB  B GLN   A 53  ? 0.2143 0.2782 0.2092 -0.0310 -0.0077 0.0007  59  GLN   A CB  
417  C CG  A GLN   A 53  ? 0.1669 0.2377 0.1630 -0.0307 -0.0105 0.0050  59  GLN   A CG  
418  C CG  B GLN   A 53  ? 0.2669 0.3367 0.2604 -0.0321 -0.0097 0.0036  59  GLN   A CG  
419  C CD  A GLN   A 53  ? 0.1921 0.2738 0.1911 -0.0321 -0.0134 0.0089  59  GLN   A CD  
420  C CD  B GLN   A 53  ? 0.3174 0.3826 0.3133 -0.0273 -0.0101 0.0063  59  GLN   A CD  
421  O OE1 A GLN   A 53  ? 0.2090 0.2992 0.2050 -0.0370 -0.0148 0.0093  59  GLN   A OE1 
422  O OE1 B GLN   A 53  ? 0.3284 0.3926 0.3220 -0.0279 -0.0097 0.0063  59  GLN   A OE1 
423  N NE2 A GLN   A 53  ? 0.1345 0.2166 0.1396 -0.0281 -0.0144 0.0121  59  GLN   A NE2 
424  N NE2 B GLN   A 53  ? 0.3166 0.3785 0.3172 -0.0227 -0.0105 0.0083  59  GLN   A NE2 
425  N N   . THR   A 54  ? 0.1422 0.1818 0.1352 -0.0284 0.0002  -0.0082 60  THR   A N   
426  C CA  . THR   A 54  ? 0.1530 0.1857 0.1470 -0.0267 0.0020  -0.0094 60  THR   A CA  
427  C C   . THR   A 54  ? 0.1433 0.1682 0.1377 -0.0240 0.0035  -0.0100 60  THR   A C   
428  O O   . THR   A 54  ? 0.1629 0.1869 0.1563 -0.0254 0.0047  -0.0115 60  THR   A O   
429  C CB  . THR   A 54  ? 0.2008 0.2330 0.1935 -0.0306 0.0047  -0.0127 60  THR   A CB  
430  O OG1 . THR   A 54  ? 0.2752 0.3053 0.2657 -0.0341 0.0076  -0.0163 60  THR   A OG1 
431  C CG2 . THR   A 54  ? 0.1903 0.2312 0.1830 -0.0336 0.0030  -0.0122 60  THR   A CG2 
432  N N   . GLY   A 55  ? 0.1335 0.1534 0.1294 -0.0204 0.0033  -0.0086 61  GLY   A N   
433  C CA  . GLY   A 55  ? 0.1405 0.1540 0.1375 -0.0176 0.0041  -0.0084 61  GLY   A CA  
434  C C   . GLY   A 55  ? 0.1264 0.1356 0.1241 -0.0146 0.0036  -0.0067 61  GLY   A C   
435  O O   . GLY   A 55  ? 0.1364 0.1462 0.1335 -0.0153 0.0038  -0.0065 61  GLY   A O   
436  N N   . VAL   A 56  ? 0.1271 0.1325 0.1261 -0.0117 0.0030  -0.0054 62  VAL   A N   
437  C CA  . VAL   A 56  ? 0.1145 0.1164 0.1137 -0.0092 0.0023  -0.0035 62  VAL   A CA  
438  C C   . VAL   A 56  ? 0.1188 0.1213 0.1189 -0.0065 -0.0001 -0.0019 62  VAL   A C   
439  O O   . VAL   A 56  ? 0.1344 0.1370 0.1360 -0.0060 -0.0004 -0.0021 62  VAL   A O   
440  C CB  . VAL   A 56  ? 0.1359 0.1321 0.1363 -0.0090 0.0046  -0.0035 62  VAL   A CB  
441  C CG1 . VAL   A 56  ? 0.1668 0.1601 0.1670 -0.0065 0.0034  -0.0008 62  VAL   A CG1 
442  C CG2 . VAL   A 56  ? 0.1499 0.1448 0.1496 -0.0121 0.0078  -0.0057 62  VAL   A CG2 
443  N N   . TYR   A 57  ? 0.1169 0.1197 0.1160 -0.0052 -0.0016 -0.0006 63  TYR   A N   
444  C CA  . TYR   A 57  ? 0.1148 0.1179 0.1147 -0.0031 -0.0036 0.0005  63  TYR   A CA  
445  C C   . TYR   A 57  ? 0.1240 0.1245 0.1226 -0.0020 -0.0044 0.0018  63  TYR   A C   
446  O O   . TYR   A 57  ? 0.1365 0.1356 0.1329 -0.0027 -0.0036 0.0022  63  TYR   A O   
447  C CB  . TYR   A 57  ? 0.1180 0.1249 0.1186 -0.0028 -0.0045 0.0005  63  TYR   A CB  
448  C CG  . TYR   A 57  ? 0.1105 0.1177 0.1098 -0.0029 -0.0043 0.0007  63  TYR   A CG  
449  C CD1 . TYR   A 57  ? 0.1337 0.1421 0.1323 -0.0044 -0.0031 0.0003  63  TYR   A CD1 
450  C CD2 . TYR   A 57  ? 0.1142 0.1208 0.1132 -0.0018 -0.0050 0.0008  63  TYR   A CD2 
451  C CE1 . TYR   A 57  ? 0.1352 0.1438 0.1330 -0.0045 -0.0024 0.0002  63  TYR   A CE1 
452  C CE2 . TYR   A 57  ? 0.1197 0.1263 0.1174 -0.0023 -0.0041 0.0004  63  TYR   A CE2 
453  C CZ  . TYR   A 57  ? 0.1289 0.1365 0.1262 -0.0035 -0.0028 0.0002  63  TYR   A CZ  
454  O OH  . TYR   A 57  ? 0.1469 0.1545 0.1434 -0.0040 -0.0014 -0.0004 63  TYR   A OH  
455  N N   . TYR   A 58  ? 0.1205 0.1209 0.1200 -0.0006 -0.0061 0.0026  64  TYR   A N   
456  C CA  . TYR   A 58  ? 0.1198 0.1190 0.1175 0.0000  -0.0074 0.0040  64  TYR   A CA  
457  C C   . TYR   A 58  ? 0.1223 0.1233 0.1180 -0.0003 -0.0081 0.0032  64  TYR   A C   
458  O O   . TYR   A 58  ? 0.1268 0.1296 0.1243 0.0001  -0.0085 0.0021  64  TYR   A O   
459  C CB  . TYR   A 58  ? 0.1417 0.1408 0.1420 0.0014  -0.0090 0.0053  64  TYR   A CB  
460  C CG  . TYR   A 58  ? 0.1516 0.1507 0.1498 0.0016  -0.0109 0.0074  64  TYR   A CG  
461  C CD1 . TYR   A 58  ? 0.1580 0.1551 0.1542 0.0013  -0.0105 0.0095  64  TYR   A CD1 
462  C CD2 . TYR   A 58  ? 0.1467 0.1481 0.1444 0.0016  -0.0131 0.0072  64  TYR   A CD2 
463  C CE1 . TYR   A 58  ? 0.1637 0.1617 0.1573 0.0011  -0.0126 0.0120  64  TYR   A CE1 
464  C CE2 . TYR   A 58  ? 0.1532 0.1557 0.1481 0.0010  -0.0151 0.0090  64  TYR   A CE2 
465  C CZ  . TYR   A 58  ? 0.1694 0.1703 0.1621 0.0009  -0.0150 0.0117  64  TYR   A CZ  
466  O OH  . TYR   A 58  ? 0.2061 0.2088 0.1954 0.0000  -0.0173 0.0142  64  TYR   A OH  
467  N N   . CYS   A 59  ? 0.1268 0.1270 0.1189 -0.0012 -0.0079 0.0037  65  CYS   A N   
468  C CA  . CYS   A 59  ? 0.1380 0.1393 0.1276 -0.0021 -0.0077 0.0024  65  CYS   A CA  
469  C C   . CYS   A 59  ? 0.1525 0.1537 0.1387 -0.0027 -0.0095 0.0035  65  CYS   A C   
470  O O   . CYS   A 59  ? 0.1513 0.1514 0.1340 -0.0035 -0.0096 0.0053  65  CYS   A O   
471  C CB  . CYS   A 59  ? 0.1371 0.1380 0.1250 -0.0032 -0.0056 0.0018  65  CYS   A CB  
472  S SG  . CYS   A 59  ? 0.1519 0.1534 0.1371 -0.0047 -0.0042 -0.0002 65  CYS   A SG  
473  N N   . SER   A 60  ? 0.1483 0.1512 0.1353 -0.0027 -0.0109 0.0026  66  SER   A N   
474  C CA  . SER   A 60  ? 0.1535 0.1576 0.1372 -0.0038 -0.0131 0.0036  66  SER   A CA  
475  C C   . SER   A 60  ? 0.1555 0.1598 0.1333 -0.0063 -0.0122 0.0027  66  SER   A C   
476  O O   . SER   A 60  ? 0.1738 0.1790 0.1473 -0.0075 -0.0139 0.0048  66  SER   A O   
477  C CB  . SER   A 60  ? 0.1707 0.1770 0.1567 -0.0038 -0.0146 0.0023  66  SER   A CB  
478  O OG  . SER   A 60  ? 0.1922 0.1987 0.1785 -0.0049 -0.0127 -0.0011 66  SER   A OG  
479  N N   . SER   A 61  ? 0.1330 0.1365 0.1106 -0.0071 -0.0094 -0.0002 67  SER   A N   
480  C CA  . SER   A 61  ? 0.1406 0.1439 0.1130 -0.0096 -0.0076 -0.0017 67  SER   A CA  
481  C C   . SER   A 61  ? 0.1456 0.1474 0.1145 -0.0102 -0.0068 0.0004  67  SER   A C   
482  O O   . SER   A 61  ? 0.1486 0.1501 0.1125 -0.0126 -0.0053 -0.0006 67  SER   A O   
483  C CB  . SER   A 61  ? 0.1413 0.1443 0.1165 -0.0100 -0.0042 -0.0054 67  SER   A CB  
484  O OG  . SER   A 61  ? 0.1611 0.1635 0.1407 -0.0083 -0.0025 -0.0050 67  SER   A OG  
485  N N   . ARG   A 62  ? 0.1456 0.1461 0.1169 -0.0083 -0.0076 0.0031  68  ARG   A N   
486  C CA  . ARG   A 62  ? 0.1484 0.1470 0.1171 -0.0087 -0.0069 0.0056  68  ARG   A CA  
487  C C   . ARG   A 62  ? 0.1655 0.1635 0.1350 -0.0073 -0.0093 0.0098  68  ARG   A C   
488  O O   . ARG   A 62  ? 0.1709 0.1666 0.1391 -0.0074 -0.0085 0.0125  68  ARG   A O   
489  C CB  . ARG   A 62  ? 0.1460 0.1432 0.1180 -0.0080 -0.0043 0.0045  68  ARG   A CB  
490  C CG  . ARG   A 62  ? 0.1575 0.1556 0.1297 -0.0092 -0.0016 0.0012  68  ARG   A CG  
491  C CD  . ARG   A 62  ? 0.1521 0.1492 0.1186 -0.0116 0.0002  0.0011  68  ARG   A CD  
492  N NE  . ARG   A 62  ? 0.1750 0.1728 0.1426 -0.0127 0.0033  -0.0022 68  ARG   A NE  
493  C CZ  . ARG   A 62  ? 0.1716 0.1703 0.1381 -0.0140 0.0045  -0.0049 68  ARG   A CZ  
494  N NH1 . ARG   A 62  ? 0.1794 0.1788 0.1431 -0.0147 0.0024  -0.0050 68  ARG   A NH1 
495  N NH2 . ARG   A 62  ? 0.1747 0.1736 0.1435 -0.0147 0.0080  -0.0077 68  ARG   A NH2 
496  N N   . ARG   A 63  ? 0.1779 0.1775 0.1509 -0.0059 -0.0117 0.0105  69  ARG   A N   
497  C CA  . ARG   A 63  ? 0.1905 0.1896 0.1667 -0.0040 -0.0136 0.0144  69  ARG   A CA  
498  C C   . ARG   A 63  ? 0.2082 0.2037 0.1876 -0.0029 -0.0111 0.0152  69  ARG   A C   
499  O O   . ARG   A 63  ? 0.2302 0.2236 0.2102 -0.0022 -0.0110 0.0190  69  ARG   A O   
500  C CB  . ARG   A 63  ? 0.2482 0.2488 0.2201 -0.0051 -0.0159 0.0185  69  ARG   A CB  
501  C CG  . ARG   A 63  ? 0.2968 0.3003 0.2715 -0.0039 -0.0194 0.0216  69  ARG   A CG  
502  C CD  . ARG   A 63  ? 0.2705 0.2764 0.2401 -0.0055 -0.0219 0.0260  69  ARG   A CD  
503  N NE  . ARG   A 63  ? 0.2739 0.2848 0.2404 -0.0077 -0.0247 0.0246  69  ARG   A NE  
504  C CZ  . ARG   A 63  ? 0.2330 0.2465 0.1915 -0.0112 -0.0254 0.0239  69  ARG   A CZ  
505  N NH1 . ARG   A 63  ? 0.2397 0.2508 0.1925 -0.0128 -0.0233 0.0244  69  ARG   A NH1 
506  N NH2 . ARG   A 63  ? 0.2235 0.2416 0.1795 -0.0136 -0.0276 0.0219  69  ARG   A NH2 
507  N N   . LYS   A 64  ? 0.1755 0.1703 0.1570 -0.0029 -0.0089 0.0119  70  LYS   A N   
508  C CA  . LYS   A 64  ? 0.1782 0.1703 0.1620 -0.0028 -0.0062 0.0117  70  LYS   A CA  
509  C C   . LYS   A 64  ? 0.1735 0.1664 0.1615 -0.0023 -0.0053 0.0090  70  LYS   A C   
510  O O   . LYS   A 64  ? 0.1663 0.1616 0.1546 -0.0023 -0.0060 0.0069  70  LYS   A O   
511  C CB  . LYS   A 64  ? 0.2142 0.2055 0.1944 -0.0046 -0.0040 0.0105  70  LYS   A CB  
512  C CG  . LYS   A 64  ? 0.3452 0.3343 0.3216 -0.0054 -0.0037 0.0138  70  LYS   A CG  
513  C CD  . LYS   A 64  ? 0.4499 0.4374 0.4238 -0.0072 -0.0008 0.0126  70  LYS   A CD  
514  C CE  . LYS   A 64  ? 0.5319 0.5175 0.5011 -0.0082 -0.0006 0.0161  70  LYS   A CE  
515  N NZ  . LYS   A 64  ? 0.5921 0.5804 0.5565 -0.0089 -0.0032 0.0173  70  LYS   A NZ  
516  N N   . HIS   A 65  ? 0.1597 0.1503 0.1506 -0.0022 -0.0034 0.0089  71  HIS   A N   
517  C CA  . HIS   A 65  ? 0.1532 0.1449 0.1471 -0.0026 -0.0021 0.0062  71  HIS   A CA  
518  C C   . HIS   A 65  ? 0.1736 0.1655 0.1660 -0.0046 0.0002  0.0044  71  HIS   A C   
519  O O   . HIS   A 65  ? 0.2211 0.2102 0.2125 -0.0055 0.0020  0.0052  71  HIS   A O   
520  C CB  . HIS   A 65  ? 0.1501 0.1392 0.1480 -0.0019 -0.0008 0.0067  71  HIS   A CB  
521  C CG  . HIS   A 65  ? 0.1599 0.1495 0.1606 0.0001  -0.0028 0.0084  71  HIS   A CG  
522  N ND1 . HIS   A 65  ? 0.2012 0.1926 0.2045 0.0006  -0.0033 0.0068  71  HIS   A ND1 
523  C CD2 . HIS   A 65  ? 0.1565 0.1454 0.1578 0.0015  -0.0045 0.0118  71  HIS   A CD2 
524  C CE1 . HIS   A 65  ? 0.1652 0.1567 0.1713 0.0024  -0.0050 0.0090  71  HIS   A CE1 
525  N NE2 . HIS   A 65  ? 0.1922 0.1827 0.1972 0.0030  -0.0061 0.0122  71  HIS   A NE2 
526  N N   . TYR   A 66  ? 0.1434 0.1389 0.1362 -0.0054 0.0000  0.0023  72  TYR   A N   
527  C CA  . TYR   A 66  ? 0.1529 0.1500 0.1452 -0.0074 0.0017  0.0008  72  TYR   A CA  
528  C C   . TYR   A 66  ? 0.1405 0.1402 0.1348 -0.0089 0.0024  -0.0011 72  TYR   A C   
529  O O   . TYR   A 66  ? 0.1391 0.1414 0.1349 -0.0082 0.0010  -0.0013 72  TYR   A O   
530  C CB  . TYR   A 66  ? 0.1521 0.1525 0.1437 -0.0073 0.0009  0.0005  72  TYR   A CB  
531  C CG  . TYR   A 66  ? 0.1513 0.1498 0.1397 -0.0070 0.0008  0.0015  72  TYR   A CG  
532  C CD1 . TYR   A 66  ? 0.1722 0.1687 0.1583 -0.0083 0.0026  0.0018  72  TYR   A CD1 
533  C CD2 . TYR   A 66  ? 0.1546 0.1535 0.1422 -0.0058 -0.0009 0.0019  72  TYR   A CD2 
534  C CE1 . TYR   A 66  ? 0.1692 0.1642 0.1514 -0.0085 0.0026  0.0028  72  TYR   A CE1 
535  C CE2 . TYR   A 66  ? 0.1820 0.1797 0.1658 -0.0063 -0.0009 0.0024  72  TYR   A CE2 
536  C CZ  . TYR   A 66  ? 0.1804 0.1763 0.1613 -0.0077 0.0008  0.0030  72  TYR   A CZ  
537  O OH  . TYR   A 66  ? 0.2151 0.2101 0.1914 -0.0086 0.0010  0.0035  72  TYR   A OH  
538  N N   . PRO   A 67  ? 0.1458 0.1455 0.1401 -0.0113 0.0046  -0.0025 73  PRO   A N   
539  C CA  . PRO   A 67  ? 0.1529 0.1566 0.1483 -0.0136 0.0051  -0.0046 73  PRO   A CA  
540  C C   . PRO   A 67  ? 0.1693 0.1793 0.1655 -0.0139 0.0034  -0.0043 73  PRO   A C   
541  O O   . PRO   A 67  ? 0.2163 0.2271 0.2124 -0.0136 0.0035  -0.0037 73  PRO   A O   
542  C CB  . PRO   A 67  ? 0.1764 0.1782 0.1714 -0.0167 0.0082  -0.0065 73  PRO   A CB  
543  C CG  . PRO   A 67  ? 0.1966 0.1947 0.1903 -0.0159 0.0091  -0.0050 73  PRO   A CG  
544  C CD  . PRO   A 67  ? 0.1597 0.1559 0.1526 -0.0125 0.0069  -0.0024 73  PRO   A CD  
545  N N   . VAL   A 68  ? 0.1398 0.1544 0.1372 -0.0145 0.0022  -0.0045 74  VAL   A N   
546  C CA  . VAL   A 68  ? 0.1623 0.1833 0.1616 -0.0144 0.0005  -0.0032 74  VAL   A CA  
547  C C   . VAL   A 68  ? 0.1549 0.1820 0.1547 -0.0171 -0.0001 -0.0037 74  VAL   A C   
548  O O   . VAL   A 68  ? 0.1486 0.1749 0.1470 -0.0184 0.0003  -0.0049 74  VAL   A O   
549  C CB  . VAL   A 68  ? 0.2114 0.2325 0.2124 -0.0112 -0.0013 -0.0013 74  VAL   A CB  
550  C CG1 . VAL   A 68  ? 0.2383 0.2556 0.2387 -0.0093 -0.0008 -0.0009 74  VAL   A CG1 
551  C CG2 . VAL   A 68  ? 0.2121 0.2312 0.2127 -0.0102 -0.0019 -0.0013 74  VAL   A CG2 
552  N N   . SER   A 69  ? 0.1424 0.1764 0.1445 -0.0180 -0.0013 -0.0025 75  SER   A N   
553  C CA  A SER   A 69  ? 0.1424 0.1841 0.1453 -0.0202 -0.0029 -0.0016 75  SER   A CA  
554  C CA  B SER   A 69  ? 0.1473 0.1893 0.1504 -0.0202 -0.0029 -0.0015 75  SER   A CA  
555  C C   . SER   A 69  ? 0.1357 0.1800 0.1420 -0.0169 -0.0050 0.0020  75  SER   A C   
556  O O   . SER   A 69  ? 0.1487 0.1918 0.1580 -0.0141 -0.0049 0.0034  75  SER   A O   
557  C CB  A SER   A 69  ? 0.1588 0.2074 0.1634 -0.0231 -0.0031 -0.0016 75  SER   A CB  
558  C CB  B SER   A 69  ? 0.1762 0.2246 0.1813 -0.0226 -0.0031 -0.0013 75  SER   A CB  
559  O OG  A SER   A 69  ? 0.1866 0.2321 0.1882 -0.0264 -0.0006 -0.0052 75  SER   A OG  
560  O OG  B SER   A 69  ? 0.2254 0.2829 0.2317 -0.0248 -0.0053 0.0005  75  SER   A OG  
561  N N   . PHE   A 70  ? 0.1304 0.1777 0.1363 -0.0173 -0.0063 0.0032  76  PHE   A N   
562  C CA  . PHE   A 70  ? 0.1394 0.1884 0.1489 -0.0142 -0.0079 0.0067  76  PHE   A CA  
563  C C   . PHE   A 70  ? 0.1397 0.1973 0.1504 -0.0158 -0.0100 0.0098  76  PHE   A C   
564  O O   . PHE   A 70  ? 0.1514 0.2130 0.1586 -0.0198 -0.0103 0.0086  76  PHE   A O   
565  C CB  . PHE   A 70  ? 0.1505 0.1922 0.1584 -0.0119 -0.0072 0.0057  76  PHE   A CB  
566  C CG  . PHE   A 70  ? 0.1344 0.1738 0.1382 -0.0140 -0.0064 0.0034  76  PHE   A CG  
567  C CD1 . PHE   A 70  ? 0.1371 0.1711 0.1382 -0.0152 -0.0044 0.0001  76  PHE   A CD1 
568  C CD2 . PHE   A 70  ? 0.1396 0.1821 0.1428 -0.0149 -0.0073 0.0047  76  PHE   A CD2 
569  C CE1 . PHE   A 70  ? 0.1432 0.1748 0.1418 -0.0170 -0.0030 -0.0021 76  PHE   A CE1 
570  C CE2 . PHE   A 70  ? 0.1535 0.1937 0.1533 -0.0170 -0.0059 0.0021  76  PHE   A CE2 
571  C CZ  . PHE   A 70  ? 0.1455 0.1802 0.1434 -0.0181 -0.0037 -0.0014 76  PHE   A CZ  
572  N N   . SER   A 71  ? 0.1413 0.2021 0.1572 -0.0130 -0.0112 0.0140  77  SER   A N   
573  C CA  . SER   A 71  ? 0.1420 0.2115 0.1600 -0.0141 -0.0135 0.0183  77  SER   A CA  
574  C C   . SER   A 71  ? 0.1432 0.2121 0.1575 -0.0151 -0.0139 0.0186  77  SER   A C   
575  O O   . SER   A 71  ? 0.1487 0.2098 0.1605 -0.0139 -0.0124 0.0158  77  SER   A O   
576  C CB  . SER   A 71  ? 0.1593 0.2322 0.1856 -0.0105 -0.0141 0.0231  77  SER   A CB  
577  O OG  . SER   A 71  ? 0.1995 0.2654 0.2279 -0.0067 -0.0128 0.0233  77  SER   A OG  
578  N N   . LYS   A 72  ? 0.1309 0.2080 0.1449 -0.0172 -0.0160 0.0221  78  LYS   A N   
579  C CA  . LYS   A 72  ? 0.1360 0.2129 0.1465 -0.0183 -0.0162 0.0228  78  LYS   A CA  
580  C C   . LYS   A 72  ? 0.1516 0.2248 0.1671 -0.0135 -0.0160 0.0263  78  LYS   A C   
581  O O   . LYS   A 72  ? 0.1606 0.2350 0.1829 -0.0103 -0.0163 0.0296  78  LYS   A O   
582  C CB  . LYS   A 72  ? 0.1528 0.2406 0.1611 -0.0225 -0.0187 0.0260  78  LYS   A CB  
583  C CG  . LYS   A 72  ? 0.1983 0.2889 0.2005 -0.0281 -0.0183 0.0214  78  LYS   A CG  
584  C CD  . LYS   A 72  ? 0.2972 0.3991 0.2957 -0.0333 -0.0207 0.0240  78  LYS   A CD  
585  C CE  . LYS   A 72  ? 0.3866 0.4913 0.3789 -0.0397 -0.0198 0.0185  78  LYS   A CE  
586  N NZ  . LYS   A 72  ? 0.4413 0.5550 0.4275 -0.0457 -0.0213 0.0195  78  LYS   A NZ  
587  N N   . PRO   A 73  ? 0.1463 0.2150 0.1592 -0.0132 -0.0150 0.0253  79  PRO   A N   
588  C CA  . PRO   A 73  ? 0.1482 0.2132 0.1660 -0.0091 -0.0144 0.0281  79  PRO   A CA  
589  C C   . PRO   A 73  ? 0.1609 0.2331 0.1847 -0.0076 -0.0161 0.0352  79  PRO   A C   
590  O O   . PRO   A 73  ? 0.1787 0.2591 0.2006 -0.0104 -0.0182 0.0388  79  PRO   A O   
591  C CB  . PRO   A 73  ? 0.1817 0.2431 0.1950 -0.0103 -0.0134 0.0262  79  PRO   A CB  
592  C CG  . PRO   A 73  ? 0.2254 0.2864 0.2320 -0.0144 -0.0127 0.0213  79  PRO   A CG  
593  C CD  . PRO   A 73  ? 0.1809 0.2477 0.1868 -0.0168 -0.0140 0.0213  79  PRO   A CD  
594  N N   . SER   A 74  ? 0.1527 0.2221 0.1840 -0.0035 -0.0151 0.0371  80  SER   A N   
595  C CA  . SER   A 74  ? 0.1598 0.2358 0.1991 -0.0014 -0.0162 0.0442  80  SER   A CA  
596  C C   . SER   A 74  ? 0.1449 0.2147 0.1917 0.0031  -0.0137 0.0457  80  SER   A C   
597  O O   . SER   A 74  ? 0.1411 0.2024 0.1866 0.0043  -0.0114 0.0409  80  SER   A O   
598  C CB  . SER   A 74  ? 0.2399 0.3221 0.2828 -0.0018 -0.0174 0.0456  80  SER   A CB  
599  O OG  . SER   A 74  ? 0.3078 0.3906 0.3449 -0.0051 -0.0179 0.0407  80  SER   A OG  
600  N N   . LEU   A 75  ? 0.1471 0.2218 0.2024 0.0055  -0.0139 0.0526  81  LEU   A N   
601  C CA  . LEU   A 75  ? 0.1532 0.2229 0.2175 0.0096  -0.0110 0.0548  81  LEU   A CA  
602  C C   . LEU   A 75  ? 0.1561 0.2254 0.2278 0.0118  -0.0093 0.0543  81  LEU   A C   
603  O O   . LEU   A 75  ? 0.1780 0.2553 0.2549 0.0120  -0.0109 0.0589  81  LEU   A O   
604  C CB  . LEU   A 75  ? 0.1641 0.2397 0.2345 0.0110  -0.0119 0.0635  81  LEU   A CB  
605  C CG  . LEU   A 75  ? 0.1916 0.2613 0.2715 0.0150  -0.0082 0.0659  81  LEU   A CG  
606  C CD1 . LEU   A 75  ? 0.2012 0.2618 0.2764 0.0148  -0.0060 0.0606  81  LEU   A CD1 
607  C CD2 . LEU   A 75  ? 0.2252 0.3018 0.3123 0.0166  -0.0093 0.0758  81  LEU   A CD2 
608  N N   . ILE   A 76  ? 0.1372 0.1981 0.2086 0.0129  -0.0062 0.0482  82  ILE   A N   
609  C CA  . ILE   A 76  ? 0.1395 0.1987 0.2160 0.0142  -0.0040 0.0461  82  ILE   A CA  
610  C C   . ILE   A 76  ? 0.1644 0.2163 0.2479 0.0171  0.0006  0.0447  82  ILE   A C   
611  O O   . ILE   A 76  ? 0.1598 0.2051 0.2400 0.0170  0.0020  0.0413  82  ILE   A O   
612  C CB  . ILE   A 76  ? 0.1612 0.2170 0.2282 0.0116  -0.0045 0.0391  82  ILE   A CB  
613  C CG1 . ILE   A 76  ? 0.1958 0.2586 0.2566 0.0084  -0.0082 0.0399  82  ILE   A CG1 
614  C CG2 . ILE   A 76  ? 0.1780 0.2307 0.2485 0.0125  -0.0017 0.0357  82  ILE   A CG2 
615  C CD1 . ILE   A 76  ? 0.2043 0.2641 0.2568 0.0058  -0.0086 0.0339  82  ILE   A CD1 
616  N N   . PHE   A 77  ? 0.1586 0.2116 0.2523 0.0194  0.0033  0.0468  83  PHE   A N   
617  C CA  . PHE   A 77  ? 0.1659 0.2115 0.2667 0.0216  0.0085  0.0446  83  PHE   A CA  
618  C C   . PHE   A 77  ? 0.1890 0.2282 0.2828 0.0197  0.0103  0.0363  83  PHE   A C   
619  O O   . PHE   A 77  ? 0.2194 0.2605 0.3109 0.0186  0.0097  0.0342  83  PHE   A O   
620  C CB  . PHE   A 77  ? 0.1695 0.2184 0.2843 0.0246  0.0115  0.0493  83  PHE   A CB  
621  C CG  . PHE   A 77  ? 0.1995 0.2412 0.3235 0.0270  0.0175  0.0484  83  PHE   A CG  
622  C CD1 . PHE   A 77  ? 0.2124 0.2519 0.3400 0.0284  0.0184  0.0518  83  PHE   A CD1 
623  C CD2 . PHE   A 77  ? 0.2261 0.2631 0.3552 0.0274  0.0226  0.0439  83  PHE   A CD2 
624  C CE1 . PHE   A 77  ? 0.2342 0.2666 0.3705 0.0302  0.0245  0.0505  83  PHE   A CE1 
625  C CE2 . PHE   A 77  ? 0.2380 0.2681 0.3754 0.0290  0.0287  0.0423  83  PHE   A CE2 
626  C CZ  . PHE   A 77  ? 0.2372 0.2650 0.3785 0.0305  0.0297  0.0456  83  PHE   A CZ  
627  N N   . VAL   A 78  ? 0.1590 0.1908 0.2494 0.0192  0.0124  0.0318  84  VAL   A N   
628  C CA  . VAL   A 78  ? 0.1510 0.1769 0.2340 0.0172  0.0137  0.0243  84  VAL   A CA  
629  C C   . VAL   A 78  ? 0.1479 0.1680 0.2377 0.0180  0.0195  0.0212  84  VAL   A C   
630  O O   . VAL   A 78  ? 0.1601 0.1775 0.2560 0.0194  0.0221  0.0227  84  VAL   A O   
631  C CB  . VAL   A 78  ? 0.1541 0.1772 0.2277 0.0154  0.0112  0.0216  84  VAL   A CB  
632  C CG1 . VAL   A 78  ? 0.1653 0.1828 0.2323 0.0133  0.0125  0.0146  84  VAL   A CG1 
633  C CG2 . VAL   A 78  ? 0.1617 0.1901 0.2286 0.0141  0.0063  0.0237  84  VAL   A CG2 
634  N N   . GLU   A 79  ? 0.1463 0.1643 0.2350 0.0168  0.0220  0.0168  85  GLU   A N   
635  C CA  . GLU   A 79  ? 0.1598 0.1723 0.2544 0.0169  0.0281  0.0130  85  GLU   A CA  
636  C C   . GLU   A 79  ? 0.1671 0.1735 0.2570 0.0150  0.0297  0.0080  85  GLU   A C   
637  O O   . GLU   A 79  ? 0.1650 0.1711 0.2453 0.0133  0.0258  0.0062  85  GLU   A O   
638  C CB  . GLU   A 79  ? 0.1897 0.2015 0.2813 0.0151  0.0300  0.0086  85  GLU   A CB  
639  C CG  . GLU   A 79  ? 0.2517 0.2693 0.3500 0.0168  0.0298  0.0128  85  GLU   A CG  
640  C CD  . GLU   A 79  ? 0.3370 0.3560 0.4506 0.0202  0.0337  0.0176  85  GLU   A CD  
641  O OE1 . GLU   A 79  ? 0.4104 0.4239 0.5302 0.0203  0.0398  0.0144  85  GLU   A OE1 
642  O OE2 . GLU   A 79  ? 0.3617 0.3871 0.4811 0.0224  0.0307  0.0247  85  GLU   A OE2 
643  N N   . ALA   A 80  ? 0.1719 0.1735 0.2690 0.0152  0.0357  0.0053  86  ALA   A N   
644  C CA  . ALA   A 80  ? 0.1714 0.1675 0.2647 0.0128  0.0378  -0.0001 86  ALA   A CA  
645  C C   . ALA   A 80  ? 0.1791 0.1740 0.2600 0.0090  0.0357  -0.0061 86  ALA   A C   
646  O O   . ALA   A 80  ? 0.1911 0.1870 0.2682 0.0079  0.0358  -0.0080 86  ALA   A O   
647  C CB  . ALA   A 80  ? 0.1819 0.1728 0.2852 0.0128  0.0457  -0.0030 86  ALA   A CB  
648  N N   . SER   A 81  ? 0.1806 0.1738 0.2551 0.0072  0.0336  -0.0086 87  SER   A N   
649  C CA  . SER   A 81  ? 0.1916 0.1841 0.2548 0.0036  0.0313  -0.0137 87  SER   A CA  
650  C C   . SER   A 81  ? 0.2051 0.1938 0.2676 0.0009  0.0340  -0.0187 87  SER   A C   
651  O O   . SER   A 81  ? 0.2271 0.2130 0.2980 0.0018  0.0382  -0.0186 87  SER   A O   
652  C CB  . SER   A 81  ? 0.1941 0.1902 0.2496 0.0039  0.0246  -0.0109 87  SER   A CB  
653  O OG  . SER   A 81  ? 0.1860 0.1821 0.2431 0.0049  0.0229  -0.0089 87  SER   A OG  
654  N N   . GLU   A 82  ? 0.2085 0.1975 0.2613 -0.0025 0.0314  -0.0227 88  GLU   A N   
655  C CA  . GLU   A 82  ? 0.2231 0.2097 0.2745 -0.0056 0.0330  -0.0275 88  GLU   A CA  
656  C C   . GLU   A 82  ? 0.2144 0.2013 0.2697 -0.0037 0.0311  -0.0244 88  GLU   A C   
657  O O   . GLU   A 82  ? 0.2270 0.2115 0.2850 -0.0054 0.0337  -0.0274 88  GLU   A O   
658  C CB  . GLU   A 82  ? 0.2807 0.2695 0.3206 -0.0093 0.0289  -0.0307 88  GLU   A CB  
659  C CG  . GLU   A 82  ? 0.3676 0.3560 0.4047 -0.0131 0.0292  -0.0354 88  GLU   A CG  
660  C CD  . GLU   A 82  ? 0.4532 0.4448 0.4795 -0.0166 0.0246  -0.0375 88  GLU   A CD  
661  O OE1 . GLU   A 82  ? 0.4887 0.4816 0.5128 -0.0193 0.0231  -0.0400 88  GLU   A OE1 
662  O OE2 . GLU   A 82  ? 0.4448 0.4381 0.4655 -0.0167 0.0225  -0.0363 88  GLU   A OE2 
663  N N   . TYR   A 83  ? 0.1944 0.1843 0.2497 -0.0005 0.0268  -0.0186 89  TYR   A N   
664  C CA  . TYR   A 83  ? 0.1832 0.1737 0.2400 0.0009  0.0244  -0.0157 89  TYR   A CA  
665  C C   . TYR   A 83  ? 0.1638 0.1541 0.2295 0.0043  0.0261  -0.0104 89  TYR   A C   
666  O O   . TYR   A 83  ? 0.1724 0.1622 0.2405 0.0048  0.0258  -0.0090 89  TYR   A O   
667  C CB  . TYR   A 83  ? 0.1923 0.1866 0.2415 0.0011  0.0181  -0.0136 89  TYR   A CB  
668  C CG  . TYR   A 83  ? 0.2265 0.2216 0.2675 -0.0021 0.0159  -0.0177 89  TYR   A CG  
669  C CD1 . TYR   A 83  ? 0.2579 0.2528 0.2968 -0.0046 0.0152  -0.0210 89  TYR   A CD1 
670  C CD2 . TYR   A 83  ? 0.2686 0.2649 0.3042 -0.0028 0.0146  -0.0182 89  TYR   A CD2 
671  C CE1 . TYR   A 83  ? 0.2987 0.2955 0.3302 -0.0076 0.0125  -0.0239 89  TYR   A CE1 
672  C CE2 . TYR   A 83  ? 0.2965 0.2940 0.3244 -0.0058 0.0123  -0.0211 89  TYR   A CE2 
673  C CZ  . TYR   A 83  ? 0.3173 0.3152 0.3433 -0.0082 0.0113  -0.0239 89  TYR   A CZ  
674  O OH  . TYR   A 83  ? 0.3738 0.3740 0.3924 -0.0111 0.0084  -0.0259 89  TYR   A OH  
675  N N   . TYR   A 84  ? 0.1741 0.1653 0.2449 0.0066  0.0278  -0.0071 90  TYR   A N   
676  C CA  . TYR   A 84  ? 0.1623 0.1543 0.2419 0.0099  0.0291  -0.0010 90  TYR   A CA  
677  C C   . TYR   A 84  ? 0.1631 0.1540 0.2513 0.0115  0.0339  0.0000  90  TYR   A C   
678  O O   . TYR   A 84  ? 0.1554 0.1470 0.2407 0.0106  0.0341  -0.0023 90  TYR   A O   
679  C CB  . TYR   A 84  ? 0.1648 0.1622 0.2411 0.0117  0.0237  0.0046  90  TYR   A CB  
680  C CG  . TYR   A 84  ? 0.1439 0.1429 0.2126 0.0106  0.0191  0.0046  90  TYR   A CG  
681  C CD1 . TYR   A 84  ? 0.1553 0.1536 0.2262 0.0111  0.0191  0.0066  90  TYR   A CD1 
682  C CD2 . TYR   A 84  ? 0.1346 0.1355 0.1944 0.0091  0.0151  0.0025  90  TYR   A CD2 
683  C CE1 . TYR   A 84  ? 0.1484 0.1482 0.2133 0.0101  0.0154  0.0064  90  TYR   A CE1 
684  C CE2 . TYR   A 84  ? 0.1536 0.1557 0.2079 0.0083  0.0115  0.0026  90  TYR   A CE2 
685  C CZ  . TYR   A 84  ? 0.1460 0.1476 0.2028 0.0088  0.0117  0.0043  90  TYR   A CZ  
686  O OH  . TYR   A 84  ? 0.1535 0.1562 0.2055 0.0080  0.0087  0.0039  90  TYR   A OH  
687  N N   . PRO   A 85  ? 0.1754 0.1648 0.2746 0.0140  0.0377  0.0039  91  PRO   A N   
688  C CA  . PRO   A 85  ? 0.1813 0.1709 0.2904 0.0163  0.0417  0.0066  91  PRO   A CA  
689  C C   . PRO   A 85  ? 0.1848 0.1814 0.2929 0.0185  0.0368  0.0128  91  PRO   A C   
690  O O   . PRO   A 85  ? 0.1844 0.1849 0.2849 0.0181  0.0310  0.0151  91  PRO   A O   
691  C CB  . PRO   A 85  ? 0.2006 0.1873 0.3219 0.0187  0.0464  0.0105  91  PRO   A CB  
692  C CG  . PRO   A 85  ? 0.2048 0.1931 0.3217 0.0188  0.0422  0.0135  91  PRO   A CG  
693  C CD  . PRO   A 85  ? 0.1765 0.1648 0.2799 0.0152  0.0380  0.0074  91  PRO   A CD  
694  N N   . ALA   A 86  ? 0.1903 0.1888 0.3068 0.0205  0.0393  0.0156  92  ALA   A N   
695  C CA  . ALA   A 86  ? 0.1772 0.1831 0.2938 0.0222  0.0348  0.0216  92  ALA   A CA  
696  C C   . ALA   A 86  ? 0.1767 0.1865 0.2967 0.0244  0.0318  0.0294  92  ALA   A C   
697  O O   . ALA   A 86  ? 0.1864 0.1937 0.3155 0.0263  0.0354  0.0324  92  ALA   A O   
698  C CB  . ALA   A 86  ? 0.1775 0.1850 0.3047 0.0242  0.0387  0.0235  92  ALA   A CB  
699  N N   . ARG   A 87  ? 0.1660 0.1813 0.2777 0.0236  0.0256  0.0320  93  ARG   A N   
700  C CA  . ARG   A 87  ? 0.1553 0.1746 0.2678 0.0247  0.0226  0.0387  93  ARG   A CA  
701  C C   . ARG   A 87  ? 0.1559 0.1828 0.2608 0.0236  0.0165  0.0414  93  ARG   A C   
702  O O   . ARG   A 87  ? 0.1749 0.2024 0.2729 0.0217  0.0148  0.0371  93  ARG   A O   
703  C CB  . ARG   A 87  ? 0.1819 0.1963 0.2888 0.0232  0.0226  0.0355  93  ARG   A CB  
704  C CG  . ARG   A 87  ? 0.2391 0.2548 0.3326 0.0204  0.0177  0.0318  93  ARG   A CG  
705  C CD  . ARG   A 87  ? 0.2524 0.2621 0.3408 0.0183  0.0191  0.0248  93  ARG   A CD  
706  N NE  . ARG   A 87  ? 0.1935 0.2044 0.2718 0.0163  0.0148  0.0230  93  ARG   A NE  
707  C CZ  . ARG   A 87  ? 0.2186 0.2303 0.2886 0.0145  0.0120  0.0194  93  ARG   A CZ  
708  N NH1 . ARG   A 87  ? 0.1932 0.2050 0.2627 0.0143  0.0127  0.0172  93  ARG   A NH1 
709  N NH2 . ARG   A 87  ? 0.1851 0.1972 0.2477 0.0130  0.0090  0.0178  93  ARG   A NH2 
710  N N   . TYR   A 88  ? 0.1623 0.1945 0.2672 0.0240  0.0133  0.0479  94  TYR   A N   
711  C CA  . TYR   A 88  ? 0.1704 0.2095 0.2670 0.0220  0.0078  0.0497  94  TYR   A CA  
712  C C   . TYR   A 88  ? 0.1676 0.2037 0.2529 0.0193  0.0058  0.0449  94  TYR   A C   
713  O O   . TYR   A 88  ? 0.1787 0.2115 0.2637 0.0194  0.0068  0.0451  94  TYR   A O   
714  C CB  . TYR   A 88  ? 0.1803 0.2274 0.2815 0.0231  0.0053  0.0588  94  TYR   A CB  
715  C CG  . TYR   A 88  ? 0.1869 0.2402 0.2981 0.0252  0.0055  0.0642  94  TYR   A CG  
716  C CD1 . TYR   A 88  ? 0.1965 0.2565 0.3043 0.0236  0.0022  0.0642  94  TYR   A CD1 
717  C CD2 . TYR   A 88  ? 0.2013 0.2533 0.3260 0.0288  0.0095  0.0689  94  TYR   A CD2 
718  C CE1 . TYR   A 88  ? 0.2080 0.2738 0.3255 0.0255  0.0026  0.0686  94  TYR   A CE1 
719  C CE2 . TYR   A 88  ? 0.2042 0.2621 0.3395 0.0310  0.0100  0.0740  94  TYR   A CE2 
720  C CZ  . TYR   A 88  ? 0.2123 0.2774 0.3438 0.0293  0.0062  0.0739  94  TYR   A CZ  
721  O OH  . TYR   A 88  ? 0.2405 0.3121 0.3828 0.0313  0.0065  0.0787  94  TYR   A OH  
722  N N   . GLN   A 89  ? 0.1455 0.1824 0.2221 0.0170  0.0034  0.0405  95  GLN   A N   
723  C CA  . GLN   A 89  ? 0.1475 0.1820 0.2140 0.0146  0.0015  0.0361  95  GLN   A CA  
724  C C   . GLN   A 89  ? 0.1452 0.1865 0.2063 0.0126  -0.0024 0.0391  95  GLN   A C   
725  O O   . GLN   A 89  ? 0.1451 0.1921 0.2064 0.0120  -0.0041 0.0410  95  GLN   A O   
726  C CB  . GLN   A 89  ? 0.1518 0.1819 0.2128 0.0133  0.0018  0.0292  95  GLN   A CB  
727  C CG  . GLN   A 89  ? 0.1518 0.1795 0.2041 0.0112  0.0001  0.0252  95  GLN   A CG  
728  C CD  . GLN   A 89  ? 0.1597 0.1824 0.2080 0.0104  0.0008  0.0193  95  GLN   A CD  
729  O OE1 . GLN   A 89  ? 0.1857 0.2055 0.2373 0.0111  0.0033  0.0173  95  GLN   A OE1 
730  N NE2 . GLN   A 89  ? 0.1410 0.1630 0.1822 0.0087  -0.0011 0.0165  95  GLN   A NE2 
731  N N   . SER   A 90  ? 0.1297 0.1709 0.1861 0.0112  -0.0034 0.0394  96  SER   A N   
732  C CA  . SER   A 90  ? 0.1339 0.1813 0.1843 0.0085  -0.0065 0.0414  96  SER   A CA  
733  C C   . SER   A 90  ? 0.1330 0.1783 0.1745 0.0058  -0.0075 0.0354  96  SER   A C   
734  O O   . SER   A 90  ? 0.1329 0.1718 0.1727 0.0062  -0.0061 0.0304  96  SER   A O   
735  C CB  . SER   A 90  ? 0.1549 0.2039 0.2056 0.0083  -0.0066 0.0457  96  SER   A CB  
736  O OG  . SER   A 90  ? 0.1991 0.2413 0.2473 0.0081  -0.0048 0.0415  96  SER   A OG  
737  N N   . HIS   A 91  ? 0.1291 0.1803 0.1652 0.0028  -0.0098 0.0363  97  HIS   A N   
738  C CA  . HIS   A 91  ? 0.1293 0.1790 0.1576 -0.0001 -0.0103 0.0311  97  HIS   A CA  
739  C C   . HIS   A 91  ? 0.1250 0.1703 0.1529 0.0007  -0.0095 0.0265  97  HIS   A C   
740  O O   . HIS   A 91  ? 0.1380 0.1786 0.1615 -0.0003 -0.0090 0.0219  97  HIS   A O   
741  C CB  . HIS   A 91  ? 0.1557 0.2008 0.1806 -0.0008 -0.0091 0.0286  97  HIS   A CB  
742  C CG  . HIS   A 91  ? 0.1762 0.2254 0.2003 -0.0021 -0.0096 0.0328  97  HIS   A CG  
743  N ND1 . HIS   A 91  ? 0.2041 0.2575 0.2217 -0.0060 -0.0104 0.0323  97  HIS   A ND1 
744  C CD2 . HIS   A 91  ? 0.1863 0.2360 0.2152 -0.0003 -0.0090 0.0374  97  HIS   A CD2 
745  C CE1 . HIS   A 91  ? 0.2093 0.2659 0.2273 -0.0066 -0.0106 0.0368  97  HIS   A CE1 
746  N NE2 . HIS   A 91  ? 0.2079 0.2624 0.2327 -0.0030 -0.0098 0.0403  97  HIS   A NE2 
747  N N   . LEU   A 92  ? 0.1147 0.1618 0.1471 0.0021  -0.0095 0.0280  98  LEU   A N   
748  C CA  . LEU   A 92  ? 0.1186 0.1619 0.1508 0.0027  -0.0085 0.0243  98  LEU   A CA  
749  C C   . LEU   A 92  ? 0.1171 0.1650 0.1466 0.0004  -0.0098 0.0238  98  LEU   A C   
750  O O   . LEU   A 92  ? 0.1264 0.1815 0.1581 -0.0004 -0.0113 0.0277  98  LEU   A O   
751  C CB  . LEU   A 92  ? 0.1321 0.1737 0.1718 0.0057  -0.0067 0.0257  98  LEU   A CB  
752  C CG  . LEU   A 92  ? 0.1495 0.1868 0.1888 0.0062  -0.0052 0.0217  98  LEU   A CG  
753  C CD1 . LEU   A 92  ? 0.1511 0.1819 0.1856 0.0058  -0.0046 0.0171  98  LEU   A CD1 
754  C CD2 . LEU   A 92  ? 0.1806 0.2172 0.2281 0.0087  -0.0027 0.0232  98  LEU   A CD2 
755  N N   . MET   A 93  ? 0.1261 0.1701 0.1513 -0.0006 -0.0093 0.0193  99  MET   A N   
756  C CA  . MET   A 93  ? 0.1205 0.1678 0.1431 -0.0030 -0.0099 0.0181  99  MET   A CA  
757  C C   . MET   A 93  ? 0.1353 0.1792 0.1595 -0.0017 -0.0085 0.0161  99  MET   A C   
758  O O   . MET   A 93  ? 0.1463 0.1838 0.1689 -0.0006 -0.0074 0.0133  99  MET   A O   
759  C CB  . MET   A 93  ? 0.1348 0.1796 0.1508 -0.0057 -0.0098 0.0144  99  MET   A CB  
760  C CG  . MET   A 93  ? 0.1576 0.2055 0.1712 -0.0076 -0.0105 0.0157  99  MET   A CG  
761  S SD  . MET   A 93  ? 0.1860 0.2300 0.1932 -0.0106 -0.0092 0.0110  99  MET   A SD  
762  C CE  . MET   A 93  ? 0.2304 0.2655 0.2389 -0.0072 -0.0080 0.0088  99  MET   A CE  
763  N N   . LEU   A 94  ? 0.1224 0.1707 0.1495 -0.0021 -0.0087 0.0173  100 LEU   A N   
764  C CA  . LEU   A 94  ? 0.1329 0.1781 0.1613 -0.0013 -0.0069 0.0152  100 LEU   A CA  
765  C C   . LEU   A 94  ? 0.1433 0.1882 0.1670 -0.0039 -0.0068 0.0124  100 LEU   A C   
766  O O   . LEU   A 94  ? 0.1404 0.1903 0.1624 -0.0066 -0.0081 0.0128  100 LEU   A O   
767  C CB  . LEU   A 94  ? 0.1557 0.2052 0.1921 0.0005  -0.0063 0.0184  100 LEU   A CB  
768  C CG  . LEU   A 94  ? 0.2082 0.2574 0.2512 0.0034  -0.0053 0.0213  100 LEU   A CG  
769  C CD1 . LEU   A 94  ? 0.2185 0.2707 0.2705 0.0053  -0.0036 0.0238  100 LEU   A CD1 
770  C CD2 . LEU   A 94  ? 0.2455 0.2865 0.2863 0.0047  -0.0035 0.0181  100 LEU   A CD2 
771  N N   . ALA   A 95  ? 0.1469 0.1866 0.1690 -0.0035 -0.0051 0.0097  101 ALA   A N   
772  C CA  . ALA   A 95  ? 0.1403 0.1788 0.1586 -0.0057 -0.0045 0.0073  101 ALA   A CA  
773  C C   . ALA   A 95  ? 0.1173 0.1529 0.1369 -0.0047 -0.0024 0.0062  101 ALA   A C   
774  O O   . ALA   A 95  ? 0.1288 0.1617 0.1506 -0.0026 -0.0014 0.0062  101 ALA   A O   
775  C CB  . ALA   A 95  ? 0.1608 0.1938 0.1730 -0.0067 -0.0043 0.0047  101 ALA   A CB  
776  N N   . VAL   A 96  ? 0.1207 0.1566 0.1385 -0.0066 -0.0015 0.0047  102 VAL   A N   
777  C CA  . VAL   A 96  ? 0.1136 0.1462 0.1311 -0.0063 0.0007  0.0032  102 VAL   A CA  
778  C C   . VAL   A 96  ? 0.1379 0.1634 0.1487 -0.0067 0.0011  0.0012  102 VAL   A C   
779  O O   . VAL   A 96  ? 0.1715 0.1955 0.1787 -0.0083 0.0008  0.0004  102 VAL   A O   
780  C CB  . VAL   A 96  ? 0.1177 0.1541 0.1367 -0.0084 0.0016  0.0029  102 VAL   A CB  
781  C CG1 . VAL   A 96  ? 0.1251 0.1575 0.1428 -0.0085 0.0043  0.0011  102 VAL   A CG1 
782  C CG2 . VAL   A 96  ? 0.1294 0.1739 0.1560 -0.0079 0.0008  0.0057  102 VAL   A CG2 
783  N N   . GLY   A 97  ? 0.1313 0.1529 0.1411 -0.0053 0.0019  0.0006  103 GLY   A N   
784  C CA  . GLY   A 97  ? 0.1468 0.1627 0.1508 -0.0055 0.0017  -0.0005 103 GLY   A CA  
785  C C   . GLY   A 97  ? 0.1382 0.1517 0.1418 -0.0045 0.0026  -0.0014 103 GLY   A C   
786  O O   . GLY   A 97  ? 0.1461 0.1612 0.1541 -0.0033 0.0032  -0.0012 103 GLY   A O   
787  N N   . HIS   A 98  ? 0.1482 0.1577 0.1464 -0.0053 0.0029  -0.0022 104 HIS   A N   
788  C CA  . HIS   A 98  ? 0.1489 0.1565 0.1455 -0.0053 0.0037  -0.0035 104 HIS   A CA  
789  C C   . HIS   A 98  ? 0.1378 0.1451 0.1354 -0.0040 0.0019  -0.0033 104 HIS   A C   
790  O O   . HIS   A 98  ? 0.1424 0.1491 0.1388 -0.0035 -0.0003 -0.0022 104 HIS   A O   
791  C CB  . HIS   A 98  ? 0.1542 0.1586 0.1440 -0.0069 0.0039  -0.0038 104 HIS   A CB  
792  C CG  . HIS   A 98  ? 0.1705 0.1737 0.1576 -0.0078 0.0047  -0.0056 104 HIS   A CG  
793  N ND1 . HIS   A 98  ? 0.1786 0.1821 0.1675 -0.0087 0.0079  -0.0078 104 HIS   A ND1 
794  C CD2 . HIS   A 98  ? 0.1626 0.1647 0.1460 -0.0082 0.0029  -0.0056 104 HIS   A CD2 
795  C CE1 . HIS   A 98  ? 0.1769 0.1791 0.1626 -0.0099 0.0082  -0.0096 104 HIS   A CE1 
796  N NE2 . HIS   A 98  ? 0.1843 0.1860 0.1663 -0.0098 0.0050  -0.0083 104 HIS   A NE2 
797  N N   . SER   A 99  ? 0.1418 0.1490 0.1418 -0.0037 0.0033  -0.0047 105 SER   A N   
798  C CA  . SER   A 99  ? 0.1345 0.1410 0.1350 -0.0031 0.0021  -0.0051 105 SER   A CA  
799  C C   . SER   A 99  ? 0.1519 0.1571 0.1527 -0.0040 0.0045  -0.0078 105 SER   A C   
800  O O   . SER   A 99  ? 0.1687 0.1741 0.1722 -0.0044 0.0077  -0.0090 105 SER   A O   
801  C CB  . SER   A 99  ? 0.1531 0.1616 0.1587 -0.0012 0.0010  -0.0034 105 SER   A CB  
802  O OG  . SER   A 99  ? 0.1567 0.1671 0.1686 -0.0002 0.0030  -0.0030 105 SER   A OG  
803  N N   . GLU   A 100 ? 0.1439 0.1481 0.1420 -0.0048 0.0033  -0.0089 106 GLU   A N   
804  C CA  . GLU   A 100 ? 0.1600 0.1631 0.1581 -0.0063 0.0054  -0.0120 106 GLU   A CA  
805  C C   . GLU   A 100 ? 0.1671 0.1704 0.1684 -0.0052 0.0040  -0.0119 106 GLU   A C   
806  O O   . GLU   A 100 ? 0.1500 0.1542 0.1519 -0.0037 0.0012  -0.0095 106 GLU   A O   
807  C CB  . GLU   A 100 ? 0.1847 0.1871 0.1747 -0.0093 0.0049  -0.0137 106 GLU   A CB  
808  C CG  . GLU   A 100 ? 0.1951 0.1969 0.1820 -0.0105 0.0067  -0.0138 106 GLU   A CG  
809  C CD  . GLU   A 100 ? 0.2351 0.2366 0.2132 -0.0136 0.0059  -0.0144 106 GLU   A CD  
810  O OE1 . GLU   A 100 ? 0.3031 0.3049 0.2778 -0.0159 0.0058  -0.0166 106 GLU   A OE1 
811  O OE2 . GLU   A 100 ? 0.2153 0.2165 0.1899 -0.0139 0.0056  -0.0126 106 GLU   A OE2 
812  N N   . PRO   A 101 ? 0.1665 0.1687 0.1704 -0.0061 0.0066  -0.0147 107 PRO   A N   
813  C CA  . PRO   A 101 ? 0.1665 0.1688 0.1746 -0.0050 0.0058  -0.0144 107 PRO   A CA  
814  C C   . PRO   A 101 ? 0.1654 0.1688 0.1700 -0.0051 0.0016  -0.0132 107 PRO   A C   
815  O O   . PRO   A 101 ? 0.1677 0.1718 0.1756 -0.0032 0.0001  -0.0111 107 PRO   A O   
816  C CB  . PRO   A 101 ? 0.1852 0.1856 0.1953 -0.0070 0.0098  -0.0186 107 PRO   A CB  
817  C CG  . PRO   A 101 ? 0.1902 0.1897 0.2014 -0.0075 0.0137  -0.0199 107 PRO   A CG  
818  C CD  . PRO   A 101 ? 0.1712 0.1719 0.1758 -0.0081 0.0111  -0.0182 107 PRO   A CD  
819  N N   . GLY   A 102 ? 0.1597 0.1637 0.1579 -0.0074 -0.0002 -0.0142 108 GLY   A N   
820  C CA  . GLY   A 102 ? 0.1587 0.1644 0.1546 -0.0074 -0.0042 -0.0126 108 GLY   A CA  
821  C C   . GLY   A 102 ? 0.1569 0.1630 0.1528 -0.0052 -0.0067 -0.0088 108 GLY   A C   
822  O O   . GLY   A 102 ? 0.1600 0.1672 0.1556 -0.0047 -0.0096 -0.0072 108 GLY   A O   
823  N N   . ASP   A 103 ? 0.1326 0.1378 0.1295 -0.0040 -0.0053 -0.0076 109 ASP   A N   
824  C CA  . ASP   A 103 ? 0.1386 0.1440 0.1360 -0.0023 -0.0069 -0.0048 109 ASP   A CA  
825  C C   . ASP   A 103 ? 0.1361 0.1421 0.1385 -0.0005 -0.0073 -0.0039 109 ASP   A C   
826  O O   . ASP   A 103 ? 0.1431 0.1493 0.1460 0.0004  -0.0084 -0.0021 109 ASP   A O   
827  C CB  . ASP   A 103 ? 0.1396 0.1447 0.1365 -0.0022 -0.0053 -0.0041 109 ASP   A CB  
828  C CG  . ASP   A 103 ? 0.1535 0.1577 0.1448 -0.0039 -0.0053 -0.0043 109 ASP   A CG  
829  O OD1 . ASP   A 103 ? 0.1545 0.1588 0.1426 -0.0044 -0.0075 -0.0032 109 ASP   A OD1 
830  O OD2 . ASP   A 103 ? 0.1519 0.1557 0.1425 -0.0046 -0.0030 -0.0052 109 ASP   A OD2 
831  N N   . CYS   A 104 ? 0.1254 0.1315 0.1315 -0.0003 -0.0060 -0.0051 110 CYS   A N   
832  C CA  . CYS   A 104 ? 0.1322 0.1389 0.1425 0.0012  -0.0062 -0.0039 110 CYS   A CA  
833  C C   . CYS   A 104 ? 0.1365 0.1436 0.1462 0.0014  -0.0086 -0.0032 110 CYS   A C   
834  O O   . CYS   A 104 ? 0.1448 0.1521 0.1527 0.0004  -0.0100 -0.0040 110 CYS   A O   
835  C CB  . CYS   A 104 ? 0.1392 0.1455 0.1536 0.0012  -0.0043 -0.0052 110 CYS   A CB  
836  S SG  . CYS   A 104 ? 0.1490 0.1552 0.1675 0.0020  -0.0010 -0.0047 110 CYS   A SG  
837  N N   . GLY   A 105 ? 0.1290 0.1364 0.1403 0.0023  -0.0089 -0.0017 111 GLY   A N   
838  C CA  . GLY   A 105 ? 0.1349 0.1424 0.1469 0.0027  -0.0104 -0.0010 111 GLY   A CA  
839  C C   . GLY   A 105 ? 0.1360 0.1428 0.1460 0.0028  -0.0109 0.0002  111 GLY   A C   
840  O O   . GLY   A 105 ? 0.1406 0.1471 0.1523 0.0033  -0.0113 0.0008  111 GLY   A O   
841  N N   . GLY   A 106 ? 0.1305 0.1368 0.1375 0.0023  -0.0105 0.0003  112 GLY   A N   
842  C CA  . GLY   A 106 ? 0.1248 0.1299 0.1303 0.0022  -0.0104 0.0014  112 GLY   A CA  
843  C C   . GLY   A 106 ? 0.1273 0.1326 0.1344 0.0021  -0.0091 0.0014  112 GLY   A C   
844  O O   . GLY   A 106 ? 0.1235 0.1305 0.1313 0.0018  -0.0084 0.0011  112 GLY   A O   
845  N N   . ILE   A 107 ? 0.1179 0.1218 0.1257 0.0021  -0.0087 0.0018  113 ILE   A N   
846  C CA  . ILE   A 107 ? 0.1149 0.1191 0.1236 0.0013  -0.0070 0.0010  113 ILE   A CA  
847  C C   . ILE   A 107 ? 0.1187 0.1233 0.1251 -0.0003 -0.0057 0.0006  113 ILE   A C   
848  O O   . ILE   A 107 ? 0.1289 0.1319 0.1338 -0.0005 -0.0055 0.0009  113 ILE   A O   
849  C CB  . ILE   A 107 ? 0.1215 0.1237 0.1329 0.0017  -0.0062 0.0010  113 ILE   A CB  
850  C CG1 . ILE   A 107 ? 0.1391 0.1422 0.1537 0.0027  -0.0071 0.0010  113 ILE   A CG1 
851  C CG2 . ILE   A 107 ? 0.1305 0.1321 0.1420 0.0000  -0.0035 -0.0004 113 ILE   A CG2 
852  C CD1 . ILE   A 107 ? 0.1900 0.1914 0.2087 0.0035  -0.0063 0.0014  113 ILE   A CD1 
853  N N   . LEU   A 108 ? 0.1085 0.1157 0.1147 -0.0016 -0.0051 0.0000  114 LEU   A N   
854  C CA  . LEU   A 108 ? 0.1071 0.1157 0.1115 -0.0037 -0.0038 -0.0007 114 LEU   A CA  
855  C C   . LEU   A 108 ? 0.1119 0.1197 0.1166 -0.0054 -0.0019 -0.0023 114 LEU   A C   
856  O O   . LEU   A 108 ? 0.1238 0.1327 0.1296 -0.0055 -0.0019 -0.0025 114 LEU   A O   
857  C CB  . LEU   A 108 ? 0.1155 0.1290 0.1199 -0.0044 -0.0046 0.0001  114 LEU   A CB  
858  C CG  . LEU   A 108 ? 0.1257 0.1425 0.1285 -0.0073 -0.0038 -0.0005 114 LEU   A CG  
859  C CD1 . LEU   A 108 ? 0.1334 0.1491 0.1350 -0.0079 -0.0031 -0.0011 114 LEU   A CD1 
860  C CD2 . LEU   A 108 ? 0.1446 0.1674 0.1485 -0.0077 -0.0051 0.0014  114 LEU   A CD2 
861  N N   . ARG   A 109 ? 0.1158 0.1215 0.1197 -0.0070 0.0001  -0.0037 115 ARG   A N   
862  C CA  . ARG   A 109 ? 0.1265 0.1307 0.1310 -0.0091 0.0029  -0.0059 115 ARG   A CA  
863  C C   . ARG   A 109 ? 0.1370 0.1422 0.1392 -0.0125 0.0050  -0.0080 115 ARG   A C   
864  O O   . ARG   A 109 ? 0.1413 0.1468 0.1422 -0.0129 0.0046  -0.0076 115 ARG   A O   
865  C CB  . ARG   A 109 ? 0.1444 0.1435 0.1524 -0.0072 0.0043  -0.0057 115 ARG   A CB  
866  C CG  . ARG   A 109 ? 0.1568 0.1526 0.1648 -0.0065 0.0049  -0.0048 115 ARG   A CG  
867  C CD  . ARG   A 109 ? 0.1609 0.1524 0.1733 -0.0043 0.0059  -0.0034 115 ARG   A CD  
868  N NE  . ARG   A 109 ? 0.1728 0.1654 0.1865 -0.0015 0.0026  -0.0008 115 ARG   A NE  
869  C CZ  . ARG   A 109 ? 0.1695 0.1617 0.1874 0.0003  0.0022  0.0000  115 ARG   A CZ  
870  N NH1 . ARG   A 109 ? 0.1901 0.1811 0.2111 -0.0006 0.0051  -0.0020 115 ARG   A NH1 
871  N NH2 . ARG   A 109 ? 0.1729 0.1666 0.1915 0.0023  -0.0010 0.0022  115 ARG   A NH2 
872  N N   . CYS   A 110 ? 0.1499 0.1559 0.1513 -0.0156 0.0074  -0.0106 116 CYS   A N   
873  C CA  . CYS   A 110 ? 0.1807 0.1880 0.1797 -0.0199 0.0099  -0.0135 116 CYS   A CA  
874  C C   . CYS   A 110 ? 0.2070 0.2091 0.2080 -0.0215 0.0145  -0.0166 116 CYS   A C   
875  O O   . CYS   A 110 ? 0.2042 0.2021 0.2090 -0.0187 0.0153  -0.0159 116 CYS   A O   
876  C CB  . CYS   A 110 ? 0.1646 0.1791 0.1602 -0.0232 0.0086  -0.0139 116 CYS   A CB  
877  S SG  . CYS   A 110 ? 0.1730 0.1885 0.1678 -0.0250 0.0101  -0.0154 116 CYS   A SG  
878  N N   . GLN   A 111 ? 0.2307 0.2332 0.2297 -0.0262 0.0179  -0.0204 117 GLN   A N   
879  C CA  . GLN   A 111 ? 0.2594 0.2565 0.2608 -0.0282 0.0233  -0.0240 117 GLN   A CA  
880  C C   . GLN   A 111 ? 0.2638 0.2607 0.2665 -0.0283 0.0246  -0.0252 117 GLN   A C   
881  O O   . GLN   A 111 ? 0.2921 0.2835 0.2991 -0.0280 0.0289  -0.0270 117 GLN   A O   
882  C CB  . GLN   A 111 ? 0.2987 0.2967 0.2973 -0.0342 0.0271  -0.0287 117 GLN   A CB  
883  C CG  . GLN   A 111 ? 0.3637 0.3694 0.3567 -0.0392 0.0262  -0.0308 117 GLN   A CG  
884  C CD  . GLN   A 111 ? 0.4553 0.4633 0.4449 -0.0458 0.0294  -0.0356 117 GLN   A CD  
885  O OE1 . GLN   A 111 ? 0.4632 0.4767 0.4500 -0.0477 0.0269  -0.0349 117 GLN   A OE1 
886  N NE2 . GLN   A 111 ? 0.4596 0.4638 0.4496 -0.0497 0.0353  -0.0407 117 GLN   A NE2 
887  N N   . HIS   A 112 ? 0.2273 0.2300 0.2269 -0.0285 0.0214  -0.0238 118 HIS   A N   
888  C CA  . HIS   A 112 ? 0.2241 0.2269 0.2242 -0.0292 0.0229  -0.0249 118 HIS   A CA  
889  C C   . HIS   A 112 ? 0.2256 0.2261 0.2304 -0.0237 0.0207  -0.0216 118 HIS   A C   
890  O O   . HIS   A 112 ? 0.2490 0.2486 0.2558 -0.0237 0.0225  -0.0226 118 HIS   A O   
891  C CB  . HIS   A 112 ? 0.2181 0.2286 0.2121 -0.0328 0.0207  -0.0249 118 HIS   A CB  
892  C CG  . HIS   A 112 ? 0.2428 0.2572 0.2320 -0.0388 0.0224  -0.0282 118 HIS   A CG  
893  N ND1 . HIS   A 112 ? 0.2530 0.2735 0.2392 -0.0398 0.0187  -0.0261 118 HIS   A ND1 
894  C CD2 . HIS   A 112 ? 0.2925 0.3056 0.2798 -0.0443 0.0276  -0.0337 118 HIS   A CD2 
895  C CE1 . HIS   A 112 ? 0.2994 0.3227 0.2817 -0.0458 0.0212  -0.0301 118 HIS   A CE1 
896  N NE2 . HIS   A 112 ? 0.3148 0.3337 0.2973 -0.0490 0.0267  -0.0350 118 HIS   A NE2 
897  N N   . GLY   A 113 ? 0.1995 0.1997 0.2059 -0.0196 0.0169  -0.0178 119 GLY   A N   
898  C CA  . GLY   A 113 ? 0.1867 0.1856 0.1970 -0.0151 0.0146  -0.0149 119 GLY   A CA  
899  C C   . GLY   A 113 ? 0.1543 0.1566 0.1629 -0.0127 0.0096  -0.0114 119 GLY   A C   
900  O O   . GLY   A 113 ? 0.1540 0.1583 0.1597 -0.0135 0.0082  -0.0108 119 GLY   A O   
901  N N   . VAL   A 114 ? 0.1342 0.1370 0.1450 -0.0099 0.0075  -0.0094 120 VAL   A N   
902  C CA  . VAL   A 114 ? 0.1378 0.1431 0.1477 -0.0077 0.0036  -0.0066 120 VAL   A CA  
903  C C   . VAL   A 114 ? 0.1250 0.1354 0.1316 -0.0095 0.0024  -0.0059 120 VAL   A C   
904  O O   . VAL   A 114 ? 0.1376 0.1499 0.1433 -0.0112 0.0034  -0.0065 120 VAL   A O   
905  C CB  . VAL   A 114 ? 0.1486 0.1527 0.1624 -0.0046 0.0021  -0.0051 120 VAL   A CB  
906  C CG1 . VAL   A 114 ? 0.1587 0.1652 0.1717 -0.0029 -0.0010 -0.0029 120 VAL   A CG1 
907  C CG2 . VAL   A 114 ? 0.1520 0.1523 0.1696 -0.0026 0.0026  -0.0046 120 VAL   A CG2 
908  N N   . VAL   A 115 ? 0.1274 0.1401 0.1324 -0.0091 0.0003  -0.0043 121 VAL   A N   
909  C CA  . VAL   A 115 ? 0.1240 0.1422 0.1271 -0.0104 -0.0011 -0.0027 121 VAL   A CA  
910  C C   . VAL   A 115 ? 0.1306 0.1498 0.1360 -0.0076 -0.0032 0.0000  121 VAL   A C   
911  O O   . VAL   A 115 ? 0.1425 0.1654 0.1477 -0.0081 -0.0039 0.0019  121 VAL   A O   
912  C CB  . VAL   A 115 ? 0.1384 0.1589 0.1396 -0.0119 -0.0015 -0.0027 121 VAL   A CB  
913  C CG1 . VAL   A 115 ? 0.1583 0.1853 0.1590 -0.0126 -0.0035 -0.0001 121 VAL   A CG1 
914  C CG2 . VAL   A 115 ? 0.1503 0.1699 0.1492 -0.0154 0.0011  -0.0058 121 VAL   A CG2 
915  N N   . GLY   A 116 ? 0.1283 0.1446 0.1356 -0.0049 -0.0041 0.0004  122 GLY   A N   
916  C CA  . GLY   A 116 ? 0.1333 0.1501 0.1429 -0.0027 -0.0055 0.0023  122 GLY   A CA  
917  C C   . GLY   A 116 ? 0.1211 0.1348 0.1316 -0.0008 -0.0061 0.0019  122 GLY   A C   
918  O O   . GLY   A 116 ? 0.1207 0.1318 0.1305 -0.0008 -0.0058 0.0008  122 GLY   A O   
919  N N   . ILE   A 117 ? 0.1203 0.1343 0.1328 0.0007  -0.0068 0.0029  123 ILE   A N   
920  C CA  . ILE   A 117 ? 0.1126 0.1241 0.1252 0.0019  -0.0074 0.0021  123 ILE   A CA  
921  C C   . ILE   A 117 ? 0.1146 0.1271 0.1277 0.0022  -0.0072 0.0027  123 ILE   A C   
922  O O   . ILE   A 117 ? 0.1124 0.1273 0.1278 0.0025  -0.0067 0.0042  123 ILE   A O   
923  C CB  . ILE   A 117 ? 0.1272 0.1373 0.1420 0.0028  -0.0078 0.0016  123 ILE   A CB  
924  C CG1 . ILE   A 117 ? 0.1491 0.1605 0.1667 0.0032  -0.0072 0.0025  123 ILE   A CG1 
925  C CG2 . ILE   A 117 ? 0.1490 0.1578 0.1640 0.0027  -0.0080 0.0010  123 ILE   A CG2 
926  C CD1 . ILE   A 117 ? 0.1566 0.1666 0.1766 0.0038  -0.0074 0.0014  123 ILE   A CD1 
927  N N   . VAL   A 118 ? 0.1143 0.1252 0.1257 0.0023  -0.0073 0.0018  124 VAL   A N   
928  C CA  . VAL   A 118 ? 0.1115 0.1229 0.1237 0.0025  -0.0064 0.0017  124 VAL   A CA  
929  C C   . VAL   A 118 ? 0.1104 0.1217 0.1263 0.0034  -0.0055 0.0017  124 VAL   A C   
930  O O   . VAL   A 118 ? 0.1181 0.1279 0.1343 0.0035  -0.0060 0.0006  124 VAL   A O   
931  C CB  . VAL   A 118 ? 0.1178 0.1271 0.1268 0.0019  -0.0064 0.0004  124 VAL   A CB  
932  C CG1 . VAL   A 118 ? 0.1215 0.1309 0.1314 0.0018  -0.0048 -0.0004 124 VAL   A CG1 
933  C CG2 . VAL   A 118 ? 0.1253 0.1342 0.1312 0.0011  -0.0067 0.0007  124 VAL   A CG2 
934  N N   . SER   A 119 ? 0.1070 0.1201 0.1265 0.0040  -0.0042 0.0030  125 SER   A N   
935  C CA  . SER   A 119 ? 0.1164 0.1290 0.1408 0.0050  -0.0027 0.0034  125 SER   A CA  
936  C C   . SER   A 119 ? 0.1369 0.1494 0.1647 0.0054  -0.0003 0.0032  125 SER   A C   
937  O O   . SER   A 119 ? 0.1478 0.1584 0.1791 0.0058  0.0018  0.0020  125 SER   A O   
938  C CB  . SER   A 119 ? 0.1315 0.1465 0.1588 0.0057  -0.0030 0.0063  125 SER   A CB  
939  O OG  . SER   A 119 ? 0.1428 0.1573 0.1756 0.0068  -0.0012 0.0075  125 SER   A OG  
940  N N   . THR   A 120 ? 0.1252 0.1399 0.1532 0.0053  -0.0001 0.0042  126 THR   A N   
941  C CA  . THR   A 120 ? 0.1287 0.1436 0.1615 0.0060  0.0027  0.0043  126 THR   A CA  
942  C C   . THR   A 120 ? 0.1390 0.1542 0.1685 0.0048  0.0028  0.0029  126 THR   A C   
943  O O   . THR   A 120 ? 0.1198 0.1351 0.1436 0.0037  0.0007  0.0025  126 THR   A O   
944  C CB  . THR   A 120 ? 0.1245 0.1435 0.1644 0.0076  0.0031  0.0086  126 THR   A CB  
945  O OG1 . THR   A 120 ? 0.1441 0.1675 0.1823 0.0070  0.0010  0.0106  126 THR   A OG1 
946  C CG2 . THR   A 120 ? 0.1327 0.1520 0.1756 0.0087  0.0027  0.0109  126 THR   A CG2 
947  N N   . GLY   A 121 ? 0.1425 0.1576 0.1757 0.0050  0.0057  0.0022  127 GLY   A N   
948  C CA  . GLY   A 121 ? 0.1534 0.1692 0.1841 0.0039  0.0061  0.0013  127 GLY   A CA  
949  C C   . GLY   A 121 ? 0.1587 0.1731 0.1931 0.0038  0.0101  -0.0006 127 GLY   A C   
950  O O   . GLY   A 121 ? 0.1674 0.1806 0.2077 0.0048  0.0129  -0.0009 127 GLY   A O   
951  N N   . GLY   A 122 ? 0.1601 0.1744 0.1908 0.0023  0.0108  -0.0021 128 GLY   A N   
952  C CA  . GLY   A 122 ? 0.1698 0.1825 0.2023 0.0014  0.0149  -0.0047 128 GLY   A CA  
953  C C   . GLY   A 122 ? 0.1759 0.1918 0.2105 0.0013  0.0154  -0.0035 128 GLY   A C   
954  O O   . GLY   A 122 ? 0.1723 0.1927 0.2102 0.0023  0.0132  -0.0001 128 GLY   A O   
955  N N   . ASN   A 123 ? 0.1667 0.1807 0.1996 -0.0004 0.0186  -0.0063 129 ASN   A N   
956  C CA  . ASN   A 123 ? 0.1640 0.1810 0.1997 -0.0007 0.0200  -0.0056 129 ASN   A CA  
957  C C   . ASN   A 123 ? 0.1629 0.1830 0.1951 -0.0013 0.0162  -0.0034 129 ASN   A C   
958  O O   . ASN   A 123 ? 0.1742 0.1990 0.2116 -0.0009 0.0162  -0.0014 129 ASN   A O   
959  C CB  . ASN   A 123 ? 0.1726 0.1930 0.2207 0.0015  0.0227  -0.0036 129 ASN   A CB  
960  C CG  . ASN   A 123 ? 0.2109 0.2274 0.2632 0.0016  0.0278  -0.0065 129 ASN   A CG  
961  O OD1 . ASN   A 123 ? 0.2319 0.2451 0.2804 -0.0006 0.0312  -0.0106 129 ASN   A OD1 
962  N ND2 . ASN   A 123 ? 0.2228 0.2395 0.2827 0.0039  0.0286  -0.0047 129 ASN   A ND2 
963  N N   . GLY   A 124 ? 0.1502 0.1676 0.1737 -0.0025 0.0136  -0.0041 130 GLY   A N   
964  C CA  . GLY   A 124 ? 0.1372 0.1564 0.1572 -0.0033 0.0109  -0.0027 130 GLY   A CA  
965  C C   . GLY   A 124 ? 0.1292 0.1521 0.1519 -0.0022 0.0078  0.0000  130 GLY   A C   
966  O O   . GLY   A 124 ? 0.1463 0.1711 0.1667 -0.0034 0.0061  0.0007  130 GLY   A O   
967  N N   . LEU   A 125 ? 0.1310 0.1544 0.1575 -0.0004 0.0073  0.0012  131 LEU   A N   
968  C CA  . LEU   A 125 ? 0.1316 0.1579 0.1591 0.0003  0.0043  0.0037  131 LEU   A CA  
969  C C   . LEU   A 125 ? 0.1388 0.1610 0.1617 0.0006  0.0030  0.0027  131 LEU   A C   
970  O O   . LEU   A 125 ? 0.1475 0.1655 0.1686 0.0007  0.0044  0.0006  131 LEU   A O   
971  C CB  . LEU   A 125 ? 0.1297 0.1604 0.1661 0.0023  0.0047  0.0068  131 LEU   A CB  
972  C CG  . LEU   A 125 ? 0.1492 0.1858 0.1918 0.0022  0.0054  0.0088  131 LEU   A CG  
973  C CD1 . LEU   A 125 ? 0.1832 0.2229 0.2362 0.0048  0.0070  0.0119  131 LEU   A CD1 
974  C CD2 . LEU   A 125 ? 0.1594 0.2014 0.1997 0.0004  0.0024  0.0104  131 LEU   A CD2 
975  N N   . VAL   A 126 ? 0.1208 0.1443 0.1418 0.0004  0.0005  0.0040  132 VAL   A N   
976  C CA  . VAL   A 126 ? 0.1244 0.1448 0.1426 0.0008  -0.0008 0.0034  132 VAL   A CA  
977  C C   . VAL   A 126 ? 0.1195 0.1438 0.1406 0.0014  -0.0024 0.0060  132 VAL   A C   
978  O O   . VAL   A 126 ? 0.1226 0.1509 0.1437 0.0003  -0.0034 0.0074  132 VAL   A O   
979  C CB  . VAL   A 126 ? 0.1299 0.1469 0.1415 -0.0004 -0.0017 0.0018  132 VAL   A CB  
980  C CG1 . VAL   A 126 ? 0.1420 0.1610 0.1519 -0.0019 -0.0024 0.0022  132 VAL   A CG1 
981  C CG2 . VAL   A 126 ? 0.1434 0.1580 0.1535 0.0002  -0.0030 0.0015  132 VAL   A CG2 
982  N N   . GLY   A 127 ? 0.1164 0.1395 0.1394 0.0027  -0.0025 0.0067  133 GLY   A N   
983  C CA  . GLY   A 127 ? 0.1152 0.1415 0.1402 0.0030  -0.0038 0.0093  133 GLY   A CA  
984  C C   . GLY   A 127 ? 0.1212 0.1445 0.1426 0.0027  -0.0048 0.0080  133 GLY   A C   
985  O O   . GLY   A 127 ? 0.1263 0.1455 0.1464 0.0031  -0.0043 0.0059  133 GLY   A O   
986  N N   . PHE   A 128 ? 0.1075 0.1335 0.1275 0.0017  -0.0060 0.0092  134 PHE   A N   
987  C CA  . PHE   A 128 ? 0.1061 0.1296 0.1232 0.0012  -0.0066 0.0079  134 PHE   A CA  
988  C C   . PHE   A 128 ? 0.1164 0.1423 0.1356 0.0014  -0.0069 0.0102  134 PHE   A C   
989  O O   . PHE   A 128 ? 0.1212 0.1522 0.1415 0.0006  -0.0075 0.0129  134 PHE   A O   
990  C CB  . PHE   A 128 ? 0.1136 0.1373 0.1264 -0.0010 -0.0069 0.0065  134 PHE   A CB  
991  C CG  . PHE   A 128 ? 0.1171 0.1390 0.1278 -0.0015 -0.0064 0.0049  134 PHE   A CG  
992  C CD1 . PHE   A 128 ? 0.1201 0.1372 0.1288 -0.0009 -0.0062 0.0032  134 PHE   A CD1 
993  C CD2 . PHE   A 128 ? 0.1408 0.1660 0.1515 -0.0028 -0.0063 0.0053  134 PHE   A CD2 
994  C CE1 . PHE   A 128 ? 0.1218 0.1371 0.1283 -0.0015 -0.0056 0.0022  134 PHE   A CE1 
995  C CE2 . PHE   A 128 ? 0.1374 0.1605 0.1462 -0.0034 -0.0055 0.0038  134 PHE   A CE2 
996  C CZ  . PHE   A 128 ? 0.1296 0.1474 0.1359 -0.0028 -0.0051 0.0024  134 PHE   A CZ  
997  N N   . ALA   A 129 ? 0.1109 0.1337 0.1306 0.0022  -0.0066 0.0094  135 ALA   A N   
998  C CA  . ALA   A 129 ? 0.1178 0.1422 0.1389 0.0023  -0.0066 0.0114  135 ALA   A CA  
999  C C   . ALA   A 129 ? 0.1138 0.1392 0.1307 0.0000  -0.0070 0.0104  135 ALA   A C   
1000 O O   . ALA   A 129 ? 0.1179 0.1399 0.1328 -0.0004 -0.0067 0.0076  135 ALA   A O   
1001 C CB  . ALA   A 129 ? 0.1186 0.1391 0.1421 0.0037  -0.0058 0.0103  135 ALA   A CB  
1002 N N   . ASP   A 130 ? 0.1183 0.1486 0.1341 -0.0018 -0.0075 0.0125  136 ASP   A N   
1003 C CA  . ASP   A 130 ? 0.1268 0.1582 0.1383 -0.0046 -0.0072 0.0109  136 ASP   A CA  
1004 C C   . ASP   A 130 ? 0.1316 0.1604 0.1431 -0.0046 -0.0062 0.0101  136 ASP   A C   
1005 O O   . ASP   A 130 ? 0.1386 0.1674 0.1531 -0.0031 -0.0061 0.0123  136 ASP   A O   
1006 C CB  . ASP   A 130 ? 0.1443 0.1827 0.1542 -0.0071 -0.0082 0.0137  136 ASP   A CB  
1007 C CG  . ASP   A 130 ? 0.2320 0.2723 0.2368 -0.0111 -0.0075 0.0116  136 ASP   A CG  
1008 O OD1 . ASP   A 130 ? 0.1879 0.2253 0.1904 -0.0123 -0.0063 0.0078  136 ASP   A OD1 
1009 O OD2 . ASP   A 130 ? 0.2953 0.3395 0.2982 -0.0131 -0.0077 0.0135  136 ASP   A OD2 
1010 N N   . VAL   A 131 ? 0.1250 0.1516 0.1340 -0.0062 -0.0050 0.0069  137 VAL   A N   
1011 C CA  . VAL   A 131 ? 0.1192 0.1439 0.1284 -0.0067 -0.0036 0.0059  137 VAL   A CA  
1012 C C   . VAL   A 131 ? 0.1354 0.1623 0.1405 -0.0105 -0.0021 0.0044  137 VAL   A C   
1013 O O   . VAL   A 131 ? 0.1332 0.1587 0.1382 -0.0114 -0.0004 0.0031  137 VAL   A O   
1014 C CB  . VAL   A 131 ? 0.1342 0.1537 0.1459 -0.0048 -0.0029 0.0034  137 VAL   A CB  
1015 C CG1 . VAL   A 131 ? 0.1435 0.1612 0.1586 -0.0018 -0.0042 0.0044  137 VAL   A CG1 
1016 C CG2 . VAL   A 131 ? 0.1373 0.1544 0.1477 -0.0056 -0.0020 0.0007  137 VAL   A CG2 
1017 N N   . ARG   A 132 ? 0.1409 0.1714 0.1425 -0.0132 -0.0024 0.0041  138 ARG   A N   
1018 C CA  . ARG   A 132 ? 0.1448 0.1773 0.1419 -0.0177 -0.0004 0.0016  138 ARG   A CA  
1019 C C   . ARG   A 132 ? 0.1543 0.1910 0.1489 -0.0201 -0.0003 0.0036  138 ARG   A C   
1020 O O   . ARG   A 132 ? 0.1554 0.1926 0.1463 -0.0239 0.0022  0.0008  138 ARG   A O   
1021 C CB  . ARG   A 132 ? 0.1371 0.1730 0.1311 -0.0205 -0.0009 0.0007  138 ARG   A CB  
1022 C CG  . ARG   A 132 ? 0.1418 0.1727 0.1376 -0.0189 -0.0001 -0.0019 138 ARG   A CG  
1023 C CD  . ARG   A 132 ? 0.1538 0.1885 0.1467 -0.0220 -0.0004 -0.0027 138 ARG   A CD  
1024 N NE  . ARG   A 132 ? 0.1424 0.1824 0.1366 -0.0206 -0.0036 0.0014  138 ARG   A NE  
1025 C CZ  . ARG   A 132 ? 0.1704 0.2142 0.1638 -0.0223 -0.0046 0.0016  138 ARG   A CZ  
1026 N NH1 . ARG   A 132 ? 0.1834 0.2271 0.1737 -0.0260 -0.0027 -0.0021 138 ARG   A NH1 
1027 N NH2 . ARG   A 132 ? 0.1743 0.2226 0.1705 -0.0204 -0.0071 0.0056  138 ARG   A NH2 
1028 N N   . ASP   A 133 ? 0.1461 0.1859 0.1426 -0.0181 -0.0024 0.0084  139 ASP   A N   
1029 C CA  . ASP   A 133 ? 0.1584 0.2023 0.1526 -0.0203 -0.0023 0.0111  139 ASP   A CA  
1030 C C   . ASP   A 133 ? 0.1583 0.1976 0.1547 -0.0188 -0.0003 0.0104  139 ASP   A C   
1031 O O   . ASP   A 133 ? 0.1785 0.2205 0.1724 -0.0210 0.0005  0.0121  139 ASP   A O   
1032 C CB  . ASP   A 133 ? 0.1817 0.2311 0.1780 -0.0187 -0.0052 0.0174  139 ASP   A CB  
1033 C CG  . ASP   A 133 ? 0.2205 0.2656 0.2236 -0.0136 -0.0057 0.0195  139 ASP   A CG  
1034 O OD1 . ASP   A 133 ? 0.1996 0.2399 0.2052 -0.0112 -0.0054 0.0166  139 ASP   A OD1 
1035 O OD2 . ASP   A 133 ? 0.2436 0.2904 0.2494 -0.0121 -0.0061 0.0240  139 ASP   A OD2 
1036 N N   . LEU   A 134 ? 0.1418 0.1749 0.1426 -0.0156 0.0005  0.0080  140 LEU   A N   
1037 C CA  . LEU   A 134 ? 0.1438 0.1730 0.1478 -0.0141 0.0022  0.0072  140 LEU   A CA  
1038 C C   . LEU   A 134 ? 0.1482 0.1751 0.1504 -0.0167 0.0054  0.0027  140 LEU   A C   
1039 O O   . LEU   A 134 ? 0.1519 0.1744 0.1574 -0.0152 0.0065  -0.0005 140 LEU   A O   
1040 C CB  . LEU   A 134 ? 0.1420 0.1668 0.1517 -0.0098 0.0012  0.0068  140 LEU   A CB  
1041 C CG  . LEU   A 134 ? 0.1660 0.1924 0.1781 -0.0073 -0.0010 0.0105  140 LEU   A CG  
1042 C CD1 . LEU   A 134 ? 0.1844 0.2065 0.2009 -0.0041 -0.0016 0.0091  140 LEU   A CD1 
1043 C CD2 . LEU   A 134 ? 0.1986 0.2274 0.2120 -0.0071 -0.0011 0.0147  140 LEU   A CD2 
1044 N N   . LEU   A 135 ? 0.1510 0.1812 0.1482 -0.0209 0.0070  0.0025  141 LEU   A N   
1045 C CA  . LEU   A 135 ? 0.1650 0.1933 0.1601 -0.0243 0.0109  -0.0025 141 LEU   A CA  
1046 C C   . LEU   A 135 ? 0.1718 0.1953 0.1720 -0.0225 0.0135  -0.0046 141 LEU   A C   
1047 O O   . LEU   A 135 ? 0.1744 0.1944 0.1764 -0.0233 0.0165  -0.0088 141 LEU   A O   
1048 C CB  . LEU   A 135 ? 0.1754 0.2090 0.1630 -0.0300 0.0122  -0.0024 141 LEU   A CB  
1049 C CG  . LEU   A 135 ? 0.1959 0.2362 0.1785 -0.0324 0.0092  0.0003  141 LEU   A CG  
1050 C CD1 . LEU   A 135 ? 0.2069 0.2527 0.1816 -0.0390 0.0110  -0.0007 141 LEU   A CD1 
1051 C CD2 . LEU   A 135 ? 0.2012 0.2403 0.1845 -0.0319 0.0086  -0.0022 141 LEU   A CD2 
1052 N N   . TRP   A 136 ? 0.1536 0.1768 0.1571 -0.0199 0.0123  -0.0016 142 TRP   A N   
1053 C CA  . TRP   A 136 ? 0.1550 0.1745 0.1638 -0.0183 0.0144  -0.0032 142 TRP   A CA  
1054 C C   . TRP   A 136 ? 0.1655 0.1808 0.1805 -0.0149 0.0140  -0.0054 142 TRP   A C   
1055 O O   . TRP   A 136 ? 0.1803 0.1930 0.2004 -0.0140 0.0161  -0.0074 142 TRP   A O   
1056 C CB  . TRP   A 136 ? 0.1507 0.1710 0.1613 -0.0168 0.0134  0.0007  142 TRP   A CB  
1057 C CG  . TRP   A 136 ? 0.1521 0.1730 0.1649 -0.0134 0.0097  0.0042  142 TRP   A CG  
1058 C CD1 . TRP   A 136 ? 0.1694 0.1940 0.1794 -0.0137 0.0076  0.0085  142 TRP   A CD1 
1059 C CD2 . TRP   A 136 ? 0.1557 0.1735 0.1743 -0.0096 0.0082  0.0038  142 TRP   A CD2 
1060 N NE1 . TRP   A 136 ? 0.1768 0.2003 0.1910 -0.0101 0.0054  0.0104  142 TRP   A NE1 
1061 C CE2 . TRP   A 136 ? 0.1642 0.1835 0.1831 -0.0079 0.0057  0.0073  142 TRP   A CE2 
1062 C CE3 . TRP   A 136 ? 0.1601 0.1746 0.1839 -0.0078 0.0087  0.0009  142 TRP   A CE3 
1063 C CZ2 . TRP   A 136 ? 0.1780 0.1951 0.2013 -0.0048 0.0042  0.0073  142 TRP   A CZ2 
1064 C CZ3 . TRP   A 136 ? 0.1848 0.1979 0.2126 -0.0048 0.0065  0.0014  142 TRP   A CZ3 
1065 C CH2 . TRP   A 136 ? 0.1800 0.1941 0.2072 -0.0036 0.0045  0.0042  142 TRP   A CH2 
1066 N N   . LEU   A 137 ? 0.1460 0.1611 0.1610 -0.0130 0.0113  -0.0047 143 LEU   A N   
1067 C CA  . LEU   A 137 ? 0.1723 0.1841 0.1925 -0.0102 0.0108  -0.0063 143 LEU   A CA  
1068 C C   . LEU   A 137 ? 0.1955 0.2048 0.2176 -0.0116 0.0144  -0.0100 143 LEU   A C   
1069 O O   . LEU   A 137 ? 0.1935 0.2002 0.2218 -0.0092 0.0147  -0.0108 143 LEU   A O   
1070 C CB  . LEU   A 137 ? 0.1682 0.1804 0.1871 -0.0087 0.0078  -0.0050 143 LEU   A CB  
1071 C CG  . LEU   A 137 ? 0.1590 0.1724 0.1785 -0.0064 0.0047  -0.0019 143 LEU   A CG  
1072 C CD1 . LEU   A 137 ? 0.1751 0.1892 0.1925 -0.0057 0.0025  -0.0010 143 LEU   A CD1 
1073 C CD2 . LEU   A 137 ? 0.1657 0.1771 0.1911 -0.0036 0.0038  -0.0020 143 LEU   A CD2 
1074 N N   . ASP   A 138 ? 0.2201 0.2304 0.2375 -0.0158 0.0175  -0.0121 144 ASP   A N   
1075 C CA  . ASP   A 138 ? 0.2612 0.2687 0.2803 -0.0177 0.0220  -0.0163 144 ASP   A CA  
1076 C C   . ASP   A 138 ? 0.3111 0.3171 0.3340 -0.0186 0.0260  -0.0184 144 ASP   A C   
1077 O O   . ASP   A 138 ? 0.3220 0.3252 0.3479 -0.0201 0.0305  -0.0221 144 ASP   A O   
1078 C CB  . ASP   A 138 ? 0.2701 0.2794 0.2818 -0.0227 0.0241  -0.0185 144 ASP   A CB  
1079 C CG  . ASP   A 138 ? 0.3390 0.3496 0.3474 -0.0225 0.0212  -0.0174 144 ASP   A CG  
1080 O OD1 . ASP   A 138 ? 0.3640 0.3731 0.3762 -0.0185 0.0183  -0.0154 144 ASP   A OD1 
1081 O OD2 . ASP   A 138 ? 0.4124 0.4262 0.4143 -0.0267 0.0218  -0.0185 144 ASP   A OD2 
1082 N N   . GLU   A 139 ? 0.3345 0.3421 0.3580 -0.0180 0.0250  -0.0164 145 GLU   A N   
1083 C CA  . GLU   A 139 ? 0.3807 0.3872 0.4076 -0.0192 0.0291  -0.0186 145 GLU   A CA  
1084 C C   . GLU   A 139 ? 0.4051 0.4113 0.4387 -0.0157 0.0273  -0.0166 145 GLU   A C   
1085 O O   . GLU   A 139 ? 0.3929 0.3999 0.4275 -0.0127 0.0229  -0.0136 145 GLU   A O   
1086 C CB  . GLU   A 139 ? 0.4370 0.4463 0.4557 -0.0241 0.0312  -0.0189 145 GLU   A CB  
1087 C CG  . GLU   A 139 ? 0.5267 0.5395 0.5415 -0.0234 0.0271  -0.0141 145 GLU   A CG  
1088 C CD  . GLU   A 139 ? 0.6368 0.6539 0.6423 -0.0280 0.0274  -0.0128 145 GLU   A CD  
1089 O OE1 . GLU   A 139 ? 0.6341 0.6539 0.6376 -0.0275 0.0250  -0.0084 145 GLU   A OE1 
1090 O OE2 . GLU   A 139 ? 0.6882 0.7062 0.6887 -0.0324 0.0302  -0.0160 145 GLU   A OE2 
1091 N N   . GLU   A 140 ? 0.4401 0.4452 0.4782 -0.0165 0.0310  -0.0185 146 GLU   A N   
1092 C CA  . GLU   A 140 ? 0.4838 0.4891 0.5287 -0.0142 0.0304  -0.0175 146 GLU   A CA  
1093 C C   . GLU   A 140 ? 0.5113 0.5155 0.5654 -0.0102 0.0286  -0.0174 146 GLU   A C   
1094 O O   . GLU   A 140 ? 0.5255 0.5291 0.5876 -0.0094 0.0310  -0.0187 146 GLU   A O   
1095 C CB  . GLU   A 140 ? 0.5271 0.5344 0.5683 -0.0136 0.0270  -0.0139 146 GLU   A CB  
1096 C CG  . GLU   A 140 ? 0.6075 0.6149 0.6559 -0.0109 0.0253  -0.0128 146 GLU   A CG  
1097 C CD  . GLU   A 140 ? 0.7150 0.7226 0.7641 -0.0125 0.0280  -0.0127 146 GLU   A CD  
1098 O OE1 . GLU   A 140 ? 0.7495 0.7582 0.7936 -0.0135 0.0271  -0.0099 146 GLU   A OE1 
1099 O OE2 . GLU   A 140 ? 0.7313 0.7382 0.7866 -0.0128 0.0313  -0.0151 146 GLU   A OE2 
1100 N N   . SER   B 1   ? 0.1970 0.2129 0.2152 0.0006  -0.0207 0.0241  7   SER   C N   
1101 C CA  . SER   B 1   ? 0.1898 0.2062 0.2149 -0.0001 -0.0208 0.0247  7   SER   C CA  
1102 C C   . SER   B 1   ? 0.1921 0.2066 0.2168 -0.0003 -0.0202 0.0221  7   SER   C C   
1103 O O   . SER   B 1   ? 0.2087 0.2216 0.2279 -0.0001 -0.0207 0.0199  7   SER   C O   
1104 C CB  . SER   B 1   ? 0.2288 0.2463 0.2562 -0.0009 -0.0241 0.0271  7   SER   C CB  
1105 O OG  . SER   B 1   ? 0.2797 0.2958 0.3020 -0.0016 -0.0270 0.0255  7   SER   C OG  
1106 N N   . GLY   B 2   ? 0.1717 0.1863 0.2022 -0.0006 -0.0189 0.0224  8   GLY   C N   
1107 C CA  . GLY   B 2   ? 0.1700 0.1828 0.2002 -0.0007 -0.0182 0.0205  8   GLY   C CA  
1108 C C   . GLY   B 2   ? 0.1552 0.1680 0.1901 -0.0003 -0.0152 0.0205  8   GLY   C C   
1109 O O   . GLY   B 2   ? 0.1587 0.1723 0.1957 0.0002  -0.0134 0.0209  8   GLY   C O   
1110 N N   . ALA   B 3   ? 0.1483 0.1599 0.1848 -0.0006 -0.0146 0.0201  9   ALA   C N   
1111 C CA  . ALA   B 3   ? 0.1464 0.1576 0.1864 -0.0001 -0.0115 0.0200  9   ALA   C CA  
1112 C C   . ALA   B 3   ? 0.1334 0.1423 0.1705 0.0001  -0.0105 0.0185  9   ALA   C C   
1113 O O   . ALA   B 3   ? 0.1446 0.1525 0.1789 -0.0003 -0.0123 0.0179  9   ALA   C O   
1114 C CB  . ALA   B 3   ? 0.1670 0.1795 0.2146 -0.0007 -0.0112 0.0225  9   ALA   C CB  
1115 N N   . ILE   B 4   ? 0.1259 0.1339 0.1635 0.0008  -0.0075 0.0178  10  ILE   C N   
1116 C CA  . ILE   B 4   ? 0.1187 0.1246 0.1541 0.0012  -0.0059 0.0171  10  ILE   C CA  
1117 C C   . ILE   B 4   ? 0.1262 0.1321 0.1675 0.0010  -0.0038 0.0189  10  ILE   C C   
1118 O O   . ILE   B 4   ? 0.1359 0.1428 0.1814 0.0012  -0.0021 0.0197  10  ILE   C O   
1119 C CB  . ILE   B 4   ? 0.1273 0.1320 0.1581 0.0024  -0.0040 0.0151  10  ILE   C CB  
1120 C CG1 . ILE   B 4   ? 0.1383 0.1435 0.1650 0.0027  -0.0058 0.0135  10  ILE   C CG1 
1121 C CG2 . ILE   B 4   ? 0.1634 0.1658 0.1908 0.0029  -0.0028 0.0147  10  ILE   C CG2 
1122 C CD1 . ILE   B 4   ? 0.1568 0.1614 0.1804 0.0036  -0.0043 0.0115  10  ILE   C CD1 
1123 N N   . TYR   B 5   ? 0.1238 0.1287 0.1663 0.0005  -0.0038 0.0198  11  TYR   C N   
1124 C CA  . TYR   B 5   ? 0.1390 0.1440 0.1880 0.0003  -0.0014 0.0218  11  TYR   C CA  
1125 C C   . TYR   B 5   ? 0.1507 0.1532 0.1961 0.0013  0.0017  0.0214  11  TYR   C C   
1126 O O   . TYR   B 5   ? 0.1704 0.1715 0.2141 0.0010  0.0008  0.0215  11  TYR   C O   
1127 C CB  . TYR   B 5   ? 0.1493 0.1557 0.2044 -0.0012 -0.0041 0.0237  11  TYR   C CB  
1128 C CG  . TYR   B 5   ? 0.1600 0.1689 0.2181 -0.0019 -0.0071 0.0245  11  TYR   C CG  
1129 C CD1 . TYR   B 5   ? 0.1562 0.1672 0.2214 -0.0018 -0.0060 0.0264  11  TYR   C CD1 
1130 C CD2 . TYR   B 5   ? 0.1660 0.1752 0.2197 -0.0024 -0.0109 0.0235  11  TYR   C CD2 
1131 C CE1 . TYR   B 5   ? 0.1620 0.1754 0.2297 -0.0023 -0.0088 0.0276  11  TYR   C CE1 
1132 C CE2 . TYR   B 5   ? 0.1852 0.1966 0.2406 -0.0029 -0.0136 0.0244  11  TYR   C CE2 
1133 C CZ  . TYR   B 5   ? 0.1867 0.2002 0.2491 -0.0029 -0.0127 0.0266  11  TYR   C CZ  
1134 O OH  . TYR   B 5   ? 0.2070 0.2227 0.2709 -0.0032 -0.0153 0.0280  11  TYR   C OH  
1135 N N   . VAL   B 6   ? 0.1535 0.1551 0.1978 0.0024  0.0053  0.0209  12  VAL   C N   
1136 C CA  . VAL   B 6   ? 0.1670 0.1660 0.2067 0.0035  0.0084  0.0206  12  VAL   C CA  
1137 C C   . VAL   B 6   ? 0.1712 0.1698 0.2155 0.0041  0.0129  0.0220  12  VAL   C C   
1138 O O   . VAL   B 6   ? 0.1588 0.1583 0.2058 0.0044  0.0142  0.0216  12  VAL   C O   
1139 C CB  . VAL   B 6   ? 0.1827 0.1804 0.2138 0.0046  0.0082  0.0179  12  VAL   C CB  
1140 C CG1 . VAL   B 6   ? 0.1913 0.1900 0.2231 0.0049  0.0086  0.0164  12  VAL   C CG1 
1141 C CG2 . VAL   B 6   ? 0.2102 0.2052 0.2358 0.0059  0.0112  0.0178  12  VAL   C CG2 
1142 N N   . GLY   B 7   ? 0.1805 0.1778 0.2266 0.0042  0.0155  0.0239  13  GLY   C N   
1143 C CA  . GLY   B 7   ? 0.1797 0.1767 0.2308 0.0049  0.0203  0.0255  13  GLY   C CA  
1144 C C   . GLY   B 7   ? 0.1793 0.1792 0.2405 0.0040  0.0198  0.0270  13  GLY   C C   
1145 O O   . GLY   B 7   ? 0.1854 0.1875 0.2517 0.0026  0.0159  0.0281  13  GLY   C O   
1146 N N   . ASN   B 8   ? 0.1682 0.1681 0.2318 0.0050  0.0230  0.0267  14  ASN   C N   
1147 C CA  . ASN   B 8   ? 0.1700 0.1728 0.2433 0.0044  0.0224  0.0283  14  ASN   C CA  
1148 C C   . ASN   B 8   ? 0.1528 0.1563 0.2238 0.0045  0.0202  0.0262  14  ASN   C C   
1149 O O   . ASN   B 8   ? 0.1524 0.1569 0.2292 0.0048  0.0216  0.0268  14  ASN   C O   
1150 C CB  . ASN   B 8   ? 0.1951 0.1978 0.2759 0.0053  0.0279  0.0302  14  ASN   C CB  
1151 C CG  . ASN   B 8   ? 0.2820 0.2853 0.3693 0.0047  0.0292  0.0333  14  ASN   C CG  
1152 O OD1 . ASN   B 8   ? 0.3011 0.3074 0.3985 0.0034  0.0271  0.0358  14  ASN   C OD1 
1153 N ND2 . ASN   B 8   ? 0.3099 0.3106 0.3916 0.0055  0.0324  0.0332  14  ASN   C ND2 
1154 N N   . TYR   B 9   ? 0.1405 0.1435 0.2039 0.0041  0.0167  0.0242  15  TYR   C N   
1155 C CA  . TYR   B 9   ? 0.1399 0.1436 0.2009 0.0041  0.0145  0.0224  15  TYR   C CA  
1156 C C   . TYR   B 9   ? 0.1227 0.1285 0.1834 0.0028  0.0093  0.0228  15  TYR   C C   
1157 O O   . TYR   B 9   ? 0.1301 0.1356 0.1879 0.0022  0.0071  0.0229  15  TYR   C O   
1158 C CB  . TYR   B 9   ? 0.1421 0.1434 0.1937 0.0051  0.0154  0.0191  15  TYR   C CB  
1159 C CG  . TYR   B 9   ? 0.1532 0.1518 0.2027 0.0064  0.0203  0.0179  15  TYR   C CG  
1160 C CD1 . TYR   B 9   ? 0.1773 0.1757 0.2320 0.0070  0.0233  0.0179  15  TYR   C CD1 
1161 C CD2 . TYR   B 9   ? 0.1931 0.1891 0.2350 0.0073  0.0220  0.0169  15  TYR   C CD2 
1162 C CE1 . TYR   B 9   ? 0.2031 0.1986 0.2552 0.0083  0.0281  0.0164  15  TYR   C CE1 
1163 C CE2 . TYR   B 9   ? 0.2293 0.2226 0.2679 0.0086  0.0266  0.0156  15  TYR   C CE2 
1164 C CZ  . TYR   B 9   ? 0.2518 0.2447 0.2951 0.0092  0.0296  0.0151  15  TYR   C CZ  
1165 O OH  . TYR   B 9   ? 0.3147 0.3044 0.3540 0.0106  0.0344  0.0136  15  TYR   C OH  
1166 N N   . ARG   B 10  ? 0.1193 0.1268 0.1826 0.0026  0.0075  0.0230  16  ARG   C N   
1167 C CA  . ARG   B 10  ? 0.1212 0.1304 0.1828 0.0017  0.0030  0.0232  16  ARG   C CA  
1168 C C   . ARG   B 10  ? 0.1247 0.1334 0.1819 0.0022  0.0030  0.0211  16  ARG   C C   
1169 O O   . ARG   B 10  ? 0.1221 0.1308 0.1826 0.0027  0.0051  0.0210  16  ARG   C O   
1170 C CB  . ARG   B 10  ? 0.1293 0.1414 0.1991 0.0009  0.0010  0.0262  16  ARG   C CB  
1171 C CG  . ARG   B 10  ? 0.1376 0.1513 0.2052 0.0003  -0.0031 0.0265  16  ARG   C CG  
1172 C CD  . ARG   B 10  ? 0.1497 0.1662 0.2247 -0.0005 -0.0056 0.0298  16  ARG   C CD  
1173 N NE  . ARG   B 10  ? 0.1525 0.1706 0.2278 -0.0004 -0.0074 0.0309  16  ARG   C NE  
1174 C CZ  . ARG   B 10  ? 0.1638 0.1828 0.2349 -0.0009 -0.0111 0.0311  16  ARG   C CZ  
1175 N NH1 . ARG   B 10  ? 0.1725 0.1907 0.2383 -0.0017 -0.0136 0.0299  16  ARG   C NH1 
1176 N NH2 . ARG   B 10  ? 0.1796 0.1999 0.2512 -0.0007 -0.0121 0.0327  16  ARG   C NH2 
1177 N N   . VAL   B 11  ? 0.1342 0.1423 0.1845 0.0022  0.0010  0.0193  17  VAL   C N   
1178 C CA  . VAL   B 11  ? 0.1172 0.1252 0.1639 0.0025  0.0008  0.0173  17  VAL   C CA  
1179 C C   . VAL   B 11  ? 0.1189 0.1288 0.1655 0.0019  -0.0023 0.0183  17  VAL   C C   
1180 O O   . VAL   B 11  ? 0.1326 0.1428 0.1761 0.0015  -0.0047 0.0185  17  VAL   C O   
1181 C CB  . VAL   B 11  ? 0.1273 0.1334 0.1665 0.0031  0.0009  0.0147  17  VAL   C CB  
1182 C CG1 . VAL   B 11  ? 0.1560 0.1621 0.1929 0.0034  0.0008  0.0126  17  VAL   C CG1 
1183 C CG2 . VAL   B 11  ? 0.1545 0.1585 0.1923 0.0037  0.0037  0.0141  17  VAL   C CG2 
1184 N N   . VAL   B 12  ? 0.1129 0.1239 0.1625 0.0020  -0.0020 0.0189  18  VAL   C N   
1185 C CA  A VAL   B 12  ? 0.1073 0.1201 0.1565 0.0016  -0.0046 0.0203  18  VAL   C CA  
1186 C CA  B VAL   B 12  ? 0.1258 0.1386 0.1751 0.0016  -0.0046 0.0203  18  VAL   C CA  
1187 C C   . VAL   B 12  ? 0.1154 0.1282 0.1641 0.0019  -0.0037 0.0193  18  VAL   C C   
1188 O O   . VAL   B 12  ? 0.1177 0.1294 0.1680 0.0023  -0.0014 0.0177  18  VAL   C O   
1189 C CB  A VAL   B 12  ? 0.1038 0.1185 0.1592 0.0012  -0.0056 0.0237  18  VAL   C CB  
1190 C CB  B VAL   B 12  ? 0.1605 0.1751 0.2165 0.0012  -0.0053 0.0237  18  VAL   C CB  
1191 C CG1 A VAL   B 12  ? 0.1275 0.1427 0.1835 0.0005  -0.0077 0.0249  18  VAL   C CG1 
1192 C CG1 B VAL   B 12  ? 0.1612 0.1776 0.2163 0.0009  -0.0081 0.0256  18  VAL   C CG1 
1193 C CG2 A VAL   B 12  ? 0.0657 0.0804 0.1282 0.0016  -0.0029 0.0247  18  VAL   C CG2 
1194 C CG2 B VAL   B 12  ? 0.1933 0.2079 0.2516 0.0007  -0.0059 0.0247  18  VAL   C CG2 
1195 N N   . ASN   B 13  ? 0.1041 0.1183 0.1511 0.0018  -0.0054 0.0202  19  ASN   C N   
1196 C CA  . ASN   B 13  ? 0.1081 0.1227 0.1563 0.0020  -0.0043 0.0200  19  ASN   C CA  
1197 C C   . ASN   B 13  ? 0.1140 0.1290 0.1696 0.0020  -0.0028 0.0220  19  ASN   C C   
1198 O O   . ASN   B 13  ? 0.1094 0.1256 0.1682 0.0019  -0.0038 0.0249  19  ASN   C O   
1199 C CB  . ASN   B 13  ? 0.1289 0.1449 0.1743 0.0019  -0.0060 0.0214  19  ASN   C CB  
1200 C CG  . ASN   B 13  ? 0.1236 0.1391 0.1624 0.0021  -0.0072 0.0195  19  ASN   C CG  
1201 O OD1 . ASN   B 13  ? 0.1454 0.1606 0.1809 0.0019  -0.0090 0.0197  19  ASN   C OD1 
1202 N ND2 . ASN   B 13  ? 0.1377 0.1529 0.1750 0.0024  -0.0063 0.0174  19  ASN   C ND2 
1203 N N   . ARG   B 14  ? 0.1102 0.1242 0.1687 0.0022  -0.0006 0.0206  20  ARG   C N   
1204 C CA  . ARG   B 14  ? 0.1112 0.1251 0.1771 0.0023  0.0012  0.0224  20  ARG   C CA  
1205 C C   . ARG   B 14  ? 0.1245 0.1404 0.1934 0.0023  0.0001  0.0263  20  ARG   C C   
1206 O O   . ARG   B 14  ? 0.1251 0.1418 0.1995 0.0025  0.0002  0.0292  20  ARG   C O   
1207 C CB  . ARG   B 14  ? 0.1100 0.1222 0.1781 0.0024  0.0035  0.0197  20  ARG   C CB  
1208 C CG  . ARG   B 14  ? 0.1110 0.1223 0.1871 0.0027  0.0059  0.0210  20  ARG   C CG  
1209 C CD  . ARG   B 14  ? 0.1276 0.1369 0.2053 0.0025  0.0078  0.0179  20  ARG   C CD  
1210 N NE  . ARG   B 14  ? 0.1320 0.1395 0.2171 0.0029  0.0106  0.0180  20  ARG   C NE  
1211 C CZ  . ARG   B 14  ? 0.1444 0.1525 0.2365 0.0029  0.0114  0.0208  20  ARG   C CZ  
1212 N NH1 . ARG   B 14  ? 0.1498 0.1602 0.2421 0.0027  0.0097  0.0242  20  ARG   C NH1 
1213 N NH2 . ARG   B 14  ? 0.1325 0.1384 0.2311 0.0033  0.0142  0.0203  20  ARG   C NH2 
1214 N N   . HIS   B 15  ? 0.1171 0.1341 0.1822 0.0022  -0.0012 0.0267  21  HIS   C N   
1215 C CA  . HIS   B 15  ? 0.1194 0.1381 0.1862 0.0023  -0.0021 0.0307  21  HIS   C CA  
1216 C C   . HIS   B 15  ? 0.1329 0.1530 0.1978 0.0022  -0.0049 0.0334  21  HIS   C C   
1217 O O   . HIS   B 15  ? 0.1573 0.1788 0.2239 0.0024  -0.0060 0.0371  21  HIS   C O   
1218 C CB  . HIS   B 15  ? 0.1372 0.1564 0.2006 0.0023  -0.0019 0.0306  21  HIS   C CB  
1219 C CG  . HIS   B 15  ? 0.1338 0.1533 0.1892 0.0023  -0.0038 0.0294  21  HIS   C CG  
1220 N ND1 . HIS   B 15  ? 0.1586 0.1772 0.2102 0.0023  -0.0037 0.0257  21  HIS   C ND1 
1221 C CD2 . HIS   B 15  ? 0.1425 0.1630 0.1930 0.0025  -0.0057 0.0314  21  HIS   C CD2 
1222 C CE1 . HIS   B 15  ? 0.1809 0.1998 0.2262 0.0024  -0.0052 0.0255  21  HIS   C CE1 
1223 N NE2 . HIS   B 15  ? 0.1569 0.1769 0.2010 0.0026  -0.0064 0.0287  21  HIS   C NE2 
1224 N N   . LEU   B 16  ? 0.1250 0.1447 0.1867 0.0019  -0.0063 0.0316  22  LEU   C N   
1225 C CA  . LEU   B 16  ? 0.1393 0.1602 0.2000 0.0016  -0.0093 0.0337  22  LEU   C CA  
1226 C C   . LEU   B 16  ? 0.1473 0.1683 0.2144 0.0015  -0.0089 0.0345  22  LEU   C C   
1227 O O   . LEU   B 16  ? 0.1686 0.1906 0.2359 0.0010  -0.0115 0.0358  22  LEU   C O   
1228 C CB  . LEU   B 16  ? 0.1405 0.1608 0.1934 0.0013  -0.0112 0.0314  22  LEU   C CB  
1229 C CG  . LEU   B 16  ? 0.1548 0.1751 0.2015 0.0016  -0.0115 0.0310  22  LEU   C CG  
1230 C CD1 . LEU   B 16  ? 0.1710 0.1902 0.2103 0.0014  -0.0131 0.0285  22  LEU   C CD1 
1231 C CD2 . LEU   B 16  ? 0.1613 0.1831 0.2078 0.0018  -0.0128 0.0347  22  LEU   C CD2 
1232 N N   . ALA   B 17  ? 0.1442 0.1641 0.2164 0.0018  -0.0057 0.0333  23  ALA   C N   
1233 C CA  . ALA   B 17  ? 0.1385 0.1583 0.2167 0.0019  -0.0046 0.0340  23  ALA   C CA  
1234 C C   . ALA   B 17  ? 0.1523 0.1744 0.2374 0.0020  -0.0062 0.0384  23  ALA   C C   
1235 O O   . ALA   B 17  ? 0.1621 0.1852 0.2494 0.0023  -0.0065 0.0409  23  ALA   C O   
1236 C CB  . ALA   B 17  ? 0.1519 0.1696 0.2335 0.0025  -0.0005 0.0319  23  ALA   C CB  
1237 N N   . THR   B 18  ? 0.1434 0.1665 0.2324 0.0017  -0.0072 0.0395  24  THR   C N   
1238 C CA  . THR   B 18  ? 0.1447 0.1704 0.2411 0.0017  -0.0092 0.0438  24  THR   C CA  
1239 C C   . THR   B 18  ? 0.1488 0.1743 0.2552 0.0026  -0.0056 0.0451  24  THR   C C   
1240 O O   . THR   B 18  ? 0.1477 0.1708 0.2546 0.0031  -0.0015 0.0423  24  THR   C O   
1241 C CB  . THR   B 18  ? 0.1631 0.1901 0.2595 0.0007  -0.0126 0.0443  24  THR   C CB  
1242 O OG1 . THR   B 18  ? 0.1701 0.1959 0.2695 0.0008  -0.0097 0.0425  24  THR   C OG1 
1243 C CG2 . THR   B 18  ? 0.1883 0.2150 0.2748 -0.0001 -0.0161 0.0426  24  THR   C CG2 
1244 N N   . HIS   B 19  ? 0.1518 0.1799 0.2667 0.0029  -0.0071 0.0495  25  HIS   C N   
1245 C CA  . HIS   B 19  ? 0.1573 0.1854 0.2828 0.0038  -0.0036 0.0509  25  HIS   C CA  
1246 C C   . HIS   B 19  ? 0.1394 0.1665 0.2668 0.0037  -0.0012 0.0489  25  HIS   C C   
1247 O O   . HIS   B 19  ? 0.1508 0.1758 0.2815 0.0046  0.0035  0.0472  25  HIS   C O   
1248 C CB  . HIS   B 19  ? 0.1625 0.1940 0.2970 0.0041  -0.0065 0.0564  25  HIS   C CB  
1249 C CG  . HIS   B 19  ? 0.1937 0.2258 0.3404 0.0051  -0.0032 0.0582  25  HIS   C CG  
1250 N ND1 . HIS   B 19  ? 0.2203 0.2505 0.3725 0.0063  0.0013  0.0583  25  HIS   C ND1 
1251 C CD2 . HIS   B 19  ? 0.2179 0.2516 0.3717 0.0049  -0.0032 0.0594  25  HIS   C CD2 
1252 C CE1 . HIS   B 19  ? 0.2190 0.2501 0.3819 0.0071  0.0037  0.0600  25  HIS   C CE1 
1253 N NE2 . HIS   B 19  ? 0.2151 0.2484 0.3793 0.0063  0.0013  0.0607  25  HIS   C NE2 
1254 N N   . ASN   B 20  ? 0.1453 0.1737 0.2702 0.0026  -0.0043 0.0487  26  ASN   C N   
1255 C CA  . ASN   B 20  ? 0.1596 0.1870 0.2867 0.0026  -0.0016 0.0471  26  ASN   C CA  
1256 C C   . ASN   B 20  ? 0.1471 0.1707 0.2665 0.0030  0.0024  0.0426  26  ASN   C C   
1257 O O   . ASN   B 20  ? 0.1511 0.1730 0.2733 0.0037  0.0068  0.0413  26  ASN   C O   
1258 C CB  . ASN   B 20  ? 0.1716 0.2006 0.2975 0.0012  -0.0056 0.0477  26  ASN   C CB  
1259 C CG  . ASN   B 20  ? 0.2596 0.2879 0.3897 0.0012  -0.0024 0.0469  26  ASN   C CG  
1260 O OD1 . ASN   B 20  ? 0.2912 0.3210 0.4318 0.0017  -0.0004 0.0494  26  ASN   C OD1 
1261 N ND2 . ASN   B 20  ? 0.3000 0.3259 0.4222 0.0007  -0.0015 0.0437  26  ASN   C ND2 
1262 N N   . ASP   B 21  ? 0.1317 0.1540 0.2415 0.0026  0.0010  0.0401  27  ASP   C N   
1263 C CA  . ASP   B 21  ? 0.1422 0.1612 0.2450 0.0030  0.0041  0.0359  27  ASP   C CA  
1264 C C   . ASP   B 21  ? 0.1349 0.1519 0.2417 0.0042  0.0086  0.0349  27  ASP   C C   
1265 O O   . ASP   B 21  ? 0.1396 0.1541 0.2452 0.0048  0.0125  0.0324  27  ASP   C O   
1266 C CB  . ASP   B 21  ? 0.1439 0.1623 0.2374 0.0025  0.0016  0.0340  27  ASP   C CB  
1267 C CG  . ASP   B 21  ? 0.1506 0.1695 0.2378 0.0016  -0.0019 0.0335  27  ASP   C CG  
1268 O OD1 . ASP   B 21  ? 0.1631 0.1815 0.2502 0.0013  -0.0014 0.0328  27  ASP   C OD1 
1269 O OD2 . ASP   B 21  ? 0.1417 0.1615 0.2243 0.0011  -0.0051 0.0338  27  ASP   C OD2 
1270 N N   . TRP   B 22  ? 0.1297 0.1476 0.2413 0.0045  0.0083  0.0370  28  TRP   C N   
1271 C CA  . TRP   B 22  ? 0.1381 0.1539 0.2544 0.0055  0.0125  0.0360  28  TRP   C CA  
1272 C C   . TRP   B 22  ? 0.1396 0.1551 0.2647 0.0065  0.0162  0.0373  28  TRP   C C   
1273 O O   . TRP   B 22  ? 0.1538 0.1663 0.2798 0.0074  0.0207  0.0347  28  TRP   C O   
1274 C CB  . TRP   B 22  ? 0.1327 0.1495 0.2528 0.0057  0.0114  0.0385  28  TRP   C CB  
1275 C CG  . TRP   B 22  ? 0.1293 0.1451 0.2417 0.0051  0.0101  0.0362  28  TRP   C CG  
1276 C CD1 . TRP   B 22  ? 0.1346 0.1523 0.2420 0.0044  0.0062  0.0376  28  TRP   C CD1 
1277 C CD2 . TRP   B 22  ? 0.1177 0.1303 0.2269 0.0053  0.0127  0.0322  28  TRP   C CD2 
1278 N NE1 . TRP   B 22  ? 0.1378 0.1540 0.2398 0.0042  0.0066  0.0350  28  TRP   C NE1 
1279 C CE2 . TRP   B 22  ? 0.1298 0.1430 0.2334 0.0046  0.0103  0.0318  28  TRP   C CE2 
1280 C CE3 . TRP   B 22  ? 0.1489 0.1583 0.2600 0.0059  0.0168  0.0291  28  TRP   C CE3 
1281 C CZ2 . TRP   B 22  ? 0.1373 0.1483 0.2381 0.0044  0.0116  0.0285  28  TRP   C CZ2 
1282 C CZ3 . TRP   B 22  ? 0.1598 0.1667 0.2669 0.0057  0.0178  0.0253  28  TRP   C CZ3 
1283 C CH2 . TRP   B 22  ? 0.1554 0.1633 0.2581 0.0049  0.0151  0.0252  28  TRP   C CH2 
1284 N N   . ALA   B 23  ? 0.1240 0.1426 0.2553 0.0063  0.0143  0.0410  29  ALA   C N   
1285 C CA  . ALA   B 23  ? 0.1393 0.1582 0.2802 0.0072  0.0178  0.0426  29  ALA   C CA  
1286 C C   . ALA   B 23  ? 0.1646 0.1814 0.3016 0.0074  0.0210  0.0399  29  ALA   C C   
1287 O O   . ALA   B 23  ? 0.1810 0.1974 0.3249 0.0084  0.0253  0.0406  29  ALA   C O   
1288 C CB  . ALA   B 23  ? 0.1488 0.1721 0.2984 0.0068  0.0142  0.0476  29  ALA   C CB  
1289 N N   . ASN   B 24  ? 0.1599 0.1756 0.2862 0.0065  0.0192  0.0371  30  ASN   C N   
1290 C CA  . ASN   B 24  ? 0.1512 0.1648 0.2726 0.0067  0.0220  0.0347  30  ASN   C CA  
1291 C C   . ASN   B 24  ? 0.1433 0.1535 0.2529 0.0067  0.0227  0.0301  30  ASN   C C   
1292 O O   . ASN   B 24  ? 0.1494 0.1584 0.2513 0.0063  0.0221  0.0283  30  ASN   C O   
1293 C CB  . ASN   B 24  ? 0.1588 0.1748 0.2797 0.0054  0.0184  0.0366  30  ASN   C CB  
1294 C CG  . ASN   B 24  ? 0.1768 0.1960 0.3100 0.0053  0.0180  0.0408  30  ASN   C CG  
1295 O OD1 . ASN   B 24  ? 0.2134 0.2322 0.3528 0.0062  0.0225  0.0416  30  ASN   C OD1 
1296 N ND2 . ASN   B 24  ? 0.1971 0.2196 0.3343 0.0045  0.0131  0.0437  30  ASN   C ND2 
1297 N N   . LEU   B 25  ? 0.1546 0.1631 0.2635 0.0072  0.0239  0.0283  31  LEU   C N   
1298 C CA  . LEU   B 25  ? 0.1480 0.1538 0.2471 0.0071  0.0236  0.0242  31  LEU   C CA  
1299 C C   . LEU   B 25  ? 0.1654 0.1676 0.2580 0.0078  0.0273  0.0206  31  LEU   C C   
1300 O O   . LEU   B 25  ? 0.1824 0.1827 0.2786 0.0090  0.0319  0.0202  31  LEU   C O   
1301 C CB  . LEU   B 25  ? 0.1556 0.1605 0.2578 0.0073  0.0242  0.0234  31  LEU   C CB  
1302 C CG  . LEU   B 25  ? 0.1627 0.1654 0.2565 0.0069  0.0233  0.0194  31  LEU   C CG  
1303 C CD1 . LEU   B 25  ? 0.1696 0.1747 0.2581 0.0058  0.0185  0.0201  31  LEU   C CD1 
1304 C CD2 . LEU   B 25  ? 0.1900 0.1913 0.2884 0.0072  0.0248  0.0184  31  LEU   C CD2 
1305 N N   . VAL   B 26  ? 0.1544 0.1557 0.2371 0.0074  0.0253  0.0181  32  VAL   C N   
1306 C CA  . VAL   B 26  ? 0.1692 0.1670 0.2441 0.0081  0.0282  0.0146  32  VAL   C CA  
1307 C C   . VAL   B 26  ? 0.1760 0.1717 0.2451 0.0080  0.0274  0.0107  32  VAL   C C   
1308 O O   . VAL   B 26  ? 0.1900 0.1823 0.2565 0.0089  0.0306  0.0075  32  VAL   C O   
1309 C CB  . VAL   B 26  ? 0.1816 0.1798 0.2497 0.0078  0.0264  0.0149  32  VAL   C CB  
1310 C CG1 . VAL   B 26  ? 0.1978 0.1924 0.2561 0.0086  0.0285  0.0114  32  VAL   C CG1 
1311 C CG2 . VAL   B 26  ? 0.1969 0.1968 0.2713 0.0078  0.0275  0.0186  32  VAL   C CG2 
1312 N N   . TRP   B 27  ? 0.1604 0.1579 0.2276 0.0070  0.0231  0.0107  33  TRP   C N   
1313 C CA  . TRP   B 27  ? 0.1555 0.1515 0.2179 0.0067  0.0219  0.0071  33  TRP   C CA  
1314 C C   . TRP   B 27  ? 0.1564 0.1553 0.2206 0.0057  0.0180  0.0087  33  TRP   C C   
1315 O O   . TRP   B 27  ? 0.1552 0.1566 0.2195 0.0052  0.0155  0.0114  33  TRP   C O   
1316 C CB  . TRP   B 27  ? 0.1689 0.1630 0.2209 0.0069  0.0213  0.0041  33  TRP   C CB  
1317 C CG  . TRP   B 27  ? 0.1840 0.1774 0.2310 0.0064  0.0189  0.0007  33  TRP   C CG  
1318 C CD1 . TRP   B 27  ? 0.2140 0.2046 0.2595 0.0065  0.0200  -0.0031 33  TRP   C CD1 
1319 C CD2 . TRP   B 27  ? 0.1703 0.1659 0.2141 0.0057  0.0149  0.0009  33  TRP   C CD2 
1320 N NE1 . TRP   B 27  ? 0.2168 0.2081 0.2587 0.0058  0.0166  -0.0052 33  TRP   C NE1 
1321 C CE2 . TRP   B 27  ? 0.1909 0.1853 0.2317 0.0054  0.0137  -0.0027 33  TRP   C CE2 
1322 C CE3 . TRP   B 27  ? 0.1718 0.1701 0.2150 0.0052  0.0122  0.0036  33  TRP   C CE3 
1323 C CZ2 . TRP   B 27  ? 0.1865 0.1826 0.2243 0.0048  0.0102  -0.0033 33  TRP   C CZ2 
1324 C CZ3 . TRP   B 27  ? 0.1724 0.1720 0.2118 0.0048  0.0090  0.0026  33  TRP   C CZ3 
1325 C CH2 . TRP   B 27  ? 0.1788 0.1775 0.2161 0.0046  0.0081  -0.0005 33  TRP   C CH2 
1326 N N   . GLU   B 28  ? 0.1421 0.1404 0.2081 0.0053  0.0176  0.0071  34  GLU   C N   
1327 C CA  . GLU   B 28  ? 0.1489 0.1498 0.2160 0.0044  0.0144  0.0086  34  GLU   C CA  
1328 C C   . GLU   B 28  ? 0.1577 0.1572 0.2230 0.0040  0.0139  0.0052  34  GLU   C C   
1329 O O   . GLU   B 28  ? 0.1622 0.1589 0.2286 0.0042  0.0162  0.0024  34  GLU   C O   
1330 C CB  . GLU   B 28  ? 0.1629 0.1659 0.2386 0.0044  0.0145  0.0127  34  GLU   C CB  
1331 C CG  . GLU   B 28  ? 0.1627 0.1638 0.2457 0.0049  0.0177  0.0126  34  GLU   C CG  
1332 C CD  . GLU   B 28  ? 0.1908 0.1908 0.2765 0.0044  0.0179  0.0109  34  GLU   C CD  
1333 O OE1 . GLU   B 28  ? 0.2270 0.2241 0.3165 0.0048  0.0209  0.0090  34  GLU   C OE1 
1334 O OE2 . GLU   B 28  ? 0.1713 0.1730 0.2553 0.0037  0.0154  0.0114  34  GLU   C OE2 
1335 N N   . ASP   B 29  ? 0.1512 0.1527 0.2144 0.0033  0.0110  0.0055  35  ASP   C N   
1336 C CA  . ASP   B 29  ? 0.1507 0.1516 0.2136 0.0027  0.0102  0.0027  35  ASP   C CA  
1337 C C   . ASP   B 29  ? 0.1449 0.1487 0.2104 0.0021  0.0082  0.0052  35  ASP   C C   
1338 O O   . ASP   B 29  ? 0.1456 0.1513 0.2068 0.0021  0.0061  0.0063  35  ASP   C O   
1339 C CB  . ASP   B 29  ? 0.1646 0.1642 0.2194 0.0028  0.0089  -0.0010 35  ASP   C CB  
1340 C CG  . ASP   B 29  ? 0.2253 0.2243 0.2797 0.0021  0.0076  -0.0043 35  ASP   C CG  
1341 O OD1 . ASP   B 29  ? 0.2344 0.2353 0.2932 0.0014  0.0065  -0.0031 35  ASP   C OD1 
1342 O OD2 . ASP   B 29  ? 0.2589 0.2557 0.3083 0.0023  0.0073  -0.0080 35  ASP   C OD2 
1343 N N   . SER   B 30  ? 0.1381 0.1420 0.2105 0.0018  0.0092  0.0065  36  SER   C N   
1344 C CA  A SER   B 30  ? 0.1335 0.1399 0.2086 0.0013  0.0079  0.0093  36  SER   C CA  
1345 C CA  B SER   B 30  ? 0.1415 0.1480 0.2164 0.0013  0.0079  0.0093  36  SER   C CA  
1346 C C   . SER   B 30  ? 0.1436 0.1510 0.2151 0.0008  0.0060  0.0071  36  SER   C C   
1347 O O   . SER   B 30  ? 0.1294 0.1392 0.1991 0.0008  0.0046  0.0093  36  SER   C O   
1348 C CB  A SER   B 30  ? 0.1402 0.1461 0.2239 0.0011  0.0098  0.0108  36  SER   C CB  
1349 C CB  B SER   B 30  ? 0.1693 0.1755 0.2526 0.0012  0.0096  0.0115  36  SER   C CB  
1350 O OG  A SER   B 30  ? 0.1239 0.1319 0.2100 0.0006  0.0090  0.0133  36  SER   C OG  
1351 O OG  B SER   B 30  ? 0.1897 0.1933 0.2761 0.0007  0.0110  0.0078  36  SER   C OG  
1352 N N   . SER   B 31  ? 0.1420 0.1475 0.2123 0.0004  0.0059  0.0028  37  SER   C N   
1353 C CA  . SER   B 31  ? 0.1366 0.1434 0.2045 -0.0001 0.0039  0.0010  37  SER   C CA  
1354 C C   . SER   B 31  ? 0.1339 0.1421 0.1946 0.0005  0.0020  0.0012  37  SER   C C   
1355 O O   . SER   B 31  ? 0.1431 0.1533 0.2029 0.0003  0.0004  0.0012  37  SER   C O   
1356 C CB  . SER   B 31  ? 0.1826 0.1871 0.2505 -0.0006 0.0035  -0.0038 37  SER   C CB  
1357 O OG  . SER   B 31  ? 0.2534 0.2560 0.3142 -0.0001 0.0030  -0.0065 37  SER   C OG  
1358 N N   . ARG   B 32  ? 0.1245 0.1319 0.1807 0.0012  0.0022  0.0017  38  ARG   C N   
1359 C CA  . ARG   B 32  ? 0.1207 0.1290 0.1704 0.0017  0.0005  0.0022  38  ARG   C CA  
1360 C C   . ARG   B 32  ? 0.1145 0.1246 0.1643 0.0019  0.0003  0.0060  38  ARG   C C   
1361 O O   . ARG   B 32  ? 0.1274 0.1382 0.1724 0.0023  -0.0010 0.0065  38  ARG   C O   
1362 C CB  . ARG   B 32  ? 0.1490 0.1551 0.1935 0.0023  0.0010  0.0003  38  ARG   C CB  
1363 C CG  . ARG   B 32  ? 0.1615 0.1658 0.2036 0.0022  0.0006  -0.0037 38  ARG   C CG  
1364 C CD  . ARG   B 32  ? 0.1440 0.1457 0.1802 0.0030  0.0015  -0.0054 38  ARG   C CD  
1365 N NE  . ARG   B 32  ? 0.1375 0.1400 0.1679 0.0036  0.0001  -0.0043 38  ARG   C NE  
1366 C CZ  . ARG   B 32  ? 0.1542 0.1550 0.1780 0.0043  -0.0002 -0.0060 38  ARG   C CZ  
1367 N NH1 . ARG   B 32  ? 0.1618 0.1599 0.1829 0.0046  0.0008  -0.0088 38  ARG   C NH1 
1368 N NH2 . ARG   B 32  ? 0.1532 0.1547 0.1727 0.0049  -0.0016 -0.0047 38  ARG   C NH2 
1369 N N   . ASP   B 33  ? 0.1138 0.1244 0.1689 0.0018  0.0015  0.0087  39  ASP   C N   
1370 C CA  . ASP   B 33  ? 0.1168 0.1288 0.1718 0.0019  0.0010  0.0123  39  ASP   C CA  
1371 C C   . ASP   B 33  ? 0.1161 0.1273 0.1679 0.0023  0.0006  0.0124  39  ASP   C C   
1372 O O   . ASP   B 33  ? 0.1193 0.1316 0.1683 0.0023  -0.0009 0.0141  39  ASP   C O   
1373 C CB  . ASP   B 33  ? 0.1170 0.1311 0.1695 0.0020  -0.0005 0.0137  39  ASP   C CB  
1374 C CG  . ASP   B 33  ? 0.1447 0.1600 0.1965 0.0021  -0.0013 0.0172  39  ASP   C CG  
1375 O OD1 . ASP   B 33  ? 0.1432 0.1587 0.1997 0.0020  -0.0007 0.0197  39  ASP   C OD1 
1376 O OD2 . ASP   B 33  ? 0.1298 0.1458 0.1767 0.0023  -0.0028 0.0176  39  ASP   C OD2 
1377 N N   . LEU   B 34  ? 0.1143 0.1236 0.1667 0.0025  0.0022  0.0107  40  LEU   C N   
1378 C CA  . LEU   B 34  ? 0.1307 0.1392 0.1807 0.0028  0.0025  0.0111  40  LEU   C CA  
1379 C C   . LEU   B 34  ? 0.1304 0.1382 0.1860 0.0030  0.0047  0.0124  40  LEU   C C   
1380 O O   . LEU   B 34  ? 0.1228 0.1293 0.1822 0.0031  0.0067  0.0113  40  LEU   C O   
1381 C CB  . LEU   B 34  ? 0.1407 0.1473 0.1848 0.0032  0.0026  0.0080  40  LEU   C CB  
1382 C CG  . LEU   B 34  ? 0.1393 0.1466 0.1777 0.0033  0.0003  0.0070  40  LEU   C CG  
1383 C CD1 . LEU   B 34  ? 0.1577 0.1630 0.1906 0.0038  0.0006  0.0044  40  LEU   C CD1 
1384 C CD2 . LEU   B 34  ? 0.1521 0.1607 0.1891 0.0032  -0.0012 0.0094  40  LEU   C CD2 
1385 N N   . LEU   B 35  ? 0.1228 0.1313 0.1794 0.0031  0.0045  0.0146  41  LEU   C N   
1386 C CA  . LEU   B 35  ? 0.1234 0.1313 0.1855 0.0034  0.0068  0.0160  41  LEU   C CA  
1387 C C   . LEU   B 35  ? 0.1220 0.1297 0.1819 0.0035  0.0068  0.0165  41  LEU   C C   
1388 O O   . LEU   B 35  ? 0.1344 0.1432 0.1913 0.0031  0.0042  0.0175  41  LEU   C O   
1389 C CB  . LEU   B 35  ? 0.1212 0.1312 0.1904 0.0032  0.0061  0.0197  41  LEU   C CB  
1390 C CG  . LEU   B 35  ? 0.1175 0.1274 0.1941 0.0037  0.0085  0.0216  41  LEU   C CG  
1391 C CD1 . LEU   B 35  ? 0.1490 0.1599 0.2330 0.0038  0.0089  0.0241  41  LEU   C CD1 
1392 C CD2 . LEU   B 35  ? 0.1266 0.1382 0.2047 0.0034  0.0070  0.0241  41  LEU   C CD2 
1393 N N   . VAL   B 36  ? 0.1268 0.1326 0.1880 0.0041  0.0099  0.0158  42  VAL   C N   
1394 C CA  . VAL   B 36  ? 0.1289 0.1343 0.1895 0.0043  0.0109  0.0166  42  VAL   C CA  
1395 C C   . VAL   B 36  ? 0.1221 0.1281 0.1913 0.0046  0.0132  0.0192  42  VAL   C C   
1396 O O   . VAL   B 36  ? 0.1303 0.1351 0.2031 0.0053  0.0163  0.0185  42  VAL   C O   
1397 C CB  . VAL   B 36  ? 0.1358 0.1383 0.1894 0.0050  0.0129  0.0136  42  VAL   C CB  
1398 C CG1 . VAL   B 36  ? 0.1558 0.1578 0.2090 0.0053  0.0143  0.0150  42  VAL   C CG1 
1399 C CG2 . VAL   B 36  ? 0.1497 0.1521 0.1959 0.0048  0.0101  0.0114  42  VAL   C CG2 
1400 N N   . SER   B 37  ? 0.1149 0.1228 0.1877 0.0041  0.0118  0.0220  43  SER   C N   
1401 C CA  . SER   B 37  ? 0.1251 0.1342 0.2071 0.0044  0.0138  0.0248  43  SER   C CA  
1402 C C   . SER   B 37  ? 0.1384 0.1469 0.2204 0.0044  0.0155  0.0254  43  SER   C C   
1403 O O   . SER   B 37  ? 0.1364 0.1440 0.2117 0.0041  0.0141  0.0243  43  SER   C O   
1404 C CB  . SER   B 37  ? 0.1471 0.1595 0.2353 0.0036  0.0103  0.0282  43  SER   C CB  
1405 O OG  . SER   B 37  ? 0.1416 0.1555 0.2266 0.0025  0.0062  0.0289  43  SER   C OG  
1406 N N   . SER   B 38  ? 0.1362 0.1451 0.2263 0.0049  0.0186  0.0275  44  SER   C N   
1407 C CA  . SER   B 38  ? 0.1590 0.1675 0.2505 0.0050  0.0207  0.0286  44  SER   C CA  
1408 C C   . SER   B 38  ? 0.1778 0.1895 0.2759 0.0037  0.0170  0.0319  44  SER   C C   
1409 O O   . SER   B 38  ? 0.1883 0.2028 0.2927 0.0031  0.0141  0.0340  44  SER   C O   
1410 C CB  . SER   B 38  ? 0.1859 0.1930 0.2827 0.0064  0.0266  0.0290  44  SER   C CB  
1411 O OG  . SER   B 38  ? 0.2289 0.2384 0.3363 0.0065  0.0266  0.0315  44  SER   C OG  
1412 N N   . THR   B 39  ? 0.1785 0.1898 0.2754 0.0031  0.0170  0.0324  45  THR   C N   
1413 C CA  . THR   B 39  ? 0.1850 0.1989 0.2879 0.0016  0.0133  0.0349  45  THR   C CA  
1414 C C   . THR   B 39  ? 0.2050 0.2192 0.3160 0.0018  0.0170  0.0373  45  THR   C C   
1415 O O   . THR   B 39  ? 0.2083 0.2199 0.3164 0.0029  0.0220  0.0365  45  THR   C O   
1416 C CB  . THR   B 39  ? 0.1943 0.2072 0.2888 0.0006  0.0096  0.0333  45  THR   C CB  
1417 O OG1 . THR   B 39  ? 0.2115 0.2215 0.3005 0.0013  0.0128  0.0321  45  THR   C OG1 
1418 C CG2 . THR   B 39  ? 0.1998 0.2124 0.2862 0.0005  0.0062  0.0311  45  THR   C CG2 
1419 N N   . THR   B 40  ? 0.2236 0.2409 0.3441 0.0005  0.0140  0.0402  46  THR   C N   
1420 C CA  . THR   B 40  ? 0.2481 0.2662 0.3778 0.0003  0.0170  0.0428  46  THR   C CA  
1421 C C   . THR   B 40  ? 0.2480 0.2642 0.3728 -0.0006 0.0164  0.0421  46  THR   C C   
1422 O O   . THR   B 40  ? 0.2701 0.2845 0.3953 0.0002  0.0214  0.0427  46  THR   C O   
1423 C CB  . THR   B 40  ? 0.2985 0.3210 0.4412 -0.0008 0.0137  0.0462  46  THR   C CB  
1424 O OG1 . THR   B 40  ? 0.3539 0.3779 0.4942 -0.0027 0.0066  0.0460  46  THR   C OG1 
1425 C CG2 . THR   B 40  ? 0.2904 0.3144 0.4381 0.0003  0.0146  0.0472  46  THR   C CG2 
1426 N N   . ALA   B 41  ? 0.2244 0.2407 0.3438 -0.0020 0.0108  0.0408  47  ALA   C N   
1427 C CA  . ALA   B 41  ? 0.2320 0.2463 0.3471 -0.0028 0.0100  0.0401  47  ALA   C CA  
1428 C C   . ALA   B 41  ? 0.2164 0.2271 0.3182 -0.0017 0.0115  0.0371  47  ALA   C C   
1429 O O   . ALA   B 41  ? 0.2231 0.2333 0.3183 -0.0009 0.0107  0.0350  47  ALA   C O   
1430 C CB  . ALA   B 41  ? 0.2514 0.2673 0.3680 -0.0049 0.0032  0.0402  47  ALA   C CB  
1431 N N   . GLN   B 42  ? 0.2018 0.2100 0.3002 -0.0016 0.0134  0.0370  48  GLN   C N   
1432 C CA  . GLN   B 42  ? 0.2109 0.2159 0.2972 -0.0005 0.0145  0.0345  48  GLN   C CA  
1433 C C   . GLN   B 42  ? 0.2040 0.2086 0.2843 -0.0015 0.0089  0.0325  48  GLN   C C   
1434 O O   . GLN   B 42  ? 0.2157 0.2213 0.3003 -0.0031 0.0053  0.0332  48  GLN   C O   
1435 C CB  . GLN   B 42  ? 0.2715 0.2738 0.3565 0.0001  0.0187  0.0356  48  GLN   C CB  
1436 C CG  . GLN   B 42  ? 0.3944 0.3959 0.4814 0.0018  0.0253  0.0369  48  GLN   C CG  
1437 C CD  . GLN   B 42  ? 0.5251 0.5237 0.6090 0.0026  0.0294  0.0382  48  GLN   C CD  
1438 O OE1 . GLN   B 42  ? 0.5792 0.5781 0.6700 0.0016  0.0298  0.0407  48  GLN   C OE1 
1439 N NE2 . GLN   B 42  ? 0.5660 0.5617 0.6393 0.0044  0.0324  0.0366  48  GLN   C NE2 
1440 N N   . GLY   B 43  ? 0.1852 0.1885 0.2560 -0.0005 0.0085  0.0299  49  GLY   C N   
1441 C CA  . GLY   B 43  ? 0.1797 0.1825 0.2438 -0.0010 0.0042  0.0278  49  GLY   C CA  
1442 C C   . GLY   B 43  ? 0.1894 0.1891 0.2468 -0.0004 0.0051  0.0270  49  GLY   C C   
1443 O O   . GLY   B 43  ? 0.2222 0.2201 0.2784 0.0007  0.0093  0.0279  49  GLY   C O   
1444 N N   . CYS   B 44  ? 0.1714 0.1704 0.2243 -0.0008 0.0016  0.0254  50  CYS   C N   
1445 C CA  . CYS   B 44  ? 0.1703 0.1664 0.2181 -0.0003 0.0021  0.0250  50  CYS   C CA  
1446 C C   . CYS   B 44  ? 0.1883 0.1834 0.2272 0.0008  0.0008  0.0226  50  CYS   C C   
1447 O O   . CYS   B 44  ? 0.2147 0.2075 0.2496 0.0013  0.0007  0.0223  50  CYS   C O   
1448 C CB  . CYS   B 44  ? 0.1733 0.1688 0.2256 -0.0020 -0.0006 0.0257  50  CYS   C CB  
1449 S SG  . CYS   B 44  ? 0.2242 0.2211 0.2886 -0.0034 0.0008  0.0289  50  CYS   C SG  
1450 N N   . ASP   B 45  ? 0.1536 0.1503 0.1900 0.0012  -0.0002 0.0210  51  ASP   C N   
1451 C CA  . ASP   B 45  ? 0.1565 0.1525 0.1855 0.0022  -0.0014 0.0188  51  ASP   C CA  
1452 C C   . ASP   B 45  ? 0.1765 0.1710 0.2006 0.0038  0.0017  0.0186  51  ASP   C C   
1453 O O   . ASP   B 45  ? 0.1991 0.1935 0.2249 0.0042  0.0049  0.0195  51  ASP   C O   
1454 C CB  . ASP   B 45  ? 0.1712 0.1695 0.1998 0.0020  -0.0031 0.0175  51  ASP   C CB  
1455 C CG  . ASP   B 45  ? 0.2158 0.2154 0.2468 0.0007  -0.0065 0.0175  51  ASP   C CG  
1456 O OD1 . ASP   B 45  ? 0.2233 0.2217 0.2537 0.0001  -0.0084 0.0173  51  ASP   C OD1 
1457 O OD2 . ASP   B 45  ? 0.1818 0.1836 0.2151 0.0003  -0.0074 0.0177  51  ASP   C OD2 
1458 N N   . THR   B 46  ? 0.1693 0.1625 0.1872 0.0048  0.0008  0.0174  52  THR   C N   
1459 C CA  . THR   B 46  ? 0.1630 0.1548 0.1750 0.0064  0.0028  0.0169  52  THR   C CA  
1460 C C   . THR   B 46  ? 0.1747 0.1678 0.1829 0.0069  0.0011  0.0145  52  THR   C C   
1461 O O   . THR   B 46  ? 0.1762 0.1702 0.1840 0.0066  -0.0016 0.0135  52  THR   C O   
1462 C CB  . THR   B 46  ? 0.1918 0.1813 0.1999 0.0072  0.0027  0.0178  52  THR   C CB  
1463 O OG1 . THR   B 46  ? 0.2297 0.2177 0.2419 0.0067  0.0046  0.0202  52  THR   C OG1 
1464 C CG2 . THR   B 46  ? 0.2036 0.1917 0.2043 0.0090  0.0040  0.0172  52  THR   C CG2 
1465 N N   . ILE   B 47  ? 0.1626 0.1557 0.1685 0.0076  0.0026  0.0134  53  ILE   C N   
1466 C CA  . ILE   B 47  ? 0.1627 0.1570 0.1657 0.0080  0.0010  0.0110  53  ILE   C CA  
1467 C C   . ILE   B 47  ? 0.1437 0.1368 0.1403 0.0093  0.0000  0.0103  53  ILE   C C   
1468 O O   . ILE   B 47  ? 0.1564 0.1475 0.1491 0.0102  0.0017  0.0111  53  ILE   C O   
1469 C CB  . ILE   B 47  ? 0.1753 0.1698 0.1787 0.0081  0.0030  0.0099  53  ILE   C CB  
1470 C CG1 . ILE   B 47  ? 0.1724 0.1679 0.1827 0.0071  0.0045  0.0111  53  ILE   C CG1 
1471 C CG2 . ILE   B 47  ? 0.1740 0.1697 0.1755 0.0082  0.0011  0.0073  53  ILE   C CG2 
1472 C CD1 . ILE   B 47  ? 0.2021 0.2000 0.2167 0.0059  0.0017  0.0113  53  ILE   C CD1 
1473 N N   . ALA   B 48  ? 0.1391 0.1336 0.1348 0.0094  -0.0027 0.0090  54  ALA   C N   
1474 C CA  . ALA   B 48  ? 0.1370 0.1308 0.1275 0.0107  -0.0042 0.0083  54  ALA   C CA  
1475 C C   . ALA   B 48  ? 0.1388 0.1323 0.1252 0.0113  -0.0037 0.0067  54  ALA   C C   
1476 O O   . ALA   B 48  ? 0.1472 0.1417 0.1355 0.0107  -0.0034 0.0051  54  ALA   C O   
1477 C CB  . ALA   B 48  ? 0.1429 0.1387 0.1348 0.0106  -0.0069 0.0072  54  ALA   C CB  
1478 N N   . ARG   B 49  ? 0.1447 0.1366 0.1252 0.0127  -0.0039 0.0071  55  ARG   C N   
1479 C CA  . ARG   B 49  ? 0.1522 0.1435 0.1274 0.0135  -0.0040 0.0053  55  ARG   C CA  
1480 C C   . ARG   B 49  ? 0.1614 0.1532 0.1328 0.0146  -0.0072 0.0050  55  ARG   C C   
1481 O O   . ARG   B 49  ? 0.1756 0.1658 0.1428 0.0158  -0.0072 0.0068  55  ARG   C O   
1482 C CB  . ARG   B 49  ? 0.1563 0.1447 0.1269 0.0142  -0.0006 0.0063  55  ARG   C CB  
1483 C CG  . ARG   B 49  ? 0.1468 0.1348 0.1224 0.0132  0.0028  0.0071  55  ARG   C CG  
1484 C CD  . ARG   B 49  ? 0.1745 0.1637 0.1534 0.0123  0.0030  0.0045  55  ARG   C CD  
1485 N NE  . ARG   B 49  ? 0.1714 0.1606 0.1559 0.0116  0.0062  0.0058  55  ARG   C NE  
1486 C CZ  . ARG   B 49  ? 0.1753 0.1658 0.1654 0.0106  0.0065  0.0047  55  ARG   C CZ  
1487 N NH1 . ARG   B 49  ? 0.1759 0.1679 0.1668 0.0101  0.0042  0.0024  55  ARG   C NH1 
1488 N NH2 . ARG   B 49  ? 0.1905 0.1810 0.1861 0.0100  0.0092  0.0063  55  ARG   C NH2 
1489 N N   . CYS   B 50  ? 0.1507 0.1450 0.1247 0.0141  -0.0099 0.0030  56  CYS   C N   
1490 C CA  . CYS   B 50  ? 0.1443 0.1401 0.1176 0.0150  -0.0132 0.0029  56  CYS   C CA  
1491 C C   . CYS   B 50  ? 0.1480 0.1467 0.1254 0.0142  -0.0155 0.0005  56  CYS   C C   
1492 O O   . CYS   B 50  ? 0.1522 0.1516 0.1329 0.0130  -0.0144 -0.0009 56  CYS   C O   
1493 C CB  . CYS   B 50  ? 0.1501 0.1459 0.1266 0.0152  -0.0130 0.0051  56  CYS   C CB  
1494 S SG  . CYS   B 50  ? 0.1521 0.1500 0.1362 0.0135  -0.0126 0.0045  56  CYS   C SG  
1495 N N   . ASP   B 51  ? 0.1586 0.1591 0.1364 0.0150  -0.0185 0.0003  57  ASP   C N   
1496 C CA  . ASP   B 51  ? 0.1620 0.1657 0.1449 0.0144  -0.0206 -0.0014 57  ASP   C CA  
1497 C C   . ASP   B 51  ? 0.1658 0.1712 0.1533 0.0148  -0.0211 -0.0001 57  ASP   C C   
1498 O O   . ASP   B 51  ? 0.1688 0.1768 0.1598 0.0150  -0.0232 -0.0008 57  ASP   C O   
1499 C CB  . ASP   B 51  ? 0.1864 0.1910 0.1667 0.0148  -0.0238 -0.0032 57  ASP   C CB  
1500 C CG  . ASP   B 51  ? 0.2416 0.2462 0.2183 0.0166  -0.0263 -0.0018 57  ASP   C CG  
1501 O OD1 . ASP   B 51  ? 0.2381 0.2415 0.2140 0.0175  -0.0251 0.0007  57  ASP   C OD1 
1502 O OD2 . ASP   B 51  ? 0.3075 0.3134 0.2825 0.0170  -0.0297 -0.0031 57  ASP   C OD2 
1503 N N   . CYS   B 52  ? 0.1535 0.1573 0.1413 0.0148  -0.0191 0.0017  58  CYS   C N   
1504 C CA  . CYS   B 52  ? 0.1457 0.1507 0.1374 0.0152  -0.0192 0.0025  58  CYS   C CA  
1505 C C   . CYS   B 52  ? 0.1381 0.1458 0.1352 0.0143  -0.0193 0.0013  58  CYS   C C   
1506 O O   . CYS   B 52  ? 0.1419 0.1502 0.1406 0.0130  -0.0184 0.0003  58  CYS   C O   
1507 C CB  . CYS   B 52  ? 0.1504 0.1530 0.1419 0.0149  -0.0171 0.0040  58  CYS   C CB  
1508 S SG  . CYS   B 52  ? 0.1569 0.1562 0.1438 0.0162  -0.0166 0.0063  58  CYS   C SG  
1509 N N   . GLN   B 53  ? 0.1330 0.1424 0.1331 0.0152  -0.0201 0.0016  59  GLN   C N   
1510 C CA  . GLN   B 53  ? 0.1455 0.1574 0.1509 0.0146  -0.0196 0.0009  59  GLN   C CA  
1511 C C   . GLN   B 53  ? 0.1309 0.1420 0.1372 0.0152  -0.0181 0.0019  59  GLN   C C   
1512 O O   . GLN   B 53  ? 0.1309 0.1440 0.1410 0.0153  -0.0174 0.0016  59  GLN   C O   
1513 C CB  . GLN   B 53  ? 0.1319 0.1470 0.1412 0.0151  -0.0217 0.0001  59  GLN   C CB  
1514 C CG  . GLN   B 53  ? 0.1716 0.1875 0.1808 0.0140  -0.0231 -0.0015 59  GLN   C CG  
1515 C CD  . GLN   B 53  ? 0.2208 0.2401 0.2352 0.0140  -0.0254 -0.0026 59  GLN   C CD  
1516 O OE1 . GLN   B 53  ? 0.2289 0.2488 0.2419 0.0145  -0.0284 -0.0034 59  GLN   C OE1 
1517 N NE2 . GLN   B 53  ? 0.1804 0.2020 0.2010 0.0134  -0.0241 -0.0027 59  GLN   C NE2 
1518 N N   . THR   B 54  ? 0.1421 0.1503 0.1451 0.0156  -0.0174 0.0028  60  THR   C N   
1519 C CA  . THR   B 54  ? 0.1560 0.1629 0.1594 0.0159  -0.0161 0.0032  60  THR   C CA  
1520 C C   . THR   B 54  ? 0.1484 0.1525 0.1490 0.0149  -0.0151 0.0037  60  THR   C C   
1521 O O   . THR   B 54  ? 0.1544 0.1570 0.1527 0.0147  -0.0153 0.0043  60  THR   C O   
1522 C CB  . THR   B 54  ? 0.1920 0.1979 0.1954 0.0178  -0.0166 0.0038  60  THR   C CB  
1523 O OG1 . THR   B 54  ? 0.2549 0.2586 0.2553 0.0183  -0.0173 0.0049  60  THR   C OG1 
1524 C CG2 . THR   B 54  ? 0.1898 0.1987 0.1967 0.0189  -0.0178 0.0036  60  THR   C CG2 
1525 N N   . GLY   B 55  ? 0.1312 0.1348 0.1324 0.0142  -0.0140 0.0035  61  GLY   C N   
1526 C CA  . GLY   B 55  ? 0.1318 0.1331 0.1313 0.0130  -0.0135 0.0039  61  GLY   C CA  
1527 C C   . GLY   B 55  ? 0.1196 0.1203 0.1191 0.0125  -0.0129 0.0034  61  GLY   C C   
1528 O O   . GLY   B 55  ? 0.1387 0.1400 0.1386 0.0135  -0.0125 0.0027  61  GLY   C O   
1529 N N   . VAL   B 56  ? 0.1207 0.1203 0.1196 0.0111  -0.0129 0.0037  62  VAL   C N   
1530 C CA  . VAL   B 56  ? 0.1220 0.1208 0.1198 0.0105  -0.0129 0.0032  62  VAL   C CA  
1531 C C   . VAL   B 56  ? 0.1234 0.1236 0.1222 0.0091  -0.0130 0.0039  62  VAL   C C   
1532 O O   . VAL   B 56  ? 0.1352 0.1353 0.1353 0.0082  -0.0132 0.0047  62  VAL   C O   
1533 C CB  . VAL   B 56  ? 0.1326 0.1279 0.1290 0.0103  -0.0135 0.0029  62  VAL   C CB  
1534 C CG1 . VAL   B 56  ? 0.1584 0.1525 0.1530 0.0094  -0.0140 0.0021  62  VAL   C CG1 
1535 C CG2 . VAL   B 56  ? 0.1477 0.1412 0.1435 0.0120  -0.0132 0.0025  62  VAL   C CG2 
1536 N N   . TYR   B 57  ? 0.1237 0.1252 0.1221 0.0089  -0.0127 0.0038  63  TYR   C N   
1537 C CA  . TYR   B 57  ? 0.1065 0.1094 0.1061 0.0076  -0.0130 0.0048  63  TYR   C CA  
1538 C C   . TYR   B 57  ? 0.1269 0.1286 0.1239 0.0069  -0.0139 0.0047  63  TYR   C C   
1539 O O   . TYR   B 57  ? 0.1359 0.1364 0.1298 0.0077  -0.0136 0.0036  63  TYR   C O   
1540 C CB  . TYR   B 57  ? 0.1154 0.1212 0.1174 0.0077  -0.0119 0.0054  63  TYR   C CB  
1541 C CG  . TYR   B 57  ? 0.1157 0.1226 0.1166 0.0082  -0.0110 0.0054  63  TYR   C CG  
1542 C CD1 . TYR   B 57  ? 0.1316 0.1388 0.1321 0.0096  -0.0100 0.0045  63  TYR   C CD1 
1543 C CD2 . TYR   B 57  ? 0.1227 0.1306 0.1234 0.0075  -0.0109 0.0067  63  TYR   C CD2 
1544 C CE1 . TYR   B 57  ? 0.1404 0.1486 0.1400 0.0103  -0.0085 0.0047  63  TYR   C CE1 
1545 C CE2 . TYR   B 57  ? 0.1342 0.1431 0.1335 0.0082  -0.0096 0.0070  63  TYR   C CE2 
1546 C CZ  . TYR   B 57  ? 0.1391 0.1481 0.1378 0.0096  -0.0082 0.0060  63  TYR   C CZ  
1547 O OH  . TYR   B 57  ? 0.1635 0.1733 0.1609 0.0104  -0.0063 0.0065  63  TYR   C OH  
1548 N N   . TYR   B 58  ? 0.1222 0.1245 0.1205 0.0056  -0.0149 0.0059  64  TYR   C N   
1549 C CA  . TYR   B 58  ? 0.1301 0.1316 0.1257 0.0049  -0.0164 0.0060  64  TYR   C CA  
1550 C C   . TYR   B 58  ? 0.1291 0.1328 0.1241 0.0050  -0.0157 0.0072  64  TYR   C C   
1551 O O   . TYR   B 58  ? 0.1387 0.1446 0.1373 0.0047  -0.0152 0.0088  64  TYR   C O   
1552 C CB  . TYR   B 58  ? 0.1356 0.1366 0.1335 0.0034  -0.0183 0.0070  64  TYR   C CB  
1553 C CG  . TYR   B 58  ? 0.1541 0.1543 0.1489 0.0025  -0.0206 0.0068  64  TYR   C CG  
1554 C CD1 . TYR   B 58  ? 0.1634 0.1608 0.1534 0.0028  -0.0214 0.0047  64  TYR   C CD1 
1555 C CD2 . TYR   B 58  ? 0.1510 0.1531 0.1474 0.0016  -0.0219 0.0087  64  TYR   C CD2 
1556 C CE1 . TYR   B 58  ? 0.1600 0.1563 0.1460 0.0021  -0.0238 0.0042  64  TYR   C CE1 
1557 C CE2 . TYR   B 58  ? 0.1645 0.1658 0.1574 0.0008  -0.0246 0.0086  64  TYR   C CE2 
1558 C CZ  . TYR   B 58  ? 0.1674 0.1658 0.1547 0.0011  -0.0255 0.0061  64  TYR   C CZ  
1559 O OH  . TYR   B 58  ? 0.2026 0.2000 0.1853 0.0004  -0.0284 0.0056  64  TYR   C OH  
1560 N N   . CYS   B 59  ? 0.1294 0.1321 0.1195 0.0056  -0.0158 0.0064  65  CYS   C N   
1561 C CA  . CYS   B 59  ? 0.1335 0.1379 0.1218 0.0059  -0.0149 0.0077  65  CYS   C CA  
1562 C C   . CYS   B 59  ? 0.1422 0.1456 0.1263 0.0051  -0.0173 0.0081  65  CYS   C C   
1563 O O   . CYS   B 59  ? 0.1583 0.1593 0.1367 0.0054  -0.0180 0.0063  65  CYS   C O   
1564 C CB  . CYS   B 59  ? 0.1392 0.1435 0.1250 0.0075  -0.0124 0.0067  65  CYS   C CB  
1565 S SG  . CYS   B 59  ? 0.1693 0.1753 0.1523 0.0082  -0.0106 0.0086  65  CYS   C SG  
1566 N N   . SER   B 60  ? 0.1525 0.1577 0.1394 0.0040  -0.0187 0.0104  66  SER   C N   
1567 C CA  A SER   B 60  ? 0.1669 0.1713 0.1503 0.0031  -0.0218 0.0109  66  SER   C CA  
1568 C CA  B SER   B 60  ? 0.1565 0.1609 0.1400 0.0031  -0.0218 0.0110  66  SER   C CA  
1569 C C   . SER   B 60  ? 0.1753 0.1792 0.1514 0.0040  -0.0214 0.0110  66  SER   C C   
1570 O O   . SER   B 60  ? 0.1990 0.2009 0.1694 0.0036  -0.0238 0.0098  66  SER   C O   
1571 C CB  A SER   B 60  ? 0.2036 0.2103 0.1924 0.0020  -0.0235 0.0136  66  SER   C CB  
1572 C CB  B SER   B 60  ? 0.1606 0.1676 0.1494 0.0021  -0.0231 0.0139  66  SER   C CB  
1573 O OG  A SER   B 60  ? 0.2418 0.2509 0.2337 0.0025  -0.0213 0.0159  66  SER   C OG  
1574 O OG  B SER   B 60  ? 0.1593 0.1658 0.1453 0.0012  -0.0266 0.0145  66  SER   C OG  
1575 N N   . SER   B 61  ? 0.1540 0.1595 0.1303 0.0052  -0.0183 0.0123  67  SER   C N   
1576 C CA  . SER   B 61  ? 0.1764 0.1814 0.1455 0.0062  -0.0172 0.0128  67  SER   C CA  
1577 C C   . SER   B 61  ? 0.1920 0.1940 0.1546 0.0073  -0.0161 0.0097  67  SER   C C   
1578 O O   . SER   B 61  ? 0.1999 0.2009 0.1555 0.0083  -0.0151 0.0097  67  SER   C O   
1579 C CB  . SER   B 61  ? 0.1767 0.1844 0.1489 0.0071  -0.0139 0.0155  67  SER   C CB  
1580 O OG  . SER   B 61  ? 0.1893 0.1975 0.1654 0.0079  -0.0109 0.0142  67  SER   C OG  
1581 N N   . ARG   B 62  ? 0.1680 0.1683 0.1326 0.0073  -0.0160 0.0071  68  ARG   C N   
1582 C CA  . ARG   B 62  ? 0.1803 0.1773 0.1396 0.0083  -0.0151 0.0039  68  ARG   C CA  
1583 C C   . ARG   B 62  ? 0.1897 0.1837 0.1481 0.0071  -0.0185 0.0015  68  ARG   C C   
1584 O O   . ARG   B 62  ? 0.2066 0.1972 0.1613 0.0078  -0.0180 -0.0014 68  ARG   C O   
1585 C CB  . ARG   B 62  ? 0.1928 0.1904 0.1559 0.0098  -0.0116 0.0031  68  ARG   C CB  
1586 C CG  . ARG   B 62  ? 0.2238 0.2243 0.1885 0.0109  -0.0082 0.0053  68  ARG   C CG  
1587 C CD  . ARG   B 62  ? 0.2181 0.2169 0.1751 0.0123  -0.0060 0.0047  68  ARG   C CD  
1588 N NE  . ARG   B 62  ? 0.2564 0.2580 0.2155 0.0135  -0.0022 0.0071  68  ARG   C NE  
1589 C CZ  . ARG   B 62  ? 0.3022 0.3057 0.2607 0.0132  -0.0018 0.0102  68  ARG   C CZ  
1590 N NH1 . ARG   B 62  ? 0.3304 0.3336 0.2858 0.0120  -0.0051 0.0113  68  ARG   C NH1 
1591 N NH2 . ARG   B 62  ? 0.3179 0.3236 0.2787 0.0143  0.0021  0.0123  68  ARG   C NH2 
1592 N N   . ARG   B 63  ? 0.1878 0.1829 0.1509 0.0054  -0.0214 0.0027  69  ARG   C N   
1593 C CA  . ARG   B 63  ? 0.2122 0.2049 0.1768 0.0040  -0.0243 0.0009  69  ARG   C CA  
1594 C C   . ARG   B 63  ? 0.2233 0.2139 0.1897 0.0048  -0.0224 -0.0012 69  ARG   C C   
1595 O O   . ARG   B 63  ? 0.2503 0.2372 0.2140 0.0046  -0.0236 -0.0039 69  ARG   C O   
1596 C CB  . ARG   B 63  ? 0.2351 0.2249 0.1929 0.0032  -0.0276 -0.0010 69  ARG   C CB  
1597 C CG  . ARG   B 63  ? 0.2643 0.2561 0.2201 0.0023  -0.0302 0.0013  69  ARG   C CG  
1598 C CD  . ARG   B 63  ? 0.3134 0.3078 0.2772 0.0007  -0.0326 0.0037  69  ARG   C CD  
1599 N NE  . ARG   B 63  ? 0.3717 0.3671 0.3334 -0.0005 -0.0366 0.0051  69  ARG   C NE  
1600 C CZ  . ARG   B 63  ? 0.3776 0.3763 0.3408 -0.0004 -0.0368 0.0086  69  ARG   C CZ  
1601 N NH1 . ARG   B 63  ? 0.3510 0.3521 0.3177 0.0007  -0.0330 0.0108  69  ARG   C NH1 
1602 N NH2 . ARG   B 63  ? 0.3815 0.3809 0.3430 -0.0014 -0.0409 0.0100  69  ARG   C NH2 
1603 N N   . LYS   B 64  ? 0.1883 0.1811 0.1591 0.0059  -0.0196 -0.0001 70  LYS   C N   
1604 C CA  . LYS   B 64  ? 0.1985 0.1896 0.1708 0.0070  -0.0178 -0.0017 70  LYS   C CA  
1605 C C   . LYS   B 64  ? 0.1739 0.1673 0.1527 0.0071  -0.0168 -0.0001 70  LYS   C C   
1606 O O   . LYS   B 64  ? 0.1734 0.1700 0.1551 0.0069  -0.0162 0.0019  70  LYS   C O   
1607 C CB  . LYS   B 64  ? 0.2483 0.2391 0.2170 0.0090  -0.0147 -0.0026 70  LYS   C CB  
1608 C CG  . LYS   B 64  ? 0.3990 0.3858 0.3607 0.0096  -0.0149 -0.0055 70  LYS   C CG  
1609 C CD  . LYS   B 64  ? 0.5162 0.5022 0.4757 0.0118  -0.0113 -0.0067 70  LYS   C CD  
1610 C CE  . LYS   B 64  ? 0.5911 0.5728 0.5425 0.0124  -0.0113 -0.0096 70  LYS   C CE  
1611 N NZ  . LYS   B 64  ? 0.6402 0.6221 0.5856 0.0114  -0.0131 -0.0090 70  LYS   C NZ  
1612 N N   . HIS   B 65  ? 0.1639 0.1555 0.1447 0.0074  -0.0167 -0.0011 71  HIS   C N   
1613 C CA  . HIS   B 65  ? 0.1671 0.1603 0.1527 0.0078  -0.0156 0.0000  71  HIS   C CA  
1614 C C   . HIS   B 65  ? 0.1751 0.1687 0.1605 0.0098  -0.0134 -0.0007 71  HIS   C C   
1615 O O   . HIS   B 65  ? 0.2144 0.2052 0.1974 0.0107  -0.0129 -0.0024 71  HIS   C O   
1616 C CB  . HIS   B 65  ? 0.1650 0.1561 0.1530 0.0071  -0.0168 0.0000  71  HIS   C CB  
1617 C CG  . HIS   B 65  ? 0.1444 0.1358 0.1343 0.0052  -0.0187 0.0010  71  HIS   C CG  
1618 N ND1 . HIS   B 65  ? 0.1886 0.1820 0.1828 0.0045  -0.0185 0.0030  71  HIS   C ND1 
1619 C CD2 . HIS   B 65  ? 0.1466 0.1363 0.1349 0.0038  -0.0209 0.0003  71  HIS   C CD2 
1620 C CE1 . HIS   B 65  ? 0.1646 0.1577 0.1604 0.0029  -0.0204 0.0036  71  HIS   C CE1 
1621 N NE2 . HIS   B 65  ? 0.1903 0.1814 0.1830 0.0023  -0.0222 0.0021  71  HIS   C NE2 
1622 N N   . TYR   B 66  ? 0.1445 0.1412 0.1329 0.0104  -0.0121 0.0004  72  TYR   C N   
1623 C CA  . TYR   B 66  ? 0.1509 0.1484 0.1402 0.0122  -0.0102 -0.0001 72  TYR   C CA  
1624 C C   . TYR   B 66  ? 0.1431 0.1417 0.1362 0.0127  -0.0104 0.0005  72  TYR   C C   
1625 O O   . TYR   B 66  ? 0.1366 0.1371 0.1321 0.0118  -0.0110 0.0016  72  TYR   C O   
1626 C CB  . TYR   B 66  ? 0.1640 0.1648 0.1543 0.0125  -0.0086 0.0009  72  TYR   C CB  
1627 C CG  . TYR   B 66  ? 0.1784 0.1784 0.1642 0.0126  -0.0078 0.0006  72  TYR   C CG  
1628 C CD1 . TYR   B 66  ? 0.2022 0.2004 0.1847 0.0141  -0.0060 -0.0008 72  TYR   C CD1 
1629 C CD2 . TYR   B 66  ? 0.1910 0.1920 0.1755 0.0113  -0.0086 0.0019  72  TYR   C CD2 
1630 C CE1 . TYR   B 66  ? 0.2121 0.2093 0.1892 0.0143  -0.0051 -0.0012 72  TYR   C CE1 
1631 C CE2 . TYR   B 66  ? 0.2086 0.2089 0.1880 0.0115  -0.0080 0.0019  72  TYR   C CE2 
1632 C CZ  . TYR   B 66  ? 0.2191 0.2174 0.1944 0.0130  -0.0062 0.0003  72  TYR   C CZ  
1633 O OH  . TYR   B 66  ? 0.2395 0.2367 0.2085 0.0133  -0.0054 0.0002  72  TYR   C OH  
1634 N N   . PRO   B 67  ? 0.1329 0.1303 0.1265 0.0142  -0.0099 -0.0002 73  PRO   C N   
1635 C CA  . PRO   B 67  ? 0.1404 0.1393 0.1372 0.0149  -0.0103 0.0006  73  PRO   C CA  
1636 C C   . PRO   B 67  ? 0.1544 0.1572 0.1545 0.0154  -0.0095 0.0010  73  PRO   C C   
1637 O O   . PRO   B 67  ? 0.1685 0.1722 0.1690 0.0163  -0.0078 0.0006  73  PRO   C O   
1638 C CB  . PRO   B 67  ? 0.1736 0.1700 0.1702 0.0165  -0.0100 -0.0001 73  PRO   C CB  
1639 C CG  . PRO   B 67  ? 0.1885 0.1832 0.1827 0.0171  -0.0086 -0.0015 73  PRO   C CG  
1640 C CD  . PRO   B 67  ? 0.1527 0.1473 0.1439 0.0155  -0.0089 -0.0017 73  PRO   C CD  
1641 N N   . VAL   B 68  ? 0.1311 0.1360 0.1336 0.0149  -0.0104 0.0018  74  VAL   C N   
1642 C CA  . VAL   B 68  ? 0.1332 0.1418 0.1396 0.0151  -0.0099 0.0020  74  VAL   C CA  
1643 C C   . VAL   B 68  ? 0.1297 0.1396 0.1382 0.0154  -0.0115 0.0021  74  VAL   C C   
1644 O O   . VAL   B 68  ? 0.1280 0.1363 0.1346 0.0150  -0.0127 0.0024  74  VAL   C O   
1645 C CB  . VAL   B 68  ? 0.1557 0.1658 0.1628 0.0135  -0.0095 0.0025  74  VAL   C CB  
1646 C CG1 . VAL   B 68  ? 0.1894 0.1990 0.1944 0.0134  -0.0079 0.0027  74  VAL   C CG1 
1647 C CG2 . VAL   B 68  ? 0.1692 0.1780 0.1749 0.0121  -0.0107 0.0029  74  VAL   C CG2 
1648 N N   . SER   B 69  ? 0.1156 0.1285 0.1284 0.0160  -0.0115 0.0021  75  SER   C N   
1649 C CA  . SER   B 69  ? 0.1227 0.1378 0.1381 0.0158  -0.0134 0.0019  75  SER   C CA  
1650 C C   . SER   B 69  ? 0.1187 0.1354 0.1360 0.0142  -0.0131 0.0017  75  SER   C C   
1651 O O   . SER   B 69  ? 0.1195 0.1372 0.1386 0.0137  -0.0113 0.0021  75  SER   C O   
1652 C CB  . SER   B 69  ? 0.1423 0.1601 0.1624 0.0172  -0.0138 0.0019  75  SER   C CB  
1653 O OG  . SER   B 69  ? 0.1934 0.2096 0.2123 0.0189  -0.0141 0.0022  75  SER   C OG  
1654 N N   . PHE   B 70  ? 0.1097 0.1262 0.1263 0.0134  -0.0145 0.0013  76  PHE   C N   
1655 C CA  . PHE   B 70  ? 0.1128 0.1304 0.1316 0.0119  -0.0141 0.0009  76  PHE   C CA  
1656 C C   . PHE   B 70  ? 0.1200 0.1389 0.1407 0.0115  -0.0161 -0.0003 76  PHE   C C   
1657 O O   . PHE   B 70  ? 0.1294 0.1477 0.1477 0.0123  -0.0180 -0.0007 76  PHE   C O   
1658 C CB  . PHE   B 70  ? 0.1253 0.1406 0.1409 0.0108  -0.0132 0.0014  76  PHE   C CB  
1659 C CG  . PHE   B 70  ? 0.1136 0.1264 0.1248 0.0110  -0.0140 0.0014  76  PHE   C CG  
1660 C CD1 . PHE   B 70  ? 0.1333 0.1440 0.1414 0.0117  -0.0139 0.0021  76  PHE   C CD1 
1661 C CD2 . PHE   B 70  ? 0.1188 0.1311 0.1292 0.0104  -0.0146 0.0007  76  PHE   C CD2 
1662 C CE1 . PHE   B 70  ? 0.1272 0.1355 0.1318 0.0118  -0.0143 0.0024  76  PHE   C CE1 
1663 C CE2 . PHE   B 70  ? 0.1315 0.1414 0.1377 0.0107  -0.0148 0.0010  76  PHE   C CE2 
1664 C CZ  . PHE   B 70  ? 0.1347 0.1428 0.1384 0.0114  -0.0146 0.0020  76  PHE   C CZ  
1665 N N   . SER   B 71  ? 0.1111 0.1317 0.1361 0.0104  -0.0158 -0.0008 77  SER   C N   
1666 C CA  . SER   B 71  ? 0.1283 0.1502 0.1558 0.0098  -0.0179 -0.0025 77  SER   C CA  
1667 C C   . SER   B 71  ? 0.1298 0.1493 0.1528 0.0092  -0.0187 -0.0037 77  SER   C C   
1668 O O   . SER   B 71  ? 0.1377 0.1548 0.1566 0.0092  -0.0173 -0.0029 77  SER   C O   
1669 C CB  . SER   B 71  ? 0.1374 0.1618 0.1720 0.0088  -0.0172 -0.0027 77  SER   C CB  
1670 O OG  . SER   B 71  ? 0.1474 0.1708 0.1824 0.0077  -0.0151 -0.0022 77  SER   C OG  
1671 N N   . LYS   B 72  ? 0.1314 0.1515 0.1555 0.0088  -0.0208 -0.0056 78  LYS   C N   
1672 C CA  . LYS   B 72  ? 0.1324 0.1499 0.1516 0.0083  -0.0213 -0.0071 78  LYS   C CA  
1673 C C   . LYS   B 72  ? 0.1551 0.1719 0.1772 0.0069  -0.0193 -0.0076 78  LYS   C C   
1674 O O   . LYS   B 72  ? 0.1679 0.1867 0.1964 0.0060  -0.0188 -0.0076 78  LYS   C O   
1675 C CB  . LYS   B 72  ? 0.1534 0.1717 0.1723 0.0084  -0.0247 -0.0093 78  LYS   C CB  
1676 C CG  . LYS   B 72  ? 0.1891 0.2082 0.2053 0.0099  -0.0271 -0.0084 78  LYS   C CG  
1677 C CD  . LYS   B 72  ? 0.2872 0.3074 0.3031 0.0099  -0.0311 -0.0106 78  LYS   C CD  
1678 C CE  . LYS   B 72  ? 0.4205 0.4423 0.4357 0.0115  -0.0339 -0.0095 78  LYS   C CE  
1679 N NZ  . LYS   B 72  ? 0.4865 0.5100 0.5025 0.0113  -0.0383 -0.0116 78  LYS   C NZ  
1680 N N   . PRO   B 73  ? 0.1391 0.1531 0.1573 0.0066  -0.0178 -0.0079 79  PRO   C N   
1681 C CA  . PRO   B 73  ? 0.1442 0.1575 0.1659 0.0054  -0.0157 -0.0081 79  PRO   C CA  
1682 C C   . PRO   B 73  ? 0.1584 0.1725 0.1849 0.0043  -0.0168 -0.0105 79  PRO   C C   
1683 O O   . PRO   B 73  ? 0.1739 0.1873 0.1980 0.0043  -0.0191 -0.0131 79  PRO   C O   
1684 C CB  . PRO   B 73  ? 0.1613 0.1714 0.1778 0.0056  -0.0143 -0.0085 79  PRO   C CB  
1685 C CG  . PRO   B 73  ? 0.1915 0.2008 0.2019 0.0069  -0.0151 -0.0075 79  PRO   C CG  
1686 C CD  . PRO   B 73  ? 0.1553 0.1668 0.1663 0.0076  -0.0178 -0.0077 79  PRO   C CD  
1687 N N   . SER   B 74  ? 0.1324 0.1480 0.1658 0.0034  -0.0154 -0.0096 80  SER   C N   
1688 C CA  . SER   B 74  ? 0.1363 0.1528 0.1757 0.0022  -0.0164 -0.0117 80  SER   C CA  
1689 C C   . SER   B 74  ? 0.1388 0.1554 0.1846 0.0012  -0.0138 -0.0104 80  SER   C C   
1690 O O   . SER   B 74  ? 0.1386 0.1549 0.1839 0.0015  -0.0115 -0.0078 80  SER   C O   
1691 C CB  . SER   B 74  ? 0.1659 0.1856 0.2091 0.0023  -0.0187 -0.0118 80  SER   C CB  
1692 O OG  . SER   B 74  ? 0.2079 0.2300 0.2554 0.0026  -0.0170 -0.0090 80  SER   C OG  
1693 N N   . LEU   B 75  ? 0.1484 0.1654 0.2005 0.0000  -0.0143 -0.0123 81  LEU   C N   
1694 C CA  . LEU   B 75  ? 0.1526 0.1696 0.2120 -0.0010 -0.0119 -0.0110 81  LEU   C CA  
1695 C C   . LEU   B 75  ? 0.1500 0.1705 0.2156 -0.0011 -0.0113 -0.0086 81  LEU   C C   
1696 O O   . LEU   B 75  ? 0.1711 0.1937 0.2411 -0.0016 -0.0133 -0.0099 81  LEU   C O   
1697 C CB  . LEU   B 75  ? 0.1678 0.1830 0.2311 -0.0024 -0.0127 -0.0146 81  LEU   C CB  
1698 C CG  . LEU   B 75  ? 0.1937 0.2083 0.2650 -0.0035 -0.0102 -0.0136 81  LEU   C CG  
1699 C CD1 . LEU   B 75  ? 0.1950 0.2072 0.2636 -0.0029 -0.0074 -0.0118 81  LEU   C CD1 
1700 C CD2 . LEU   B 75  ? 0.2253 0.2382 0.3012 -0.0050 -0.0117 -0.0178 81  LEU   C CD2 
1701 N N   . ILE   B 76  ? 0.1413 0.1625 0.2070 -0.0006 -0.0088 -0.0049 82  ILE   C N   
1702 C CA  . ILE   B 76  ? 0.1373 0.1614 0.2069 -0.0003 -0.0076 -0.0022 82  ILE   C CA  
1703 C C   . ILE   B 76  ? 0.1386 0.1629 0.2137 -0.0008 -0.0047 0.0006  82  ILE   C C   
1704 O O   . ILE   B 76  ? 0.1361 0.1584 0.2092 -0.0008 -0.0034 0.0019  82  ILE   C O   
1705 C CB  . ILE   B 76  ? 0.1795 0.2040 0.2421 0.0012  -0.0075 -0.0004 82  ILE   C CB  
1706 C CG1 . ILE   B 76  ? 0.2317 0.2562 0.2898 0.0019  -0.0103 -0.0027 82  ILE   C CG1 
1707 C CG2 . ILE   B 76  ? 0.2002 0.2270 0.2652 0.0018  -0.0054 0.0028  82  ILE   C CG2 
1708 C CD1 . ILE   B 76  ? 0.2556 0.2800 0.3076 0.0033  -0.0103 -0.0014 82  ILE   C CD1 
1709 N N   . PHE   B 77  ? 0.1438 0.1705 0.2261 -0.0012 -0.0037 0.0020  83  PHE   C N   
1710 C CA  . PHE   B 77  ? 0.1471 0.1741 0.2345 -0.0016 -0.0006 0.0054  83  PHE   C CA  
1711 C C   . PHE   B 77  ? 0.1688 0.1965 0.2506 -0.0002 0.0011  0.0089  83  PHE   C C   
1712 O O   . PHE   B 77  ? 0.1908 0.2204 0.2708 0.0008  0.0011  0.0094  83  PHE   C O   
1713 C CB  . PHE   B 77  ? 0.1504 0.1797 0.2478 -0.0025 0.0003  0.0058  83  PHE   C CB  
1714 C CG  . PHE   B 77  ? 0.1630 0.1920 0.2661 -0.0029 0.0035  0.0093  83  PHE   C CG  
1715 C CD1 . PHE   B 77  ? 0.1733 0.1998 0.2801 -0.0040 0.0038  0.0085  83  PHE   C CD1 
1716 C CD2 . PHE   B 77  ? 0.1822 0.2130 0.2862 -0.0021 0.0064  0.0135  83  PHE   C CD2 
1717 C CE1 . PHE   B 77  ? 0.1957 0.2218 0.3079 -0.0042 0.0068  0.0122  83  PHE   C CE1 
1718 C CE2 . PHE   B 77  ? 0.1998 0.2302 0.3084 -0.0024 0.0094  0.0172  83  PHE   C CE2 
1719 C CZ  . PHE   B 77  ? 0.1981 0.2263 0.3111 -0.0034 0.0095  0.0167  83  PHE   C CZ  
1720 N N   . VAL   B 78  ? 0.1322 0.1584 0.2116 0.0000  0.0025  0.0112  84  VAL   C N   
1721 C CA  . VAL   B 78  ? 0.1458 0.1723 0.2192 0.0012  0.0036  0.0143  84  VAL   C CA  
1722 C C   . VAL   B 78  ? 0.1369 0.1641 0.2147 0.0012  0.0064  0.0183  84  VAL   C C   
1723 O O   . VAL   B 78  ? 0.1428 0.1692 0.2260 0.0003  0.0073  0.0192  84  VAL   C O   
1724 C CB  . VAL   B 78  ? 0.1482 0.1725 0.2153 0.0015  0.0023  0.0139  84  VAL   C CB  
1725 C CG1 . VAL   B 78  ? 0.1553 0.1797 0.2159 0.0025  0.0028  0.0167  84  VAL   C CG1 
1726 C CG2 . VAL   B 78  ? 0.1642 0.1874 0.2274 0.0015  -0.0001 0.0102  84  VAL   C CG2 
1727 N N   . GLU   B 79  ? 0.1253 0.1540 0.2007 0.0022  0.0081  0.0210  85  GLU   C N   
1728 C CA  . GLU   B 79  ? 0.1314 0.1608 0.2097 0.0024  0.0111  0.0253  85  GLU   C CA  
1729 C C   . GLU   B 79  ? 0.1385 0.1664 0.2125 0.0026  0.0108  0.0278  85  GLU   C C   
1730 O O   . GLU   B 79  ? 0.1456 0.1721 0.2140 0.0028  0.0086  0.0263  85  GLU   C O   
1731 C CB  . GLU   B 79  ? 0.1527 0.1838 0.2284 0.0036  0.0133  0.0275  85  GLU   C CB  
1732 C CG  . GLU   B 79  ? 0.1766 0.2098 0.2590 0.0033  0.0141  0.0259  85  GLU   C CG  
1733 C CD  . GLU   B 79  ? 0.2480 0.2820 0.3417 0.0020  0.0155  0.0267  85  GLU   C CD  
1734 O OE1 . GLU   B 79  ? 0.2975 0.3310 0.3943 0.0018  0.0177  0.0301  85  GLU   C OE1 
1735 O OE2 . GLU   B 79  ? 0.2672 0.3025 0.3673 0.0012  0.0144  0.0240  85  GLU   C OE2 
1736 N N   . ALA   B 80  ? 0.1508 0.1789 0.2285 0.0027  0.0132  0.0320  86  ALA   C N   
1737 C CA  . ALA   B 80  ? 0.1602 0.1871 0.2349 0.0030  0.0127  0.0348  86  ALA   C CA  
1738 C C   . ALA   B 80  ? 0.1695 0.1963 0.2337 0.0040  0.0112  0.0353  86  ALA   C C   
1739 O O   . ALA   B 80  ? 0.1807 0.2082 0.2400 0.0049  0.0120  0.0355  86  ALA   C O   
1740 C CB  . ALA   B 80  ? 0.1717 0.1991 0.2512 0.0032  0.0156  0.0397  86  ALA   C CB  
1741 N N   . SER   B 81  ? 0.1515 0.1771 0.2128 0.0039  0.0091  0.0355  87  SER   C N   
1742 C CA  . SER   B 81  ? 0.1711 0.1964 0.2234 0.0047  0.0072  0.0361  87  SER   C CA  
1743 C C   . SER   B 81  ? 0.1735 0.1986 0.2257 0.0049  0.0067  0.0403  87  SER   C C   
1744 O O   . SER   B 81  ? 0.1767 0.2020 0.2361 0.0046  0.0081  0.0427  87  SER   C O   
1745 C CB  . SER   B 81  ? 0.1706 0.1948 0.2197 0.0043  0.0045  0.0322  87  SER   C CB  
1746 O OG  . SER   B 81  ? 0.1642 0.1876 0.2178 0.0036  0.0036  0.0319  87  SER   C OG  
1747 N N   . GLU   B 82  ? 0.1950 0.2199 0.2397 0.0053  0.0044  0.0410  88  GLU   C N   
1748 C CA  . GLU   B 82  ? 0.2095 0.2345 0.2544 0.0055  0.0033  0.0451  88  GLU   C CA  
1749 C C   . GLU   B 82  ? 0.2079 0.2325 0.2601 0.0047  0.0023  0.0447  88  GLU   C C   
1750 O O   . GLU   B 82  ? 0.2292 0.2542 0.2851 0.0049  0.0021  0.0485  88  GLU   C O   
1751 C CB  . GLU   B 82  ? 0.2730 0.2979 0.3083 0.0060  0.0006  0.0460  88  GLU   C CB  
1752 C CG  . GLU   B 82  ? 0.3911 0.4152 0.4235 0.0055  -0.0026 0.0429  88  GLU   C CG  
1753 C CD  . GLU   B 82  ? 0.4963 0.5203 0.5204 0.0058  -0.0057 0.0442  88  GLU   C CD  
1754 O OE1 . GLU   B 82  ? 0.5082 0.5321 0.5255 0.0066  -0.0050 0.0456  88  GLU   C OE1 
1755 O OE2 . GLU   B 82  ? 0.5137 0.5375 0.5382 0.0052  -0.0087 0.0438  88  GLU   C OE2 
1756 N N   . TYR   B 83  ? 0.1721 0.1959 0.2267 0.0041  0.0020  0.0405  89  TYR   C N   
1757 C CA  . TYR   B 83  ? 0.1616 0.1846 0.2219 0.0036  0.0014  0.0398  89  TYR   C CA  
1758 C C   . TYR   B 83  ? 0.1615 0.1835 0.2294 0.0030  0.0035  0.0373  89  TYR   C C   
1759 O O   . TYR   B 83  ? 0.1757 0.1968 0.2486 0.0027  0.0037  0.0369  89  TYR   C O   
1760 C CB  . TYR   B 83  ? 0.1642 0.1867 0.2200 0.0033  -0.0012 0.0372  89  TYR   C CB  
1761 C CG  . TYR   B 83  ? 0.1596 0.1815 0.2096 0.0033  -0.0016 0.0333  89  TYR   C CG  
1762 C CD1 . TYR   B 83  ? 0.1782 0.2004 0.2205 0.0037  -0.0027 0.0335  89  TYR   C CD1 
1763 C CD2 . TYR   B 83  ? 0.1524 0.1734 0.2045 0.0029  -0.0010 0.0295  89  TYR   C CD2 
1764 C CE1 . TYR   B 83  ? 0.1653 0.1870 0.2032 0.0039  -0.0029 0.0301  89  TYR   C CE1 
1765 C CE2 . TYR   B 83  ? 0.1643 0.1850 0.2116 0.0030  -0.0015 0.0264  89  TYR   C CE2 
1766 C CZ  . TYR   B 83  ? 0.1637 0.1847 0.2043 0.0035  -0.0023 0.0268  89  TYR   C CZ  
1767 O OH  . TYR   B 83  ? 0.1734 0.1941 0.2099 0.0038  -0.0027 0.0239  89  TYR   C OH  
1768 N N   . TYR   B 84  ? 0.1456 0.1677 0.2145 0.0027  0.0051  0.0354  90  TYR   C N   
1769 C CA  . TYR   B 84  ? 0.1384 0.1596 0.2146 0.0020  0.0067  0.0330  90  TYR   C CA  
1770 C C   . TYR   B 84  ? 0.1406 0.1628 0.2204 0.0019  0.0088  0.0343  90  TYR   C C   
1771 O O   . TYR   B 84  ? 0.1452 0.1687 0.2203 0.0024  0.0090  0.0353  90  TYR   C O   
1772 C CB  . TYR   B 84  ? 0.1391 0.1594 0.2128 0.0016  0.0055  0.0277  90  TYR   C CB  
1773 C CG  . TYR   B 84  ? 0.1338 0.1527 0.2058 0.0015  0.0043  0.0258  90  TYR   C CG  
1774 C CD1 . TYR   B 84  ? 0.1439 0.1615 0.2215 0.0014  0.0052  0.0262  90  TYR   C CD1 
1775 C CD2 . TYR   B 84  ? 0.1310 0.1499 0.1962 0.0018  0.0024  0.0238  90  TYR   C CD2 
1776 C CE1 . TYR   B 84  ? 0.1325 0.1488 0.2088 0.0015  0.0046  0.0245  90  TYR   C CE1 
1777 C CE2 . TYR   B 84  ? 0.1354 0.1530 0.1993 0.0018  0.0017  0.0224  90  TYR   C CE2 
1778 C CZ  . TYR   B 84  ? 0.1335 0.1498 0.2029 0.0016  0.0029  0.0227  90  TYR   C CZ  
1779 O OH  . TYR   B 84  ? 0.1364 0.1515 0.2050 0.0017  0.0027  0.0214  90  TYR   C OH  
1780 N N   . PRO   B 85  ? 0.1462 0.1676 0.2347 0.0012  0.0106  0.0342  91  PRO   C N   
1781 C CA  . PRO   B 85  ? 0.1353 0.1577 0.2285 0.0008  0.0126  0.0348  91  PRO   C CA  
1782 C C   . PRO   B 85  ? 0.1417 0.1646 0.2332 0.0004  0.0115  0.0301  91  PRO   C C   
1783 O O   . PRO   B 85  ? 0.1465 0.1687 0.2332 0.0003  0.0094  0.0265  91  PRO   C O   
1784 C CB  . PRO   B 85  ? 0.1403 0.1612 0.2437 0.0000  0.0143  0.0350  91  PRO   C CB  
1785 C CG  . PRO   B 85  ? 0.1564 0.1752 0.2593 -0.0003 0.0127  0.0313  91  PRO   C CG  
1786 C CD  . PRO   B 85  ? 0.1530 0.1724 0.2474 0.0006  0.0108  0.0325  91  PRO   C CD  
1787 N N   . ALA   B 86  ? 0.1450 0.1693 0.2409 0.0000  0.0131  0.0304  92  ALA   C N   
1788 C CA  . ALA   B 86  ? 0.1517 0.1767 0.2481 -0.0005 0.0119  0.0263  92  ALA   C CA  
1789 C C   . ALA   B 86  ? 0.1560 0.1791 0.2566 -0.0017 0.0105  0.0219  92  ALA   C C   
1790 O O   . ALA   B 86  ? 0.1809 0.2025 0.2886 -0.0024 0.0118  0.0225  92  ALA   C O   
1791 C CB  . ALA   B 86  ? 0.1550 0.1820 0.2575 -0.0008 0.0142  0.0279  92  ALA   C CB  
1792 N N   . ARG   B 87  ? 0.1478 0.1704 0.2434 -0.0017 0.0080  0.0177  93  ARG   C N   
1793 C CA  . ARG   B 87  ? 0.1357 0.1560 0.2331 -0.0026 0.0067  0.0136  93  ARG   C CA  
1794 C C   . ARG   B 87  ? 0.1462 0.1667 0.2379 -0.0025 0.0040  0.0095  93  ARG   C C   
1795 O O   . ARG   B 87  ? 0.1461 0.1682 0.2320 -0.0016 0.0032  0.0101  93  ARG   C O   
1796 C CB  . ARG   B 87  ? 0.1542 0.1722 0.2494 -0.0022 0.0071  0.0144  93  ARG   C CB  
1797 C CG  . ARG   B 87  ? 0.1492 0.1674 0.2351 -0.0011 0.0057  0.0147  93  ARG   C CG  
1798 C CD  . ARG   B 87  ? 0.1572 0.1737 0.2421 -0.0008 0.0061  0.0158  93  ARG   C CD  
1799 N NE  . ARG   B 87  ? 0.1590 0.1754 0.2359 -0.0001 0.0044  0.0150  93  ARG   C NE  
1800 C CZ  . ARG   B 87  ? 0.1854 0.2000 0.2601 0.0001  0.0041  0.0135  93  ARG   C CZ  
1801 N NH1 . ARG   B 87  ? 0.1918 0.2045 0.2716 -0.0002 0.0056  0.0129  93  ARG   C NH1 
1802 N NH2 . ARG   B 87  ? 0.1738 0.1885 0.2417 0.0006  0.0027  0.0128  93  ARG   C NH2 
1803 N N   . TYR   B 88  ? 0.1500 0.1685 0.2427 -0.0033 0.0026  0.0053  94  TYR   C N   
1804 C CA  . TYR   B 88  ? 0.1588 0.1770 0.2449 -0.0030 -0.0001 0.0016  94  TYR   C CA  
1805 C C   . TYR   B 88  ? 0.1423 0.1586 0.2210 -0.0021 -0.0001 0.0019  94  TYR   C C   
1806 O O   . TYR   B 88  ? 0.1712 0.1854 0.2514 -0.0022 0.0013  0.0023  94  TYR   C O   
1807 C CB  . TYR   B 88  ? 0.1764 0.1929 0.2658 -0.0042 -0.0017 -0.0030 94  TYR   C CB  
1808 C CG  . TYR   B 88  ? 0.1869 0.2058 0.2832 -0.0052 -0.0026 -0.0037 94  TYR   C CG  
1809 C CD1 . TYR   B 88  ? 0.2001 0.2213 0.2940 -0.0048 -0.0049 -0.0048 94  TYR   C CD1 
1810 C CD2 . TYR   B 88  ? 0.1950 0.2137 0.3012 -0.0064 -0.0012 -0.0031 94  TYR   C CD2 
1811 C CE1 . TYR   B 88  ? 0.2127 0.2366 0.3142 -0.0056 -0.0057 -0.0051 94  TYR   C CE1 
1812 C CE2 . TYR   B 88  ? 0.2089 0.2302 0.3226 -0.0074 -0.0018 -0.0034 94  TYR   C CE2 
1813 C CZ  . TYR   B 88  ? 0.2191 0.2430 0.3306 -0.0070 -0.0042 -0.0045 94  TYR   C CZ  
1814 O OH  . TYR   B 88  ? 0.2446 0.2713 0.3646 -0.0080 -0.0049 -0.0047 94  TYR   C OH  
1815 N N   . GLN   B 89  ? 0.1305 0.1476 0.2020 -0.0012 -0.0016 0.0016  95  GLN   C N   
1816 C CA  . GLN   B 89  ? 0.1397 0.1552 0.2044 -0.0004 -0.0018 0.0016  95  GLN   C CA  
1817 C C   . GLN   B 89  ? 0.1377 0.1522 0.1972 -0.0002 -0.0039 -0.0020 95  GLN   C C   
1818 O O   . GLN   B 89  ? 0.1504 0.1667 0.2092 -0.0001 -0.0057 -0.0030 95  GLN   C O   
1819 C CB  . GLN   B 89  ? 0.1386 0.1555 0.1994 0.0005  -0.0015 0.0049  95  GLN   C CB  
1820 C CG  . GLN   B 89  ? 0.1573 0.1727 0.2122 0.0011  -0.0019 0.0051  95  GLN   C CG  
1821 C CD  . GLN   B 89  ? 0.1368 0.1531 0.1894 0.0016  -0.0015 0.0085  95  GLN   C CD  
1822 O OE1 . GLN   B 89  ? 0.1568 0.1742 0.2127 0.0015  -0.0005 0.0115  95  GLN   C OE1 
1823 N NE2 . GLN   B 89  ? 0.1546 0.1702 0.2015 0.0021  -0.0026 0.0083  95  GLN   C NE2 
1824 N N   . SER   B 90  ? 0.1216 0.1335 0.1776 0.0000  -0.0038 -0.0039 96  SER   C N   
1825 C CA  . SER   B 90  ? 0.1357 0.1464 0.1859 0.0003  -0.0056 -0.0071 96  SER   C CA  
1826 C C   . SER   B 90  ? 0.1334 0.1439 0.1763 0.0014  -0.0061 -0.0059 96  SER   C C   
1827 O O   . SER   B 90  ? 0.1281 0.1389 0.1707 0.0018  -0.0048 -0.0030 96  SER   C O   
1828 C CB  . SER   B 90  ? 0.1578 0.1652 0.2077 -0.0001 -0.0049 -0.0102 96  SER   C CB  
1829 O OG  . SER   B 90  ? 0.1718 0.1775 0.2206 0.0005  -0.0026 -0.0086 96  SER   C OG  
1830 N N   . HIS   B 91  ? 0.1273 0.1373 0.1647 0.0020  -0.0080 -0.0080 97  HIS   C N   
1831 C CA  . HIS   B 91  ? 0.1303 0.1398 0.1611 0.0030  -0.0085 -0.0071 97  HIS   C CA  
1832 C C   . HIS   B 91  ? 0.1356 0.1471 0.1667 0.0034  -0.0085 -0.0041 97  HIS   C C   
1833 O O   . HIS   B 91  ? 0.1429 0.1537 0.1708 0.0039  -0.0078 -0.0025 97  HIS   C O   
1834 C CB  . HIS   B 91  ? 0.1450 0.1518 0.1728 0.0033  -0.0064 -0.0069 97  HIS   C CB  
1835 C CG  . HIS   B 91  ? 0.1668 0.1709 0.1926 0.0032  -0.0061 -0.0102 97  HIS   C CG  
1836 N ND1 . HIS   B 91  ? 0.2055 0.2079 0.2241 0.0040  -0.0071 -0.0120 97  HIS   C ND1 
1837 C CD2 . HIS   B 91  ? 0.1813 0.1841 0.2113 0.0025  -0.0050 -0.0121 97  HIS   C CD2 
1838 C CE1 . HIS   B 91  ? 0.2073 0.2073 0.2251 0.0037  -0.0065 -0.0151 97  HIS   C CE1 
1839 N NE2 . HIS   B 91  ? 0.2031 0.2030 0.2278 0.0028  -0.0051 -0.0153 97  HIS   C NE2 
1840 N N   . LEU   B 92  ? 0.1178 0.1317 0.1530 0.0031  -0.0090 -0.0036 98  LEU   C N   
1841 C CA  . LEU   B 92  ? 0.1152 0.1308 0.1506 0.0036  -0.0087 -0.0011 98  LEU   C CA  
1842 C C   . LEU   B 92  ? 0.1151 0.1319 0.1481 0.0044  -0.0104 -0.0017 98  LEU   C C   
1843 O O   . LEU   B 92  ? 0.1257 0.1435 0.1604 0.0043  -0.0120 -0.0036 98  LEU   C O   
1844 C CB  . LEU   B 92  ? 0.1269 0.1443 0.1687 0.0029  -0.0073 0.0005  98  LEU   C CB  
1845 C CG  . LEU   B 92  ? 0.1358 0.1546 0.1772 0.0034  -0.0064 0.0033  98  LEU   C CG  
1846 C CD1 . LEU   B 92  ? 0.1353 0.1528 0.1734 0.0036  -0.0058 0.0052  98  LEU   C CD1 
1847 C CD2 . LEU   B 92  ? 0.1596 0.1803 0.2073 0.0029  -0.0049 0.0049  98  LEU   C CD2 
1848 N N   . MET   B 93  ? 0.1184 0.1353 0.1481 0.0052  -0.0103 -0.0001 99  MET   C N   
1849 C CA  . MET   B 93  ? 0.1146 0.1324 0.1425 0.0063  -0.0116 -0.0004 99  MET   C CA  
1850 C C   . MET   B 93  ? 0.1171 0.1363 0.1463 0.0067  -0.0104 0.0015  99  MET   C C   
1851 O O   . MET   B 93  ? 0.1250 0.1433 0.1526 0.0065  -0.0092 0.0030  99  MET   C O   
1852 C CB  . MET   B 93  ? 0.1369 0.1526 0.1588 0.0071  -0.0123 -0.0003 99  MET   C CB  
1853 C CG  . MET   B 93  ? 0.1490 0.1630 0.1683 0.0069  -0.0131 -0.0019 99  MET   C CG  
1854 S SD  . MET   B 93  ? 0.1610 0.1722 0.1737 0.0077  -0.0130 -0.0013 99  MET   C SD  
1855 C CE  . MET   B 93  ? 0.1703 0.1807 0.1839 0.0070  -0.0110 0.0008  99  MET   C CE  
1856 N N   . LEU   B 94  ? 0.1117 0.1330 0.1437 0.0073  -0.0106 0.0014  100 LEU   C N   
1857 C CA  . LEU   B 94  ? 0.1234 0.1458 0.1561 0.0078  -0.0088 0.0030  100 LEU   C CA  
1858 C C   . LEU   B 94  ? 0.1186 0.1405 0.1478 0.0093  -0.0092 0.0029  100 LEU   C C   
1859 O O   . LEU   B 94  ? 0.1265 0.1485 0.1554 0.0099  -0.0110 0.0018  100 LEU   C O   
1860 C CB  . LEU   B 94  ? 0.1279 0.1531 0.1675 0.0076  -0.0079 0.0034  100 LEU   C CB  
1861 C CG  . LEU   B 94  ? 0.1303 0.1561 0.1749 0.0062  -0.0071 0.0037  100 LEU   C CG  
1862 C CD1 . LEU   B 94  ? 0.1650 0.1938 0.2172 0.0061  -0.0059 0.0043  100 LEU   C CD1 
1863 C CD2 . LEU   B 94  ? 0.1500 0.1744 0.1924 0.0058  -0.0054 0.0056  100 LEU   C CD2 
1864 N N   . ALA   B 95  ? 0.1255 0.1468 0.1524 0.0098  -0.0076 0.0041  101 ALA   C N   
1865 C CA  . ALA   B 95  ? 0.1264 0.1471 0.1507 0.0113  -0.0073 0.0040  101 ALA   C CA  
1866 C C   . ALA   B 95  ? 0.1178 0.1395 0.1429 0.0119  -0.0047 0.0052  101 ALA   C C   
1867 O O   . ALA   B 95  ? 0.1170 0.1391 0.1427 0.0110  -0.0035 0.0065  101 ALA   C O   
1868 C CB  . ALA   B 95  ? 0.1365 0.1541 0.1547 0.0114  -0.0081 0.0038  101 ALA   C CB  
1869 N N   . VAL   B 96  ? 0.1207 0.1425 0.1453 0.0134  -0.0037 0.0050  102 VAL   C N   
1870 C CA  . VAL   B 96  ? 0.1280 0.1499 0.1517 0.0142  -0.0008 0.0060  102 VAL   C CA  
1871 C C   . VAL   B 96  ? 0.1423 0.1609 0.1583 0.0142  -0.0007 0.0058  102 VAL   C C   
1872 O O   . VAL   B 96  ? 0.1639 0.1802 0.1764 0.0149  -0.0018 0.0046  102 VAL   C O   
1873 C CB  . VAL   B 96  ? 0.1525 0.1758 0.1793 0.0159  0.0005  0.0056  102 VAL   C CB  
1874 C CG1 . VAL   B 96  ? 0.1732 0.1962 0.1982 0.0170  0.0042  0.0066  102 VAL   C CG1 
1875 C CG2 . VAL   B 96  ? 0.1657 0.1926 0.2010 0.0157  -0.0002 0.0057  102 VAL   C CG2 
1876 N N   . GLY   B 97  ? 0.1516 0.1700 0.1654 0.0135  0.0002  0.0072  103 GLY   C N   
1877 C CA  . GLY   B 97  ? 0.1641 0.1795 0.1708 0.0133  -0.0004 0.0070  103 GLY   C CA  
1878 C C   . GLY   B 97  ? 0.1694 0.1852 0.1745 0.0125  0.0003  0.0089  103 GLY   C C   
1879 O O   . GLY   B 97  ? 0.1873 0.2055 0.1972 0.0119  0.0012  0.0104  103 GLY   C O   
1880 N N   . HIS   B 98  ? 0.1701 0.1835 0.1686 0.0123  -0.0005 0.0087  104 HIS   C N   
1881 C CA  . HIS   B 98  ? 0.1732 0.1868 0.1693 0.0117  -0.0004 0.0108  104 HIS   C CA  
1882 C C   . HIS   B 98  ? 0.1602 0.1741 0.1584 0.0101  -0.0028 0.0117  104 HIS   C C   
1883 O O   . HIS   B 98  ? 0.1646 0.1770 0.1622 0.0094  -0.0051 0.0104  104 HIS   C O   
1884 C CB  . HIS   B 98  ? 0.2050 0.2158 0.1927 0.0122  -0.0006 0.0100  104 HIS   C CB  
1885 C CG  . HIS   B 98  ? 0.2492 0.2603 0.2334 0.0119  -0.0004 0.0123  104 HIS   C CG  
1886 N ND1 . HIS   B 98  ? 0.2730 0.2860 0.2585 0.0126  0.0026  0.0147  104 HIS   C ND1 
1887 C CD2 . HIS   B 98  ? 0.2784 0.2884 0.2588 0.0108  -0.0032 0.0130  104 HIS   C CD2 
1888 C CE1 . HIS   B 98  ? 0.2968 0.3096 0.2785 0.0121  0.0017  0.0168  104 HIS   C CE1 
1889 N NE2 . HIS   B 98  ? 0.3028 0.3139 0.2813 0.0110  -0.0020 0.0158  104 HIS   C NE2 
1890 N N   . SER   B 99  ? 0.1600 0.1756 0.1607 0.0095  -0.0021 0.0142  105 SER   C N   
1891 C CA  . SER   B 99  ? 0.1736 0.1895 0.1769 0.0081  -0.0039 0.0155  105 SER   C CA  
1892 C C   . SER   B 99  ? 0.1958 0.2130 0.1996 0.0080  -0.0029 0.0186  105 SER   C C   
1893 O O   . SER   B 99  ? 0.2229 0.2418 0.2306 0.0083  -0.0005 0.0200  105 SER   C O   
1894 C CB  . SER   B 99  ? 0.1989 0.2161 0.2091 0.0076  -0.0038 0.0147  105 SER   C CB  
1895 O OG  . SER   B 99  ? 0.2144 0.2318 0.2277 0.0065  -0.0050 0.0158  105 SER   C OG  
1896 N N   . GLU   B 100 ? 0.1905 0.2069 0.1907 0.0075  -0.0049 0.0200  106 GLU   C N   
1897 C CA  . GLU   B 100 ? 0.1986 0.2161 0.1990 0.0073  -0.0046 0.0235  106 GLU   C CA  
1898 C C   . GLU   B 100 ? 0.1837 0.2018 0.1895 0.0062  -0.0065 0.0245  106 GLU   C C   
1899 O O   . GLU   B 100 ? 0.1824 0.1998 0.1899 0.0055  -0.0081 0.0226  106 GLU   C O   
1900 C CB  . GLU   B 100 ? 0.2576 0.2736 0.2492 0.0077  -0.0062 0.0240  106 GLU   C CB  
1901 C CG  . GLU   B 100 ? 0.3960 0.4113 0.3818 0.0091  -0.0037 0.0236  106 GLU   C CG  
1902 C CD  . GLU   B 100 ? 0.4494 0.4624 0.4253 0.0094  -0.0055 0.0228  106 GLU   C CD  
1903 O OE1 . GLU   B 100 ? 0.5002 0.5128 0.4739 0.0086  -0.0089 0.0238  106 GLU   C OE1 
1904 O OE2 . GLU   B 100 ? 0.4821 0.4935 0.4528 0.0106  -0.0037 0.0209  106 GLU   C OE2 
1905 N N   . PRO   B 101 ? 0.1881 0.2075 0.1970 0.0060  -0.0061 0.0279  107 PRO   C N   
1906 C CA  . PRO   B 101 ? 0.1854 0.2053 0.2001 0.0050  -0.0075 0.0290  107 PRO   C CA  
1907 C C   . PRO   B 101 ? 0.1866 0.2055 0.1993 0.0043  -0.0108 0.0279  107 PRO   C C   
1908 O O   . PRO   B 101 ? 0.1845 0.2033 0.2020 0.0037  -0.0112 0.0268  107 PRO   C O   
1909 C CB  . PRO   B 101 ? 0.2064 0.2276 0.2231 0.0052  -0.0068 0.0333  107 PRO   C CB  
1910 C CG  . PRO   B 101 ? 0.2448 0.2664 0.2595 0.0062  -0.0039 0.0341  107 PRO   C CG  
1911 C CD  . PRO   B 101 ? 0.2182 0.2386 0.2262 0.0067  -0.0038 0.0311  107 PRO   C CD  
1912 N N   . GLY   B 102 ? 0.1692 0.1872 0.1750 0.0044  -0.0129 0.0279  108 GLY   C N   
1913 C CA  . GLY   B 102 ? 0.1692 0.1863 0.1737 0.0035  -0.0163 0.0269  108 GLY   C CA  
1914 C C   . GLY   B 102 ? 0.1608 0.1764 0.1653 0.0032  -0.0165 0.0234  108 GLY   C C   
1915 O O   . GLY   B 102 ? 0.1775 0.1923 0.1826 0.0024  -0.0189 0.0226  108 GLY   C O   
1916 N N   . ASP   B 103 ? 0.1450 0.1600 0.1489 0.0039  -0.0141 0.0213  109 ASP   C N   
1917 C CA  . ASP   B 103 ? 0.1412 0.1548 0.1450 0.0039  -0.0141 0.0183  109 ASP   C CA  
1918 C C   . ASP   B 103 ? 0.1322 0.1464 0.1426 0.0034  -0.0134 0.0181  109 ASP   C C   
1919 O O   . ASP   B 103 ? 0.1370 0.1499 0.1475 0.0033  -0.0137 0.0161  109 ASP   C O   
1920 C CB  . ASP   B 103 ? 0.1654 0.1785 0.1666 0.0050  -0.0120 0.0165  109 ASP   C CB  
1921 C CG  . ASP   B 103 ? 0.1771 0.1887 0.1708 0.0056  -0.0125 0.0159  109 ASP   C CG  
1922 O OD1 . ASP   B 103 ? 0.1733 0.1835 0.1635 0.0050  -0.0150 0.0153  109 ASP   C OD1 
1923 O OD2 . ASP   B 103 ? 0.1887 0.2007 0.1804 0.0067  -0.0102 0.0159  109 ASP   C OD2 
1924 N N   . CYS   B 104 ? 0.1143 0.1300 0.1299 0.0032  -0.0123 0.0200  110 CYS   C N   
1925 C CA  . CYS   B 104 ? 0.1221 0.1379 0.1434 0.0029  -0.0114 0.0195  110 CYS   C CA  
1926 C C   . CYS   B 104 ? 0.1284 0.1433 0.1505 0.0022  -0.0130 0.0192  110 CYS   C C   
1927 O O   . CYS   B 104 ? 0.1504 0.1655 0.1721 0.0017  -0.0150 0.0208  110 CYS   C O   
1928 C CB  . CYS   B 104 ? 0.1297 0.1469 0.1567 0.0027  -0.0101 0.0218  110 CYS   C CB  
1929 S SG  . CYS   B 104 ? 0.1521 0.1703 0.1808 0.0033  -0.0075 0.0219  110 CYS   C SG  
1930 N N   . GLY   B 105 ? 0.1146 0.1285 0.1377 0.0022  -0.0121 0.0174  111 GLY   C N   
1931 C CA  . GLY   B 105 ? 0.1266 0.1395 0.1511 0.0017  -0.0129 0.0172  111 GLY   C CA  
1932 C C   . GLY   B 105 ? 0.1270 0.1380 0.1469 0.0017  -0.0140 0.0154  111 GLY   C C   
1933 O O   . GLY   B 105 ? 0.1466 0.1566 0.1678 0.0014  -0.0142 0.0152  111 GLY   C O   
1934 N N   . GLY   B 106 ? 0.1323 0.1429 0.1474 0.0023  -0.0145 0.0143  112 GLY   C N   
1935 C CA  . GLY   B 106 ? 0.1347 0.1433 0.1459 0.0025  -0.0152 0.0124  112 GLY   C CA  
1936 C C   . GLY   B 106 ? 0.1353 0.1430 0.1472 0.0031  -0.0138 0.0111  112 GLY   C C   
1937 O O   . GLY   B 106 ? 0.1292 0.1379 0.1426 0.0036  -0.0123 0.0108  112 GLY   C O   
1938 N N   . ILE   B 107 ? 0.1308 0.1366 0.1417 0.0030  -0.0143 0.0105  113 ILE   C N   
1939 C CA  . ILE   B 107 ? 0.1339 0.1388 0.1449 0.0036  -0.0130 0.0096  113 ILE   C CA  
1940 C C   . ILE   B 107 ? 0.1257 0.1300 0.1334 0.0048  -0.0128 0.0081  113 ILE   C C   
1941 O O   . ILE   B 107 ? 0.1284 0.1317 0.1334 0.0050  -0.0137 0.0074  113 ILE   C O   
1942 C CB  . ILE   B 107 ? 0.1678 0.1708 0.1799 0.0030  -0.0133 0.0102  113 ILE   C CB  
1943 C CG1 . ILE   B 107 ? 0.2045 0.2086 0.2215 0.0022  -0.0124 0.0119  113 ILE   C CG1 
1944 C CG2 . ILE   B 107 ? 0.1623 0.1635 0.1724 0.0039  -0.0123 0.0094  113 ILE   C CG2 
1945 C CD1 . ILE   B 107 ? 0.2479 0.2508 0.2677 0.0015  -0.0125 0.0129  113 ILE   C CD1 
1946 N N   . LEU   B 108 ? 0.1151 0.1199 0.1231 0.0055  -0.0118 0.0075  114 LEU   C N   
1947 C CA  . LEU   B 108 ? 0.1205 0.1248 0.1263 0.0067  -0.0118 0.0063  114 LEU   C CA  
1948 C C   . LEU   B 108 ? 0.1136 0.1160 0.1183 0.0070  -0.0116 0.0064  114 LEU   C C   
1949 O O   . LEU   B 108 ? 0.1175 0.1198 0.1232 0.0067  -0.0107 0.0069  114 LEU   C O   
1950 C CB  . LEU   B 108 ? 0.1085 0.1149 0.1157 0.0071  -0.0113 0.0056  114 LEU   C CB  
1951 C CG  . LEU   B 108 ? 0.1218 0.1283 0.1277 0.0083  -0.0117 0.0045  114 LEU   C CG  
1952 C CD1 . LEU   B 108 ? 0.1320 0.1383 0.1367 0.0091  -0.0120 0.0042  114 LEU   C CD1 
1953 C CD2 . LEU   B 108 ? 0.1334 0.1419 0.1415 0.0083  -0.0115 0.0037  114 LEU   C CD2 
1954 N N   . ARG   B 109 ? 0.1192 0.1198 0.1218 0.0076  -0.0121 0.0062  115 ARG   C N   
1955 C CA  . ARG   B 109 ? 0.1347 0.1333 0.1362 0.0081  -0.0117 0.0069  115 ARG   C CA  
1956 C C   . ARG   B 109 ? 0.1429 0.1407 0.1421 0.0096  -0.0121 0.0064  115 ARG   C C   
1957 O O   . ARG   B 109 ? 0.1508 0.1489 0.1497 0.0102  -0.0127 0.0056  115 ARG   C O   
1958 C CB  . ARG   B 109 ? 0.1850 0.1815 0.1874 0.0071  -0.0118 0.0078  115 ARG   C CB  
1959 C CG  . ARG   B 109 ? 0.2456 0.2407 0.2469 0.0073  -0.0129 0.0070  115 ARG   C CG  
1960 C CD  . ARG   B 109 ? 0.3256 0.3186 0.3283 0.0061  -0.0136 0.0075  115 ARG   C CD  
1961 N NE  . ARG   B 109 ? 0.3995 0.3939 0.4043 0.0046  -0.0145 0.0077  115 ARG   C NE  
1962 C CZ  . ARG   B 109 ? 0.4944 0.4889 0.5026 0.0034  -0.0144 0.0091  115 ARG   C CZ  
1963 N NH1 . ARG   B 109 ? 0.5233 0.5167 0.5330 0.0035  -0.0130 0.0103  115 ARG   C NH1 
1964 N NH2 . ARG   B 109 ? 0.5022 0.4983 0.5125 0.0022  -0.0155 0.0095  115 ARG   C NH2 
1965 N N   . CYS   B 110 ? 0.1361 0.1329 0.1337 0.0103  -0.0116 0.0070  116 CYS   C N   
1966 C CA  . CYS   B 110 ? 0.1411 0.1371 0.1366 0.0119  -0.0123 0.0071  116 CYS   C CA  
1967 C C   . CYS   B 110 ? 0.1547 0.1477 0.1489 0.0121  -0.0115 0.0088  116 CYS   C C   
1968 O O   . CYS   B 110 ? 0.1619 0.1538 0.1577 0.0110  -0.0106 0.0096  116 CYS   C O   
1969 C CB  . CYS   B 110 ? 0.1370 0.1348 0.1311 0.0126  -0.0128 0.0066  116 CYS   C CB  
1970 S SG  . CYS   B 110 ? 0.1396 0.1362 0.1313 0.0123  -0.0114 0.0072  116 CYS   C SG  
1971 N N   . GLN   B 111 ? 0.1635 0.1553 0.1556 0.0136  -0.0119 0.0096  117 GLN   C N   
1972 C CA  . GLN   B 111 ? 0.1885 0.1773 0.1796 0.0140  -0.0108 0.0116  117 GLN   C CA  
1973 C C   . GLN   B 111 ? 0.1906 0.1789 0.1806 0.0134  -0.0090 0.0128  117 GLN   C C   
1974 O O   . GLN   B 111 ? 0.2109 0.1968 0.2014 0.0132  -0.0076 0.0146  117 GLN   C O   
1975 C CB  . GLN   B 111 ? 0.2095 0.1972 0.1984 0.0159  -0.0115 0.0128  117 GLN   C CB  
1976 C CG  . GLN   B 111 ? 0.2528 0.2419 0.2380 0.0171  -0.0122 0.0128  117 GLN   C CG  
1977 C CD  . GLN   B 111 ? 0.4013 0.3898 0.3844 0.0191  -0.0135 0.0141  117 GLN   C CD  
1978 O OE1 . GLN   B 111 ? 0.4393 0.4298 0.4234 0.0200  -0.0153 0.0132  117 GLN   C OE1 
1979 N NE2 . GLN   B 111 ? 0.4152 0.4012 0.3956 0.0199  -0.0124 0.0166  117 GLN   C NE2 
1980 N N   . HIS   B 112 ? 0.1655 0.1557 0.1541 0.0133  -0.0089 0.0117  118 HIS   C N   
1981 C CA  . HIS   B 112 ? 0.1679 0.1574 0.1551 0.0130  -0.0068 0.0126  118 HIS   C CA  
1982 C C   . HIS   B 112 ? 0.1739 0.1640 0.1653 0.0114  -0.0055 0.0125  118 HIS   C C   
1983 O O   . HIS   B 112 ? 0.1888 0.1780 0.1800 0.0112  -0.0032 0.0135  118 HIS   C O   
1984 C CB  . HIS   B 112 ? 0.1703 0.1610 0.1536 0.0138  -0.0074 0.0112  118 HIS   C CB  
1985 C CG  . HIS   B 112 ? 0.1722 0.1628 0.1517 0.0155  -0.0092 0.0115  118 HIS   C CG  
1986 N ND1 . HIS   B 112 ? 0.1493 0.1422 0.1296 0.0159  -0.0118 0.0098  118 HIS   C ND1 
1987 C CD2 . HIS   B 112 ? 0.1980 0.1865 0.1732 0.0169  -0.0089 0.0134  118 HIS   C CD2 
1988 C CE1 . HIS   B 112 ? 0.1844 0.1768 0.1614 0.0175  -0.0132 0.0107  118 HIS   C CE1 
1989 N NE2 . HIS   B 112 ? 0.2066 0.1963 0.1800 0.0182  -0.0116 0.0129  118 HIS   C NE2 
1990 N N   . GLY   B 113 ? 0.1532 0.1448 0.1481 0.0103  -0.0068 0.0115  119 GLY   C N   
1991 C CA  . GLY   B 113 ? 0.1497 0.1422 0.1488 0.0088  -0.0060 0.0117  119 GLY   C CA  
1992 C C   . GLY   B 113 ? 0.1318 0.1269 0.1326 0.0081  -0.0072 0.0101  119 GLY   C C   
1993 O O   . GLY   B 113 ? 0.1316 0.1276 0.1313 0.0086  -0.0088 0.0089  119 GLY   C O   
1994 N N   . VAL   B 114 ? 0.1301 0.1262 0.1341 0.0071  -0.0063 0.0103  120 VAL   C N   
1995 C CA  . VAL   B 114 ? 0.1341 0.1326 0.1402 0.0065  -0.0072 0.0093  120 VAL   C CA  
1996 C C   . VAL   B 114 ? 0.1329 0.1324 0.1373 0.0072  -0.0070 0.0078  120 VAL   C C   
1997 O O   . VAL   B 114 ? 0.1414 0.1402 0.1447 0.0075  -0.0054 0.0076  120 VAL   C O   
1998 C CB  . VAL   B 114 ? 0.1520 0.1512 0.1628 0.0053  -0.0063 0.0105  120 VAL   C CB  
1999 C CG1 . VAL   B 114 ? 0.1612 0.1627 0.1741 0.0048  -0.0069 0.0100  120 VAL   C CG1 
2000 C CG2 . VAL   B 114 ? 0.1758 0.1743 0.1890 0.0044  -0.0072 0.0118  120 VAL   C CG2 
2001 N N   . VAL   B 115 ? 0.1178 0.1188 0.1220 0.0073  -0.0084 0.0067  121 VAL   C N   
2002 C CA  . VAL   B 115 ? 0.1184 0.1207 0.1220 0.0078  -0.0087 0.0051  121 VAL   C CA  
2003 C C   . VAL   B 115 ? 0.1342 0.1381 0.1416 0.0069  -0.0081 0.0048  121 VAL   C C   
2004 O O   . VAL   B 115 ? 0.1343 0.1384 0.1420 0.0069  -0.0075 0.0036  121 VAL   C O   
2005 C CB  . VAL   B 115 ? 0.1300 0.1333 0.1326 0.0085  -0.0104 0.0043  121 VAL   C CB  
2006 C CG1 . VAL   B 115 ? 0.1518 0.1569 0.1553 0.0087  -0.0111 0.0028  121 VAL   C CG1 
2007 C CG2 . VAL   B 115 ? 0.1514 0.1530 0.1506 0.0096  -0.0110 0.0048  121 VAL   C CG2 
2008 N N   . GLY   B 116 ? 0.1247 0.1295 0.1348 0.0061  -0.0083 0.0059  122 GLY   C N   
2009 C CA  . GLY   B 116 ? 0.1399 0.1463 0.1539 0.0054  -0.0078 0.0062  122 GLY   C CA  
2010 C C   . GLY   B 116 ? 0.1239 0.1312 0.1394 0.0048  -0.0085 0.0076  122 GLY   C C   
2011 O O   . GLY   B 116 ? 0.1272 0.1336 0.1409 0.0048  -0.0094 0.0082  122 GLY   C O   
2012 N N   . ILE   B 117 ? 0.1252 0.1341 0.1442 0.0043  -0.0081 0.0084  123 ILE   C N   
2013 C CA  . ILE   B 117 ? 0.1120 0.1218 0.1318 0.0038  -0.0090 0.0100  123 ILE   C CA  
2014 C C   . ILE   B 117 ? 0.1145 0.1259 0.1350 0.0040  -0.0088 0.0101  123 ILE   C C   
2015 O O   . ILE   B 117 ? 0.1184 0.1306 0.1414 0.0040  -0.0079 0.0094  123 ILE   C O   
2016 C CB  . ILE   B 117 ? 0.1304 0.1405 0.1540 0.0031  -0.0087 0.0119  123 ILE   C CB  
2017 C CG1 . ILE   B 117 ? 0.1361 0.1466 0.1638 0.0030  -0.0069 0.0118  123 ILE   C CG1 
2018 C CG2 . ILE   B 117 ? 0.1405 0.1492 0.1640 0.0028  -0.0089 0.0123  123 ILE   C CG2 
2019 C CD1 . ILE   B 117 ? 0.1356 0.1468 0.1686 0.0024  -0.0064 0.0142  123 ILE   C CD1 
2020 N N   . VAL   B 118 ? 0.1134 0.1253 0.1320 0.0040  -0.0097 0.0110  124 VAL   C N   
2021 C CA  . VAL   B 118 ? 0.1206 0.1341 0.1398 0.0042  -0.0090 0.0116  124 VAL   C CA  
2022 C C   . VAL   B 118 ? 0.1065 0.1212 0.1306 0.0037  -0.0080 0.0132  124 VAL   C C   
2023 O O   . VAL   B 118 ? 0.1154 0.1299 0.1413 0.0032  -0.0084 0.0148  124 VAL   C O   
2024 C CB  . VAL   B 118 ? 0.1166 0.1300 0.1320 0.0044  -0.0100 0.0125  124 VAL   C CB  
2025 C CG1 . VAL   B 118 ? 0.1271 0.1419 0.1427 0.0048  -0.0088 0.0137  124 VAL   C CG1 
2026 C CG2 . VAL   B 118 ? 0.1259 0.1376 0.1368 0.0050  -0.0107 0.0107  124 VAL   C CG2 
2027 N N   . SER   B 119 ? 0.1040 0.1199 0.1310 0.0039  -0.0068 0.0129  125 SER   C N   
2028 C CA  . SER   B 119 ? 0.1088 0.1255 0.1411 0.0034  -0.0056 0.0143  125 SER   C CA  
2029 C C   . SER   B 119 ? 0.1229 0.1412 0.1571 0.0036  -0.0044 0.0157  125 SER   C C   
2030 O O   . SER   B 119 ? 0.1166 0.1355 0.1545 0.0033  -0.0035 0.0179  125 SER   C O   
2031 C CB  . SER   B 119 ? 0.1194 0.1354 0.1548 0.0032  -0.0049 0.0123  125 SER   C CB  
2032 O OG  . SER   B 119 ? 0.1379 0.1542 0.1789 0.0027  -0.0036 0.0132  125 SER   C OG  
2033 N N   . THR   B 120 ? 0.1204 0.1393 0.1528 0.0042  -0.0041 0.0145  126 THR   C N   
2034 C CA  . THR   B 120 ? 0.1207 0.1412 0.1556 0.0044  -0.0025 0.0160  126 THR   C CA  
2035 C C   . THR   B 120 ? 0.1185 0.1393 0.1486 0.0053  -0.0022 0.0160  126 THR   C C   
2036 O O   . THR   B 120 ? 0.1205 0.1401 0.1459 0.0058  -0.0035 0.0144  126 THR   C O   
2037 C CB  . THR   B 120 ? 0.1187 0.1401 0.1594 0.0041  -0.0017 0.0143  126 THR   C CB  
2038 O OG1 . THR   B 120 ? 0.1352 0.1567 0.1739 0.0046  -0.0026 0.0118  126 THR   C OG1 
2039 C CG2 . THR   B 120 ? 0.1441 0.1645 0.1889 0.0032  -0.0019 0.0132  126 THR   C CG2 
2040 N N   . GLY   B 121 ? 0.1350 0.1571 0.1663 0.0057  -0.0004 0.0180  127 GLY   C N   
2041 C CA  . GLY   B 121 ? 0.1578 0.1801 0.1848 0.0068  0.0007  0.0182  127 GLY   C CA  
2042 C C   . GLY   B 121 ? 0.1910 0.2151 0.2219 0.0072  0.0035  0.0202  127 GLY   C C   
2043 O O   . GLY   B 121 ? 0.2187 0.2433 0.2528 0.0067  0.0046  0.0228  127 GLY   C O   
2044 N N   . GLY   B 122 ? 0.2226 0.2476 0.2539 0.0081  0.0050  0.0194  128 GLY   C N   
2045 C CA  . GLY   B 122 ? 0.2341 0.2610 0.2697 0.0085  0.0082  0.0216  128 GLY   C CA  
2046 C C   . GLY   B 122 ? 0.2358 0.2639 0.2737 0.0094  0.0094  0.0201  128 GLY   C C   
2047 O O   . GLY   B 122 ? 0.2354 0.2637 0.2750 0.0092  0.0075  0.0174  128 GLY   C O   
2048 N N   . ASN   B 123 ? 0.2168 0.2462 0.2553 0.0104  0.0129  0.0221  129 ASN   C N   
2049 C CA  . ASN   B 123 ? 0.2113 0.2424 0.2538 0.0114  0.0146  0.0211  129 ASN   C CA  
2050 C C   . ASN   B 123 ? 0.1977 0.2274 0.2350 0.0123  0.0128  0.0182  129 ASN   C C   
2051 O O   . ASN   B 123 ? 0.2260 0.2572 0.2681 0.0128  0.0126  0.0167  129 ASN   C O   
2052 C CB  . ASN   B 123 ? 0.2429 0.2765 0.2966 0.0102  0.0140  0.0205  129 ASN   C CB  
2053 C CG  . ASN   B 123 ? 0.3099 0.3457 0.3713 0.0099  0.0175  0.0234  129 ASN   C CG  
2054 O OD1 . ASN   B 123 ? 0.3154 0.3514 0.3746 0.0111  0.0212  0.0260  129 ASN   C OD1 
2055 N ND2 . ASN   B 123 ? 0.3330 0.3702 0.4037 0.0084  0.0167  0.0231  129 ASN   C ND2 
2056 N N   . GLY   B 124 ? 0.1796 0.2066 0.2078 0.0127  0.0116  0.0176  130 GLY   C N   
2057 C CA  . GLY   B 124 ? 0.1776 0.2028 0.2012 0.0136  0.0100  0.0149  130 GLY   C CA  
2058 C C   . GLY   B 124 ? 0.1710 0.1958 0.1964 0.0127  0.0065  0.0127  130 GLY   C C   
2059 O O   . GLY   B 124 ? 0.1772 0.2011 0.2008 0.0135  0.0054  0.0107  130 GLY   C O   
2060 N N   . LEU   B 125 ? 0.1529 0.1784 0.1820 0.0112  0.0049  0.0130  131 LEU   C N   
2061 C CA  . LEU   B 125 ? 0.1408 0.1656 0.1710 0.0104  0.0019  0.0111  131 LEU   C CA  
2062 C C   . LEU   B 125 ? 0.1551 0.1779 0.1811 0.0094  0.0002  0.0114  131 LEU   C C   
2063 O O   . LEU   B 125 ? 0.1870 0.2099 0.2126 0.0089  0.0011  0.0134  131 LEU   C O   
2064 C CB  . LEU   B 125 ? 0.1633 0.1904 0.2017 0.0094  0.0014  0.0107  131 LEU   C CB  
2065 C CG  . LEU   B 125 ? 0.1935 0.2233 0.2380 0.0102  0.0026  0.0105  131 LEU   C CG  
2066 C CD1 . LEU   B 125 ? 0.2374 0.2696 0.2908 0.0090  0.0028  0.0108  131 LEU   C CD1 
2067 C CD2 . LEU   B 125 ? 0.2098 0.2394 0.2532 0.0111  0.0007  0.0085  131 LEU   C CD2 
2068 N N   . VAL   B 126 ? 0.1244 0.1457 0.1479 0.0092  -0.0020 0.0097  132 VAL   C N   
2069 C CA  . VAL   B 126 ? 0.1211 0.1407 0.1421 0.0082  -0.0036 0.0099  132 VAL   C CA  
2070 C C   . VAL   B 126 ? 0.1136 0.1333 0.1380 0.0075  -0.0049 0.0085  132 VAL   C C   
2071 O O   . VAL   B 126 ? 0.1179 0.1378 0.1430 0.0080  -0.0058 0.0069  132 VAL   C O   
2072 C CB  . VAL   B 126 ? 0.1254 0.1425 0.1400 0.0086  -0.0048 0.0092  132 VAL   C CB  
2073 C CG1 . VAL   B 126 ? 0.1399 0.1562 0.1534 0.0095  -0.0055 0.0073  132 VAL   C CG1 
2074 C CG2 . VAL   B 126 ? 0.1277 0.1435 0.1413 0.0075  -0.0064 0.0096  132 VAL   C CG2 
2075 N N   . GLY   B 127 ? 0.1074 0.1269 0.1339 0.0065  -0.0050 0.0093  133 GLY   C N   
2076 C CA  . GLY   B 127 ? 0.1018 0.1209 0.1307 0.0059  -0.0060 0.0077  133 GLY   C CA  
2077 C C   . GLY   B 127 ? 0.1163 0.1335 0.1424 0.0054  -0.0068 0.0078  133 GLY   C C   
2078 O O   . GLY   B 127 ? 0.1224 0.1391 0.1476 0.0051  -0.0066 0.0095  133 GLY   C O   
2079 N N   . PHE   B 128 ? 0.0964 0.1124 0.1214 0.0055  -0.0077 0.0060  134 PHE   C N   
2080 C CA  . PHE   B 128 ? 0.1063 0.1205 0.1290 0.0053  -0.0081 0.0060  134 PHE   C CA  
2081 C C   . PHE   B 128 ? 0.1061 0.1196 0.1310 0.0048  -0.0077 0.0048  134 PHE   C C   
2082 O O   . PHE   B 128 ? 0.1128 0.1265 0.1383 0.0049  -0.0083 0.0030  134 PHE   C O   
2083 C CB  . PHE   B 128 ? 0.1129 0.1256 0.1310 0.0060  -0.0092 0.0050  134 PHE   C CB  
2084 C CG  . PHE   B 128 ? 0.1217 0.1346 0.1375 0.0067  -0.0095 0.0055  134 PHE   C CG  
2085 C CD1 . PHE   B 128 ? 0.1240 0.1358 0.1375 0.0065  -0.0097 0.0066  134 PHE   C CD1 
2086 C CD2 . PHE   B 128 ? 0.1401 0.1540 0.1561 0.0076  -0.0097 0.0046  134 PHE   C CD2 
2087 C CE1 . PHE   B 128 ? 0.1354 0.1468 0.1461 0.0071  -0.0099 0.0065  134 PHE   C CE1 
2088 C CE2 . PHE   B 128 ? 0.1422 0.1559 0.1560 0.0084  -0.0095 0.0048  134 PHE   C CE2 
2089 C CZ  . PHE   B 128 ? 0.1358 0.1479 0.1465 0.0082  -0.0095 0.0056  134 PHE   C CZ  
2090 N N   . ALA   B 129 ? 0.1134 0.1260 0.1395 0.0043  -0.0069 0.0058  135 ALA   C N   
2091 C CA  . ALA   B 129 ? 0.1160 0.1274 0.1436 0.0040  -0.0061 0.0046  135 ALA   C CA  
2092 C C   . ALA   B 129 ? 0.1225 0.1320 0.1454 0.0045  -0.0064 0.0035  135 ALA   C C   
2093 O O   . ALA   B 129 ? 0.1245 0.1332 0.1456 0.0046  -0.0063 0.0047  135 ALA   C O   
2094 C CB  . ALA   B 129 ? 0.1329 0.1441 0.1642 0.0035  -0.0047 0.0065  135 ALA   C CB  
2095 N N   . ASP   B 130 ? 0.1136 0.1225 0.1346 0.0049  -0.0069 0.0012  136 ASP   C N   
2096 C CA  . ASP   B 130 ? 0.1149 0.1220 0.1308 0.0056  -0.0072 0.0004  136 ASP   C CA  
2097 C C   . ASP   B 130 ? 0.1262 0.1312 0.1419 0.0055  -0.0051 0.0007  136 ASP   C C   
2098 O O   . ASP   B 130 ? 0.1245 0.1293 0.1437 0.0050  -0.0037 0.0002  136 ASP   C O   
2099 C CB  . ASP   B 130 ? 0.1328 0.1397 0.1465 0.0060  -0.0085 -0.0021 136 ASP   C CB  
2100 C CG  . ASP   B 130 ? 0.1861 0.1912 0.1937 0.0069  -0.0090 -0.0027 136 ASP   C CG  
2101 O OD1 . ASP   B 130 ? 0.1752 0.1800 0.1804 0.0075  -0.0094 -0.0012 136 ASP   C OD1 
2102 O OD2 . ASP   B 130 ? 0.2225 0.2260 0.2274 0.0071  -0.0088 -0.0046 136 ASP   C OD2 
2103 N N   . VAL   B 131 ? 0.1239 0.1275 0.1362 0.0060  -0.0046 0.0016  137 VAL   C N   
2104 C CA  . VAL   B 131 ? 0.1161 0.1178 0.1280 0.0062  -0.0022 0.0020  137 VAL   C CA  
2105 C C   . VAL   B 131 ? 0.1397 0.1392 0.1453 0.0072  -0.0019 0.0011  137 VAL   C C   
2106 O O   . VAL   B 131 ? 0.1435 0.1411 0.1480 0.0075  0.0006  0.0014  137 VAL   C O   
2107 C CB  . VAL   B 131 ? 0.1373 0.1391 0.1524 0.0058  -0.0012 0.0046  137 VAL   C CB  
2108 C CG1 . VAL   B 131 ? 0.1433 0.1472 0.1641 0.0049  -0.0016 0.0059  137 VAL   C CG1 
2109 C CG2 . VAL   B 131 ? 0.1438 0.1454 0.1563 0.0060  -0.0025 0.0059  137 VAL   C CG2 
2110 N N   . ARG   B 132 ? 0.1380 0.1378 0.1396 0.0078  -0.0041 0.0001  138 ARG   C N   
2111 C CA  . ARG   B 132 ? 0.1449 0.1427 0.1401 0.0089  -0.0040 -0.0001 138 ARG   C CA  
2112 C C   . ARG   B 132 ? 0.1516 0.1474 0.1430 0.0093  -0.0029 -0.0023 138 ARG   C C   
2113 O O   . ARG   B 132 ? 0.1742 0.1678 0.1597 0.0103  -0.0018 -0.0021 138 ARG   C O   
2114 C CB  . ARG   B 132 ? 0.1333 0.1320 0.1258 0.0095  -0.0069 -0.0004 138 ARG   C CB  
2115 C CG  . ARG   B 132 ? 0.1290 0.1289 0.1241 0.0094  -0.0077 0.0016  138 ARG   C CG  
2116 C CD  . ARG   B 132 ? 0.1374 0.1381 0.1305 0.0102  -0.0102 0.0012  138 ARG   C CD  
2117 N NE  . ARG   B 132 ? 0.1313 0.1345 0.1275 0.0098  -0.0118 -0.0005 138 ARG   C NE  
2118 C CZ  . ARG   B 132 ? 0.1487 0.1535 0.1455 0.0103  -0.0139 -0.0009 138 ARG   C CZ  
2119 N NH1 . ARG   B 132 ? 0.1316 0.1358 0.1255 0.0115  -0.0150 0.0001  138 ARG   C NH1 
2120 N NH2 . ARG   B 132 ? 0.1458 0.1529 0.1466 0.0098  -0.0149 -0.0021 138 ARG   C NH2 
2121 N N   . ASP   B 133 ? 0.1435 0.1399 0.1378 0.0086  -0.0029 -0.0045 139 ASP   C N   
2122 C CA  . ASP   B 133 ? 0.1593 0.1533 0.1498 0.0089  -0.0018 -0.0072 139 ASP   C CA  
2123 C C   . ASP   B 133 ? 0.1624 0.1544 0.1545 0.0090  0.0023  -0.0067 139 ASP   C C   
2124 O O   . ASP   B 133 ? 0.1820 0.1714 0.1699 0.0095  0.0039  -0.0089 139 ASP   C O   
2125 C CB  . ASP   B 133 ? 0.1794 0.1745 0.1731 0.0080  -0.0037 -0.0101 139 ASP   C CB  
2126 C CG  . ASP   B 133 ? 0.1929 0.1893 0.1948 0.0069  -0.0024 -0.0093 139 ASP   C CG  
2127 O OD1 . ASP   B 133 ? 0.1966 0.1949 0.2024 0.0066  -0.0023 -0.0065 139 ASP   C OD1 
2128 O OD2 . ASP   B 133 ? 0.2181 0.2136 0.2226 0.0064  -0.0016 -0.0116 139 ASP   C OD2 
2129 N N   . LEU   B 134 ? 0.1512 0.1442 0.1489 0.0085  0.0039  -0.0039 140 LEU   C N   
2130 C CA  . LEU   B 134 ? 0.1519 0.1436 0.1529 0.0086  0.0078  -0.0029 140 LEU   C CA  
2131 C C   . LEU   B 134 ? 0.1597 0.1496 0.1565 0.0096  0.0102  -0.0012 140 LEU   C C   
2132 O O   . LEU   B 134 ? 0.1585 0.1492 0.1587 0.0094  0.0110  0.0018  140 LEU   C O   
2133 C CB  . LEU   B 134 ? 0.1472 0.1413 0.1567 0.0076  0.0078  -0.0005 140 LEU   C CB  
2134 C CG  . LEU   B 134 ? 0.1633 0.1593 0.1771 0.0067  0.0057  -0.0017 140 LEU   C CG  
2135 C CD1 . LEU   B 134 ? 0.1746 0.1730 0.1956 0.0059  0.0054  0.0012  140 LEU   C CD1 
2136 C CD2 . LEU   B 134 ? 0.1819 0.1762 0.1968 0.0066  0.0072  -0.0045 140 LEU   C CD2 
2137 N N   . LEU   B 135 ? 0.1744 0.1615 0.1633 0.0107  0.0112  -0.0030 141 LEU   C N   
2138 C CA  . LEU   B 135 ? 0.1872 0.1724 0.1709 0.0119  0.0135  -0.0011 141 LEU   C CA  
2139 C C   . LEU   B 135 ? 0.1791 0.1634 0.1672 0.0121  0.0181  0.0011  141 LEU   C C   
2140 O O   . LEU   B 135 ? 0.1987 0.1826 0.1865 0.0125  0.0197  0.0040  141 LEU   C O   
2141 C CB  . LEU   B 135 ? 0.1864 0.1688 0.1598 0.0131  0.0134  -0.0034 141 LEU   C CB  
2142 C CG  . LEU   B 135 ? 0.1948 0.1783 0.1643 0.0130  0.0086  -0.0058 141 LEU   C CG  
2143 C CD1 . LEU   B 135 ? 0.2102 0.1907 0.1687 0.0143  0.0083  -0.0081 141 LEU   C CD1 
2144 C CD2 . LEU   B 135 ? 0.1943 0.1803 0.1656 0.0127  0.0053  -0.0035 141 LEU   C CD2 
2145 N N   . TRP   B 136 ? 0.1735 0.1576 0.1668 0.0117  0.0202  0.0000  142 TRP   C N   
2146 C CA  . TRP   B 136 ? 0.1895 0.1731 0.1885 0.0120  0.0248  0.0020  142 TRP   C CA  
2147 C C   . TRP   B 136 ? 0.1908 0.1772 0.1980 0.0110  0.0240  0.0059  142 TRP   C C   
2148 O O   . TRP   B 136 ? 0.2095 0.1957 0.2215 0.0112  0.0274  0.0083  142 TRP   C O   
2149 C CB  . TRP   B 136 ? 0.1882 0.1710 0.1915 0.0119  0.0268  -0.0002 142 TRP   C CB  
2150 C CG  . TRP   B 136 ? 0.1847 0.1700 0.1935 0.0106  0.0232  -0.0011 142 TRP   C CG  
2151 C CD1 . TRP   B 136 ? 0.1974 0.1823 0.2034 0.0102  0.0206  -0.0044 142 TRP   C CD1 
2152 C CD2 . TRP   B 136 ? 0.1809 0.1692 0.1995 0.0095  0.0223  0.0015  142 TRP   C CD2 
2153 N NE1 . TRP   B 136 ? 0.2009 0.1886 0.2143 0.0090  0.0183  -0.0037 142 TRP   C NE1 
2154 C CE2 . TRP   B 136 ? 0.1898 0.1795 0.2105 0.0086  0.0194  -0.0001 142 TRP   C CE2 
2155 C CE3 . TRP   B 136 ? 0.1794 0.1694 0.2051 0.0092  0.0236  0.0052  142 TRP   C CE3 
2156 C CZ2 . TRP   B 136 ? 0.1836 0.1761 0.2125 0.0077  0.0179  0.0020  142 TRP   C CZ2 
2157 C CZ3 . TRP   B 136 ? 0.1816 0.1746 0.2155 0.0082  0.0217  0.0070  142 TRP   C CZ3 
2158 C CH2 . TRP   B 136 ? 0.1835 0.1776 0.2184 0.0075  0.0189  0.0055  142 TRP   C CH2 
2159 N N   . LEU   B 137 ? 0.1773 0.1663 0.1864 0.0099  0.0196  0.0064  143 LEU   C N   
2160 C CA  . LEU   B 137 ? 0.1812 0.1724 0.1968 0.0090  0.0184  0.0096  143 LEU   C CA  
2161 C C   . LEU   B 137 ? 0.2088 0.1988 0.2223 0.0095  0.0200  0.0119  143 LEU   C C   
2162 O O   . LEU   B 137 ? 0.2296 0.2209 0.2496 0.0087  0.0202  0.0147  143 LEU   C O   
2163 C CB  . LEU   B 137 ? 0.1747 0.1682 0.1908 0.0080  0.0136  0.0094  143 LEU   C CB  
2164 C CG  . LEU   B 137 ? 0.1779 0.1733 0.1984 0.0072  0.0120  0.0082  143 LEU   C CG  
2165 C CD1 . LEU   B 137 ? 0.1748 0.1721 0.1939 0.0066  0.0079  0.0078  143 LEU   C CD1 
2166 C CD2 . LEU   B 137 ? 0.1700 0.1671 0.1996 0.0065  0.0131  0.0106  143 LEU   C CD2 
2167 N N   . ASP   B 138 ? 0.2007 0.1882 0.2055 0.0107  0.0210  0.0110  144 ASP   C N   
2168 C CA  . ASP   B 138 ? 0.2127 0.1988 0.2149 0.0113  0.0226  0.0135  144 ASP   C CA  
2169 C C   . ASP   B 138 ? 0.2468 0.2310 0.2503 0.0122  0.0282  0.0152  144 ASP   C C   
2170 O O   . ASP   B 138 ? 0.2692 0.2522 0.2715 0.0127  0.0302  0.0177  144 ASP   C O   
2171 C CB  . ASP   B 138 ? 0.2144 0.1986 0.2063 0.0125  0.0210  0.0124  144 ASP   C CB  
2172 C CG  . ASP   B 138 ? 0.2329 0.2189 0.2238 0.0118  0.0159  0.0113  144 ASP   C CG  
2173 O OD1 . ASP   B 138 ? 0.2347 0.2231 0.2322 0.0105  0.0137  0.0119  144 ASP   C OD1 
2174 O OD2 . ASP   B 138 ? 0.2509 0.2360 0.2343 0.0127  0.0140  0.0101  144 ASP   C OD2 
2175 N N   . GLU   B 139 ? 0.2658 0.2497 0.2721 0.0125  0.0311  0.0139  145 GLU   C N   
2176 C CA  . GLU   B 139 ? 0.3224 0.3043 0.3295 0.0137  0.0370  0.0153  145 GLU   C CA  
2177 C C   . GLU   B 139 ? 0.3764 0.3599 0.3944 0.0131  0.0394  0.0162  145 GLU   C C   
2178 O O   . GLU   B 139 ? 0.3833 0.3694 0.4072 0.0120  0.0363  0.0156  145 GLU   C O   
2179 C CB  . GLU   B 139 ? 0.3761 0.3545 0.3724 0.0153  0.0394  0.0123  145 GLU   C CB  
2180 C CG  . GLU   B 139 ? 0.4803 0.4586 0.4764 0.0151  0.0381  0.0084  145 GLU   C CG  
2181 C CD  . GLU   B 139 ? 0.5992 0.5745 0.5838 0.0162  0.0377  0.0045  145 GLU   C CD  
2182 O OE1 . GLU   B 139 ? 0.6119 0.5864 0.5967 0.0161  0.0377  0.0012  145 GLU   C OE1 
2183 O OE2 . GLU   B 139 ? 0.6294 0.6030 0.6050 0.0171  0.0374  0.0049  145 GLU   C OE2 
2184 N N   . GLU   B 140 ? 0.4162 0.3983 0.4368 0.0142  0.0452  0.0178  146 GLU   C N   
2185 C CA  . GLU   B 140 ? 0.4598 0.4430 0.4907 0.0142  0.0486  0.0190  146 GLU   C CA  
2186 C C   . GLU   B 140 ? 0.5004 0.4873 0.5434 0.0127  0.0468  0.0226  146 GLU   C C   
2187 O O   . GLU   B 140 ? 0.5289 0.5163 0.5798 0.0130  0.0509  0.0254  146 GLU   C O   
2188 C CB  . GLU   B 140 ? 0.4792 0.4622 0.5106 0.0143  0.0480  0.0156  146 GLU   C CB  
2189 C CG  . GLU   B 140 ? 0.5468 0.5318 0.5905 0.0140  0.0498  0.0171  146 GLU   C CG  
2190 C CD  . GLU   B 140 ? 0.6234 0.6054 0.6672 0.0157  0.0561  0.0156  146 GLU   C CD  
2191 O OE1 . GLU   B 140 ? 0.6460 0.6262 0.6860 0.0161  0.0559  0.0119  146 GLU   C OE1 
2192 O OE2 . GLU   B 140 ? 0.6374 0.6189 0.6853 0.0167  0.0614  0.0180  146 GLU   C OE2 
2193 C C4  A A1B22 C .   ? 0.1706 0.1744 0.1959 -0.0011 0.0158  -0.0117 201 A1B22 A C4  
2194 C C4  B A1B22 C .   ? 0.1705 0.1744 0.1963 -0.0012 0.0165  -0.0118 201 A1B22 A C4  
2195 C C5  A A1B22 C .   ? 0.1901 0.1931 0.2197 -0.0001 0.0161  -0.0115 201 A1B22 A C5  
2196 C C5  B A1B22 C .   ? 0.1892 0.1928 0.2208 0.0004  0.0170  -0.0108 201 A1B22 A C5  
2197 C C6  A A1B22 C .   ? 0.1853 0.1893 0.2134 0.0009  0.0123  -0.0093 201 A1B22 A C6  
2198 C C6  B A1B22 C .   ? 0.1843 0.1890 0.2148 0.0015  0.0132  -0.0084 201 A1B22 A C6  
2199 C C7  A A1B22 C .   ? 0.2366 0.2393 0.2691 0.0017  0.0132  -0.0094 201 A1B22 A C7  
2200 C C7  B A1B22 C .   ? 0.2340 0.2386 0.2716 0.0034  0.0141  -0.0067 201 A1B22 A C7  
2201 C C8  A A1B22 C .   ? 0.2476 0.2527 0.2868 0.0045  0.0124  -0.0048 201 A1B22 A C8  
2202 C C8  B A1B22 C .   ? 0.2505 0.2529 0.2853 0.0022  0.0132  -0.0089 201 A1B22 A C8  
2203 C C10 A A1B22 C .   ? 0.1732 0.1775 0.2160 0.0060  0.0098  -0.0020 201 A1B22 A C10 
2204 C C10 B A1B22 C .   ? 0.1737 0.1780 0.2155 0.0058  0.0096  -0.0023 201 A1B22 A C10 
2205 O O   A A1B22 C .   ? 0.2784 0.2859 0.3220 0.0059  0.0131  -0.0020 201 A1B22 A O   
2206 O O   B A1B22 C .   ? 0.2865 0.2871 0.3165 -0.0003 0.0138  -0.0128 201 A1B22 A O   
2207 N N   A A1B22 C .   ? 0.1874 0.1923 0.2274 0.0051  0.0110  -0.0037 201 A1B22 A N   
2208 N N   B A1B22 C .   ? 0.1888 0.1921 0.2265 0.0038  0.0116  -0.0062 201 A1B22 A N   
2209 C C11 A A1B22 C .   ? 0.1801 0.1835 0.2161 0.0039  0.0091  -0.0056 201 A1B22 A C11 
2210 C C11 B A1B22 C .   ? 0.1809 0.1834 0.2166 0.0032  0.0098  -0.0070 201 A1B22 A C11 
2211 O O1  A A1B22 C .   ? 0.1709 0.1769 0.2114 0.0065  0.0065  0.0002  201 A1B22 A O1  
2212 O O1  B A1B22 C .   ? 0.1711 0.1774 0.2103 0.0063  0.0061  0.0001  201 A1B22 A O1  
2213 C C9  A A1B22 C .   ? 0.1870 0.1936 0.2329 0.0073  0.0106  0.0006  201 A1B22 A C9  
2214 C C9  B A1B22 C .   ? 0.1881 0.1942 0.2308 0.0063  0.0105  -0.0013 201 A1B22 A C9  
2215 C C1  A A1B22 C .   ? 0.1392 0.1418 0.1587 -0.0008 0.0067  -0.0068 201 A1B22 A C1  
2216 C C1  B A1B22 C .   ? 0.1395 0.1420 0.1598 -0.0007 0.0073  -0.0066 201 A1B22 A C1  
2217 S S   A A1B22 C .   ? 0.1371 0.1379 0.1515 -0.0007 0.0025  -0.0043 201 A1B22 A S   
2218 S S   B A1B22 C .   ? 0.1372 0.1377 0.1527 -0.0008 0.0030  -0.0041 201 A1B22 A S   
2219 C C   A A1B22 C .   ? 0.1366 0.1378 0.1424 -0.0001 0.0002  -0.0026 201 A1B22 A C   
2220 C C   B A1B22 C .   ? 0.1367 0.1377 0.1429 -0.0002 0.0005  -0.0026 201 A1B22 A C   
2221 C C3  A A1B22 C .   ? 0.1507 0.1562 0.1706 -0.0011 0.0117  -0.0096 201 A1B22 A C3  
2222 C C3  B A1B22 C .   ? 0.1514 0.1565 0.1707 -0.0016 0.0124  -0.0103 201 A1B22 A C3  
2223 C C2  A A1B22 C .   ? 0.1387 0.1404 0.1534 -0.0019 0.0057  -0.0067 201 A1B22 A C2  
2224 C C2  B A1B22 C .   ? 0.1390 0.1407 0.1538 -0.0023 0.0062  -0.0072 201 A1B22 A C2  
# 
